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ProteomicsAn ultrasensitive method for analysis of viral spike N-glycoforms
Viruses can evade the host immune system by displaying numerous glycans on their surface "spike-proteins" that cover immune epitopes. We have developed an ultrasensitive "single pot" method to assess glycan occupancy and the extent of glycan processing from high-mannose to complex forms at each N-gl...
ORGANISM(S): Bg505 Sosip.664 Md39 Bg505 Sosip.664 Homo Sapiens (ncbitaxon:9606) 
2021-05-12 | MSV000087414 | MassIVE
ProteomicsGlobal mapping of GalNAc-T isoform-specificities and O-glycosylation site-occupancy in a tissue-forming human cell line
Mucin-type-O-glycosylation on proteins is integrally involved in human health and disease and is coordinated by an enzyme family of 20 N-acetylgalactosaminyltransferases (GalNAc-Ts). Detailed knowledge on the biological effects of site-specific O-glycosylation is limited due to lack of information o...
ORGANISM(S): Homo sapiens (Human) 
2022-10-22 | PXD036791 | Pride
Galnt   fibronectin  ldlr  lrp  col17a1 Differential glycoproteomics. Crispr 3d tissue models  oragnoid 
ProteomicsGlycoproteomics identify disease-associated N-glycans and reduced occupancy of glycosylation sites in PMM2-CDG
The routine diagnostic pathway for congenital disorders of glycosylation (CDG) relies on carbohydrate deficient transferrin, a test that incompletely captures defects in N linked glycosylation and may yield false negative results even in classical N glycosylation disorders such as PMM2 CDG. To explo...
ORGANISM(S): Homo sapiens (Human) 
2026-09-28 | PXD080194 | Pride
N‐linked glycosylation Carbohydrate metabolism Glycoproteomics Congenital disorders of glycosylation (cdg) Glycopeptide Glycomics Biomarker Inborn error of metabolism 
ProteomicsN-glycosylation site occupancy in human prostaglandin H synthases expressed in Pichia pastoris
Prostaglandin H synthases (PGHSs) are N-glycosylated membrane proteins that catalyse the committed step in prostaglandin synthesis. Unlike PGHS-2, the production of recombinant PGHS-1 in non-mammalian expression systems is complicated. The majority of the heterologous enzyme is inactive due to misfo...
ORGANISM(S): Homo sapiens (Human) Komagataella pastoris (Yeast) (Pichia pastoris) 
2014-08-18 | PXD000965 | Pride
Proteomics Recombinant protein Pghs N-glycosylation Lc-ms/ms 
UnknownLarge-scale quantitative glycoproteomics analysis of site-specific glycosylation occupancy.
Not available
S-EPMC3463725 | biostudies-literature
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 
ProteomicsGlycoproteomic Analyses of Prostate Cancer Cells
Integrated Proteomic and Glycoproteomic Analyses of Prostate Cancer Cells Reveals Glycoprotein Alteration in Protein Abundance and Glycosylation
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-29 | MSV000080799 | MassIVE
ProteomicsAn Insight into Glyco-microheterogeneity of Plasma von Willebrand Factor (vWF) by Mass Spectrometry
Von Willebrand Factor (vWF), a plasma glycoprotein, plays essential roles in primary hemostasis, in cooperation with other coagulation factors. The glycosylation affects many biological phases during the protein life-cycle. In this work, we comprehensively characterized the microheterogeneity at all...
ORGANISM(S): Homo sapiens (Human) 
2022-02-23 | PXD006567 | Pride
Glycosylation Cid Microheterogeneit Plasma von willebrand factore N-glycan Vwf Mass spectrometry Hcd O-glycan Occupancy 
ProteomicsCombining FAIMS based Glycoproteomic and DIA Proteomic of reveals widespread proteome alteration in response to changes in N. gonorrhoeae glycosylation occupancy.
Protein glycosylation is increasingly recognized as a common protein modification across bacterial species. Within pathogenic members of the Neisseria genus O-linked protein glycosylation is associated with virulence yet the depth of the glycoproteome, or if glycosylation plays additional roles in N...
ORGANISM(S): Neisseria gonorrhoeae FA19 
2024-02-01 | PXD045142 | Pride
Faims Lc-ms Glycosylation Neisseria 
ProteomicsAnalysis of Substrate Specificity of Trypanosoma brucei OSTs by Functional Expression in Yeast
N-linked protein glycosylation is an essential and highly conserved post-translational modification in eukaryotes. The transfer of a glycan from a lipid-linked oligosaccharide (LLO) donor to asparagine residues of nascent polypeptide chains is catalyzed by the oligosaccharyltransferase (OST) in the ...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2017-11-03 | PXD007215 | Pride
Lipid linked oligosaccharide specificity Oligosaccharyltransferase N-linked glycosylation Glycosylation occupancy analysis Trypanosoma brucei 
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