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GalNAc-transferase (GalNAc-T) isoforms modify distinct subsets of the O-glycoproteome and GalNAc-type O-glycosylation is found on most proteins trafficking through the secretory pathway in metazoan cells. The O-glycoproteome is regulated by up to 20 polypeptide GalNAc-Ts and the contributions and bi...
ORGANISM(S): Homo sapiens 
Deconstruction of O-glycosylation – Polypeptide GalNAc-T Isoforms Direct Distinct Subsets of the O-Glycoproteome
The UDP-N-acetylgalactosamine polypeptide:N-acetylgalactosaminyltransferase (GalNAc-T) family of enzymes initiates O-linked glycosylation by catalyzing the addition of the first GalNAc sugar to serine or threonine on proteins destined to be membrane-bound or secreted. Defects in individual isoforms ...
ORGANISM(S): Mus musculus (Mouse) 
2025-05-07 | PXD052978 | Pride
Mucin-type-O-glycosylation on proteins is integrally involved in human health and disease and is coordinated by an enzyme family of 20 N-acetylgalactosaminyltransferases (GalNAc-Ts). Detailed knowledge on the biological effects of site-specific O-glycosylation is limited due to lack of information o...
ORGANISM(S): Homo sapiens (Human) 
2022-10-22 | PXD036791 | Pride
TEO-GalNAc is a chemoenzymatic strategy for tag-free enrichment and quantitative mapping of Tn/T O-GalNAc glycopeptides. Ketone-modified CMP-Sia is transferred by ST6GalNAc1 for selective tagging, followed by reversible oxime capture using hydroxylamine beads. Mild acid release enables tag-free reco...
ORGANISM(S): Homo Sapiens 
2026-03-04 | PXD075239 |
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