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ProteomicsGlobal mapping of GalNAc-T isoform-specificities and O-glycosylation site-occupancy in a tissue-forming human cell line
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
Galnt   fibronectin  ldlr  lrp  col17a1 Differential glycoproteomics. Crispr 3d tissue models  oragnoid 
ProteomicsC18 nanoLC-MS and Glycogenomics to Facilitate O-Glycan profiling in Human Cells
O-glycosylation is an abundant modification throughout the human proteome and plays a role in, amongst others, regulation of protein cleavage, protein folding, and modulation of cell-cell and -matrix interactions. O-glycosylation type and structure are important for biological function, demanding an...
ORGANISM(S): Homo sapiens (Human) 
2022-04-04 | PXD029644 | Pride
Keratinocytes Glycogenomics Glycomics Hek293 O-glycan 
ProteomicsTAILS N-Terminomics and Proteomics Show Complex Regulation of Proteolytic Processing by O-glycosylation
Proteolytic processing is an irreversible post-translational modification functioning as a ubiquitous regulator of cellular activity. Protease activity is tightly regulated by control of gene expression, compartmentalisation of enzyme and substrate, zymogen activation, enzyme inactivation, and subst...
ORGANISM(S): Homo sapiens (Human) 
2018-10-08 | PXD009453 | Pride
Human Lc-msms Degradomics O-glycoproteomics Tails 
ProteomicsProteome-wide identification of SUMO2 modification sites
Posttranslational modification with small ubiquitin-like modifiers (SUMOs) alters the function of proteins involved in diverse cellular processes. SUMOs are conjugated to lysine residues in target proteins by SUMO-specific enzymes. Although proteomic studies have identified hundreds of sumoylated su...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080741 | MassIVE
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