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MetabolomicsAbsence of tmRNA Increases the Persistence to Cefotaxime and the Intercellular Accumulation of Metabolite GlcNAc in Aeromonas veronii
Bacterial persisters are a small proportion of phenotypically heterogeneous variants with the transient capability to survive in high concentrations of antibiotics, causing recurrent infections in both human and aquatic animals. Transfer-messenger RNA (tmRNA), which was encoded by the ssrA ge...
2021-10-18 | MTBLS1182 | MetaboLights
MetabolomicsAbsence of tmRNA increases the persistence to cefotaxime by upregulating the metabolites GlcNAc in Aeromonas veronii

Bacterial persisters refer to a small proportion of phenotypically heterogeneous variants with transient capability for survival when exposing to high concentrations of antibiotic, which constitute the major cause for recurrent infections both in human and aquatic infections. In pathogenic bacter...

2020-01-10 | MTBLS1191 | MetaboLights
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
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 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
ProteomicsComparison of affinity enrichment methods for O-GlcNAc proteomics
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
ProteomicsA reference dataset of O-GlcNAc proteins in quadriceps skeletal muscle from mice
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
Glycoproteomics Skeletal muscle O-glcnac Mouse quadriceps Tissue atlas 
ProteomicsCombined Antibody/Lectin-Enrichment Identifies Extensive Changes in the O-GlcNAc Subproteome Upon Oxidative Stress
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
Oxidative stress Affinity chromatography Silac O-glcnac 
ProteomicsIdentification of enriched O-GlcNAc proteins in hypertrophic and normal mouse hearts
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
GenomicsGenome-wide maps of O-GlcNAc-Oct4 binding regions in ZHBTc4 F-Oct4 mouse embryonic stem cells
We report that Oct4 is modified by O-GlcNAc in stem cells. To find O-GlcNAc-Oct4 target genes, we ChIPed Oct4 with Flag(Oct4) antibody and then O-GlcNAc modified proteins are enriched by sWGA beads (succinylated wheat germ agglutinin (sWGA), which specifically binds O-GlcNAc). Results show that seve...
ORGANISM(S): Mus musculus 
2012-08-27 | E-GEOD-36388 | biostudies-arrayexpress
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