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ProteomicsSite-specific O-Glycosylation Analysis of Human Blood Plasma Proteins
Here, we report on the site-specific O-glycosylation analysis of human blood plasma glycoproteins. To this end pooled human blood plasma of healthy donors was digested non-specifically using Protein-ase K, followed by a precipitation step, as well as a glycopeptide enrichment and fractionation step ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2015-06-05 | MSV000079141 | MassIVE
ProteomicsIn-depth site-specific O-glycosylation analysis of glycoproteins and endogenous peptides in cerebrospinal fluid (CSF) from healthy individual mild cognitive impairment (MCI) and Alzheimer disease (AD) patients
Site-specific O-glycoproteome mapping in complex biological system provides molecular basis for understanding the structure-function relationships of glycoproteins and their roles in physiological and pathological processes. Previous O-glycoproteome analysis in cerebrospinal fluid (CSF) focused on s...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-04-05 | MSV000087160 | MassIVE
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 
TranscriptomicsDeconstruction of O-glycosylation – Polypeptide GalNAc-T Isoforms Direct Distinct Subsets of the O-Glycoproteome
GalNAc-transferase (GalNAc-T) isoforms modify distinct subsets of the O-glycoproteome and GalNAc-type O-glycosylation is found on most proteins trafficking through the secretory pathway in metazoan cells. The O-glycoproteome is regulated by up to 20 polypeptide GalNAc-Ts and the contributions and bi...
ORGANISM(S): Homo sapiens 
2015-09-30 | E-MTAB-3844 | biostudies-arrayexpress
Proteomics1. Site-specific O-glycosylation analysis of SARS-CoV-2 spike protein produced in insect and human cells
2. Enveloped viruses hijack not only host translation processes, but also its glycosylation machinery and to a variable extent cover viral surface proteins with tolerogenic host-like structures. SARS-CoV-2 surface protein S presents as a trimer on the viral surface and is covered by a dense shield o...
ORGANISM(S): Homo sapiens (Human) Drosophila melanogaster (Fruit fly) 
2021-04-07 | PXD024767 | Pride
Sars-cov-2 O-glycosylation Lc-ms N-glycosylation Etd 
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
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 
ProteomicsA “Two birds One Stone” Strategy for Site-specific Analysis of the Core Fucosylation and O-GlcNAcylation
Core fucosylation and O-GlcNAcylation are two most famous protein glycosylations and regulate diverse physiological and pathological processes in living organism. Core fucosylation is a protein glycosylation in which a L-fucose residue attaches to the innermost N-acetylglucosamine (GlcNAc) of N-glyc...
ORGANISM(S): Homo Sapiens 
2023-12-04 | PXD047486 |
TranscriptomicsRole of the polypeptide N-acetylgalactosaminyltransferase 3 in ovarian cancer progression: possible implications in abnormal mucin O-glycosylation
Previously, we have identified the polypeptide N-acetylgalactosaminyltransferase 3 (GALNT3) gene as notably hypomethylated in low-malignant potential (LMP) and high-grade (HG) serous epithelial ovarian tumors, compared to normal ovarian tissues. Here we show that GALNT3 is strongly overexpressed in ...
ORGANISM(S): Homo sapiens 
2014-05-22 | E-GEOD-52602 | biostudies-arrayexpress
ProteomicsO-linked Glycosylation of the SARS-CoV-2 Spike is Suppressed by Quaternary Structural Restraints
Understanding the glycosylation of envelope spike (S) protein of SARS-CoV-2 is important in defining the antigenic surface of this key viral target. However, the underlying protein architecture may significantly influence glycan occupancy and processing. There is, therefore, potential for different ...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-07-28 | MSV000087897 | MassIVE
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