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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
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 
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 
ProteomicsTAILS N-Terminomics and Proteomics Show Complex Regulation of Proteolytic Processing by O-glycosylation
Proteolytic processing is an irreversible post-translational modification functioning as a ubiquitous regulator of cellular activity. Protease activity is tightly regulated by control of gene expression, compartmentalisation of enzyme and substrate, zymogen activation, enzyme inactivation, and subst...
ORGANISM(S): Homo sapiens (Human) 
2018-10-08 | PXD009453 | Pride
Human Lc-msms Degradomics O-glycoproteomics Tails 
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 
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 
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
ProteomicsO-glycosylation in fruit development and ripening
O-glycosylation is a critical post-translational modification (PTM) regulating protein function, yet its role in plant transcription factors remains poorly understood.
ORGANISM(S): Solanum Lycopersicum 
2025-12-16 | PXD072030 |
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 
ProteomicsSite-specific N- and O-glycosylation Analysis of Human Plasma Fibronectin
Human plasma fibronectin is an adhesive protein that plays a crucial role in wound healing. Many studies had indicated that glycans may mediate the expression and functions of fibronectin, yet a comprehensive understanding of its glycosylation is still missing. Here, we performed a comprehensive N- ...
ORGANISM(S): Homo sapiens (Human) 
2022-02-17 | PXD025886 | Pride
Mass spectrometer Glycosylation Stepped normalized collision energy Operator Fibronectin 
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