{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Kang T"],"funding":["National Cancer Institute","NCI NIH HHS","NIH"],"pagination":["100744"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11046030"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["4(4)"],"pubmed_abstract":["A comprehensive analysis of site-specific protein O-glycosylation is hindered by the absence of a consensus O-glycosylation motif, the diversity of O-glycan structures, and the lack of a universal enzyme that cleaves attached O-glycans. Here, we report the development of a robust O-glycoproteomic workflow for analyzing complex biological samples by combining four different strategies: removal of N-glycans, complementary digestion using O-glycoprotease (IMPa) with/without another protease, glycopeptide enrichment, and mass spectrometry with fragmentation of glycopeptides using stepped collision energy. Using this workflow, we cataloged 474 O-glycopeptides on 189 O-glycosites derived from 79 O-glycoproteins from human plasma. These data revealed O-glycosylation of several abundant proteins t"],"journal":["Cell reports methods"],"pubmed_title":["Global O-glycoproteome enrichment and analysis enabled by a combinatorial enzymatic workflow."],"pmcid":["PMC11046030"],"funding_grant_id":["U01 CA271410","P30CA15083","U01CA271410"],"pubmed_authors":["Garapati K","Joshi N","Kang T","Budhraja R","Kim J","Pandey A"],"additional_accession":[]},"is_claimable":false,"name":"Global O-glycoproteome enrichment and analysis enabled by a combinatorial enzymatic workflow.","description":"A comprehensive analysis of site-specific protein O-glycosylation is hindered by the absence of a consensus O-glycosylation motif, the diversity of O-glycan structures, and the lack of a universal enzyme that cleaves attached O-glycans. Here, we report the development of a robust O-glycoproteomic workflow for analyzing complex biological samples by combining four different strategies: removal of N-glycans, complementary digestion using O-glycoprotease (IMPa) with/without another protease, glycopeptide enrichment, and mass spectrometry with fragmentation of glycopeptides using stepped collision energy. Using this workflow, we cataloged 474 O-glycopeptides on 189 O-glycosites derived from 79 O-glycoproteins from human plasma. These data revealed O-glycosylation of several abundant proteins t","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Apr","modification":"2026-06-01T19:57:45.149Z","creation":"2026-05-20T03:07:43.565Z"},"accession":"S-EPMC11046030","cross_references":{"pubmed":["38582075"],"doi":["10.1016/j.crmeth.2024.100744"]}}