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The dynamic modification of specific serine and threonine residues of intracellular proteins by O-linked N-acetyl-β-D-glucosamine (O-GlcNAc) mitigates injury and promotes cytoprotection in a variety of stress models. The O-GlcNAc transferase (OGT) and the O-GlcNAcase (OGA) are the sole enzymes that ...
ORGANISM(S): Mus Musculus 
In this study, we demonstrated that OTX2 was transcriptionally and post-transcriptionally regulated by O-GlcNAcylation. We describe the modes of degradation of this essential homeobox protein involving both the proteasome and macroautophagy. While the proteasome remains the canonical degradation pat...
ORGANISM(S): Homo sapiens (Human) 
2024-01-22 | PXD040353 | Pride
The modification of intracellular proteins by monosaccharides of O-linked linked β-N-acetylglucosamine (O-GlcNAc) is thought to mediate proteins by regulating protein phosphorylation, either by modifying and modulating protein kinases or by competing with phosphorylation for hydroxyl residues. To pr...
ORGANISM(S): Mus musculus (Mouse) 
2015-01-28 | PXD001153 | Pride

In this era of precision medicine, there is an increasingly urgent need for highly sensitive tests for detecting tumors such as colon cancer (CC), a silent disease where the first symptoms may take 10-15 yr to appear. Mass spectrometry-based lipidomics is an emerging tool for such clinical diagno...

2023-11-13 | MTBLS1584 | MetaboLights
Human catechol-O-methyltransferase (COMT) has emerged as a model for understanding enzyme catalyzed methyl transfer from S-adenosylmethionine (AdoMet) to small molecule catecholate acceptors. Mutation of a single residue (Tyrosine 68) behind the methyl-bearing sulfonium of AdoMet was previously show...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-04-01 | MSV000085213 | MassIVE
SILAC labeled mouse embryonic fibroblasts were treated with hydrogen peroxide to induce the stress reponse. OGT was immunoprecipitated and interactors identified via LC-MS/MS.
ORGANISM(S): Mus musculus (Mouse) 
2021-04-14 | PXD013645 | Pride
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