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We report a LC-MS/MS O-glycoproteomics strategy using Data Independent Acquisition (DIA) mode that holds the potential for enabling direct analysis of O-glycoproteins with characterization of sites and structures of O-glycans on a proteome-wide scale with quantification of stoichiometries. To explor...
ORGANISM(S): Homo sapiens (Human) 
2019-11-19 | PXD011063 | Pride
Post-translational modifications (PTMs) on proteins often function to regulate signaling cascades, with the activation of T cells during an adaptive immune response being a classic example. Mounting evidence indicates that the modification of proteins by O-linked Nacetylglucosamine (O-GlcNAc), the o...
ORGANISM(S): Homo sapiens (Human) 
2018-01-25 | PXD004559 | Pride
Protein O-linked mannose (O-Man) glycosylation is an evolutionary conserved post-translational modification, whose biosynthesis is initiated by three non-redundant enzyme families, POMT1/POMT2, TMTC1-4 and TMEM260. In this study, we applied a targeted workflow for membrane glycoproteomics to five hu...
ORGANISM(S): Homo sapiens (Human) 
2024-06-10 | PXD045597 | Pride
Clinical O-glycoproteomics for the development of diagnostic marker for colorectal cancer based on changes in O-glycosylation of serum protein.
ORGANISM(S): Homo Sapiens (human) 
Clinical O-glycoproteomics for the development of diagnostic marker for colorectal cancer based on changes in O-glycosylation of serum protein.
ORGANISM(S): Homo Sapiens (human) 
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