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GenomicsO-GlcNAcylation Modulates Expression and Abundance of N-Glycosylation Machinery in an Inherited Glycosylation Disorder
O-GlcNAcylation Modulates Expression and Abundance of N-Glycosylation Machinery in an Inherited Glycosylation Disorder
PRJNA1120060 | ENA
TranscriptomicsO-GlcNAcylation Modulates Expression and Abundance of N-Glycosylation Machinery in an Inherited Glycosylation Disorder
Much of the N-glycosylation machinery was identified decades ago, but the regulatory mechanisms influencing normal and disease states are only beginning to be discovered. Recent studies highlight a role for key metabolites and metabolic enzymes in this process, revising the view of the relationship ...
ORGANISM(S): Danio rerio 
2024-12-27 | GSE269074 | GEO
ProteomicsPosition-specific N- and O-glycosylation of the reactive centre loop impacts neutrophil elastase-mediated proteolysis of corticosteroid-binding globulin
Corticosteroid-binding globulin (CBG) delivers anti-inflammatory cortisol to inflamed tissues through the proteolytic cleavage of an exposed reactive centre loop (RCL) by neutrophil elastase (NE). We previously demonstrated that RCL-localised Asn347-linked N-glycans impact NE proteolysis, but a comp...
ORGANISM(S): Homo sapiens (Human) 
2023-12-05 | PXD046405 | Pride
Glycosylation O-glycosylation Corticosteroid-binding globulin Cortisol N-glycosylation Proteolysis Reactive centre loop Neutrophil elastase 
ProteomicsDeciphering the O-glycosylation of HKU1 Spike Protein with the Dual-Functional Hydrophilic Interaction Chromatography Materials
HKU1 is a human betacoronavirus and infects host cells via highly glycosylated spike protein (S). At present, N-glycosylation of HKU1 S has been reported, however, little is known about its O-glycosylation, which hinders an in-depth understanding of its biological functions. Herein, a comprehensive ...
ORGANISM(S): Human coronavirus HKU1 (isolate N1) 
2022-02-17 | PXD025967 | Pride
O-glycosylation sites O-glycosylation abundance Spike glycoprotein Enrichment Hku1 
ProteomicsGenotype-dependent N-glycosylation and newly discovered O-glycosylation affecting HRG plasmin cleavage
Histidine-rich glycoprotein (HRG) is an abundant plasma glycoprotein with three reported N-glycosylation sites, which integrates many biological processes such as antiangiogenic activity, immune complex clearance and pathogen clearance. Importantly, the protein is known to have five genetic variants...
ORGANISM(S): Homo sapiens (Human) 
2024-05-21 | PXD044353 | Pride
Histidine-rich glycoprotein (hrg) O-glycosylation Glycoproteomics Plasmin cleavage N-glycosylation 
ProteomicsTargeted Proteomics Reveals Quantitative Differences in Low Abundance Glycosyltransferases of Patients with Congenital Disorders of Glycosylation
Protein glycosylation is an essential posttranslational modification in all domains of life. Its impairment in human can result in severe diseases named Congenital Disorders of Glycosylation (CDGs). Most of the glycosyltransferases (GTs) responsible for proper glycosylation are polytopic membrane p...
ORGANISM(S): Homo Sapiens 
2024-01-30 | PXD048072 | panorama
UnknownO-GlcNAcylation modulates expression and abundance of N-glycosylation machinery in an inherited glycosylation disorder.
Not available
S-EPMC11656453 | biostudies-literature
ProteomicsThe metacaspase Mca1p restricts O-glycosylation during farnesol-induced apoptosis in Candida albicans
Protein glycolysation is an essential posttranslational modification in eukaryotic cells. In pathogenic yeasts, it is involved in a large number of biological processes, such as protein folding quality control, cell viability and host/pathogen relationships. A link between protein glycosylation and ...
ORGANISM(S): Candida albicans (Yeast) 
2016-05-02 | PXD003677 | Pride
Candida albicans O-glycosylation Glycoproteomics Ssb1 N-glycosylation Metacaspase Bgl2 Farnesol Glycomics Cdc48 Aminoxytmt Erad Pdi1 Orbitrap fusion. Apoptosis Glycans quantification 
ProteomicsAn integrated MS data processing strategy for fast identification, in-depth and reproducible quantification of protein O-glycosylation in large cohorts of human urine samples
Protein O-glycosylation has long been recognized to be closely associated with many diseases, particularly with tumor proliferation, invasion and metastasis. The ability to efficiently profile the variation of O-glycosylation in large-scale clinical samples provides an important approach for the devel...
ORGANISM(S): Homo sapiens (Human) 
2020-02-04 | PXD015987 | Pride
O-glycopeptide  urine  sialic acid 
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 
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