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ProteomicsProbing the contribution of individual polypeptide GalNAc-transferase isoforms to the O-glycoproteome by inducible expression in isogenic cell lines
The GalNAc-type O-glycoproteome is orchestrated by a large family of polypeptide GalNAc-transferase isoenzymes (GalNAc-Ts) with partially overlapping contributions to the O-glycoproteome as well as distinct non-redundant functions. Increasing evidence indicate that individual GalNAc-Ts co-regulate a...
ORGANISM(S): Homo sapiens (Human) 
2018-10-16 | PXD010155 | Pride
Inducible expression Galnac-transferase O-glycosylation Glycoproteomics Mass spectrometry 
TranscriptomicsDeconstruction of O-glycosylation – Polypeptide GalNAc-T Isoforms Direct Distinct Subsets of the O-Glycoproteome
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 
2015-09-30 | E-MTAB-3844 | biostudies-arrayexpress
UnknownConservation of peptide acceptor preferences between Drosophila and mammalian polypeptide-GalNAc transferase ortholog pairs.
Not available
S-EPMC2574660 | biostudies-literature
UnknownEmerging paradigms for the initiation of mucin-type protein O-glycosylation by the polypeptide GalNAc transferase family of glycosyltransferases.
Not available
S-EPMC3077648 | biostudies-literature
UnknownO-glycosylation modulates proprotein convertase activation of angiopoietin-like protein 3: possible role of polypeptide GalNAc-transferase-2 in regulation of concentrations of plasma lipids.
Not available
S-EPMC2978557 | biostudies-literature
UnknownProbing the contribution of individual polypeptide GalNAc-transferase isoforms to the O-glycoproteome by inducible expression in isogenic cell lines.
Not available
S-EPMC6295722 | biostudies-literature
UnknownA computational and experimental study of O-glycosylation. Catalysis by human UDP-GalNAc polypeptide:GalNAc transferase-T2.
Not available
S-EPMC4744471 | biostudies-literature
TranscriptomicsRole of the polypeptide N-acetylgalactosaminyltransferase 3 in ovarian cancer progression: possible implications in abnormal mucin O-glycosylation
Previously, we have identified the polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) gene as notably hypomethylated in low-malignant potential (LMP) and high-grade (HG) serous epithelial ovarian tumors, compared to normal ovarian tissues. Here we show that GALNT3 is strongly overexpressed in ...
ORGANISM(S): Homo sapiens 
2014-05-22 | E-GEOD-52602 | biostudies-arrayexpress
UnknownSite-specific O-Glycosylation by Polypeptide N-Acetylgalactosaminyltransferase 2 (GalNAc-transferase T2) Co-regulates β1-Adrenergic Receptor N-terminal Cleavage.
Not available
S-EPMC5377785 | biostudies-literature
UnknownThe lectin domain of the polypeptide GalNAc transferase family of glycosyltransferases (ppGalNAc Ts) acts as a switch directing glycopeptide substrate glycosylation in an N- or C-terminal direction, further controlling mucin type O-glycosylation.
Not available
S-EPMC3707691 | biostudies-literature
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