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Samudrala Gourinath | Jawaharlal Nehru University,New Delhi,India - Academia.edu
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class="user-content-wrapper"><div class="uploads-container" id="social-redesign-work-container"><div class="upload-header"><h2 class="ds2-5-heading-sans-serif-xs">Uploads</h2></div><div class="nav-container backbone-profile-documents-nav hidden-xs"><ul class="nav-tablist" role="tablist"><li class="nav-chip active" role="presentation"><a data-section-name="" data-toggle="tab" href="#all" role="tab">all</a></li><li class="nav-chip" role="presentation"><a class="js-profile-docs-nav-section u-textTruncate" data-click-track="profile-works-tab" data-section-name="Papers" data-toggle="tab" href="#papers" role="tab" title="Papers"><span>122</span> <span class="ds2-5-body-sm-bold">Papers</span></a></li><li class="nav-chip" role="presentation"><a class="js-profile-docs-nav-section u-textTruncate" data-click-track="profile-works-tab" data-section-name="Research-articles" data-toggle="tab" href="#researcharticles" role="tab" title="Research articles"><span>1</span> <span 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bioinformatics tools" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" rel="nofollow" href="https://www.academia.edu/87271883/Identification_of_Actin_binding_proteins_in_Entamoeba_histolytica_proteome_using_bioinformatics_tools">Identification of Actin binding proteins in Entamoeba histolytica proteome using bioinformatics tools</a></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="87271883"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa 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href="https://www.academia.edu/87271875/Cdc42_Rac_Interactive_Binding_Containing_Effector_Proteins_in_Unicellular_Protozoans_With_Reference_to_Human_Host_Locks_of_the_Rho_Signaling"><img alt="Research paper thumbnail of Cdc42/Rac Interactive Binding Containing Effector Proteins in Unicellular Protozoans With Reference to Human Host: Locks of the Rho Signaling" class="work-thumbnail" src="https://attachments.academia-assets.com/91528072/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/87271875/Cdc42_Rac_Interactive_Binding_Containing_Effector_Proteins_in_Unicellular_Protozoans_With_Reference_to_Human_Host_Locks_of_the_Rho_Signaling">Cdc42/Rac Interactive Binding Containing Effector Proteins in Unicellular Protozoans With Reference to Human Host: Locks of the Rho Signaling</a></div><div class="wp-workCard_item"><span>Frontiers in Genetics</span><span>, 2022</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Small GTPases are the key to actin cytoskeleton signaling, which opens the lock of effector prote...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Small GTPases are the key to actin cytoskeleton signaling, which opens the lock of effector proteins to forward the signal downstream in several cellular pathways. Actin cytoskeleton assembly is associated with cell polarity, adhesion, movement and other functions in eukaryotic cells. Rho proteins, specifically Cdc42 and Rac, are the primary regulators of actin cytoskeleton dynamics in higher and lower eukaryotes. Effector proteins, present in an inactive state gets activated after binding to the GTP bound Cdc42/Rac to relay a signal downstream. Cdc42/Rac interactive binding (CRIB) motif is an essential conserved sequence found in effector proteins to interact with Cdc42 or Rac. A diverse range of Cdc42/Rac and their effector proteins have evolved from lower to higher eukaryotes. The present study has identified and further classified CRIB containing effector proteins in lower eukaryotes, focusing on parasitic protozoans causing neglected tropical diseases and taking human proteins ...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="ed23e0a42cfbe44af5fa8157ae465ddd" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":91528072,"asset_id":87271875,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/91528072/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="87271875"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="87271875"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 87271875; 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</script> <div class="js-work-strip profile--work_container" data-work-id="87271848"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/87271848/Expression_and_characterization_of_human_malaria_parasite_Plasmodium_falciparum_origin_recognition_complex_subunit_1"><img alt="Research paper thumbnail of Expression and characterization of human malaria parasite Plasmodium falciparum origin recognition complex subunit 1" class="work-thumbnail" src="https://attachments.academia-assets.com/91528063/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/87271848/Expression_and_characterization_of_human_malaria_parasite_Plasmodium_falciparum_origin_recognition_complex_subunit_1">Expression and characterization of human malaria parasite Plasmodium falciparum origin recognition complex subunit 1</a></div><div class="wp-workCard_item"><span>Biochemical and Biophysical Research Communications</span><span>, 2005</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">In eukaryotes, the origin recognition complex (ORC) is essential for the initiation of DNA replic...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">In eukaryotes, the origin recognition complex (ORC) is essential for the initiation of DNA replication. The largest subunit of this complex (ORC1) has a regulatory role in origin activation. Here we report the cloning and functional characterization of Plasmodium falciparum ORC1 homolog. Using immunofluorescence and immunoelectron microscopy, we show here that PfORC1 is expressed in the nucleus during the late trophozoite and schizont stages where maximum amount of DNA replication takes place. Homology modelling of the carboxy terminal region of PfORC1 (781-1033) using Saccharomyces pombe Cdc6/Cdc18 homolog as a template reveals the presence of a similar AAA+ type nucleotide-binding fold. This region shows ATPase activity in vitro that is important for the origin activity. To our knowledge, this is the first evidence of an individual ORC subunit that shows ATPase activity. These observations strongly suggest that PfORC1 might be involved in DNA replication initiation during the blood stage of the parasitic life cycle.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="fb1b63dedbb0fd764eb99e378bf24e9a" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":91528063,"asset_id":87271848,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/91528063/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="87271848"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="87271848"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 87271848; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=87271848]").text(description); $(".js-view-count[data-work-id=87271848]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 87271848; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='87271848']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "fb1b63dedbb0fd764eb99e378bf24e9a" } } $('.js-work-strip[data-work-id=87271848]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":87271848,"title":"Expression and characterization of human malaria parasite Plasmodium falciparum origin recognition complex subunit 1","internal_url":"https://www.academia.edu/87271848/Expression_and_characterization_of_human_malaria_parasite_Plasmodium_falciparum_origin_recognition_complex_subunit_1","owner_id":43612383,"coauthors_can_edit":true,"owner":{"id":43612383,"first_name":"Samudrala","middle_initials":null,"last_name":"Gourinath","page_name":"SamudralaGourinath","domain_name":"jawaharlalanehrunewdelhiindia","created_at":"2016-02-21T00:03:42.034-08:00","display_name":"Samudrala Gourinath","url":"https://jawaharlalanehrunewdelhiindia.academia.edu/SamudralaGourinath"},"attachments":[{"id":91528063,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/91528063/thumbnails/1.jpg","file_name":"j.bbrc.2005.09.13120220925-1-1grh4vh.pdf","download_url":"https://www.academia.edu/attachments/91528063/download_file","bulk_download_file_name":"Expression_and_characterization_of_human.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/91528063/j.bbrc.2005.09.13120220925-1-1grh4vh-libre.pdf?1664121072=\u0026response-content-disposition=attachment%3B+filename%3DExpression_and_characterization_of_human.pdf\u0026Expires=1740158334\u0026Signature=LhUltMdJMp3u5DnsFXwDk~NJFGQuTXuV4RJ~WDzUY5x9J-dnCfBpqmaPYcrzWzqGa7m1f4jjIFtBeXqqNKfK-X4huFHPqvc3TO4b6vJqpUsR4FSfhGt19rjcZ47A7LxtclDMmg6TO4VHo2kbDfMoH5E~0Hs27Oiy98-gcHSkTw-yPmAai2OQADY37fAloygZKmmQ7HpduuZuLp7sYwlzkEpOTV6jI3Rag5GPbvbfuXZ0L0iAsxls-RyQEF4-aKrYQHNH~mNlfQ4tyDgF29DWiX5mhqe1JGfBYSahDzsHZYXE6a91cRRyA9DdZrBWjitYmJzd~XXuDJeXR2mD51A-kw__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="87271356"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/87271356/Analysis_of_the_Protein_Phosphotome_of_Entamoeba_histolytica_Reveals_an_Intricate_Phosphorylation_Network"><img alt="Research paper thumbnail of Analysis of the Protein Phosphotome of Entamoeba histolytica Reveals an Intricate Phosphorylation Network" class="work-thumbnail" src="https://attachments.academia-assets.com/91527699/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/87271356/Analysis_of_the_Protein_Phosphotome_of_Entamoeba_histolytica_Reveals_an_Intricate_Phosphorylation_Network">Analysis of the Protein Phosphotome of Entamoeba histolytica Reveals an Intricate Phosphorylation Network</a></div><div class="wp-workCard_item"><span>PLoS ONE</span><span>, 2013</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Phosphorylation is the most common mechanism for the propagation of intracellular signals. Protei...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Phosphorylation is the most common mechanism for the propagation of intracellular signals. Protein phosphatases and protein kinases play a dynamic antagonistic role in protein phosphorylation. Protein phosphatases make up a significant fraction of eukaryotic proteome. In this article, we report the identification and analysis of protein phosphatases in the intracellular parasite Entamoeba histolytica. Based on an in silico analysis, we classified 250 non-redundant protein phosphatases in E. histolytica. The phosphotome of E. histolytica is 3.1% of its proteome and 1.3 times of the human phosphotome. In this extensive study, we identified 42 new putative phosphatases (39 hypothetical proteins and 3 pseudophosphatases). The presence of pseudophosphatases may have an important role in virulence of E. histolytica. A comprehensive phosphotome analysis of E. histolytica shows spectacular low similarity to human phosphatases, making them potent candidates for drug target.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="59baa648e3ae78653e81c8ce309fd3e3" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":91527699,"asset_id":87271356,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/91527699/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="87271356"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="87271356"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 87271356; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344626"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344626/Crystal_structure_of_the_VapBC_15_complex_from_Mycobacterium_tuberculosis_reveals_a_two_metal_ion_dependent_PIN_domain_ribonuclease_and_a_variable_mode_of_toxin_antitoxin_assembly"><img alt="Research paper thumbnail of Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis reveals a two-metal ion dependent PIN-domain ribonuclease and a variable mode of toxin-antitoxin assembly" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344626/Crystal_structure_of_the_VapBC_15_complex_from_Mycobacterium_tuberculosis_reveals_a_two_metal_ion_dependent_PIN_domain_ribonuclease_and_a_variable_mode_of_toxin_antitoxin_assembly">Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis reveals a two-metal ion dependent PIN-domain ribonuclease and a variable mode of toxin-antitoxin assembly</a></div><div class="wp-workCard_item"><span>Journal of structural biology</span><span>, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Although PIN (PilT N-terminal)-domain proteins are known to have ribonuclease activity, their spe...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Although PIN (PilT N-terminal)-domain proteins are known to have ribonuclease activity, their specific mechanism of action remains unknown. VapCs form a family of ribonucleases that possess a PIN-domain assembly and are known as toxins. The activities of VapCs are impaired by VapB antitoxins. Here we present the crystal structure of the VapBC-15 toxin-antitoxin complex from Mycobacterium tuberculosis determined to 2.1Å resolution. The VapB-15 and VapC-15 components assemble into one heterotetramer (VapB2C2) and two heterotrimers (VapBC2) in each asymmetric unit of the crystal. The active site of VapC-15 toxin consists of a cluster of acidic amino acid residues and two divalent metal ions, forming a well organised ribonuclease active site. The distribution of the catalytic-site residues of the VapC-15 toxin is similar to that of T4 RNase H and of Methanococcus jannaschii FEN-1, providing strong evidence that these three proteins share a similar mechanism of activity. The presence of ...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="f502bb380035da29b60763517ecdd230" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420300,"asset_id":81344626,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420300/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344626"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344626"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344626; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=81344626]").text(description); $(".js-view-count[data-work-id=81344626]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 81344626; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='81344626']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344609"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344609/Crystal_Structure_of_Calcium_Binding_Protein_5_from_Entamoeba_histolytica_and_Its_Involvement_in_Initiation_of_Phagocytosis_of_Human_Erythrocytes"><img alt="Research paper thumbnail of Crystal Structure of Calcium Binding Protein-5 from Entamoeba histolytica and Its Involvement in Initiation of Phagocytosis of Human Erythrocytes" class="work-thumbnail" src="https://attachments.academia-assets.com/87420287/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344609/Crystal_Structure_of_Calcium_Binding_Protein_5_from_Entamoeba_histolytica_and_Its_Involvement_in_Initiation_of_Phagocytosis_of_Human_Erythrocytes">Crystal Structure of Calcium Binding Protein-5 from Entamoeba histolytica and Its Involvement in Initiation of Phagocytosis of Human Erythrocytes</a></div><div class="wp-workCard_item"><span>PLoS pathogens</span><span>, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Entamoeba histolytica is the etiological agent of human amoebic colitis and liver abscess, and ca...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Entamoeba histolytica is the etiological agent of human amoebic colitis and liver abscess, and causes a high level of morbidity and mortality worldwide, particularly in developing countries. There are a number of studies that have shown a crucial role for Ca2+ and its binding protein in amoebic biology. EhCaBP5 is one of the EF hand calcium-binding proteins of E. histolytica. We have determined the crystal structure of EhCaBP5 at 1.9 Å resolution in the Ca2+-bound state, which shows an unconventional mode of Ca2+ binding involving coordination to a closed yet canonical EF-hand motif. Structurally, EhCaBP5 is more similar to the essential light chain of myosin than to Calmodulin despite its somewhat greater sequence identity with Calmodulin. This structure-based analysis suggests that EhCaBP5 could be a light chain of myosin. Surface plasmon resonance studies confirmed this hypothesis, and in particular showed that EhCaBP5 interacts with the IQ motif of myosin 1B in calcium independe...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="52acff103270de1bb5b624260bb78191" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420287,"asset_id":81344609,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420287/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344609"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344609"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344609; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=81344609]").text(description); $(".js-view-count[data-work-id=81344609]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 81344609; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='81344609']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344572"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344572/Crystal_structure_of_stationary_phase_survival_protein_SurE_from_Brucella_abortus"><img alt="Research paper thumbnail of Crystal structure of stationary phase survival protein (SurE) from Brucella abortus" class="work-thumbnail" src="https://attachments.academia-assets.com/87420265/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344572/Crystal_structure_of_stationary_phase_survival_protein_SurE_from_Brucella_abortus">Crystal structure of stationary phase survival protein (SurE) from Brucella abortus</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">6 Change in population size and composition u<age>bg changed to 1995 values Constant Constant Con...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">6 Change in population size and composition u<age>bg changed to 1995 values Constant Constant Constant Constant Constant 7 Change in labour force activity rate Constant USBGQ changed to 1995 values Constant Constant Constant Constant 8 Change in commuting pattern Constant Constant QABEQ YLORABEQ changed to 1995 values Constant Constant Constant 9 Change in educational composition of population Constant Constant Constant QBEGQ YLORBEGQ changed to 1995 values Constant Constant 10 Change in transfer rates Constant Constant Constant Constant T<cat>BGQ changed to 1995 values Constant 11 Change in transfer structure Constant Constant Constant Constant UT<cat>BGQ changed to 1995 values Constant 12 Change in tax rate Constant Constant Constant Constant Constant S<type>BGQ changed to 1995 values 13 Change in tax structure Constant Constant Constant Constant Constant y(ti)<type>bgq changed to 1995 values Note: Disposable income, ydibg, is endogenous in each of these calculations. Names of variables, see section 4 in the text.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="65710ecf9a65c11fac0850c32d2271cc" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420265,"asset_id":81344572,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420265/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344572"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344572"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344572; 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</script> <div class="js-work-strip profile--work_container" data-work-id="81344506"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344506/Biophysical_aspects_of_lysozyme_adduct_with_monocrotophos"><img alt="Research paper thumbnail of Biophysical aspects of lysozyme adduct with monocrotophos" class="work-thumbnail" src="https://attachments.academia-assets.com/87420221/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344506/Biophysical_aspects_of_lysozyme_adduct_with_monocrotophos">Biophysical aspects of lysozyme adduct with monocrotophos</a></div><div class="wp-workCard_item"><span>Analytical and Bioanalytical Chemistry</span><span>, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The present study on in vitro formation and characterization of lysozyme adduct with monocrotopho...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">The present study on in vitro formation and characterization of lysozyme adduct with monocrotophos (MP) evaluates the potential of lysozyme to be used as a sensitive biomarker to monitor exposure levels to the commonly used organophosphorus pesticide monocrotophos. Crystallization of lysozyme protein adduct with monocrotophos was also undertaken to understand the adduct formation mechanism at a molecular level. The binding of organophosphorus pesticides to lysozyme is one of the key steps in their mutagenicity. The formation and structural characterization of lysozyme adduct with monocrotophos was done using MALDI-TOFMS, fluorescence, UV/Vis spectroscopy, circular dichroism, and X-ray diffraction studies. We report the crystal structure of lysozyme adduct with monocrotophos at 1.9 Å. It crystallized in the P4 3 space group with two monomers in one asymmetric unit having one molecule of monocrotophos bound to each protein chain. The results proved that the fluorescence quenching of lysozyme by monocrotophos is due to binding of monocrotophos with a tryptophan residue of lysozyme. Monocrotophos interacts most strongly with the Trp-108 and Asp-52 of lysozyme. The interactions of the monocrotophos molecule with the lysozyme suggest the formation of a stable adduct. In addition, the alteration of lysozyme secondary structure in the presence of monocrotophos was confirmed by circular dichroism and fluorescence inhibition of lysozyme by increasing monocrotophos and UV/Vis spectrophotometry. The formation of lysozyme adduct with monocrotophos was confirmed by MALDI-TOFMS.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="5d3fb45e448932e07530da69bab021c8" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420221,"asset_id":81344506,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420221/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344506"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344506"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344506; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=81344506]").text(description); $(".js-view-count[data-work-id=81344506]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 81344506; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='81344506']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "5d3fb45e448932e07530da69bab021c8" } } $('.js-work-strip[data-work-id=81344506]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":81344506,"title":"Biophysical aspects of lysozyme adduct with monocrotophos","internal_url":"https://www.academia.edu/81344506/Biophysical_aspects_of_lysozyme_adduct_with_monocrotophos","owner_id":43612383,"coauthors_can_edit":true,"owner":{"id":43612383,"first_name":"Samudrala","middle_initials":null,"last_name":"Gourinath","page_name":"SamudralaGourinath","domain_name":"jawaharlalanehrunewdelhiindia","created_at":"2016-02-21T00:03:42.034-08:00","display_name":"Samudrala Gourinath","url":"https://jawaharlalanehrunewdelhiindia.academia.edu/SamudralaGourinath"},"attachments":[{"id":87420221,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/87420221/thumbnails/1.jpg","file_name":"s00216-014-7953-y20220613-1-b8kbvx.pdf","download_url":"https://www.academia.edu/attachments/87420221/download_file","bulk_download_file_name":"Biophysical_aspects_of_lysozyme_adduct_w.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/87420221/s00216-014-7953-y20220613-1-b8kbvx-libre.pdf?1655097079=\u0026response-content-disposition=attachment%3B+filename%3DBiophysical_aspects_of_lysozyme_adduct_w.pdf\u0026Expires=1740158334\u0026Signature=Ko~I-G7Na8jqltr7pVvOuZliWdB4Gna2RUI6RCMuxZAwzt670bHH6hilQTlTzztGxBCYXno10lEiKfDlxhcV7p2Jm2zjn~6nonVjhPgA15p2orbPonViodbTSr2vjzmJLO4A0qLoD64UaTyKSuZl8w0Z3l6hcjvht~MHY2e3Pg~gSwHOy-5NnEKVuTxdAac7yzF7PHg2jOPA3m-bPcUZsyg93aMhDzEvmPTWoFhiQ11skifVEOrzwrjD8njwlFfZbjn9Gd8aF3H6k2USkhQRsrbvAJanS-~p5vLkHGGpazxOdZO3oIYMdqjmGFvxVFFvBNc9XfRorLYLvYfSwPT4sg__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344483"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344483/Inhibiting_Pyridoxal_Kinase_of_Entamoeba_histolytica_Is_Lethal_for_This_Pathogen"><img alt="Research paper thumbnail of Inhibiting Pyridoxal Kinase of Entamoeba histolytica Is Lethal for This Pathogen" class="work-thumbnail" src="https://attachments.academia-assets.com/87420196/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344483/Inhibiting_Pyridoxal_Kinase_of_Entamoeba_histolytica_Is_Lethal_for_This_Pathogen">Inhibiting Pyridoxal Kinase of Entamoeba histolytica Is Lethal for This Pathogen</a></div><div class="wp-workCard_item"><span>Frontiers in Cellular and Infection Microbiology</span><span>, 2021</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Pyridoxal 5’-phosphate (PLP) functions as a cofactor for hundreds of different enzymes that are c...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Pyridoxal 5’-phosphate (PLP) functions as a cofactor for hundreds of different enzymes that are crucial to the survival of microorganisms. PLP-dependent enzymes have been extensively characterized and proposed as drug targets in Entamoeba histolytica. This pathogen is unable to synthesize vitamin B6via de-novo pathway and relies on the uptake of vitamin B6 vitamers from the host which are then phosphorylated by the enzyme pyridoxal kinase to produce PLP, the active form of vitamin B6. Previous studies from our lab shows that EhPLK is essential for the survival and growth of this protozoan parasite and its active site differs significantly with respect to its human homologue making it a potential drug target. In-silico screening of EhPLK against small molecule libraries were performed and top five ranked molecules were shortlisted on the basis of docking scores. These compounds dock into the PLP binding site of the enzyme such that binding of these compounds hinders the binding of su...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="97b48950515a954ff2f220084cb912ed" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420196,"asset_id":81344483,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420196/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344483"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344483"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344483; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344481"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344481/Structural_and_functional_characterization_of_a_novel_Alpha_Kinase_from_Entamoeba_histolytica"><img alt="Research paper thumbnail of Structural and functional characterization of a novel Alpha Kinase from Entamoeba histolytica" class="work-thumbnail" src="https://attachments.academia-assets.com/87420191/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344481/Structural_and_functional_characterization_of_a_novel_Alpha_Kinase_from_Entamoeba_histolytica">Structural and functional characterization of a novel Alpha Kinase from Entamoeba histolytica</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Diamond films are extensively studied for applications as functional material for UV photoconduct...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Diamond films are extensively studied for applications as functional material for UV photoconductors. CVD-grown polycrystalline diamond films show very interesting performances, but their complete exploitation is actually limited by a slow time response if compared to other materials, by a relatively high concentration of structural defects, impurities and grain boundaries, which may affect the collection length of photogenerated charges. High-quality single crystal diamonds could solve some of these problems. The absence of grain boundaries can produce longer collection lengths. The nitrogen and impurity contents can be reduced and then large type-IIa diamond single-crystals can be obtained. In this work, a detailed structural and functional characterization of type Ib HPHT diamond crystals has been carried out and the results have been compared to similar characterizations of CVD films to evaluate the different behavior, taking also into account that these high pressure high temperature (HPHT) diamond crystals contain several tens ppm of nitrogen.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="03756c02b3220ea1cc6ee3eb3e07919e" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420191,"asset_id":81344481,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420191/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344481"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344481"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344481; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344480"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344480/Crystal_structure_of_O_Acetylserine_sulfhydralase_OASS_isoform_3_from_Entamoeba_histolytica_Pharmacophore_based_virtual_screening_and_validation_of_novel_inhibitors"><img alt="Research paper thumbnail of Crystal structure of O-Acetylserine sulfhydralase (OASS) isoform 3 from Entamoeba histolytica: Pharmacophore-based virtual screening and validation of novel inhibitors" class="work-thumbnail" src="https://attachments.academia-assets.com/87420192/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344480/Crystal_structure_of_O_Acetylserine_sulfhydralase_OASS_isoform_3_from_Entamoeba_histolytica_Pharmacophore_based_virtual_screening_and_validation_of_novel_inhibitors">Crystal structure of O-Acetylserine sulfhydralase (OASS) isoform 3 from Entamoeba histolytica: Pharmacophore-based virtual screening and validation of novel inhibitors</a></div><div class="wp-workCard_item"><span>European Journal of Medicinal Chemistry</span><span>, 2020</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">This is a PDF file of an article that has undergone enhancements after acceptance, such as the ad...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="314c7acb706aa4d18680d92f75e8cd9e" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420192,"asset_id":81344480,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420192/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344480"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344480"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344480; 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</script> <div class="js-work-strip profile--work_container" data-work-id="87271875"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/87271875/Cdc42_Rac_Interactive_Binding_Containing_Effector_Proteins_in_Unicellular_Protozoans_With_Reference_to_Human_Host_Locks_of_the_Rho_Signaling"><img alt="Research paper thumbnail of Cdc42/Rac Interactive Binding Containing Effector Proteins in Unicellular Protozoans With Reference to Human Host: Locks of the Rho Signaling" class="work-thumbnail" src="https://attachments.academia-assets.com/91528072/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/87271875/Cdc42_Rac_Interactive_Binding_Containing_Effector_Proteins_in_Unicellular_Protozoans_With_Reference_to_Human_Host_Locks_of_the_Rho_Signaling">Cdc42/Rac Interactive Binding Containing Effector Proteins in Unicellular Protozoans With Reference to Human Host: Locks of the Rho Signaling</a></div><div class="wp-workCard_item"><span>Frontiers in Genetics</span><span>, 2022</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Small GTPases are the key to actin cytoskeleton signaling, which opens the lock of effector prote...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Small GTPases are the key to actin cytoskeleton signaling, which opens the lock of effector proteins to forward the signal downstream in several cellular pathways. Actin cytoskeleton assembly is associated with cell polarity, adhesion, movement and other functions in eukaryotic cells. Rho proteins, specifically Cdc42 and Rac, are the primary regulators of actin cytoskeleton dynamics in higher and lower eukaryotes. Effector proteins, present in an inactive state gets activated after binding to the GTP bound Cdc42/Rac to relay a signal downstream. Cdc42/Rac interactive binding (CRIB) motif is an essential conserved sequence found in effector proteins to interact with Cdc42 or Rac. A diverse range of Cdc42/Rac and their effector proteins have evolved from lower to higher eukaryotes. The present study has identified and further classified CRIB containing effector proteins in lower eukaryotes, focusing on parasitic protozoans causing neglected tropical diseases and taking human proteins ...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="ed23e0a42cfbe44af5fa8157ae465ddd" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":91528072,"asset_id":87271875,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/91528072/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="87271875"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="87271875"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 87271875; 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window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=87271853]").text(description); $(".js-view-count[data-work-id=87271853]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 87271853; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='87271853']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (false){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "-1" } } $('.js-work-strip[data-work-id=87271853]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":87271853,"title":"Crystal structure of phosphoglycerate oxidoreductase from Vibrio Cholerae o395","internal_url":"https://www.academia.edu/87271853/Crystal_structure_of_phosphoglycerate_oxidoreductase_from_Vibrio_Cholerae_o395","owner_id":43612383,"coauthors_can_edit":true,"owner":{"id":43612383,"first_name":"Samudrala","middle_initials":null,"last_name":"Gourinath","page_name":"SamudralaGourinath","domain_name":"jawaharlalanehrunewdelhiindia","created_at":"2016-02-21T00:03:42.034-08:00","display_name":"Samudrala Gourinath","url":"https://jawaharlalanehrunewdelhiindia.academia.edu/SamudralaGourinath"},"attachments":[]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="87271848"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/87271848/Expression_and_characterization_of_human_malaria_parasite_Plasmodium_falciparum_origin_recognition_complex_subunit_1"><img alt="Research paper thumbnail of Expression and characterization of human malaria parasite Plasmodium falciparum origin recognition complex subunit 1" class="work-thumbnail" src="https://attachments.academia-assets.com/91528063/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/87271848/Expression_and_characterization_of_human_malaria_parasite_Plasmodium_falciparum_origin_recognition_complex_subunit_1">Expression and characterization of human malaria parasite Plasmodium falciparum origin recognition complex subunit 1</a></div><div class="wp-workCard_item"><span>Biochemical and Biophysical Research Communications</span><span>, 2005</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">In eukaryotes, the origin recognition complex (ORC) is essential for the initiation of DNA replic...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">In eukaryotes, the origin recognition complex (ORC) is essential for the initiation of DNA replication. The largest subunit of this complex (ORC1) has a regulatory role in origin activation. Here we report the cloning and functional characterization of Plasmodium falciparum ORC1 homolog. Using immunofluorescence and immunoelectron microscopy, we show here that PfORC1 is expressed in the nucleus during the late trophozoite and schizont stages where maximum amount of DNA replication takes place. Homology modelling of the carboxy terminal region of PfORC1 (781-1033) using Saccharomyces pombe Cdc6/Cdc18 homolog as a template reveals the presence of a similar AAA+ type nucleotide-binding fold. This region shows ATPase activity in vitro that is important for the origin activity. To our knowledge, this is the first evidence of an individual ORC subunit that shows ATPase activity. These observations strongly suggest that PfORC1 might be involved in DNA replication initiation during the blood stage of the parasitic life cycle.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="fb1b63dedbb0fd764eb99e378bf24e9a" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":91528063,"asset_id":87271848,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/91528063/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="87271848"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="87271848"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 87271848; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=87271848]").text(description); $(".js-view-count[data-work-id=87271848]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 87271848; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='87271848']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "fb1b63dedbb0fd764eb99e378bf24e9a" } } $('.js-work-strip[data-work-id=87271848]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":87271848,"title":"Expression and characterization of human malaria parasite Plasmodium falciparum origin recognition complex subunit 1","internal_url":"https://www.academia.edu/87271848/Expression_and_characterization_of_human_malaria_parasite_Plasmodium_falciparum_origin_recognition_complex_subunit_1","owner_id":43612383,"coauthors_can_edit":true,"owner":{"id":43612383,"first_name":"Samudrala","middle_initials":null,"last_name":"Gourinath","page_name":"SamudralaGourinath","domain_name":"jawaharlalanehrunewdelhiindia","created_at":"2016-02-21T00:03:42.034-08:00","display_name":"Samudrala Gourinath","url":"https://jawaharlalanehrunewdelhiindia.academia.edu/SamudralaGourinath"},"attachments":[{"id":91528063,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/91528063/thumbnails/1.jpg","file_name":"j.bbrc.2005.09.13120220925-1-1grh4vh.pdf","download_url":"https://www.academia.edu/attachments/91528063/download_file","bulk_download_file_name":"Expression_and_characterization_of_human.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/91528063/j.bbrc.2005.09.13120220925-1-1grh4vh-libre.pdf?1664121072=\u0026response-content-disposition=attachment%3B+filename%3DExpression_and_characterization_of_human.pdf\u0026Expires=1740158334\u0026Signature=LhUltMdJMp3u5DnsFXwDk~NJFGQuTXuV4RJ~WDzUY5x9J-dnCfBpqmaPYcrzWzqGa7m1f4jjIFtBeXqqNKfK-X4huFHPqvc3TO4b6vJqpUsR4FSfhGt19rjcZ47A7LxtclDMmg6TO4VHo2kbDfMoH5E~0Hs27Oiy98-gcHSkTw-yPmAai2OQADY37fAloygZKmmQ7HpduuZuLp7sYwlzkEpOTV6jI3Rag5GPbvbfuXZ0L0iAsxls-RyQEF4-aKrYQHNH~mNlfQ4tyDgF29DWiX5mhqe1JGfBYSahDzsHZYXE6a91cRRyA9DdZrBWjitYmJzd~XXuDJeXR2mD51A-kw__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="87271356"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/87271356/Analysis_of_the_Protein_Phosphotome_of_Entamoeba_histolytica_Reveals_an_Intricate_Phosphorylation_Network"><img alt="Research paper thumbnail of Analysis of the Protein Phosphotome of Entamoeba histolytica Reveals an Intricate Phosphorylation Network" class="work-thumbnail" src="https://attachments.academia-assets.com/91527699/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/87271356/Analysis_of_the_Protein_Phosphotome_of_Entamoeba_histolytica_Reveals_an_Intricate_Phosphorylation_Network">Analysis of the Protein Phosphotome of Entamoeba histolytica Reveals an Intricate Phosphorylation Network</a></div><div class="wp-workCard_item"><span>PLoS ONE</span><span>, 2013</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Phosphorylation is the most common mechanism for the propagation of intracellular signals. Protei...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Phosphorylation is the most common mechanism for the propagation of intracellular signals. Protein phosphatases and protein kinases play a dynamic antagonistic role in protein phosphorylation. Protein phosphatases make up a significant fraction of eukaryotic proteome. In this article, we report the identification and analysis of protein phosphatases in the intracellular parasite Entamoeba histolytica. Based on an in silico analysis, we classified 250 non-redundant protein phosphatases in E. histolytica. The phosphotome of E. histolytica is 3.1% of its proteome and 1.3 times of the human phosphotome. In this extensive study, we identified 42 new putative phosphatases (39 hypothetical proteins and 3 pseudophosphatases). The presence of pseudophosphatases may have an important role in virulence of E. histolytica. A comprehensive phosphotome analysis of E. histolytica shows spectacular low similarity to human phosphatases, making them potent candidates for drug target.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="59baa648e3ae78653e81c8ce309fd3e3" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":91527699,"asset_id":87271356,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/91527699/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="87271356"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="87271356"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 87271356; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=87271356]").text(description); $(".js-view-count[data-work-id=87271356]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 87271356; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='87271356']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "59baa648e3ae78653e81c8ce309fd3e3" } } $('.js-work-strip[data-work-id=87271356]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":87271356,"title":"Analysis of the Protein Phosphotome of Entamoeba histolytica Reveals an Intricate Phosphorylation Network","internal_url":"https://www.academia.edu/87271356/Analysis_of_the_Protein_Phosphotome_of_Entamoeba_histolytica_Reveals_an_Intricate_Phosphorylation_Network","owner_id":43612383,"coauthors_can_edit":true,"owner":{"id":43612383,"first_name":"Samudrala","middle_initials":null,"last_name":"Gourinath","page_name":"SamudralaGourinath","domain_name":"jawaharlalanehrunewdelhiindia","created_at":"2016-02-21T00:03:42.034-08:00","display_name":"Samudrala Gourinath","url":"https://jawaharlalanehrunewdelhiindia.academia.edu/SamudralaGourinath"},"attachments":[{"id":91527699,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/91527699/thumbnails/1.jpg","file_name":"be21023ac917d294a8ee320b9bd3ce616eb7.pdf","download_url":"https://www.academia.edu/attachments/91527699/download_file","bulk_download_file_name":"Analysis_of_the_Protein_Phosphotome_of_E.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/91527699/be21023ac917d294a8ee320b9bd3ce616eb7-libre.pdf?1664122886=\u0026response-content-disposition=attachment%3B+filename%3DAnalysis_of_the_Protein_Phosphotome_of_E.pdf\u0026Expires=1740158334\u0026Signature=HL5BGJ2LIkjgK-eQ3cA2uT5mbYHXKYsT--9n-CvLCxqgWnEu7B-L6WsYEZr-4016i2DJCOjI5CGcfCTFUgPhucy2vo8FJ4z9-mvgm4domE5Ip0UYuEnWCrcofBiD6EKCBHZSN-733mWQSkSC7xjHkvelqFZluwhxFK7UCuipy4p8sIvAQWElVkwFBk1PTf5gwrmusvHsIfnvjOg4MYOvLXCZvndAIqHLQ2io5Yl-2dmsDnXQgjIY4Bmo70OOJ5pp1FpPZ-Cza9jFJW8LWRhzyB4eVgq61uSvTTHzRSFxNKsWAC3nLRIAKL6vjMfRYLtoF0Y6G7v62oUAhqOSH3WcJg__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344626"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344626/Crystal_structure_of_the_VapBC_15_complex_from_Mycobacterium_tuberculosis_reveals_a_two_metal_ion_dependent_PIN_domain_ribonuclease_and_a_variable_mode_of_toxin_antitoxin_assembly"><img alt="Research paper thumbnail of Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis reveals a two-metal ion dependent PIN-domain ribonuclease and a variable mode of toxin-antitoxin assembly" class="work-thumbnail" src="https://a.academia-assets.com/images/blank-paper.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344626/Crystal_structure_of_the_VapBC_15_complex_from_Mycobacterium_tuberculosis_reveals_a_two_metal_ion_dependent_PIN_domain_ribonuclease_and_a_variable_mode_of_toxin_antitoxin_assembly">Crystal structure of the VapBC-15 complex from Mycobacterium tuberculosis reveals a two-metal ion dependent PIN-domain ribonuclease and a variable mode of toxin-antitoxin assembly</a></div><div class="wp-workCard_item"><span>Journal of structural biology</span><span>, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Although PIN (PilT N-terminal)-domain proteins are known to have ribonuclease activity, their spe...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Although PIN (PilT N-terminal)-domain proteins are known to have ribonuclease activity, their specific mechanism of action remains unknown. VapCs form a family of ribonucleases that possess a PIN-domain assembly and are known as toxins. The activities of VapCs are impaired by VapB antitoxins. Here we present the crystal structure of the VapBC-15 toxin-antitoxin complex from Mycobacterium tuberculosis determined to 2.1Å resolution. The VapB-15 and VapC-15 components assemble into one heterotetramer (VapB2C2) and two heterotrimers (VapBC2) in each asymmetric unit of the crystal. The active site of VapC-15 toxin consists of a cluster of acidic amino acid residues and two divalent metal ions, forming a well organised ribonuclease active site. The distribution of the catalytic-site residues of the VapC-15 toxin is similar to that of T4 RNase H and of Methanococcus jannaschii FEN-1, providing strong evidence that these three proteins share a similar mechanism of activity. The presence of ...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="f502bb380035da29b60763517ecdd230" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420300,"asset_id":81344626,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420300/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344626"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344626"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344626; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344609"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344609/Crystal_Structure_of_Calcium_Binding_Protein_5_from_Entamoeba_histolytica_and_Its_Involvement_in_Initiation_of_Phagocytosis_of_Human_Erythrocytes"><img alt="Research paper thumbnail of Crystal Structure of Calcium Binding Protein-5 from Entamoeba histolytica and Its Involvement in Initiation of Phagocytosis of Human Erythrocytes" class="work-thumbnail" src="https://attachments.academia-assets.com/87420287/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344609/Crystal_Structure_of_Calcium_Binding_Protein_5_from_Entamoeba_histolytica_and_Its_Involvement_in_Initiation_of_Phagocytosis_of_Human_Erythrocytes">Crystal Structure of Calcium Binding Protein-5 from Entamoeba histolytica and Its Involvement in Initiation of Phagocytosis of Human Erythrocytes</a></div><div class="wp-workCard_item"><span>PLoS pathogens</span><span>, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Entamoeba histolytica is the etiological agent of human amoebic colitis and liver abscess, and ca...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Entamoeba histolytica is the etiological agent of human amoebic colitis and liver abscess, and causes a high level of morbidity and mortality worldwide, particularly in developing countries. There are a number of studies that have shown a crucial role for Ca2+ and its binding protein in amoebic biology. EhCaBP5 is one of the EF hand calcium-binding proteins of E. histolytica. We have determined the crystal structure of EhCaBP5 at 1.9 Å resolution in the Ca2+-bound state, which shows an unconventional mode of Ca2+ binding involving coordination to a closed yet canonical EF-hand motif. Structurally, EhCaBP5 is more similar to the essential light chain of myosin than to Calmodulin despite its somewhat greater sequence identity with Calmodulin. This structure-based analysis suggests that EhCaBP5 could be a light chain of myosin. Surface plasmon resonance studies confirmed this hypothesis, and in particular showed that EhCaBP5 interacts with the IQ motif of myosin 1B in calcium independe...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="52acff103270de1bb5b624260bb78191" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420287,"asset_id":81344609,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420287/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344609"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344609"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344609; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344572"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344572/Crystal_structure_of_stationary_phase_survival_protein_SurE_from_Brucella_abortus"><img alt="Research paper thumbnail of Crystal structure of stationary phase survival protein (SurE) from Brucella abortus" class="work-thumbnail" src="https://attachments.academia-assets.com/87420265/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344572/Crystal_structure_of_stationary_phase_survival_protein_SurE_from_Brucella_abortus">Crystal structure of stationary phase survival protein (SurE) from Brucella abortus</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">6 Change in population size and composition u<age>bg changed to 1995 values Constant Constant Con...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">6 Change in population size and composition u<age>bg changed to 1995 values Constant Constant Constant Constant Constant 7 Change in labour force activity rate Constant USBGQ changed to 1995 values Constant Constant Constant Constant 8 Change in commuting pattern Constant Constant QABEQ YLORABEQ changed to 1995 values Constant Constant Constant 9 Change in educational composition of population Constant Constant Constant QBEGQ YLORBEGQ changed to 1995 values Constant Constant 10 Change in transfer rates Constant Constant Constant Constant T<cat>BGQ changed to 1995 values Constant 11 Change in transfer structure Constant Constant Constant Constant UT<cat>BGQ changed to 1995 values Constant 12 Change in tax rate Constant Constant Constant Constant Constant S<type>BGQ changed to 1995 values 13 Change in tax structure Constant Constant Constant Constant Constant y(ti)<type>bgq changed to 1995 values Note: Disposable income, ydibg, is endogenous in each of these calculations. Names of variables, see section 4 in the text.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="65710ecf9a65c11fac0850c32d2271cc" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420265,"asset_id":81344572,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420265/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344572"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344572"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344572; 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</script> <div class="js-work-strip profile--work_container" data-work-id="81344506"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344506/Biophysical_aspects_of_lysozyme_adduct_with_monocrotophos"><img alt="Research paper thumbnail of Biophysical aspects of lysozyme adduct with monocrotophos" class="work-thumbnail" src="https://attachments.academia-assets.com/87420221/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344506/Biophysical_aspects_of_lysozyme_adduct_with_monocrotophos">Biophysical aspects of lysozyme adduct with monocrotophos</a></div><div class="wp-workCard_item"><span>Analytical and Bioanalytical Chemistry</span><span>, 2014</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The present study on in vitro formation and characterization of lysozyme adduct with monocrotopho...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">The present study on in vitro formation and characterization of lysozyme adduct with monocrotophos (MP) evaluates the potential of lysozyme to be used as a sensitive biomarker to monitor exposure levels to the commonly used organophosphorus pesticide monocrotophos. Crystallization of lysozyme protein adduct with monocrotophos was also undertaken to understand the adduct formation mechanism at a molecular level. The binding of organophosphorus pesticides to lysozyme is one of the key steps in their mutagenicity. The formation and structural characterization of lysozyme adduct with monocrotophos was done using MALDI-TOFMS, fluorescence, UV/Vis spectroscopy, circular dichroism, and X-ray diffraction studies. We report the crystal structure of lysozyme adduct with monocrotophos at 1.9 Å. It crystallized in the P4 3 space group with two monomers in one asymmetric unit having one molecule of monocrotophos bound to each protein chain. The results proved that the fluorescence quenching of lysozyme by monocrotophos is due to binding of monocrotophos with a tryptophan residue of lysozyme. Monocrotophos interacts most strongly with the Trp-108 and Asp-52 of lysozyme. The interactions of the monocrotophos molecule with the lysozyme suggest the formation of a stable adduct. In addition, the alteration of lysozyme secondary structure in the presence of monocrotophos was confirmed by circular dichroism and fluorescence inhibition of lysozyme by increasing monocrotophos and UV/Vis spectrophotometry. The formation of lysozyme adduct with monocrotophos was confirmed by MALDI-TOFMS.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="5d3fb45e448932e07530da69bab021c8" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420221,"asset_id":81344506,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420221/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344506"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344506"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344506; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=81344506]").text(description); $(".js-view-count[data-work-id=81344506]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 81344506; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='81344506']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); dispatcherData = { dispatcher: window.WowProfile.dispatcher, downloadLinkId: "5d3fb45e448932e07530da69bab021c8" } } $('.js-work-strip[data-work-id=81344506]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":81344506,"title":"Biophysical aspects of lysozyme adduct with monocrotophos","internal_url":"https://www.academia.edu/81344506/Biophysical_aspects_of_lysozyme_adduct_with_monocrotophos","owner_id":43612383,"coauthors_can_edit":true,"owner":{"id":43612383,"first_name":"Samudrala","middle_initials":null,"last_name":"Gourinath","page_name":"SamudralaGourinath","domain_name":"jawaharlalanehrunewdelhiindia","created_at":"2016-02-21T00:03:42.034-08:00","display_name":"Samudrala Gourinath","url":"https://jawaharlalanehrunewdelhiindia.academia.edu/SamudralaGourinath"},"attachments":[{"id":87420221,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/87420221/thumbnails/1.jpg","file_name":"s00216-014-7953-y20220613-1-b8kbvx.pdf","download_url":"https://www.academia.edu/attachments/87420221/download_file","bulk_download_file_name":"Biophysical_aspects_of_lysozyme_adduct_w.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/87420221/s00216-014-7953-y20220613-1-b8kbvx-libre.pdf?1655097079=\u0026response-content-disposition=attachment%3B+filename%3DBiophysical_aspects_of_lysozyme_adduct_w.pdf\u0026Expires=1740158334\u0026Signature=Ko~I-G7Na8jqltr7pVvOuZliWdB4Gna2RUI6RCMuxZAwzt670bHH6hilQTlTzztGxBCYXno10lEiKfDlxhcV7p2Jm2zjn~6nonVjhPgA15p2orbPonViodbTSr2vjzmJLO4A0qLoD64UaTyKSuZl8w0Z3l6hcjvht~MHY2e3Pg~gSwHOy-5NnEKVuTxdAac7yzF7PHg2jOPA3m-bPcUZsyg93aMhDzEvmPTWoFhiQ11skifVEOrzwrjD8njwlFfZbjn9Gd8aF3H6k2USkhQRsrbvAJanS-~p5vLkHGGpazxOdZO3oIYMdqjmGFvxVFFvBNc9XfRorLYLvYfSwPT4sg__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}]}, dispatcherData: dispatcherData }); $(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344483"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344483/Inhibiting_Pyridoxal_Kinase_of_Entamoeba_histolytica_Is_Lethal_for_This_Pathogen"><img alt="Research paper thumbnail of Inhibiting Pyridoxal Kinase of Entamoeba histolytica Is Lethal for This Pathogen" class="work-thumbnail" src="https://attachments.academia-assets.com/87420196/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344483/Inhibiting_Pyridoxal_Kinase_of_Entamoeba_histolytica_Is_Lethal_for_This_Pathogen">Inhibiting Pyridoxal Kinase of Entamoeba histolytica Is Lethal for This Pathogen</a></div><div class="wp-workCard_item"><span>Frontiers in Cellular and Infection Microbiology</span><span>, 2021</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Pyridoxal 5’-phosphate (PLP) functions as a cofactor for hundreds of different enzymes that are c...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Pyridoxal 5’-phosphate (PLP) functions as a cofactor for hundreds of different enzymes that are crucial to the survival of microorganisms. PLP-dependent enzymes have been extensively characterized and proposed as drug targets in Entamoeba histolytica. This pathogen is unable to synthesize vitamin B6via de-novo pathway and relies on the uptake of vitamin B6 vitamers from the host which are then phosphorylated by the enzyme pyridoxal kinase to produce PLP, the active form of vitamin B6. Previous studies from our lab shows that EhPLK is essential for the survival and growth of this protozoan parasite and its active site differs significantly with respect to its human homologue making it a potential drug target. In-silico screening of EhPLK against small molecule libraries were performed and top five ranked molecules were shortlisted on the basis of docking scores. These compounds dock into the PLP binding site of the enzyme such that binding of these compounds hinders the binding of su...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="97b48950515a954ff2f220084cb912ed" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420196,"asset_id":81344483,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420196/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344483"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344483"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344483; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344481"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344481/Structural_and_functional_characterization_of_a_novel_Alpha_Kinase_from_Entamoeba_histolytica"><img alt="Research paper thumbnail of Structural and functional characterization of a novel Alpha Kinase from Entamoeba histolytica" class="work-thumbnail" src="https://attachments.academia-assets.com/87420191/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344481/Structural_and_functional_characterization_of_a_novel_Alpha_Kinase_from_Entamoeba_histolytica">Structural and functional characterization of a novel Alpha Kinase from Entamoeba histolytica</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Diamond films are extensively studied for applications as functional material for UV photoconduct...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">Diamond films are extensively studied for applications as functional material for UV photoconductors. CVD-grown polycrystalline diamond films show very interesting performances, but their complete exploitation is actually limited by a slow time response if compared to other materials, by a relatively high concentration of structural defects, impurities and grain boundaries, which may affect the collection length of photogenerated charges. High-quality single crystal diamonds could solve some of these problems. The absence of grain boundaries can produce longer collection lengths. The nitrogen and impurity contents can be reduced and then large type-IIa diamond single-crystals can be obtained. In this work, a detailed structural and functional characterization of type Ib HPHT diamond crystals has been carried out and the results have been compared to similar characterizations of CVD films to evaluate the different behavior, taking also into account that these high pressure high temperature (HPHT) diamond crystals contain several tens ppm of nitrogen.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="03756c02b3220ea1cc6ee3eb3e07919e" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420191,"asset_id":81344481,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420191/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344481"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344481"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344481; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344480"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344480/Crystal_structure_of_O_Acetylserine_sulfhydralase_OASS_isoform_3_from_Entamoeba_histolytica_Pharmacophore_based_virtual_screening_and_validation_of_novel_inhibitors"><img alt="Research paper thumbnail of Crystal structure of O-Acetylserine sulfhydralase (OASS) isoform 3 from Entamoeba histolytica: Pharmacophore-based virtual screening and validation of novel inhibitors" class="work-thumbnail" src="https://attachments.academia-assets.com/87420192/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344480/Crystal_structure_of_O_Acetylserine_sulfhydralase_OASS_isoform_3_from_Entamoeba_histolytica_Pharmacophore_based_virtual_screening_and_validation_of_novel_inhibitors">Crystal structure of O-Acetylserine sulfhydralase (OASS) isoform 3 from Entamoeba histolytica: Pharmacophore-based virtual screening and validation of novel inhibitors</a></div><div class="wp-workCard_item"><span>European Journal of Medicinal Chemistry</span><span>, 2020</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">This is a PDF file of an article that has undergone enhancements after acceptance, such as the ad...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">This is a PDF file of an article that has undergone enhancements after acceptance, such as the addition of a cover page and metadata, and formatting for readability, but it is not yet the definitive version of record. This version will undergo additional copyediting, typesetting and review before it is published in its final form, but we are providing this version to give early visibility of the article. Please note that, during the production process, errors may be discovered which could affect the content, and all legal disclaimers that apply to the journal pertain.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="314c7acb706aa4d18680d92f75e8cd9e" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420192,"asset_id":81344480,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420192/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344480"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344480"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344480; 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> <div class="js-work-strip profile--work_container" data-work-id="81344478"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/81344478/Deciphering_the_Essential_Interaction_between_Primase_and_Helicase_in_Mycobacterium_tuberculosis"><img alt="Research paper thumbnail of Deciphering the Essential Interaction between Primase and Helicase in Mycobacterium tuberculosis" class="work-thumbnail" src="https://attachments.academia-assets.com/87420189/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/81344478/Deciphering_the_Essential_Interaction_between_Primase_and_Helicase_in_Mycobacterium_tuberculosis">Deciphering the Essential Interaction between Primase and Helicase in Mycobacterium tuberculosis</a></div><div class="wp-workCard_item"><span>Biophysical Journal</span><span>, 2019</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="3c84c8d13866021ca2655c95649a2992" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":87420189,"asset_id":81344478,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/87420189/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="81344478"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="81344478"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 81344478; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=81344478]").text(description); $(".js-view-count[data-work-id=81344478]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 81344478; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='81344478']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span></div><div id="work-strip-premium-row-container"></div></div></div><script> require.config({ waitSeconds: 90 })(["https://a.academia-assets.com/assets/wow_profile-a9bf3a2bc8c89fa2a77156577594264ee8a0f214d74241bc0fcd3f69f8d107ac.js","https://a.academia-assets.com/assets/work_edit-ad038b8c047c1a8d4fa01b402d530ff93c45fee2137a149a4a5398bc8ad67560.js"], function() { // from javascript_helper.rb var dispatcherData = {} if (true){ window.WowProfile.dispatcher = window.WowProfile.dispatcher || _.clone(Backbone.Events); 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$(this).data('initialized', true); } }); $a.trackClickSource(".js-work-strip-work-link", "profile_work_strip") }); </script> </div><div class="profile--tab_content_container js-tab-pane tab-pane" data-section-id="8970861" id="researcharticles"><div class="js-work-strip profile--work_container" data-work-id="2316028"><div class="profile--work_thumbnail hidden-xs"><a class="js-work-strip-work-link" data-click-track="profile-work-strip-thumbnail" href="https://www.academia.edu/2316028/Virtual_Screening_Identification_and_in_vitro_Testing_of_Novel_Inhibitors_of_O_Acetyl_L_Serine_Sulfhydrylase_of_Entamoeba_histolytica"><img alt="Research paper thumbnail of Virtual Screening, Identification and in vitro Testing of Novel Inhibitors of O-Acetyl-L-Serine Sulfhydrylase of Entamoeba histolytica" class="work-thumbnail" src="https://attachments.academia-assets.com/60200869/thumbnails/1.jpg" /></a></div><div class="wp-workCard wp-workCard_itemContainer"><div class="wp-workCard_item wp-workCard--title"><a class="js-work-strip-work-link text-gray-darker" data-click-track="profile-work-strip-title" href="https://www.academia.edu/2316028/Virtual_Screening_Identification_and_in_vitro_Testing_of_Novel_Inhibitors_of_O_Acetyl_L_Serine_Sulfhydrylase_of_Entamoeba_histolytica">Virtual Screening, Identification and in vitro Testing of Novel Inhibitors of O-Acetyl-L-Serine Sulfhydrylase of Entamoeba histolytica</a></div><div class="wp-workCard_item wp-workCard--coauthors"><span>by </span><span><a class="" data-click-track="profile-work-strip-authors" href="https://hsph-harvard.academia.edu/IshaNagpal">Isha Nagpal</a> and <a class="" data-click-track="profile-work-strip-authors" href="https://jawaharlalanehrunewdelhiindia.academia.edu/SamudralaGourinath">Samudrala Gourinath</a></span></div><div class="wp-workCard_item"><span>PLoS one</span><span>, 2012</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The explosive epidemicity of amoebiasis caused by the facultative gastrointestinal protozoan para...</span><a class="js-work-more-abstract" data-broccoli-component="work_strip.more_abstract" data-click-track="profile-work-strip-more-abstract" href="javascript:;"><span> more </span><span><i class="fa fa-caret-down"></i></span></a><span class="js-work-more-abstract-untruncated hidden">The explosive epidemicity of amoebiasis caused by the facultative gastrointestinal protozoan parasite Entamoeba histolytica is a major public health problem in developing countries. Multidrug resistance and side effects of various available antiamoebic drugs necessitate the design of novel antiamobeic agents. The cysteine biosynthetic pathway is the critical target for drug design due to its significance in the growth, survival and other cellular activities of E. histolytica. Here, we have screened 0.15 million natural compounds from the ZINC database against the active site of the EhOASS enzyme (PDB ID. 3BM5, 2PQM), whose structure we previously determined to 2.4 Å and 1.86 Å resolution. For this purpose, the incremental construction algorithm of GLIDE and the genetic algorithm of GOLD were used. We analyzed docking results for top ranking compounds using a consensus scoring function of X-Score to calculate the binding affinity and using ligplot to measure protein-ligand interactions. Fifteen compounds that possess good inhibitory activity against EhOASS active site were identified that may act as potential high affinity inhibitors. In vitro screening of a few commercially available compounds established their biological activity. The first ranked compound ZINC08931589 had a binding affinity of ~8.05 µM and inhibited about 73% activity at 0.1 mM concentration, indicating good correlation between in silico prediction and in vitro inhibition studies. This compound is thus a good starting point for further development of strong inhibitors.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="e6d32f3b5b36dc29cdb98fdd6a1f8a5f" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":60200869,"asset_id":2316028,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/60200869/download_file?s=profile"><span><i class="fa fa-arrow-down"></i></span><span>Download</span></a><span class="wp-workCard--action visible-if-viewed-by-owner inline-block" style="display: none;"><span class="js-profile-work-strip-edit-button-wrapper profile-work-strip-edit-button-wrapper" data-work-id="2316028"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="2316028"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 2316028; 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