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Discriminating pathogenic bacteria from energy-harvesting commensals is key to host immunity. Using mutants defective in the enzymes of O-linked N-acetylglucosamine (O-GlcNAc) cycling, we examined the role of this nutrient-sensing pathway in the Caenorhabidits elegans innate immune response. Using w...
ORGANISM(S): Caenorhabditis elegans 
Nutrient-driven O-GlcNAcylation of key components of the transcription machinery may epigenetically modulate gene expression in metazoans. Knockouts of the O-GlcNAc cycling enzymes in C. elegans are viable and fertile, allowing a global analysis of the impact of GlcNAcylation. Whole genome transcrip...
ORGANISM(S): Caenorhabditis elegans 
Nutrient-driven O-GlcNAcylation of key components of the transcription machinery may epigenetically modulate gene expression in metazoans. Knockouts of the O-GlcNAc cycling enzymes in C. elegans are viable and fertile, allowing a global analysis of the impact of GlcNAcylation. Whole genome transcrip...
ORGANISM(S): Caenorhabditis elegans 
In this work, by using the lysates of PANC-1 (a pancreatic cancer cell line), we provided a head-to-head comparison of three affinity enrichment methods/materials (i.e., antibody, lectin AANL6, and an OGA mutant) for O-GlcNAc proteomics. The enrichment was performed before or after high-pH HPLC frac...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) Saccharomyces Cerevisiae (ncbitaxon:4932) 
2024-04-23 | MSV000094604 | MassIVE
A key nutrient sensing process in all animal tissues is the dynamic attachment of O-linked N-acetylglucosamine (O-GlcNAc). Determining the targets and roles of O-GlcNAc glycoproteins has the potential to reveal insights into healthy and diseased metabolic states. In cell studies, thousands of protei...
ORGANISM(S): Mus musculus (Mouse) 
2026-07-21 | PXD060554 | Pride
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
O-GlcNAc is thought to regulate proteins in a mannaer analogous to other PTMs, modulating cellular functions including the cellular stress response. The aim of this study was to identify specific cellular networks and protein complexes that are differentially O-GlcNAcylated and/or expressed upon acu...
ORGANISM(S): Mus musculus (Mouse) 
2016-09-29 | PXD000849 | Pride
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
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 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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