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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
TranscriptomicsExpression from C. elegans L1 animals
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 
2009-12-31 | E-GEOD-18130 | biostudies-arrayexpress
TranscriptomicsExpression from C. elegans L4 animals
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 
2010-01-01 | E-GEOD-18131 | 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
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
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
ProteomicsZscan4 as a candidate conveyor of early developmental defects in O-GlcNAc transferase intellectual disability
Variants in the human β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) gene give rise to an intellectual disability (ID) syndrome termed OGT congenital disorder of glycosylation (OGT-CDG). The mechanisms by which loss of OGT and/or protein O-GlcNAcylation lead to this syndrome are not understood, ...
ORGANISM(S): Mus musculus (Mouse) 
2025-10-03 | PXD064425 | Pride
O-glcnac transferase Tmt Mouse 
Proteomicsselective protein O-glcNAcylation in cells by a proximity-directed O-GlcNAc transferase
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
Ogt Glycoproteomics Nanobody O-glcnac 
GenomicsInhibition of O-GlcNAcylation via O-GlcNAc transferase fosters megakaryopoiesis and induces thrombopoiesis
Inhibition of O-GlcNAcylation via O-GlcNAc transferase fosters megakaryopoiesis and induces thrombopoiesis
PRJNA633908 | ENA
ProteomicsE. coli expressed SECRET AGENT O-GlcNAc modifies threonine 829 of GIGANTEA
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
Arabidopsis thaliana Gigantea Protein modification O-glcnac E. coli 
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