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Bottom up proteomics of O-GlcNAc antibody enriched proteins from mouse heart tissue (hypertrophic vs. normal). O-GlcNAc proteins were labeled with a click chemistry kit with the tetramethylrhodamine (TAMRA) tag, then the labeled proteins were enriched with TAMRA antibody for proteomics experiments.
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2021-12-06 | MSV000088525 | MassIVE
We used C57/Bl6 mice subjected to sham or transverse aortic constriction (TAC) to create pressure-overload hypertrophy (POH). From the hearts, we stabilized and labelled the O-GlcNAc moiety with tetramethylrhodamine azide (TAMRA) before enriching by TAMRA immunoprecipitation (files with "TAMRAIP"). ...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2022-02-07 | MSV000088797 | MassIVE
O-GlcNAcylation is a dynamic and reversible post-translational modification involving the attachment of a single β-N-acetylglucosamine (GlcNAc) moiety to the hydroxyl groups of serine or threonine residues. This modification occurs in thousands of cytoplasmic, nuclear, and mitochondrial proteins in ...
ORGANISM(S): Vaccinia virus WR 
2025-05-21 | PXD062753 | Pride
Mice were i.p. injected Thiamet G (TG) or saline, and mouse brain cortex tissues were analyzed for O-GlcNAc by LC-MS/MS with TMT based quantification. Data was searched with MS-GF+ using PNNL's DMS processing pipeline.
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
The reversible posttranslational O-GlcNAc modification of serine or threonine residues of intracellular proteins is involved in many cellular events from signaling cascades to epigenetic and transcriptional regulation. O-GlcNAcylation is a conserved nutrient-dependent process involving two enzymes,...
ORGANISM(S): Drosophila melanogaster (Fruit fly) 
2021-04-26 | PXD025344 | Pride
O-GlcNAc proteins in LNM and non-LNM breast tumors of IDCs were identified by using the strategy of chemo-enzymatic labeling in combination with click chemistry and LC-MS/MS.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080753 | MassIVE
O-GlcNAcylation occurs on thousands of proteins involved in various cellular events. O-GlcNAc transferase (OGT), one of the enzymes responsible for protein O-GlcNAcylation, is known to be auto-O-GlcNAcylated at multiple sites. However, the role of O-GlcNAcylation on OGT is still unknown. Here, we re...
ORGANISM(S): Homo sapiens (Human) 
2019-09-16 | PXD009731 | Pride
O-Linked N-acetylglucosamine (O-GlcNAc) is a monosaccharide that plays an essential role in cellular signaling throughout the nucleocytoplasmic proteome of eukaryotic cells. Yet, the study of post-translational modifications like O-GlcNAc has been limited by the lack of strategies to induce O-GlcNA...
ORGANISM(S): Homo sapiens (Human) 
2021-09-08 | PXD016041 | Pride
Bioorthogonal chemistries have revolutionized many fields. For example, metabolic chemical reporters (MCRs) of glycosylation are analogs of monosaccharides that contain bioorthogonal functionality, like azides or alkynes. MCRs are metabolically incorporated into glycoproteins by living systems, and ...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD027333 | Pride
The Arabidopsis thaliana glycosyl transferases SPINDLY (SPY) and SECRET AGENT (SEC) modify nuclear and cytosolic proteins with O-linked fucose or O-linked Nacetylglucosamine (O-GlcNAc), respectively. O-fucose and O-GlcNAc modifications can occur at the same sites. SPY interacts physically and geneti...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2024-07-15 | PXD053909 | Pride
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