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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
ProteomicsIdentification of O-GlcNAcylation sites of hemocyanin in Penaeus vannamei in response to pathogenic bacteria
Detection of the O-GlcNAcylation sites of hemocyanin in response to Vibrio parahaemolyticus stimulation using the ThermoFisher Orbitrap Exploris 480.
ORGANISM(S): Penaeus vannamei 
2026-08-24 | PXD046737 | Pride
Hemocyanin  o-glcnacylation sites  vibrio parahaemolyticus 
ProteomicsCancer-cell-secreted miR-122 suppresses O-GlcNAcylation to promote muscle proteolysis
Decline in skeletal muscle mass and lower muscular strength are prognostic factors in advanced human cancers. We found that breast cancer suppressed O-linked N-acetylglucosamine (O-GlcNAc) protein modification in skeletal muscle through extracellular-vesicle-encapsulated miR-122 that targeted O-GlcN...
ORGANISM(S): Mus musculus (Mouse) 
2023-03-10 | PXD021232 | Pride
Mouse cancer glycosylation 
ProteomicsDynamic Yin-Yang regulation network of O-GlcNAcylation and phosphorylation mediates vernalization response for flowering in winter wheat
Protein post-translational modification (PTM) increases the functional diversity of the proteome and regulates numerous biological processes in eukaryotes. Two types of PTMs, O-linked-acetyl glucosamine modification (O-GlcNAc) and phosphorylation have been identified on the same amino acid, are cons...
ORGANISM(S): Triticum aestivum (Wheat) 
2020-12-18 | PXD008285 | Pride
Proteomics O-glcnacylation modification Phosphorylation modification 
ProteomicsSystematic Quantification of Protein O-GlcNAcylation Reveals Common and Cell-Type-Specific Responses to N-Glycosylation Inhibition in Human Cells
In this work, we systematically and site-specifically analyzed protein O-GlcNAcylation under the N-glycosylation inhibition through the integration of metabolic labeling, bio-orthogonal chemistry, and multiplexed proteomics. The experiments were performed in three types of human cells, i.e., HEK293T...
ORGANISM(S): Homo sapiens (Human) 
2026-06-02 | PXD073249 | Pride
Glycoproteomics Protein o-glcnacylation 
GenomicsTargeted O-GlcNAcylation Enables Functional Rewiring of c-Myc
Targeted O-GlcNAcylation Enables Functional Rewiring of c-Myc
PRJNA1415248 | ENA
MetabolomicsGNPS - A novel quantitative mass spectrometry platform for determining site-specific protein O-GlcNAcylation dynamics
Over the past decades, protein O-GlcNAcylation has been found to play a fundamental role in cell cycle control, metabolism, transcriptional regulation, and cellular signaling. Nevertheless, quantitative approaches to determine in vivo GlcNAc dynamics at a large-scale are still not readily available....
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080705 | GNPS
ProteomicsDynamic Yin-Yang regulation network of O-GlcNAcylation and phosphorylation mediatesvernalization response for flowering in winter wheat, part 2
Protein post-translational modification (PTM) increases the functional diversity of the proteome and regulates numerous biological processes in eukaryotes. Two types of PTMs, O-linked-acetyl glucosamine modification (O-GlcNAc) and phosphorylation have been identified on the same amino acid, are cons...
ORGANISM(S): Triticum aestivum (Wheat) 
2021-05-18 | PXD008298 | Pride
Proteomics O-glcnacylation modification Phosphorylation modification 
ProteomicsA novel quantitative mass spectrometry platform for determining site-specific protein O-GlcNAcylation dynamics
Over the past decades, protein O-GlcNAcylation has been found to play a fundamental role in cell cycle control, metabolism, transcriptional regulation, and cellular signaling. Nevertheless, quantitative approaches to determine in vivo GlcNAc dynamics at a large-scale are still not readily available....
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-28 | MSV000080705 | MassIVE
ProteomicsO-GlcNAcylation of FOXK1 orchestrates the E2F pathway
Gene transcription is a highly regulated process, and deregulation of transcription factors activity underlie numerous pathologies including cancer. FOXK1 and FOXK2 (FOXK1/2) transcription factors have recently emerged as important regulators of cell metabolism, autophagy and cell differentiation. W...
ORGANISM(S): Homo sapiens (Human) 
2024-06-10 | PXD050014 | Pride
E2f pathway O-glcnacylation Foxk1 
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