<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>6(5)</volume><submitter>Shatnyeva OM</submitter><pubmed_abstract>Protein modifications of death receptor pathways play a central role in the regulation of apoptosis. It has been demonstrated that O-glycosylation of TRAIL-receptor (R) is essential for sensitivity and resistance towards TRAIL-mediated apoptosis. In this study we ask whether and how glycosylation of CD95 (Fas/APO-1), another death receptor, influences DISC formation and procaspase-8 activation at the CD95 DISC and thereby the onset of apoptosis. We concentrated on N-glycostructure since O-glycosylation of CD95 was not found. We applied different approaches to analyze the role of CD95 N-glycosylation on the signal transduction: in silico modeling of CD95 DISC, generation of CD95 glycosylation mutants (at N136 and N118), modulation of N-glycosylation by deoxymannojirimycin (DMM) and sialidas</pubmed_abstract><journal>PloS one</journal><pagination>e19927</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3097226</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation.</pubmed_title><pmcid>PMC3097226</pmcid><pubmed_authors>Schwartz-Albiez R</pubmed_authors><pubmed_authors>Lavrik IN</pubmed_authors><pubmed_authors>Pappa A</pubmed_authors><pubmed_authors>Weber AN</pubmed_authors><pubmed_authors>Weber CE</pubmed_authors><pubmed_authors>Krammer PH</pubmed_authors><pubmed_authors>Kubarenko AV</pubmed_authors><pubmed_authors>Shatnyeva OM</pubmed_authors></additional><is_claimable>false</is_claimable><name>Modulation of the CD95-induced apoptosis: the role of CD95 N-glycosylation.</name><description>Protein modifications of death receptor pathways play a central role in the regulation of apoptosis. It has been demonstrated that O-glycosylation of TRAIL-receptor (R) is essential for sensitivity and resistance towards TRAIL-mediated apoptosis. In this study we ask whether and how glycosylation of CD95 (Fas/APO-1), another death receptor, influences DISC formation and procaspase-8 activation at the CD95 DISC and thereby the onset of apoptosis. We concentrated on N-glycostructure since O-glycosylation of CD95 was not found. We applied different approaches to analyze the role of CD95 N-glycosylation on the signal transduction: in silico modeling of CD95 DISC, generation of CD95 glycosylation mutants (at N136 and N118), modulation of N-glycosylation by deoxymannojirimycin (DMM) and sialidas</description><dates><release>2011-01-01T00:00:00Z</release><publication>2011</publication><modification>2026-04-07T14:27:33.382Z</modification><creation>2019-03-26T23:13:27Z</creation></dates><accession>S-EPMC3097226</accession><cross_references><pubmed>21625644</pubmed><doi>10.1371/journal.pone.0019927</doi></cross_references></HashMap>