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TranscriptomicsConserved nutrient sensor O-GlcNAc transferase is integral to the C. elegans pathogen-specific immune response
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 
2015-05-01 | E-GEOD-53732 | biostudies-arrayexpress
ProteomicsThe OGT TPR Interactome defined by BioID
BioID performed in HeLa cells for the TPR domain of The O-GlcNAc Transferase and eGFP (negative control). Used to determine TPR interactors and the TPR interactome in HeLa cells. Three biological replicates were performed, with each replicate having an experimental (TPR-BirA*) and negative (eGFP-Bir...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-06-24 | MSV000085626 | MassIVE
UnknownComputational Analysis of N-acetyl transferase in Tribolium castaneum.
Not available
S-EPMC3746093 | biostudies-literature
ProteomicsQuantitative Proteomics Reveals that the OGT Interactome is Remodeled in Response to Oxidative Stress
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 
2021-04-05 | PXD021091 | panorama
TranscriptomicsCharacterization of a novel mutation in O-GlcNAc transferase that segregates with disease in a family with X-linked intellectual disability
An X-chromosome exome sequencing analysis identified a mutation in O-GlcNAc transferase (OGT) (pL254F) in a family with X-linked intellectual disability (XLID). Affected patient lymohoblastoids exhibit decreased steady state OGT levels owing to an unstable protein compared to the unaffected, related...
ORGANISM(S): Homo sapiens 
2016-02-25 | E-GEOD-74263 | biostudies-arrayexpress
ProteomicsN-terminal acetylation determination of PEXEL proteins
We have knocked out a putative N-acetyl transferase, Pf3D7_1437000, from the malaria parasite plasmodium falciparum. Pf3D7_1437000 resides in the ER. Proteins in the Plasmodium falciparum secretory pathway are known to be extensively N-terminally acetylated. We have isolated two such proteins, HRP2 ...
ORGANISM(S): Plasmodium falciparum NF54 
2023-02-13 | PXD038231 | Pride
Plasmodium falciparum Er N-acetyl transferase 
TranscriptomicsDrosophila Oga deletion perturbs O-GlcNAcylation of chromatin factors
Drosophila development is a complex and dynamic process regulated, in part, by members of the Polycomb (Pc), Trithorax (Trx) and Compass chromatin modifier complexes. O-GlcNAc Transferase (OGT/SXC) is essential for Pc repression suggesting that the O-GlcNAcylation of proteins plays a key role in re...
ORGANISM(S): Drosophila melanogaster 
2016-07-21 | E-GEOD-74846 | biostudies-arrayexpress
ProteomicsO-GlcNAc Containing Proteins in Normal and Idiopathic Pulmonary Fibrosis Human Fibroblasts
Isolated normal and IPF fibroblasts were homogenized in cold MilliQ water using a bullet blender. Samples were centrifuged and inhibitors were added: HALT (Thermo Fisher Scientific), Z-Pugnac (Tocris), Thiamet G (Cayman Chemicals), and benzonase (E1014, Millipore, Sigma). O-GlcNAc enzymatic labeling...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2023-11-21 | MSV000093453 | MassIVE
UnknownRhizobial NodL O-acetyl transferase and NodS N-methyl transferase functionally interfere in production of modified Nod factors.
Not available
S-EPMC99639 | biostudies-literature
TranscriptomicsGlycosylation regulates the stability of c-MYC
Tumorigenesis is characterised by changes in transcriptional regulation and the androgen receptor (AR) has been identified as a key driver in prostate cancer. In this study, we show that the hexosamine biosynthetic pathway (HBP) genes are overexpressed in clinical prostate cancer and androgen-regula...
ORGANISM(S): Homo sapiens 
2013-05-30 | E-GEOD-44624 | biostudies-arrayexpress
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