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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="documents-container backbone-social-profile-documents" style="width: 100%;"><div class="u-taCenter"></div><div class="profile--tab_content_container js-tab-pane tab-pane active" id="all"><div class="profile--tab_heading_container js-section-heading" data-section="Papers" id="Papers"><h3 class="profile--tab_heading_container">Papers by Nazneen Dewji</h3></div><div class="js-work-strip profile--work_container" data-work-id="84234644"><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/84234644/Processing_of_Alzheimers_Disease_Associated_3_Amyloid_Precursor_Protein"><img alt="Research paper thumbnail of Processing of Alzheimer's Disease-Associated (3-Amyloid Precursor Protein" 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/84234644/Processing_of_Alzheimers_Disease_Associated_3_Amyloid_Precursor_Protein">Processing of Alzheimer's Disease-Associated (3-Amyloid Precursor Protein</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="84234644"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span 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this, workJSON: {"id":84234644,"title":"Processing of Alzheimer's Disease-Associated (3-Amyloid Precursor 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Dewji","url":"https://independent.academia.edu/NazneenDewji"},"attachments":[],"research_interests":[],"urls":[{"id":22676867,"url":"http://rd.springer.com/content/pdf/10.1007%2FBF02896922.pdf"}]}, 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="84234643"><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/84234643/RESEARCH_ARTICLE_Peptides_of_Presenilin_1_Bind_the_Amyloid_Precursor_Protein_Ectodomain_and_Offer_a_Novel_and_Specific_Therapeutic_Approach_to_Reduce_%C3%9F_Amyloid_in_Alzheimer_s_Disease"><img alt="Research paper thumbnail of RESEARCH ARTICLE Peptides of Presenilin-1 Bind the Amyloid Precursor Protein Ectodomain and Offer a Novel and Specific Therapeutic Approach to Reduce ß-Amyloid in Alzheimer’s Disease" 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/84234643/RESEARCH_ARTICLE_Peptides_of_Presenilin_1_Bind_the_Amyloid_Precursor_Protein_Ectodomain_and_Offer_a_Novel_and_Specific_Therapeutic_Approach_to_Reduce_%C3%9F_Amyloid_in_Alzheimer_s_Disease">RESEARCH ARTICLE Peptides of Presenilin-1 Bind the Amyloid Precursor Protein Ectodomain and Offer a Novel and Specific Therapeutic Approach to Reduce ß-Amyloid in Alzheimer’s Disease</a></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">β-Amyloid (Aβ) accumulation in the brain is widely accepted to be critical to the develop-ment of...</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">β-Amyloid (Aβ) accumulation in the brain is widely accepted to be critical to the develop-ment of Alzheimer’s disease (AD). Current efforts at reducing toxic Aβ40 or 42 have largely focused on modulating γ-secretase activity to produce shorter, less toxic Aβ, while attempt-ing to spare other secretase functions. In this paper we provide data that offer the potential for a new approach for the treatment of AD. The method is based on our previous findings that the production of Aβ from the interaction between the β-amyloid precursor protein (APP) and Presenilin (PS), as part of the γ-secretase complex, in cell culture is largely inhib-ited if the entire water-soluble NH2-terminal domain of PS is first added to the culture. Here we demonstrate that two small, non-overlapping water-soluble peptides from the PS-1 NH2-terminal domain can substantially and specifically inhibit the production of total Aβ as well as Aβ40 and 42 in vitro and in vivo in the brains of APP transgenic mice. These...</span></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="84234643"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234643"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234643; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234643]").text(description); $(".js-view-count[data-work-id=84234643]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234643; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234643']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234643, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=84234643]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234643,"title":"RESEARCH ARTICLE Peptides of Presenilin-1 Bind the Amyloid Precursor Protein Ectodomain and Offer a Novel and Specific Therapeutic Approach to Reduce ß-Amyloid in Alzheimer’s Disease","translated_title":"","metadata":{"abstract":"β-Amyloid (Aβ) accumulation in the brain is widely accepted to be critical to the develop-ment of Alzheimer’s disease (AD). Current efforts at reducing toxic Aβ40 or 42 have largely focused on modulating γ-secretase activity to produce shorter, less toxic Aβ, while attempt-ing to spare other secretase functions. In this paper we provide data that offer the potential for a new approach for the treatment of AD. The method is based on our previous findings that the production of Aβ from the interaction between the β-amyloid precursor protein (APP) and Presenilin (PS), as part of the γ-secretase complex, in cell culture is largely inhib-ited if the entire water-soluble NH2-terminal domain of PS is first added to the culture. Here we demonstrate that two small, non-overlapping water-soluble peptides from the PS-1 NH2-terminal domain can substantially and specifically inhibit the production of total Aβ as well as Aβ40 and 42 in vitro and in vivo in the brains of APP transgenic mice. These...","publication_date":{"day":null,"month":null,"year":2016,"errors":{}}},"translated_abstract":"β-Amyloid (Aβ) accumulation in the brain is widely accepted to be critical to the develop-ment of Alzheimer’s disease (AD). Current efforts at reducing toxic Aβ40 or 42 have largely focused on modulating γ-secretase activity to produce shorter, less toxic Aβ, while attempt-ing to spare other secretase functions. In this paper we provide data that offer the potential for a new approach for the treatment of AD. The method is based on our previous findings that the production of Aβ from the interaction between the β-amyloid precursor protein (APP) and Presenilin (PS), as part of the γ-secretase complex, in cell culture is largely inhib-ited if the entire water-soluble NH2-terminal domain of PS is first added to the culture. 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These...","internal_url":"https://www.academia.edu/84234643/RESEARCH_ARTICLE_Peptides_of_Presenilin_1_Bind_the_Amyloid_Precursor_Protein_Ectodomain_and_Offer_a_Novel_and_Specific_Therapeutic_Approach_to_Reduce_%C3%9F_Amyloid_in_Alzheimer_s_Disease","translated_internal_url":"","created_at":"2022-08-06T09:58:01.186-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":35510034,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"RESEARCH_ARTICLE_Peptides_of_Presenilin_1_Bind_the_Amyloid_Precursor_Protein_Ectodomain_and_Offer_a_Novel_and_Specific_Therapeutic_Approach_to_Reduce_ß_Amyloid_in_Alzheimer_s_Disease","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":35510034,"first_name":"Nazneen","middle_initials":null,"last_name":"Dewji","page_name":"NazneenDewji","domain_name":"independent","created_at":"2015-10-01T16:17:17.806-07:00","display_name":"Nazneen Dewji","url":"https://independent.academia.edu/NazneenDewji"},"attachments":[],"research_interests":[],"urls":[{"id":22676866,"url":"http://citeseerx.ist.psu.edu/viewdoc/download?doi=10.1.1.778.7024\u0026rep=rep1\u0026type=pdf"}]}, 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="84234641"><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/84234641/A_direct_role_for_protein_kinase_C_and_the_transcription_factor_Jun_AP_1_in_the_regulation_of_the_Alzheimers_beta_amyloid_precursor_protein_gene"><img alt="Research paper thumbnail of A direct role for protein kinase C and the transcription factor Jun/AP-1 in the regulation of the Alzheimer's beta-amyloid precursor protein gene" class="work-thumbnail" src="https://attachments.academia-assets.com/89328846/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/84234641/A_direct_role_for_protein_kinase_C_and_the_transcription_factor_Jun_AP_1_in_the_regulation_of_the_Alzheimers_beta_amyloid_precursor_protein_gene">A direct role for protein kinase C and the transcription factor Jun/AP-1 in the regulation of the Alzheimer's beta-amyloid precursor protein gene</a></div><div class="wp-workCard_item"><span>Journal of Biological Chemistry</span><span>, 1994</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="1b61d4e7a439f6056e7bdc1693d44ec0" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" 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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/84234639/Coding_of_Two_Sphingolipid_Activator_Proteins_SAP_1_and_SAP_2_by_Same_Genetic_Locus">Coding of Two Sphingolipid Activator Proteins (SAP-1 and SAP-2) by Same Genetic Locus</a></div><div class="wp-workCard_item"><span>Science</span><span>, 1988</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isola...</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">Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies. The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA). The coding sequence for mature SAP-2 was located 3&amp;#39; to that coding for SAP-1 in the SAP precursor cDNA. Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10. Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein. Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues. Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges. Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.</span></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="84234639"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234639"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234639; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234639]").text(description); $(".js-view-count[data-work-id=84234639]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234639; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234639']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234639, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=84234639]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234639,"title":"Coding of Two Sphingolipid Activator Proteins (SAP-1 and SAP-2) by Same Genetic Locus","translated_title":"","metadata":{"abstract":"Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies. The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA). The coding sequence for mature SAP-2 was located 3\u0026amp;#39; to that coding for SAP-1 in the SAP precursor cDNA. Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10. Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein. Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues. Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges. Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.","publisher":"American Association for the Advancement of Science (AAAS)","publication_date":{"day":null,"month":null,"year":1988,"errors":{}},"publication_name":"Science"},"translated_abstract":"Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies. The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA). The coding sequence for mature SAP-2 was located 3\u0026amp;#39; to that coding for SAP-1 in the SAP precursor cDNA. Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10. Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein. Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues. Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges. Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.","internal_url":"https://www.academia.edu/84234639/Coding_of_Two_Sphingolipid_Activator_Proteins_SAP_1_and_SAP_2_by_Same_Genetic_Locus","translated_internal_url":"","created_at":"2022-08-06T09:58:00.594-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":35510034,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Coding_of_Two_Sphingolipid_Activator_Proteins_SAP_1_and_SAP_2_by_Same_Genetic_Locus","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":35510034,"first_name":"Nazneen","middle_initials":null,"last_name":"Dewji","page_name":"NazneenDewji","domain_name":"independent","created_at":"2015-10-01T16:17:17.806-07:00","display_name":"Nazneen Dewji","url":"https://independent.academia.edu/NazneenDewji"},"attachments":[],"research_interests":[{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics"},{"id":6779,"name":"Science","url":"https://www.academia.edu/Documents/in/Science"},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary"},{"id":48057,"name":"DNA","url":"https://www.academia.edu/Documents/in/DNA"},{"id":64568,"name":"Humans","url":"https://www.academia.edu/Documents/in/Humans"},{"id":84760,"name":"Mice","url":"https://www.academia.edu/Documents/in/Mice"},{"id":99234,"name":"Animals","url":"https://www.academia.edu/Documents/in/Animals"},{"id":103360,"name":"Nucleic acid hybridization","url":"https://www.academia.edu/Documents/in/Nucleic_acid_hybridization"},{"id":111545,"name":"Male","url":"https://www.academia.edu/Documents/in/Male"},{"id":111972,"name":"Hepatocellular Carcinoma","url":"https://www.academia.edu/Documents/in/Hepatocellular_Carcinoma"},{"id":191439,"name":"Glycoproteins","url":"https://www.academia.edu/Documents/in/Glycoproteins"},{"id":375054,"name":"Rats","url":"https://www.academia.edu/Documents/in/Rats"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation"},{"id":809881,"name":"Amino Acid Sequence","url":"https://www.academia.edu/Documents/in/Amino_Acid_Sequence"},{"id":809882,"name":"Base Sequence","url":"https://www.academia.edu/Documents/in/Base_Sequence"},{"id":2467566,"name":"Molecular Sequence Data","url":"https://www.academia.edu/Documents/in/Molecular_Sequence_Data"},{"id":2950651,"name":"Tissue distribution","url":"https://www.academia.edu/Documents/in/Tissue_distribution"},{"id":3562342,"name":"Liver neoplasms","url":"https://www.academia.edu/Documents/in/Liver_neoplasms"}],"urls":[{"id":22676862,"url":"https://syndication.highwire.org/content/doi/10.1126/science.2842863"}]}, 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="84234638"><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/84234638/On_the_spurious_endoproteolytic_processing_of_the_presenilin_proteins_in_cultured_cells_and_tissues"><img alt="Research paper thumbnail of On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissues" class="work-thumbnail" src="https://attachments.academia-assets.com/89328842/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/84234638/On_the_spurious_endoproteolytic_processing_of_the_presenilin_proteins_in_cultured_cells_and_tissues">On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissues</a></div><div class="wp-workCard_item"><span>Proceedings of the National Academy of Sciences</span><span>, 1997</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">It has been widely reported that the presenilin proteins PS-1 and PS-2 in extracts derived from a...</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">It has been widely reported that the presenilin proteins PS-1 and PS-2 in extracts derived from a variety of cultured cells and from tissues are fragmented extensively by endoproteolytic processing events. It generally has been presumed that this endoproteolysis is a physiologically normal intracellular event following presenilin expression, which might play an important role in the still unknown functions of these molecules in connection with Alzheimer disease. We demonstrate herein, however, that, if a variety of cultured cells and several mouse tissues are examined under conditions minimizing cell trauma, the presenilin molecules in the extracts are found to be intact but that, if the cells and tissues are prepared under somewhat more stressful conditions, the endoproteolytic fragments are then observed. We conclude that these particular endoproteolytic events are not the result of physiologically normal processing of the presenilins but are rather artifacts occurring during the ...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="86bf5cbe109bb2732142e7b6249f2267" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":89328842,"asset_id":84234638,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/89328842/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="84234638"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234638"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234638; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234638]").text(description); $(".js-view-count[data-work-id=84234638]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234638; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234638']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234638, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "86bf5cbe109bb2732142e7b6249f2267" } } $('.js-work-strip[data-work-id=84234638]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234638,"title":"On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissues","translated_title":"","metadata":{"abstract":"It has been widely reported that the presenilin proteins PS-1 and PS-2 in extracts derived from a variety of cultured cells and from tissues are fragmented extensively by endoproteolytic processing events. It generally has been presumed that this endoproteolysis is a physiologically normal intracellular event following presenilin expression, which might play an important role in the still unknown functions of these molecules in connection with Alzheimer disease. We demonstrate herein, however, that, if a variety of cultured cells and several mouse tissues are examined under conditions minimizing cell trauma, the presenilin molecules in the extracts are found to be intact but that, if the cells and tissues are prepared under somewhat more stressful conditions, the endoproteolytic fragments are then observed. We conclude that these particular endoproteolytic events are not the result of physiologically normal processing of the presenilins but are rather artifacts occurring during the ...","publisher":"Proceedings of the National Academy of Sciences","publication_date":{"day":null,"month":null,"year":1997,"errors":{}},"publication_name":"Proceedings of the National Academy of Sciences"},"translated_abstract":"It has been widely reported that the presenilin proteins PS-1 and PS-2 in extracts derived from a variety of cultured cells and from tissues are fragmented extensively by endoproteolytic processing events. It generally has been presumed that this endoproteolysis is a physiologically normal intracellular event following presenilin expression, which might play an important role in the still unknown functions of these molecules in connection with Alzheimer disease. We demonstrate herein, however, that, if a variety of cultured cells and several mouse tissues are examined under conditions minimizing cell trauma, the presenilin molecules in the extracts are found to be intact but that, if the cells and tissues are prepared under somewhat more stressful conditions, the endoproteolytic fragments are then observed. We conclude that these particular endoproteolytic events are not the result of physiologically normal processing of the presenilins but are rather artifacts occurring during the ...","internal_url":"https://www.academia.edu/84234638/On_the_spurious_endoproteolytic_processing_of_the_presenilin_proteins_in_cultured_cells_and_tissues","translated_internal_url":"","created_at":"2022-08-06T09:58:00.459-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":35510034,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":89328842,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/89328842/thumbnails/1.jpg","file_name":"0bad0b75e6ca521682904528f8b236dba778.pdf","download_url":"https://www.academia.edu/attachments/89328842/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"On_the_spurious_endoproteolytic_processi.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/89328842/0bad0b75e6ca521682904528f8b236dba778-libre.pdf?1659806402=\u0026response-content-disposition=attachment%3B+filename%3DOn_the_spurious_endoproteolytic_processi.pdf\u0026Expires=1732460250\u0026Signature=alYpK-GIprYfvmWQNa5MuR8t86AoNu~Rzv3dKXFy2dNX~fj~ImvnVHTAEQvyFabv86Z5d6rR9k74swrUxVeaier7I~ArBsWG9NPsUguWXfhX3JhlKhZ3uUGNewfE~uTzo41tHbP5E3nLu8Y2vRWSAkbCawSSTZF2-vRM3E06EO74eXqIs2gVkevNKt~3SVorWiP9Eiiqvdo6M-Tf~zcpkqRKLcWar2UH1ckhdw9bidN8n5hdeAydDAB9Xky~0kDb3PZCdFeBCfXtcDZAoku3MdLyy6k2iPibAapJ9G8jnZpSXdVErhfawdqiMtjiJqOc-U55Ro0Y7AGUQN-u2DiwHA__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"On_the_spurious_endoproteolytic_processing_of_the_presenilin_proteins_in_cultured_cells_and_tissues","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":35510034,"first_name":"Nazneen","middle_initials":null,"last_name":"Dewji","page_name":"NazneenDewji","domain_name":"independent","created_at":"2015-10-01T16:17:17.806-07:00","display_name":"Nazneen Dewji","url":"https://independent.academia.edu/NazneenDewji"},"attachments":[{"id":89328842,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/89328842/thumbnails/1.jpg","file_name":"0bad0b75e6ca521682904528f8b236dba778.pdf","download_url":"https://www.academia.edu/attachments/89328842/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"On_the_spurious_endoproteolytic_processi.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/89328842/0bad0b75e6ca521682904528f8b236dba778-libre.pdf?1659806402=\u0026response-content-disposition=attachment%3B+filename%3DOn_the_spurious_endoproteolytic_processi.pdf\u0026Expires=1732460250\u0026Signature=alYpK-GIprYfvmWQNa5MuR8t86AoNu~Rzv3dKXFy2dNX~fj~ImvnVHTAEQvyFabv86Z5d6rR9k74swrUxVeaier7I~ArBsWG9NPsUguWXfhX3JhlKhZ3uUGNewfE~uTzo41tHbP5E3nLu8Y2vRWSAkbCawSSTZF2-vRM3E06EO74eXqIs2gVkevNKt~3SVorWiP9Eiiqvdo6M-Tf~zcpkqRKLcWar2UH1ckhdw9bidN8n5hdeAydDAB9Xky~0kDb3PZCdFeBCfXtcDZAoku3MdLyy6k2iPibAapJ9G8jnZpSXdVErhfawdqiMtjiJqOc-U55Ro0Y7AGUQN-u2DiwHA__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":11298,"name":"Membrane Proteins","url":"https://www.academia.edu/Documents/in/Membrane_Proteins"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary"},{"id":57808,"name":"Cell line","url":"https://www.academia.edu/Documents/in/Cell_line"},{"id":61474,"name":"Brain","url":"https://www.academia.edu/Documents/in/Brain"},{"id":64568,"name":"Humans","url":"https://www.academia.edu/Documents/in/Humans"},{"id":71294,"name":"Kidney","url":"https://www.academia.edu/Documents/in/Kidney"},{"id":71437,"name":"Liver","url":"https://www.academia.edu/Documents/in/Liver"},{"id":84760,"name":"Mice","url":"https://www.academia.edu/Documents/in/Mice"},{"id":99234,"name":"Animals","url":"https://www.academia.edu/Documents/in/Animals"},{"id":452440,"name":"Presenilin-2","url":"https://www.academia.edu/Documents/in/Presenilin-2"},{"id":620070,"name":"Transfection","url":"https://www.academia.edu/Documents/in/Transfection"},{"id":788677,"name":"Rabbits","url":"https://www.academia.edu/Documents/in/Rabbits"},{"id":1120234,"name":"Alzheimer Disease","url":"https://www.academia.edu/Documents/in/Alzheimer_Disease"},{"id":2950651,"name":"Tissue distribution","url":"https://www.academia.edu/Documents/in/Tissue_distribution"}],"urls":[]}, 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="84234637"><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/84234637/The_presenilins_turned_inside_out_Implications_for_their_structures_and_functions"><img alt="Research paper thumbnail of The presenilins turned inside out: Implications for their structures and functions" class="work-thumbnail" src="https://attachments.academia-assets.com/89328841/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/84234637/The_presenilins_turned_inside_out_Implications_for_their_structures_and_functions">The presenilins turned inside out: Implications for their structures and functions</a></div><div class="wp-workCard_item"><span>Proceedings of the National Academy of Sciences</span><span>, 2004</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The presenilin (PS) proteins are polytopic integral membrane proteins that are critically involve...</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 presenilin (PS) proteins are polytopic integral membrane proteins that are critically involved in the development of Alzheimer&#39;s disease. The topography of the PS molecule in the endoplasmic reticulum membrane is widely accepted as exhibiting eight-hydrophobic-transmembrane (8-TM) helices. We have previously provided evidence, however, that the intact PS molecule is also present in the cell surface where it exhibits exclusively a 7-TM topography, which differs in significant structural features from the 8-TM model. This evidence, however, has been disparaged and generally rejected by researchers in Alzheimer&#39;s disease. The 7-TM model is definitively demonstrated in the present study for PS-1 at the surfaces of PS-1-transfected cells and for endogenous PS-1 at the surfaces of untransfected cells, by immunofluorescence studies using mAbs. These studies force substantial revision of current views of the structural and functional properties of the PS proteins.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="bc9204b4a9f4a46c2e24ad76494095af" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":89328841,"asset_id":84234637,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/89328841/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="84234637"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234637"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234637; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234637]").text(description); $(".js-view-count[data-work-id=84234637]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234637; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234637']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234637, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "bc9204b4a9f4a46c2e24ad76494095af" } } $('.js-work-strip[data-work-id=84234637]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234637,"title":"The presenilins turned inside out: Implications for their structures and functions","translated_title":"","metadata":{"abstract":"The presenilin (PS) proteins are polytopic integral membrane proteins that are critically involved in the development of Alzheimer\u0026#39;s disease. The topography of the PS molecule in the endoplasmic reticulum membrane is widely accepted as exhibiting eight-hydrophobic-transmembrane (8-TM) helices. We have previously provided evidence, however, that the intact PS molecule is also present in the cell surface where it exhibits exclusively a 7-TM topography, which differs in significant structural features from the 8-TM model. This evidence, however, has been disparaged and generally rejected by researchers in Alzheimer\u0026#39;s disease. The 7-TM model is definitively demonstrated in the present study for PS-1 at the surfaces of PS-1-transfected cells and for endogenous PS-1 at the surfaces of untransfected cells, by immunofluorescence studies using mAbs. These studies force substantial revision of current views of the structural and functional properties of the PS proteins.","publisher":"Proceedings of the National Academy of Sciences","publication_date":{"day":null,"month":null,"year":2004,"errors":{}},"publication_name":"Proceedings of the National Academy of Sciences"},"translated_abstract":"The presenilin (PS) proteins are polytopic integral membrane proteins that are critically involved in the development of Alzheimer\u0026#39;s disease. The topography of the PS molecule in the endoplasmic reticulum membrane is widely accepted as exhibiting eight-hydrophobic-transmembrane (8-TM) helices. We have previously provided evidence, however, that the intact PS molecule is also present in the cell surface where it exhibits exclusively a 7-TM topography, which differs in significant structural features from the 8-TM model. This evidence, however, has been disparaged and generally rejected by researchers in Alzheimer\u0026#39;s disease. The 7-TM model is definitively demonstrated in the present study for PS-1 at the surfaces of PS-1-transfected cells and for endogenous PS-1 at the surfaces of untransfected cells, by immunofluorescence studies using mAbs. These studies force substantial revision of current views of the structural and functional properties of the PS proteins.","internal_url":"https://www.academia.edu/84234637/The_presenilins_turned_inside_out_Implications_for_their_structures_and_functions","translated_internal_url":"","created_at":"2022-08-06T09:58:00.226-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":35510034,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":89328841,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/89328841/thumbnails/1.jpg","file_name":"1057.full.pdf","download_url":"https://www.academia.edu/attachments/89328841/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"The_presenilins_turned_inside_out_Implic.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/89328841/1057.full-libre.pdf?1659806399=\u0026response-content-disposition=attachment%3B+filename%3DThe_presenilins_turned_inside_out_Implic.pdf\u0026Expires=1732460250\u0026Signature=fwKzLEN~qj~WMx7nfOHhTLJjVBZ~VM3fTUXkY3RGFQoeBymRNSmG55~en7ju9l~Z6cw634clZNbMTAW6k~znU67ivoqMcd7nTiQER6AsslChjbP1y0wyR8zCEOIeomOPQLhNsGp34asTIGKGtxTEc8tMwLFVAvDxh61eLC8fqSrwXlDHWwBwOqltFBkM5XMppiVPCAEQPrT8viHEDqXiE9Lf5wl1ycGj-NnFVJDkBnnUhDePa9lU7wZySHOtCzTSaQn~lzT~aaArFuFv6T3ywxV3C0nDrowxMdc6RmojqY8Ygf2XqHbVng9IQy122UK1ymf1NZnlwEowMl9Ra4g14Q__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"The_presenilins_turned_inside_out_Implications_for_their_structures_and_functions","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":35510034,"first_name":"Nazneen","middle_initials":null,"last_name":"Dewji","page_name":"NazneenDewji","domain_name":"independent","created_at":"2015-10-01T16:17:17.806-07:00","display_name":"Nazneen Dewji","url":"https://independent.academia.edu/NazneenDewji"},"attachments":[{"id":89328841,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/89328841/thumbnails/1.jpg","file_name":"1057.full.pdf","download_url":"https://www.academia.edu/attachments/89328841/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"The_presenilins_turned_inside_out_Implic.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/89328841/1057.full-libre.pdf?1659806399=\u0026response-content-disposition=attachment%3B+filename%3DThe_presenilins_turned_inside_out_Implic.pdf\u0026Expires=1732460250\u0026Signature=fwKzLEN~qj~WMx7nfOHhTLJjVBZ~VM3fTUXkY3RGFQoeBymRNSmG55~en7ju9l~Z6cw634clZNbMTAW6k~znU67ivoqMcd7nTiQER6AsslChjbP1y0wyR8zCEOIeomOPQLhNsGp34asTIGKGtxTEc8tMwLFVAvDxh61eLC8fqSrwXlDHWwBwOqltFBkM5XMppiVPCAEQPrT8viHEDqXiE9Lf5wl1ycGj-NnFVJDkBnnUhDePa9lU7wZySHOtCzTSaQn~lzT~aaArFuFv6T3ywxV3C0nDrowxMdc6RmojqY8Ygf2XqHbVng9IQy122UK1ymf1NZnlwEowMl9Ra4g14Q__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":11298,"name":"Membrane Proteins","url":"https://www.academia.edu/Documents/in/Membrane_Proteins"},{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary"},{"id":49646,"name":"Protein Structure and Function","url":"https://www.academia.edu/Documents/in/Protein_Structure_and_Function"},{"id":122187,"name":"Endoplasmic Reticulum","url":"https://www.academia.edu/Documents/in/Endoplasmic_Reticulum"},{"id":323597,"name":"Fluorescent Antibody Technique","url":"https://www.academia.edu/Documents/in/Fluorescent_Antibody_Technique"},{"id":452440,"name":"Presenilin-2","url":"https://www.academia.edu/Documents/in/Presenilin-2"},{"id":620070,"name":"Transfection","url":"https://www.academia.edu/Documents/in/Transfection"},{"id":900881,"name":"Membrane Protein","url":"https://www.academia.edu/Documents/in/Membrane_Protein"},{"id":967839,"name":"Structure activity Relationship","url":"https://www.academia.edu/Documents/in/Structure_activity_Relationship"},{"id":1078292,"name":"Cell Surface Markers","url":"https://www.academia.edu/Documents/in/Cell_Surface_Markers"}],"urls":[{"id":22676861,"url":"https://pnas.org/doi/pdf/10.1073/pnas.0307290101"}]}, 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="84234636"><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/84234636/Cell_surface_expression_of_the_Alzheimer_disease_related_presenilin_proteins"><img alt="Research paper thumbnail of Cell surface expression of the Alzheimer disease-related presenilin proteins" class="work-thumbnail" src="https://attachments.academia-assets.com/89328845/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/84234636/Cell_surface_expression_of_the_Alzheimer_disease_related_presenilin_proteins">Cell surface expression of the Alzheimer disease-related presenilin proteins</a></div><div class="wp-workCard_item"><span>Proceedings of the National Academy of Sciences</span><span>, 1997</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The presenilin proteins PS-1 and PS-2 are crucially involved in Alzheimer disease (AD), but their...</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 presenilin proteins PS-1 and PS-2 are crucially involved in Alzheimer disease (AD), but their molecular functions are not known. They are integral membrane proteins, but whether they can be expressed at the surface of cells has been in dispute. Here we show by immunofluorescence experiments, using anti-peptide antibodies specific for either PS-1 or PS-2, that live cultured DAMI cells and differentiated human NT2N neuronal cells are specifically immunolabeled for their endogenous as well as transfected presenilins, although the cells cannot be immunolabeled for their intracellular tubulin, unless they are first fixed and permeabilized. These and other results establish that portions of the presenilins are indeed expressed at the surfaces of these cells. These findings support our previous proposal that the presenilins on the surface of a cell engage in intercellular interactions with the β-amyloid precursor protein on the surface of a neighboring cell, as a critical step in the m...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="9ce7ccf3bae9c4c14d0e42d8d57efd6a" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":89328845,"asset_id":84234636,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/89328845/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="84234636"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234636"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234636; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234636]").text(description); $(".js-view-count[data-work-id=84234636]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234636; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234636']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234636, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "9ce7ccf3bae9c4c14d0e42d8d57efd6a" } } $('.js-work-strip[data-work-id=84234636]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234636,"title":"Cell surface expression of the Alzheimer disease-related presenilin proteins","translated_title":"","metadata":{"abstract":"The presenilin proteins PS-1 and PS-2 are crucially involved in Alzheimer disease (AD), but their molecular functions are not known. They are integral membrane proteins, but whether they can be expressed at the surface of cells has been in dispute. Here we show by immunofluorescence experiments, using anti-peptide antibodies specific for either PS-1 or PS-2, that live cultured DAMI cells and differentiated human NT2N neuronal cells are specifically immunolabeled for their endogenous as well as transfected presenilins, although the cells cannot be immunolabeled for their intracellular tubulin, unless they are first fixed and permeabilized. These and other results establish that portions of the presenilins are indeed expressed at the surfaces of these cells. These findings support our previous proposal that the presenilins on the surface of a cell engage in intercellular interactions with the β-amyloid precursor protein on the surface of a neighboring cell, as a critical step in the m...","publisher":"Proceedings of the National Academy of Sciences","publication_date":{"day":null,"month":null,"year":1997,"errors":{}},"publication_name":"Proceedings of the National Academy of Sciences"},"translated_abstract":"The presenilin proteins PS-1 and PS-2 are crucially involved in Alzheimer disease (AD), but their molecular functions are not known. They are integral membrane proteins, but whether they can be expressed at the surface of cells has been in dispute. Here we show by immunofluorescence experiments, using anti-peptide antibodies specific for either PS-1 or PS-2, that live cultured DAMI cells and differentiated human NT2N neuronal cells are specifically immunolabeled for their endogenous as well as transfected presenilins, although the cells cannot be immunolabeled for their intracellular tubulin, unless they are first fixed and permeabilized. These and other results establish that portions of the presenilins are indeed expressed at the surfaces of these cells. These findings support our previous proposal that the presenilins on the surface of a cell engage in intercellular interactions with the β-amyloid precursor protein on the surface of a neighboring cell, as a critical step in the m...","internal_url":"https://www.academia.edu/84234636/Cell_surface_expression_of_the_Alzheimer_disease_related_presenilin_proteins","translated_internal_url":"","created_at":"2022-08-06T09:58:00.076-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":35510034,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":89328845,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/89328845/thumbnails/1.jpg","file_name":"pmc23298.pdf","download_url":"https://www.academia.edu/attachments/89328845/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Cell_surface_expression_of_the_Alzheimer.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/89328845/pmc23298-libre.pdf?1659806397=\u0026response-content-disposition=attachment%3B+filename%3DCell_surface_expression_of_the_Alzheimer.pdf\u0026Expires=1732460250\u0026Signature=bTlwOUhhW5zXNG85IMavDjB4kb~HnSRhgquw8sfXeeaiDziIXzxUaYjL8j9HS9d4mSEt0M0fpIv8chLk~TbLo~ahOPnnpx5cY-5S7rwCTMvp5JTDgXxWaNo3SkdyQffrHNCrXYMpBRTSvoQxYwwtwbzumhj54pwexcU0n0GBa8ZbEWpTI~ZS3u9GCWk72RuWwJ0tav-YMKWtmR0Ap0U42R4JbsldHLW8tGpefwxV0URTFTicqMRjvIYR7pNp3hduo4V6DoS4hpjE6VD-mlIHJLtrZYlXEDyf5Kol8Hezb3tVqBNFkDa9WqoUhQxZ4zDTu7blSLjYI3BYIGEagnTdwg__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Cell_surface_expression_of_the_Alzheimer_disease_related_presenilin_proteins","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":35510034,"first_name":"Nazneen","middle_initials":null,"last_name":"Dewji","page_name":"NazneenDewji","domain_name":"independent","created_at":"2015-10-01T16:17:17.806-07:00","display_name":"Nazneen Dewji","url":"https://independent.academia.edu/NazneenDewji"},"attachments":[{"id":89328845,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/89328845/thumbnails/1.jpg","file_name":"pmc23298.pdf","download_url":"https://www.academia.edu/attachments/89328845/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Cell_surface_expression_of_the_Alzheimer.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/89328845/pmc23298-libre.pdf?1659806397=\u0026response-content-disposition=attachment%3B+filename%3DCell_surface_expression_of_the_Alzheimer.pdf\u0026Expires=1732460250\u0026Signature=bTlwOUhhW5zXNG85IMavDjB4kb~HnSRhgquw8sfXeeaiDziIXzxUaYjL8j9HS9d4mSEt0M0fpIv8chLk~TbLo~ahOPnnpx5cY-5S7rwCTMvp5JTDgXxWaNo3SkdyQffrHNCrXYMpBRTSvoQxYwwtwbzumhj54pwexcU0n0GBa8ZbEWpTI~ZS3u9GCWk72RuWwJ0tav-YMKWtmR0Ap0U42R4JbsldHLW8tGpefwxV0URTFTicqMRjvIYR7pNp3hduo4V6DoS4hpjE6VD-mlIHJLtrZYlXEDyf5Kol8Hezb3tVqBNFkDa9WqoUhQxZ4zDTu7blSLjYI3BYIGEagnTdwg__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":11298,"name":"Membrane Proteins","url":"https://www.academia.edu/Documents/in/Membrane_Proteins"},{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary"},{"id":51789,"name":"Antibodies","url":"https://www.academia.edu/Documents/in/Antibodies"},{"id":57808,"name":"Cell line","url":"https://www.academia.edu/Documents/in/Cell_line"},{"id":64568,"name":"Humans","url":"https://www.academia.edu/Documents/in/Humans"},{"id":193974,"name":"Neurons","url":"https://www.academia.edu/Documents/in/Neurons"},{"id":452440,"name":"Presenilin-2","url":"https://www.academia.edu/Documents/in/Presenilin-2"},{"id":1120234,"name":"Alzheimer Disease","url":"https://www.academia.edu/Documents/in/Alzheimer_Disease"},{"id":2468093,"name":"Cell Membrane","url":"https://www.academia.edu/Documents/in/Cell_Membrane"}],"urls":[]}, 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="84234635"><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/84234635/Increased_gene_expression_of_Alzheimer_disease_beta_amyloid_precursor_protein_in_senescent_cultured_fibroblasts"><img alt="Research paper thumbnail of Increased gene expression of Alzheimer disease beta-amyloid precursor protein in senescent cultured fibroblasts" class="work-thumbnail" src="https://attachments.academia-assets.com/89328857/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/84234635/Increased_gene_expression_of_Alzheimer_disease_beta_amyloid_precursor_protein_in_senescent_cultured_fibroblasts">Increased gene expression of Alzheimer disease beta-amyloid precursor protein in senescent cultured fibroblasts</a></div><div class="wp-workCard_item"><span>Proceedings of the National Academy of Sciences</span><span>, 1991</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The pathological hallmark of Alzheimer disease is the accumulation of neurofibrillary tangles and...</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 pathological hallmark of Alzheimer disease is the accumulation of neurofibrillary tangles and neuritic plaques in the brains of patients. Plaque cores contain a 4- to 5-kDa amyloid beta-protein fragment which is also found in the cerebral blood vessels of affected individuals. Since amyloid deposition in the brain increases with age even in normal people, we sought to establish whether the disease state bears a direct relationship with normal aging processes. As a model for biological aging, the process of cellular senescence in vitro was used. mRNA levels of beta-amyloid precursor protein associated with Alzheimer disease were compared in human fibroblasts in culture at early passage and when the same fibroblasts were grown to senescence after more than 52 population doublings. A dramatic increase in mRNA was observed in senescent IMR-90 fibroblasts compared with early-passage cells. Hybridization of mRNA from senescent and early proliferating fibroblasts with oligonucleotide p...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="ae0e9938f7f8f4d8694c85679a1f8888" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":89328857,"asset_id":84234635,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/89328857/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="84234635"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234635"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234635; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234635]").text(description); $(".js-view-count[data-work-id=84234635]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234635; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234635']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234635, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "ae0e9938f7f8f4d8694c85679a1f8888" } } $('.js-work-strip[data-work-id=84234635]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234635,"title":"Increased gene expression of Alzheimer disease beta-amyloid precursor protein in senescent cultured fibroblasts","translated_title":"","metadata":{"abstract":"The pathological hallmark of Alzheimer disease is the accumulation of neurofibrillary tangles and neuritic plaques in the brains of patients. Plaque cores contain a 4- to 5-kDa amyloid beta-protein fragment which is also found in the cerebral blood vessels of affected individuals. Since amyloid deposition in the brain increases with age even in normal people, we sought to establish whether the disease state bears a direct relationship with normal aging processes. As a model for biological aging, the process of cellular senescence in vitro was used. mRNA levels of beta-amyloid precursor protein associated with Alzheimer disease were compared in human fibroblasts in culture at early passage and when the same fibroblasts were grown to senescence after more than 52 population doublings. A dramatic increase in mRNA was observed in senescent IMR-90 fibroblasts compared with early-passage cells. Hybridization of mRNA from senescent and early proliferating fibroblasts with oligonucleotide p...","publisher":"Proceedings of the National Academy of Sciences","publication_date":{"day":null,"month":null,"year":1991,"errors":{}},"publication_name":"Proceedings of the National Academy of Sciences"},"translated_abstract":"The pathological hallmark of Alzheimer disease is the accumulation of neurofibrillary tangles and neuritic plaques in the brains of patients. Plaque cores contain a 4- to 5-kDa amyloid beta-protein fragment which is also found in the cerebral blood vessels of affected individuals. Since amyloid deposition in the brain increases with age even in normal people, we sought to establish whether the disease state bears a direct relationship with normal aging processes. As a model for biological aging, the process of cellular senescence in vitro was used. mRNA levels of beta-amyloid precursor protein associated with Alzheimer disease were compared in human fibroblasts in culture at early passage and when the same fibroblasts were grown to senescence after more than 52 population doublings. A dramatic increase in mRNA was observed in senescent IMR-90 fibroblasts compared with early-passage cells. Hybridization of mRNA from senescent and early proliferating fibroblasts with oligonucleotide 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data-work-id="84234632"><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/84234632/Purification_and_characterization_of_an_N_acetylglucosaminidase_produced_by_a_Trichoderma_harzianum_strain_which_controls_Crinipellis_perniciosa"><img alt="Research paper thumbnail of Purification and characterization of an N -acetylglucosaminidase produced by a Trichoderma harzianum strain which controls Crinipellis perniciosa" class="work-thumbnail" src="https://attachments.academia-assets.com/89328794/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" 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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/84234572/Lysosomal_storage_of_subunit_c_of_mitochondrial_ATP_synthase_in_Battens_disease_ceroid_lipofuscinosis_">Lysosomal storage of subunit c of mitochondrial ATP synthase in Batten's disease (ceroid-lipofuscinosis)</a></div><div class="wp-workCard_item"><span>Biochemical Journal</span><span>, 1991</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Immunochemical studies demonstrate that subunit c of mitochondrial ATP synthase is stored in the ...</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">Immunochemical studies demonstrate that subunit c of mitochondrial ATP synthase is stored in the late-infantile, juvenile and adult forms of Batten&#39;s disease. It does not accumulate in the infantile form, or in other conditions involving lysosomal hypertrophy. These results suggest that the defective metabolism of subunit c is central to the pathogenesis of these three forms of Batten&#39;s disease.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="e71da228833148dfa7921ed4d64d5b50" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":89328797,"asset_id":84234572,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/89328797/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="84234572"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234572"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234572; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234572]").text(description); $(".js-view-count[data-work-id=84234572]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234572; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234572']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234572, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "e71da228833148dfa7921ed4d64d5b50" } } $('.js-work-strip[data-work-id=84234572]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234572,"title":"Lysosomal storage of subunit c of mitochondrial ATP synthase in Batten's disease (ceroid-lipofuscinosis)","translated_title":"","metadata":{"abstract":"Immunochemical studies demonstrate that subunit c of mitochondrial ATP synthase is stored in the late-infantile, juvenile and adult forms of Batten\u0026#39;s disease. 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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="55932677"><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/55932677/Pharmacokinetics_in_Rat_of_P8_a_Peptide_Drug_Candidate_for_the_Treatment_of_Alzheimers_Disease_Stability_and_Delivery_to_the_Brain"><img alt="Research paper thumbnail of Pharmacokinetics in Rat of P8, a Peptide Drug Candidate for the Treatment of Alzheimer's Disease: Stability and Delivery to the Brain" class="work-thumbnail" src="https://attachments.academia-assets.com/71567557/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/55932677/Pharmacokinetics_in_Rat_of_P8_a_Peptide_Drug_Candidate_for_the_Treatment_of_Alzheimers_Disease_Stability_and_Delivery_to_the_Brain">Pharmacokinetics in Rat of P8, a Peptide Drug Candidate for the Treatment of Alzheimer's Disease: Stability and Delivery to the Brain</a></div><div class="wp-workCard_item"><span>Journal of Alzheimer's disease reports</span><span>, Jan 24, 2018</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Strategies to achieve a therapy for Alzheimer&#39;s disease (AD) aimed at reducing the effects of...</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">Strategies to achieve a therapy for Alzheimer&#39;s disease (AD) aimed at reducing the effects of amyloid-β (Aβ) have largely involved inhibiting or modifying the activities of the β- or -secretases or by the use of monoclonal antibodies (MAb). We previously offered the potential for a new, early and effective approach for the treatment of AD by a strategy that does not target the secretases. We showed that a family of peptides containing the DEEEDEEL sequence and another independent peptide, all derived from the amino terminus of PS-1, are each capable of markedly reducing the production of Aβ and in mThy1-hAPP transgenic mice. These peptides gave a strong and specific binding with the ectodomain of amyloid-β protein precursor (AβPP) and did not affect the catalytic activities of β- or -secretase, or the level of AβPP. Critical to the development of any therapeutic for AD is the requirement that it is stable and can be delivered to the brain. We report here data on the metabolic st...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="a0efeef7b37b658ea184ac9c67628fba" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":71567557,"asset_id":55932677,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/71567557/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="55932677"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="55932677"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 55932677; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=55932677]").text(description); $(".js-view-count[data-work-id=55932677]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 55932677; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='55932677']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 55932677, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "a0efeef7b37b658ea184ac9c67628fba" } } $('.js-work-strip[data-work-id=55932677]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":55932677,"title":"Pharmacokinetics in Rat of P8, a Peptide Drug Candidate for the Treatment of Alzheimer's Disease: Stability and Delivery to the Brain","translated_title":"","metadata":{"abstract":"Strategies to achieve a therapy for Alzheimer\u0026#39;s disease (AD) aimed at reducing the effects of amyloid-β (Aβ) have largely involved inhibiting or modifying the activities of the β- or -secretases or by the use of monoclonal antibodies (MAb). We previously offered the potential for a new, early and effective approach for the treatment of AD by a strategy that does not target the secretases. We showed that a family of peptides containing the DEEEDEEL sequence and another independent peptide, all derived from the amino terminus of PS-1, are each capable of markedly reducing the production of Aβ and in mThy1-hAPP transgenic mice. These peptides gave a strong and specific binding with the ectodomain of amyloid-β protein precursor (AβPP) and did not affect the catalytic activities of β- or -secretase, or the level of AβPP. Critical to the development of any therapeutic for AD is the requirement that it is stable and can be delivered to the brain. 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These peptides gave a strong and specific binding with the ectodomain of amyloid-β protein precursor (AβPP) and did not affect the catalytic activities of β- or -secretase, or the level of AβPP. Critical to the development of any therapeutic for AD is the requirement that it is stable and can be delivered to the brain. 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Current efforts at reducing toxic Aβ40 or 42 have largely focused on modulating γ-secretase activity to produce shorter, less toxic Aβ, while attempt-ing to spare other secretase functions. In this paper we provide data that offer the potential for a new approach for the treatment of AD. The method is based on our previous findings that the production of Aβ from the interaction between the β-amyloid precursor protein (APP) and Presenilin (PS), as part of the γ-secretase complex, in cell culture is largely inhib-ited if the entire water-soluble NH2-terminal domain of PS is first added to the culture. Here we demonstrate that two small, non-overlapping water-soluble peptides from the PS-1 NH2-terminal domain can substantially and specifically inhibit the production of total Aβ as well as Aβ40 and 42 in vitro and in vivo in the brains of APP transgenic mice. 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These...","publication_date":{"day":null,"month":null,"year":2016,"errors":{}}},"translated_abstract":"β-Amyloid (Aβ) accumulation in the brain is widely accepted to be critical to the develop-ment of Alzheimer’s disease (AD). Current efforts at reducing toxic Aβ40 or 42 have largely focused on modulating γ-secretase activity to produce shorter, less toxic Aβ, while attempt-ing to spare other secretase functions. In this paper we provide data that offer the potential for a new approach for the treatment of AD. The method is based on our previous findings that the production of Aβ from the interaction between the β-amyloid precursor protein (APP) and Presenilin (PS), as part of the γ-secretase complex, in cell culture is largely inhib-ited if the entire water-soluble NH2-terminal domain of PS is first added to the culture. 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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/84234639/Coding_of_Two_Sphingolipid_Activator_Proteins_SAP_1_and_SAP_2_by_Same_Genetic_Locus">Coding of Two Sphingolipid Activator Proteins (SAP-1 and SAP-2) by Same Genetic Locus</a></div><div class="wp-workCard_item"><span>Science</span><span>, 1988</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isola...</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">Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies. The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA). The coding sequence for mature SAP-2 was located 3&amp;#39; to that coding for SAP-1 in the SAP precursor cDNA. Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10. Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein. Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues. Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges. Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.</span></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="84234639"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234639"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234639; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234639]").text(description); $(".js-view-count[data-work-id=84234639]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234639; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234639']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234639, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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" } } $('.js-work-strip[data-work-id=84234639]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234639,"title":"Coding of Two Sphingolipid Activator Proteins (SAP-1 and SAP-2) by Same Genetic Locus","translated_title":"","metadata":{"abstract":"Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies. The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA). The coding sequence for mature SAP-2 was located 3\u0026amp;#39; to that coding for SAP-1 in the SAP precursor cDNA. Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10. Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein. Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues. Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges. Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.","publisher":"American Association for the Advancement of Science (AAAS)","publication_date":{"day":null,"month":null,"year":1988,"errors":{}},"publication_name":"Science"},"translated_abstract":"Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies. The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA). The coding sequence for mature SAP-2 was located 3\u0026amp;#39; to that coding for SAP-1 in the SAP precursor cDNA. Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10. Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein. Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues. Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges. Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.","internal_url":"https://www.academia.edu/84234639/Coding_of_Two_Sphingolipid_Activator_Proteins_SAP_1_and_SAP_2_by_Same_Genetic_Locus","translated_internal_url":"","created_at":"2022-08-06T09:58:00.594-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":35510034,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[],"slug":"Coding_of_Two_Sphingolipid_Activator_Proteins_SAP_1_and_SAP_2_by_Same_Genetic_Locus","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":35510034,"first_name":"Nazneen","middle_initials":null,"last_name":"Dewji","page_name":"NazneenDewji","domain_name":"independent","created_at":"2015-10-01T16:17:17.806-07:00","display_name":"Nazneen Dewji","url":"https://independent.academia.edu/NazneenDewji"},"attachments":[],"research_interests":[{"id":156,"name":"Genetics","url":"https://www.academia.edu/Documents/in/Genetics"},{"id":6779,"name":"Science","url":"https://www.academia.edu/Documents/in/Science"},{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary"},{"id":48057,"name":"DNA","url":"https://www.academia.edu/Documents/in/DNA"},{"id":64568,"name":"Humans","url":"https://www.academia.edu/Documents/in/Humans"},{"id":84760,"name":"Mice","url":"https://www.academia.edu/Documents/in/Mice"},{"id":99234,"name":"Animals","url":"https://www.academia.edu/Documents/in/Animals"},{"id":103360,"name":"Nucleic acid hybridization","url":"https://www.academia.edu/Documents/in/Nucleic_acid_hybridization"},{"id":111545,"name":"Male","url":"https://www.academia.edu/Documents/in/Male"},{"id":111972,"name":"Hepatocellular Carcinoma","url":"https://www.academia.edu/Documents/in/Hepatocellular_Carcinoma"},{"id":191439,"name":"Glycoproteins","url":"https://www.academia.edu/Documents/in/Glycoproteins"},{"id":375054,"name":"Rats","url":"https://www.academia.edu/Documents/in/Rats"},{"id":653665,"name":"Protein Conformation","url":"https://www.academia.edu/Documents/in/Protein_Conformation"},{"id":809881,"name":"Amino Acid Sequence","url":"https://www.academia.edu/Documents/in/Amino_Acid_Sequence"},{"id":809882,"name":"Base Sequence","url":"https://www.academia.edu/Documents/in/Base_Sequence"},{"id":2467566,"name":"Molecular Sequence Data","url":"https://www.academia.edu/Documents/in/Molecular_Sequence_Data"},{"id":2950651,"name":"Tissue distribution","url":"https://www.academia.edu/Documents/in/Tissue_distribution"},{"id":3562342,"name":"Liver neoplasms","url":"https://www.academia.edu/Documents/in/Liver_neoplasms"}],"urls":[{"id":22676862,"url":"https://syndication.highwire.org/content/doi/10.1126/science.2842863"}]}, 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="84234638"><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/84234638/On_the_spurious_endoproteolytic_processing_of_the_presenilin_proteins_in_cultured_cells_and_tissues"><img alt="Research paper thumbnail of On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissues" class="work-thumbnail" src="https://attachments.academia-assets.com/89328842/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/84234638/On_the_spurious_endoproteolytic_processing_of_the_presenilin_proteins_in_cultured_cells_and_tissues">On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissues</a></div><div class="wp-workCard_item"><span>Proceedings of the National Academy of Sciences</span><span>, 1997</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">It has been widely reported that the presenilin proteins PS-1 and PS-2 in extracts derived from a...</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">It has been widely reported that the presenilin proteins PS-1 and PS-2 in extracts derived from a variety of cultured cells and from tissues are fragmented extensively by endoproteolytic processing events. It generally has been presumed that this endoproteolysis is a physiologically normal intracellular event following presenilin expression, which might play an important role in the still unknown functions of these molecules in connection with Alzheimer disease. We demonstrate herein, however, that, if a variety of cultured cells and several mouse tissues are examined under conditions minimizing cell trauma, the presenilin molecules in the extracts are found to be intact but that, if the cells and tissues are prepared under somewhat more stressful conditions, the endoproteolytic fragments are then observed. We conclude that these particular endoproteolytic events are not the result of physiologically normal processing of the presenilins but are rather artifacts occurring during the ...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="86bf5cbe109bb2732142e7b6249f2267" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":89328842,"asset_id":84234638,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/89328842/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="84234638"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234638"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234638; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234638]").text(description); $(".js-view-count[data-work-id=84234638]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234638; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234638']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234638, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "86bf5cbe109bb2732142e7b6249f2267" } } $('.js-work-strip[data-work-id=84234638]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234638,"title":"On the spurious endoproteolytic processing of the presenilin proteins in cultured cells and tissues","translated_title":"","metadata":{"abstract":"It has been widely reported that the presenilin proteins PS-1 and PS-2 in extracts derived from a variety of cultured cells and from tissues are fragmented extensively by endoproteolytic processing events. It generally has been presumed that this endoproteolysis is a physiologically normal intracellular event following presenilin expression, which might play an important role in the still unknown functions of these molecules in connection with Alzheimer disease. We demonstrate herein, however, that, if a variety of cultured cells and several mouse tissues are examined under conditions minimizing cell trauma, the presenilin molecules in the extracts are found to be intact but that, if the cells and tissues are prepared under somewhat more stressful conditions, the endoproteolytic fragments are then observed. We conclude that these particular endoproteolytic events are not the result of physiologically normal processing of the presenilins but are rather artifacts occurring during the ...","publisher":"Proceedings of the National Academy of Sciences","publication_date":{"day":null,"month":null,"year":1997,"errors":{}},"publication_name":"Proceedings of the National Academy of Sciences"},"translated_abstract":"It has been widely reported that the presenilin proteins PS-1 and PS-2 in extracts derived from a variety of cultured cells and from tissues are fragmented extensively by endoproteolytic processing events. It generally has been presumed that this endoproteolysis is a physiologically normal intracellular event following presenilin expression, which might play an important role in the still unknown functions of these molecules in connection with Alzheimer disease. We demonstrate herein, however, that, if a variety of cultured cells and several mouse tissues are examined under conditions minimizing cell trauma, the presenilin molecules in the extracts are found to be intact but that, if the cells and tissues are prepared under somewhat more stressful conditions, the endoproteolytic fragments are then observed. We conclude that these particular endoproteolytic events are not the result of physiologically normal processing of the presenilins but are rather artifacts occurring during the ...","internal_url":"https://www.academia.edu/84234638/On_the_spurious_endoproteolytic_processing_of_the_presenilin_proteins_in_cultured_cells_and_tissues","translated_internal_url":"","created_at":"2022-08-06T09:58:00.459-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":35510034,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":89328842,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/89328842/thumbnails/1.jpg","file_name":"0bad0b75e6ca521682904528f8b236dba778.pdf","download_url":"https://www.academia.edu/attachments/89328842/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"On_the_spurious_endoproteolytic_processi.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/89328842/0bad0b75e6ca521682904528f8b236dba778-libre.pdf?1659806402=\u0026response-content-disposition=attachment%3B+filename%3DOn_the_spurious_endoproteolytic_processi.pdf\u0026Expires=1732460250\u0026Signature=alYpK-GIprYfvmWQNa5MuR8t86AoNu~Rzv3dKXFy2dNX~fj~ImvnVHTAEQvyFabv86Z5d6rR9k74swrUxVeaier7I~ArBsWG9NPsUguWXfhX3JhlKhZ3uUGNewfE~uTzo41tHbP5E3nLu8Y2vRWSAkbCawSSTZF2-vRM3E06EO74eXqIs2gVkevNKt~3SVorWiP9Eiiqvdo6M-Tf~zcpkqRKLcWar2UH1ckhdw9bidN8n5hdeAydDAB9Xky~0kDb3PZCdFeBCfXtcDZAoku3MdLyy6k2iPibAapJ9G8jnZpSXdVErhfawdqiMtjiJqOc-U55Ro0Y7AGUQN-u2DiwHA__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"On_the_spurious_endoproteolytic_processing_of_the_presenilin_proteins_in_cultured_cells_and_tissues","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":35510034,"first_name":"Nazneen","middle_initials":null,"last_name":"Dewji","page_name":"NazneenDewji","domain_name":"independent","created_at":"2015-10-01T16:17:17.806-07:00","display_name":"Nazneen Dewji","url":"https://independent.academia.edu/NazneenDewji"},"attachments":[{"id":89328842,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/89328842/thumbnails/1.jpg","file_name":"0bad0b75e6ca521682904528f8b236dba778.pdf","download_url":"https://www.academia.edu/attachments/89328842/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"On_the_spurious_endoproteolytic_processi.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/89328842/0bad0b75e6ca521682904528f8b236dba778-libre.pdf?1659806402=\u0026response-content-disposition=attachment%3B+filename%3DOn_the_spurious_endoproteolytic_processi.pdf\u0026Expires=1732460250\u0026Signature=alYpK-GIprYfvmWQNa5MuR8t86AoNu~Rzv3dKXFy2dNX~fj~ImvnVHTAEQvyFabv86Z5d6rR9k74swrUxVeaier7I~ArBsWG9NPsUguWXfhX3JhlKhZ3uUGNewfE~uTzo41tHbP5E3nLu8Y2vRWSAkbCawSSTZF2-vRM3E06EO74eXqIs2gVkevNKt~3SVorWiP9Eiiqvdo6M-Tf~zcpkqRKLcWar2UH1ckhdw9bidN8n5hdeAydDAB9Xky~0kDb3PZCdFeBCfXtcDZAoku3MdLyy6k2iPibAapJ9G8jnZpSXdVErhfawdqiMtjiJqOc-U55Ro0Y7AGUQN-u2DiwHA__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":7710,"name":"Biology","url":"https://www.academia.edu/Documents/in/Biology"},{"id":11298,"name":"Membrane Proteins","url":"https://www.academia.edu/Documents/in/Membrane_Proteins"},{"id":26327,"name":"Medicine","url":"https://www.academia.edu/Documents/in/Medicine"},{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary"},{"id":57808,"name":"Cell line","url":"https://www.academia.edu/Documents/in/Cell_line"},{"id":61474,"name":"Brain","url":"https://www.academia.edu/Documents/in/Brain"},{"id":64568,"name":"Humans","url":"https://www.academia.edu/Documents/in/Humans"},{"id":71294,"name":"Kidney","url":"https://www.academia.edu/Documents/in/Kidney"},{"id":71437,"name":"Liver","url":"https://www.academia.edu/Documents/in/Liver"},{"id":84760,"name":"Mice","url":"https://www.academia.edu/Documents/in/Mice"},{"id":99234,"name":"Animals","url":"https://www.academia.edu/Documents/in/Animals"},{"id":452440,"name":"Presenilin-2","url":"https://www.academia.edu/Documents/in/Presenilin-2"},{"id":620070,"name":"Transfection","url":"https://www.academia.edu/Documents/in/Transfection"},{"id":788677,"name":"Rabbits","url":"https://www.academia.edu/Documents/in/Rabbits"},{"id":1120234,"name":"Alzheimer Disease","url":"https://www.academia.edu/Documents/in/Alzheimer_Disease"},{"id":2950651,"name":"Tissue distribution","url":"https://www.academia.edu/Documents/in/Tissue_distribution"}],"urls":[]}, 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="84234637"><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/84234637/The_presenilins_turned_inside_out_Implications_for_their_structures_and_functions"><img alt="Research paper thumbnail of The presenilins turned inside out: Implications for their structures and functions" class="work-thumbnail" src="https://attachments.academia-assets.com/89328841/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/84234637/The_presenilins_turned_inside_out_Implications_for_their_structures_and_functions">The presenilins turned inside out: Implications for their structures and functions</a></div><div class="wp-workCard_item"><span>Proceedings of the National Academy of Sciences</span><span>, 2004</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The presenilin (PS) proteins are polytopic integral membrane proteins that are critically involve...</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 presenilin (PS) proteins are polytopic integral membrane proteins that are critically involved in the development of Alzheimer&#39;s disease. The topography of the PS molecule in the endoplasmic reticulum membrane is widely accepted as exhibiting eight-hydrophobic-transmembrane (8-TM) helices. We have previously provided evidence, however, that the intact PS molecule is also present in the cell surface where it exhibits exclusively a 7-TM topography, which differs in significant structural features from the 8-TM model. This evidence, however, has been disparaged and generally rejected by researchers in Alzheimer&#39;s disease. The 7-TM model is definitively demonstrated in the present study for PS-1 at the surfaces of PS-1-transfected cells and for endogenous PS-1 at the surfaces of untransfected cells, by immunofluorescence studies using mAbs. These studies force substantial revision of current views of the structural and functional properties of the PS proteins.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="bc9204b4a9f4a46c2e24ad76494095af" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":89328841,"asset_id":84234637,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/89328841/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="84234637"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234637"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234637; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234637]").text(description); $(".js-view-count[data-work-id=84234637]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234637; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234637']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234637, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "bc9204b4a9f4a46c2e24ad76494095af" } } $('.js-work-strip[data-work-id=84234637]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234637,"title":"The presenilins turned inside out: Implications for their structures and functions","translated_title":"","metadata":{"abstract":"The presenilin (PS) proteins are polytopic integral membrane proteins that are critically involved in the development of Alzheimer\u0026#39;s disease. 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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="84234636"><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/84234636/Cell_surface_expression_of_the_Alzheimer_disease_related_presenilin_proteins"><img alt="Research paper thumbnail of Cell surface expression of the Alzheimer disease-related presenilin proteins" class="work-thumbnail" src="https://attachments.academia-assets.com/89328845/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/84234636/Cell_surface_expression_of_the_Alzheimer_disease_related_presenilin_proteins">Cell surface expression of the Alzheimer disease-related presenilin proteins</a></div><div class="wp-workCard_item"><span>Proceedings of the National Academy of Sciences</span><span>, 1997</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The presenilin proteins PS-1 and PS-2 are crucially involved in Alzheimer disease (AD), but their...</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 presenilin proteins PS-1 and PS-2 are crucially involved in Alzheimer disease (AD), but their molecular functions are not known. They are integral membrane proteins, but whether they can be expressed at the surface of cells has been in dispute. Here we show by immunofluorescence experiments, using anti-peptide antibodies specific for either PS-1 or PS-2, that live cultured DAMI cells and differentiated human NT2N neuronal cells are specifically immunolabeled for their endogenous as well as transfected presenilins, although the cells cannot be immunolabeled for their intracellular tubulin, unless they are first fixed and permeabilized. These and other results establish that portions of the presenilins are indeed expressed at the surfaces of these cells. These findings support our previous proposal that the presenilins on the surface of a cell engage in intercellular interactions with the β-amyloid precursor protein on the surface of a neighboring cell, as a critical step in the m...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="9ce7ccf3bae9c4c14d0e42d8d57efd6a" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":89328845,"asset_id":84234636,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/89328845/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="84234636"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234636"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234636; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234636]").text(description); $(".js-view-count[data-work-id=84234636]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234636; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234636']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234636, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "9ce7ccf3bae9c4c14d0e42d8d57efd6a" } } $('.js-work-strip[data-work-id=84234636]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234636,"title":"Cell surface expression of the Alzheimer disease-related presenilin proteins","translated_title":"","metadata":{"abstract":"The presenilin proteins PS-1 and PS-2 are crucially involved in Alzheimer disease (AD), but their molecular functions are not known. 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Here we show by immunofluorescence experiments, using anti-peptide antibodies specific for either PS-1 or PS-2, that live cultured DAMI cells and differentiated human NT2N neuronal cells are specifically immunolabeled for their endogenous as well as transfected presenilins, although the cells cannot be immunolabeled for their intracellular tubulin, unless they are first fixed and permeabilized. These and other results establish that portions of the presenilins are indeed expressed at the surfaces of these cells. These findings support our previous proposal that the presenilins on the surface of a cell engage in intercellular interactions with the β-amyloid precursor protein on the surface of a neighboring cell, as a critical step in the m...","internal_url":"https://www.academia.edu/84234636/Cell_surface_expression_of_the_Alzheimer_disease_related_presenilin_proteins","translated_internal_url":"","created_at":"2022-08-06T09:58:00.076-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":35510034,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":89328845,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/89328845/thumbnails/1.jpg","file_name":"pmc23298.pdf","download_url":"https://www.academia.edu/attachments/89328845/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Cell_surface_expression_of_the_Alzheimer.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/89328845/pmc23298-libre.pdf?1659806397=\u0026response-content-disposition=attachment%3B+filename%3DCell_surface_expression_of_the_Alzheimer.pdf\u0026Expires=1732460250\u0026Signature=bTlwOUhhW5zXNG85IMavDjB4kb~HnSRhgquw8sfXeeaiDziIXzxUaYjL8j9HS9d4mSEt0M0fpIv8chLk~TbLo~ahOPnnpx5cY-5S7rwCTMvp5JTDgXxWaNo3SkdyQffrHNCrXYMpBRTSvoQxYwwtwbzumhj54pwexcU0n0GBa8ZbEWpTI~ZS3u9GCWk72RuWwJ0tav-YMKWtmR0Ap0U42R4JbsldHLW8tGpefwxV0URTFTicqMRjvIYR7pNp3hduo4V6DoS4hpjE6VD-mlIHJLtrZYlXEDyf5Kol8Hezb3tVqBNFkDa9WqoUhQxZ4zDTu7blSLjYI3BYIGEagnTdwg__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Cell_surface_expression_of_the_Alzheimer_disease_related_presenilin_proteins","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":35510034,"first_name":"Nazneen","middle_initials":null,"last_name":"Dewji","page_name":"NazneenDewji","domain_name":"independent","created_at":"2015-10-01T16:17:17.806-07:00","display_name":"Nazneen Dewji","url":"https://independent.academia.edu/NazneenDewji"},"attachments":[{"id":89328845,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/89328845/thumbnails/1.jpg","file_name":"pmc23298.pdf","download_url":"https://www.academia.edu/attachments/89328845/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Cell_surface_expression_of_the_Alzheimer.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/89328845/pmc23298-libre.pdf?1659806397=\u0026response-content-disposition=attachment%3B+filename%3DCell_surface_expression_of_the_Alzheimer.pdf\u0026Expires=1732460250\u0026Signature=bTlwOUhhW5zXNG85IMavDjB4kb~HnSRhgquw8sfXeeaiDziIXzxUaYjL8j9HS9d4mSEt0M0fpIv8chLk~TbLo~ahOPnnpx5cY-5S7rwCTMvp5JTDgXxWaNo3SkdyQffrHNCrXYMpBRTSvoQxYwwtwbzumhj54pwexcU0n0GBa8ZbEWpTI~ZS3u9GCWk72RuWwJ0tav-YMKWtmR0Ap0U42R4JbsldHLW8tGpefwxV0URTFTicqMRjvIYR7pNp3hduo4V6DoS4hpjE6VD-mlIHJLtrZYlXEDyf5Kol8Hezb3tVqBNFkDa9WqoUhQxZ4zDTu7blSLjYI3BYIGEagnTdwg__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"research_interests":[{"id":11298,"name":"Membrane Proteins","url":"https://www.academia.edu/Documents/in/Membrane_Proteins"},{"id":28235,"name":"Multidisciplinary","url":"https://www.academia.edu/Documents/in/Multidisciplinary"},{"id":51789,"name":"Antibodies","url":"https://www.academia.edu/Documents/in/Antibodies"},{"id":57808,"name":"Cell line","url":"https://www.academia.edu/Documents/in/Cell_line"},{"id":64568,"name":"Humans","url":"https://www.academia.edu/Documents/in/Humans"},{"id":193974,"name":"Neurons","url":"https://www.academia.edu/Documents/in/Neurons"},{"id":452440,"name":"Presenilin-2","url":"https://www.academia.edu/Documents/in/Presenilin-2"},{"id":1120234,"name":"Alzheimer Disease","url":"https://www.academia.edu/Documents/in/Alzheimer_Disease"},{"id":2468093,"name":"Cell Membrane","url":"https://www.academia.edu/Documents/in/Cell_Membrane"}],"urls":[]}, 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="84234635"><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/84234635/Increased_gene_expression_of_Alzheimer_disease_beta_amyloid_precursor_protein_in_senescent_cultured_fibroblasts"><img alt="Research paper thumbnail of Increased gene expression of Alzheimer disease beta-amyloid precursor protein in senescent cultured fibroblasts" class="work-thumbnail" src="https://attachments.academia-assets.com/89328857/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/84234635/Increased_gene_expression_of_Alzheimer_disease_beta_amyloid_precursor_protein_in_senescent_cultured_fibroblasts">Increased gene expression of Alzheimer disease beta-amyloid precursor protein in senescent cultured fibroblasts</a></div><div class="wp-workCard_item"><span>Proceedings of the National Academy of Sciences</span><span>, 1991</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">The pathological hallmark of Alzheimer disease is the accumulation of neurofibrillary tangles and...</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 pathological hallmark of Alzheimer disease is the accumulation of neurofibrillary tangles and neuritic plaques in the brains of patients. Plaque cores contain a 4- to 5-kDa amyloid beta-protein fragment which is also found in the cerebral blood vessels of affected individuals. Since amyloid deposition in the brain increases with age even in normal people, we sought to establish whether the disease state bears a direct relationship with normal aging processes. As a model for biological aging, the process of cellular senescence in vitro was used. mRNA levels of beta-amyloid precursor protein associated with Alzheimer disease were compared in human fibroblasts in culture at early passage and when the same fibroblasts were grown to senescence after more than 52 population doublings. A dramatic increase in mRNA was observed in senescent IMR-90 fibroblasts compared with early-passage cells. Hybridization of mRNA from senescent and early proliferating fibroblasts with oligonucleotide p...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="ae0e9938f7f8f4d8694c85679a1f8888" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":89328857,"asset_id":84234635,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/89328857/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="84234635"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234635"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234635; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234635]").text(description); $(".js-view-count[data-work-id=84234635]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234635; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234635']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234635, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "ae0e9938f7f8f4d8694c85679a1f8888" } } $('.js-work-strip[data-work-id=84234635]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234635,"title":"Increased gene expression of Alzheimer disease beta-amyloid precursor protein in senescent cultured fibroblasts","translated_title":"","metadata":{"abstract":"The pathological hallmark of Alzheimer disease is the accumulation of neurofibrillary tangles and neuritic plaques in the brains of patients. Plaque cores contain a 4- to 5-kDa amyloid beta-protein fragment which is also found in the cerebral blood vessels of affected individuals. Since amyloid deposition in the brain increases with age even in normal people, we sought to establish whether the disease state bears a direct relationship with normal aging processes. As a model for biological aging, the process of cellular senescence in vitro was used. mRNA levels of beta-amyloid precursor protein associated with Alzheimer disease were compared in human fibroblasts in culture at early passage and when the same fibroblasts were grown to senescence after more than 52 population doublings. A dramatic increase in mRNA was observed in senescent IMR-90 fibroblasts compared with early-passage cells. Hybridization of mRNA from senescent and early proliferating fibroblasts with oligonucleotide p...","publisher":"Proceedings of the National Academy of Sciences","publication_date":{"day":null,"month":null,"year":1991,"errors":{}},"publication_name":"Proceedings of the National Academy of Sciences"},"translated_abstract":"The pathological hallmark of Alzheimer disease is the accumulation of neurofibrillary tangles and neuritic plaques in the brains of patients. Plaque cores contain a 4- to 5-kDa amyloid beta-protein fragment which is also found in the cerebral blood vessels of affected individuals. Since amyloid deposition in the brain increases with age even in normal people, we sought to establish whether the disease state bears a direct relationship with normal aging processes. As a model for biological aging, the process of cellular senescence in vitro was used. mRNA levels of beta-amyloid precursor protein associated with Alzheimer disease were compared in human fibroblasts in culture at early passage and when the same fibroblasts were grown to senescence after more than 52 population doublings. A dramatic increase in mRNA was observed in senescent IMR-90 fibroblasts compared with early-passage cells. Hybridization of mRNA from senescent and early proliferating fibroblasts with oligonucleotide p...","internal_url":"https://www.academia.edu/84234635/Increased_gene_expression_of_Alzheimer_disease_beta_amyloid_precursor_protein_in_senescent_cultured_fibroblasts","translated_internal_url":"","created_at":"2022-08-06T09:57:59.889-07:00","preview_url":null,"current_user_can_edit":null,"current_user_is_owner":null,"owner_id":35510034,"coauthors_can_edit":true,"document_type":"paper","co_author_tags":[],"downloadable_attachments":[{"id":89328857,"title":"","file_type":"pdf","scribd_thumbnail_url":"https://attachments.academia-assets.com/89328857/thumbnails/1.jpg","file_name":"16.full.pdf","download_url":"https://www.academia.edu/attachments/89328857/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&","bulk_download_file_name":"Increased_gene_expression_of_Alzheimer_d.pdf","bulk_download_url":"https://d1wqtxts1xzle7.cloudfront.net/89328857/16.full-libre.pdf?1659806398=\u0026response-content-disposition=attachment%3B+filename%3DIncreased_gene_expression_of_Alzheimer_d.pdf\u0026Expires=1732460250\u0026Signature=A5AC~2BNmrcOSpaWLaymvCaHy5Ks7kHvotyyRxRr3EZx95YznpoY53gSBUcpxxmzrYJflgzESdY2gyRmeCeMuxyXVly311Z2HgL~x6iDCpvcdwBH4y2TywUely5zV~fbvqwpv5iO606GLdDa5bVjG-Ble1~wIDV486~EMot9uuY42y9WqnFxMppKEeplkmVvDi4wBK6x2~Gq~gTnjVZm9ERGvMrGUskD-H8fyLZw1yXPR9zhcD7XIr9bU7Rn-ufDCjGoGoepJUtC~lU6KRXcRdQj2xE6uFZn2e4m2qeNCWA~tQJzTnA7QJIZNAP-MgAaN12tsO6hnabez-JVnGr~lQ__\u0026Key-Pair-Id=APKAJLOHF5GGSLRBV4ZA"}],"slug":"Increased_gene_expression_of_Alzheimer_disease_beta_amyloid_precursor_protein_in_senescent_cultured_fibroblasts","translated_slug":"","page_count":null,"language":"en","content_type":"Work","owner":{"id":35510034,"first_name":"Nazneen","middle_initials":null,"last_name":"Dewji","page_name":"NazneenDewji","domain_name":"independent","created_at":"2015-10-01T16:17:17.806-07:00","display_name":"Nazneen 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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="84234634"><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/84234634/Heat_shock_factor_1_mediates_the_transcriptional_activation_of_Alzheimers_%CE%B2_amyloid_precursor_protein_gene_in_response_to_stress"><img alt="Research paper thumbnail of Heat shock factor-1 mediates the transcriptional activation of Alzheimer's β-amyloid precursor protein gene in response to stress" class="work-thumbnail" src="https://attachments.academia-assets.com/89328840/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" 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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/84234572/Lysosomal_storage_of_subunit_c_of_mitochondrial_ATP_synthase_in_Battens_disease_ceroid_lipofuscinosis_">Lysosomal storage of subunit c of mitochondrial ATP synthase in Batten's disease (ceroid-lipofuscinosis)</a></div><div class="wp-workCard_item"><span>Biochemical Journal</span><span>, 1991</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Immunochemical studies demonstrate that subunit c of mitochondrial ATP synthase is stored in the ...</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">Immunochemical studies demonstrate that subunit c of mitochondrial ATP synthase is stored in the late-infantile, juvenile and adult forms of Batten&#39;s disease. It does not accumulate in the infantile form, or in other conditions involving lysosomal hypertrophy. These results suggest that the defective metabolism of subunit c is central to the pathogenesis of these three forms of Batten&#39;s disease.</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="e71da228833148dfa7921ed4d64d5b50" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":89328797,"asset_id":84234572,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/89328797/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="84234572"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="84234572"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 84234572; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=84234572]").text(description); $(".js-view-count[data-work-id=84234572]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 84234572; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='84234572']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 84234572, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "e71da228833148dfa7921ed4d64d5b50" } } $('.js-work-strip[data-work-id=84234572]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":84234572,"title":"Lysosomal storage of subunit c of mitochondrial ATP synthase in Batten's disease (ceroid-lipofuscinosis)","translated_title":"","metadata":{"abstract":"Immunochemical studies demonstrate that subunit c of mitochondrial ATP synthase is stored in the late-infantile, juvenile and adult forms of Batten\u0026#39;s disease. 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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="55932677"><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/55932677/Pharmacokinetics_in_Rat_of_P8_a_Peptide_Drug_Candidate_for_the_Treatment_of_Alzheimers_Disease_Stability_and_Delivery_to_the_Brain"><img alt="Research paper thumbnail of Pharmacokinetics in Rat of P8, a Peptide Drug Candidate for the Treatment of Alzheimer's Disease: Stability and Delivery to the Brain" class="work-thumbnail" src="https://attachments.academia-assets.com/71567557/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/55932677/Pharmacokinetics_in_Rat_of_P8_a_Peptide_Drug_Candidate_for_the_Treatment_of_Alzheimers_Disease_Stability_and_Delivery_to_the_Brain">Pharmacokinetics in Rat of P8, a Peptide Drug Candidate for the Treatment of Alzheimer's Disease: Stability and Delivery to the Brain</a></div><div class="wp-workCard_item"><span>Journal of Alzheimer's disease reports</span><span>, Jan 24, 2018</span></div><div class="wp-workCard_item"><span class="js-work-more-abstract-truncated">Strategies to achieve a therapy for Alzheimer&#39;s disease (AD) aimed at reducing the effects of...</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">Strategies to achieve a therapy for Alzheimer&#39;s disease (AD) aimed at reducing the effects of amyloid-β (Aβ) have largely involved inhibiting or modifying the activities of the β- or -secretases or by the use of monoclonal antibodies (MAb). We previously offered the potential for a new, early and effective approach for the treatment of AD by a strategy that does not target the secretases. We showed that a family of peptides containing the DEEEDEEL sequence and another independent peptide, all derived from the amino terminus of PS-1, are each capable of markedly reducing the production of Aβ and in mThy1-hAPP transgenic mice. These peptides gave a strong and specific binding with the ectodomain of amyloid-β protein precursor (AβPP) and did not affect the catalytic activities of β- or -secretase, or the level of AβPP. Critical to the development of any therapeutic for AD is the requirement that it is stable and can be delivered to the brain. We report here data on the metabolic st...</span></div><div class="wp-workCard_item wp-workCard--actions"><span class="work-strip-bookmark-button-container"></span><a id="a0efeef7b37b658ea184ac9c67628fba" class="wp-workCard--action" rel="nofollow" data-click-track="profile-work-strip-download" data-download="{"attachment_id":71567557,"asset_id":55932677,"asset_type":"Work","button_location":"profile"}" href="https://www.academia.edu/attachments/71567557/download_file?st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&st=MTczMjQ1NjY1MCw4LjIyMi4yMDguMTQ2&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="55932677"><a class="js-profile-work-strip-edit-button" tabindex="0"><span><i class="fa fa-pencil"></i></span><span>Edit</span></a></span></span><span id="work-strip-rankings-button-container"></span></div><div class="wp-workCard_item wp-workCard--stats"><span><span><span class="js-view-count view-count u-mr2x" data-work-id="55932677"><i class="fa fa-spinner fa-spin"></i></span><script>$(function () { var workId = 55932677; window.Academia.workViewCountsFetcher.queue(workId, function (count) { var description = window.$h.commaizeInt(count) + " " + window.$h.pluralize(count, 'View'); $(".js-view-count[data-work-id=55932677]").text(description); $(".js-view-count[data-work-id=55932677]").attr('title', description).tooltip(); }); });</script></span></span><span><span class="percentile-widget hidden"><span class="u-mr2x work-percentile"></span></span><script>$(function () { var workId = 55932677; window.Academia.workPercentilesFetcher.queue(workId, function (percentileText) { var container = $(".js-work-strip[data-work-id='55932677']"); container.find('.work-percentile').text(percentileText.charAt(0).toUpperCase() + percentileText.slice(1)); container.find('.percentile-widget').show(); container.find('.percentile-widget').removeClass('hidden'); }); });</script></span><span><script>$(function() { new Works.PaperRankView({ workId: 55932677, container: "", }); });</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-f77ea15d77ce96025a6048a514272ad8becbad23c641fc2b3bd6e24ca6ff1932.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: "a0efeef7b37b658ea184ac9c67628fba" } } $('.js-work-strip[data-work-id=55932677]').each(function() { if (!$(this).data('initialized')) { new WowProfile.WorkStripView({ el: this, workJSON: {"id":55932677,"title":"Pharmacokinetics in Rat of P8, a Peptide Drug Candidate for the Treatment of Alzheimer's Disease: Stability and Delivery to the Brain","translated_title":"","metadata":{"abstract":"Strategies to achieve a therapy for Alzheimer\u0026#39;s disease (AD) aimed at reducing the effects of amyloid-β (Aβ) have largely involved inhibiting or modifying the activities of the β- or -secretases or by the use of monoclonal antibodies (MAb). 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