overview on glutathione in Saccharomyces versus non-conventional yeasts | FEMS Yeast Research

<!DOCTYPE html> <html lang="en" class="no-js"> <head>  <meta http-equiv="Content-Type" content="text/html; charset=utf-8" /> <title>overview on glutathione in Saccharomyces versus non-conventional yeasts | FEMS Yeast Research | Oxford Academic</title> <script type='text/javascript' defer src='//js.trendmd.com/trendmd.min.js' data-trendmdconfig='{"element":"#trendmd-suggestions"}' class='optanon-category-C0002'></script> <script src="https://ajax.googleapis.com/ajax/libs/jquery/3.7.1/jquery.min.js" type="text/javascript"></script> <script>window.jQuery || document.write('<script src="//oup.silverchair-cdn.com/Themes/Silver/app/js/jquery.3.7.1.min.js" type="text/javascript">\x3C/script>')</script> <script src="//oup.silverchair-cdn.com/Themes/Silver/app/vendor/v-638673063114460124/jquery-migrate-1.4.1.min.js" type="text/javascript"></script> <script type='text/javascript' src='https://platform-api.sharethis.com/js/sharethis.js#property=643701de45aa460012e1032e&product=sop' async='async' class='optanon-category-C0004'></script> <meta name="viewport" content="width=device-width, initial-scale=1, maximum-scale=10" /> <meta http-equiv="X-UA-Compatible" content="IE=Edge" />  <meta name="format-detection" content="telephone=no" />  <link rel="apple-touch-icon" sizes="180x180" href="//oup.silverchair-cdn.com/UI/app/img/v-638673062239174859/apple-touch-icon.png"> <link rel="icon" type="image/png" href="//oup.silverchair-cdn.com/UI/app/img/v-638673062239324857/favicon-32x32.png" sizes="32x32"> <link rel="icon" type="image/png" href="//oup.silverchair-cdn.com/UI/app/img/v-638673062239274861/favicon-16x16.png" sizes="16x16"> <link rel="mask-icon" href="//oup.silverchair-cdn.com/UI/app/img/v-638673062239974847/safari-pinned-tab.svg" color="#001C54"> <link rel="icon" href="//oup.silverchair-cdn.com/UI/app/img/v-638673062239424863/favicon.ico"> <link rel="manifest" href="//oup.silverchair-cdn.com/UI/app/img/v-638673062239674810/manifest.json"> <meta name="msapplication-config" content="//oup.silverchair-cdn.com/UI/app/img/v-638673062239174859/browserconfig.xml"> <meta name="theme-color" content="#002f65"> <link rel="stylesheet" type="text/css" href="//oup.silverchair-cdn.com/UI/app/fonts/icons.css" /> <link rel="stylesheet" type="text/css" href="//oup.silverchair-cdn.com/Themes/Client/app/css/v-638687870534111495/site.min.css" /> <link rel="preload" href="https://fonts.googleapis.com/css?family=Merriweather:300,400,400italic,700,700italic|Source+Sans+Pro:400,400italic,700,700italic" as="style" onload="this.onload=null;this.rel='stylesheet'"> <link href="//oup.silverchair-cdn.com/data/SiteBuilderAssetsOriginals/Live/CSS/journals/v-638683065031606590/global.css" rel="stylesheet" type="text/css" /> <link href="//oup.silverchair-cdn.com/data/SiteBuilderAssets/Live/CSS/femsyr/v-638566352717263870/Site.css" rel="stylesheet" type="text/css" /> <script> var dataLayer = [{"full_title":"An overview on glutathione in Saccharomyces versus non-conventional yeasts","short_title":"overview on glutathione in Saccharomyces versus non-conventional yeasts","authors":"Michel J Penninckx","issue_and_volume":"Volume 2 | Issue 3","type":"review-article","online_publication_date":"2002-08-01","access_type":"Free","license_type":"free","event_type":"full-text","supplier_tag":"SC_Journals","object_type":"Article","taxonomy":"taxId%3a39%7ctaxLabel%3aAcademicSubjects%7cnodeId%3aSCI01150%7cnodeLabel%3aMicrobiology%7cnodeLevel%3a3","siteid":"femsyr","authzrequired":"false","doi":"10.1016/S1567-1356(02)00081-8"}]; </script> <script> (function (w, d, s, l, i) { w[l] = w[l] || []; w[l].push({ 'gtm.start': new Date().getTime(), event: 'gtm.js' }); var f = d.getElementsByTagName(s)[0], j = d.createElement(s), dl = l != 'dataLayer' ? '&l=' + l : ''; j.async = true; j.src = 'https://www.googletagmanager.com/gtm.js?id=' + i + dl; f.parentNode.insertBefore(j, f); })(window, document, 'script', 'dataLayer', 'GTM-W6DD7HV'); </script> <script type="text/javascript"> var App = App || {}; App.LoginUserInfo = { isInstLoggedIn: 0, isIndividualLoggedIn: 0 }; App.CurrentSubdomain = 'femsyr'; App.SiteURL = 'academic.oup.com/femsyr'; </script> <link href="https://cdn.jsdelivr.net/chartist.js/latest/chartist.min.css" media="print" onload="this.onload=null;this.removeAttribute('media');" rel="stylesheet" type="text/css" /> <script type="application/ld+json"> {"@context":"https://schema.org","@type":"ScholarlyArticle","@id":"https://academic.oup.com/femsyr/article/2/3/295/562518","name":"An overview on glutathione in Saccharomyces versus non-conventional yeasts","about":["oxidative stress","detoxification therapy","glutathione","tissue membrane","metabolic detoxication, drug","metals, heavy","nitrogen","saccharomyces","starvation","sulfhydryl compounds","sulfur","xenobiotics","yeasts","cadmium","stress"],"datePublished":"2002-08-01","isPartOf":{"@id":"https://academic.oup.com/femsyr/issue/2/3","@type":"PublicationIssue","issueNumber":"3","datePublished":"2002-08-01","isPartOf":{"@id":"https://academic.oup.com/femsyr/femsyr","@type":"Periodical","name":"FEMS Yeast Research","issn":["1567-1364"]}},"url":"https://dx.doi.org/10.1016/S1567-1356(02)00081-8","keywords":["oxidative stress","detoxification therapy","glutathione","tissue membrane","metabolic detoxication, drug","metals, heavy","nitrogen","saccharomyces","starvation","sulfhydryl compounds","sulfur","xenobiotics","yeasts","cadmium","stress","Glutathione","Saccharomyces","Non-conventional yeast","Oxidative stress","Heavy-metal stress","Detoxification"],"inLanguage":"en","copyrightHolder":"Federation of European Microbiological Societies","copyrightYear":"2024","publisher":"Oxford University Press","author":[{"name":"Penninckx, Michel J","affiliation":"Université Libre de Bruxelles, Laboratory of Microbial Physiology and Ecology, c/o Pasteur Institute, 642, Rue Engeland, B-1180 Brussels, Belgium","@type":"Person"}],"description":"Abstract. Glutathione (GSH: l-γ-glutamyl-l-cysteinylglycine) is present in high concentrations up to 10 mM in yeast cells. Its very low redox potential (E′","pageStart":"295","pageEnd":"305","siteName":"OUP Academic","thumbnailURL":"https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/m_FYR_295_f1.jpeg?Expires=1796335806&Signature=Xmbb5FNuubUyO0N3lUs~OlYbEoqfLIZxSmK5cwtyRrgZTqkwEQ~8gvFlCwVThC2XQ-8yHzSPX6JSf4MWwZcLFHoto3d-H~5Ht06KVdgBxMrBFK4dgNR9mnnOtdjWe4OIpXPxsi48KDE4h3flEe7QthwJS0j7RkeHeV4uAygSm-oSsHY04xPMbCJhQewtsRRPFJRwI6VEpDVj2jg5vxa-Y~8xJyxLDFgp10P9P2AomkjATpXN3oxU3tnnVFR5cvP5jqt~fla-EHSPF18iqT8LOn3FPCIsky5NTeKKkXvkwr4d0tJud7lubY3OzIRHYtPagbXZyp0rk4RhHZvfO9-jkw__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA","headline":"An overview on glutathione in Saccharomyces versus non-conventional yeasts","image":"https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/m_FYR_295_f1.jpeg?Expires=1796335806&Signature=Xmbb5FNuubUyO0N3lUs~OlYbEoqfLIZxSmK5cwtyRrgZTqkwEQ~8gvFlCwVThC2XQ-8yHzSPX6JSf4MWwZcLFHoto3d-H~5Ht06KVdgBxMrBFK4dgNR9mnnOtdjWe4OIpXPxsi48KDE4h3flEe7QthwJS0j7RkeHeV4uAygSm-oSsHY04xPMbCJhQewtsRRPFJRwI6VEpDVj2jg5vxa-Y~8xJyxLDFgp10P9P2AomkjATpXN3oxU3tnnVFR5cvP5jqt~fla-EHSPF18iqT8LOn3FPCIsky5NTeKKkXvkwr4d0tJud7lubY3OzIRHYtPagbXZyp0rk4RhHZvfO9-jkw__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA","image:alt":"The interrelationship of GSH with cellular biochemical systems [3]."} </script> <meta property="og:site_name" content="OUP Academic" /> <meta property="og:title" content="An overview on glutathione in Saccharomyces versus non-conventional yeasts" /> <meta property="og:description" content="Abstract. Glutathione (GSH: l-γ-glutamyl-l-cysteinylglycine) is present in high concentrations up to 10 mM in yeast cells. Its very low redox potential (E′" /> <meta property="og:type" content="article" /> <meta property="og:url" content="https://dx.doi.org/10.1016/S1567-1356(02)00081-8" /> <meta property="og:updated_time" content="" /> <meta property="og:image" content="https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/m_FYR_295_f1.jpeg?Expires=1796335806&Signature=Xmbb5FNuubUyO0N3lUs~OlYbEoqfLIZxSmK5cwtyRrgZTqkwEQ~8gvFlCwVThC2XQ-8yHzSPX6JSf4MWwZcLFHoto3d-H~5Ht06KVdgBxMrBFK4dgNR9mnnOtdjWe4OIpXPxsi48KDE4h3flEe7QthwJS0j7RkeHeV4uAygSm-oSsHY04xPMbCJhQewtsRRPFJRwI6VEpDVj2jg5vxa-Y~8xJyxLDFgp10P9P2AomkjATpXN3oxU3tnnVFR5cvP5jqt~fla-EHSPF18iqT8LOn3FPCIsky5NTeKKkXvkwr4d0tJud7lubY3OzIRHYtPagbXZyp0rk4RhHZvfO9-jkw__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" /> <meta property="og:image:url" content="https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/m_FYR_295_f1.jpeg?Expires=1796335806&Signature=Xmbb5FNuubUyO0N3lUs~OlYbEoqfLIZxSmK5cwtyRrgZTqkwEQ~8gvFlCwVThC2XQ-8yHzSPX6JSf4MWwZcLFHoto3d-H~5Ht06KVdgBxMrBFK4dgNR9mnnOtdjWe4OIpXPxsi48KDE4h3flEe7QthwJS0j7RkeHeV4uAygSm-oSsHY04xPMbCJhQewtsRRPFJRwI6VEpDVj2jg5vxa-Y~8xJyxLDFgp10P9P2AomkjATpXN3oxU3tnnVFR5cvP5jqt~fla-EHSPF18iqT8LOn3FPCIsky5NTeKKkXvkwr4d0tJud7lubY3OzIRHYtPagbXZyp0rk4RhHZvfO9-jkw__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" /> <meta property="og:image:secure_url" content="https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/m_FYR_295_f1.jpeg?Expires=1796335806&Signature=Xmbb5FNuubUyO0N3lUs~OlYbEoqfLIZxSmK5cwtyRrgZTqkwEQ~8gvFlCwVThC2XQ-8yHzSPX6JSf4MWwZcLFHoto3d-H~5Ht06KVdgBxMrBFK4dgNR9mnnOtdjWe4OIpXPxsi48KDE4h3flEe7QthwJS0j7RkeHeV4uAygSm-oSsHY04xPMbCJhQewtsRRPFJRwI6VEpDVj2jg5vxa-Y~8xJyxLDFgp10P9P2AomkjATpXN3oxU3tnnVFR5cvP5jqt~fla-EHSPF18iqT8LOn3FPCIsky5NTeKKkXvkwr4d0tJud7lubY3OzIRHYtPagbXZyp0rk4RhHZvfO9-jkw__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" /> <meta property="og:image:alt" content="The interrelationship of GSH with cellular biochemical systems [3]." /> <meta name="twitter:card" content="summary_large_image" /> <meta name="citation_author" content="Penninckx, Michel J" /><meta name="citation_author_institution" content="Université Libre de Bruxelles, Laboratory of Microbial Physiology and Ecology, c/o Pasteur Institute, 642, Rue Engeland, B-1180 Brussels, Belgium" /><meta name="citation_title" content="An overview on glutathione in Saccharomyces versus non-conventional yeasts" /><meta name="citation_firstpage" content="295" /><meta name="citation_lastpage" content="305" /><meta name="citation_doi" content="10.1016/S1567-1356(02)00081-8" /><meta name="citation_keyword" content="xenobiotics" /><meta name="citation_journal_title" content="FEMS Yeast Research" /><meta name="citation_journal_abbrev" content="FEMS Yeast Res" /><meta name="citation_volume" content="2" /><meta name="citation_issue" content="3" /><meta name="citation_publication_date" content="2002/08/01" /><meta name="citation_issn" content="1567-1356" /><meta name="citation_publisher" content="Oxford Academic" /><meta name="citation_reference" content="citation_title=On the discovery of glutathione; citation_author=Meister A.; citation_journal_title=Trends Biochem. Sci.; citation_year=1988; citation_volume=13; citation_pages=185-188; " /><meta name="citation_reference" content="citation_title=Glutathione; citation_author=Meister A.; citation_author=Anderson M.E.; citation_journal_title=Annu. Rev. Biochem.; citation_year=1983; citation_volume=52; citation_pages=711-760; " /><meta name="citation_reference" content="citation_title=Metabolism and functions of glutathione in micro-organisms; citation_author=Penninckx M.J.; citation_author=Elskens M.T.; citation_journal_title=Adv. Microb. Physiol.; citation_year=1993; citation_volume=32; citation_pages=239-240; " /><meta name="citation_reference" content="citation_title=Molecular physiology of plant sulfur metabolism; citation_author=Hell R.; citation_journal_title=Planta; citation_year=1997; citation_volume=202; citation_pages=138-148; " /><meta name="citation_reference" content="citation_title=Genomic expression programs in the response of yeast cells to environmental changes; citation_author=Gasch A.P.; citation_author=Spellman P.T.; citation_author=Kao C.M.; citation_author=Carmel-Harel O.; citation_author=Eisen M.B.; citation_author=Storz G.; citation_author=Botstein D.; citation_author=Brown P.O.; citation_journal_title=Mol. Biol. Cell; citation_year=2000; citation_volume=11; citation_pages=4241-4257; " /><meta name="citation_reference" content="citation_author=Walker G.; citation_publisher=J. Wiley and Sons, New York; citation_title=Yeast Physiology and Biotechnology; citation_year=1998; " /><meta name="citation_reference" content="citation_title=Metabolism of methanol by yeasts; citation_author=Sahm H.; citation_journal_title=Adv. Biochem. Eng.; citation_year=1977; citation_volume=6; citation_pages=103-127; " /><meta name="citation_reference" content="citation_title=Heterologous protein expression in the methylotrophic yeast Pichia pastoris; citation_author=Cereghino L.; citation_author=Cregg J.M.; citation_journal_title=FEMS Microbiol. Rev.; citation_year=2000; citation_volume=24; citation_pages=45-66; " /><meta name="citation_reference" content="citation_title=Novel thiols of prokaryotes; citation_author=Fahey R.C.; citation_journal_title=Annu. Rev. Microbiol.; citation_year=2001; citation_volume=55; citation_pages=533-556; " /><meta name="citation_reference" content="citation_title=Distribution of thiols in micro-organisms: mycothiol is a major thiol in most actinomycetes; citation_author=Newton G.L.; citation_author=Arnold K.; citation_author=Price M.S.; citation_author=Sherrill C.; citation_author=Delcardayre S.B.; citation_author=Aharonowitz Y.; citation_author=Cohen G.; citation_author=Davies J.; citation_author=Fahey R.; citation_author=Davis C.; citation_journal_title=J. Bacteriol.; citation_year=1996; citation_volume=178; citation_pages=1990-1995; " /><meta name="citation_reference" content="citation_title=Bacterial glutathione S-transferases: what are they good for; citation_author=Vuilleumier S.; citation_journal_title=J. Bacteriol.; citation_year=1997; citation_volume=179; citation_pages=1431-1441; " /><meta name="citation_reference" content="citation_title=γ-Glutamylcysteine and thiosulfate are the major low molecular weight thiols in halobacteria; citation_author=Newton G.L.; citation_author=Javor B.; citation_journal_title=J. Bacteriol.; citation_year=1985; citation_volume=161; citation_pages=438-441; " /><meta name="citation_reference" content="citation_title=Entamoeba histolytica: a eukaryote without glutathione metabolism; citation_author=Fahey R.C.; citation_author=Newton G.L.; citation_author=Arrick B.; citation_author=Overdank-Bogart T.; citation_author=Aley S.B.; citation_journal_title=Science; citation_year=1984; citation_volume=224; citation_pages=70-73; " /><meta name="citation_reference" content="citation_title=An important role for glutathione and γ-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast Saccharomyces cerevisiae; citation_author=Mehdi K.; citation_author=Penninckx M.J.; citation_journal_title=Microbiology; citation_year=1997; citation_volume=143; citation_pages=1885-1889; " /><meta name="citation_reference" content="citation_title=Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast Saccharomyces cerevisiae; citation_author=Grant C.M.; citation_author=MacIver F.H.; citation_author=Dawes I.W.; citation_journal_title=Curr. Genet.; citation_year=1996; citation_volume=29; citation_pages=511-515; " /><meta name="citation_reference" content="citation_title=A genetic investigation of the essential role of glutathione. Mutations in the proline biosynthesis pathway are the only suppressors of glutathione auxotrophy in yeast; citation_author=Spector D.; citation_author=Labarre J.; citation_author=Toledano M.B.; citation_journal_title=J. Biol. Chem.; citation_year=2001; citation_volume=276; citation_pages=7011-7016; " /><meta name="citation_reference" content="citation_title=Glutathione is an important antioxidant molecule in the yeast Saccharomyces cerevisiae; citation_author=Stephen W.S.; citation_author=Jamieson S.D.; citation_journal_title=FEMS Lett.; citation_year=1996; citation_volume=141; citation_pages=207-212; " /><meta name="citation_reference" content="citation_title=Isolation of glutathione-dependent mutants of the yeast Saccharomyces cerevisiae; citation_author=Kistler M.; citation_author=Summer K.H.; citation_author=Eckardt F.; citation_journal_title=Mutat. Res.; citation_year=1986; citation_volume=173; citation_pages=117-120; " /><meta name="citation_reference" content="citation_title=The essential and ancillary role of glutathione in Saccharomyces cerevisiae analysed using a grande gsh1 disruptant strain; citation_author=Lee J.C.; citation_author=Straffon M.J.; citation_author=Jang T.Y.; citation_author=Higgins V.J.; citation_author=Grant C.M.; citation_author=Dawes I.W.; citation_journal_title=FEMS Yeast Res.; citation_year=2001; citation_volume=1; citation_pages=57-65; " /><meta name="citation_reference" content="citation_title=Biochemical basis of oxidative protein folding in the endoplasmic reticulum; citation_author=Tu B.P.; citation_author=Ho-Schleyer S.C.; citation_author=Travers K.J.; citation_author=Weissman J.S.; citation_journal_title=Science; citation_year=2000; citation_volume=290; citation_pages=1571-1574; " /><meta name="citation_reference" content="citation_title=Glutathione synthetase is dispensable for growth under both normal and oxidative stress conditions in the yeast Saccharomyces cerevisiae due to the accumulation of the dipeptide γ-glutamylcysteine; citation_author=Grant C.M.; citation_author=MacIver F.H.; citation_author=Dawes I.W.; citation_journal_title=Mol. Biol. Cell; citation_year=1997; citation_volume=8; citation_pages=1699-1707; " /><meta name="citation_reference" content="citation_title=The glutathione-dependent glyoxalase pathway in the yeast Saccharomyces cerevisiae. A vital defence line against methylglyoxal produced during glycerol catabolism; citation_author=Penninckx M.J.; citation_author=Jaspers Ch.; citation_author=Legrain M.; citation_journal_title=J. Biol. Chem.; citation_year=1983; citation_volume=258; citation_pages=6030-6036; " /><meta name="citation_reference" content="citation_title=Glutathione metabolism in plants; citation_author=Bergmann L.; citation_author=Rennenberg H.; citation_author=de Kok L.J.; citation_author=Stulen I.; citation_author=Rennenberg H.; citation_author=Brunold C.; citation_author=Rauser W.; citation_publisher=SPB Academic, The Hague; citation_title=Sulfur Nutrition and Assimilation in Higher Plants. Regulatory, agricultural and environmental aspects; citation_year=1993; citation_pages=102-123; " /><meta name="citation_reference" content="citation_title=Pathways of glutathione degradation in the yeast Saccharomyces cerevisiae; citation_author=Jaspers Ch.J.; citation_author=Gigot D.; citation_author=Penninckx M.J.; citation_journal_title=Phytochemistry; citation_year=1985; citation_volume=24; citation_pages=703-707; " /><meta name="citation_reference" content="citation_title=The amino acid sequence of rat kidney 5-oxo-l-prolinase determined by cDNA cloning; citation_author=Guo J.; citation_author=Breslow E.; citation_author=Meister A.; citation_journal_title=J. Biol. Chem.; citation_year=1996; citation_volume=271; citation_pages=32293-32300; " /><meta name="citation_reference" content="citation_title=Synthesis and role of glutathione in protection against oxidative stress in yeast; citation_author=Grant C.M.; citation_author=Dawes I.; citation_journal_title=Redox Rep.; citation_year=1996; citation_volume=2; citation_pages=223-229; " /><meta name="citation_reference" content="citation_title=Yap1 and Skn7 control two specialized oxidative stress response regulons in yeast; citation_author=Lee J.; citation_author=Godon C.; citation_author=Lagniel G.; citation_author=Spector D.; citation_author=Garin J.; citation_author=Labarre J.; citation_author=Toledano M.B.; citation_journal_title=J. Biol. Chem.; citation_year=1999; citation_volume=274; citation_pages=16040-16046; " /><meta name="citation_reference" content="citation_title=Roles of glutathione and thioredoxin-dependent reduction systems in the Escherichia coli and Saccharomyces cerevisiae responses to oxidative stress; citation_author=Carmel-Harel O.; citation_author=Storz G.; citation_journal_title=Annu. Rev. Microbiol.; citation_year=2000; citation_volume=54; citation_pages=439-461; " /><meta name="citation_reference" content="citation_title=Molecular identification of glutathione synthetase (GSH2) gene from Saccharomyces cerevisiae; citation_author=Inoue Y.; citation_author=Sugiyama K.; citation_author=Izawa S.; citation_author=Kimura A.; citation_journal_title=Biochim. Biophys. Acta; citation_year=1998; citation_volume=1395; citation_pages=315-320; " /><meta name="citation_reference" content="citation_title=Glutathione metabolism in relation to the amino acid permeation systems in the yeast Saccharomyces cerevisiae; citation_author=Penninckx M.J.; citation_author=Jaspers Ch.J.; citation_author=Wiame J.M.; citation_journal_title=Eur. J. Biochem.; citation_year=1980; citation_volume=104; citation_pages=119-123; " /><meta name="citation_reference" content="citation_title=γ-Glutamyltranspeptidase in the yeast Saccharomyces cerevisiae and its role in the vacuolar transport and metabolism of glutathione; citation_author=Mehdi K.; citation_author=Thierie J.; citation_author=Penninckx M.J.; citation_journal_title=Biochem. J.; citation_year=2001; citation_volume=359; citation_pages=631-637; " /><meta name="citation_reference" content="citation_title=γ-Glutamyltranspeptidase: catalytical, structural and functional aspects; citation_author=Tate S.; citation_author=Meister A.; citation_journal_title=Mol. Cell. Biochem.; citation_year=1981; citation_volume=39; citation_pages=357-368; " /><meta name="citation_reference" content="citation_title=DNA sequence of the Escherichia coli K-12 γ-glutamyltranspeptidase gene, ggt; citation_author=Suzuki H.; citation_author=Kumagai H.; citation_author=Echigo T.; citation_author=Tochikura T.; citation_journal_title=J. Bacteriol.; citation_year=1989; citation_volume=171; citation_pages=5169-5172; " /><meta name="citation_reference" content="citation_title=membrane protein sorting: biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase; citation_author=Klionsky D.J.; citation_author=Emer S.D.; citation_journal_title=EMBO J.; citation_year=1989; citation_volume=8; citation_pages=2241-2250; " /><meta name="citation_reference" content="citation_title=Glutathione metabolism in yeast Saccharomyces cerevisiae. Evidence that γ-glutamyltranspeptidase is a vacuolar enzyme; citation_author=Jaspers Ch.; citation_author=Penninckx M.J.; citation_journal_title=Biochimie; citation_year=1984; citation_volume=66; citation_pages=71-74; " /><meta name="citation_reference" content="citation_title=Biosynthesis and function of yeast vacuolar proteases; citation_author=Van Den Hazel H.B.; citation_author=Kielland-Brandt M.C.; citation_author=Winther J.; citation_journal_title=Yeast; citation_year=1996; citation_volume=12; citation_pages=1-16; " /><meta name="citation_reference" content="citation_title=Brush border membrane hydrolysis of S-benzyl-cysteine-p-nitroanilide, and activity of aminopeptidase M; citation_author=Rankin B.B.; citation_author=McIntyre T.; citation_author=Curthoys T.; citation_journal_title=Biochem. Biophys. Res. Commun.; citation_year=1980; citation_volume=96; citation_pages=991-996; " /><meta name="citation_reference" content="citation_title=Renal catabolism of glutathione; citation_author=Mc Intyre T.; citation_author=Curthoys N.P.; citation_journal_title=J. Biol. Chem.; citation_year=1982; citation_volume=257; citation_pages=11915-11921; " /><meta name="citation_reference" content="citation_title=γ-Glutamyltranspeptidase is not involved in the bulk uptake of amino acids, peptides or γ-glutamyl amino acids in the yeast Saccharomyces cerevisiae; citation_author=Payne G.M.; citation_author=Payne J.W.; citation_journal_title=Biochem. J.; citation_year=1984; citation_volume=218; citation_pages=147-151; " /><meta name="citation_reference" content="citation_title=Import and metabolism of glutathione in Streptococcus mutans; citation_author=Sherrill C.; citation_author=Fahey R.C.; citation_journal_title=J. Bacteriol.; citation_year=1998; citation_volume=180; citation_pages=1454-1459; " /><meta name="citation_reference" content="citation_title=Glutathione transport in human small intestine epithelial cells; citation_author=Iantomasi T.; citation_author=Favilli F.; citation_author=Marriani P.; citation_author=Magaldi T.; citation_author=Bruni P.; citation_author=Vincenzini M.T.; citation_journal_title=Biochim. Biophys. Acta; citation_year=1997; citation_volume=1330; citation_pages=274-283; " /><meta name="citation_reference" content="citation_title=Glutathione transport systems of the budding yeast Saccharomyces cerevisiae; citation_author=Miyake T.; citation_author=Hazu T.; citation_author=Yoshida S.; citation_author=Kanayama M.; citation_author=Tomochika K.; citation_author=Shinoda S.; citation_author=Ono B.; citation_journal_title=Biosci. Biotechnol. Biochem.; citation_year=1998; citation_volume=62; citation_pages=1858-1864; " /><meta name="citation_reference" content="citation_title=Hgt1p, a high affinity glutathione transporter from the yeast Saccharomyces cerevisiae; citation_author=Bourbouloux A.; citation_author=Shahi P.; citation_author=Chakladar A.; citation_author=Delrot S.; citation_author=Bachhawat A.K.; citation_journal_title=J. Biol. Chem.; citation_year=2000; citation_volume=275; citation_pages=13259-13265; " /><meta name="citation_reference" content="citation_title=The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugates pump; citation_author=Li Z.S.; citation_author=Szczypka M.; citation_author=Lu Y.P.; citation_author=Thiele D.J.; citation_author=Rea P.A.; citation_journal_title=J. Biol. Chem.; citation_year=1996; citation_volume=271; citation_pages=6509-6517; " /><meta name="citation_reference" content="citation_title=ATP-dependent transport of reduced glutathione on YCF1, the yeast orthologue of mammalian multidrug resistance associated proteins; citation_author=Rebbeor J.F.; citation_author=Connolly G.C.; citation_author=Dumont M.E.; citation_author=Ballatori N.; citation_journal_title=J. Biol. Chem.; citation_year=1998; citation_volume=273; citation_pages=33449-33454; " /><meta name="citation_reference" content="citation_title=Glutathione as an endogenous sulfur source in the yeast Saccharomyces cerevisiae; citation_author=Elskens M.T.; citation_author=Jaspers C.J.; citation_author=Penninckx M.J.; citation_journal_title=J. Gen. Microbiol.; citation_year=1991; citation_volume=137; citation_pages=637-644; " /><meta name="citation_reference" content="citation_title=Role of the sulphate assimilation pathway in utilization of glutathione as a sulphur source by Saccharomyces cerevisiae; citation_author=Miyake T.; citation_author=Sammoto H.; citation_author=Kanayama M.; citation_author=Tomochika K.; citation_author=Shinoda S.; citation_author=Ono B.; citation_journal_title=Yeast; citation_year=1999; citation_volume=15; citation_pages=1449-1457; " /><meta name="citation_reference" content="citation_title=Identification and characterization of genes induced during sexual differentiation in Schizosaccharomyces pombe; citation_author=Sato S.; citation_author=Suzuki H.; citation_author=Widyastuti U.; citation_author=Hotta Y.; citation_author=Tabata S.; citation_journal_title=Curr. Genet.; citation_year=1994; citation_volume=26; citation_pages=31-37; " /><meta name="citation_reference" content="citation_title=The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway; citation_author=Piper R.C.; citation_author=Bryant N.J.; citation_author=Stevens T.C.; citation_journal_title=J. Cell. Biol.; citation_year=1997; citation_volume=138; citation_pages=531-545; " /><meta name="citation_reference" content="citation_title=A comprehensive two-hybrid analysis to explore the yeast protein interactome; citation_author=Ito T.; citation_author=Chiba T.; citation_author=Ozawa R.; citation_author=Yoshida M.; citation_author=Hattori M.; citation_author=Sakaki Y.; citation_journal_title=Proc. Natl. Acad. Sci. USA; citation_year=2001; citation_volume=98; citation_pages=4569-4574; " /><meta name="citation_reference" content="citation_title=Isolation and characterization of glutathione-deficient mutants of the methylotrophic yeast Hansenula polymorpha; citation_author=Ubiivovk V.M.; citation_author=Telegus Y.V.; citation_author=Sibirniy A.; citation_journal_title=Microbiologiya (Moscow); citation_year=1999; citation_volume=68; citation_pages=26-31; " /><meta name="citation_reference" content="citation_title=Reactions of direct formaldehyde oxidation to CO2 are non-essential for energy supply of yeast methylotrophic growth; citation_author=Sibirniy A.; citation_author=Ubiivovk V.M.; citation_author=Gonchar M.V.; citation_author=Titorenko V.I.; citation_author=Voronovsky A.Y.; citation_author=Kapultsevich Y.G.; citation_author=Bliznik K.M.; citation_journal_title=Arch. Microbiol.; citation_year=1990; citation_volume=154; citation_pages=566-575; " /><meta name="citation_reference" content="citation_title=Glutathione peroxidase in yeast. Presence of the enzyme and induction by oxidative conditions; citation_author=Galiazzo F.; citation_author=Schiesser A.; citation_author=Rotilio G.; citation_journal_title=Biochem. Biophys. Res. Commun.; citation_year=1987; citation_volume=147; citation_pages=1200-1205; " /><meta name="citation_reference" content="citation_title=Oxidative stress response in Hansenula mrakii: a new type of glutathione peroxidase in yeast; citation_author=Inoue Y.; citation_author=Kimura A.; citation_journal_title=Recent Res. Dev. Agric. Biol. Chem.; citation_year=1998; citation_volume=2; citation_pages=29-39; " /><meta name="citation_reference" content="citation_title=Antioxidant system within yeast peroxisome. Biochemical and physiological characterization of CbPmp20 in the methylotrophic yeast Candida boidinii; citation_author=Horiguchi H.; citation_author=Yurimoto H.; citation_author=Kato N.; citation_author=Sakai Y.; citation_journal_title=J. Biol. Chem.; citation_year=2001; citation_volume=276; citation_pages=14279-14288; " /><meta name="citation_reference" content="citation_title=Genetic analysis of glutathione peroxidase in oxidative stress response of Saccharomyces cerevisiae; citation_author=Inoue Y.; citation_author=Matsuda T.; citation_author=Sugiyama K.; citation_author=Izawa S.; citation_author=Kimura A.; citation_journal_title=J. Biol. Chem.; citation_year=1999; citation_volume=274; citation_pages=27002-27009; " /><meta name="citation_reference" content="citation_title=Saccharomyces cerevisiae expresses three phospholipid hydroperoxide glutathione peroxidases; citation_author=Avery A.M.; citation_author=Avery S.V.; citation_journal_title=J. Biol. Chem.; citation_year=2001; citation_volume=276; citation_pages=33730-33735; " /><meta name="citation_reference" content="citation_title=Thioredoxin; citation_author=Holmgren A.; citation_journal_title=Annu. Rev. Biochem.; citation_year=1985; citation_volume=54; citation_pages=237-271; " /><meta name="citation_reference" content="citation_title=The Yap1p-dependent induction of glutathione synthesis in heat shock response of Saccharomyces cerevisiae; citation_author=Sugiyama K.; citation_author=Izawa S.; citation_author=Inoue Y.; citation_journal_title=J. Biol. Chem.; citation_year=2000; citation_volume=275; citation_pages=15535-15540; " /><meta name="citation_reference" content="citation_title=Adaptative response of Schizosaccharomyces pombe to hydrogen peroxide and menadione; citation_author=Lee J.; citation_author=Dawes I.W.; citation_author=Roe J.H.; citation_journal_title=Microbiology; citation_year=1995; citation_volume=141; citation_pages=3127-3132; " /><meta name="citation_reference" content="citation_title=Schizosaccharomyces pombe homologue of glutathione peroxidase, which does not contain selenocysteine, is induced by several stresses and works as an antioxidant; citation_author=Yamada K.; citation_author=Nakagawa C.W.; citation_author=Mutoh N.; citation_journal_title=Yeast; citation_year=1999; citation_volume=15; citation_pages=1125-1132; " /><meta name="citation_reference" content="citation_title=Use of a simplex technique and contour diagrams for the determination of the reaction rate constant between glutathione and thiram in the presence of NADPH; citation_author=Elskens M.; citation_author=Penninckx M.J.; citation_author=Vandeloise R.; citation_author=Vander Donckt E.; citation_journal_title=Int. J. Chem. Kinet.; citation_year=1988; citation_volume=20; citation_pages=837-848; " /><meta name="citation_reference" content="citation_title=Interconversion of thiram and dimethyldithiocarbamic acid in Saccharomyces cerevisiae: a plausible metabolic pathway under the control of the glutathione redox cycle; citation_author=Elskens M.; citation_author=Penninckx M.J.; citation_journal_title=Appl. Environ. Microbiol.; citation_year=1997; citation_volume=63; citation_pages=2857-2862; " /><meta name="citation_reference" content="citation_title=Transport of glutathione-S-conjugates in the yeast Saccharomyces cerevisiae; citation_author=Zadzinski R.; citation_author=Maszewski J.; citation_author=Bartosz G.; citation_journal_title=Cell Biol. Int.; citation_year=1996; citation_volume=20; citation_pages=325-330; " /><meta name="citation_reference" content="citation_title=Global response of Saccharomyces cerevisiae to an alkylating agent; citation_author=Jelinsky S.A.; citation_author=Samson L.D.; citation_journal_title=Proc. Natl. Acad. Sci. USA; citation_year=1999; citation_volume=96; citation_pages=1486-1491; " /><meta name="citation_reference" content="citation_title=Pathways of As(III) detoxification in Saccharomyces cerevisiae; citation_author=Ghosh M.; citation_author=Shen J.; citation_author=Rosen B.P.; citation_journal_title=Proc. Natl. Acad. Sci. USA; citation_year=1999; citation_volume=96; citation_pages=5001-5006; " /><meta name="citation_reference" content="citation_title=Phytochelatins; citation_author=Rauser W.E.; citation_journal_title=Annu. Rev. Biochem.; citation_year=1990; citation_volume=59; citation_pages=61-86; " /><meta name="citation_reference" content="citation_title=Phytochelatins and related peptides. Structure, biosynthesis and function; citation_author=Rauser W.E.; citation_journal_title=Plant Physiol.; citation_year=1995; citation_volume=109; citation_pages=1141-1149; " /><meta name="citation_reference" content="citation_title=Heavy metal tolerance in the fission yeast requires an ATP-binding cassette-type vacuolar membrane transporter; citation_author=Ortiz D.E.; citation_author=Kreppel L.; citation_author=Speiser D.M.; citation_author=Scheel G.; citation_author=McDonald G.; citation_author=Ow D.M.; citation_journal_title=EMBO J.; citation_year=1992; citation_volume=11; citation_pages=3491-3499; " /><meta name="citation_reference" content="citation_title=The role of glutathione biosynthesis in heavy metal resistance in the fission yeast Schizosaccharomyces pombe; citation_author=Coblenz A.; citation_author=Wolf K.; citation_journal_title=FEMS Microbiol. Rev.; citation_year=1994; citation_volume=14; citation_pages=303-308; " /><meta name="citation_reference" content="citation_title=Phytochelatin synthase genes from Arabidopsis and the yeast Schizosaccharomyces pombe; citation_author=Ha S.B.; citation_author=Smith A.P.; citation_author=Howden R.; citation_author=Dietrich W.M.; citation_author=Bugg S.; citation_author=O' Connel M.J.; citation_author=Goldsbrough P.B.; citation_author=Cobbet C.S.; citation_journal_title=Plant Cell; citation_year=1999; citation_volume=11; citation_pages=1153-1164; " /><meta name="citation_reference" content="citation_title=Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast; citation_author=Clemens S.; citation_author=Kim E.J.; citation_author=Neumann D.; citation_author=Schroeder J.I.; citation_journal_title=EMBO J.; citation_year=1999; citation_volume=18; citation_pages=3325-3333; " /><meta name="citation_reference" content="citation_title=biosynthesis of phytochelatins in the fission yeast. Phytochelatin synthesis: a second role for the glutathione synthetase gene of Schizosaccharomyces pombe; citation_author=Al-Lahham A.; citation_author=Rohde V.; citation_author=Heim P.; citation_author=Leuchter R.; citation_author=Veeck J.; citation_author=Wunderlich C.; citation_author=Wolf K.; citation_author=Zimmermann M.; citation_journal_title=Yeast; citation_year=1999; citation_volume=15; citation_pages=385-396; " /><meta name="citation_reference" content="citation_title=A new pathway for vacuolar cadmium sequestration in Saccharomyces cerevisiae: YCF1-catalysed transport of bis (glutathionato) cadmium; citation_author=Li Z.S.; citation_author=Lu Y.P.; citation_author=Zhen R.G.; citation_author=Szczypka M.; citation_author=Thiele D.J.; citation_author=Rea P.A.; citation_journal_title=Proc. Natl. Acad. Sci. USA; citation_year=1997; citation_volume=94; citation_pages=42-47; " /><meta name="citation_reference" content="citation_title=A proteome analysis of the cadmium response in Saccharomyces cerevisiae; citation_author=Vido K.; citation_author=Spector D.; citation_author=Lagniel G.; citation_author=Lopez S.; citation_author=Toledano M.B.; citation_author=Labarre J.; citation_journal_title=J. Biol. Chem.; citation_year=2001; citation_volume=276; citation_pages=8469-8474; " /><meta name="citation_reference" content="citation_title=Cadmium-inducible expression of the yeast GSH1 gene requires a functional sulfur-amino acid regulatory network; citation_author=Dormer U.H.; citation_author=Westwater J.; citation_author=McLaren N.F.; citation_author=Kent N.A.; citation_author=Mellor J.; citation_author=Jamieson D.; citation_journal_title=J. Biol. Chem.; citation_year=2000; citation_volume=275; citation_pages=32611-32616; " /><meta name="citation_reference" content="citation_title=Glutathione levels during thermal induction of the yeast to mycelial transition in Candida albicans; citation_author=Thomas D.; citation_author=Klein K.; citation_author=Manavathu E.; citation_author=Dimmock J.R.; citation_author=Mutus B.; citation_journal_title=FEMS Microbiol. Lett.; citation_year=1991; citation_volume=77; citation_pages=31-334; " /><meta name="citation_reference" content="citation_title=Changes in glutathione metabolic enzymes during yeast to mycelium conversion of Candida albicans; citation_author=Manavathu M.; citation_author=Gunasekaran S.; citation_author=Porte Q.; citation_author=Manavathu E.; citation_author=Gunasekaran M.; citation_journal_title=Can. J. Microbiol.; citation_year=1996; citation_volume=42; citation_pages=76-79; " /><meta name="citation_reference" content="citation_title=Glutathione metabolism and dimorphism in Aureobasidium pullulans; citation_author=Würtz-Jürgensen C.; citation_author=Raun Jacobsen N.; citation_author=Emri T.; citation_author=Havn Eriksen S.; citation_author=Pocsi I.; citation_journal_title=J. Basic Microbiol.; citation_year=2001; citation_volume=41; citation_pages=131-137; " /><meta name="citation_reference" content="citation_author=Griffin D.M.; citation_publisher=Chapman and Hall, London; citation_title=Ecology of Soil Fungi; citation_year=1972; " /><meta name="citation_fulltext_world_readable" content="" /><meta name="citation_pdf_url" content="https://academic.oup.com/femsyr/article-pdf/2/3/295/17937459/2-3-295.pdf" /><meta name="description" content="Abstract. Glutathione (GSH: l-γ-glutamyl-l-cysteinylglycine) is present in high concentrations up to 10 mM in yeast cells. Its very low redox potential (E′" /><meta name="citation_xml_url" content="https://academic.oup.com/femsyr/article-xml/2/3/295/562518" /> <link rel="canonical" href="https://academic.oup.com/femsyr/article/2/3/295/562518" /> <meta name="product_code" content="femsyr_oa_flip_archive_free" /> <meta name="product_code" content="femsyr_FBI_12m" /> <meta name="product_code" content="J_FEMSYR_2001_01_168" /> <meta name="product_code" content="J_FEMSYR_2001_01_9999" /> <meta name="product_code" content="FREE_NEW" /> <meta name="product_code" content="J_femsyr_2001_01_216" /> <meta name="product_code" content="j_ALLJOURNALS" /> <meta name="product_code" content="J_femsyr_2001_01_240" /> <meta name="product_code" content="SOLR_FACET_FREE" /> <meta name="product_code" content="J_562518" /> <meta name="product_code" content="I_22564" /> <script> var SCM = SCM || {}; SCM.pubGradeAdsEnabled = true; SCM.pubGradeJSLibrary = 'https://cdn.pbgrd.com/core-oup-new.js'; </script> <script async="async" src="https://securepubads.g.doubleclick.net/tag/js/gpt.js"></script> <script> var googletag = googletag || {}; googletag.cmd = googletag.cmd || []; </script> <script type='text/javascript'> var gptAdSlots = []; googletag.cmd.push(function() { var mapping_ad1 = googletag.sizeMapping() .addSize([1024, 0], [[970, 90], [728, 90]]) .addSize([768, 0], [728, 90]) .addSize([0, 0], [320, 50]) .build(); gptAdSlots["ad1"] = googletag.defineSlot('/116097782/femsyr_Behind_Ad1', [[970, 90], [728, 90], [320, 50]], 'adBlockHeader') .defineSizeMapping(mapping_ad1) .addService(googletag.pubads()); var mapping_ad2 = googletag.sizeMapping() .addSize([768, 0], [[300, 250], [300, 600], [160, 600]]) .build(); gptAdSlots["ad2"] = googletag.defineSlot('/116097782/femsyr_Behind_Ad2', [[300, 250], [160, 600], [300, 600]], 'adBlockMainBodyTop') .defineSizeMapping(mapping_ad2) .addService(googletag.pubads()); var mapping_ad3 = googletag.sizeMapping() .addSize([768, 0], [[300, 250], [300, 600], [160, 600]]) .build(); gptAdSlots["ad3"] = googletag.defineSlot('/116097782/femsyr_Behind_Ad3', [[300, 250], [160, 600], [300, 600]], 'adBlockMainBodyBottom') .defineSizeMapping(mapping_ad3) .addService(googletag.pubads()); var mapping_ad4 = googletag.sizeMapping() .addSize([0,0], [320, 50]) .addSize([768, 0], [728, 90]) .build(); gptAdSlots["ad4"] = googletag.defineSlot('/116097782/femsyr_Behind_Ad4', [728, 90], 'adBlockFooter') .defineSizeMapping(mapping_ad4) .addService(googletag.pubads()); var mapping_ad6 = googletag.sizeMapping() .addSize([1024, 0], [[970, 90], [728, 90]]) .addSize([768, 0], [728, 90]) .addSize([0, 0], [320, 50]) .build(); gptAdSlots["ad6"] = googletag.defineSlot('/116097782/femsyr_Behind_Ad6', [[728, 90], [970, 90]], 'adBlockStickyFooter') .defineSizeMapping(mapping_ad6) .addService(googletag.pubads()); gptAdSlots["adInterstitial"] = googletag.defineOutOfPageSlot('/116097782/femsyr_Interstitial_Ad', googletag.enums.OutOfPageFormat.INTERSTITIAL) .addService(googletag.pubads()); googletag.pubads().addEventListener('slotRenderEnded', function (event) { if (!event.isEmpty) { $('.js-' + event.slot.getSlotElementId()).each(function () { if ($(this).find('iframe').length) { $(this).removeClass('hide'); } }); } }); googletag.pubads().addEventListener('impressionViewable', function (event) { if (!event.isEmpty) { $('.js-' + event.slot.getSlotElementId()).each(function () { var $adblockDiv = $(this).find('.js-adblock'); var $adText = $(this).find('.js-adblock-advertisement-text'); if ($adblockDiv && $adblockDiv.is(':visible') && $adblockDiv.find('*').length > 1) { $adText.removeClass('hide'); App.CenterAdBlock.Init($adblockDiv, $adText); } else { $adText.addClass('hide'); } //Initialize logic for Sticky Footer Ad var $stickyFooterDiv = $(this).parents('.js-sticky-footer-ad'); if ($stickyFooterDiv && $stickyFooterDiv.is(':visible') && $stickyFooterDiv.find('*').length > 1) { App.StickyFooterAd.Init(); } }); } }); googletag.pubads().setTargeting("jnlspage", "article"); googletag.pubads().setTargeting("jnlsurl", "femsyr/article/2/3/295/562518"); googletag.pubads().enableSingleRequest(); googletag.pubads().disableInitialLoad(); googletag.pubads().collapseEmptyDivs(); }); </script> <input type="hidden" class="hfInterstitial" data-interstitiallinks="femsyr/issue,femsyr/advance-articles,femsyr/advance-article,femsyr/supplements,femsyr/article,femsyr/article-abstract,femsyr/pages" data-subdomain="femsyr" /> <script type="text/javascript"> googletag.cmd.push(function () { googletag.pubads().setTargeting("jnlsdoi", "10.1016/S1567-1356(02)00081-8"); googletag.enableServices(); }); </script> <script type="text/javascript"> var NTPT_PGEXTRA= 'event_type=full-text&supplier_tag=SC_Journals&object_type=Article&taxonomy=taxId%3a39%7ctaxLabel%3aAcademicSubjects%7cnodeId%3aSCI01150%7cnodeLabel%3aMicrobiology%7cnodeLevel%3a3&siteid=femsyr&authzrequired=false&doi=10.1016/S1567-1356(02)00081-8'; </script> <script src="https://scholar.google.com/scholar_js/casa.js" async></script> </head> <body data-sitename="femsyeastresearch" class="off-canvas pg_Article pg_article " theme-femsyr data-sitestyletemplate="Journal" > <noscript> <iframe src="https://www.googletagmanager.com/ns.html?id=GTM-W6DD7HV" height="0" width="0" style="display:none;visibility:hidden"></iframe> </noscript> <a href="#skipNav" class="skipnav">Skip to Main Content</a> <input id="hdnSiteID" name="hdnSiteID" type="hidden" value="5387" /><input id="hdnAdDelaySeconds" name="hdnAdDelaySeconds" type="hidden" value="5000" /><input id="hdnAdConfigurationTop" name="hdnAdConfigurationTop" type="hidden" value="scrolldelay" /><input id="hdnAdConfigurationRightRail" name="hdnAdConfigurationRightRail" type="hidden" value="sticky" /> <div class="master-container js-master-container"> <section class="master-header row js-master-header vt-site-page-header"> <div class="widget widget-SitePageHeader widget-instance-SitePageHeader"> <div class="ad-banner js-ad-banner-header"> <div class="widget widget-AdBlock widget-instance-HeaderAd"> <div class="js-adBlock-parent-wrap adblock-parent-wrap"> <div class="adBlockHeader-wrap js-adBlockHeader hide"> <div id="adBlockHeader" class="js-adblock at-adblock" data-lazy-load-margin="150"> <script> googletag.cmd.push(function () { googletag.display('adBlockHeader'); }); </script> </div> <div class="advertisement-text at-adblock js-adblock-advertisement-text hide">Advertisement</div> </div> </div> </div> </div> <div class="oup-header sigma "> <div class="center-inner-row"> <div class="oup-header-logo"> <a href="/"> <img src="//oup.silverchair-cdn.com/UI/app/svg/umbrella/oxford-academic-logo.svg" alt="Oxford Academic" class="oup-header-image at-oup-header-image " /> </a> </div> <div class="widget widget-CustomNavLinks widget-instance-CustomNavLinksDeskTop"> <div class="custom-nav-links-box"> <div class="custom-nav-link"> <a href="/journals">Journals</a> </div> <div class="custom-nav-link"> <a href="/books">Books</a> </div> </div> </div> <ul class="oup-header-menu account-menu sigma-account-menu "> <li class="oup-header-menu-item mobile"> <a href="javascript:;" class="mobile-dropdown-toggle mobile-search-toggle"> <i class="icon-menu_search"><span class="screenreader-text">Search Menu</span></i> </a> </li> <li class="oup-header-menu-item mobile info-icon-menu-item"> <a href="/pages/information" target="_blank" class="at-info-button sigma-info-wrapper" role="button"> <img class="sigma-info-icon" src="//oup.silverchair-cdn.com/UI/app/svg/i.svg" alt="Information" /> </a> </li> <li class="oup-header-menu-item mobile account-icon-menu-item"> <a href="javascript:;" class="account-button js-account-button at-account-button " role="button" data-turnawayparams="journal%3dfemsyr"> <img class="sigma-account-icon" src="//oup.silverchair-cdn.com/UI/app/svg/account.svg" alt="Account" /> </a> </li> <li class="oup-header-menu-item mobile"> <a href="javascript:;" class="mobile-dropdown-toggle mobile-nav-toggle"> <i class="icon-menu_hamburger"><span class="screenreader-text">Menu</span></i> </a> </li> <li class="oup-header-menu-item desktop info-icon-menu-item"> <a href="/pages/information" target="_blank" class="at-info-button sigma-info-wrapper" role="button"> <img class="sigma-info-icon" src="//oup.silverchair-cdn.com/UI/app/svg/i.svg" alt="Information" /> </a> </li> <li class="oup-header-menu-item desktop account-icon-menu-item"> <a href="javascript:;" class="account-button js-account-button at-account-button sigma-logo-wrapper" role="button" data-turnawayparams="journal%3dfemsyr"> <img class="sigma-account-icon" src="//oup.silverchair-cdn.com/UI/app/svg/account.svg" alt="Account" /> </a> </li> <li class="oup-header-menu-item desktop account-icon-menu-item"> <div class="widget widget-SeamlessAccess widget-instance-SitePageHeader"> <a href="javascript:;" class="js-shibboleth-action seamless-access-button seamless-button-header button-call-to-action at-institutional-sign-in" rel="nofollow" data-action-type="" data-entity-id=""> <span class="seamless-access-text">Sign in through your institution</span> </a> </div> </li> </ul> <div class="login-box-placeholder js-login-box-placeholder hide"> <div class="spinner"></div> </div> </div> </div> <div class="dropdown-panel-wrap"> <div class="dropdown-panel mobile-search-dropdown"> <div class="mobile-search-inner-wrap"> <div class="navbar-search"> <div class="mobile-microsite-search"> <label for="SitePageHeader-mobile-navbar-search-filter" class="screenreader-text js-mobile-navbar-search-filter-label"> Navbar Search Filter </label> <select class="mobile-navbar-search-filter js-mobile-navbar-search-filter at-navbar-search-filter" id="SitePageHeader-mobile-navbar-search-filter"> <option class="navbar-search-filter-option at-navbar-search-filter-option" value="">FEMS Yeast Research</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Issue">This issue</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Parent">FEMS Journals</option> <optgroup class="navbar-search-optgroup" label="Search across Oxford Academic"> <option class="navbar-search-filter-option at-navbar-search-filter-option" value="AcademicSubjects/SCI01150">Microbiology</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Books">Books</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Journals">Journals</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Umbrella">Oxford Academic</option> </optgroup> </select> <label for="SitePageHeader-mobile-microsite-search-term" class="screenreader-text js-mobile-microsite-search-term-label"> Mobile Enter search term </label> <input class="mobile-search-input mobile-microsite-search-term js-mobile-microsite-search-term at-microsite-search-term" type="text" maxlength="255" placeholder="Search" id="SitePageHeader-mobile-microsite-search-term"> <a href="javascript:;" class="mobile-microsite-search-icon mobile-search-submit icon-menu_search"> <span class="screenreader-text">Search</span> </a> </div> </div> </div> </div> <div class="dropdown-panel mobile-nav-dropdown"> <ul class="site-menu site-menu-lvl-0 at-site-menu"> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-1703788"> <a href="javascript:;" class="nav-link js-nav-dropdown at-nav-dropdown" role="button" aria-expanded="false"> Issues <i class="desktop-nav-arrow icon-general-arrow-filled-down arrow-icon"></i> </a> <i class="mobile-nav-arrow icon-general_arrow-down"></i> <ul class="site-menu site-menu-lvl-1 at-site-menu"> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-100"> <a href="/femsyr/issue/volume/24/" class="nav-link"> Volume 24, 2024 (In Progress) </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-101"> <a href="/femsyr/issue/volume/23/" class="nav-link"> Volume 23, 2023 </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-102"> <a href="/femsyr/issue/volume/24/" class="nav-link"> Browse all </a> </li> </ul> </li> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-1703784"> <a href="javascript:;" class="nav-link js-nav-dropdown at-nav-dropdown" role="button" aria-expanded="false"> More Content <i class="desktop-nav-arrow icon-general-arrow-filled-down arrow-icon"></i> </a> <i class="mobile-nav-arrow icon-general_arrow-down"></i> <ul class="site-menu site-menu-lvl-1 at-site-menu"> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703789"> <a href="/femsyr/advance-articles" class="nav-link"> Advance articles </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703790"> <a href="/femsyr/pages/editors-choice" class="nav-link"> Editor's Choice </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703791"> <a href="/femsyr/pages/thematic_issues" class="nav-link"> Thematic Issues </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703792"> <a href="/femsyr/pages/virtual_issues_" class="nav-link"> Virtual Special Issues </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703793"> <a href="/femsyr/search-results?allJournals=1&f_TocHeadingTitleList=research+articlesANDResearch+articleANDArticles&fl_SiteID=5387&page=1&sort=Date+%e2%80%93+Newest+First" class="nav-link"> Research Articles </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703794"> <a href="https://academic.oup.com/femsyr/search-results?sort=Date+%e2%80%93+Newest+First&allJournals=1&f_TocHeadingTitleList=MinireviewANDMinireviews&fl_SiteID=5387&page=1" class="nav-link"> Minireviews </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703795"> <a href="https://academic.oup.com/femsyr/search-results?sort=Date+%e2%80%93+Newest+First&allJournals=1&f_TocHeadingTitleList=Retrospective&fl_SiteID=5387&page=1" class="nav-link"> Retrospectives </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703796"> <a href="https://academic.oup.com/femsyr/search-results?sort=Date+%e2%80%93+Newest+First&allJournals=1&f_TocHeadingTitleList=Protocol&fl_SiteID=5387&page=1" class="nav-link"> Protocols </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703797"> <a href="https://academic.oup.com/femsyr/search-results?sort=Date+%e2%80%93+Newest+First&allJournals=1&f_TocHeadingTitleList=Editorial&fl_SiteID=5387&page=1" class="nav-link"> Editorials </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703798"> <a href="https://fems-microbiology.org/opportunities/abstracts-from-the-international-conference-on-yeast-genetics-and-molecular-biology-icygmb/" class="nav-link"> Yeast Conference Abstracts </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703799"> <a href="https://fems-microbiology.org/about_fems/network-and-activities/awards/" class="nav-link"> Awards & Prizes </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703800"> <a href="https://academic.oup.com/fems-journals/pages/webinars" class="nav-link"> Webinars </a> </li> </ul> </li> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-1703785"> <a href="javascript:;" class="nav-link js-nav-dropdown at-nav-dropdown" role="button" aria-expanded="false"> FEMS Journals <i class="desktop-nav-arrow icon-general-arrow-filled-down arrow-icon"></i> </a> <i class="mobile-nav-arrow icon-general_arrow-down"></i> <ul class="site-menu site-menu-lvl-1 at-site-menu"> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703801"> <a href="/fems-journals" class="nav-link"> FEMS Journals </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703802"> <a href="/femsec" class="nav-link"> FEMS Microbiology Ecology </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703803"> <a href="/femsle" class="nav-link"> FEMS Microbiology Letters </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703804"> <a href="/femsre" class="nav-link"> FEMS Microbiology Reviews </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703805"> <a href="/femspd" class="nav-link"> Pathogens and Disease </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703806"> <a href="/femsmicrobes" class="nav-link"> FEMS Microbes </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703807"> <a href="/microlife" class="nav-link"> microLife </a> </li> </ul> </li> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-1703786"> <a href="javascript:;" class="nav-link js-nav-dropdown at-nav-dropdown" role="button" aria-expanded="false"> Submit <i class="desktop-nav-arrow icon-general-arrow-filled-down arrow-icon"></i> </a> <i class="mobile-nav-arrow icon-general_arrow-down"></i> <ul class="site-menu site-menu-lvl-1 at-site-menu"> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703808"> <a href="/femsyr/pages/Manuscript_Preparation" class="nav-link"> Author Guidelines </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703809"> <a href="http://mc.manuscriptcentral.com/femsyr" class="nav-link"> Submission Site </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703810"> <a href="/femsyr/pages/Manuscript_Preparation#COPYRIGHT AND LICENCE INCLUDING OPEN ACCESS" class="nav-link"> Open Access </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703811"> <a href="https://academic.oup.com/fems-journals/pages/policies" class="nav-link"> Policies </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703812"> <a href="/femsyr/pages/call-for-papers" class="nav-link"> Calls for Papers </a> </li> </ul> </li> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-1703787"> <a href="javascript:;" class="nav-link js-nav-dropdown at-nav-dropdown" role="button" aria-expanded="false"> About <i class="desktop-nav-arrow icon-general-arrow-filled-down arrow-icon"></i> </a> <i class="mobile-nav-arrow icon-general_arrow-down"></i> <ul class="site-menu site-menu-lvl-1 at-site-menu"> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703813"> <a href="http://academic.oup.com/femsyr/pages/About" class="nav-link"> About FEMS Yeast Research </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703814"> <a href="http://fems-microbiology.org/about/" class="nav-link"> About the Federation of European Microbiological Societies </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703815"> <a href="/femsyr/pages/Editorial_Board" class="nav-link"> Editorial Board </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703816"> <a href="https://academic.oup.com/advertising-and-corporate-services/pages/femsyr-media-kit" class="nav-link"> Advertising and Corporate Services </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703817"> <a href="https://academic.oup.com/fems-journals/pages/policies" class="nav-link"> Policies </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703818"> <a href="https://academic.oup.com/pages/self_archiving_policy_c" class="nav-link"> Self-Archiving Policy </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703819"> <a href="https://fems-microbiology.org/contact/" class="nav-link"> Contact Us </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703820"> <a href="/my-account/email-alerts" class="nav-link"> Alerts </a> </li> </ul> </li> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-custom"> <a href="/journals" class="nav-link">Journals on Oxford Academic</a> </li> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-custom"> <a href="/books" class="nav-link">Books on Oxford Academic</a> </li> </ul> </div> </div> <div class="journal-header journal-bg"> <div class="center-inner-row"> <div class="site-parent-link-wrap"> <a href="//academic.oup.com/fems-journals" class="site-parent-link">FEMS Journals</a> </div> <a href="/femsyr" class="journal-logo-container"> <img id="logo-FEMSYeastResearch" class="journal-logo" src="//oup.silverchair-cdn.com/data/SiteBuilderAssets/Live/Images/femsyr/femsyr_title1568517285.svg" alt="FEMS Yeast Research" /> </a> <div class="society-logo-block"> <div class="society-block-inner-wrap"> <a href="http://www.fems-microbiology.org/" target="" class="society-logo-container"> <img id="logo-FederationofEuropeanMicrobiologicalSocieties" class="society-logo" src="//oup.silverchair-cdn.com/data/SiteBuilderAssets/Live/Images/femsyr/femsyr_h1-12939081.svg" alt="Federation of European Microbiological Societies" /> </a> </div> </div> </div> </div> <div class="navbar"> <div class="center-inner-row"> <nav class="navbar-menu"> <ul class="site-menu site-menu-lvl-0 at-site-menu"> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-1703788"> <a href="javascript:;" class="nav-link js-nav-dropdown at-nav-dropdown" role="button" aria-expanded="false"> Issues <i class="desktop-nav-arrow icon-general-arrow-filled-down arrow-icon"></i> </a> <i class="mobile-nav-arrow icon-general_arrow-down"></i> <ul class="site-menu site-menu-lvl-1 at-site-menu"> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-100"> <a href="/femsyr/issue/volume/24/" class="nav-link"> Volume 24, 2024 (In Progress) </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-101"> <a href="/femsyr/issue/volume/23/" class="nav-link"> Volume 23, 2023 </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-102"> <a href="/femsyr/issue/volume/24/" class="nav-link"> Browse all </a> </li> </ul> </li> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-1703784"> <a href="javascript:;" class="nav-link js-nav-dropdown at-nav-dropdown" role="button" aria-expanded="false"> More Content <i class="desktop-nav-arrow icon-general-arrow-filled-down arrow-icon"></i> </a> <i class="mobile-nav-arrow icon-general_arrow-down"></i> <ul class="site-menu site-menu-lvl-1 at-site-menu"> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703789"> <a href="/femsyr/advance-articles" class="nav-link"> Advance articles </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703790"> <a href="/femsyr/pages/editors-choice" class="nav-link"> Editor's Choice </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703791"> <a href="/femsyr/pages/thematic_issues" class="nav-link"> Thematic Issues </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703792"> <a href="/femsyr/pages/virtual_issues_" class="nav-link"> Virtual Special Issues </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703793"> <a href="/femsyr/search-results?allJournals=1&f_TocHeadingTitleList=research+articlesANDResearch+articleANDArticles&fl_SiteID=5387&page=1&sort=Date+%e2%80%93+Newest+First" class="nav-link"> Research Articles </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703794"> <a href="https://academic.oup.com/femsyr/search-results?sort=Date+%e2%80%93+Newest+First&allJournals=1&f_TocHeadingTitleList=MinireviewANDMinireviews&fl_SiteID=5387&page=1" class="nav-link"> Minireviews </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703795"> <a href="https://academic.oup.com/femsyr/search-results?sort=Date+%e2%80%93+Newest+First&allJournals=1&f_TocHeadingTitleList=Retrospective&fl_SiteID=5387&page=1" class="nav-link"> Retrospectives </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703796"> <a href="https://academic.oup.com/femsyr/search-results?sort=Date+%e2%80%93+Newest+First&allJournals=1&f_TocHeadingTitleList=Protocol&fl_SiteID=5387&page=1" class="nav-link"> Protocols </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703797"> <a href="https://academic.oup.com/femsyr/search-results?sort=Date+%e2%80%93+Newest+First&allJournals=1&f_TocHeadingTitleList=Editorial&fl_SiteID=5387&page=1" class="nav-link"> Editorials </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703798"> <a href="https://fems-microbiology.org/opportunities/abstracts-from-the-international-conference-on-yeast-genetics-and-molecular-biology-icygmb/" class="nav-link"> Yeast Conference Abstracts </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703799"> <a href="https://fems-microbiology.org/about_fems/network-and-activities/awards/" class="nav-link"> Awards & Prizes </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703800"> <a href="https://academic.oup.com/fems-journals/pages/webinars" class="nav-link"> Webinars </a> </li> </ul> </li> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-1703785"> <a href="javascript:;" class="nav-link js-nav-dropdown at-nav-dropdown" role="button" aria-expanded="false"> FEMS Journals <i class="desktop-nav-arrow icon-general-arrow-filled-down arrow-icon"></i> </a> <i class="mobile-nav-arrow icon-general_arrow-down"></i> <ul class="site-menu site-menu-lvl-1 at-site-menu"> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703801"> <a href="/fems-journals" class="nav-link"> FEMS Journals </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703802"> <a href="/femsec" class="nav-link"> FEMS Microbiology Ecology </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703803"> <a href="/femsle" class="nav-link"> FEMS Microbiology Letters </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703804"> <a href="/femsre" class="nav-link"> FEMS Microbiology Reviews </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703805"> <a href="/femspd" class="nav-link"> Pathogens and Disease </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703806"> <a href="/femsmicrobes" class="nav-link"> FEMS Microbes </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703807"> <a href="/microlife" class="nav-link"> microLife </a> </li> </ul> </li> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-1703786"> <a href="javascript:;" class="nav-link js-nav-dropdown at-nav-dropdown" role="button" aria-expanded="false"> Submit <i class="desktop-nav-arrow icon-general-arrow-filled-down arrow-icon"></i> </a> <i class="mobile-nav-arrow icon-general_arrow-down"></i> <ul class="site-menu site-menu-lvl-1 at-site-menu"> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703808"> <a href="/femsyr/pages/Manuscript_Preparation" class="nav-link"> Author Guidelines </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703809"> <a href="http://mc.manuscriptcentral.com/femsyr" class="nav-link"> Submission Site </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703810"> <a href="/femsyr/pages/Manuscript_Preparation#COPYRIGHT AND LICENCE INCLUDING OPEN ACCESS" class="nav-link"> Open Access </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703811"> <a href="https://academic.oup.com/fems-journals/pages/policies" class="nav-link"> Policies </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703812"> <a href="/femsyr/pages/call-for-papers" class="nav-link"> Calls for Papers </a> </li> </ul> </li> <li class="site-menu-item site-menu-lvl-0 at-site-menu-item" id="site-menu-item-1703787"> <a href="javascript:;" class="nav-link js-nav-dropdown at-nav-dropdown" role="button" aria-expanded="false"> About <i class="desktop-nav-arrow icon-general-arrow-filled-down arrow-icon"></i> </a> <i class="mobile-nav-arrow icon-general_arrow-down"></i> <ul class="site-menu site-menu-lvl-1 at-site-menu"> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703813"> <a href="http://academic.oup.com/femsyr/pages/About" class="nav-link"> About FEMS Yeast Research </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703814"> <a href="http://fems-microbiology.org/about/" class="nav-link"> About the Federation of European Microbiological Societies </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703815"> <a href="/femsyr/pages/Editorial_Board" class="nav-link"> Editorial Board </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703816"> <a href="https://academic.oup.com/advertising-and-corporate-services/pages/femsyr-media-kit" class="nav-link"> Advertising and Corporate Services </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703817"> <a href="https://academic.oup.com/fems-journals/pages/policies" class="nav-link"> Policies </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703818"> <a href="https://academic.oup.com/pages/self_archiving_policy_c" class="nav-link"> Self-Archiving Policy </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703819"> <a href="https://fems-microbiology.org/contact/" class="nav-link"> Contact Us </a> </li> <li class="site-menu-item site-menu-lvl-1 at-site-menu-item" id="site-menu-item-1703820"> <a href="/my-account/email-alerts" class="nav-link"> Alerts </a> </li> </ul> </li> </ul> </nav> <div class="navbar-search-container js-navbar-search-container"> <a href="javascript:;" class="navbar-search-close js_close-navsearch">Close</a> <div class="navbar-search"> <div class="microsite-search"> <label for="SitePageHeader-navbar-search-filter" class="screenreader-text js-navbar-search-filter-label"> Navbar Search Filter </label> <select class="navbar-search-filter js-navbar-search-filter at-navbar-search-filter" id="SitePageHeader-navbar-search-filter"> <option class="navbar-search-filter-option at-navbar-search-filter-option" value="">FEMS Yeast Research</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Issue">This issue</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Parent">FEMS Journals</option> <optgroup class="navbar-search-optgroup" label="Search across Oxford Academic"> <option class="navbar-search-filter-option at-navbar-search-filter-option" value="AcademicSubjects/SCI01150">Microbiology</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Books">Books</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Journals">Journals</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Umbrella">Oxford Academic</option> </optgroup> </select> <label for="SitePageHeader-microsite-search-term" class="screenreader-text js-microsite-search-term-label"> Enter search term </label> <input class="navbar-search-input microsite-search-term js-microsite-search-term at-microsite-search-term" type="text" maxlength="255" placeholder="Search" id="SitePageHeader-microsite-search-term"> <a href="javascript:;" class="microsite-search-icon navbar-search-submit icon-menu_search"> <span class="screenreader-text">Search</span> </a> </div> </div> <input id="hfCurrentBookSearch" name="hfCurrentBookSearch" type="hidden" value="" /><input id="hfCurrentBookScope" name="hfCurrentBookScope" type="hidden" value="CurrentBook" /><input id="hfBookSiteScope" name="hfBookSiteScope" type="hidden" value="Books" /><input id="hfSeriesScope" name="hfSeriesScope" type="hidden" value="taxWithOr" /><input id="hfParentSiteName" name="hfParentSiteName" type="hidden" value="FEMS Journals" /><input id="hfParentSiteUrl" name="hfParentSiteUrl" type="hidden" value="academic.oup.com/fems-journals" /><input id="hfSiteID" name="hfSiteID" type="hidden" value="5387" /><input id="hfParentSiteID" name="hfParentSiteID" type="hidden" value="5543" /><input id="hfJournalSiteScope" name="hfJournalSiteScope" type="hidden" value="Journals" /><input id="hfParentSiteScope" name="hfParentSiteScope" type="hidden" value="Parent" /><input id="hfDefaultSearchURL" name="hfDefaultSearchURL" type="hidden" value="search-results?page=1&q=" /><input id="hfIssueSearch" name="hfIssueSearch" type="hidden" value="&fl_IssueID=22564" /><input id="hfIssueSiteScope" name="hfIssueSiteScope" type="hidden" value="Issue" /><input id="hfUmbrellaScope" name="hfUmbrellaScope" type="hidden" value="Umbrella" /><input id="hfUmbrellaSiteUrl" name="hfUmbrellaSiteUrl" type="hidden" value="academic.oup.com" /><input id="hfUmbrellaSiteId" name="hfUmbrellaSiteId" type="hidden" value="191" /><input id="hfDefaultAdvancedSearchUrl" name="hfDefaultAdvancedSearchUrl" type="hidden" value="advanced-search?page=1&q=" /><input id="hfTaggedCollectionScope" name="hfTaggedCollectionScope" type="hidden" value="" /> <div class="navbar-search-advanced"><a href="/femsyr/advanced-search" class="advanced-search js-advanced-search">Advanced Search</a></div> </div> <div class="navbar-search-collapsed"><a href="javascript:;" class="icon-menu_search js_expand-navsearch"><span class="screenreader-text">Search Menu</span></a></div> </div> </div> <input type="hidden" name="searchScope" id="hfSolrJournalID" value="" /> <input type="hidden" id="hfSolrJournalName" value="" /> <input type="hidden" id="hfSolrMaxAllowSearchChar" value="100" /> <input type="hidden" id="hfJournalShortName" value="" /> <input type="hidden" id="hfSearchPlaceholder" value="" /> <input type="hidden" name="hfGlobalSearchSiteURL" id="hfGlobalSearchSiteURL" value="" /> <input type="hidden" name="hfSearchSiteURL" id="hfSiteURL" value="academic.oup.com/femsyr" /> <input type="hidden" name="RedirectSiteUrl" id="RedirectSiteUrl" value="httpszazjzjacademiczwoupzwcom" /> <script type="text/javascript"> (function () { var hfSiteUrl = document.getElementById('hfSiteURL'); var siteUrl = hfSiteUrl.value; var subdomainIndex = siteUrl.indexOf('/'); hfSiteUrl.value = location.host + (subdomainIndex >= 0 ? siteUrl.substring(subdomainIndex) : ''); })(); </script> <input id="routename" name="RouteName" type="hidden" value="femsyr" /> </div> </section> <div class="widget widget-SitewideBanner widget-instance-"> </div> <div id="main" class="content-main js-main ui-base"> <section class="master-main row"> <div class="center-inner-row no-overflow"> <div id="skipNav" tabindex="-1"></div> <div class="page-column-wrap"> <div id="InfoColumn" class="page-column page-column--left js-left-nav-col"> <div class="mobile-content-topbar hide"> <button class="toggle-left-col toggle-left-col__article">Article Navigation</button> </div> <div class="info-inner-wrap js-left-nav"> <button class="toggle-left-col__close btn-as-icon icon-general-close"> <span class="screenreader-text">Close mobile search navigation</span> </button> <div class="responsive-nav-title">Article Navigation</div> <div class="info-widget-wrap"> <div class="widget widget-IssueInfo widget-instance-OUP_IssueInfo_Article"> <div id="issueInfo-OUP_IssueInfo_Article" class="article-info-wrap clearfix"> <i class="icon-general-close mobile-nav-btn nav-open"></i> <a class="article-issue-link" href="/femsyr/issue/2/3"> <div class="article-issue-img"> <img id="issueImage" class="fb-featured-image" src="https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/Issue/2/3/0/m_femsyr2_3.cover.gif?Expires=1736287804&Signature=FiOFg0xbnK~vTVf82ofPVsBi01dp3PL2FBg1E8aNykwNDuPz78-B8GcfPXSM9~1pGg2BVR2Rj9fjxMIyNCtudgr0fOC8vUKF1L8BEyLvHJZiq0nLI3j3kHHgZhzJrdvDdCeSdoKk5G8-lgIRxiT5gCbfMaMS81x-NWuh1hK94XHvKJY8OvxNVTPpPW9AJ5Fo6dZZ3gR1LB4AJvNvHPVQAMexZPIiiZ05F~75TZx3fxoKWwYgZ6C5g6uRr~DgEDlaGS2P6mZlHuqcfZGv0bhdt41P0oUzWv4rSMJdRhvrniso6z4wyBul71DysNgSsNnO1WQVl39cyXjF4LZL~TSz1A__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" alt="Issue Cover" /> </div> <div class="article-issue-info"> <div class="volume-issue__wrap"> <div class="volume trailing-comma">Volume 2</div> <div class="issue">Issue 3</div> </div> <div class="ii-pub-date"> August 2002 </div> </div> </a> </div> </div> <div class="content-nav"> <div class="widget widget-ArticleJumpLinks widget-instance-OUP_ArticleJumpLinks_Widget"> <h3 class="contents-title" >Article Contents</h3> <ul class="jumplink-list js-jumplink-list"> <li class="section-jump-link head-1" link-destination="89588898"> <div class="section-jump-link__link-wrap"> <a class="js-jumplink scrollTo" href="#89588898">Abstract</a> </div> </li> <li class="section-jump-link head-1" link-destination="89588900"> <div class="section-jump-link__link-wrap"> <a class="js-jumplink scrollTo" href="#89588900">1 Introduction</a> </div> </li> <li class="section-jump-link head-1" link-destination="89588903"> <div class="section-jump-link__link-wrap"> <a class="js-jumplink scrollTo" href="#89588903">2 A general survey on properties and metabolic functions of GSH</a> </div> </li> <li class="section-jump-link head-1" link-destination="89588909"> <div class="section-jump-link__link-wrap"> <a class="js-jumplink scrollTo" href="#89588909">3 Glutathione metabolism and transport in yeasts</a> </div> </li> <li class="section-jump-link head-1" link-destination="89588940"> <div class="section-jump-link__link-wrap"> <a class="js-jumplink scrollTo" href="#89588940">4 Main roles of GSH in S. cerevisiae and NCY</a> </div> </li> <li class="section-jump-link head-1" link-destination="89589022"> <div class="section-jump-link__link-wrap"> <a class="js-jumplink scrollTo" href="#89589022">5 Concluding remarks</a> </div> </li> <li class="section-jump-link head-1" link-destination="89589032"> <div class="section-jump-link__link-wrap"> <a class="js-jumplink scrollTo" href="#89589032">Acknowledgements</a> </div> </li> <li class="section-jump-link head-1 backReferenceLink" link-destination="89589035"> <div class="section-jump-link__link-wrap"> <a class="js-jumplink scrollTo" href="#89589035">References</a> </div> </li> </ul> </div> </div> <div class="widget widget-ArticleNavLinks widget-instance-OUP_ArticleNavLinks_Article"> <ul class="inline-list"> <li class="prev arrow"> <a href="/femsyr/article/2/3/293/562515">< Previous</a> </li> <li class="next arrow"> <a href="/femsyr/article/2/3/307/562606">Next ></a> </li> </ul> </div> </div> </div> </div> <div class="sticky-toolbar js-sticky-toolbar"></div> <div id="ContentColumn" class="page-column page-column--center"> <div class="article-browse-top article-browse-mobile-nav js-mobile-nav"> <div class="article-browse-mobile-nav-inner js-mobile-nav-inner"> <button class="toggle-left-col toggle-left-col__article btn-as-link"> Article Navigation </button> </div> </div> <div class="article-browse-top article-browse-mobile-nav mobile-sticky-toolbar js-mobile-nav-sticky"> <div class="article-browse-mobile-nav-inner"> <button class="toggle-left-col toggle-left-col__article btn-as-link"> Article Navigation </button> </div> </div> <div class="content-inner-wrap"> <div class="widget widget-ArticleTopInfo widget-instance-OUP_ArticleTop_Info_Widget"> <div class="module-widget article-top-widget"> <div class="access-state-logos all-viewports"> <span class="journal-info__format-label">Journal Article</span> </div> <div class="widget-items"> <div class="title-wrap"> <h1 class="wi-article-title article-title-main accessible-content-title at-articleTitle"> An overview on glutathione in <em>Saccharomyces</em> versus non-conventional yeasts <i class='icon-availability_free' title='Free' ></i> </h1> </div> <div class="wi-authors at-ArticleAuthors"> <div class="al-authors-list"> <span class="al-author-name-more js-flyout-wrap"> <button type="button" class="linked-name js-linked-name-trigger btn-as-link">Michel J Penninckx</button><span class='delimiter'></span> <span class="al-author-info-wrap arrow-up"> <div class="info-card-author authorInfo_OUP_ArticleTop_Info_Widget"> <div class="name-role-wrap"> <div class="info-card-name"> Michel J Penninckx <span class="info-card-footnote"><span class="xrefLink" id="jumplink-cor1"></span><a href="javascript:;" reveal-id="cor1" data-open="cor1" class="link link-ref link-reveal xref-default"></a></span> </div> </div> <div class="info-card-affilitation"> <div class="aff">Université Libre de Bruxelles, Laboratory of Microbial Physiology and Ecology, c/o Pasteur Institute, 642, Rue Engeland, B-1180 Brussels, Belgium</div> </div> <div class="info-author-correspondence"> <div content-id="cor1"><span class="label title-label">*</span>Tel.: +32 (2) 3733303; Fax: +32 (2) 3733309, <em>E-mail address</em>: <a href="mailto:upemulb@resulb.ulb.ac.be" target="_blank">upemulb@resulb.ulb.ac.be</a></div> </div> <div class="info-card-search-label"> Search for other works by this author on: </div> <div class="info-card-search info-card-search-internal"> <a href="/femsyr/search-results?f_Authors=Michel+J+Penninckx" rel="nofollow">Oxford Academic</a> </div> <div class="info-card-search info-card-search-pubmed"> <a href="http://www.ncbi.nlm.nih.gov/pubmed?cmd=search&term=Penninckx M">PubMed</a> </div> <div class="info-card-search info-card-search-google"> <a href="http://scholar.google.com/scholar?q=author:%22Penninckx Michel J%22">Google Scholar</a> </div> </div> </span> </span> </div> </div> <div class="pub-history-wrap clearfix js-history-dropdown-wrap"> <div class="pub-history-row clearfix"> <div class="ww-citation-primary"><em>FEMS Yeast Research</em>, Volume 2, Issue 3, August 2002, Pages 295–305, <a href='https://doi.org/10.1016/S1567-1356(02)00081-8'>https://doi.org/10.1016/S1567-1356(02)00081-8</a></div> </div> <div class="pub-history-row clearfix"> <div class="ww-citation-date-wrap"> <div class="citation-label">Published:</div> <div class="citation-date">01 August 2002</div> </div> <a href="javascript:;" class="history-label js-history-dropdown-trigger st-article-history at-ArticleHistory"> <span>Article history</span><i class="icon-general-arrow-filled-down arrow-icon"></i> </a> </div> <div class="ww-history js-history-entries-wrap at-history-entries-wrap"> <div class="history-entry at-history-entry"> <div class="wi-state">Received:</div> <div class="wi-date">18 October 2001</div> </div> <div class="history-entry at-history-entry"> <div class="wi-state">Revision received:</div> <div class="wi-date">01 March 2002</div> </div> <div class="history-entry at-history-entry"> <div class="wi-state">Accepted:</div> <div class="wi-date">12 March 2002</div> </div> <div class="history-entry at-history-entry"> <div class="wi-state">Published:</div> <div class="wi-date">01 August 2002</div> </div> </div> </div> </div> </div> <script> $(document).ready(function () { $('.article-top-widget').on('click', '.ati-toggle-trigger', function () { $(this).find('.icon-general-add, .icon-minus').toggleClass('icon-minus icon-general-add'); $(this).siblings('.ati-toggle-content').toggleClass('hide'); }); // In Chrome, an anchor tag with target="_blank" and a "mailto:" href opens a new tab/window as well as the email client // I suspect this behavior will be corrected in the future // Remove the target="_blank" $('ul.wi-affiliationList').find('a[href^="mailto:"]').each(function () { $(this).removeAttr('target'); }); }); </script> </div> <div class="widget widget-ArticleLinks widget-instance-OUP_Article_Links_Widget"> </div> <div class="article-body js-content-body"> <div class="toolbar-wrap js-toolbar-wrap"> <div class="toolbar-inner-wrap"> <ul id="Toolbar" role="navigation"> <li class="toolbar-item item-pdf js-item-pdf "> <a class="al-link pdf article-pdfLink" data-article-id="562518" href="/femsyr/article-pdf/2/3/295/17937459/2-3-295.pdf"> <img src=//oup.silverchair-cdn.com/UI/app/svg/pdf.svg alt="pdf" /><span class="pdf-link-text">PDF</span> </a> </li> <li class="toolbar-item item-link item-split-view"> <a href="javascript:;" class="split-view js-split-view st-split-view at-split-view" target=""> <i class="icon-menu-split"></i> Split View </a> </li> <li class="toolbar-item item-with-dropdown item-views"> <a class="at-views-dropdown drop-trigger" href="javascript:;" data-dropdown="FilterDrop" aria-haspopup="true"> <i class="icon-menu_views"></i> <div class="toolbar-label"> <div class="toolbar-text">Views</div> <i class="icon-general-arrow-filled-down arrow-icon"></i> </div> </a> <ul id="ViewsDrop" class="f-dropdown js-dropdown-content" data-dropdown-content aria-label="submenu"> <div class="arrow-up"></div> <li class="article-content-filter js-article-content-filter" data-content-filter="article-content"> <a href="javascript:;"><span>Article contents</span></a> </li> <li class="at-figures-tables article-content-filter js-article-content-filter" data-content-filter="figures-tables"> <a href="javascript:;"><span>Figures & tables</span></a> </li> <li class="article-content-filter js-article-content-filter" data-content-filter="video"> <a href="javascript:;"><span>Video</span></a> </li> <li class="article-content-filter js-article-content-filter" data-content-filter="audio"> <a href="javascript:;"><span>Audio</span></a> </li> <li class="article-content-filter js-article-content-filter" data-content-filter="supplementary-data"> <a href="javascript:;"><span>Supplementary Data</span></a> </li> </ul> </li> <li class="toolbar-item item-cite js-item-cite"> <div class="widget widget-ToolboxGetCitation widget-instance-OUP_Get_Citation"> <a href="#" class="js-cite-button at-CiteButton" data-reveal-id="getCitation" data-reveal> <i class="icon-read-more"></i> <span>Cite</span> </a> <div id="getCitation" class="reveal-modal js-citation-modal" data-reveal> <h3 class="modal-title">Cite</h3> <div class="oxford-citation-text"> <p>Michel J Penninckx, An overview on glutathione in <em>Saccharomyces</em> versus non-conventional yeasts, <em>FEMS Yeast Research</em>, Volume 2, Issue 3, August 2002, Pages 295–305, <a href="https://doi.org/10.1016/S1567-1356(02)00081-8">https://doi.org/10.1016/S1567-1356(02)00081-8</a></p> </div> <div class="citation-download-wrap"> <form action="/Citation/Download" method="get" id="citationModal"> <input type="hidden" name="resourceId" value="562518" /> <input type="hidden" name="resourceType" value="3" /> <label for="selectFormat" class="hide js-citation-format-label">Select Format</label> <select required name="citationFormat" class="citation-download-format js-citation-format" id="selectFormat"> <option selected disabled >Select format</option> <option value="0" >.ris (Mendeley, Papers, Zotero)</option> <option value="1" >.enw (EndNote)</option> <option value="2" >.bibtex (BibTex)</option> <option value="3" >.txt (Medlars, RefWorks)</option> </select> <button class="btn citation-download-link disabled" type="submit">Download citation</button> </form> </div> <a class="close-reveal-modal" href="javascript:;"><i class="icon-general-close"></i><span class="screenreader-text">Close</span></a> </div> </div> </li> <li class="toolbar-item item-tools"> <div class="widget widget-ToolboxPermissions widget-instance-OUP_Get_Permissions"> <div class="module-widget"> <a href="https://s100.copyright.com/AppDispatchServlet?publisherName=OUP&publication=1567-1364&title=An%20overview%20on%20glutathione%20in%20%26lt%3Bem%26gt%3BSaccharomyces%26lt%3B%2Fem%26gt%3B%20versus%20non-conventional%20yeasts&publicationDate=2002-08-01&volumeNum=2&issueNum=3&author=Penninckx%2C%20Michel%20J&startPage=295&endPage=305&contentId=10.1016%2FS1567-1356%2802%2900081-8&oa=&copyright=%C2%A9%202002%20Federation%20of%20European%20Microbiological%20Societies.%20Published%20by%20Elsevier%20Science%20B.V.%20All%20rights%20reserved.&orderBeanReset=True" id="PermissionsLink" class="" target="_blank" rel=nofollow> <i class="icon-menu_permissions"> <span class="screenreader-text">Permissions Icon</span> </i> Permissions </a> </div> </div> </li> <li class="toolbar-item item-with-dropdown item-share"> <a href="javascript:;" class="drop-trigger js-toolbar-dropdown at-ShareButton" data-dropdown="ShareDrop"> <i class="icon-menu_share"><span class="screenreader-text">Share Icon</span></i> <span class="toolbar-label"> <span class="toolbar-text">Share</span> <i class="arrow-icon icon-general-arrow-filled-down js-toolbar-arrow-icon"></i> </span> </a> <ul id="ShareDrop" class="addthis_toolbox addthis_default_style addthis_20x20_style f-dropdown js-dropdown-content" data-dropdown-content> <li> <a class="st-custom-button addthis_button_facebook js-share-link" data-network="facebook" data-title="overview on glutathione in Saccharomyces versus non-conventional yeasts" data-url="https://academic.oup.com/femsyr/article/2/3/295/562518" data-email-subject="overview on glutathione in Saccharomyces versus non-conventional yeasts" href="javascript:;" rel=nofollow><span>Facebook</span></a> </li> <li> <a class="st-custom-button addthis_button_twitter js-share-link" data-network="twitter" data-title="overview on glutathione in Saccharomyces versus non-conventional yeasts" data-url="https://academic.oup.com/femsyr/article/2/3/295/562518" data-email-subject="overview on glutathione in Saccharomyces versus non-conventional yeasts" href="javascript:;" rel=nofollow><span>Twitter</span></a> </li> <li> <a class="st-custom-button addthis_button_linkedin js-share-link" data-network="linkedin" data-title="overview on glutathione in Saccharomyces versus non-conventional yeasts" data-url="https://academic.oup.com/femsyr/article/2/3/295/562518" data-email-subject="overview on glutathione in Saccharomyces versus non-conventional yeasts" href="javascript:;" rel=nofollow><span>LinkedIn</span></a> </li> <li> <a class="st-custom-button addthis_button_email js-share-link" data-network="email" data-title="overview on glutathione in Saccharomyces versus non-conventional yeasts" data-url="https://academic.oup.com/femsyr/article/2/3/295/562518" data-email-subject="overview on glutathione in Saccharomyces versus non-conventional yeasts" href="javascript:;" rel=nofollow><span>Email</span></a> </li> </ul> </li> </ul> <div class="toolbar-search"> <div class="widget widget-SitePageHeader widget-instance-OUP_ArticleToolbarSearchBox"> <div class="dropdown-panel-wrap"> <div class="dropdown-panel mobile-search-dropdown"> <div class="mobile-search-inner-wrap"> <div class="navbar-search"> <div class="mobile-microsite-search"> <label for="OUP_ArticleToolbarSearchBox-mobile-navbar-search-filter" class="screenreader-text js-mobile-navbar-search-filter-label"> Navbar Search Filter </label> <select class="mobile-navbar-search-filter js-mobile-navbar-search-filter at-navbar-search-filter" id="OUP_ArticleToolbarSearchBox-mobile-navbar-search-filter"> <option class="navbar-search-filter-option at-navbar-search-filter-option" value="">FEMS Yeast Research</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Issue">This issue</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Parent">FEMS Journals</option> <optgroup class="navbar-search-optgroup" label="Search across Oxford Academic"> <option class="navbar-search-filter-option at-navbar-search-filter-option" value="AcademicSubjects/SCI01150">Microbiology</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Books">Books</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Journals">Journals</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Umbrella">Oxford Academic</option> </optgroup> </select> <label for="OUP_ArticleToolbarSearchBox-mobile-microsite-search-term" class="screenreader-text js-mobile-microsite-search-term-label"> Mobile Enter search term </label> <input class="mobile-search-input mobile-microsite-search-term js-mobile-microsite-search-term at-microsite-search-term" type="text" maxlength="255" placeholder="Search" id="OUP_ArticleToolbarSearchBox-mobile-microsite-search-term"> <a href="javascript:;" class="mobile-microsite-search-icon mobile-search-submit icon-menu_search"> <span class="screenreader-text">Search</span> </a> </div> </div> </div> </div> <div class="dropdown-panel mobile-nav-dropdown"> </div> </div> <div class="navbar"> <div class="center-inner-row"> <nav class="navbar-menu"> </nav> <div class="navbar-search-container js-navbar-search-container"> <a href="javascript:;" class="navbar-search-close js_close-navsearch">Close</a> <div class="navbar-search"> <div class="microsite-search"> <label for="OUP_ArticleToolbarSearchBox-navbar-search-filter" class="screenreader-text js-navbar-search-filter-label"> Navbar Search Filter </label> <select class="navbar-search-filter js-navbar-search-filter at-navbar-search-filter" id="OUP_ArticleToolbarSearchBox-navbar-search-filter"> <option class="navbar-search-filter-option at-navbar-search-filter-option" value="">FEMS Yeast Research</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Issue">This issue</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Parent">FEMS Journals</option> <optgroup class="navbar-search-optgroup" label="Search across Oxford Academic"> <option class="navbar-search-filter-option at-navbar-search-filter-option" value="AcademicSubjects/SCI01150">Microbiology</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Books">Books</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Journals">Journals</option><option class="navbar-search-filter-option at-navbar-search-filter-option" value="Umbrella">Oxford Academic</option> </optgroup> </select> <label for="OUP_ArticleToolbarSearchBox-microsite-search-term" class="screenreader-text js-microsite-search-term-label"> Enter search term </label> <input class="navbar-search-input microsite-search-term js-microsite-search-term at-microsite-search-term" type="text" maxlength="255" placeholder="Search" id="OUP_ArticleToolbarSearchBox-microsite-search-term"> <a href="javascript:;" class="microsite-search-icon navbar-search-submit icon-menu_search"> <span class="screenreader-text">Search</span> </a> </div> </div> <div class="navbar-search-advanced"><a href="/femsyr/advanced-search" class="advanced-search js-advanced-search">Advanced Search</a></div> </div> <div class="navbar-search-collapsed"><a href="javascript:;" class="icon-menu_search js_expand-navsearch"><span class="screenreader-text">Search Menu</span></a></div> </div> </div> <input id="routename" name="RouteName" type="hidden" value="femsyr" /> </div> </div> </div> </div> <div id="ContentTab" class="content active"> <div class="widget widget-ArticleFulltext widget-instance-OUP_Article_FullText_Widget"> <div class="module-widget"> <div class="widget-items" data-widgetname="ArticleFulltext"> <h2 scrollto-destination=89588898 id="89588898" class="abstract-title js-splitscreen-abstract-title" >Abstract</h2> <section class="abstract"><p class="chapter-para">Glutathione (GSH: <span class="small-caps">l</span>-γ-glutamyl-<span class="small-caps">l</span>-cysteinylglycine) is present in high concentrations up to 10 mM in yeast cells. Its very low redox potential (<em>E</em>′<sub>o</sub>=−240 mV for thiol disulfide exchange) gives this tripeptide the properties of a cellular redox buffer. In <em>Saccharomyces cerevisiae</em> and non-conventional yeasts (NCY), GSH may be involved in basic cellular functions such as the maintenance of mitochondrial and membrane integrity. GSH also assumes pivotal roles in (i) response to sulfur and nitrogen starvation; (ii) detoxification of endogenous toxic metabolites, such as excess formaldehyde produced during the growth of the methylotrophic yeasts <em>Hansenula polymorpha, Candida boidinii</em> and <em>Kloeckera</em> sp.; (iii) protection against oxidative stress provoked by exposure of the cells to reactive oxygen species including peroxides and hydroperoxides; (iv) detoxification of xenobiotics such as halogenated aromatics, alkylating agents and arsenite; (v) resistance to heavy-metal stress exemplified by the responses of <em>S. cerevisiae</em> and <em>Schizosaccharomyces pombe</em> to cadmium salts; (vi) yeast↔mycelium transition in <em>Candida</em> and <em>Aureobasidium</em> sp.</p></section> <div class="article-metadata-panel clearfix at-ArticleMetadata"></div> <div class="kwd-group"><a class="kwd-part kwd-main" href="javascript:;" data-keyword="Glutathione">Glutathione</a>, <a class="kwd-part kwd-main" href="javascript:;" data-keyword="Saccharomyces"><em>Saccharomyces</em></a>, <a class="kwd-part kwd-main" href="javascript:;" data-keyword=""Non-conventional yeast"">Non-conventional yeast</a>, <a class="kwd-part kwd-main" href="javascript:;" data-keyword=""Oxidative stress"">Oxidative stress</a>, <a class="kwd-part kwd-main" href="javascript:;" data-keyword=""Heavy-metal stress"">Heavy-metal stress</a>, <a class="kwd-part kwd-main" href="javascript:;" data-keyword="Detoxification">Detoxification</a></div> <h2 scrollto-destination=89588900 id="89588900" class="section-title js-splitscreen-section-title" data-legacy-id=ss1>1 Introduction</h2> <p class="chapter-para">Philothion was discovered 120 years ago in baker's yeast as a substance having the property of reducing elemental sulfur at room temperature [<span class="xrefLink" id="jumplink-b1"></span><a href="javascript:;" reveal-id="b1" data-open="b1" class="link link-ref link-reveal xref-bibr">1</a>]. Its correct structure was further assessed and the agent was renamed glutathione (GSH: <span class="small-caps">l</span>-γ-glutamyl-<span class="small-caps">l</span>-cysteinyl glycine). Research on GSH was very active in animal tissues [<span class="xrefLink" id="jumplink-b2"></span><a href="javascript:;" reveal-id="b2" data-open="b2" class="link link-ref link-reveal xref-bibr">2</a>], but until 20 years ago much less in plant and microbial cells [<span class="xrefLink" id="jumplink-b3"></span><a href="javascript:;" reveal-id="b3" data-open="b3" class="link link-ref link-reveal xref-bibr">3</a>,<span class="xrefLink" id="jumplink-b4"></span><a href="javascript:;" reveal-id="b4" data-open="b4" class="link link-ref link-reveal xref-bibr">4</a>]. However, the domain has progressed considerably in the last decade, especially in the case of <em>Saccharomyces cerevisiae</em>, where the new tools of molecular biology have permitted decisive advances [<span class="xrefLink" id="jumplink-b5"></span><a href="javascript:;" reveal-id="b5" data-open="b5" class="link link-ref link-reveal xref-bibr">5</a>].</p><p class="chapter-para">The biotechnology, food, and pharmaceutical industries employ many <em>Saccharomyces</em> but also non-<em>Saccharomyces</em> yeasts [<span class="xrefLink" id="jumplink-b6"></span><a href="javascript:;" reveal-id="b6" data-open="b6" class="link link-ref link-reveal xref-bibr">6</a>]. This already long and profitable association has created the necessity of a better understanding of metabolic peculiarities of non-conventional yeasts (NCY). For example GSH is implicated in a detoxification mechanism of formaldehyde produced during the growth of methylotrophic yeasts of the genera <em>Pichia, Hansenula</em> and <em>Candida</em>[<span class="xrefLink" id="jumplink-b7"></span><a href="javascript:;" reveal-id="b7" data-open="b7" class="link link-ref link-reveal xref-bibr">7</a>]. However, these strains, recognized as useful industrial platforms for single-cell protein production and heterologous gene expression [<span class="xrefLink" id="jumplink-b8"></span><a href="javascript:;" reveal-id="b8" data-open="b8" class="link link-ref link-reveal xref-bibr">8</a>], require more basic studies, in particular of the formaldehyde detoxification mechanism to be exploited more efficiently in industrial conditions. Thus it seems that study of GSH in NCY is not something of interest only to academic researchers, but also an indispensable step in opening up new and broader fields of application. It is the purpose of this review to attract attention to some important aspects of GSH, from investigators both of NCY and of conventional yeasts.</p> <h2 scrollto-destination=89588903 id="89588903" class="section-title js-splitscreen-section-title" data-legacy-id=ss2>2 A general survey on properties and metabolic functions of GSH</h2> <p class="chapter-para">GSH is present in high concentrations up to 10 mM in most living cells from prokaryotes to eukaryotes. Its very low redox potential (<em>E</em>′<sub>o</sub>=−240 mV for thiol disulfide exchange) and the fact that its reduced state is maintained by NADPH-dependent glutathione reductase give this tripeptide the properties of a cellular redox buffer [<span class="xrefLink" id="jumplink-b2"></span><a href="javascript:;" reveal-id="b2" data-open="b2" class="link link-ref link-reveal xref-bibr">2</a>]. Quite prophetically this property was already anticipated in the original papers of de Rey-Pahlade, the French discoverer of GSH [<span class="xrefLink" id="jumplink-b1"></span><a href="javascript:;" reveal-id="b1" data-open="b1" class="link link-ref link-reveal xref-bibr">1</a>]. In bacteria GSH occurs primarily in Gram-negative aerobic species but very rarely in anaerobes and Gram-positive strains [<span class="xrefLink" id="jumplink-b9"></span><a href="javascript:;" reveal-id="b9" data-open="b9" class="link link-ref link-reveal xref-bibr">9</a>]. GSH can occur under the reduced GSH form, the oxidized form GS-SG, and different mixed disulfides, for example GS-S-CoA and GS-S-Cys [<span class="xrefLink" id="jumplink-b2 b4"></span><a href="javascript:;" reveal-id="b2 b4" data-open="b2 b4" class="link link-ref link-reveal xref-bibr">2–4</a>,<span class="xrefLink" id="jumplink-b9"></span><a href="javascript:;" reveal-id="b9" data-open="b9" class="link link-ref link-reveal xref-bibr">9</a>]. Mycothiol (2-(<em>N</em>-acetylcysteinyl) amido-2-deoxy-α-<span class="small-caps">d</span>-glucopyranosyl-(1→1)-<em>myo</em>-inositol) is an alternative thiol produced by Gram-positive bacteria of the Actinomycetes lineage [<span class="xrefLink" id="jumplink-b10"></span><a href="javascript:;" reveal-id="b10" data-open="b10" class="link link-ref link-reveal xref-bibr">10</a>].</p><p class="chapter-para">The thiol moiety of GSH also has strong nucleophilic properties permitting its conjugation with electrophilic compounds, in particular xenobiotics [<span class="xrefLink" id="jumplink-b11"></span><a href="javascript:;" reveal-id="b11" data-open="b11" class="link link-ref link-reveal xref-bibr">11</a>]. The γ-glutamyl linkage present in GSH may confer on the tripeptide a privileged resistance to proteolytic action [<span class="xrefLink" id="jumplink-b2"></span><a href="javascript:;" reveal-id="b2" data-open="b2" class="link link-ref link-reveal xref-bibr">2</a>].</p><p class="chapter-para">There seems to be a connection between GSH and the aerobic style of life. High levels of GSH present in cyanobacteria and in purple photosynthetic bacteria point in favor of a bacterial emergence of GSH at a time when aerobic conditions became widespread on earth [<span class="xrefLink" id="jumplink-b9"></span><a href="javascript:;" reveal-id="b9" data-open="b9" class="link link-ref link-reveal xref-bibr">9</a>]. GSH could thus have appeared in the evolution as a protective agent against oxidative damages. The only reported phototrophic bacteria that tolerate oxygen without producing GSH are halobacteria, members of the Archaebacteria lineage. However, these strains produce large amounts of <span class="small-caps">l</span>-γ-glutamylcysteine and a disulfide reductase maintaining the dipeptide in its reduced state [<span class="xrefLink" id="jumplink-b12"></span><a href="javascript:;" reveal-id="b12" data-open="b12" class="link link-ref link-reveal xref-bibr">12</a>]. As far as has been reported, the presence of GSH in eukaryotes appears to be a general rule. Only primitive anaerobic protozoa where mitochondria are absent, e.g. <em>Entamoeba histolytica</em>, are lacking GSH [<span class="xrefLink" id="jumplink-b13"></span><a href="javascript:;" reveal-id="b13" data-open="b13" class="link link-ref link-reveal xref-bibr">13</a>]. Fahey and collaborators have suggested that endosymbiotic processes giving rise to mitochondria and chloroplasts might represent a plausible mechanism for acquisition of GSH in eukaryotes [<span class="xrefLink" id="jumplink-b13"></span><a href="javascript:;" reveal-id="b13" data-open="b13" class="link link-ref link-reveal xref-bibr">13</a>]. Whether GSH is really essential in yeast, in particular as a protective agent against oxidative stress, was debated. Previous experiments concluded that below a critical level corresponding to about 10% of the normal value of the cellular GSH pool, viability of <em>S. cerevisiae</em> was strongly impaired [<span class="xrefLink" id="jumplink-b14"></span><a href="javascript:;" reveal-id="b14" data-open="b14" class="link link-ref link-reveal xref-bibr">14</a>]. Mutants that lack a functional copy of <em>GSH1</em>, the structural gene governing production of <span class="small-caps">l</span>-γ-glutamate-<span class="small-caps">l</span>-cysteine ligase (γ-GCS), the first enzyme in GSH biosynthesis, are unable to synthesize the tripeptide and require exogenous GSH to survive and grow on minimal media. In addition, growth of the mutants can be restored with other thiols such as dithiothreitol, indicating that GSH is required as a reductant during normal growth conditions [<span class="xrefLink" id="jumplink-b15"></span><a href="javascript:;" reveal-id="b15" data-open="b15" class="link link-ref link-reveal xref-bibr">15</a>,<span class="xrefLink" id="jumplink-b16"></span><a href="javascript:;" reveal-id="b16" data-open="b16" class="link link-ref link-reveal xref-bibr">16</a>]. The <em>gsh1</em> mutants showed hypersensitivity to reactive oxygen species (ROS) including H<sub>2</sub>O<sub>2</sub>, superoxide anion and lipid hydroperoxides [<span class="xrefLink" id="jumplink-b17"></span><a href="javascript:;" reveal-id="b17" data-open="b17" class="link link-ref link-reveal xref-bibr">17</a>]. Growth of yeast strains deleted for <em>GSH1</em> was reported to be impossible on non-fermentable carbon sources, reflecting a significance of GSH for mitochondrial function [<span class="xrefLink" id="jumplink-b15"></span><a href="javascript:;" reveal-id="b15" data-open="b15" class="link link-ref link-reveal xref-bibr">15</a>,<span class="xrefLink" id="jumplink-b18"></span><a href="javascript:;" reveal-id="b18" data-open="b18" class="link link-ref link-reveal xref-bibr">18</a>]. Spector et al. [<span class="xrefLink" id="jumplink-b16"></span><a href="javascript:;" reveal-id="b16" data-open="b16" class="link link-ref link-reveal xref-bibr">16</a>] did not confirm these observations, which casts some doubt on the role of GSH in mitochondrial function. Recent studies with a grande <em>gsh1</em> deletant strain of <em>S. cerevisiae</em> conclude, however, that GSH is essential for mitochondrial genome integrity [<span class="xrefLink" id="jumplink-b19"></span><a href="javascript:;" reveal-id="b19" data-open="b19" class="link link-ref link-reveal xref-bibr">19</a>]. Quite interestingly it was reported in the same study that the intracellular GSH level needed to support growth was at least two orders of magnitude less than normally present in wild-type cells. This was also observed in anaerobic conditions, indicating that this essential function does not involve protection from oxidative stress. Discrepancies between the above-mentioned results might be in part explained by the different mitochondrial status of the strains used in these studies. Suppressors of the GSH auxotrophy of <em>gsh1</em> mutants were isolated [<span class="xrefLink" id="jumplink-b16"></span><a href="javascript:;" reveal-id="b16" data-open="b16" class="link link-ref link-reveal xref-bibr">16</a>]. The only reported suppressors of the lethal phenotype of a <em>gsh1</em> disruptant under both aerobic and anaerobic conditions were mutations of the proline biosynthetic pathway allowing production of a small amount of GSH via γ-glutamyl phosphate, the product of Pro1p. The data also indicate that the requirement for minute amounts of GSH in <em>S. cerevisiae</em> is not related to ribonucleotide reduction or to preventing toxic accumulation of non-native protein disulfide. In fact, it was shown that the oxidative protein folding in the endoplasmic reticulum of yeast is largely independent of GSH [<span class="xrefLink" id="jumplink-b20"></span><a href="javascript:;" reveal-id="b20" data-open="b20" class="link link-ref link-reveal xref-bibr">20</a>]. Disruptants of <em>GSH2</em>, the gene governing production of <span class="small-caps">l</span>-γ-glutamylcysteine-glycine-γ-ligase (GSH synthetase) accumulate the dipeptide γ-Glu-Cys, an intermediate in GSH biosynthesis [<span class="xrefLink" id="jumplink-b21"></span><a href="javascript:;" reveal-id="b21" data-open="b21" class="link link-ref link-reveal xref-bibr">21</a>]. However, the dipeptide could not fully substitute for the essential function of GSH in the cell as shown by the poor growth of the <em>gsh2</em> mutant on minimal medium. Possibly GSH might be involved in other essential cell functions, for example detoxification of harmful intermediates generated during normal cellular metabolism [<span class="xrefLink" id="jumplink-b21"></span><a href="javascript:;" reveal-id="b21" data-open="b21" class="link link-ref link-reveal xref-bibr">21</a>,<span class="xrefLink" id="jumplink-b22"></span><a href="javascript:;" reveal-id="b22" data-open="b22" class="link link-ref link-reveal xref-bibr">22</a>] or the integrity of the mitotic apparatus and/or other membrane systems [<span class="xrefLink" id="jumplink-b3"></span><a href="javascript:;" reveal-id="b3" data-open="b3" class="link link-ref link-reveal xref-bibr">3</a>].</p><p class="chapter-para"><span class="xrefLink" id="jumplink-f1"></span><a href="javascript:;" data-modal-source-id="f1" class="link xref-fig">Fig. 1</a> summarizes the interrelationship of GSH with cellular biochemical systems [<span class="xrefLink" id="jumplink-b3"></span><a href="javascript:;" reveal-id="b3" data-open="b3" class="link link-ref link-reveal xref-bibr">3</a>]. In living tissues, GSH assumes pivotal roles in bioreduction, protection against oxidative stress, detoxification of xenobiotics and endogenous toxic metabolites, transport, enzyme activity and sulfur and nitrogen metabolism. The present review has not the ambition to present an extensive account of GSH research but will cover some recent data relevant to <em>S. cerevisiae</em> and NCY.</p> <a id="89588908" scrollto-destination="89588908"></a> <div data-id="f1" data-content-id="f1" class="fig fig-section js-fig-section" swap-content-for-modal="true"><div class="graphic-wrap"><img class="content-image" src="https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/m_FYR_295_f1.jpeg?Expires=1736287804&Signature=OXxj2b4MH99FHnDMh-wYdMGMN~BvRnmj5OeCbhffK-6VIp4297daOXQK0JnQASX~5pgiv4SqBKX-EjwtnFT6DzlwCcPi2Q1A15nhwoH-Dj666lnTw7gtBbd2JkN5gvqahNRoFCL-WRELs9GLEVm4EH25fBuZi-0a8SNhsQ5KdPznWr89zGMHRvR3LzF~CYa9W6Y-o5sjJLdJhUKPfAaCxY2bbo-kvlt2HDLvs4JaywyygtNwqptXLp0z8ChHJychgACgRVcVXSv1xyqbER1lc5YpldhS3sNlBU6pHCPeWRYpc72bGjoNxyh-SbS88QjlQCYs8rzygA39D78nGo1evA__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" alt="The interrelationship of GSH with cellular biochemical systems [3]." data-path-from-xml="FYR_295_f1.jpeg" /><div class="graphic-bottom"><div class="label fig-label" id="label-89588908">1</div><div class="caption fig-caption"><p class="chapter-para">The interrelationship of GSH with cellular biochemical systems [<span class="xrefLink" id="jumplink-b3"></span><a href="javascript:;" reveal-id="b3" data-open="b3" class="link link-ref link-reveal xref-bibr">3</a>].</p></div><div class="ajax-articleAbstract-exclude-regex fig-orig original-slide figure-button-wrap"><a class="fig-view-orig js-view-large at-figureViewLarge openInAnotherWindow" role="button" aria-describedby="label-89588908" href="/view-large/figure/89588908/FYR_295_f1.jpeg" data-path-from-xml="FYR_295_f1.jpeg" target="_blank">Open in new tab</a><a class="download-slide" role="button" aria-describedby="label-89588908" data-section="89588908" href="/DownloadFile/DownloadImage.aspx?image=https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/FYR_295_f1.jpeg?Expires=1736287804&Signature=0wn75~uXH5NQUInBYtln83JdWfSpJstTn6FrsUgo8DzdWzGpko83CkQriEHiMHesAlcTvDooQDTbHQbL5sJjwrtwl6YcHUlNq9HwZQ82g9~y3LDzlM4mNbZkXMQ26BY0jFM2ihr-cIWmmWRYqV7lePfwfYlW8DPm0Lb7K8lTO2mFkF-t9XDvjndkjFFV4kV02uAyo41maLnvG14~xTVg-a~KoHzB1jlkazPNY~egyGivIGQ3hOaVUAN7IX4F~N5fjOju~uIYDbQGjExQ4gza6MAUnc0lJbzyv9Ep2Fibkj1ZR-yoMhSWpS3cqQktBJC4Mp-slVOcXH5-caBHPAvBnQ__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA&sec=89588908&ar=562518&xsltPath=~/UI/app/XSLT&imagename=&siteId=5387" data-path-from-xml="FYR_295_f1.jpeg">Download slide</a></div></div></div></div> <h2 scrollto-destination=89588909 id="89588909" class="section-title js-splitscreen-section-title" data-legacy-id=ss3>3 Glutathione metabolism and transport in yeasts</h2> <h3 scrollto-destination=89588910 id="89588910" class="section-title js-splitscreen-section-title" data-legacy-id=ss3-1>3.1 Outlines of biosynthesis and degradation of GSH in yeast. The γ-glutamyl cycle</h3> <p class="chapter-para">Several lines of evidence indicate that GSH metabolism proceeds in plant and animal cells through the γ-glutamyl cycle [<span class="xrefLink" id="jumplink-b2"></span><a href="javascript:;" reveal-id="b2" data-open="b2" class="link link-ref link-reveal xref-bibr">2</a>,<span class="xrefLink" id="jumplink-b23"></span><a href="javascript:;" reveal-id="b23" data-open="b23" class="link link-ref link-reveal xref-bibr">23</a>]. In its complete version the cycle accounts for six reactions (<span class="xrefLink" id="jumplink-f2"></span><a href="javascript:;" data-modal-source-id="f2" class="link xref-fig">Fig. 2</a>). Yet no evidence for the existence of a complete γ-glutamyl cycle in <em>S. cerevisiae</em> and NCY has been presented. Direct labelling experiments of intact yeast cells with [U-<sup>14</sup>C]GSH and [<sup>14</sup>C]5-oxoproline, have demonstrated the existence of a truncated version of the γ-glutamyl cycle [<span class="xrefLink" id="jumplink-b24"></span><a href="javascript:;" reveal-id="b24" data-open="b24" class="link link-ref link-reveal xref-bibr">24</a>]. In <em>S. cerevisiae</em>, GSH catabolism might thus be mediated only by γ-glutamyltranspeptidase and cysteinylglycine dipeptidase. However, inspection of the Proteome database revealed the presence in both <em>S. cerevisiae</em> and <em>Schizosaccharomyces pombe</em> of proteins having strong similarities (respectively 48.4 and 44% identity) with rat kidney 5-oxoprolinase [<span class="xrefLink" id="jumplink-b25"></span><a href="javascript:;" reveal-id="b25" data-open="b25" class="link link-ref link-reveal xref-bibr">25</a>]. This thus left open the question of the existence of an operative γ-glutamyl cycle in yeasts.</p> <a id="89588912" scrollto-destination="89588912"></a> <div data-id="f2" data-content-id="f2" class="fig fig-section js-fig-section" swap-content-for-modal="true"><div class="graphic-wrap"><img class="content-image" src="https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/m_FYR_295_f2.jpeg?Expires=1736287804&Signature=aYrFvkSoZ2LWrTG7Ikp6oItMBQZ0cRalzWF4o43xHUP030--qZfJXBEd6iN7U-4B76JTvxQY6MVXXdFfHUrQZb9DwrPaKQv-PvsyNpLfTVg76Ttd6e-bpr5Mz5qXdPiJrIW3l1aN4n2yu4dCg-pcyrlPZpBmW5p0G~QaGFErb3t9hKQTlisRv72aU201xQIh5lIT2vzpSdXP6OkxUOUOZobly88QCLtzBNeZ3kdqH7gZZ1YIsB2Rep7h3HoLt1VUxrit0874dxg85qarnOFMRZ2jaJm6q~4TF6ZKd~Oqb5ijfpuTGJbg47Szxhhur3XmSkkmGOrdigRhlN4xaTErXg__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" alt="The γ-glutamyl cycle [2]: (1) γ-glutamylcysteine synthetase; (2) GSH synthetase; (3) γ-glutamyltranspeptidase; (4) cysteinylglycine dipeptidase; (5) γ-glutamylcyclotransferase; (6) 5-oxoprolinase." data-path-from-xml="FYR_295_f2.jpeg" /><div class="graphic-bottom"><div class="label fig-label" id="label-89588912">2</div><div class="caption fig-caption"><p class="chapter-para">The γ-glutamyl cycle [<span class="xrefLink" id="jumplink-b2"></span><a href="javascript:;" reveal-id="b2" data-open="b2" class="link link-ref link-reveal xref-bibr">2</a>]: (1) γ-glutamylcysteine synthetase; (2) GSH synthetase; (3) γ-glutamyltranspeptidase; (4) cysteinylglycine dipeptidase; (5) γ-glutamylcyclotransferase; (6) 5-oxoprolinase.</p></div><div class="ajax-articleAbstract-exclude-regex fig-orig original-slide figure-button-wrap"><a class="fig-view-orig js-view-large at-figureViewLarge openInAnotherWindow" role="button" aria-describedby="label-89588912" href="/view-large/figure/89588912/FYR_295_f2.jpeg" data-path-from-xml="FYR_295_f2.jpeg" target="_blank">Open in new tab</a><a class="download-slide" role="button" aria-describedby="label-89588912" data-section="89588912" href="/DownloadFile/DownloadImage.aspx?image=https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/FYR_295_f2.jpeg?Expires=1736287804&Signature=IbcWEJEvLB2mXnl8DBT0YTBqR3JAqCGUsie2UadQqjldLKs01YJXAi~ipCJ4VFqRgVVrHa48JT~7gXF7KFrWzEiq0FtN~J1xX-b80Mo7zRAzpyICCuUoROcGcJXg8D6QKlqrbgI3lh3IwkGzspmfyfaNNMooYgtCJ4AExvOFAOgIvcx1fc8zJ-c89GAkbSJzNUShogOjvd4DmyQDT7HEoL8uB~eZFLG7iIf~VFCeu4UXXh9fs-yUSKm1gjonOFdOLJul330x25Nb1YJ2VE3R5S9bwANjQpsgdVvbOzxjyi8A3gswEURXJ-a6BLozfXHX5nGhnG7ex~0uXSiW4kfxLQ__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA&sec=89588912&ar=562518&xsltPath=~/UI/app/XSLT&imagename=&siteId=5387" data-path-from-xml="FYR_295_f2.jpeg">Download slide</a></div></div></div></div> <h3 scrollto-destination=89588913 id="89588913" class="section-title js-splitscreen-section-title" data-legacy-id=ss3-2>3.2 Biosynthesis of GSH</h3> <p class="chapter-para">GSH is synthesized by the consecutive action of γ-GCS (<span class="small-caps">l</span>-glutamate+<span class="small-caps">l</span>-cysteine+ATP→<span class="small-caps">l</span>-γ-glutamyl-<span class="small-caps">l</span>-cysteine+ADP, EC 6.3.2.2) and <span class="small-caps">l</span>-γ-glutamylcysteine-glycine γ-ligase (<span class="small-caps">l</span>-γ-glutamyl-<span class="small-caps">l</span>-cysteine+glycine+ATP→GSH+ADP: GSH synthetase, EC 6.3.2.3), encoded respectively by the <em>GSH1</em> and <em>GSH2</em> genes [<span class="xrefLink" id="jumplink-b26"></span><a href="javascript:;" reveal-id="b26" data-open="b26" class="link link-ref link-reveal xref-bibr">26</a>]. In <em>S. cerevisiae GSH1</em> comprises a segment of 2034 bp that encodes a protein Gsh1p (γ-GCS) of 678 amino acid residues. Blast search revealed that <em>S. cerevisiae</em>γ-GCS shares sequence homology with the γ-GCS of the NCY <em>S. pombe</em> (41% of identity over 669 residues).</p><p class="chapter-para">γ-GCS appears to be a highly regulated enzyme transcriptionally responsive to the Yap1 [<span class="xrefLink" id="jumplink-b27"></span><a href="javascript:;" reveal-id="b27" data-open="b27" class="link link-ref link-reveal xref-bibr">27</a>] protein, a central modulator in mechanisms for drug and metal resistance (reviewed in [<span class="xrefLink" id="jumplink-b28"></span><a href="javascript:;" reveal-id="b28" data-open="b28" class="link link-ref link-reveal xref-bibr">28</a>]). Skn7p, another yeast transcriptional regulator, apparently exerts a negative effect upon the response to cadmium [<span class="xrefLink" id="jumplink-b27"></span><a href="javascript:;" reveal-id="b27" data-open="b27" class="link link-ref link-reveal xref-bibr">27</a>]. γ-GCS activity was also shown to be feedback-inhibited by GSH, preventing over-accumulation of the tripeptide [<span class="xrefLink" id="jumplink-b2"></span><a href="javascript:;" reveal-id="b2" data-open="b2" class="link link-ref link-reveal xref-bibr">2</a>,<span class="xrefLink" id="jumplink-b3"></span><a href="javascript:;" reveal-id="b3" data-open="b3" class="link link-ref link-reveal xref-bibr">3</a>]. Unlike γ-GCS, GSH synthetase appeared to be a constitutive unregulated enzyme [<span class="xrefLink" id="jumplink-b29"></span><a href="javascript:;" reveal-id="b29" data-open="b29" class="link link-ref link-reveal xref-bibr">29</a>].</p> <h3 scrollto-destination=89588920 id="89588920" class="section-title js-splitscreen-section-title" data-legacy-id=ss3-3>3.3 Degradation of GSH</h3> <p class="chapter-para">γ-Glutamyltranspeptidase [γ-GT: GSH+amino acid (H<sub>2</sub>O)→<span class="small-caps">l</span>-γ-glutamyl-amino acid (<span class="small-caps">l</span>-glutamate), EC 2.3.2.2] is the only GSH-degrading enzyme currently characterized in yeast [<span class="xrefLink" id="jumplink-b30"></span><a href="javascript:;" reveal-id="b30" data-open="b30" class="link link-ref link-reveal xref-bibr">30</a>,<span class="xrefLink" id="jumplink-b31"></span><a href="javascript:;" reveal-id="b31" data-open="b31" class="link link-ref link-reveal xref-bibr">31</a>]. It catalyzes transfer of the γ-glutamyl moiety of GSH and other γ-glutamyl compounds to amino acids and also the hydrolytic release of <span class="small-caps">l</span>-glutamate from GSH, various γ-glutamyl compounds, and S-substituted derivatives [<span class="xrefLink" id="jumplink-b32"></span><a href="javascript:;" reveal-id="b32" data-open="b32" class="link link-ref link-reveal xref-bibr">32</a>]. <em>S. cerevisiae</em>γ-GT has been identified as a vacuolar membrane-bound glycosylated protein with an apparent molecular mass around 90 000 Da. 73 162 Da is the molecular mass predicted for the non-glycosylated form of the enzyme on the basis of its amino acid sequence. The small chain of yeast γ-GT located at the carboxy-terminal moiety contains at position 470–494 the TAHFSIVDSHGNAVSLTTTINLLFG sequence that matches the γ-GT signature T(STA)HX(ST)X<sub>4</sub>G(SN)XV(STA)XTXT(LIVM)(NE)X<sub>1,2</sub>(FY)G (PS00462). Blast search revealed that <em>S. cerevisiae</em>γ-GT shares sequence homology with the γ-GTs of <em>Escherichia coli</em> (27% of identity over 486 residues), rat (30% of identity over 557 residues), <em>Homo sapiens</em> (32% of identity over 575 residues) and <em>S. pombe</em> (36% identity over 630 residues). In contrast to the <em>E. coli</em> enzyme [<span class="xrefLink" id="jumplink-b33"></span><a href="javascript:;" reveal-id="b33" data-open="b33" class="link link-ref link-reveal xref-bibr">33</a>], yeast γ-GT lacks an N-terminal signal peptide. It is more similar to mammalian γ-GTs. As in the rat and human enzymes, one potential transmembrane helix α domain, preceded by a short hydrophilic tail in the N-terminal region, has been located in <em>S. cerevisiae</em>γ-GT. The organization of γ-GT is highly similar to that of alkaline phosphatase, a typical integral yeast type II vacuolar membrane protein with a short hydrophilic tail extending into the cytoplasm and with its C-terminus bearing the active site inside the vacuolar lumen [<span class="xrefLink" id="jumplink-b34"></span><a href="javascript:;" reveal-id="b34" data-open="b34" class="link link-ref link-reveal xref-bibr">34</a>].</p><p class="chapter-para"><span class="small-caps">l</span>-Cysteinyl glycine dipeptidase (CGase: <span class="small-caps">l</span>-cysteinyl glycine+H<sub>2</sub>O→<span class="small-caps">l</span>-cysteine+glycine, EC 3.4.13.6) is assumed to catalyze the last step in GSH hydrolysis (<span class="xrefLink" id="jumplink-f2"></span><a href="javascript:;" data-modal-source-id="f2" class="link xref-fig">Fig. 2</a>). This activity was reported to be present in <em>S. cerevisiae</em> and associated with the vacuolar membrane [<span class="xrefLink" id="jumplink-b35"></span><a href="javascript:;" reveal-id="b35" data-open="b35" class="link link-ref link-reveal xref-bibr">35</a>]. A variety of <span class="small-caps">l</span>-Cys-Gly-hydrolyzing peptidases are produced by microorganisms and mammals [<span class="xrefLink" id="jumplink-b2"></span><a href="javascript:;" reveal-id="b2" data-open="b2" class="link link-ref link-reveal xref-bibr">2</a>,<span class="xrefLink" id="jumplink-b3"></span><a href="javascript:;" reveal-id="b3" data-open="b3" class="link link-ref link-reveal xref-bibr">3</a>,<span class="xrefLink" id="jumplink-b36 b38"></span><a href="javascript:;" reveal-id="b36 b38" data-open="b36 b38" class="link link-ref link-reveal xref-bibr">36–38</a>]. Yet a Blast search for homologues in <em>S. cerevisiae</em> revealed no similarities to known hydrolases in yeast. The open reading frame (ORF) encoding yeast CGase thus remains to be identified.</p><p class="chapter-para">γ-GT biosynthesis was found to be regulated by at least two distinct pathways. Ammonium ions as a nitrogen source repressed the transpeptidase, whereas the cellular enzyme level was higher in the presence of a variety of other nitrogen sources, including amino acids or urea [<span class="xrefLink" id="jumplink-b30"></span><a href="javascript:;" reveal-id="b30" data-open="b30" class="link link-ref link-reveal xref-bibr">30</a>]. The enzyme production was strongly derepressed by nitrogen starvation as was shown previously [<span class="xrefLink" id="jumplink-b14"></span><a href="javascript:;" reveal-id="b14" data-open="b14" class="link link-ref link-reveal xref-bibr">14</a>,<span class="xrefLink" id="jumplink-b30"></span><a href="javascript:;" reveal-id="b30" data-open="b30" class="link link-ref link-reveal xref-bibr">30</a>] and recently confirmed in an exploration of genomic expression patterns in <em>S. cerevisiae</em> responding to environmental changes [<span class="xrefLink" id="jumplink-b5"></span><a href="javascript:;" reveal-id="b5" data-open="b5" class="link link-ref link-reveal xref-bibr">5</a>]. At least seven GATTA consensus sequences, known to be implicated in nitrogen regulation, and one characteristic CCCCT stress-responding sequence were found in the region upstream of the ORF encoding γ-GT (Springael and Penninckx, unpublished data).</p><p class="chapter-para">It has been suggested that γ-GT might play a role in amino acid transport in yeast [<span class="xrefLink" id="jumplink-b30"></span><a href="javascript:;" reveal-id="b30" data-open="b30" class="link link-ref link-reveal xref-bibr">30</a>], but this has been ruled out as far as bulk transport of amino acids in <em>S. cerevisiae</em> is concerned [<span class="xrefLink" id="jumplink-b24"></span><a href="javascript:;" reveal-id="b24" data-open="b24" class="link link-ref link-reveal xref-bibr">24</a>,<span class="xrefLink" id="jumplink-b39"></span><a href="javascript:;" reveal-id="b39" data-open="b39" class="link link-ref link-reveal xref-bibr">39</a>]. A possible role for γ-GT in the mobilization of GSH as alternative sulfur and nitrogen source during starvation will be discussed below.</p> <h3 scrollto-destination=89588930 id="89588930" class="section-title js-splitscreen-section-title" data-legacy-id=ss3-4>3.4 Transport of GSH</h3> <p class="chapter-para">In addition to endogenous biosynthesis, GSH may also be taken up from the extracellular environment. Specific transporters mediating GSH uptake in microorganisms [<span class="xrefLink" id="jumplink-b40"></span><a href="javascript:;" reveal-id="b40" data-open="b40" class="link link-ref link-reveal xref-bibr">40</a>], plants [<span class="xrefLink" id="jumplink-b4"></span><a href="javascript:;" reveal-id="b4" data-open="b4" class="link link-ref link-reveal xref-bibr">4</a>] and animal tissues [<span class="xrefLink" id="jumplink-b41"></span><a href="javascript:;" reveal-id="b41" data-open="b41" class="link link-ref link-reveal xref-bibr">41</a>] have been described. Two kinetically distinguishable GSH transport systems were shown in <em>S. cerevisiae</em>. GSH-P1 is a high-affinity (<em>K</em><sub>m</sub>=45 μM) ATP-driven and regulated system, responding to sulfur starvation, whereas GSH-P2 has a lower affinity (<em>K</em><sub>m</sub>>2 mM) and is not regulated (<span class="xrefLink" id="jumplink-f3"></span><a href="javascript:;" data-modal-source-id="f3" class="link xref-fig">Fig. 3</a>) [<span class="xrefLink" id="jumplink-b42"></span><a href="javascript:;" reveal-id="b42" data-open="b42" class="link link-ref link-reveal xref-bibr">42</a>]. Hgt1p, a high-affinity plasma membrane GSH transporter (<em>K</em><sub>m</sub>=54 μM) was recently cloned and characterized in <em>S. cerevisiae</em>[<span class="xrefLink" id="jumplink-b43"></span><a href="javascript:;" reveal-id="b43" data-open="b43" class="link link-ref link-reveal xref-bibr">43</a>]. Apparently nothing is known about a possible relationship between GSH P-1 and Hgt1p.</p> <a id="89588935" scrollto-destination="89588935"></a> <div data-id="f3" data-content-id="f3" class="fig fig-section js-fig-section" swap-content-for-modal="true"><div class="graphic-wrap"><img class="content-image" src="https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/m_FYR_295_f3.jpeg?Expires=1736287804&Signature=3s9hzfplvps1cSusqQVtWs-U0DSmXCG5~T4DpiGJ3psfLvIgaMlSd06W1DmngslSlWXGjs1dXCHTDWgTr-IPpZekB5mYmSSLiz~nQYQkjmGkiUUQhXlaIxpWckHDozni1PvMn9bcP3KBchc2URIZlDCdomzzXVqUleXT2lJup59szBo0eonLG0qqWb4NFnuCWg7asn2NVMNCzaeY6wblen~O4Cdqla0qi4a6AfKxDXyjoEUNRMIuvVJDyMiGoxVt4P-Wpjp2RiuyC7X984iRLlMi7RJldUS7ePb2m9HOow8GO5bxEa6oRPOnaBPszrsvwbKN9ASh8kKhy1hkZnmngw__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" alt="Transport and metabolism of sulfur in S. cerevisiae[38,42]. GSH can be taken up by the yeast cell through two transport systems, GSH-P1 (high-affinity) and GSH-P2 (low-affinity). Sulfur flows from GSH to other metabolites along the sulfur metabolic pathway. SO42− is also taken up and metabolized as indicated. In case of total sulfur deprivation GSH stored in the cell is used as an endogenous sulfur source. (1) Serine acetyltransferase; (2) cysteine synthase; (3) homoserine acetyltransferase; (4) homocysteine synthase; (5) γ-cystathionine synthase; (6) γ-cystathionase; (7) β-cystathionase; (8) β-cystathionine synthase; (9) homocysteine methyltransferase; (10) S-adenosylmethionine synthase; (11) S-adenosylmethionine demethylase; (12) adenosylhomocysteinase; (13) sulfate-reducing pathway; (14) γ-GCS; (15) GSH synthetase; (16) γ-GT; (17) CGase." data-path-from-xml="FYR_295_f3.jpeg" /><div class="graphic-bottom"><div class="label fig-label" id="label-89588935">3</div><div class="caption fig-caption"><p class="chapter-para">Transport and metabolism of sulfur in <em>S. cerevisiae</em>[<span class="xrefLink" id="jumplink-b38"></span><a href="javascript:;" reveal-id="b38" data-open="b38" class="link link-ref link-reveal xref-bibr">38</a>,<span class="xrefLink" id="jumplink-b42"></span><a href="javascript:;" reveal-id="b42" data-open="b42" class="link link-ref link-reveal xref-bibr">42</a>]. GSH can be taken up by the yeast cell through two transport systems, GSH-P1 (high-affinity) and GSH-P2 (low-affinity). Sulfur flows from GSH to other metabolites along the sulfur metabolic pathway. SO<sub>4</sub><sup>2−</sup> is also taken up and metabolized as indicated. In case of total sulfur deprivation GSH stored in the cell is used as an endogenous sulfur source. (1) Serine acetyltransferase; (2) cysteine synthase; (3) homoserine acetyltransferase; (4) homocysteine synthase; (5) γ-cystathionine synthase; (6) γ-cystathionase; (7) β-cystathionase; (8) β-cystathionine synthase; (9) homocysteine methyltransferase; (10) <em>S</em>-adenosylmethionine synthase; (11) <em>S</em>-adenosylmethionine demethylase; (12) adenosylhomocysteinase; (13) sulfate-reducing pathway; (14) γ-GCS; (15) GSH synthetase; (16) γ-GT; (17) CGase.</p></div><div class="ajax-articleAbstract-exclude-regex fig-orig original-slide figure-button-wrap"><a class="fig-view-orig js-view-large at-figureViewLarge openInAnotherWindow" role="button" aria-describedby="label-89588935" href="/view-large/figure/89588935/FYR_295_f3.jpeg" data-path-from-xml="FYR_295_f3.jpeg" target="_blank">Open in new tab</a><a class="download-slide" role="button" aria-describedby="label-89588935" data-section="89588935" href="/DownloadFile/DownloadImage.aspx?image=https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/FYR_295_f3.jpeg?Expires=1736287804&Signature=i13jWnV~n0OUouY77PwAefPUEbMHQ6QsNqbdFxy3hDML-nB0T8rOgnzSytrZzS8A0Juqd9qu~5cvBuJcN1l91WOqrUuSi20UYYH8OzBjOqYOfgHQw2PhsyBfKviI~mWmOieRML8jdp0xsXNYlw-8ru9tz~Yf79c2vO6rtThENuEonTdo~m1BQ3ri~9ojXSApqRh92cyc7~Cs1-5euu0NVYuNbfhw6tD1J5HUu9pBiKs23OeAx2iwYu5fE3iIlO0ZRtcznhOq79anfGS3LhAOAYLhqI28EtdVT33yeKYF~YorHdQhTocexIXWFoxA2yAfejgh9Vzmdp8mZHEj-cFmTw__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA&sec=89588935&ar=562518&xsltPath=~/UI/app/XSLT&imagename=&siteId=5387" data-path-from-xml="FYR_295_f3.jpeg">Download slide</a></div></div></div></div><p class="chapter-para">Sequence analysis of Hgt1p revealed virtually no homology with the yeast YCF1 vacuolar pump mediating low-affinity vacuolar transport of GSH and different GSH conjugates (GS-X) [<span class="xrefLink" id="jumplink-b31"></span><a href="javascript:;" reveal-id="b31" data-open="b31" class="link link-ref link-reveal xref-bibr">31</a>,<span class="xrefLink" id="jumplink-b44"></span><a href="javascript:;" reveal-id="b44" data-open="b44" class="link link-ref link-reveal xref-bibr">44</a>,<span class="xrefLink" id="jumplink-b45"></span><a href="javascript:;" reveal-id="b45" data-open="b45" class="link link-ref link-reveal xref-bibr">45</a>]. The <em>YCF1</em> gene was initially isolated according to its ability to confer cadmium resistance to <em>S. cerevisiae</em>. It encodes a 1515-amino acid ATP-binding cassette (ABC) protein with extensive sequence homology to the human multidrug resistance-associated protein (MRP1).</p> <h2 scrollto-destination=89588940 id="89588940" class="section-title js-splitscreen-section-title" data-legacy-id=ss4>4 Main roles of GSH in <em>S. cerevisiae</em> and NCY</h2> <h3 scrollto-destination=89588942 id="89588942" class="section-title js-splitscreen-section-title" data-legacy-id=ss4-1>4.1 Sulfur and nitrogen metabolism</h3> <p class="chapter-para"><em>S. cerevisiae</em> can use methionine, homocysteine, cysteine or GSH as a sole source of sulfur because of the existence of a metabolic network in which these compounds can readily exchange their sulfur atoms (<span class="xrefLink" id="jumplink-f3"></span><a href="javascript:;" data-modal-source-id="f3" class="link xref-fig">Fig. 3</a>) [<span class="xrefLink" id="jumplink-b46"></span><a href="javascript:;" reveal-id="b46" data-open="b46" class="link link-ref link-reveal xref-bibr">46</a>]. Mutants unable to grow on GSH as a sole source of sulfur were isolated from <em>S. cerevisiae met17</em> strains deficient in homocysteine synthase (<em>O</em>-acetylhomoserine sulfhydrylase) and cysteine synthase (<em>O</em>-acetylserine sulfhydrylase) [<span class="xrefLink" id="jumplink-b47"></span><a href="javascript:;" reveal-id="b47" data-open="b47" class="link link-ref link-reveal xref-bibr">47</a>]. These mutant strains were defective in the high-affinity transport system GSH-P1 but apparently not affected in γ-GT and CGase activity. The existence of an alternative GSH-degrading pathway providing SO<sub>4</sub><sup>2−</sup> to the cell independently of the GSH cycle was suggested [<span class="xrefLink" id="jumplink-b47"></span><a href="javascript:;" reveal-id="b47" data-open="b47" class="link link-ref link-reveal xref-bibr">47</a>]. The method used in this investigation to estimate γ-GT activity was, however, proven to give erratic results [<span class="xrefLink" id="jumplink-b30"></span><a href="javascript:;" reveal-id="b30" data-open="b30" class="link link-ref link-reveal xref-bibr">30</a>]. This casts serious doubt on the existence of a sulfur-providing pathway independent of the GSH cycle.</p><p class="chapter-para">When cells of <em>S. cerevisiae</em> were totally deprived of any external sulfur source, GSH was apparently able to serve as an endogenous sulfur source until it reached a residual concentration of about 10% of its normal value [<span class="xrefLink" id="jumplink-b46"></span><a href="javascript:;" reveal-id="b46" data-open="b46" class="link link-ref link-reveal xref-bibr">46</a>]. A strong derepression of γ-GT and of the enzymes of the transsulfuration pathway was observed during sulfur starvation and as a consequence the turnover rate of GSH increased (<span class="xrefLink" id="jumplink-f3"></span><a href="javascript:;" data-modal-source-id="f3" class="link xref-fig">Fig. 3</a>).</p><p class="chapter-para">In <em>S. pombe</em> the product of <em>ISP4</em> is a close homolog of the high-affinity transporter encoded by <em>HGT1</em> in <em>S. cerevisiae</em> (38% identity). <em>ISP4</em> was identified as a gene induced during sporulation of <em>S. pombe</em> probably to meet an increased GSH requirement [<span class="xrefLink" id="jumplink-b48"></span><a href="javascript:;" reveal-id="b48" data-open="b48" class="link link-ref link-reveal xref-bibr">48</a>]. Transport and metabolism of GSH to provide cysteine for sporulation was reported previously in the case of <em>Bacillus</em> sp. (reviewed in [<span class="xrefLink" id="jumplink-b3"></span><a href="javascript:;" reveal-id="b3" data-open="b3" class="link link-ref link-reveal xref-bibr">3</a>]).</p><p class="chapter-para">When <em>S. cerevisiae</em> was subjected to nitrogen starvation, more than 90% of the cellular GSH shifted toward the central vacuole of the yeast [<span class="xrefLink" id="jumplink-b14"></span><a href="javascript:;" reveal-id="b14" data-open="b14" class="link link-ref link-reveal xref-bibr">14</a>]. γ-GT induced during N starvation was translocated from the Golgi toward the vacuolar membrane via a pathway alternative to the prevacuolar compartment (Mehdi and Penninckx, unpublished), possibly similar to the vacuolar delivery route of alkaline phosphatase [<span class="xrefLink" id="jumplink-b49"></span><a href="javascript:;" reveal-id="b49" data-open="b49" class="link link-ref link-reveal xref-bibr">49</a>]. The kinetic parameters of vacuolar GSH transport were measured on intact vacuoles isolated from a wild-type <em>S. cerevisiae</em> strain, under conditions of γ-GT synthesis (N starvation) and repression (growth in the presence of ammonium ions) [<span class="xrefLink" id="jumplink-b31"></span><a href="javascript:;" reveal-id="b31" data-open="b31" class="link link-ref link-reveal xref-bibr">31</a>]. Vacuoles containing γ-GT displayed practically the same <em>K</em><sub>m</sub> of 18 mM for GSH transport as vacuoles devoid of γ-GT, but a threefold higher apparent maximal rate(<em>V</em><sup>app</sup>) of 150 nmol GSH (mg protein)<sup>−1</sup> min<sup>−1</sup>. Vacuoles prepared from a disruptant lacking γ-GT showed no increase in <em>V</em><sup>app</sup> with nitrogen starvation. From a comparison of the transport data obtained for vacuoles isolated from various reference and mutant strains, it appears that the YCF1 transport system accounts for about 70% of the GSH transport capacity of the vacuoles, the remaining 30% being due to a V-ATPase-coupled system (<span class="xrefLink" id="jumplink-f4"></span><a href="javascript:;" data-modal-source-id="f4" class="link xref-fig">Fig. 4</a>). This anion uniport system pathway is most probably related, if not identical, to a YCF1-independent system secondarily involved in the transport of GS-X in <em>S. cerevisiae</em>[<span class="xrefLink" id="jumplink-b44"></span><a href="javascript:;" reveal-id="b44" data-open="b44" class="link link-ref link-reveal xref-bibr">44</a>]. The <em>V</em><sup>app</sup>-increasing effect of γ-GT concerns only the YCF1 system. γ-GT in the vacuolar membrane activates the Ycf1p transporter, either directly or indirectly. Although no experimental data are currently available to base a conclusion on, it is noteworthy that in a two-hybrid system, γ-GT interacts with another yeast membrane protein of unknown function [<span class="xrefLink" id="jumplink-b50"></span><a href="javascript:;" reveal-id="b50" data-open="b50" class="link link-ref link-reveal xref-bibr">50</a>]. Moreover, GSH accumulating in the vacuolar space may exert a feedback effect on its own entry. GSH stored in the vacuole is further degraded. It is proposed that γ-GT and a CGase catalyze the complete hydrolysis of GSH stored in the central vacuole of the yeast cell, prior to release of its constitutive amino acids <span class="small-caps">l</span>-Glu, <span class="small-caps">l</span>-Cys, and Gly into the cytosol (<span class="xrefLink" id="jumplink-f4"></span><a href="javascript:;" data-modal-source-id="f4" class="link xref-fig">Fig. 4</a>). This mechanism can apparently enable the starved yeast to use the constituent amino acids from GSH to satisfy at least in part its growth requirements for nitrogen [<span class="xrefLink" id="jumplink-b14"></span><a href="javascript:;" reveal-id="b14" data-open="b14" class="link link-ref link-reveal xref-bibr">14</a>].</p> <a id="89588952" scrollto-destination="89588952"></a> <div data-id="f4" data-content-id="f4" class="fig fig-section js-fig-section" swap-content-for-modal="true"><div class="graphic-wrap"><img class="content-image" src="https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/m_FYR_295_f4.jpeg?Expires=1736287804&Signature=mTVCGX8DhDcJB6NnvMI9uA3DapV0xT9OEvtpS82hIPZsEpH8TOq4KK4gBuA~QhyTBda91Hhthjf1xE5XTA1L4Vyn6a650QBgH6yUt-pnqB0oWmBf6Sd9MTLJDncvmKBncJ5B4EkGdmvPlt~qz4A-q-mhw4hhq3AVEOW6YIWcrTDHaS4uqxeCb~qMRubX0yami3BbM621zRKrlxiYw68Jqoxo2FuuF~AkQJXdSwCNYG6Tr~QQYeVAWP1hnxrBh6fP0ogKIlKlKxepuM6Qdwi1vP17QXZcmODUmdFiWvkUSW5bSIqyiAJEa5OSIzTejmjBmTxHFWKitFxUXfAVz3X08g__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" alt="A synthetic model for GSH and GS-X transport and metabolism in S. cerevisiae[27,58]. GSH and GS-X are transported into the central vacuole by Ycf1p (1) and a V ATPase-coupled anion uniport system (2 and 3). GSH is further degraded by γ-GT (4) and CGase (5). Ycf1p is activated by γ-GT (solid arrow). GSH accumulated in the vacuole exerts a feedback effect on its transport by Ycf1p (dotted arrow). GS-X is also possibly transported out of the cell by an ATP-linked system (6)." data-path-from-xml="FYR_295_f4.jpeg" /><div class="graphic-bottom"><div class="label fig-label" id="label-89588952">4</div><div class="caption fig-caption"><p class="chapter-para">A synthetic model for GSH and GS-X transport and metabolism in <em>S. cerevisiae</em>[<span class="xrefLink" id="jumplink-b27"></span><a href="javascript:;" reveal-id="b27" data-open="b27" class="link link-ref link-reveal xref-bibr">27</a>,<span class="xrefLink" id="jumplink-b58"></span><a href="javascript:;" reveal-id="b58" data-open="b58" class="link link-ref link-reveal xref-bibr">58</a>]. GSH and GS-X are transported into the central vacuole by Ycf1p (1) and a V ATPase-coupled anion uniport system (2 and 3). GSH is further degraded by γ-GT (4) and CGase (5). Ycf1p is activated by γ-GT (solid arrow). GSH accumulated in the vacuole exerts a feedback effect on its transport by Ycf1p (dotted arrow). GS-X is also possibly transported out of the cell by an ATP-linked system (6).</p></div><div class="ajax-articleAbstract-exclude-regex fig-orig original-slide figure-button-wrap"><a class="fig-view-orig js-view-large at-figureViewLarge openInAnotherWindow" role="button" aria-describedby="label-89588952" href="/view-large/figure/89588952/FYR_295_f4.jpeg" data-path-from-xml="FYR_295_f4.jpeg" target="_blank">Open in new tab</a><a class="download-slide" role="button" aria-describedby="label-89588952" data-section="89588952" href="/DownloadFile/DownloadImage.aspx?image=https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/FYR_295_f4.jpeg?Expires=1736287804&Signature=N7br-UxN~j07~QTA4R0LyEzUoTmY6crD2zXbz3aqLM4eM0-g~GqSRKZLdYhrLtJBOoklNaAj78A3k3uezbnVkPOl7N3xn1CUbq6nMJtRag~CDEJY~I4K8RwC~RKtwmurYgbroaN22miGIBqG2bs38DH7YiyvAGOEHWzd~~t3Xuue6MuCl4bkOG1Mpo0~jSTWQ34MPH-50tFtj5bA9mJlc5yJcROXBLpHOc5WLJO0cxfBQfcifn2ao2EsFXmyjcCEBYPnCgIqWHje9gLKXAEzpV67LP4qF27wWjnNw~LiYCuKszuZJhaJS-YXzndJsH5WVo5e-sbgNZh7Wh~EAB-76w__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA&sec=89588952&ar=562518&xsltPath=~/UI/app/XSLT&imagename=&siteId=5387" data-path-from-xml="FYR_295_f4.jpeg">Download slide</a></div></div></div></div> <h3 scrollto-destination=89588956 id="89588956" class="section-title js-splitscreen-section-title" data-legacy-id=ss4-2>4.2 Growth on methanol</h3> <p class="chapter-para">When growing on methanol as a carbon and energy source, <em>Hansenula polymorpha</em>, <em>Candida boidinii</em>, certain <em>Kloeckera</em> and <em>Pichia</em> spp., synthesized spectacular cytoplasmic peroxisome organelles containing at least two matrix enzymes, a H<sub>2</sub>O<sub>2</sub>-generating methanol oxidase and a H<sub>2</sub>O<sub>2</sub>-decomposing catalase (<span class="xrefLink" id="jumplink-f5"></span><a href="javascript:;" data-modal-source-id="f5" class="link xref-fig">Fig. 5</a>) [<span class="xrefLink" id="jumplink-b7"></span><a href="javascript:;" reveal-id="b7" data-open="b7" class="link link-ref link-reveal xref-bibr">7</a>]. Formaldehyde produced by the oxidase is exported to the cytosol and incorporated in part in the central metabolism of the yeast. Excess of formaldehyde is metabolized through the formaldehyde dehydrogenase–<em>S</em>-formyl glutathione system which uses GSH as a cofactor. Methanol induces elevation of the intracellular GSH pool possibly via a positive transcriptional factor related to YAP-1 and acting on biosynthesis of γ-GCS [<span class="xrefLink" id="jumplink-b51"></span><a href="javascript:;" reveal-id="b51" data-open="b51" class="link link-ref link-reveal xref-bibr">51</a>]. GSH-deficient mutants of <em>H. polymorpha</em> failed to grow on methanol due to the accumulation of formaldehyde in toxic amounts. This was also observed with mutants deficient in formaldehyde dehydrogenase, confirming that methanol induces a situation of metabolic stress [<span class="xrefLink" id="jumplink-b51"></span><a href="javascript:;" reveal-id="b51" data-open="b51" class="link link-ref link-reveal xref-bibr">51</a>,<span class="xrefLink" id="jumplink-b52"></span><a href="javascript:;" reveal-id="b52" data-open="b52" class="link link-ref link-reveal xref-bibr">52</a>].</p> <a id="89588962" scrollto-destination="89588962"></a> <div data-id="f5" data-content-id="f5" class="fig fig-section js-fig-section" swap-content-for-modal="true"><div class="graphic-wrap"><img class="content-image" src="https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/m_FYR_295_f5.jpeg?Expires=1736287804&Signature=CaVvGG0eWCQKOQKvahbXheSUTmplPwFqTW9w1K0dXjgMor1ZmscKHaNLzfRwW3AS~eStYdpdgpZ5vUXfnDUlSAnuRPQam7GXA1Sg1shSR35mcSGKRiOzUhp38FEZ7XsjrBdmA83L-Y5pzWQwZfhL7K8Bc4Sm4M1ifoJ8~YjYULlB5QqGGWVTUKRL7FWOr7WM9gNOpW-NbpKRQWjuHpd4z3uet0IX3QNRdSLguFaDlmOwT1yiI9d-URc7~uBqHkWwD4vOujZvA7NoYxKVdUwNbpxibjcgtv2IraBOKbPhQfa1MLecmtTKIpt2FF~bpsHXtjSHAHtg3W78mAeEYdZ3sw__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" alt="The metabolism of methanol in methylotrophic yeasts [7]. (1) Methanol oxidase; (2) catalase; (3) formaldehyde dehydrogenase; (4) S-formyl GSH hydrolase; (5) formate dehydrogenase; (6) formaldehyde assimilation pathway." data-path-from-xml="FYR_295_f5.jpeg" /><div class="graphic-bottom"><div class="label fig-label" id="label-89588962">5</div><div class="caption fig-caption"><p class="chapter-para">The metabolism of methanol in methylotrophic yeasts [<span class="xrefLink" id="jumplink-b7"></span><a href="javascript:;" reveal-id="b7" data-open="b7" class="link link-ref link-reveal xref-bibr">7</a>]. (1) Methanol oxidase; (2) catalase; (3) formaldehyde dehydrogenase; (4) <em>S</em>-formyl GSH hydrolase; (5) formate dehydrogenase; (6) formaldehyde assimilation pathway.</p></div><div class="ajax-articleAbstract-exclude-regex fig-orig original-slide figure-button-wrap"><a class="fig-view-orig js-view-large at-figureViewLarge openInAnotherWindow" role="button" aria-describedby="label-89588962" href="/view-large/figure/89588962/FYR_295_f5.jpeg" data-path-from-xml="FYR_295_f5.jpeg" target="_blank">Open in new tab</a><a class="download-slide" role="button" aria-describedby="label-89588962" data-section="89588962" href="/DownloadFile/DownloadImage.aspx?image=https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/FYR_295_f5.jpeg?Expires=1736287804&Signature=FKJMGTk2sL-QnMWDgLplMezVmzzegg5ZkRaK3J9tTxDS-a6n2tSjpHl93MVtAprSEyt7pHI2hz0Ibi9o54u-F1NjnGiNzHjJFmbvGnaIqhhinmOhKWPKtqJqgq5Y8RZdea7MjvqeN5IWUCECnFKpzYV2RQHX~1y0nwdLjXpTd15G8TsRU8danCwhJKQgwXuHu2344D39uTBeaMX-Wdy6Vi0NFfQh4X-HBstFwy2-IVQu5r40FhsYfo~anZW-AmFOZrTSYuiQoRMgmBiMLTeOesIrWjOwfa0ygl9UoQ7NMVg2m7gU18cs01mSrqideKPa5XDXaWzKlSMWOm71w5W13A__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA&sec=89588962&ar=562518&xsltPath=~/UI/app/XSLT&imagename=&siteId=5387" data-path-from-xml="FYR_295_f5.jpeg">Download slide</a></div></div></div></div> <h3 scrollto-destination=89588964 id="89588964" class="section-title js-splitscreen-section-title" data-legacy-id=ss4-3>4.3 Response to the oxidative stress</h3> <p class="chapter-para">Oxidative stress occurs when cells are exposed to high levels of ROS such as peroxides, including H<sub>2</sub>O<sub>2</sub> and alkylhydroperoxides (ROOH), and the superoxide anion (O<sub>2</sub><sup>●−</sup>). Many investigators have shown that GSH plays an important role in the response of yeasts to oxidative stress, in particular to ROOH such as cumene hydroperoxide, <em>t</em>-butyl hydroperoxide or endogenous lipid hydroperoxide (LOOH) generated in biological membranes from unsaturated fatty acids [<span class="xrefLink" id="jumplink-b15"></span><a href="javascript:;" reveal-id="b15" data-open="b15" class="link link-ref link-reveal xref-bibr">15</a>,<span class="xrefLink" id="jumplink-b17"></span><a href="javascript:;" reveal-id="b17" data-open="b17" class="link link-ref link-reveal xref-bibr">17</a>,<span class="xrefLink" id="jumplink-b28"></span><a href="javascript:;" reveal-id="b28" data-open="b28" class="link link-ref link-reveal xref-bibr">28</a>]. High levels of GSH in yeast are apparently important for surviving acute peroxide stress but not for growth adaptation under moderate peroxide concentration [<span class="xrefLink" id="jumplink-b16"></span><a href="javascript:;" reveal-id="b16" data-open="b16" class="link link-ref link-reveal xref-bibr">16</a>]. Glutathione peroxidase (GPx: 2 GSH+ROOH→GSSG+H<sub>2</sub>O+ROH, EC 1.11.1.9)) is a key enzyme in the defence mechanisms against hydroperoxides. It was found to be induced by oxidative conditions in <em>S. cerevisiae</em>[<span class="xrefLink" id="jumplink-b53"></span><a href="javascript:;" reveal-id="b53" data-open="b53" class="link link-ref link-reveal xref-bibr">53</a>]. Later GPx was purified from <em>Hansenula mrakii</em> and found to be localized in both the cytoplasmic membrane and the inner membrane of mitochondria, where large amounts of ROS are generated [<span class="xrefLink" id="jumplink-b54"></span><a href="javascript:;" reveal-id="b54" data-open="b54" class="link link-ref link-reveal xref-bibr">54</a>]. A peroxiredoxin encoded by the <em>PMP20</em> gene was also found in the peroxisome membrane of <em>C. boidinii</em> growing on methanol [<span class="xrefLink" id="jumplink-b55"></span><a href="javascript:;" reveal-id="b55" data-open="b55" class="link link-ref link-reveal xref-bibr">55</a>]. The Pmp20 antioxidant system relies on GSH as an electron donor and may function within peroxisomes as a GPx. Three GPxs, named Gpx1p, Gpx2p and Gpx3p, were found in <em>S. cerevisiae</em>[<span class="xrefLink" id="jumplink-b56"></span><a href="javascript:;" reveal-id="b56" data-open="b56" class="link link-ref link-reveal xref-bibr">56</a>]. A genetic and phenotypic analysis has shown that <em>GPX1</em> was induced by glucose starvation. <em>GPX2</em> was induced by oxidative stress, although apparently not playing a significant role in the response to this stress, at least against H<sub>2</sub>O<sub>2</sub> and <em>t</em>-butyl hydroperoxide used in these studies as model ROS. The <em>GPX3</em> gene was found to be expressed constitutively. Apparently Gpx3p is the major GPx that scavenges peroxides in the yeast. Recently it was shown that the <em>GPx</em> genes of <em>S. cerevisiae</em>, previously reported to encode classical soluble GPxs, encode partially membrane-associated phospholipid hydroperoxide GPxs [<span class="xrefLink" id="jumplink-b57"></span><a href="javascript:;" reveal-id="b57" data-open="b57" class="link link-ref link-reveal xref-bibr">57</a>]. A thioredoxin (Trx)-dependent reduction system [<span class="xrefLink" id="jumplink-b58"></span><a href="javascript:;" reveal-id="b58" data-open="b58" class="link link-ref link-reveal xref-bibr">58</a>] is also closely involved in the response of <em>S. cerevisiae</em> against ROS [<span class="xrefLink" id="jumplink-b28"></span><a href="javascript:;" reveal-id="b28" data-open="b28" class="link link-ref link-reveal xref-bibr">28</a>,<span class="xrefLink" id="jumplink-b56"></span><a href="javascript:;" reveal-id="b56" data-open="b56" class="link link-ref link-reveal xref-bibr">56</a>] (<span class="xrefLink" id="jumplink-f6"></span><a href="javascript:;" data-modal-source-id="f6" class="link xref-fig">Fig. 6</a>). Several studies have clearly implicated the Yap1p and Snk7p transcription factors in regulating the expression of genes induced by oxidative stress (reviewed in [<span class="xrefLink" id="jumplink-b28"></span><a href="javascript:;" reveal-id="b28" data-open="b28" class="link link-ref link-reveal xref-bibr">28</a>]). These target genes include <em>GSH1</em> (γ-GCS), <em>GPX2</em> (GPx2), <em>GLR1</em> [glutathione reductase (GLR): GS-SG+NADPH+H<sup>+</sup>→2 GSH+NADP<sup>+</sup>, EC 1.6.4.2], <em>TRX2</em> (Trx) and <em>TRR1</em> (thioredoxin reductase (TR)).</p> <a id="89588972" scrollto-destination="89588972"></a> <div data-id="f6" data-content-id="f6" class="fig fig-section js-fig-section" swap-content-for-modal="true"><div class="graphic-wrap"><img class="content-image" src="https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/m_FYR_295_f6.jpeg?Expires=1736287804&Signature=cqzpke-x72oAXiV6msT4VkBPEp9e0Md8rj40~j2Ts3QGC~2JpPODvfiJw80mJuxRG-mBODeAEXZQZHF0E7G8wRMfV3FyyjErnGXLK4Np2xk72wNyEavItwqXiXrS9zkc8L4OuFSvA4i7Lq7uDaB7vJjq4RbdfdcmvmGEF7ZGd1sXAAkb1RCn2KdzlqRH1~SkoMKgAN-oU5LJUWxy3Sza6iH2inFdy9UTYed1b7i-I0aNtGd6ldBUVjP7TKZRUqtJhT-ZMaJYpDFWp8spNZwGfmpRskrEpt573yJ30712oX~avTspFVpwF46igYwAKNip2nts-OXxMZZeiUz1tdIH7w__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA" alt="Roles of GPx and thioredoxin reductase in the response of S. cerevisiae to hydroperoxides. GLR, glutathione reductase; TR, thioredoxin reductase; Trx, thioredoxin; TPx, thioredoxin peroxidase." data-path-from-xml="FYR_295_f6.jpeg" /><div class="graphic-bottom"><div class="label fig-label" id="label-89588972">6</div><div class="caption fig-caption"><p class="chapter-para">Roles of GPx and thioredoxin reductase in the response of <em>S. cerevisiae</em> to hydroperoxides. GLR, glutathione reductase; TR, thioredoxin reductase; Trx, thioredoxin; TPx, thioredoxin peroxidase.</p></div><div class="ajax-articleAbstract-exclude-regex fig-orig original-slide figure-button-wrap"><a class="fig-view-orig js-view-large at-figureViewLarge openInAnotherWindow" role="button" aria-describedby="label-89588972" href="/view-large/figure/89588972/FYR_295_f6.jpeg" data-path-from-xml="FYR_295_f6.jpeg" target="_blank">Open in new tab</a><a class="download-slide" role="button" aria-describedby="label-89588972" data-section="89588972" href="/DownloadFile/DownloadImage.aspx?image=https://oup.silverchair-cdn.com/oup/backfile/Content_public/Journal/femsyr/2/3/10.1016_S1567-1356%2802%2900081-8/1/FYR_295_f6.jpeg?Expires=1736287804&Signature=b2mOUwPQLO2MYCa5fPN9AJp28TXNa~rNW~2N3dTO1DZav46kJq2EHFBYwxA2~X9-C-28bAmuuRhPcui9Wf9M-e6pI59XE3hH4jEWPshs5JweiNm-DnWXJp7Sw1GvpqpjBfJXfZKWjktDASwi7fRYq-~cNpgnGZRheiHlj6dZNy8mf6t8clD7RUg1oA29FWcrDAi7nJb0oTVsfy1rY4tUZ2YR475V-wRJUIWS9c8ZiLpESi2jNpw~v0QVINML97ciE0xW9J8OTbiwpgxTcNJ3oUb-q~58g~LlNyMLXLi4wyiYJbu98s5~UYGgQrBUjB4nseP3m3cxOUARm8diYHiifw__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA&sec=89588972&ar=562518&xsltPath=~/UI/app/XSLT&imagename=&siteId=5387" data-path-from-xml="FYR_295_f6.jpeg">Download slide</a></div></div></div></div><p class="chapter-para">A Yap1p-dependent induction of GSH synthesis in heat shock response of <em>S. cerevisiae</em> was reported. Apparently heat shock stress enhances oxygen respiration, which in turn results in the increase of ROS in the mitochondria, necessitating the operation of a detoxification mechanism [<span class="xrefLink" id="jumplink-b59"></span><a href="javascript:;" reveal-id="b59" data-open="b59" class="link link-ref link-reveal xref-bibr">59</a>].</p><p class="chapter-para">The adaptive response of <em>S. pombe</em> to ROS may involve systems similar to those found in <em>S. cerevisiae</em>[<span class="xrefLink" id="jumplink-b60"></span><a href="javascript:;" reveal-id="b60" data-open="b60" class="link link-ref link-reveal xref-bibr">60</a>], but differences may exist. For example only one gene <em>GPX1</em> encoding a GPx was found in the fission yeast. As was found for <em>S. cerevisiae</em> GPxs, the <em>S. pombe</em> enzyme does not contain selenocysteine at its active center but rather a cysteine residue [<span class="xrefLink" id="jumplink-b57"></span><a href="javascript:;" reveal-id="b57" data-open="b57" class="link link-ref link-reveal xref-bibr">57</a>,<span class="xrefLink" id="jumplink-b61"></span><a href="javascript:;" reveal-id="b61" data-open="b61" class="link link-ref link-reveal xref-bibr">61</a>].</p><p class="chapter-para">Diamide [(CH<sub>3</sub>)<sub>2</sub>NC(O)NN(O)CN(CH<sub>3</sub>)<sub>2</sub>] and thiram [(CH<sub>3</sub>)<sub>2</sub>NC(S)S–S(S)CN(CH<sub>3</sub>)<sub>2</sub>], its dithiocarbamate homolog, may also be considered agents provoking oxidative stress because of their strong thiol-oxidizing properties [<span class="xrefLink" id="jumplink-b62"></span><a href="javascript:;" reveal-id="b62" data-open="b62" class="link link-ref link-reveal xref-bibr">62</a>]. GSH may play a protecting role against thiram in <em>S. cerevisiae</em>[<span class="xrefLink" id="jumplink-b63"></span><a href="javascript:;" reveal-id="b63" data-open="b63" class="link link-ref link-reveal xref-bibr">63</a>].</p> <h3 scrollto-destination=89588987 id="89588987" class="section-title js-splitscreen-section-title" data-legacy-id=ss4-4>4.4 Detoxification of xenobiotics</h3> <p class="chapter-para">GSH plays a key role in cellular defence against reactive electrophiles such as halogenated aromatics. Many xenobiotics can react either spontaneously with the thiol moiety of GSH to form GSH <em>S</em>-conjugates, or via GSH <em>S</em>-transferases (GST: GSH+RX→GS-X+RH, EC 2.5.1.18) [<span class="xrefLink" id="jumplink-b11"></span><a href="javascript:;" reveal-id="b11" data-open="b11" class="link link-ref link-reveal xref-bibr">11</a>]. As mentioned above, Ycf1p appears as the major GS-X vacuolar transporter in <em>S. cerevisiae</em>, but yeasts may also transport GS-X outside the cells (<span class="xrefLink" id="jumplink-f4"></span><a href="javascript:;" data-modal-source-id="f4" class="link xref-fig">Fig. 4</a>) [<span class="xrefLink" id="jumplink-b64"></span><a href="javascript:;" reveal-id="b64" data-open="b64" class="link link-ref link-reveal xref-bibr">64</a>].</p><p class="chapter-para">A study of the global response of <em>S. cerevisiae</em> to methyl methanesulfonate (MMS) has shown that the transcripts of 325 ORFs were induced over four-fold by the reagent [<span class="xrefLink" id="jumplink-b65"></span><a href="javascript:;" reveal-id="b65" data-open="b65" class="link link-ref link-reveal xref-bibr">65</a>]. One of the strongest inductions observed (28.8-fold) was for <em>GTT2</em>, a gene encoding a putative GST. Moreover <em>CIS2</em> encoding γ-GT [<span class="xrefLink" id="jumplink-b31"></span><a href="javascript:;" reveal-id="b31" data-open="b31" class="link link-ref link-reveal xref-bibr">31</a>] and <em>PDR10</em> encoding a plasma membrane ABC transporter protein were induced respectively 7.7- and 8.8-fold in the same conditions. MMS is an alkylating agent that could react with GSH, and it is thus tempting to speculate about the existence in yeast of a prototype of the mammalian and plant mercapturic detoxification pathway [<span class="xrefLink" id="jumplink-b2"></span><a href="javascript:;" reveal-id="b2" data-open="b2" class="link link-ref link-reveal xref-bibr">2</a>].</p><p class="chapter-para">As(III) detoxification in <em>S. cerevisiae</em> involves two independent transport systems for the removal of arsenite from the cytosol [<span class="xrefLink" id="jumplink-b66"></span><a href="javascript:;" reveal-id="b66" data-open="b66" class="link link-ref link-reveal xref-bibr">66</a>]. Acr3p is a plasma membrane protein mediating arsenite extrusion from the cells and Ycf1p catalyzes the ATP-driven uptake of the GSH conjugate As(GS)<sub>3</sub> into the central vacuole.</p> <h3 scrollto-destination=89589001 id="89589001" class="section-title js-splitscreen-section-title" data-legacy-id=ss4-5>4.5 Heavy metal stress. The cadmium story</h3> <p class="chapter-para">On a chemical reactivity basis it was expected that GSH would be able to form chelation complexes with heavy metals and may, in this way, be involved in detoxification. Studies of the cadmium response in yeasts have shed new light on the mechanisms of intervention of GSH in heavy metal detoxification. The story started with the NCY <em>S. pombe</em> and <em>Torulopsis glabrata</em>, where it was shown that exposure to Cd<sup>2+</sup> salts resulted in the biosynthesis of cadystins [phytochelatins (PhCs)]. PhCs are polymers of general structure (γ-Glu-Cys)<em><sub>n</sub></em>-Gly (2≥<em>n</em>≥11) (reviewed in [<span class="xrefLink" id="jumplink-b67"></span><a href="javascript:;" reveal-id="b67" data-open="b67" class="link link-ref link-reveal xref-bibr">67</a>,<span class="xrefLink" id="jumplink-b68"></span><a href="javascript:;" reveal-id="b68" data-open="b68" class="link link-ref link-reveal xref-bibr">68</a>]). These polypeptides, also found in some plant species [<span class="xrefLink" id="jumplink-b68"></span><a href="javascript:;" reveal-id="b68" data-open="b68" class="link link-ref link-reveal xref-bibr">68</a>], can chelate Cd<sup>2+</sup>, Cu<sup>2+</sup> and Zn<sup>2+</sup> ions in the cytosol. The complexes are then conveyed by an ABC transporter into the vacuole where they are deposited after bonding with acid-labile sulfide [<span class="xrefLink" id="jumplink-b69"></span><a href="javascript:;" reveal-id="b69" data-open="b69" class="link link-ref link-reveal xref-bibr">69</a>]. Mutants of <em>S. pombe</em> deficient in GSH have lost the ability to neutralize Cd<sup>2+</sup> and were also shown to be more sensitive to Cu<sup>2+</sup>, Zn<sup>2+</sup> and Pb<sup>2+</sup> ions [<span class="xrefLink" id="jumplink-b70"></span><a href="javascript:;" reveal-id="b70" data-open="b70" class="link link-ref link-reveal xref-bibr">70</a>]. The nature of the ‘phytochelatin synthetase’ (PCS) in <em>S. pombe</em> has been debated. PCS genes have been identified in <em>Arabidopsis</em> and <em>S. pombe</em>[<span class="xrefLink" id="jumplink-b71"></span><a href="javascript:;" reveal-id="b71" data-open="b71" class="link link-ref link-reveal xref-bibr">71</a>,<span class="xrefLink" id="jumplink-b72"></span><a href="javascript:;" reveal-id="b72" data-open="b72" class="link link-ref link-reveal xref-bibr">72</a>]. Disruption of the PCS gene in <em>S. pombe</em> leads to cadmium-sensitive mutants lacking PhCs. Expression of the protein in <em>S. cerevisiae</em> leads to PhC production and the recombinant purified <em>S. pombe</em> protein displayed PCS activity. Wolf and collaborators have shown that <em>GSH2</em> encodes a bifunctional enzyme able to catalyze both the synthesis of GSH by adding glycine to γ-Glu-Cys and the synthesis of PhCs [<span class="xrefLink" id="jumplink-b73"></span><a href="javascript:;" reveal-id="b73" data-open="b73" class="link link-ref link-reveal xref-bibr">73</a>]. However, the precise enzymatic mechanism of PhC synthesis remains to be determined.</p><p class="chapter-para"><em>S. cerevisiae</em> has evolved a cadmium sequestration mechanism independent of PhCs. In this yeast Cd<sup>2+</sup>(GSH)<sub>2</sub> complexes are transported into the vacuole by Ycf1p [<span class="xrefLink" id="jumplink-b74"></span><a href="javascript:;" reveal-id="b74" data-open="b74" class="link link-ref link-reveal xref-bibr">74</a>]. Challenge of the cells with Cd<sup>2+</sup> resulted in the induction of γ-GCS and eight other enzymes of the sulfur amino acid biosynthetic pathway [<span class="xrefLink" id="jumplink-b75"></span><a href="javascript:;" reveal-id="b75" data-open="b75" class="link link-ref link-reveal xref-bibr">75</a>]. The induction of these nine proteins is dependent on the Yap1p, Met-4, Met-31 and Met-32 transcription factors [<span class="xrefLink" id="jumplink-b76"></span><a href="javascript:;" reveal-id="b76" data-open="b76" class="link link-ref link-reveal xref-bibr">76</a>] Trx and TR also seem to play an important role in cadmium tolerance, which indicates that the two cellular thiol redox systems are essential for defence of <em>S. cerevisiae</em> against cadmium, as was similarly observed in the response to oxidative stress (see above).</p> <h3 scrollto-destination=89589012 id="89589012" class="section-title js-splitscreen-section-title" data-legacy-id=ss4-6>4.6 Glutathione and dimorphism</h3> <p class="chapter-para">Studies on <em>Candida albicans</em> have provided experimental data on the possible involvement of GSH in the regulation of yeast↔mycelium (Y↔M) transition [<span class="xrefLink" id="jumplink-b77"></span><a href="javascript:;" reveal-id="b77" data-open="b77" class="link link-ref link-reveal xref-bibr">77</a>,<span class="xrefLink" id="jumplink-b78"></span><a href="javascript:;" reveal-id="b78" data-open="b78" class="link link-ref link-reveal xref-bibr">78</a>]. In this fungus, the intracellular level of GSH decreased significantly during Y→M transition possibly due to an increase of the level of γ-GT in the germ tubes as compared to the yeast-form cells [<span class="xrefLink" id="jumplink-b77"></span><a href="javascript:;" reveal-id="b77" data-open="b77" class="link link-ref link-reveal xref-bibr">77</a>]. The hypothesis was made that changes in the intracellular level of GSH may trigger the initiation of a cascade of events leading ultimately to Y↔M conversion in <em>C. albicans</em>. Recent studies with <em>Aureobasidium pullulans</em>, an important industrial microorganism, support the view that key parameters governing cell morphology may modulate the intracellular level of GSH and lead to Y↔M transitions, as has been discussed for <em>C. albicans</em>[<span class="xrefLink" id="jumplink-b79"></span><a href="javascript:;" reveal-id="b79" data-open="b79" class="link link-ref link-reveal xref-bibr">79</a>]. Nevertheless, the mechanism is unlikely to proceed through modulation of protein thiol levels and none of the tested enzyme activities, including γ-GT, can satisfactorily explain the differences in GSH and GSSG in the mycelial and yeast forms of <em>A. pullulans</em>.</p> <h2 scrollto-destination=89589022 id="89589022" class="section-title js-splitscreen-section-title" data-legacy-id=ss5>5 Concluding remarks</h2> <p class="chapter-para">The widespread distribution of yeasts, even in hostile environments, may be explained in great part by powerful defence barriers becoming operative when these microorganisms are challenged with various exogenous stresses [<span class="xrefLink" id="jumplink-b6"></span><a href="javascript:;" reveal-id="b6" data-open="b6" class="link link-ref link-reveal xref-bibr">6</a>,<span class="xrefLink" id="jumplink-b80"></span><a href="javascript:;" reveal-id="b80" data-open="b80" class="link link-ref link-reveal xref-bibr">80</a>]. While it seems obvious that GSH is implicated in numerous stress response mechanisms, the tripeptide may also play a role in the maintenance of basic functions like cellular structure integrity. However, as these endogenous protection mechanisms often appear linked to detoxification problematics, for example of ROS generated during membrane electron transport, or of harmful metabolic by-products [<span class="xrefLink" id="jumplink-b22"></span><a href="javascript:;" reveal-id="b22" data-open="b22" class="link link-ref link-reveal xref-bibr">22</a>], other mechanisms are possible [<span class="xrefLink" id="jumplink-b19"></span><a href="javascript:;" reveal-id="b19" data-open="b19" class="link link-ref link-reveal xref-bibr">19</a>]. Intervention of GSH in the <em>Aureobasidium</em> Y↔M transition may represent another category of mechanisms where the thiol plays a role not related to detoxification.</p><p class="chapter-para">Investigations of GSH in NCY have revealed common traits with <em>S. cerevisiae</em> but, as shown in this review, differences may exist. These could reflect specific adaptation to the ecological niches where these strains are living. From the point of view of microbial technology it might be profitable to exploit these differences, in order to obtain strains better adapted to the frequent environmental stresses occurring before, during and after the fermentation process [<span class="xrefLink" id="jumplink-b6"></span><a href="javascript:;" reveal-id="b6" data-open="b6" class="link link-ref link-reveal xref-bibr">6</a>]. <em>S. cerevisiae</em> has played and still plays a leading role in yeast GSH research. However, the advent of genome databases for NCY will certainly stimulate research on other fascinating members of the yeast community.</p> <h2 scrollto-destination=89589032 id="89589032" class="backacknowledgements-title js-splitscreen-backacknowledgements-title" >Acknowledgements</h2> <p class="chapter-para">Many thanks are addressed to the GSH community of the laboratory, Charles Jaspers, Jean Yves Springael and Sophie Pomorski, for their communicating enthusiasm. I do not forget my colleague and friend Istvan Pocsi from the University of Debrecen in Hungary for his unfailing dynamism. I am strongly indebted to Atef Jaouani for his skilful assistance in the preparation of the figures illustrating this review.</p> <h2 scrollto-destination=89589035 id="89589035" class="backreferences-title js-splitscreen-backreferences-title" >References</h2> <div class="ref-list js-splitview-ref-list"><div content-id="b1" class="js-splitview-ref-item" data-legacy-id="b1"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b1" href="javascript:;" aria-label="jumplink-b1" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b1" class="ref-content " data-id="b1"><span class="label title-label">[1]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Meister</div> <div class="given-names">A.</div> </div> </span> (<div class="year">1988</div>) <div class="article-title">On the discovery of glutathione</div>. <div class="source ">Trends Biochem. Sci.</div><div class="volume">13</div>, <div class="fpage">185</div>–<div class="lpage">188</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=On%20the%20discovery%20of%20glutathione&author=A.%20Meister&publication_year=1988&journal=Trends%20Biochem.%20Sci.&volume=13&pages=185-188" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1016/0968-0004(88)90148-X" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1016%2F0968-0004(88)90148-X" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1016%2F0968-0004(88)90148-X"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/3076280" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:On%20the%20discovery%20of%20glutathione&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b2" class="js-splitview-ref-item" data-legacy-id="b2"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b2" href="javascript:;" aria-label="jumplink-b2" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b2" class="ref-content " data-id="b2"><span class="label title-label">[2]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Meister</div> <div class="given-names">A.</div> </div> <div class="name"> <div class="surname">Anderson</div> <div class="given-names">M.E.</div> </div> </span> (<div class="year">1983</div>) <div class="article-title">Glutathione</div>. <div class="source ">Annu. Rev. Biochem.</div><div class="volume">52</div>, <div class="fpage">711</div>–<div class="lpage">760</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione&author=A.%20Meister&author=M.E.%20Anderson&publication_year=1983&journal=Annu.%20Rev.%20Biochem.&volume=52&pages=711-760" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1146/annurev.bi.52.070183.003431" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1146%2Fannurev.bi.52.070183.003431" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1146%2Fannurev.bi.52.070183.003431"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/6137189" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b3" class="js-splitview-ref-item" data-legacy-id="b3"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b3" href="javascript:;" aria-label="jumplink-b3" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b3" class="ref-content " data-id="b3"><span class="label title-label">[3]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Penninckx</div> <div class="given-names">M.J.</div> </div> <div class="name"> <div class="surname">Elskens</div> <div class="given-names">M.T.</div> </div> </span> (<div class="year">1993</div>) <div class="article-title">Metabolism and functions of glutathione in micro-organisms</div>. <div class="source ">Adv. Microb. Physiol.</div><div class="volume">32</div>, <div class="fpage">239</div>–<div class="lpage">240</div>. </p><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Metabolism%20and%20functions%20of%20glutathione%20in%20micro-organisms&author=M.J.%20Penninckx&author=M.T.%20Elskens&publication_year=1993&journal=Adv.%20Microb.%20Physiol.&volume=32&pages=239-240" target="_blank">Google Scholar</a></span></p><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=Metabolism+and+functions+of+glutathione+in+micro-organisms&aulast=Penninckx&title=Adv.+Microb.+Physiol.&date=1993&spage=239&epage=240&volume=32" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Metabolism%20and%20functions%20of%20glutathione%20in%20micro-organisms&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b4" class="js-splitview-ref-item" data-legacy-id="b4"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b4" href="javascript:;" aria-label="jumplink-b4" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b4" class="ref-content " data-id="b4"><span class="label title-label">[4]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Hell</div> <div class="given-names">R.</div> </div> </span> (<div class="year">1997</div>) <div class="article-title">Molecular physiology of plant sulfur metabolism</div>. <div class="source ">Planta</div><div class="volume">202</div>, <div class="fpage">138</div>–<div class="lpage">148</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Molecular%20physiology%20of%20plant%20sulfur%20metabolism&author=R.%20Hell&publication_year=1997&journal=Planta&volume=202&pages=138-148" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1007/s004250050112" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1007%2Fs004250050112" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1007%2Fs004250050112"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/9202491" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Molecular%20physiology%20of%20plant%20sulfur%20metabolism&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b5" class="js-splitview-ref-item" data-legacy-id="b5"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b5" href="javascript:;" aria-label="jumplink-b5" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b5" class="ref-content " data-id="b5"><span class="label title-label">[5]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Gasch</div> <div class="given-names">A.P.</div> </div> <div class="name"> <div class="surname">Spellman</div> <div class="given-names">P.T.</div> </div> <div class="name"> <div class="surname">Kao</div> <div class="given-names">C.M.</div> </div> <div class="name"> <div class="surname">Carmel-Harel</div> <div class="given-names">O.</div> </div> <div class="name"> <div class="surname">Eisen</div> <div class="given-names">M.B.</div> </div> <div class="name"> <div class="surname">Storz</div> <div class="given-names">G.</div> </div> <div class="name"> <div class="surname">Botstein</div> <div class="given-names">D.</div> </div> <div class="name"> <div class="surname">Brown</div> <div class="given-names">P.O.</div> </div> </span> (<div class="year">2000</div>) <div class="article-title">Genomic expression programs in the response of yeast cells to environmental changes</div>. <div class="source ">Mol. Biol. Cell</div><div class="volume">11</div>, <div class="fpage">4241</div>–<div class="lpage">4257</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Genomic%20expression%20programs%20in%20the%20response%20of%20yeast%20cells%20to%20environmental%20changes&author=A.P.%20Gasch&author=P.T.%20Spellman&author=C.M.%20Kao&author=O.%20Carmel-Harel&author=M.B.%20Eisen&author=G.%20Storz&author=D.%20Botstein&author=P.O.%20Brown&publication_year=2000&journal=Mol.%20Biol.%20Cell&volume=11&pages=4241-4257" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1091/mbc.11.12.4241" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1091%2Fmbc.11.12.4241" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1091%2Fmbc.11.12.4241"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11102521" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Genomic%20expression%20programs%20in%20the%20response%20of%20yeast%20cells%20to%20environmental%20changes&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b6" class="js-splitview-ref-item" data-legacy-id="b6"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b6" href="javascript:;" aria-label="jumplink-b6" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b6" class="ref-content " data-id="b6"><span class="label title-label">[6]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Walker</div> <div class="given-names">G.</div> </div> </span> (<div class="year">1998</div>) <div class="source ">Yeast Physiology and Biotechnology</div>. <div class="publisher-name">J. Wiley and Sons</div>, <div class="publisher-loc">New York</div>.</p><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Yeast%20Physiology%20and%20Biotechnology&author=G.%20Walker&publication_year=1998&book=Yeast%20Physiology%20and%20Biotechnology" target="_blank">Google Scholar</a></span></p><p class="citation-links-compatibility"><span class="google-preview-ref-link js-google-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.google.com/search?q=Yeast%20Physiology%20and%20Biotechnology&btnG=Search+Books&tbm=bks&tbo=1" target="_blank">Google Preview</a></span></p><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=book&title=Yeast+Physiology+and+Biotechnology&aulast=Walker&date=1998" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Yeast%20Physiology%20and%20Biotechnology&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p><div class="copac-reference-ref-link js-copac-preview-ref-link" style="display:none" data-pubtype="book"><span class="inst-copac"><a class="openInAnotherWindow" target="_blank" href="http://copac.ac.uk/search?ti=Yeast%20Physiology%20and%20Biotechnology">COPAC</a></span></div> </div></div></div></div></div><div content-id="b7" class="js-splitview-ref-item" data-legacy-id="b7"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b7" href="javascript:;" aria-label="jumplink-b7" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b7" class="ref-content " data-id="b7"><span class="label title-label">[7]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Sahm</div> <div class="given-names">H.</div> </div> </span> (<div class="year">1977</div>) <div class="article-title">Metabolism of methanol by yeasts</div>. <div class="source ">Adv. Biochem. Eng.</div><div class="volume">6</div>, <div class="fpage">103</div>–<div class="lpage">127</div>. </p><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Metabolism%20of%20methanol%20by%20yeasts&author=H.%20Sahm&publication_year=1977&journal=Adv.%20Biochem.%20Eng.&volume=6&pages=103-127" target="_blank">Google Scholar</a></span></p><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=Metabolism+of+methanol+by+yeasts&aulast=Sahm&title=Adv.+Biochem.+Eng.&date=1977&spage=103&epage=127&volume=6" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Metabolism%20of%20methanol%20by%20yeasts&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b8" class="js-splitview-ref-item" data-legacy-id="b8"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b8" href="javascript:;" aria-label="jumplink-b8" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b8" class="ref-content " data-id="b8"><span class="label title-label">[8]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Cereghino</div> <div class="given-names">L.</div> </div> <div class="name"> <div class="surname">Cregg</div> <div class="given-names">J.M.</div> </div> </span> (<div class="year">2000</div>) <div class="article-title">Heterologous protein expression in the methylotrophic yeast <em>Pichia pastoris</em></div>. <div class="source ">FEMS Microbiol. Rev.</div><div class="volume">24</div>, <div class="fpage">45</div>–<div class="lpage">66</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Heterologous%20protein%20expression%20in%20the%20methylotrophic%20yeast%20Pichia%20pastoris&author=L.%20Cereghino&author=J.M.%20Cregg&publication_year=2000&journal=FEMS%20Microbiol.%20Rev.&volume=24&pages=45-66" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1111/j.1574-6976.2000.tb00532.x" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1111%2Fj.1574-6976.2000.tb00532.x" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1111%2Fj.1574-6976.2000.tb00532.x"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/10640598" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Heterologous%20protein%20expression%20in%20the%20methylotrophic%20yeast%20Pichia%20pastoris&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b9" class="js-splitview-ref-item" data-legacy-id="b9"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b9" href="javascript:;" aria-label="jumplink-b9" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b9" class="ref-content " data-id="b9"><span class="label title-label">[9]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Fahey</div> <div class="given-names">R.C.</div> </div> </span> (<div class="year">2001</div>) <div class="article-title">Novel thiols of prokaryotes</div>. <div class="source ">Annu. Rev. Microbiol.</div><div class="volume">55</div>, <div class="fpage">533</div>–<div class="lpage">556</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Novel%20thiols%20of%20prokaryotes&author=R.C.%20Fahey&publication_year=2001&journal=Annu.%20Rev.%20Microbiol.&volume=55&pages=533-556" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1146/annurev.micro.55.1.333" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1146%2Fannurev.micro.55.1.333" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1146%2Fannurev.micro.55.1.333"> </span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Novel%20thiols%20of%20prokaryotes&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b10" class="js-splitview-ref-item" data-legacy-id="b10"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b10" href="javascript:;" aria-label="jumplink-b10" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b10" class="ref-content " data-id="b10"><span class="label title-label">[10]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Newton</div> <div class="given-names">G.L.</div> </div> <div class="name"> <div class="surname">Arnold</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Price</div> <div class="given-names">M.S.</div> </div> <div class="name"> <div class="surname">Sherrill</div> <div class="given-names">C.</div> </div> <div class="name"> <div class="surname">Delcardayre</div> <div class="given-names">S.B.</div> </div> <div class="name"> <div class="surname">Aharonowitz</div> <div class="given-names">Y.</div> </div> <div class="name"> <div class="surname">Cohen</div> <div class="given-names">G.</div> </div> <div class="name"> <div class="surname">Davies</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Fahey</div> <div class="given-names">R.</div> </div> <div class="name"> <div class="surname">Davis</div> <div class="given-names">C.</div> </div> </span> (<div class="year">1996</div>) <div class="article-title">Distribution of thiols in micro-organisms: mycothiol is a major thiol in most actinomycetes</div>. <div class="source ">J. Bacteriol.</div><div class="volume">178</div>, <div class="fpage">1990</div>–<div class="lpage">1995</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Distribution%20of%20thiols%20in%20micro-organisms%3A%20mycothiol%20is%20a%20major%20thiol%20in%20most%20actinomycetes&author=G.L.%20Newton&author=K.%20Arnold&author=M.S.%20Price&author=C.%20Sherrill&author=S.B.%20Delcardayre&author=Y.%20Aharonowitz&author=G.%20Cohen&author=J.%20Davies&author=R.%20Fahey&author=C.%20Davis&publication_year=1996&journal=J.%20Bacteriol.&volume=178&pages=1990-1995" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1128/jb.178.7.1990-1995.1996" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1128%2Fjb.178.7.1990-1995.1996" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1128%2Fjb.178.7.1990-1995.1996"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/8606174" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Distribution%20of%20thiols%20in%20micro-organisms%3A%20mycothiol%20is%20a%20major%20thiol%20in%20most%20actinomycetes&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b11" class="js-splitview-ref-item" data-legacy-id="b11"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b11" href="javascript:;" aria-label="jumplink-b11" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b11" class="ref-content " data-id="b11"><span class="label title-label">[11]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Vuilleumier</div> <div class="given-names">S.</div> </div> </span> (<div class="year">1997</div>) <div class="article-title">Bacterial glutathione S-transferases: what are they good for</div>. <div class="source ">J. Bacteriol.</div><div class="volume">179</div>, <div class="fpage">1431</div>–<div class="lpage">1441</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Bacterial%20glutathione%20S-transferases%3A%20what%20are%20they%20good%20for&author=S.%20Vuilleumier&publication_year=1997&journal=J.%20Bacteriol.&volume=179&pages=1431-1441" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1128/jb.179.5.1431-1441.1997" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1128%2Fjb.179.5.1431-1441.1997" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1128%2Fjb.179.5.1431-1441.1997"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/9045797" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Bacterial%20glutathione%20S-transferases%3A%20what%20are%20they%20good%20for&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b12" class="js-splitview-ref-item" data-legacy-id="b12"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b12" href="javascript:;" aria-label="jumplink-b12" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b12" class="ref-content " data-id="b12"><span class="label title-label">[12]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Newton</div> <div class="given-names">G.L.</div> </div> <div class="name"> <div class="surname">Javor</div> <div class="given-names">B.</div> </div> </span> (<div class="year">1985</div>) <div class="article-title">γ-Glutamylcysteine and thiosulfate are the major low molecular weight thiols in halobacteria</div>. <div class="source ">J. Bacteriol.</div><div class="volume">161</div>, <div class="fpage">438</div>–<div class="lpage">441</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=%CE%B3-Glutamylcysteine%20and%20thiosulfate%20are%20the%20major%20low%20molecular%20weight%20thiols%20in%20halobacteria&author=G.L.%20Newton&author=B.%20Javor&publication_year=1985&journal=J.%20Bacteriol.&volume=161&pages=438-441" target="_blank">Google Scholar</a></span></p><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/2857165" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=%ce%b3-Glutamylcysteine+and+thiosulfate+are+the+major+low+molecular+weight+thiols+in+halobacteria&aulast=Newton&title=J.+Bacteriol.&date=1985&spage=438&epage=441&volume=161" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:%CE%B3-Glutamylcysteine%20and%20thiosulfate%20are%20the%20major%20low%20molecular%20weight%20thiols%20in%20halobacteria&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b13" class="js-splitview-ref-item" data-legacy-id="b13"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b13" href="javascript:;" aria-label="jumplink-b13" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b13" class="ref-content " data-id="b13"><span class="label title-label">[13]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Fahey</div> <div class="given-names">R.C.</div> </div> <div class="name"> <div class="surname">Newton</div> <div class="given-names">G.L.</div> </div> <div class="name"> <div class="surname">Arrick</div> <div class="given-names">B.</div> </div> <div class="name"> <div class="surname">Overdank-Bogart</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Aley</div> <div class="given-names">S.B.</div> </div> </span> (<div class="year">1984</div>) <div class="article-title"><em>Entamoeba histolytica</em>: a eukaryote without glutathione metabolism</div>. <div class="source ">Science</div><div class="volume">224</div>, <div class="fpage">70</div>–<div class="lpage">73</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Entamoeba%20histolytica%3A%20a%20eukaryote%20without%20glutathione%20metabolism&author=R.C.%20Fahey&author=G.L.%20Newton&author=B.%20Arrick&author=T.%20Overdank-Bogart&author=S.B.%20Aley&publication_year=1984&journal=Science&volume=224&pages=70-73" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1126/science.6322306" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1126%2Fscience.6322306" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1126%2Fscience.6322306"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/6322306" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Entamoeba%20histolytica%3A%20a%20eukaryote%20without%20glutathione%20metabolism&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b14" class="js-splitview-ref-item" data-legacy-id="b14"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b14" href="javascript:;" aria-label="jumplink-b14" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b14" class="ref-content " data-id="b14"><span class="label title-label">[14]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Mehdi</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Penninckx</div> <div class="given-names">M.J.</div> </div> </span> (<div class="year">1997</div>) <div class="article-title">An important role for glutathione and γ-glutamyltranspeptidase in the supply of growth requirements during nitrogen starvation of the yeast <em>Saccharomyces cerevisiae</em></div>. <div class="source ">Microbiology</div><div class="volume">143</div>, <div class="fpage">1885</div>–<div class="lpage">1889</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=An%20important%20role%20for%20glutathione%20and%20%CE%B3-glutamyltranspeptidase%20in%20the%20supply%20of%20growth%20requirements%20during%20nitrogen%20starvation%20of%20the%20yeast%20Saccharomyces%20cerevisiae&author=K.%20Mehdi&author=M.J.%20Penninckx&publication_year=1997&journal=Microbiology&volume=143&pages=1885-1889" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1099/00221287-143-6-1885" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1099%2F00221287-143-6-1885" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1099%2F00221287-143-6-1885"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/9202464" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:An%20important%20role%20for%20glutathione%20and%20%CE%B3-glutamyltranspeptidase%20in%20the%20supply%20of%20growth%20requirements%20during%20nitrogen%20starvation%20of%20the%20yeast%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b15" class="js-splitview-ref-item" data-legacy-id="b15"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b15" href="javascript:;" aria-label="jumplink-b15" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b15" class="ref-content " data-id="b15"><span class="label title-label">[15]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Grant</div> <div class="given-names">C.M.</div> </div> <div class="name"> <div class="surname">MacIver</div> <div class="given-names">F.H.</div> </div> <div class="name"> <div class="surname">Dawes</div> <div class="given-names">I.W.</div> </div> </span> (<div class="year">1996</div>) <div class="article-title">Glutathione is an essential metabolite required for resistance to oxidative stress in the yeast <em>Saccharomyces cerevisiae</em></div>. <div class="source ">Curr. Genet.</div><div class="volume">29</div>, <div class="fpage">511</div>–<div class="lpage">515</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione%20is%20an%20essential%20metabolite%20required%20for%20resistance%20to%20oxidative%20stress%20in%20the%20yeast%20Saccharomyces%20cerevisiae&author=C.M.%20Grant&author=F.H.%20MacIver&author=I.W.%20Dawes&publication_year=1996&journal=Curr.%20Genet.&volume=29&pages=511-515" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1007/BF02426954" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1007%2FBF02426954" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1007%2FBF02426954"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/8662189" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione%20is%20an%20essential%20metabolite%20required%20for%20resistance%20to%20oxidative%20stress%20in%20the%20yeast%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b16" class="js-splitview-ref-item" data-legacy-id="b16"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b16" href="javascript:;" aria-label="jumplink-b16" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b16" class="ref-content " data-id="b16"><span class="label title-label">[16]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Spector</div> <div class="given-names">D.</div> </div> <div class="name"> <div class="surname">Labarre</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Toledano</div> <div class="given-names">M.B.</div> </div> </span> (<div class="year">2001</div>) <div class="article-title">A genetic investigation of the essential role of glutathione. Mutations in the proline biosynthesis pathway are the only suppressors of glutathione auxotrophy in yeast</div>. <div class="source ">J. Biol. Chem.</div><div class="volume">276</div>, <div class="fpage">7011</div>–<div class="lpage">7016</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=A%20genetic%20investigation%20of%20the%20essential%20role%20of%20glutathione.%20Mutations%20in%20the%20proline%20biosynthesis%20pathway%20are%20the%20only%20suppressors%20of%20glutathione%20auxotrophy%20in%20yeast&author=D.%20Spector&author=J.%20Labarre&author=M.B.%20Toledano&publication_year=2001&journal=J.%20Biol.%20Chem.&volume=276&pages=7011-7016" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.M009814200" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.M009814200" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.M009814200"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11084050" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:A%20genetic%20investigation%20of%20the%20essential%20role%20of%20glutathione.%20Mutations%20in%20the%20proline%20biosynthesis%20pathway%20are%20the%20only%20suppressors%20of%20glutathione%20auxotrophy%20in%20yeast&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b17" class="js-splitview-ref-item" data-legacy-id="b17"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b17" href="javascript:;" aria-label="jumplink-b17" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b17" class="ref-content " data-id="b17"><span class="label title-label">[17]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Stephen</div> <div class="given-names">W.S.</div> </div> <div class="name"> <div class="surname">Jamieson</div> <div class="given-names">S.D.</div> </div> </span> (<div class="year">1996</div>) <div class="article-title">Glutathione is an important antioxidant molecule in the yeast <em>Saccharomyces cerevisiae</em></div>. <div class="source ">FEMS Lett.</div><div class="volume">141</div>, <div class="fpage">207</div>–<div class="lpage">212</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione%20is%20an%20important%20antioxidant%20molecule%20in%20the%20yeast%20Saccharomyces%20cerevisiae&author=W.S.%20Stephen&author=S.D.%20Jamieson&publication_year=1996&journal=FEMS%20Lett.&volume=141&pages=207-212" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1111/fml.1996.141.issue-2-3" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1111%2Ffml.1996.141.issue-2-3" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1111%2Ffml.1996.141.issue-2-3"> </span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione%20is%20an%20important%20antioxidant%20molecule%20in%20the%20yeast%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b18" class="js-splitview-ref-item" data-legacy-id="b18"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b18" href="javascript:;" aria-label="jumplink-b18" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b18" class="ref-content " data-id="b18"><span class="label title-label">[18]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Kistler</div> <div class="given-names">M.</div> </div> <div class="name"> <div class="surname">Summer</div> <div class="given-names">K.H.</div> </div> <div class="name"> <div class="surname">Eckardt</div> <div class="given-names">F.</div> </div> </span> (<div class="year">1986</div>) <div class="article-title">Isolation of glutathione-dependent mutants of the yeast <em>Saccharomyces cerevisiae</em></div>. <div class="source ">Mutat. Res.</div><div class="volume">173</div>, <div class="fpage">117</div>–<div class="lpage">120</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Isolation%20of%20glutathione-dependent%20mutants%20of%20the%20yeast%20Saccharomyces%20cerevisiae&author=M.%20Kistler&author=K.H.%20Summer&author=F.%20Eckardt&publication_year=1986&journal=Mutat.%20Res.&volume=173&pages=117-120" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1016/0165-7992(86)90087-4" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1016%2F0165-7992(86)90087-4" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1016%2F0165-7992(86)90087-4"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/3511368" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Isolation%20of%20glutathione-dependent%20mutants%20of%20the%20yeast%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b19" class="js-splitview-ref-item" data-legacy-id="b19"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b19" href="javascript:;" aria-label="jumplink-b19" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b19" class="ref-content " data-id="b19"><span class="label title-label">[19]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Lee</div> <div class="given-names">J.C.</div> </div> <div class="name"> <div class="surname">Straffon</div> <div class="given-names">M.J.</div> </div> <div class="name"> <div class="surname">Jang</div> <div class="given-names">T.Y.</div> </div> <div class="name"> <div class="surname">Higgins</div> <div class="given-names">V.J.</div> </div> <div class="name"> <div class="surname">Grant</div> <div class="given-names">C.M.</div> </div> <div class="name"> <div class="surname">Dawes</div> <div class="given-names">I.W.</div> </div> </span> (<div class="year">2001</div>) <div class="article-title">The essential and ancillary role of glutathione in <em>Saccharomyces cerevisiae</em> analysed using a grande <em>gsh1</em> disruptant strain</div>. <div class="source ">FEMS Yeast Res.</div><div class="volume">1</div>, <div class="fpage">57</div>–<div class="lpage">65</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=The%20essential%20and%20ancillary%20role%20of%20glutathione%20in%20Saccharomyces%20cerevisiae%20analysed%20using%20a%20grande%20gsh1%20disruptant%20strain&author=J.C.%20Lee&author=M.J.%20Straffon&author=T.Y.%20Jang&author=V.J.%20Higgins&author=C.M.%20Grant&author=I.W.%20Dawes&publication_year=2001&journal=FEMS%20Yeast%20Res.&volume=1&pages=57-65" target="_blank">Google Scholar</a></span></p><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/12702463" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=The+essential+and+ancillary+role+of+glutathione+in+Saccharomyces+cerevisiae+analysed+using+a+grande+gsh1+disruptant+strain&aulast=Lee&title=FEMS+Yeast+Res.&date=2001&spage=57&epage=65&volume=1" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:The%20essential%20and%20ancillary%20role%20of%20glutathione%20in%20Saccharomyces%20cerevisiae%20analysed%20using%20a%20grande%20gsh1%20disruptant%20strain&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b20" class="js-splitview-ref-item" data-legacy-id="b20"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b20" href="javascript:;" aria-label="jumplink-b20" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b20" class="ref-content " data-id="b20"><span class="label title-label">[20]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Tu</div> <div class="given-names">B.P.</div> </div> <div class="name"> <div class="surname">Ho-Schleyer</div> <div class="given-names">S.C.</div> </div> <div class="name"> <div class="surname">Travers</div> <div class="given-names">K.J.</div> </div> <div class="name"> <div class="surname">Weissman</div> <div class="given-names">J.S.</div> </div> </span> (<div class="year">2000</div>) <div class="article-title">Biochemical basis of oxidative protein folding in the endoplasmic reticulum</div>. <div class="source ">Science</div><div class="volume">290</div>, <div class="fpage">1571</div>–<div class="lpage">1574</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Biochemical%20basis%20of%20oxidative%20protein%20folding%20in%20the%20endoplasmic%20reticulum&author=B.P.%20Tu&author=S.C.%20Ho-Schleyer&author=K.J.%20Travers&author=J.S.%20Weissman&publication_year=2000&journal=Science&volume=290&pages=1571-1574" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1126/science.290.5496.1571" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1126%2Fscience.290.5496.1571" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1126%2Fscience.290.5496.1571"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11090354" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Biochemical%20basis%20of%20oxidative%20protein%20folding%20in%20the%20endoplasmic%20reticulum&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b21" class="js-splitview-ref-item" data-legacy-id="b21"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b21" href="javascript:;" aria-label="jumplink-b21" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b21" class="ref-content " data-id="b21"><span class="label title-label">[21]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Grant</div> <div class="given-names">C.M.</div> </div> <div class="name"> <div class="surname">MacIver</div> <div class="given-names">F.H.</div> </div> <div class="name"> <div class="surname">Dawes</div> <div class="given-names">I.W.</div> </div> </span> (<div class="year">1997</div>) <div class="article-title">Glutathione synthetase is dispensable for growth under both normal and oxidative stress conditions in the yeast <em>Saccharomyces cerevisiae</em> due to the accumulation of the dipeptide γ-glutamylcysteine</div>. <div class="source ">Mol. Biol. Cell</div><div class="volume">8</div>, <div class="fpage">1699</div>–<div class="lpage">1707</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione%20synthetase%20is%20dispensable%20for%20growth%20under%20both%20normal%20and%20oxidative%20stress%20conditions%20in%20the%20yeast%20Saccharomyces%20cerevisiae%20due%20to%20the%20accumulation%20of%20the%20dipeptide%20%CE%B3-glutamylcysteine&author=C.M.%20Grant&author=F.H.%20MacIver&author=I.W.%20Dawes&publication_year=1997&journal=Mol.%20Biol.%20Cell&volume=8&pages=1699-1707" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1091/mbc.8.9.1699" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1091%2Fmbc.8.9.1699" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1091%2Fmbc.8.9.1699"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/9307967" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione%20synthetase%20is%20dispensable%20for%20growth%20under%20both%20normal%20and%20oxidative%20stress%20conditions%20in%20the%20yeast%20Saccharomyces%20cerevisiae%20due%20to%20the%20accumulation%20of%20the%20dipeptide%20%CE%B3-glutamylcysteine&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b22" class="js-splitview-ref-item" data-legacy-id="b22"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b22" href="javascript:;" aria-label="jumplink-b22" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b22" class="ref-content " data-id="b22"><span class="label title-label">[22]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Penninckx</div> <div class="given-names">M.J.</div> </div> <div class="name"> <div class="surname">Jaspers</div> <div class="given-names">Ch.</div> </div> <div class="name"> <div class="surname">Legrain</div> <div class="given-names">M.</div> </div> </span> (<div class="year">1983</div>) <div class="article-title">The glutathione-dependent glyoxalase pathway in the yeast <em>Saccharomyces cerevisiae</em>. A vital defence line against methylglyoxal produced during glycerol catabolism</div>. <div class="source ">J. Biol. Chem.</div><div class="volume">258</div>, <div class="fpage">6030</div>–<div class="lpage">6036</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=The%20glutathione-dependent%20glyoxalase%20pathway%20in%20the%20yeast%20Saccharomyces%20cerevisiae.%20A%20vital%20defence%20line%20against%20methylglyoxal%20produced%20during%20glycerol%20catabolism&author=M.J.%20Penninckx&author=Ch.%20Jaspers&author=M.%20Legrain&publication_year=1983&journal=J.%20Biol.%20Chem.&volume=258&pages=6030-6036" target="_blank">Google Scholar</a></span></p><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/6343368" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=The+glutathione-dependent+glyoxalase+pathway+in+the+yeast+Saccharomyces+cerevisiae.+A+vital+defence+line+against+methylglyoxal+produced+during+glycerol+catabolism&aulast=Penninckx&title=J.+Biol.+Chem.&date=1983&spage=6030&epage=6036&volume=258" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:The%20glutathione-dependent%20glyoxalase%20pathway%20in%20the%20yeast%20Saccharomyces%20cerevisiae.%20A%20vital%20defence%20line%20against%20methylglyoxal%20produced%20during%20glycerol%20catabolism&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b23" class="js-splitview-ref-item" data-legacy-id="b23"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b23" href="javascript:;" aria-label="jumplink-b23" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b23" class="ref-content " data-id="b23"><span class="label title-label">[23]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Bergmann</div> <div class="given-names">L.</div> </div> <div class="name"> <div class="surname">Rennenberg</div> <div class="given-names">H.</div> </div> </span> (<div class="year">1993</div>) <div class="article-title">Glutathione metabolism in plants</div>. In: <div class="source ">Sulfur Nutrition and Assimilation in Higher Plants. Regulatory, agricultural and environmental aspects</div> ( <span class="person-group"><div class="name"><div class="surname">de Kok</div> <div class="given-names">L.J.</div></div> <div class="name"><div class="surname">Stulen</div> <div class="given-names">I.</div></div> <div class="name"><div class="surname">Rennenberg</div> <div class="given-names">H.</div></div> <div class="name"><div class="surname">Brunold</div> <div class="given-names">C.</div></div> <div class="name"><div class="surname">Rauser</div> <div class="given-names">W.</div></div></span>, Eds.), pp. <div class="fpage">102</div>–<div class="lpage">123</div>. <div class="publisher-name">SPB Academic</div>, <div class="publisher-loc">The Hague</div>.</p><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Sulfur%20Nutrition%20and%20Assimilation%20in%20Higher%20Plants.%20Regulatory%2C%20agricultural%20and%20environmental%20aspects&author=L.%20Bergmann&author=H.%20Rennenberg&author=L.J.%20de%20Kok&author=I.%20Stulen&author=H.%20Rennenberg&author=C.%20Brunold&author=W.%20Rauser&publication_year=1993&book=Sulfur%20Nutrition%20and%20Assimilation%20in%20Higher%20Plants.%20Regulatory%2C%20agricultural%20and%20environmental%20aspects" target="_blank">Google Scholar</a></span></p><p class="citation-links-compatibility"><span class="google-preview-ref-link js-google-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.google.com/search?q=Sulfur%20Nutrition%20and%20Assimilation%20in%20Higher%20Plants.%20Regulatory%2C%20agricultural%20and%20environmental%20aspects&btnG=Search+Books&tbm=bks&tbo=1" target="_blank">Google Preview</a></span></p><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=book&title=Sulfur+Nutrition+and+Assimilation+in+Higher+Plants.+Regulatory%2c+agricultural+and+environmental+aspects&aulast=Bergmann&date=1993&spage=102&epage=123" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Sulfur%20Nutrition%20and%20Assimilation%20in%20Higher%20Plants.%20Regulatory%2C%20agricultural%20and%20environmental%20aspects&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p><div class="copac-reference-ref-link js-copac-preview-ref-link" style="display:none" data-pubtype="book"><span class="inst-copac"><a class="openInAnotherWindow" target="_blank" href="http://copac.ac.uk/search?ti=Sulfur%20Nutrition%20and%20Assimilation%20in%20Higher%20Plants.%20Regulatory%2C%20agricultural%20and%20environmental%20aspects">COPAC</a></span></div> </div></div></div></div></div><div content-id="b24" class="js-splitview-ref-item" data-legacy-id="b24"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b24" href="javascript:;" aria-label="jumplink-b24" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b24" class="ref-content " data-id="b24"><span class="label title-label">[24]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Jaspers</div> <div class="given-names">Ch.J.</div> </div> <div class="name"> <div class="surname">Gigot</div> <div class="given-names">D.</div> </div> <div class="name"> <div class="surname">Penninckx</div> <div class="given-names">M.J.</div> </div> </span> (<div class="year">1985</div>) <div class="article-title">Pathways of glutathione degradation in the yeast <em>Saccharomyces cerevisiae</em></div>. <div class="source ">Phytochemistry</div><div class="volume">24</div>, <div class="fpage">703</div>–<div class="lpage">707</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Pathways%20of%20glutathione%20degradation%20in%20the%20yeast%20Saccharomyces%20cerevisiae&author=Ch.J.%20Jaspers&author=D.%20Gigot&author=M.J.%20Penninckx&publication_year=1985&journal=Phytochemistry&volume=24&pages=703-707" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1016/S0031-9422(00)84880-3" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1016%2FS0031-9422(00)84880-3" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1016%2FS0031-9422(00)84880-3"> </span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Pathways%20of%20glutathione%20degradation%20in%20the%20yeast%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b25" class="js-splitview-ref-item" data-legacy-id="b25"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b25" href="javascript:;" aria-label="jumplink-b25" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b25" class="ref-content " data-id="b25"><span class="label title-label">[25]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Guo</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Breslow</div> <div class="given-names">E.</div> </div> <div class="name"> <div class="surname">Meister</div> <div class="given-names">A.</div> </div> </span> (<div class="year">1996</div>) <div class="article-title">The amino acid sequence of rat kidney 5-oxo-l-prolinase determined by cDNA cloning</div>. <div class="source ">J. Biol. Chem.</div><div class="volume">271</div>, <div class="fpage">32293</div>–<div class="lpage">32300</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=The%20amino%20acid%20sequence%20of%20rat%20kidney%205-oxo-l-prolinase%20determined%20by%20cDNA%20cloning&author=J.%20Guo&author=E.%20Breslow&author=A.%20Meister&publication_year=1996&journal=J.%20Biol.%20Chem.&volume=271&pages=32293-32300" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.271.50.32293" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.271.50.32293" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.271.50.32293"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/8943290" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:The%20amino%20acid%20sequence%20of%20rat%20kidney%205-oxo-l-prolinase%20determined%20by%20cDNA%20cloning&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b26" class="js-splitview-ref-item" data-legacy-id="b26"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b26" href="javascript:;" aria-label="jumplink-b26" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b26" class="ref-content " data-id="b26"><span class="label title-label">[26]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Grant</div> <div class="given-names">C.M.</div> </div> <div class="name"> <div class="surname">Dawes</div> <div class="given-names">I.</div> </div> </span> (<div class="year">1996</div>) <div class="article-title">Synthesis and role of glutathione in protection against oxidative stress in yeast</div>. <div class="source ">Redox Rep.</div><div class="volume">2</div>, <div class="fpage">223</div>–<div class="lpage">229</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Synthesis%20and%20role%20of%20glutathione%20in%20protection%20against%20oxidative%20stress%20in%20yeast&author=C.M.%20Grant&author=I.%20Dawes&publication_year=1996&journal=Redox%20Rep.&volume=2&pages=223-229" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1080/13510002.1996.11747054" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1080%2F13510002.1996.11747054" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1080%2F13510002.1996.11747054"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/27406271" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Synthesis%20and%20role%20of%20glutathione%20in%20protection%20against%20oxidative%20stress%20in%20yeast&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b27" class="js-splitview-ref-item" data-legacy-id="b27"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b27" href="javascript:;" aria-label="jumplink-b27" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b27" class="ref-content " data-id="b27"><span class="label title-label">[27]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Lee</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Godon</div> <div class="given-names">C.</div> </div> <div class="name"> <div class="surname">Lagniel</div> <div class="given-names">G.</div> </div> <div class="name"> <div class="surname">Spector</div> <div class="given-names">D.</div> </div> <div class="name"> <div class="surname">Garin</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Labarre</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Toledano</div> <div class="given-names">M.B.</div> </div> </span> (<div class="year">1999</div>) <div class="article-title">Yap1 and Skn7 control two specialized oxidative stress response regulons in yeast</div>. <div class="source ">J. Biol. Chem.</div><div class="volume">274</div>, <div class="fpage">16040</div>–<div class="lpage">16046</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Yap1%20and%20Skn7%20control%20two%20specialized%20oxidative%20stress%20response%20regulons%20in%20yeast&author=J.%20Lee&author=C.%20Godon&author=G.%20Lagniel&author=D.%20Spector&author=J.%20Garin&author=J.%20Labarre&author=M.B.%20Toledano&publication_year=1999&journal=J.%20Biol.%20Chem.&volume=274&pages=16040-16046" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.274.23.16040" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.274.23.16040" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.274.23.16040"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/10347154" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Yap1%20and%20Skn7%20control%20two%20specialized%20oxidative%20stress%20response%20regulons%20in%20yeast&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b28" class="js-splitview-ref-item" data-legacy-id="b28"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b28" href="javascript:;" aria-label="jumplink-b28" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b28" class="ref-content " data-id="b28"><span class="label title-label">[28]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Carmel-Harel</div> <div class="given-names">O.</div> </div> <div class="name"> <div class="surname">Storz</div> <div class="given-names">G.</div> </div> </span> (<div class="year">2000</div>) <div class="article-title">Roles of glutathione and thioredoxin-dependent reduction systems in the <em>Escherichia coli</em> and <em>Saccharomyces cerevisiae</em> responses to oxidative stress</div>. <div class="source ">Annu. Rev. Microbiol.</div><div class="volume">54</div>, <div class="fpage">439</div>–<div class="lpage">461</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Roles%20of%20glutathione%20and%20thioredoxin-dependent%20reduction%20systems%20in%20the%20Escherichia%20coli%20and%20Saccharomyces%20cerevisiae%20responses%20to%20oxidative%20stress&author=O.%20Carmel-Harel&author=G.%20Storz&publication_year=2000&journal=Annu.%20Rev.%20Microbiol.&volume=54&pages=439-461" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1146/annurev.micro.54.1.439" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1146%2Fannurev.micro.54.1.439" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1146%2Fannurev.micro.54.1.439"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11018134" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Roles%20of%20glutathione%20and%20thioredoxin-dependent%20reduction%20systems%20in%20the%20Escherichia%20coli%20and%20Saccharomyces%20cerevisiae%20responses%20to%20oxidative%20stress&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b29" class="js-splitview-ref-item" data-legacy-id="b29"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b29" href="javascript:;" aria-label="jumplink-b29" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b29" class="ref-content " data-id="b29"><span class="label title-label">[29]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Inoue</div> <div class="given-names">Y.</div> </div> <div class="name"> <div class="surname">Sugiyama</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Izawa</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Kimura</div> <div class="given-names">A.</div> </div> </span> (<div class="year">1998</div>) <div class="article-title">Molecular identification of glutathione synthetase (<em>GSH2</em>) gene from <em>Saccharomyces cerevisiae</em></div>. <div class="source ">Biochim. Biophys. Acta</div><div class="volume">1395</div>, <div class="fpage">315</div>–<div class="lpage">320</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Molecular%20identification%20of%20glutathione%20synthetase%20%28GSH2%29%20gene%20from%20Saccharomyces%20cerevisiae&author=Y.%20Inoue&author=K.%20Sugiyama&author=S.%20Izawa&author=A.%20Kimura&publication_year=1998&journal=Biochim.%20Biophys.%20Acta&volume=1395&pages=315-320" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1016/S0167-4781(97)00199-1" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1016%2FS0167-4781(97)00199-1" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1016%2FS0167-4781(97)00199-1"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/9512666" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Molecular%20identification%20of%20glutathione%20synthetase%20%28GSH2%29%20gene%20from%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b30" class="js-splitview-ref-item" data-legacy-id="b30"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b30" href="javascript:;" aria-label="jumplink-b30" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b30" class="ref-content " data-id="b30"><span class="label title-label">[30]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Penninckx</div> <div class="given-names">M.J.</div> </div> <div class="name"> <div class="surname">Jaspers</div> <div class="given-names">Ch.J.</div> </div> <div class="name"> <div class="surname">Wiame</div> <div class="given-names">J.M.</div> </div> </span> (<div class="year">1980</div>) <div class="article-title">Glutathione metabolism in relation to the amino acid permeation systems in the yeast <em>Saccharomyces cerevisiae</em></div>. <div class="source ">Eur. J. Biochem.</div><div class="volume">104</div>, <div class="fpage">119</div>–<div class="lpage">123</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione%20metabolism%20in%20relation%20to%20the%20amino%20acid%20permeation%20systems%20in%20the%20yeast%20Saccharomyces%20cerevisiae&author=M.J.%20Penninckx&author=Ch.J.%20Jaspers&author=J.M.%20Wiame&publication_year=1980&journal=Eur.%20J.%20Biochem.&volume=104&pages=119-123" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1111/ejb.1980.104.issue-1" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1111%2Fejb.1980.104.issue-1" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1111%2Fejb.1980.104.issue-1"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/6102906" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione%20metabolism%20in%20relation%20to%20the%20amino%20acid%20permeation%20systems%20in%20the%20yeast%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b31" class="js-splitview-ref-item" data-legacy-id="b31"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b31" href="javascript:;" aria-label="jumplink-b31" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b31" class="ref-content " data-id="b31"><span class="label title-label">[31]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Mehdi</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Thierie</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Penninckx</div> <div class="given-names">M.J.</div> </div> </span> (<div class="year">2001</div>) <div class="article-title">γ-Glutamyltranspeptidase in the yeast <em>Saccharomyces cerevisiae</em> and its role in the vacuolar transport and metabolism of glutathione</div>. <div class="source ">Biochem. J.</div><div class="volume">359</div>, <div class="fpage">631</div>–<div class="lpage">637</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=%CE%B3-Glutamyltranspeptidase%20in%20the%20yeast%20Saccharomyces%20cerevisiae%20and%20its%20role%20in%20the%20vacuolar%20transport%20and%20metabolism%20of%20glutathione&author=K.%20Mehdi&author=J.%20Thierie&author=M.J.%20Penninckx&publication_year=2001&journal=Biochem.%20J.&volume=359&pages=631-637" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1042/bj3590631" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1042%2Fbj3590631" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1042%2Fbj3590631"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11672438" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:%CE%B3-Glutamyltranspeptidase%20in%20the%20yeast%20Saccharomyces%20cerevisiae%20and%20its%20role%20in%20the%20vacuolar%20transport%20and%20metabolism%20of%20glutathione&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b32" class="js-splitview-ref-item" data-legacy-id="b32"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b32" href="javascript:;" aria-label="jumplink-b32" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b32" class="ref-content " data-id="b32"><span class="label title-label">[32]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Tate</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Meister</div> <div class="given-names">A.</div> </div> </span> (<div class="year">1981</div>) <div class="article-title">γ-Glutamyltranspeptidase: catalytical, structural and functional aspects</div>. <div class="source ">Mol. Cell. Biochem.</div><div class="volume">39</div>, <div class="fpage">357</div>–<div class="lpage">368</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=%CE%B3-Glutamyltranspeptidase%3A%20catalytical%2C%20structural%20and%20functional%20aspects&author=S.%20Tate&author=A.%20Meister&publication_year=1981&journal=Mol.%20Cell.%20Biochem.&volume=39&pages=357-368" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1007/BF00232585" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1007%2FBF00232585" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1007%2FBF00232585"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/6118826" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:%CE%B3-Glutamyltranspeptidase%3A%20catalytical%2C%20structural%20and%20functional%20aspects&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b33" class="js-splitview-ref-item" data-legacy-id="b33"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b33" href="javascript:;" aria-label="jumplink-b33" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b33" class="ref-content " data-id="b33"><span class="label title-label">[33]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Suzuki</div> <div class="given-names">H.</div> </div> <div class="name"> <div class="surname">Kumagai</div> <div class="given-names">H.</div> </div> <div class="name"> <div class="surname">Echigo</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Tochikura</div> <div class="given-names">T.</div> </div> </span> (<div class="year">1989</div>) <div class="article-title">DNA sequence of the <em>Escherichia coli</em> K-12 γ-glutamyltranspeptidase gene, <em>ggt</em></div>. <div class="source ">J. Bacteriol.</div><div class="volume">171</div>, <div class="fpage">5169</div>–<div class="lpage">5172</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=DNA%20sequence%20of%20the%20Escherichia%20coli%20K-12%20%CE%B3-glutamyltranspeptidase%20gene%2C%20ggt&author=H.%20Suzuki&author=H.%20Kumagai&author=T.%20Echigo&author=T.%20Tochikura&publication_year=1989&journal=J.%20Bacteriol.&volume=171&pages=5169-5172" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1128/jb.171.9.5169-5172.1989" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1128%2Fjb.171.9.5169-5172.1989" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1128%2Fjb.171.9.5169-5172.1989"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/2570061" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:DNA%20sequence%20of%20the%20Escherichia%20coli%20K-12%20%CE%B3-glutamyltranspeptidase%20gene%2C%20ggt&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b34" class="js-splitview-ref-item" data-legacy-id="b34"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b34" href="javascript:;" aria-label="jumplink-b34" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b34" class="ref-content " data-id="b34"><span class="label title-label">[34]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Klionsky</div> <div class="given-names">D.J.</div> </div> <div class="name"> <div class="surname">Emer</div> <div class="given-names">S.D.</div> </div> </span> (<div class="year">1989</div>) <div class="article-title">membrane protein sorting: biosynthesis, transport and processing of yeast vacuolar alkaline phosphatase</div>. <div class="source ">EMBO J.</div><div class="volume">8</div>, <div class="fpage">2241</div>–<div class="lpage">2250</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=membrane%20protein%20sorting%3A%20biosynthesis%2C%20transport%20and%20processing%20of%20yeast%20vacuolar%20alkaline%20phosphatase&author=D.J.%20Klionsky&author=S.D.%20Emer&publication_year=1989&journal=EMBO%20J.&volume=8&pages=2241-2250" target="_blank">Google Scholar</a></span></p><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/2676517" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=membrane+protein+sorting%3a+biosynthesis%2c+transport+and+processing+of+yeast+vacuolar+alkaline+phosphatase&aulast=Klionsky&title=EMBO+J.&date=1989&spage=2241&epage=2250&volume=8" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:membrane%20protein%20sorting%3A%20biosynthesis%2C%20transport%20and%20processing%20of%20yeast%20vacuolar%20alkaline%20phosphatase&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b35" class="js-splitview-ref-item" data-legacy-id="b35"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b35" href="javascript:;" aria-label="jumplink-b35" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b35" class="ref-content " data-id="b35"><span class="label title-label">[35]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Jaspers</div> <div class="given-names">Ch.</div> </div> <div class="name"> <div class="surname">Penninckx</div> <div class="given-names">M.J.</div> </div> </span> (<div class="year">1984</div>) <div class="article-title">Glutathione metabolism in yeast <em>Saccharomyces cerevisiae</em>. Evidence that γ-glutamyltranspeptidase is a vacuolar enzyme</div>. <div class="source ">Biochimie</div><div class="volume">66</div>, <div class="fpage">71</div>–<div class="lpage">74</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione%20metabolism%20in%20yeast%20Saccharomyces%20cerevisiae.%20Evidence%20that%20%CE%B3-glutamyltranspeptidase%20is%20a%20vacuolar%20enzyme&author=Ch.%20Jaspers&author=M.J.%20Penninckx&publication_year=1984&journal=Biochimie&volume=66&pages=71-74" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1016/0300-9084(84)90193-7" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1016%2F0300-9084(84)90193-7" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1016%2F0300-9084(84)90193-7"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/6143574" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione%20metabolism%20in%20yeast%20Saccharomyces%20cerevisiae.%20Evidence%20that%20%CE%B3-glutamyltranspeptidase%20is%20a%20vacuolar%20enzyme&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b36" class="js-splitview-ref-item" data-legacy-id="b36"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b36" href="javascript:;" aria-label="jumplink-b36" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b36" class="ref-content " data-id="b36"><span class="label title-label">[36]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Van Den Hazel</div> <div class="given-names">H.B.</div> </div> <div class="name"> <div class="surname">Kielland-Brandt</div> <div class="given-names">M.C.</div> </div> <div class="name"> <div class="surname">Winther</div> <div class="given-names">J.</div> </div> </span> (<div class="year">1996</div>) <div class="article-title">Biosynthesis and function of yeast vacuolar proteases</div>. <div class="source ">Yeast</div><div class="volume">12</div>, <div class="fpage">1</div>–<div class="lpage">16</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Biosynthesis%20and%20function%20of%20yeast%20vacuolar%20proteases&author=H.B.%20Van%20Den%20Hazel&author=M.C.%20Kielland-Brandt&author=J.%20Winther&publication_year=1996&journal=Yeast&volume=12&pages=1-16" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1002/(SICI)1097-0061(199601)12:1<1::AID-YEA902>3.0.CO;2-N" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1002%2F(SICI)1097-0061(199601)12:1<1::AID-YEA902>3.0.CO;2-N" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1002%2F(SICI)1097-0061(199601)12:1<1::AID-YEA902>3.0.CO;2-N"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/8789256" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Biosynthesis%20and%20function%20of%20yeast%20vacuolar%20proteases&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b37" class="js-splitview-ref-item" data-legacy-id="b37"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b37" href="javascript:;" aria-label="jumplink-b37" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b37" class="ref-content " data-id="b37"><span class="label title-label">[37]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Rankin</div> <div class="given-names">B.B.</div> </div> <div class="name"> <div class="surname">McIntyre</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Curthoys</div> <div class="given-names">T.</div> </div> </span> (<div class="year">1980</div>) <div class="article-title">Brush border membrane hydrolysis of S-benzyl-cysteine-p-nitroanilide, and activity of aminopeptidase M</div>. <div class="source ">Biochem. Biophys. Res. Commun.</div><div class="volume">96</div>, <div class="fpage">991</div>–<div class="lpage">996</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Brush%20border%20membrane%20hydrolysis%20of%20S-benzyl-cysteine-p-nitroanilide%2C%20and%20activity%20of%20aminopeptidase%20M&author=B.B.%20Rankin&author=T.%20McIntyre&author=T.%20Curthoys&publication_year=1980&journal=Biochem.%20Biophys.%20Res.%20Commun.&volume=96&pages=991-996" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1016/0006-291X(80)90050-9" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1016%2F0006-291X(80)90050-9" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1016%2F0006-291X(80)90050-9"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/6108111" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Brush%20border%20membrane%20hydrolysis%20of%20S-benzyl-cysteine-p-nitroanilide%2C%20and%20activity%20of%20aminopeptidase%20M&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b38" class="js-splitview-ref-item" data-legacy-id="b38"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b38" href="javascript:;" aria-label="jumplink-b38" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b38" class="ref-content " data-id="b38"><span class="label title-label">[38]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Mc Intyre</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Curthoys</div> <div class="given-names">N.P.</div> </div> </span> (<div class="year">1982</div>) <div class="article-title">Renal catabolism of glutathione</div>. <div class="source ">J. Biol. Chem.</div><div class="volume">257</div>, <div class="fpage">11915</div>–<div class="lpage">11921</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Renal%20catabolism%20of%20glutathione&author=T.%20Mc%20Intyre&author=N.P.%20Curthoys&publication_year=1982&journal=J.%20Biol.%20Chem.&volume=257&pages=11915-11921" target="_blank">Google Scholar</a></span></p><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/6126478" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=Renal+catabolism+of+glutathione&aulast=Mc+Intyre&title=J.+Biol.+Chem.&date=1982&spage=11915&epage=11921&volume=257" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Renal%20catabolism%20of%20glutathione&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b39" class="js-splitview-ref-item" data-legacy-id="b39"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b39" href="javascript:;" aria-label="jumplink-b39" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b39" class="ref-content " data-id="b39"><span class="label title-label">[39]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Payne</div> <div class="given-names">G.M.</div> </div> <div class="name"> <div class="surname">Payne</div> <div class="given-names">J.W.</div> </div> </span> (<div class="year">1984</div>) <div class="article-title">γ-Glutamyltranspeptidase is not involved in the bulk uptake of amino acids, peptides or γ-glutamyl amino acids in the yeast <em>Saccharomyces cerevisiae</em></div>. <div class="source ">Biochem. J.</div><div class="volume">218</div>, <div class="fpage">147</div>–<div class="lpage">151</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=%CE%B3-Glutamyltranspeptidase%20is%20not%20involved%20in%20the%20bulk%20uptake%20of%20amino%20acids%2C%20peptides%20or%20%CE%B3-glutamyl%20amino%20acids%20in%20the%20yeast%20Saccharomyces%20cerevisiae&author=G.M.%20Payne&author=J.W.%20Payne&publication_year=1984&journal=Biochem.%20J.&volume=218&pages=147-151" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1042/bj2180147" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1042%2Fbj2180147" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1042%2Fbj2180147"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/6143552" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:%CE%B3-Glutamyltranspeptidase%20is%20not%20involved%20in%20the%20bulk%20uptake%20of%20amino%20acids%2C%20peptides%20or%20%CE%B3-glutamyl%20amino%20acids%20in%20the%20yeast%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b40" class="js-splitview-ref-item" data-legacy-id="b40"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b40" href="javascript:;" aria-label="jumplink-b40" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b40" class="ref-content " data-id="b40"><span class="label title-label">[40]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Sherrill</div> <div class="given-names">C.</div> </div> <div class="name"> <div class="surname">Fahey</div> <div class="given-names">R.C.</div> </div> </span> (<div class="year">1998</div>) <div class="article-title">Import and metabolism of glutathione in <em>Streptococcus mutans</em></div>. <div class="source ">J. Bacteriol.</div><div class="volume">180</div>, <div class="fpage">1454</div>–<div class="lpage">1459</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Import%20and%20metabolism%20of%20glutathione%20in%20Streptococcus%20mutans&author=C.%20Sherrill&author=R.C.%20Fahey&publication_year=1998&journal=J.%20Bacteriol.&volume=180&pages=1454-1459" target="_blank">Google Scholar</a></span></p><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/9515913" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=Import+and+metabolism+of+glutathione+in+Streptococcus+mutans&aulast=Sherrill&title=J.+Bacteriol.&date=1998&spage=1454&epage=1459&volume=180" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Import%20and%20metabolism%20of%20glutathione%20in%20Streptococcus%20mutans&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b41" class="js-splitview-ref-item" data-legacy-id="b41"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b41" href="javascript:;" aria-label="jumplink-b41" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b41" class="ref-content " data-id="b41"><span class="label title-label">[41]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Iantomasi</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Favilli</div> <div class="given-names">F.</div> </div> <div class="name"> <div class="surname">Marriani</div> <div class="given-names">P.</div> </div> <div class="name"> <div class="surname">Magaldi</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Bruni</div> <div class="given-names">P.</div> </div> <div class="name"> <div class="surname">Vincenzini</div> <div class="given-names">M.T.</div> </div> </span> (<div class="year">1997</div>) <div class="article-title">Glutathione transport in human small intestine epithelial cells</div>. <div class="source ">Biochim. Biophys. Acta</div><div class="volume">1330</div>, <div class="fpage">274</div>–<div class="lpage">283</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione%20transport%20in%20human%20small%20intestine%20epithelial%20cells&author=T.%20Iantomasi&author=F.%20Favilli&author=P.%20Marriani&author=T.%20Magaldi&author=P.%20Bruni&author=M.T.%20Vincenzini&publication_year=1997&journal=Biochim.%20Biophys.%20Acta&volume=1330&pages=274-283" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1016/S0005-2736(97)00097-7" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1016%2FS0005-2736(97)00097-7" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1016%2FS0005-2736(97)00097-7"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/9408181" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione%20transport%20in%20human%20small%20intestine%20epithelial%20cells&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b42" class="js-splitview-ref-item" data-legacy-id="b42"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b42" href="javascript:;" aria-label="jumplink-b42" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b42" class="ref-content " data-id="b42"><span class="label title-label">[42]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Miyake</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Hazu</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Yoshida</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Kanayama</div> <div class="given-names">M.</div> </div> <div class="name"> <div class="surname">Tomochika</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Shinoda</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Ono</div> <div class="given-names">B.</div> </div> </span> (<div class="year">1998</div>) <div class="article-title">Glutathione transport systems of the budding yeast <em>Saccharomyces cerevisiae</em></div>. <div class="source ">Biosci. Biotechnol. Biochem.</div><div class="volume">62</div>, <div class="fpage">1858</div>–<div class="lpage">1864</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione%20transport%20systems%20of%20the%20budding%20yeast%20Saccharomyces%20cerevisiae&author=T.%20Miyake&author=T.%20Hazu&author=S.%20Yoshida&author=M.%20Kanayama&author=K.%20Tomochika&author=S.%20Shinoda&author=B.%20Ono&publication_year=1998&journal=Biosci.%20Biotechnol.%20Biochem.&volume=62&pages=1858-1864" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1271/bbb.62.1858" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1271%2Fbbb.62.1858" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1271%2Fbbb.62.1858"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/9836420" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione%20transport%20systems%20of%20the%20budding%20yeast%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b43" class="js-splitview-ref-item" data-legacy-id="b43"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b43" href="javascript:;" aria-label="jumplink-b43" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b43" class="ref-content " data-id="b43"><span class="label title-label">[43]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Bourbouloux</div> <div class="given-names">A.</div> </div> <div class="name"> <div class="surname">Shahi</div> <div class="given-names">P.</div> </div> <div class="name"> <div class="surname">Chakladar</div> <div class="given-names">A.</div> </div> <div class="name"> <div class="surname">Delrot</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Bachhawat</div> <div class="given-names">A.K.</div> </div> </span> (<div class="year">2000</div>) <div class="article-title">Hgt1p, a high affinity glutathione transporter from the yeast <em>Saccharomyces cerevisiae</em></div>. <div class="source ">J. Biol. Chem.</div><div class="volume">275</div>, <div class="fpage">13259</div>–<div class="lpage">13265</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Hgt1p%2C%20a%20high%20affinity%20glutathione%20transporter%20from%20the%20yeast%20Saccharomyces%20cerevisiae&author=A.%20Bourbouloux&author=P.%20Shahi&author=A.%20Chakladar&author=S.%20Delrot&author=A.K.%20Bachhawat&publication_year=2000&journal=J.%20Biol.%20Chem.&volume=275&pages=13259-13265" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.275.18.13259" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.275.18.13259" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.275.18.13259"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/10788431" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Hgt1p%2C%20a%20high%20affinity%20glutathione%20transporter%20from%20the%20yeast%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b44" class="js-splitview-ref-item" data-legacy-id="b44"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b44" href="javascript:;" aria-label="jumplink-b44" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b44" class="ref-content " data-id="b44"><span class="label title-label">[44]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Li</div> <div class="given-names">Z.S.</div> </div> <div class="name"> <div class="surname">Szczypka</div> <div class="given-names">M.</div> </div> <div class="name"> <div class="surname">Lu</div> <div class="given-names">Y.P.</div> </div> <div class="name"> <div class="surname">Thiele</div> <div class="given-names">D.J.</div> </div> <div class="name"> <div class="surname">Rea</div> <div class="given-names">P.A.</div> </div> </span> (<div class="year">1996</div>) <div class="article-title">The yeast cadmium factor protein (YCF1) is a vacuolar glutathione S-conjugates pump</div>. <div class="source ">J. Biol. Chem.</div><div class="volume">271</div>, <div class="fpage">6509</div>–<div class="lpage">6517</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=The%20yeast%20cadmium%20factor%20protein%20%28YCF1%29%20is%20a%20vacuolar%20glutathione%20S-conjugates%20pump&author=Z.S.%20Li&author=M.%20Szczypka&author=Y.P.%20Lu&author=D.J.%20Thiele&author=P.A.%20Rea&publication_year=1996&journal=J.%20Biol.%20Chem.&volume=271&pages=6509-6517" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.271.11.6509" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.271.11.6509" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.271.11.6509"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/8626454" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:The%20yeast%20cadmium%20factor%20protein%20%28YCF1%29%20is%20a%20vacuolar%20glutathione%20S-conjugates%20pump&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b45" class="js-splitview-ref-item" data-legacy-id="b45"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b45" href="javascript:;" aria-label="jumplink-b45" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b45" class="ref-content " data-id="b45"><span class="label title-label">[45]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Rebbeor</div> <div class="given-names">J.F.</div> </div> <div class="name"> <div class="surname">Connolly</div> <div class="given-names">G.C.</div> </div> <div class="name"> <div class="surname">Dumont</div> <div class="given-names">M.E.</div> </div> <div class="name"> <div class="surname">Ballatori</div> <div class="given-names">N.</div> </div> </span> (<div class="year">1998</div>) <div class="article-title">ATP-dependent transport of reduced glutathione on YCF1, the yeast orthologue of mammalian multidrug resistance associated proteins</div>. <div class="source ">J. Biol. Chem.</div><div class="volume">273</div>, <div class="fpage">33449</div>–<div class="lpage">33454</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=ATP-dependent%20transport%20of%20reduced%20glutathione%20on%20YCF1%2C%20the%20yeast%20orthologue%20of%20mammalian%20multidrug%20resistance%20associated%20proteins&author=J.F.%20Rebbeor&author=G.C.%20Connolly&author=M.E.%20Dumont&author=N.%20Ballatori&publication_year=1998&journal=J.%20Biol.%20Chem.&volume=273&pages=33449-33454" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.273.50.33449" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.273.50.33449" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.273.50.33449"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/9837923" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:ATP-dependent%20transport%20of%20reduced%20glutathione%20on%20YCF1%2C%20the%20yeast%20orthologue%20of%20mammalian%20multidrug%20resistance%20associated%20proteins&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b46" class="js-splitview-ref-item" data-legacy-id="b46"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b46" href="javascript:;" aria-label="jumplink-b46" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b46" class="ref-content " data-id="b46"><span class="label title-label">[46]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Elskens</div> <div class="given-names">M.T.</div> </div> <div class="name"> <div class="surname">Jaspers</div> <div class="given-names">C.J.</div> </div> <div class="name"> <div class="surname">Penninckx</div> <div class="given-names">M.J.</div> </div> </span> (<div class="year">1991</div>) <div class="article-title">Glutathione as an endogenous sulfur source in the yeast <em>Saccharomyces cerevisiae</em></div>. <div class="source ">J. Gen. Microbiol.</div><div class="volume">137</div>, <div class="fpage">637</div>–<div class="lpage">644</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione%20as%20an%20endogenous%20sulfur%20source%20in%20the%20yeast%20Saccharomyces%20cerevisiae&author=M.T.%20Elskens&author=C.J.%20Jaspers&author=M.J.%20Penninckx&publication_year=1991&journal=J.%20Gen.%20Microbiol.&volume=137&pages=637-644" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1099/00221287-137-3-637" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1099%2F00221287-137-3-637" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1099%2F00221287-137-3-637"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/1674526" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione%20as%20an%20endogenous%20sulfur%20source%20in%20the%20yeast%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b47" class="js-splitview-ref-item" data-legacy-id="b47"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b47" href="javascript:;" aria-label="jumplink-b47" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b47" class="ref-content " data-id="b47"><span class="label title-label">[47]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Miyake</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Sammoto</div> <div class="given-names">H.</div> </div> <div class="name"> <div class="surname">Kanayama</div> <div class="given-names">M.</div> </div> <div class="name"> <div class="surname">Tomochika</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Shinoda</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Ono</div> <div class="given-names">B.</div> </div> </span> (<div class="year">1999</div>) <div class="article-title">Role of the sulphate assimilation pathway in utilization of glutathione as a sulphur source by <em>Saccharomyces cerevisiae</em></div>. <div class="source ">Yeast</div><div class="volume">15</div>, <div class="fpage">1449</div>–<div class="lpage">1457</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Role%20of%20the%20sulphate%20assimilation%20pathway%20in%20utilization%20of%20glutathione%20as%20a%20sulphur%20source%20by%20Saccharomyces%20cerevisiae&author=T.%20Miyake&author=H.%20Sammoto&author=M.%20Kanayama&author=K.%20Tomochika&author=S.%20Shinoda&author=B.%20Ono&publication_year=1999&journal=Yeast&volume=15&pages=1449-1457" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1002/(ISSN)1097-0061" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1002%2F(ISSN)1097-0061" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1002%2F(ISSN)1097-0061"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/10514563" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Role%20of%20the%20sulphate%20assimilation%20pathway%20in%20utilization%20of%20glutathione%20as%20a%20sulphur%20source%20by%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b48" class="js-splitview-ref-item" data-legacy-id="b48"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b48" href="javascript:;" aria-label="jumplink-b48" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b48" class="ref-content " data-id="b48"><span class="label title-label">[48]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Sato</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Suzuki</div> <div class="given-names">H.</div> </div> <div class="name"> <div class="surname">Widyastuti</div> <div class="given-names">U.</div> </div> <div class="name"> <div class="surname">Hotta</div> <div class="given-names">Y.</div> </div> <div class="name"> <div class="surname">Tabata</div> <div class="given-names">S.</div> </div> </span> (<div class="year">1994</div>) <div class="article-title">Identification and characterization of genes induced during sexual differentiation in <em>Schizosaccharomyces pombe</em></div>. <div class="source ">Curr. Genet.</div><div class="volume">26</div>, <div class="fpage">31</div>–<div class="lpage">37</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Identification%20and%20characterization%20of%20genes%20induced%20during%20sexual%20differentiation%20in%20Schizosaccharomyces%20pombe&author=S.%20Sato&author=H.%20Suzuki&author=U.%20Widyastuti&author=Y.%20Hotta&author=S.%20Tabata&publication_year=1994&journal=Curr.%20Genet.&volume=26&pages=31-37" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1007/BF00326301" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1007%2FBF00326301" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1007%2FBF00326301"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/7954893" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Identification%20and%20characterization%20of%20genes%20induced%20during%20sexual%20differentiation%20in%20Schizosaccharomyces%20pombe&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b49" class="js-splitview-ref-item" data-legacy-id="b49"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b49" href="javascript:;" aria-label="jumplink-b49" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b49" class="ref-content " data-id="b49"><span class="label title-label">[49]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Piper</div> <div class="given-names">R.C.</div> </div> <div class="name"> <div class="surname">Bryant</div> <div class="given-names">N.J.</div> </div> <div class="name"> <div class="surname">Stevens</div> <div class="given-names">T.C.</div> </div> </span> (<div class="year">1997</div>) <div class="article-title">The membrane protein alkaline phosphatase is delivered to the vacuole by a route that is distinct from the VPS-dependent pathway</div>. <div class="source ">J. Cell. Biol.</div><div class="volume">138</div>, <div class="fpage">531</div>–<div class="lpage">545</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=The%20membrane%20protein%20alkaline%20phosphatase%20is%20delivered%20to%20the%20vacuole%20by%20a%20route%20that%20is%20distinct%20from%20the%20VPS-dependent%20pathway&author=R.C.%20Piper&author=N.J.%20Bryant&author=T.C.%20Stevens&publication_year=1997&journal=J.%20Cell.%20Biol.&volume=138&pages=531-545" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1083/jcb.138.3.531" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1083%2Fjcb.138.3.531" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1083%2Fjcb.138.3.531"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/9245784" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:The%20membrane%20protein%20alkaline%20phosphatase%20is%20delivered%20to%20the%20vacuole%20by%20a%20route%20that%20is%20distinct%20from%20the%20VPS-dependent%20pathway&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b50" class="js-splitview-ref-item" data-legacy-id="b50"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b50" href="javascript:;" aria-label="jumplink-b50" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b50" class="ref-content " data-id="b50"><span class="label title-label">[50]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Ito</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Chiba</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Ozawa</div> <div class="given-names">R.</div> </div> <div class="name"> <div class="surname">Yoshida</div> <div class="given-names">M.</div> </div> <div class="name"> <div class="surname">Hattori</div> <div class="given-names">M.</div> </div> <div class="name"> <div class="surname">Sakaki</div> <div class="given-names">Y.</div> </div> </span> (<div class="year">2001</div>) <div class="article-title">A comprehensive two-hybrid analysis to explore the yeast protein interactome</div>. <div class="source ">Proc. Natl. Acad. Sci. USA</div><div class="volume">98</div>, <div class="fpage">4569</div>–<div class="lpage">4574</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=A%20comprehensive%20two-hybrid%20analysis%20to%20explore%20the%20yeast%20protein%20interactome&author=T.%20Ito&author=T.%20Chiba&author=R.%20Ozawa&author=M.%20Yoshida&author=M.%20Hattori&author=Y.%20Sakaki&publication_year=2001&journal=Proc.%20Natl.%20Acad.%20Sci.%20USA&volume=98&pages=4569-4574" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1073/pnas.061034498" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1073%2Fpnas.061034498" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1073%2Fpnas.061034498"> </span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:A%20comprehensive%20two-hybrid%20analysis%20to%20explore%20the%20yeast%20protein%20interactome&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b51" class="js-splitview-ref-item" data-legacy-id="b51"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b51" href="javascript:;" aria-label="jumplink-b51" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b51" class="ref-content " data-id="b51"><span class="label title-label">[51]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Ubiivovk</div> <div class="given-names">V.M.</div> </div> <div class="name"> <div class="surname">Telegus</div> <div class="given-names">Y.V.</div> </div> <div class="name"> <div class="surname">Sibirniy</div> <div class="given-names">A.</div> </div> </span> (<div class="year">1999</div>) <div class="article-title">Isolation and characterization of glutathione-deficient mutants of the methylotrophic yeast <em>Hansenula polymorpha</em></div>. <div class="source ">Microbiologiya (Moscow)</div><div class="volume">68</div>, <div class="fpage">26</div>–<div class="lpage">31</div>. </p><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Isolation%20and%20characterization%20of%20glutathione-deficient%20mutants%20of%20the%20methylotrophic%20yeast%20Hansenula%20polymorpha&author=V.M.%20Ubiivovk&author=Y.V.%20Telegus&author=A.%20Sibirniy&publication_year=1999&journal=Microbiologiya%20%28Moscow%29&volume=68&pages=26-31" target="_blank">Google Scholar</a></span></p><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=Isolation+and+characterization+of+glutathione-deficient+mutants+of+the+methylotrophic+yeast+Hansenula+polymorpha&aulast=Ubiivovk&title=Microbiologiya+(Moscow)&date=1999&spage=26&epage=31&volume=68" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Isolation%20and%20characterization%20of%20glutathione-deficient%20mutants%20of%20the%20methylotrophic%20yeast%20Hansenula%20polymorpha&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b52" class="js-splitview-ref-item" data-legacy-id="b52"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b52" href="javascript:;" aria-label="jumplink-b52" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b52" class="ref-content " data-id="b52"><span class="label title-label">[52]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Sibirniy</div> <div class="given-names">A.</div> </div> <div class="name"> <div class="surname">Ubiivovk</div> <div class="given-names">V.M.</div> </div> <div class="name"> <div class="surname">Gonchar</div> <div class="given-names">M.V.</div> </div> <div class="name"> <div class="surname">Titorenko</div> <div class="given-names">V.I.</div> </div> <div class="name"> <div class="surname">Voronovsky</div> <div class="given-names">A.Y.</div> </div> <div class="name"> <div class="surname">Kapultsevich</div> <div class="given-names">Y.G.</div> </div> <div class="name"> <div class="surname">Bliznik</div> <div class="given-names">K.M.</div> </div> </span> (<div class="year">1990</div>) <div class="article-title">Reactions of direct formaldehyde oxidation to CO<sub>2</sub> are non-essential for energy supply of yeast methylotrophic growth</div>. <div class="source ">Arch. Microbiol.</div><div class="volume">154</div>, <div class="fpage">566</div>–<div class="lpage">575</div>. </p><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Reactions%20of%20direct%20formaldehyde%20oxidation%20to%20CO2%20are%20non-essential%20for%20energy%20supply%20of%20yeast%20methylotrophic%20growth&author=A.%20Sibirniy&author=V.M.%20Ubiivovk&author=M.V.%20Gonchar&author=V.I.%20Titorenko&author=A.Y.%20Voronovsky&author=Y.G.%20Kapultsevich&author=K.M.%20Bliznik&publication_year=1990&journal=Arch.%20Microbiol.&volume=154&pages=566-575" target="_blank">Google Scholar</a></span></p><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=Reactions+of+direct+formaldehyde+oxidation+to+CO2+are+non-essential+for+energy+supply+of+yeast+methylotrophic+growth&aulast=Sibirniy&title=Arch.+Microbiol.&date=1990&spage=566&epage=575&volume=154" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Reactions%20of%20direct%20formaldehyde%20oxidation%20to%20CO2%20are%20non-essential%20for%20energy%20supply%20of%20yeast%20methylotrophic%20growth&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b53" class="js-splitview-ref-item" data-legacy-id="b53"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b53" href="javascript:;" aria-label="jumplink-b53" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b53" class="ref-content " data-id="b53"><span class="label title-label">[53]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Galiazzo</div> <div class="given-names">F.</div> </div> <div class="name"> <div class="surname">Schiesser</div> <div class="given-names">A.</div> </div> <div class="name"> <div class="surname">Rotilio</div> <div class="given-names">G.</div> </div> </span> (<div class="year">1987</div>) <div class="article-title">Glutathione peroxidase in yeast. Presence of the enzyme and induction by oxidative conditions</div>. <div class="source ">Biochem. Biophys. Res. Commun.</div><div class="volume">147</div>, <div class="fpage">1200</div>–<div class="lpage">1205</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione%20peroxidase%20in%20yeast.%20Presence%20of%20the%20enzyme%20and%20induction%20by%20oxidative%20conditions&author=F.%20Galiazzo&author=A.%20Schiesser&author=G.%20Rotilio&publication_year=1987&journal=Biochem.%20Biophys.%20Res.%20Commun.&volume=147&pages=1200-1205" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1016/S0006-291X(87)80197-3" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1016%2FS0006-291X(87)80197-3" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1016%2FS0006-291X(87)80197-3"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/3311044" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione%20peroxidase%20in%20yeast.%20Presence%20of%20the%20enzyme%20and%20induction%20by%20oxidative%20conditions&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b54" class="js-splitview-ref-item" data-legacy-id="b54"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b54" href="javascript:;" aria-label="jumplink-b54" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b54" class="ref-content " data-id="b54"><span class="label title-label">[54]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Inoue</div> <div class="given-names">Y.</div> </div> <div class="name"> <div class="surname">Kimura</div> <div class="given-names">A.</div> </div> </span> (<div class="year">1998</div>) <div class="article-title">Oxidative stress response in <em>Hansenula mrakii</em>: a new type of glutathione peroxidase in yeast</div>. <div class="source ">Recent Res. Dev. Agric. Biol. Chem.</div><div class="volume">2</div>, <div class="fpage">29</div>–<div class="lpage">39</div>. </p><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Oxidative%20stress%20response%20in%20Hansenula%20mrakii%3A%20a%20new%20type%20of%20glutathione%20peroxidase%20in%20yeast&author=Y.%20Inoue&author=A.%20Kimura&publication_year=1998&journal=Recent%20Res.%20Dev.%20Agric.%20Biol.%20Chem.&volume=2&pages=29-39" target="_blank">Google Scholar</a></span></p><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=Oxidative+stress+response+in+Hansenula+mrakii%3a+a+new+type+of+glutathione+peroxidase+in+yeast&aulast=Inoue&title=Recent+Res.+Dev.+Agric.+Biol.+Chem.&date=1998&spage=29&epage=39&volume=2" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Oxidative%20stress%20response%20in%20Hansenula%20mrakii%3A%20a%20new%20type%20of%20glutathione%20peroxidase%20in%20yeast&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b55" class="js-splitview-ref-item" data-legacy-id="b55"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b55" href="javascript:;" aria-label="jumplink-b55" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b55" class="ref-content " data-id="b55"><span class="label title-label">[55]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Horiguchi</div> <div class="given-names">H.</div> </div> <div class="name"> <div class="surname">Yurimoto</div> <div class="given-names">H.</div> </div> <div class="name"> <div class="surname">Kato</div> <div class="given-names">N.</div> </div> <div class="name"> <div class="surname">Sakai</div> <div class="given-names">Y.</div> </div> </span> (<div class="year">2001</div>) <div class="article-title">Antioxidant system within yeast peroxisome. Biochemical and physiological characterization of CbPmp20 in the methylotrophic yeast <em>Candida boidinii</em></div>. <div class="source ">J. Biol. Chem.</div><div class="volume">276</div>, <div class="fpage">14279</div>–<div class="lpage">14288</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Antioxidant%20system%20within%20yeast%20peroxisome.%20Biochemical%20and%20physiological%20characterization%20of%20CbPmp20%20in%20the%20methylotrophic%20yeast%20Candida%20boidinii&author=H.%20Horiguchi&author=H.%20Yurimoto&author=N.%20Kato&author=Y.%20Sakai&publication_year=2001&journal=J.%20Biol.%20Chem.&volume=276&pages=14279-14288" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.M011661200" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.M011661200" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.M011661200"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11278957" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Antioxidant%20system%20within%20yeast%20peroxisome.%20Biochemical%20and%20physiological%20characterization%20of%20CbPmp20%20in%20the%20methylotrophic%20yeast%20Candida%20boidinii&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b56" class="js-splitview-ref-item" data-legacy-id="b56"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b56" href="javascript:;" aria-label="jumplink-b56" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b56" class="ref-content " data-id="b56"><span class="label title-label">[56]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Inoue</div> <div class="given-names">Y.</div> </div> <div class="name"> <div class="surname">Matsuda</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Sugiyama</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Izawa</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Kimura</div> <div class="given-names">A.</div> </div> </span> (<div class="year">1999</div>) <div class="article-title">Genetic analysis of glutathione peroxidase in oxidative stress response of <em>Saccharomyces cerevisiae</em></div>. <div class="source ">J. Biol. Chem.</div><div class="volume">274</div>, <div class="fpage">27002</div>–<div class="lpage">27009</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Genetic%20analysis%20of%20glutathione%20peroxidase%20in%20oxidative%20stress%20response%20of%20Saccharomyces%20cerevisiae&author=Y.%20Inoue&author=T.%20Matsuda&author=K.%20Sugiyama&author=S.%20Izawa&author=A.%20Kimura&publication_year=1999&journal=J.%20Biol.%20Chem.&volume=274&pages=27002-27009" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.274.38.27002" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.274.38.27002" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.274.38.27002"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/10480913" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Genetic%20analysis%20of%20glutathione%20peroxidase%20in%20oxidative%20stress%20response%20of%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b57" class="js-splitview-ref-item" data-legacy-id="b57"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b57" href="javascript:;" aria-label="jumplink-b57" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b57" class="ref-content " data-id="b57"><span class="label title-label">[57]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Avery</div> <div class="given-names">A.M.</div> </div> <div class="name"> <div class="surname">Avery</div> <div class="given-names">S.V.</div> </div> </span> (<div class="year">2001</div>) <div class="article-title"><em>Saccharomyces cerevisiae</em> expresses three phospholipid hydroperoxide glutathione peroxidases</div>. <div class="source ">J. Biol. Chem.</div><div class="volume">276</div>, <div class="fpage">33730</div>–<div class="lpage">33735</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Saccharomyces%20cerevisiae%20expresses%20three%20phospholipid%20hydroperoxide%20glutathione%20peroxidases&author=A.M.%20Avery&author=S.V.%20Avery&publication_year=2001&journal=J.%20Biol.%20Chem.&volume=276&pages=33730-33735" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.M105672200" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.M105672200" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.M105672200"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11445588" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Saccharomyces%20cerevisiae%20expresses%20three%20phospholipid%20hydroperoxide%20glutathione%20peroxidases&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b58" class="js-splitview-ref-item" data-legacy-id="b58"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b58" href="javascript:;" aria-label="jumplink-b58" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b58" class="ref-content " data-id="b58"><span class="label title-label">[58]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Holmgren</div> <div class="given-names">A.</div> </div> </span> (<div class="year">1985</div>) <div class="article-title">Thioredoxin</div>. <div class="source ">Annu. Rev. Biochem.</div><div class="volume">54</div>, <div class="fpage">237</div>–<div class="lpage">271</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Thioredoxin&author=A.%20Holmgren&publication_year=1985&journal=Annu.%20Rev.%20Biochem.&volume=54&pages=237-271" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1146/annurev.bi.54.070185.001321" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1146%2Fannurev.bi.54.070185.001321" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1146%2Fannurev.bi.54.070185.001321"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/3896121" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Thioredoxin&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b59" class="js-splitview-ref-item" data-legacy-id="b59"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b59" href="javascript:;" aria-label="jumplink-b59" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b59" class="ref-content " data-id="b59"><span class="label title-label">[59]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Sugiyama</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Izawa</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Inoue</div> <div class="given-names">Y.</div> </div> </span> (<div class="year">2000</div>) <div class="article-title">The Yap1p-dependent induction of glutathione synthesis in heat shock response of <em>Saccharomyces cerevisiae</em></div>. <div class="source ">J. Biol. Chem.</div><div class="volume">275</div>, <div class="fpage">15535</div>–<div class="lpage">15540</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=The%20Yap1p-dependent%20induction%20of%20glutathione%20synthesis%20in%20heat%20shock%20response%20of%20Saccharomyces%20cerevisiae&author=K.%20Sugiyama&author=S.%20Izawa&author=Y.%20Inoue&publication_year=2000&journal=J.%20Biol.%20Chem.&volume=275&pages=15535-15540" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.275.20.15535" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.275.20.15535" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.275.20.15535"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/10809786" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:The%20Yap1p-dependent%20induction%20of%20glutathione%20synthesis%20in%20heat%20shock%20response%20of%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b60" class="js-splitview-ref-item" data-legacy-id="b60"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b60" href="javascript:;" aria-label="jumplink-b60" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b60" class="ref-content " data-id="b60"><span class="label title-label">[60]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Lee</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Dawes</div> <div class="given-names">I.W.</div> </div> <div class="name"> <div class="surname">Roe</div> <div class="given-names">J.H.</div> </div> </span> (<div class="year">1995</div>) <div class="article-title">Adaptative response of <em>Schizosaccharomyces pombe</em> to hydrogen peroxide and menadione</div>. <div class="source ">Microbiology</div><div class="volume">141</div>, <div class="fpage">3127</div>–<div class="lpage">3132</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Adaptative%20response%20of%20Schizosaccharomyces%20pombe%20to%20hydrogen%20peroxide%20and%20menadione&author=J.%20Lee&author=I.W.%20Dawes&author=J.H.%20Roe&publication_year=1995&journal=Microbiology&volume=141&pages=3127-3132" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1099/13500872-141-12-3127" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1099%2F13500872-141-12-3127" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1099%2F13500872-141-12-3127"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/8574406" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Adaptative%20response%20of%20Schizosaccharomyces%20pombe%20to%20hydrogen%20peroxide%20and%20menadione&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b61" class="js-splitview-ref-item" data-legacy-id="b61"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b61" href="javascript:;" aria-label="jumplink-b61" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b61" class="ref-content " data-id="b61"><span class="label title-label">[61]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Yamada</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Nakagawa</div> <div class="given-names">C.W.</div> </div> <div class="name"> <div class="surname">Mutoh</div> <div class="given-names">N.</div> </div> </span> (<div class="year">1999</div>) <div class="article-title"><em>Schizosaccharomyces pombe</em> homologue of glutathione peroxidase, which does not contain selenocysteine, is induced by several stresses and works as an antioxidant</div>. <div class="source ">Yeast</div><div class="volume">15</div>, <div class="fpage">1125</div>–<div class="lpage">1132</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Schizosaccharomyces%20pombe%20homologue%20of%20glutathione%20peroxidase%2C%20which%20does%20not%20contain%20selenocysteine%2C%20is%20induced%20by%20several%20stresses%20and%20works%20as%20an%20antioxidant&author=K.%20Yamada&author=C.W.%20Nakagawa&author=N.%20Mutoh&publication_year=1999&journal=Yeast&volume=15&pages=1125-1132" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1002/(ISSN)1097-0061" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1002%2F(ISSN)1097-0061" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1002%2F(ISSN)1097-0061"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/10455235" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Schizosaccharomyces%20pombe%20homologue%20of%20glutathione%20peroxidase%2C%20which%20does%20not%20contain%20selenocysteine%2C%20is%20induced%20by%20several%20stresses%20and%20works%20as%20an%20antioxidant&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b62" class="js-splitview-ref-item" data-legacy-id="b62"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b62" href="javascript:;" aria-label="jumplink-b62" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b62" class="ref-content " data-id="b62"><span class="label title-label">[62]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Elskens</div> <div class="given-names">M.</div> </div> <div class="name"> <div class="surname">Penninckx</div> <div class="given-names">M.J.</div> </div> <div class="name"> <div class="surname">Vandeloise</div> <div class="given-names">R.</div> </div> <div class="name"> <div class="surname">Vander Donckt</div> <div class="given-names">E.</div> </div> </span> (<div class="year">1988</div>) <div class="article-title">Use of a simplex technique and contour diagrams for the determination of the reaction rate constant between glutathione and thiram in the presence of NADPH</div>. <div class="source ">Int. J. Chem. Kinet.</div><div class="volume">20</div>, <div class="fpage">837</div>–<div class="lpage">848</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Use%20of%20a%20simplex%20technique%20and%20contour%20diagrams%20for%20the%20determination%20of%20the%20reaction%20rate%20constant%20between%20glutathione%20and%20thiram%20in%20the%20presence%20of%20NADPH&author=M.%20Elskens&author=M.J.%20Penninckx&author=R.%20Vandeloise&author=E.%20Vander%20Donckt&publication_year=1988&journal=Int.%20J.%20Chem.%20Kinet.&volume=20&pages=837-848" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1002/(ISSN)1097-4601" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1002%2F(ISSN)1097-4601" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1002%2F(ISSN)1097-4601"> </span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Use%20of%20a%20simplex%20technique%20and%20contour%20diagrams%20for%20the%20determination%20of%20the%20reaction%20rate%20constant%20between%20glutathione%20and%20thiram%20in%20the%20presence%20of%20NADPH&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b63" class="js-splitview-ref-item" data-legacy-id="b63"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b63" href="javascript:;" aria-label="jumplink-b63" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b63" class="ref-content " data-id="b63"><span class="label title-label">[63]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Elskens</div> <div class="given-names">M.</div> </div> <div class="name"> <div class="surname">Penninckx</div> <div class="given-names">M.J.</div> </div> </span> (<div class="year">1997</div>) <div class="article-title">Interconversion of thiram and dimethyldithiocarbamic acid in <em>Saccharomyces cerevisiae</em>: a plausible metabolic pathway under the control of the glutathione redox cycle</div>. <div class="source ">Appl. Environ. Microbiol.</div><div class="volume">63</div>, <div class="fpage">2857</div>–<div class="lpage">2862</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Interconversion%20of%20thiram%20and%20dimethyldithiocarbamic%20acid%20in%20Saccharomyces%20cerevisiae%3A%20a%20plausible%20metabolic%20pathway%20under%20the%20control%20of%20the%20glutathione%20redox%20cycle&author=M.%20Elskens&author=M.J.%20Penninckx&publication_year=1997&journal=Appl.%20Environ.%20Microbiol.&volume=63&pages=2857-2862" target="_blank">Google Scholar</a></span></p><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/9212433" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=Interconversion+of+thiram+and+dimethyldithiocarbamic+acid+in+Saccharomyces+cerevisiae%3a+a+plausible+metabolic+pathway+under+the+control+of+the+glutathione+redox+cycle&aulast=Elskens&title=Appl.+Environ.+Microbiol.&date=1997&spage=2857&epage=2862&volume=63" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Interconversion%20of%20thiram%20and%20dimethyldithiocarbamic%20acid%20in%20Saccharomyces%20cerevisiae%3A%20a%20plausible%20metabolic%20pathway%20under%20the%20control%20of%20the%20glutathione%20redox%20cycle&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b64" class="js-splitview-ref-item" data-legacy-id="b64"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b64" href="javascript:;" aria-label="jumplink-b64" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b64" class="ref-content " data-id="b64"><span class="label title-label">[64]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Zadzinski</div> <div class="given-names">R.</div> </div> <div class="name"> <div class="surname">Maszewski</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Bartosz</div> <div class="given-names">G.</div> </div> </span> (<div class="year">1996</div>) <div class="article-title">Transport of glutathione-S-conjugates in the yeast <em>Saccharomyces cerevisiae</em></div>. <div class="source ">Cell Biol. Int.</div><div class="volume">20</div>, <div class="fpage">325</div>–<div class="lpage">330</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Transport%20of%20glutathione-S-conjugates%20in%20the%20yeast%20Saccharomyces%20cerevisiae&author=R.%20Zadzinski&author=J.%20Maszewski&author=G.%20Bartosz&publication_year=1996&journal=Cell%20Biol.%20Int.&volume=20&pages=325-330" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1006/cbir.1996.0035" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1006%2Fcbir.1996.0035" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1006%2Fcbir.1996.0035"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/8688846" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Transport%20of%20glutathione-S-conjugates%20in%20the%20yeast%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b65" class="js-splitview-ref-item" data-legacy-id="b65"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b65" href="javascript:;" aria-label="jumplink-b65" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b65" class="ref-content " data-id="b65"><span class="label title-label">[65]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Jelinsky</div> <div class="given-names">S.A.</div> </div> <div class="name"> <div class="surname">Samson</div> <div class="given-names">L.D.</div> </div> </span> (<div class="year">1999</div>) <div class="article-title">Global response of <em>Saccharomyces cerevisiae</em> to an alkylating agent</div>. <div class="source ">Proc. Natl. Acad. Sci. USA</div><div class="volume">96</div>, <div class="fpage">1486</div>–<div class="lpage">1491</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Global%20response%20of%20Saccharomyces%20cerevisiae%20to%20an%20alkylating%20agent&author=S.A.%20Jelinsky&author=L.D.%20Samson&publication_year=1999&journal=Proc.%20Natl.%20Acad.%20Sci.%20USA&volume=96&pages=1486-1491" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1073/pnas.96.4.1486" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1073%2Fpnas.96.4.1486" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1073%2Fpnas.96.4.1486"> </span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Global%20response%20of%20Saccharomyces%20cerevisiae%20to%20an%20alkylating%20agent&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b66" class="js-splitview-ref-item" data-legacy-id="b66"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b66" href="javascript:;" aria-label="jumplink-b66" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b66" class="ref-content " data-id="b66"><span class="label title-label">[66]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Ghosh</div> <div class="given-names">M.</div> </div> <div class="name"> <div class="surname">Shen</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Rosen</div> <div class="given-names">B.P.</div> </div> </span> (<div class="year">1999</div>) <div class="article-title">Pathways of As(III) detoxification in <em>Saccharomyces cerevisiae</em></div>. <div class="source ">Proc. Natl. Acad. Sci. USA</div><div class="volume">96</div>, <div class="fpage">5001</div>–<div class="lpage">5006</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Pathways%20of%20As%28III%29%20detoxification%20in%20Saccharomyces%20cerevisiae&author=M.%20Ghosh&author=J.%20Shen&author=B.P.%20Rosen&publication_year=1999&journal=Proc.%20Natl.%20Acad.%20Sci.%20USA&volume=96&pages=5001-5006" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1073/pnas.96.9.5001" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1073%2Fpnas.96.9.5001" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1073%2Fpnas.96.9.5001"> </span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Pathways%20of%20As%28III%29%20detoxification%20in%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b67" class="js-splitview-ref-item" data-legacy-id="b67"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b67" href="javascript:;" aria-label="jumplink-b67" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b67" class="ref-content " data-id="b67"><span class="label title-label">[67]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Rauser</div> <div class="given-names">W.E.</div> </div> </span> (<div class="year">1990</div>) <div class="article-title">Phytochelatins</div>. <div class="source ">Annu. Rev. Biochem.</div><div class="volume">59</div>, <div class="fpage">61</div>–<div class="lpage">86</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Phytochelatins&author=W.E.%20Rauser&publication_year=1990&journal=Annu.%20Rev.%20Biochem.&volume=59&pages=61-86" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1146/annurev.bi.59.070190.000425" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1146%2Fannurev.bi.59.070190.000425" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1146%2Fannurev.bi.59.070190.000425"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/2197985" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Phytochelatins&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b68" class="js-splitview-ref-item" data-legacy-id="b68"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b68" href="javascript:;" aria-label="jumplink-b68" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b68" class="ref-content " data-id="b68"><span class="label title-label">[68]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Rauser</div> <div class="given-names">W.E.</div> </div> </span> (<div class="year">1995</div>) <div class="article-title">Phytochelatins and related peptides. Structure, biosynthesis and function</div>. <div class="source ">Plant Physiol.</div><div class="volume">109</div>, <div class="fpage">1141</div>–<div class="lpage">1149</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Phytochelatins%20and%20related%20peptides.%20Structure%2C%20biosynthesis%20and%20function&author=W.E.%20Rauser&publication_year=1995&journal=Plant%20Physiol.&volume=109&pages=1141-1149" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1104/pp.109.4.1141" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1104%2Fpp.109.4.1141" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1104%2Fpp.109.4.1141"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/8539285" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Phytochelatins%20and%20related%20peptides.%20Structure%2C%20biosynthesis%20and%20function&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b69" class="js-splitview-ref-item" data-legacy-id="b69"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b69" href="javascript:;" aria-label="jumplink-b69" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b69" class="ref-content " data-id="b69"><span class="label title-label">[69]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Ortiz</div> <div class="given-names">D.E.</div> </div> <div class="name"> <div class="surname">Kreppel</div> <div class="given-names">L.</div> </div> <div class="name"> <div class="surname">Speiser</div> <div class="given-names">D.M.</div> </div> <div class="name"> <div class="surname">Scheel</div> <div class="given-names">G.</div> </div> <div class="name"> <div class="surname">McDonald</div> <div class="given-names">G.</div> </div> <div class="name"> <div class="surname">Ow</div> <div class="given-names">D.M.</div> </div> </span> (<div class="year">1992</div>) <div class="article-title">Heavy metal tolerance in the fission yeast requires an ATP-binding cassette-type vacuolar membrane transporter</div>. <div class="source ">EMBO J.</div><div class="volume">11</div>, <div class="fpage">3491</div>–<div class="lpage">3499</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Heavy%20metal%20tolerance%20in%20the%20fission%20yeast%20requires%20an%20ATP-binding%20cassette-type%20vacuolar%20membrane%20transporter&author=D.E.%20Ortiz&author=L.%20Kreppel&author=D.M.%20Speiser&author=G.%20Scheel&author=G.%20McDonald&author=D.M.%20Ow&publication_year=1992&journal=EMBO%20J.&volume=11&pages=3491-3499" target="_blank">Google Scholar</a></span></p><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/1396551" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=article&atitle=Heavy+metal+tolerance+in+the+fission+yeast+requires+an+ATP-binding+cassette-type+vacuolar+membrane+transporter&aulast=Ortiz&title=EMBO+J.&date=1992&spage=3491&epage=3499&volume=11" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Heavy%20metal%20tolerance%20in%20the%20fission%20yeast%20requires%20an%20ATP-binding%20cassette-type%20vacuolar%20membrane%20transporter&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b70" class="js-splitview-ref-item" data-legacy-id="b70"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b70" href="javascript:;" aria-label="jumplink-b70" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b70" class="ref-content " data-id="b70"><span class="label title-label">[70]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Coblenz</div> <div class="given-names">A.</div> </div> <div class="name"> <div class="surname">Wolf</div> <div class="given-names">K.</div> </div> </span> (<div class="year">1994</div>) <div class="article-title">The role of glutathione biosynthesis in heavy metal resistance in the fission yeast <em>Schizosaccharomyces pombe</em></div>. <div class="source ">FEMS Microbiol. Rev.</div><div class="volume">14</div>, <div class="fpage">303</div>–<div class="lpage">308</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=The%20role%20of%20glutathione%20biosynthesis%20in%20heavy%20metal%20resistance%20in%20the%20fission%20yeast%20Schizosaccharomyces%20pombe&author=A.%20Coblenz&author=K.%20Wolf&publication_year=1994&journal=FEMS%20Microbiol.%20Rev.&volume=14&pages=303-308" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1111/fmr.1994.14.issue-4" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1111%2Ffmr.1994.14.issue-4" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1111%2Ffmr.1994.14.issue-4"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/7917418" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:The%20role%20of%20glutathione%20biosynthesis%20in%20heavy%20metal%20resistance%20in%20the%20fission%20yeast%20Schizosaccharomyces%20pombe&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b71" class="js-splitview-ref-item" data-legacy-id="b71"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b71" href="javascript:;" aria-label="jumplink-b71" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b71" class="ref-content " data-id="b71"><span class="label title-label">[71]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Ha</div> <div class="given-names">S.B.</div> </div> <div class="name"> <div class="surname">Smith</div> <div class="given-names">A.P.</div> </div> <div class="name"> <div class="surname">Howden</div> <div class="given-names">R.</div> </div> <div class="name"> <div class="surname">Dietrich</div> <div class="given-names">W.M.</div> </div> <div class="name"> <div class="surname">Bugg</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">O' Connel</div> <div class="given-names">M.J.</div> </div> <div class="name"> <div class="surname">Goldsbrough</div> <div class="given-names">P.B.</div> </div> <div class="name"> <div class="surname">Cobbet</div> <div class="given-names">C.S.</div> </div> </span> (<div class="year">1999</div>) <div class="article-title">Phytochelatin synthase genes from <em>Arabidopsis</em> and the yeast <em>Schizosaccharomyces pombe</em></div>. <div class="source ">Plant Cell</div><div class="volume">11</div>, <div class="fpage">1153</div>–<div class="lpage">1164</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Phytochelatin%20synthase%20genes%20from%20Arabidopsis%20and%20the%20yeast%20Schizosaccharomyces%20pombe&author=S.B.%20Ha&author=A.P.%20Smith&author=R.%20Howden&author=W.M.%20Dietrich&author=S.%20Bugg&author=M.J.%20O%27%20Connel&author=P.B.%20Goldsbrough&author=C.S.%20Cobbet&publication_year=1999&journal=Plant%20Cell&volume=11&pages=1153-1164" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1105/tpc.11.6.1153" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1105%2Ftpc.11.6.1153" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1105%2Ftpc.11.6.1153"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/10368185" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Phytochelatin%20synthase%20genes%20from%20Arabidopsis%20and%20the%20yeast%20Schizosaccharomyces%20pombe&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b72" class="js-splitview-ref-item" data-legacy-id="b72"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b72" href="javascript:;" aria-label="jumplink-b72" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b72" class="ref-content " data-id="b72"><span class="label title-label">[72]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Clemens</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Kim</div> <div class="given-names">E.J.</div> </div> <div class="name"> <div class="surname">Neumann</div> <div class="given-names">D.</div> </div> <div class="name"> <div class="surname">Schroeder</div> <div class="given-names">J.I.</div> </div> </span> (<div class="year">1999</div>) <div class="article-title">Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast</div>. <div class="source ">EMBO J.</div><div class="volume">18</div>, <div class="fpage">3325</div>–<div class="lpage">3333</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Tolerance%20to%20toxic%20metals%20by%20a%20gene%20family%20of%20phytochelatin%20synthases%20from%20plants%20and%20yeast&author=S.%20Clemens&author=E.J.%20Kim&author=D.%20Neumann&author=J.I.%20Schroeder&publication_year=1999&journal=EMBO%20J.&volume=18&pages=3325-3333" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1093/emboj/18.12.3325" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1093%2Femboj%2F18.12.3325" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1093%2Femboj%2F18.12.3325"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/10369673" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Tolerance%20to%20toxic%20metals%20by%20a%20gene%20family%20of%20phytochelatin%20synthases%20from%20plants%20and%20yeast&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b73" class="js-splitview-ref-item" data-legacy-id="b73"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b73" href="javascript:;" aria-label="jumplink-b73" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b73" class="ref-content " data-id="b73"><span class="label title-label">[73]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Al-Lahham</div> <div class="given-names">A.</div> </div> <div class="name"> <div class="surname">Rohde</div> <div class="given-names">V.</div> </div> <div class="name"> <div class="surname">Heim</div> <div class="given-names">P.</div> </div> <div class="name"> <div class="surname">Leuchter</div> <div class="given-names">R.</div> </div> <div class="name"> <div class="surname">Veeck</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Wunderlich</div> <div class="given-names">C.</div> </div> <div class="name"> <div class="surname">Wolf</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Zimmermann</div> <div class="given-names">M.</div> </div> </span> (<div class="year">1999</div>) <div class="article-title">biosynthesis of phytochelatins in the fission yeast. Phytochelatin synthesis: a second role for the glutathione synthetase gene of <em>Schizosaccharomyces pombe</em></div>. <div class="source ">Yeast</div><div class="volume">15</div>, <div class="fpage">385</div>–<div class="lpage">396</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=biosynthesis%20of%20phytochelatins%20in%20the%20fission%20yeast.%20Phytochelatin%20synthesis%3A%20a%20second%20role%20for%20the%20glutathione%20synthetase%20gene%20of%20Schizosaccharomyces%20pombe&author=A.%20Al-Lahham&author=V.%20Rohde&author=P.%20Heim&author=R.%20Leuchter&author=J.%20Veeck&author=C.%20Wunderlich&author=K.%20Wolf&author=M.%20Zimmermann&publication_year=1999&journal=Yeast&volume=15&pages=385-396" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1002/(ISSN)1097-0061" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1002%2F(ISSN)1097-0061" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1002%2F(ISSN)1097-0061"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/10219997" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:biosynthesis%20of%20phytochelatins%20in%20the%20fission%20yeast.%20Phytochelatin%20synthesis%3A%20a%20second%20role%20for%20the%20glutathione%20synthetase%20gene%20of%20Schizosaccharomyces%20pombe&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b74" class="js-splitview-ref-item" data-legacy-id="b74"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b74" href="javascript:;" aria-label="jumplink-b74" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b74" class="ref-content " data-id="b74"><span class="label title-label">[74]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Li</div> <div class="given-names">Z.S.</div> </div> <div class="name"> <div class="surname">Lu</div> <div class="given-names">Y.P.</div> </div> <div class="name"> <div class="surname">Zhen</div> <div class="given-names">R.G.</div> </div> <div class="name"> <div class="surname">Szczypka</div> <div class="given-names">M.</div> </div> <div class="name"> <div class="surname">Thiele</div> <div class="given-names">D.J.</div> </div> <div class="name"> <div class="surname">Rea</div> <div class="given-names">P.A.</div> </div> </span> (<div class="year">1997</div>) <div class="article-title">A new pathway for vacuolar cadmium sequestration in <em>Saccharomyces cerevisiae</em>: YCF1-catalysed transport of bis (glutathionato) cadmium</div>. <div class="source ">Proc. Natl. Acad. Sci. USA</div><div class="volume">94</div>, <div class="fpage">42</div>–<div class="lpage">47</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=A%20new%20pathway%20for%20vacuolar%20cadmium%20sequestration%20in%20Saccharomyces%20cerevisiae%3A%20YCF1-catalysed%20transport%20of%20bis%20%28glutathionato%29%20cadmium&author=Z.S.%20Li&author=Y.P.%20Lu&author=R.G.%20Zhen&author=M.%20Szczypka&author=D.J.%20Thiele&author=P.A.%20Rea&publication_year=1997&journal=Proc.%20Natl.%20Acad.%20Sci.%20USA&volume=94&pages=42-47" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1073/pnas.94.1.42" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1073%2Fpnas.94.1.42" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1073%2Fpnas.94.1.42"> </span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:A%20new%20pathway%20for%20vacuolar%20cadmium%20sequestration%20in%20Saccharomyces%20cerevisiae%3A%20YCF1-catalysed%20transport%20of%20bis%20%28glutathionato%29%20cadmium&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b75" class="js-splitview-ref-item" data-legacy-id="b75"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b75" href="javascript:;" aria-label="jumplink-b75" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b75" class="ref-content " data-id="b75"><span class="label title-label">[75]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Vido</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Spector</div> <div class="given-names">D.</div> </div> <div class="name"> <div class="surname">Lagniel</div> <div class="given-names">G.</div> </div> <div class="name"> <div class="surname">Lopez</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Toledano</div> <div class="given-names">M.B.</div> </div> <div class="name"> <div class="surname">Labarre</div> <div class="given-names">J.</div> </div> </span> (<div class="year">2001</div>) <div class="article-title">A proteome analysis of the cadmium response in <em>Saccharomyces cerevisiae</em></div>. <div class="source ">J. Biol. Chem.</div><div class="volume">276</div>, <div class="fpage">8469</div>–<div class="lpage">8474</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=A%20proteome%20analysis%20of%20the%20cadmium%20response%20in%20Saccharomyces%20cerevisiae&author=K.%20Vido&author=D.%20Spector&author=G.%20Lagniel&author=S.%20Lopez&author=M.B.%20Toledano&author=J.%20Labarre&publication_year=2001&journal=J.%20Biol.%20Chem.&volume=276&pages=8469-8474" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.M008708200" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.M008708200" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.M008708200"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11078740" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:A%20proteome%20analysis%20of%20the%20cadmium%20response%20in%20Saccharomyces%20cerevisiae&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b76" class="js-splitview-ref-item" data-legacy-id="b76"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b76" href="javascript:;" aria-label="jumplink-b76" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b76" class="ref-content " data-id="b76"><span class="label title-label">[76]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Dormer</div> <div class="given-names">U.H.</div> </div> <div class="name"> <div class="surname">Westwater</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">McLaren</div> <div class="given-names">N.F.</div> </div> <div class="name"> <div class="surname">Kent</div> <div class="given-names">N.A.</div> </div> <div class="name"> <div class="surname">Mellor</div> <div class="given-names">J.</div> </div> <div class="name"> <div class="surname">Jamieson</div> <div class="given-names">D.</div> </div> </span> (<div class="year">2000</div>) <div class="article-title">Cadmium-inducible expression of the yeast <em>GSH1</em> gene requires a functional sulfur-amino acid regulatory network</div>. <div class="source ">J. Biol. Chem.</div><div class="volume">275</div>, <div class="fpage">32611</div>–<div class="lpage">32616</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Cadmium-inducible%20expression%20of%20the%20yeast%20GSH1%20gene%20requires%20a%20functional%20sulfur-amino%20acid%20regulatory%20network&author=U.H.%20Dormer&author=J.%20Westwater&author=N.F.%20McLaren&author=N.A.%20Kent&author=J.%20Mellor&author=D.%20Jamieson&publication_year=2000&journal=J.%20Biol.%20Chem.&volume=275&pages=32611-32616" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1074/jbc.M004167200" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1074%2Fjbc.M004167200" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1074%2Fjbc.M004167200"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/10921921" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Cadmium-inducible%20expression%20of%20the%20yeast%20GSH1%20gene%20requires%20a%20functional%20sulfur-amino%20acid%20regulatory%20network&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b77" class="js-splitview-ref-item" data-legacy-id="b77"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b77" href="javascript:;" aria-label="jumplink-b77" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b77" class="ref-content " data-id="b77"><span class="label title-label">[77]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Thomas</div> <div class="given-names">D.</div> </div> <div class="name"> <div class="surname">Klein</div> <div class="given-names">K.</div> </div> <div class="name"> <div class="surname">Manavathu</div> <div class="given-names">E.</div> </div> <div class="name"> <div class="surname">Dimmock</div> <div class="given-names">J.R.</div> </div> <div class="name"> <div class="surname">Mutus</div> <div class="given-names">B.</div> </div> </span> (<div class="year">1991</div>) <div class="article-title">Glutathione levels during thermal induction of the yeast to mycelial transition in <em>Candida albicans</em></div>. <div class="source ">FEMS Microbiol. Lett.</div><div class="volume">77</div>, <div class="fpage">31</div>–<div class="lpage">334</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione%20levels%20during%20thermal%20induction%20of%20the%20yeast%20to%20mycelial%20transition%20in%20Candida%20albicans&author=D.%20Thomas&author=K.%20Klein&author=E.%20Manavathu&author=J.R.%20Dimmock&author=B.%20Mutus&publication_year=1991&journal=FEMS%20Microbiol.%20Lett.&volume=77&pages=31-334" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1111/fml.1991.77.issue-2-3" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1111%2Ffml.1991.77.issue-2-3" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1111%2Ffml.1991.77.issue-2-3"> </span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione%20levels%20during%20thermal%20induction%20of%20the%20yeast%20to%20mycelial%20transition%20in%20Candida%20albicans&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b78" class="js-splitview-ref-item" data-legacy-id="b78"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b78" href="javascript:;" aria-label="jumplink-b78" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b78" class="ref-content " data-id="b78"><span class="label title-label">[78]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Manavathu</div> <div class="given-names">M.</div> </div> <div class="name"> <div class="surname">Gunasekaran</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Porte</div> <div class="given-names">Q.</div> </div> <div class="name"> <div class="surname">Manavathu</div> <div class="given-names">E.</div> </div> <div class="name"> <div class="surname">Gunasekaran</div> <div class="given-names">M.</div> </div> </span> (<div class="year">1996</div>) <div class="article-title">Changes in glutathione metabolic enzymes during yeast to mycelium conversion of <em>Candida albicans</em></div>. <div class="source ">Can. J. Microbiol.</div><div class="volume">42</div>, <div class="fpage">76</div>–<div class="lpage">79</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Changes%20in%20glutathione%20metabolic%20enzymes%20during%20yeast%20to%20mycelium%20conversion%20of%20Candida%20albicans&author=M.%20Manavathu&author=S.%20Gunasekaran&author=Q.%20Porte&author=E.%20Manavathu&author=M.%20Gunasekaran&publication_year=1996&journal=Can.%20J.%20Microbiol.&volume=42&pages=76-79" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1139/m96-011" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1139%2Fm96-011" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1139%2Fm96-011"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/8595600" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Changes%20in%20glutathione%20metabolic%20enzymes%20during%20yeast%20to%20mycelium%20conversion%20of%20Candida%20albicans&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b79" class="js-splitview-ref-item" data-legacy-id="b79"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b79" href="javascript:;" aria-label="jumplink-b79" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b79" class="ref-content " data-id="b79"><span class="label title-label">[79]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Würtz-Jürgensen</div> <div class="given-names">C.</div> </div> <div class="name"> <div class="surname">Raun Jacobsen</div> <div class="given-names">N.</div> </div> <div class="name"> <div class="surname">Emri</div> <div class="given-names">T.</div> </div> <div class="name"> <div class="surname">Havn Eriksen</div> <div class="given-names">S.</div> </div> <div class="name"> <div class="surname">Pocsi</div> <div class="given-names">I.</div> </div> </span> (<div class="year">2001</div>) <div class="article-title">Glutathione metabolism and dimorphism in <em>Aureobasidium pullulans</em></div>. <div class="source ">J. Basic Microbiol.</div><div class="volume">41</div>, <div class="fpage">131</div>–<div class="lpage">137</div>. </p><div class="citation-links"></div><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Glutathione%20metabolism%20and%20dimorphism%20in%20Aureobasidium%20pullulans&author=C.%20W%C3%BCrtz-J%C3%BCrgensen&author=N.%20Raun%20Jacobsen&author=T.%20Emri&author=S.%20Havn%20Eriksen&author=I.%20Pocsi&publication_year=2001&journal=J.%20Basic%20Microbiol.&volume=41&pages=131-137" target="_blank">Google Scholar</a></span></p><div class="crossref-doi js-ref-link"><a class="openInAnotherWindow" href="http://dx.doi.org/10.1002/(ISSN)1521-4028" target="_blank">Crossref</a></div><div class="adsDoiReference hide"><a class="openInAnotherWindow" href="http://adsabs.harvard.edu/cgi-bin/basic_connect?qsearch=10.1002%2F(ISSN)1521-4028" target="_blank">Search ADS</a></div><div class="xslopenurl empty-target"><span class="inst-open-url-holders" data-targetId="10.1002%2F(ISSN)1521-4028"> </span></div><div class="pub-id"><a href="http://www.ncbi.nlm.nih.gov/pubmed/11441460" class="link link-pub-id openInAnotherWindow" target="_blank">PubMed</a></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Glutathione%20metabolism%20and%20dimorphism%20in%20Aureobasidium%20pullulans&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p> </div></div></div></div></div><div content-id="b80" class="js-splitview-ref-item" data-legacy-id="b80"><div class="refLink-parent"><span class="refLink"><a name="jumplink-b80" href="javascript:;" aria-label="jumplink-b80" data-id=""></a></span></div><div class="ref false"><div id="ref-auto-b80" class="ref-content " data-id="b80"><span class="label title-label">[80]</span><div class="mixed-citation citation"><p class="mixed-citation-compatibility"> <span class="person-group"> <div class="name"> <div class="surname">Griffin</div> <div class="given-names">D.M.</div> </div> </span> (<div class="year">1972</div>) <div class="source ">Ecology of Soil Fungi</div>. <div class="publisher-name">Chapman and Hall</div>, <div class="publisher-loc">London</div>.</p><div class="citation-links"><p class="citation-links-compatibility"><span class="google-scholar-ref-link"><a class="openInAnotherWindow" href="https://scholar.google.com/scholar_lookup?title=Ecology%20of%20Soil%20Fungi&author=D.M.%20Griffin&publication_year=1972&book=Ecology%20of%20Soil%20Fungi" target="_blank">Google Scholar</a></span></p><p class="citation-links-compatibility"><span class="google-preview-ref-link js-google-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.google.com/search?q=Ecology%20of%20Soil%20Fungi&btnG=Search+Books&tbm=bks&tbo=1" target="_blank">Google Preview</a></span></p><div class="xslopenurl empty-target"><span class="js-inst-open-url-holders-nodoi"><a class="js-open-url-link" data-href-template="{targetURL}?sid=oup:orr&genre=book&title=Ecology+of+Soil+Fungi&aulast=Griffin&date=1972" href="javascript:;"><span class="screenreader-text">OpenURL Placeholder Text</span></a></span></div><p class="citation-links-compatibility"><span class="worldcat-reference-ref-link js-worldcat-preview-ref-link" style="display:none"><a class="openInAnotherWindow" href="https://www.worldcat.org/search?q=ti:Ecology%20of%20Soil%20Fungi&qt=advanced&dblist=638" target="_blank">WorldCat</a></span></p><div class="copac-reference-ref-link js-copac-preview-ref-link" style="display:none" data-pubtype="book"><span class="inst-copac"><a class="openInAnotherWindow" target="_blank" href="http://copac.ac.uk/search?ti=Ecology%20of%20Soil%20Fungi">COPAC</a></span></div> </div></div></div></div></div></div>  <div class="widget widget-ArticlePubStateInfo widget-instance-OUP_ArticlePubStateInfo"> </div> <div class="article-metadata-standalone-panel clearfix"></div> <div class="copyright copyright-statement">© 2002 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.</div> <span id="UserHasAccess" data-userHasAccess="True"></span> </div> </div> </div> <div class="widget widget-SolrResourceMetadata widget-instance-OUP_Article_ResourceMetadata_Widget"> </div> <div class="widget widget-EditorInformation widget-instance-OUP_Article_EditorInformation_Widget"> </div> <div id="ContentTabFilteredView"></div> <div class="downloadImagesppt js-download-images-ppt st-download-images-ppt"> <a id="lnkDownloadAllImages" class="js-download-all-images-link btn" href="/DownloadFile/DownloadImage.aspx?image=&PPTtype=SlideSet&ar=562518&xsltPath=~/UI/app/XSLT&siteId=5387">Download all slides</a> </div> <div class="widget widget-ArticleDataRepositories widget-instance-Article_DryadLink"> </div> <div class="comments"> <div class="widget widget-UserCommentBody widget-instance-UserCommentBody_Article"> </div> <div class="widget widget-UserComment widget-instance-OUP_UserComment_Article"> </div> </div> </div> </div> </div> </div> <div id="Sidebar" class="page-column page-column--right"> <div class="widget widget-AdBlock widget-instance-ArticlePageTopSidebar"> <div class="js-adBlock-parent-wrap adblock-parent-wrap"> <div class="adBlockMainBodyTop-wrap js-adBlockMainBodyTop hide"> <div id="adBlockMainBodyTop" class="js-adblock at-adblock" data-lazy-load-margin="150"> <script> googletag.cmd.push(function () { googletag.display('adBlockMainBodyTop'); }); </script> </div> <div class="advertisement-text at-adblock js-adblock-advertisement-text hide">Advertisement</div> </div> </div> </div> <div class="widget widget-dynamic " data-count="1"> <div class="widget-dynamic-inner-wrap"> <div class="widget widget-dynamic " data-count="8"> <div class="widget-dynamic-inner-wrap"> <div class="widget widget-ArticleLevelMetrics widget-instance-Article_RightRailB0Article_RightRail_ArticleLevelMetrics"> <div class="artmet-wrapper horizontal-artmet"> <div class="contentmet-border"> <div class="contentmet-wrapper horizontal-contentmet"> <div class="contentmet-citations contentmet-badges-wrap js-contentmet-citations hide"> <h3 class="contentmet-text">Citations</h3> <div class="contentmet-item contentmet-dimensions"> <div class="widget widget-DimensionsBadge widget-instance-ArticleLevelMetrics_DimensionsBadge"> <span class="__dimensions_badge_embed__" data-doi="10.1016/S1567-1356(02)00081-8" data-legend="never" data-style="small_circle" data-hide-zero-citations="false"></span> <script async src="https://badge.dimensions.ai/badge.js" charset="utf-8"></script> </div> </div> </div> <div class="contentmet-views contentmet-badges-wrap js-contentmet-views"> <h3 class="contentmet-text">Views</h3> <div class="contentmet-item circle-text circle-text-views"> <div class="contentmet-number">17,072</div> </div> </div> <div class="contentmet-item contentmet-badges-wrap"> <h3 class="contentmet-text">Altmetric</h3> <div class="contentmet-item contentmet-altmetric"> <div class="widget widget-AltmetricLink widget-instance-ArticleLevelMetrics_AltmetricLinkSummary">  <div id="altmetricEmbedId" runat="server" class='altmetric-embed' data-badge-type="donut" data-hide-no-mentions="false" data-doi="10.1016/S1567-1356(02)00081-8" ></div> <script type='text/javascript' src='https://d1bxh8uas1mnw7.cloudfront.net/assets/embed.js'></script> </div> </div> </div> <div class="contentmet-modal-trigger-wrap clearfix"> <a href="javascript:;" class="artmet-modal-trigger js-artmet-modal-trigger at-alm-metrics-modal-trigger" data-resource-id="562518" data-resource-type="3" rel=nofollow> <img class="contentmet-info-icon" src="//oup.silverchair-cdn.com/UI/app/svg/i.svg" alt="Information"> <span class="contentmet-more-info">More metrics information</span> </a> </div> </div> </div> <div class="artmet-modal js-artmet-modal" id="MetricsModal"> <div class="artmet-modal-contents js-metric-modal-contents at-alm-modal-contents"> <div class="artmet-full-wrap clearfix js-metric-full-wrap hide"> <div class="widget-title-1 artmet-widget-title-1">Metrics</div> <div class="artmet-item artmet-views-wrap"> <div class="artmet-views clearfix"> <div class="artmet-total-views"> <span class="artmet-text">Total Views</span> <span class="artmet-number">17,072</span> </div> <div class="artmet-breakdown-views-wrap"> <div class="artmet-breakdown-view breakdown-border"> <span class="artmet-number">15,083</span> <span class="artmet-text">Pageviews</span> </div> <div class="artmet-breakdown-view"> <span class="artmet-number">1,989</span> <span class="artmet-text">PDF Downloads</span> </div> </div> </div> <div class="artmet-views-since">Since 10/1/2016</div> </div> <script> var ChartistData = ChartistData || {}; ChartistData.data = { labels: ['Oct 2016', 'Jan 2017', 'Feb 2017', 'Mar 2017', 'Apr 2017', 'May 2017', 'Jun 2017', 'Jul 2017', 'Aug 2017', 'Sep 2017', 'Oct 2017', 'Nov 2017', 'Dec 2017', 'Jan 2018', 'Feb 2018', 'Mar 2018', 'Apr 2018', 'May 2018', 'Jun 2018', 'Jul 2018', 'Aug 2018', 'Sep 2018', 'Oct 2018', 'Nov 2018', 'Dec 2018', 'Jan 2019', 'Feb 2019', 'Mar 2019', 'Apr 2019', 'May 2019', 'Jun 2019', 'Jul 2019', 'Aug 2019', 'Sep 2019', 'Oct 2019', 'Nov 2019', 'Dec 2019', 'Jan 2020', 'Feb 2020', 'Mar 2020', 'Apr 2020', 'May 2020', 'Jun 2020', 'Jul 2020', 'Aug 2020', 'Sep 2020', 'Oct 2020', 'Nov 2020', 'Dec 2020', 'Jan 2021', 'Feb 2021', 'Mar 2021', 'Apr 2021', 'May 2021', 'Jun 2021', 'Jul 2021', 'Aug 2021', 'Sep 2021', 'Oct 2021', 'Nov 2021', 'Dec 2021', 'Jan 2022', 'Feb 2022', 'Mar 2022', 'Apr 2022', 'May 2022', 'Jun 2022', 'Jul 2022', 'Aug 2022', 'Sep 2022', 'Oct 2022', 'Nov 2022', 'Dec 2022', 'Jan 2023', 'Feb 2023', 'Mar 2023', 'Apr 2023', 'May 2023', 'Jun 2023', 'Jul 2023', 'Aug 2023', 'Sep 2023', 'Oct 2023', 'Nov 2023', 'Dec 2023', 'Jan 2024', 'Feb 2024', 'Mar 2024', 'Apr 2024', 'May 2024', 'Jun 2024', 'Jul 2024', 'Aug 2024', 'Sep 2024', 'Oct 2024', 'Nov 2024'], series: [[1, 10, 18, 14, 5, 3, 13, 9, 9, 6, 8, 5, 6080, 4553, 24, 41, 54, 57, 44, 49, 44, 40, 40, 44, 58, 40, 65, 57, 81, 78, 40, 64, 42, 63, 73, 77, 73, 90, 74, 54, 86, 48, 84, 79, 72, 75, 82, 91, 76, 70, 66, 181, 124, 118, 86, 87, 78, 78, 87, 76, 80, 91, 82, 72, 98, 101, 92, 65, 67, 77, 91, 80, 59, 67, 61, 116, 109, 89, 58, 70, 85, 70, 57, 106, 74, 117, 66, 145, 76, 81, 129, 110, 102, 109, 112, 64]] }; </script> <div class="artmet-item artmet-chart"> <div class="ct-chart ct-octave js-ct-chart"></div> <div class="artmet-table"> <table> <thead> <tr> <th>Month:</th> <th>Total Views:</th> </tr> </thead> <tbody> <tr> <td>October 2016</td> <td>1</td> </tr> <tr> <td>January 2017</td> <td>10</td> </tr> <tr> <td>February 2017</td> <td>18</td> </tr> <tr> <td>March 2017</td> <td>14</td> </tr> <tr> <td>April 2017</td> <td>5</td> </tr> <tr> <td>May 2017</td> <td>3</td> </tr> <tr> <td>June 2017</td> <td>13</td> </tr> <tr> <td>July 2017</td> <td>9</td> </tr> <tr> <td>August 2017</td> <td>9</td> </tr> <tr> <td>September 2017</td> <td>6</td> </tr> <tr> <td>October 2017</td> <td>8</td> </tr> <tr> <td>November 2017</td> <td>5</td> </tr> <tr> <td>December 2017</td> <td>6,080</td> </tr> <tr> <td>January 2018</td> <td>4,553</td> </tr> <tr> <td>February 2018</td> <td>24</td> </tr> <tr> <td>March 2018</td> <td>41</td> </tr> <tr> <td>April 2018</td> <td>54</td> </tr> <tr> <td>May 2018</td> <td>57</td> </tr> <tr> <td>June 2018</td> <td>44</td> </tr> <tr> <td>July 2018</td> <td>49</td> </tr> <tr> <td>August 2018</td> <td>44</td> </tr> <tr> <td>September 2018</td> <td>40</td> </tr> <tr> <td>October 2018</td> <td>40</td> </tr> <tr> <td>November 2018</td> <td>44</td> </tr> <tr> <td>December 2018</td> <td>58</td> </tr> <tr> <td>January 2019</td> <td>40</td> </tr> <tr> <td>February 2019</td> <td>65</td> </tr> <tr> <td>March 2019</td> <td>57</td> </tr> <tr> <td>April 2019</td> <td>81</td> </tr> <tr> <td>May 2019</td> <td>78</td> </tr> <tr> <td>June 2019</td> <td>40</td> </tr> <tr> <td>July 2019</td> <td>64</td> </tr> <tr> <td>August 2019</td> <td>42</td> </tr> <tr> <td>September 2019</td> <td>63</td> </tr> <tr> <td>October 2019</td> <td>73</td> </tr> <tr> <td>November 2019</td> <td>77</td> </tr> <tr> <td>December 2019</td> <td>73</td> </tr> <tr> <td>January 2020</td> <td>90</td> </tr> <tr> <td>February 2020</td> <td>74</td> </tr> <tr> <td>March 2020</td> <td>54</td> </tr> <tr> <td>April 2020</td> <td>86</td> </tr> <tr> <td>May 2020</td> <td>48</td> </tr> <tr> <td>June 2020</td> <td>84</td> </tr> <tr> <td>July 2020</td> <td>79</td> </tr> <tr> <td>August 2020</td> <td>72</td> </tr> <tr> <td>September 2020</td> <td>75</td> </tr> <tr> <td>October 2020</td> <td>82</td> </tr> <tr> <td>November 2020</td> <td>91</td> </tr> <tr> <td>December 2020</td> <td>76</td> </tr> <tr> <td>January 2021</td> <td>70</td> </tr> <tr> <td>February 2021</td> <td>66</td> </tr> <tr> <td>March 2021</td> <td>181</td> </tr> <tr> <td>April 2021</td> <td>124</td> </tr> <tr> <td>May 2021</td> <td>118</td> </tr> <tr> <td>June 2021</td> <td>86</td> </tr> <tr> <td>July 2021</td> <td>87</td> </tr> <tr> <td>August 2021</td> <td>78</td> </tr> <tr> <td>September 2021</td> <td>78</td> </tr> <tr> <td>October 2021</td> <td>87</td> </tr> <tr> <td>November 2021</td> <td>76</td> </tr> <tr> <td>December 2021</td> <td>80</td> </tr> <tr> <td>January 2022</td> <td>91</td> </tr> <tr> <td>February 2022</td> <td>82</td> </tr> <tr> <td>March 2022</td> <td>72</td> </tr> <tr> <td>April 2022</td> <td>98</td> </tr> <tr> <td>May 2022</td> <td>101</td> </tr> <tr> <td>June 2022</td> <td>92</td> </tr> <tr> <td>July 2022</td> <td>65</td> </tr> <tr> <td>August 2022</td> <td>67</td> </tr> <tr> <td>September 2022</td> <td>77</td> </tr> <tr> <td>October 2022</td> <td>91</td> </tr> <tr> <td>November 2022</td> <td>80</td> </tr> <tr> <td>December 2022</td> <td>59</td> </tr> <tr> <td>January 2023</td> <td>67</td> </tr> <tr> <td>February 2023</td> <td>61</td> </tr> <tr> <td>March 2023</td> <td>116</td> </tr> <tr> <td>April 2023</td> <td>109</td> </tr> <tr> <td>May 2023</td> <td>89</td> </tr> <tr> <td>June 2023</td> <td>58</td> </tr> <tr> <td>July 2023</td> <td>70</td> </tr> <tr> <td>August 2023</td> <td>85</td> </tr> <tr> <td>September 2023</td> <td>70</td> </tr> <tr> <td>October 2023</td> <td>57</td> </tr> <tr> <td>November 2023</td> <td>106</td> </tr> <tr> <td>December 2023</td> <td>74</td> </tr> <tr> <td>January 2024</td> <td>117</td> </tr> <tr> <td>February 2024</td> <td>66</td> </tr> <tr> <td>March 2024</td> <td>145</td> </tr> <tr> <td>April 2024</td> <td>76</td> </tr> <tr> <td>May 2024</td> <td>81</td> </tr> <tr> <td>June 2024</td> <td>129</td> </tr> <tr> <td>July 2024</td> <td>110</td> </tr> <tr> <td>August 2024</td> <td>102</td> </tr> <tr> <td>September 2024</td> <td>109</td> </tr> <tr> <td>October 2024</td> <td>112</td> </tr> <tr> <td>November 2024</td> <td>64</td> </tr> </tbody> </table> </div> </div> <div class="artmet-stats-wrap clearfix"> <div class="artmet-item artmet-citations hide"> <div class="widget-title-2 artmet-widget-title-2">Citations</div> <div class="artmet-badges-wrap artmet-dimensions"> <div class="widget widget-DimensionsBadge widget-instance-ArticleLevelMetrics_DimensionsBadgeDetails"> <span class="__dimensions_badge_embed__" data-doi="10.1016/S1567-1356(02)00081-8" data-legend="always" data-style="" data-hide-zero-citations="false"></span> <script async src="https://badge.dimensions.ai/badge.js" charset="utf-8"></script> </div> <span class="artmet-dimensions-text">Powered by Dimensions</span> </div> <div class="artmet-wos"> <span class="artmet-number"> <a href="https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=silverchair&SrcAuth=WosAPI&KeyUT=WOS:000183432900007&DestLinkType=CitingArticles&DestApp=WOS_CPL" target="_blank" rel=nofollow>225</a> </span> <span class="artmet-text">Web of Science</span> </div> </div> <div class="artmet-item artmet-altmetric js-show-if-unknown"> <div class="widget-title-2 artmet-widget-title-2">Altmetrics</div> <div class="artmet-badges-wrap js-artmet-badges"> <div class="widget widget-AltmetricLink widget-instance-ArticleLevelMetrics_AltmetricLinkDetails">  <div id="altmetricEmbedId" runat="server" class='altmetric-embed' data-badge-type="donut" data-hide-no-mentions="false" data-doi="10.1016/S1567-1356(02)00081-8" data-badge-details = "right" ></div> <script type='text/javascript' src='https://d1bxh8uas1mnw7.cloudfront.net/assets/embed.js'></script> </div> </div> </div> </div> </div> <a class="artmet-close-modal js-artmet-close-modal">×</a> </div> </div> </div> </div> <div class="widget widget-Alerts widget-instance-Article_RightRailB0Article_RightRail_Alerts"> <div class="alertsWidget"> <h3>Email alerts</h3> <div class="userAlert alertType-1"> <a href="javascript:;" class="js-user-alert" role="button" data-userLoggedIn="False" data-alertType="1" href="javascript:;">Article activity alert</a> </div> <div class="userAlert alertType-3"> <a href="javascript:;" class="js-user-alert" role="button" data-userLoggedIn="False" data-alertType="3" href="javascript:;">Advance article alerts</a> </div> <div class="userAlert alertType-5"> <a href="javascript:;" class="js-user-alert" role="button" data-userLoggedIn="False" data-alertType="5" href="javascript:;">New issue alert</a> </div> <div class="userAlert alertType-30"> <a href="javascript:;" class="js-user-alert" role="button" data-userLoggedIn="False" data-alertType="30" href="javascript:;">In progress issue alert</a> </div> <div class="userAlert alertType-MarketingLink"> <a href="javascript:;" class="js-user-alert" role="button" data-userLoggedIn="False" data-additionalUrl="/my-account/communication-preferences" href="javascript:;">Receive exclusive offers and updates from Oxford Academic</a> </div> <div class="userAlertSignUpModal reveal-modal small" data-reveal> <div class="userAlertSignUp at-userAlertSignUp"></div> <a href="javascript:;" role="button" aria-label="Close" class="close-reveal-modal" href="javascript:;"> <i class="icon-general-close"></i> </a> </div> </div> </div> <div class="widget widget-TrendMD widget-instance-Article_RightRailB0trendmd"> <div id="trendmd-suggestions"></div> <div class="options" data-suppress-if-hum-is-present="True"></div> </div> <div class="widget widget-ArticleCitedBy widget-instance-Article_RightRailB0Article_RightRail_ArticleCitedBy"> <div class="rail-widget_wrap vt-articles-cited-by"> <h3 class="article-cited-title">Citing articles via</h3> <div class="widget-links_wrap"> <div class="article-cited-link-wrap web-of-science"> <a href="https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=silverchair&SrcAuth=WosAPI&KeyUT=WOS:000183432900007&DestLinkType=CitingArticles&DestApp=WOS_CPL" target="_blank" rel="nofollow">Web of Science (225)</a> </div> <div class="article-cited-link-wrap google-scholar-url"> <a href="http://scholar.google.com/scholar?q=link:https%3A%2F%2Facademic.oup.com%2Ffemsyr%2Farticle%2F2%2F3%2F295%2F562518" target="_blank" rel="nofollow">Google Scholar</a> </div> </div> </div> </div> <div class="widget widget-ArticleListNewAndPopular widget-instance-Article_RightRailB0Article_RightRail_ArticleNewPopularCombined"> <ul class="articleListNewAndPopularCombinedView"> <li> <h3> <a href="javascript:;" class="articleListNewAndPopular-mode active" data-mode="MostRecent">Latest</a> </h3> </li> <li> <h3> <a href="javascript:;" class="articleListNewAndPopular-mode " data-mode="MostRead">Most Read</a> </h3> </li> <li> <h3> <a href="javascript:;" class="articleListNewAndPopular-mode " data-mode="MostCited">Most Cited</a> </h3> </li> </ul> <section class="articleListNewPopContent articleListNewAndPopular-ContentView-MostRecent hasContent"> <div id="newPopularList-Article_RightRailB0Article_RightRail_ArticleNewPopularCombined" class="fb"> <div class="widget-layout widget-layout--vert "> <div class="widget-columns widget-col-1"> <div class="col"> <div class="widget-dynamic-entry journalArticleItem at-widget-entry-SCL"> <span class="hfDoi" data-attribute="10.1093/femsyr/foae038" aria-hidden="true"></span> <a class="journal-link" href="/femsyr/advance-article/doi/10.1093/femsyr/foae038/7914158?searchresult=1"> <div class="widget-dynamic-journal-title"> Exploring polyamine metabolism of the yeast-like fungus, <em>Emergomyces africanus</em> </div> </a> <div class="widget-dynamic-journal-image-synopsis"> <div class="widget-dynamic-journal-synopsis"> </div> </div> </div> <div class="widget-dynamic-entry journalArticleItem at-widget-entry-SCL"> <span class="hfDoi" data-attribute="10.1093/femsyr/foae036" aria-hidden="true"></span> <a class="journal-link" href="/femsyr/advance-article/doi/10.1093/femsyr/foae036/7912556?searchresult=1"> <div class="widget-dynamic-journal-title"> Diacylglycerol metabolism and homeostasis in fungal physiology </div> </a> <div class="widget-dynamic-journal-image-synopsis"> <div class="widget-dynamic-journal-synopsis"> </div> </div> </div> <div class="widget-dynamic-entry journalArticleItem at-widget-entry-SCL"> <span class="hfDoi" data-attribute="10.1093/femsyr/foae035" aria-hidden="true"></span> <a class="journal-link" href="/femsyr/advance-article/doi/10.1093/femsyr/foae035/7900768?searchresult=1"> <div class="widget-dynamic-journal-title"> A multidimensional assessment of in-host fitness costs of drug resistance in the opportunistic fungal pathogen <em>Candida glabrata</em> </div> </a> <div class="widget-dynamic-journal-image-synopsis"> <div class="widget-dynamic-journal-synopsis"> </div> </div> </div> <div class="widget-dynamic-entry journalArticleItem at-widget-entry-SCL"> <span class="hfDoi" data-attribute="10.1093/femsyr/foae034" aria-hidden="true"></span> <a class="journal-link" href="/femsyr/article/doi/10.1093/femsyr/foae034/7885146?searchresult=1"> <div class="widget-dynamic-journal-title"> Bridging the gap: linking <em>Torulaspora delbrueckii</em> genotypes to fermentation phenotypes and wine aroma </div> </a> <div class="widget-dynamic-journal-image-synopsis"> <div class="widget-dynamic-journal-synopsis"> </div> </div> </div> <div class="widget-dynamic-entry journalArticleItem at-widget-entry-SCL"> <span class="hfDoi" data-attribute="10.1093/femsyr/foae025" aria-hidden="true"></span> <a class="journal-link" href="/femsyr/article/doi/10.1093/femsyr/foae025/7829348?searchresult=1"> <div class="widget-dynamic-journal-title"> Rapid identification of the predominant azole-resistant genotype in <em>Candida tropicalis</em> </div> </a> <div class="widget-dynamic-journal-image-synopsis"> <div class="widget-dynamic-journal-synopsis"> </div> </div> </div> </div> </div> </div></div> </section> <section class="articleListNewPopContent articleListNewAndPopular-ContentView-MostRead hide"> </section> <section class="articleListNewPopContent articleListNewAndPopular-ContentView-MostCited hide"> </section> </div> <div class="widget widget-RelatedTaxonomies widget-instance-Article_RightRailB0Article_RightRail_RelatedTaxonomies"> <div class="widget-related-taxonomies-wrap vt-related-taxonomies"> <div class="widget-related-taxonomies_title">More from Oxford Academic</div> <div class="widget-related-taxonomies"> <a id="more-from-oa-AcademicSubjects_SCI00960" class="related-taxonomies-link" href="/search-results?tax=AcademicSubjects/SCI00960">Biological Sciences</a> </div> <div class="widget-related-taxonomies"> <a id="more-from-oa-AcademicSubjects_SCI01150" class="related-taxonomies-link" href="/search-results?tax=AcademicSubjects/SCI01150">Microbiology</a> </div> <div class="widget-related-taxonomies"> <a id="more-from-oa-AcademicSubjects_SCI00010" class="related-taxonomies-link" href="/search-results?tax=AcademicSubjects/SCI00010">Science and Mathematics</a> </div> <div class="widget-related-taxonomies"> <a id="more-from-oa-format-Books" class="related-taxonomies-link" href="/books">Books</a> </div> <div class="widget-related-taxonomies"> <a id="more-from-oa-format-Journals" class="related-taxonomies-link" href="/journals">Journals</a> </div> </div> </div> </div> </div> </div> </div> <div class="widget widget-AdBlock widget-instance-ArticlePageTopMainBodyBottom"> <div class="js-adBlock-parent-wrap adblock-parent-wrap"> <div class="adBlockMainBodyBottom-wrap js-adBlockMainBodyBottom hide"> <div id="adBlockMainBodyBottom" class="js-adblock at-adblock js-adblock-lazy-loading" data-lazy-load-margin="150"> <script> googletag.cmd.push(function () { googletag.display('adBlockMainBodyBottom'); }); </script> </div> <div class="advertisement-text at-adblock js-adblock-advertisement-text hide">Advertisement</div> </div> </div> </div> </div> </div> <input id="hfArticleTitle" name="hfArticleTitle" type="hidden" value="overview on glutathione in Saccharomyces versus non-conventional yeasts | FEMS Yeast Research | Oxford Academic" /> <input id="hfLeftNavStickyOffset" name="hfLeftNavStickyOffset" type="hidden" value="29" /> </div> </section> </div> <div class="mobile-mask"> </div> <section class="footer_wrap vt-site-footer"> <div class="ad-banner-footer sticky-footer-ad js-sticky-footer-ad"> <div class="widget widget-AdBlock widget-instance-StickyFooterAd"> <div class="js-adBlock-parent-wrap adblock-parent-wrap"> <div class="adBlockStickyFooter-wrap js-adBlockStickyFooter hide"> <div id="adBlockStickyFooter" class="js-adblock at-adblock" data-lazy-load-margin="150"> <script> googletag.cmd.push(function () { googletag.display('adBlockStickyFooter'); }); </script> </div> <div class="advertisement-text at-adblock js-adblock-advertisement-text hide">Advertisement</div> <button type="button" class="close-footer-ad js-close-footer-ad"> <span class="screenreader-text">close advertisement</span> </button> </div> </div> </div> </div> <div class="widget widget-SitePageFooter widget-instance-SitePageFooter"> <div class="ad-banner ad-banner-footer"> <div class="widget widget-AdBlock widget-instance-FooterAd"> <div class="js-adBlock-parent-wrap adblock-parent-wrap"> <div class="adBlockFooter-wrap js-adBlockFooter hide"> <div id="adBlockFooter" class="js-adblock at-adblock js-adblock-lazy-loading" data-lazy-load-margin="150"> <script> googletag.cmd.push(function () { googletag.display('adBlockFooter'); }); </script> </div> <div class="advertisement-text at-adblock js-adblock-advertisement-text hide">Advertisement</div> </div> </div> </div> </div> <div class="journal-footer journal-bg"> <div class="center-inner-row"> <div class="journal-footer-menu"> <ul> <li class="link-1"> <a href="/femsyr/pages/About">About FEMS Yeast Research</a> </li> <li class="link-2"> <a href="/femsyr/pages/Editorial_Board">Editorial Board</a> </li> <li class="link-3"> <a href="https://academic.oup.com/fems-journals/pages/policies">Policies</a> </li> <li class="link-4"> <a href="/femsyr/pages/manuscript_preparation">Author Guidelines</a> </li> <li class="link-5"> <a href="http://fems-microbiology.org/contact/">Contact Us</a> </li> </ul><ul><li class="link-1"> <a href="https://www.facebook.com/FEMSmicro">Facebook</a> </li> <li class="link-2"> <a href="https://twitter.com/FEMSmicro">X (formerly Twitter)</a> </li> <li class="link-3"> <a href="https://www.linkedin.com/company/federation-of-european-microbiological-societies">LinkedIn</a> </li> <li class="link-4"> <a href="/femsyr/subscribe">Purchase</a> </li> <li class="link-5"> <a href="http://www.oxfordjournals.org/en/library-recommendation-form.html">Recommend to your Library</a> </li> </ul><ul><li class="link-1"> <a href="https://academic.oup.com/advertising-and-corporate-services/pages/femsyr-media-kit">Advertising and Corporate Services</a> </li> <li class="link-2"> <a href="http://science-and-mathematics-careernetwork.oxfordjournals.org">Journals Career Network</a> </li> </ul> </div> <div class="journal-footer-affiliations">  <a href="" target=""> <img id="footer-logo-FEMSYeastResearch" class="journal-footer-affiliations-logo" src="//oup.silverchair-cdn.com/data/SiteBuilderAssets/Live/Images/femsyr/femsyr_f1404264139.svg" alt="FEMS Yeast Research" /> </a> </div> <div class="journal-footer-colophon"> <ul> <li>Online ISSN 1567-1364</li> <li>Print ISSN 1567-1356</li> <li>Copyright © 2024 Federation of European Microbiological Societies</li> </ul> </div> </div> </div> </div> <div class="oup-footer"> <div class="center-inner-row"> <div class="widget widget-SelfServeContent widget-instance-OupUmbrellaFooterSelfServe"> <input type="hidden" class="SelfServeContentId" value="GlobalFooter_Links" /> <input type="hidden" class="SelfServeVersionId" value="0" /> <div class="oup-footer-row journal-links"> <div class="global-footer selfservelinks"> <ul> <li><a href="/pages/about-oxford-academic">About Oxford Academic</a></li> <li><a href="/pages/about-oxford-academic/publish-journals-with-us">Publish journals with us</a></li> <li><a href="/pages/about-oxford-academic/our-university-press-partners">University press partners</a></li> <li><a href="/pages/what-we-publish">What we publish</a></li> <li><a href="/pages/new-features">New features</a> </li> </ul> </div> <div class="global-footer selfservelinks"> <ul> <li><a href="/pages/authoring">Authoring</a></li> <li><a href="/pages/open-research/open-access">Open access</a></li> <li><a href="/pages/purchasing">Purchasing</a></li> <li><a href="/pages/institutional-account-management">Institutional account management</a></li> <li><a href="https://academic.oup.com/pages/purchasing/rights-and-permissions">Rights and permissions</a></li> </ul> </div> <div class="global-footer selfservelinks"> <ul> <li><a href="/pages/get-help-with-access">Get help with access</a></li> <li><a href="/pages/about-oxford-academic/accessibility">Accessibility</a></li> <li><a href="/pages/contact-us">Contact us</a></li> <li><a href="/pages/advertising">Advertising</a></li> <li><a href="/pages/media-enquiries">Media enquiries</a></li> </ul> </div> <div class="global-footer selfservelinks global-footer-external"> <ul> <li><a href="https://global.oup.com/">Oxford University Press</a></li> <li><a href="https://www.mynewsdesk.com/uk/oxford-university-press">News</a></li> <li><a href="https://languages.oup.com/">Oxford Languages</a></li> <li><a href="https://www.ox.ac.uk/">University of Oxford</a></li> </ul> </div> <div class="OUP-mission"> <p>Oxford University Press is a department of the University of Oxford. It furthers the University's objective of excellence in research, scholarship, and education by publishing worldwide</p> <img class="journal-footer-logo" src="//oup.silverchair-cdn.com/UI/app/svg/umbrella/oup-logo.svg" alt="Oxford University Press" width="150" height="42" /> </div> </div> <div class="oup-footer-row"> <div class="oup-footer-row-links"> <ul> <li>Copyright © 2024 Oxford University Press</li> <li><button id="Change-Preferences" type="button" onclick="window.top.document.dispatchEvent(new Event('changeConsent'))">Cookie settings</button></li> <li><a href="https://global.oup.com/cookiepolicy">Cookie policy</a></li> <li><a href="https://global.oup.com/privacy">Privacy policy</a></li> <li><a href="/pages/legal-and-policy/legal-notice">Legal notice</a></li> </ul> </div> </div> <style type="text/css"> /* Issue right column fix for tablet/mobile */ @media (max-width: 1200px) { .pg_issue .widget-instance-OUP_Issue { width: 100%; } } .sf-facet-list .sf-facet label, .sf-facet-list .taxonomy-label-wrap label { font-size: 0.9375rem; } .issue-pagination-wrap .pagination-container { float: right; } </style> </div> </div> </div> <div class="ss-ui-only"> </div> </section> </div> <div class="widget widget-SiteWideModals widget-instance-SiteWideModals"> <div id="revealModal" class="reveal-modal" data-reveal> <div id="revealContent"></div> <a class="close-reveal-modal" href="javascript:;"><i class="icon-general-close"></i><span class="screenreader-text">Close</span></a> </div> <div id="globalModalContainer" class="modal-global-container"> <div id="globalModalContent"> <div class="js-globalModalPlaceholder"></div> </div> <a class="close-modal js-close-modal" href="javascript:;"><i class="icon-general-close"><span class="screenreader-text">Close</span></i></a> </div> <div id="globalModalOverlay" class="modal-overlay js-modal-overlay"></div> <div id="NeedSubscription" class="reveal-modal small" data-reveal> <div class="subscription-needed"> <h5>This Feature Is Available To Subscribers Only</h5> <p><a href="/sign-in">Sign In</a> or <a href="/my-account/register?siteId=5387&returnUrl=%2ffemsyr%2farticle%2f2%2f3%2f295%2f562518">Create an Account</a></p> </div> <a class="close-reveal-modal" href="javascript:;"><i class="icon-general-close"></i><span class="screenreader-text">Close</span></a> </div> <div id="noAccessReveal" class="reveal-modal tiny" data-reveal> <p>This PDF is available to Subscribers Only</p> <a class="hide-for-article-page" id="articleLinkToPurchase" data-reveal><span>View Article Abstract & Purchase Options</span></a> <div class="issue-purchase-modal"> <p>For full access to this pdf, sign in to an existing account, or purchase an annual subscription.</p> </div> <a class="close-reveal-modal" href="javascript:;"><i class="icon-general-close"></i><span class="screenreader-text">Close</span></a> </div> </div> <script type="text/javascript"> MathJax = { tex: { inlineMath: [['|$', '$|'], ['\$', '\$']] } }; </script> <script id="MathJax-script" async src="//cdn.jsdelivr.net/npm/mathjax@3/es5/tex-mml-chtml.js"></script>   <script> var NTPT_PGEXTRA = 'event_type=full-text\u0026supplier_tag=SC_Journals\u0026object_type=Article\u0026taxonomy=taxId%3a39%7ctaxLabel%3aAcademicSubjects%7cnodeId%3aSCI01150%7cnodeLabel%3aMicrobiology%7cnodeLevel%3a3\u0026siteid=femsyr\u0026authzrequired=false\u0026doi=10.1016/S1567-1356(02)00081-8'; </script>  <script type="text/javascript" src="//ouptag.scholarlyiq.com/ntpagetag.js" class="optanon-category-C0002"></script> <noscript> <img src="//ouptag.scholarlyiq.com/ntpagetag.gif?js=0" height="1" width="1" border="0" hspace="0" vspace="0" alt="Scholarly IQ" /> </noscript> <script type="text/javascript" src="//oup.silverchair-cdn.com/Themes/Client/app/jsdist/v-638687870652913006/site.min.js"></script> <script type="text/javascript" src="https://cdn.jsdelivr.net/chartist.js/latest/chartist.min.js"></script> <script type="text/javascript" src="//oup.silverchair-cdn.com/Themes/Client/app/jsdist/v-638687870569311404/article-page.min.js"></script> <div class="ad-banner js-ad-riser ad-banner-riser"> <div class="widget widget-AdBlock widget-instance-RiserAd"> </div> </div> <script src="//oup.silverchair-cdn.com/oup/scm.proxylogging.js"></script> <div class="end-of-page-js"></div> </body> </html>

CINXE.COM

overview on glutathione in Saccharomyces versus non-conventional yeasts | FEMS Yeast Research | Oxford Academic