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MetabolomicsN-glycosylation Profiling of Colorectal Cancer Cell Lines Reveals Association of Fucosylation with Differentiation and Caudal Type Homebox 1 (CDX1)/Villin mRNA Expression
Various cancers such as colorectal cancer (CRC) are associated with alterations in protein glycosylation. CRC cell lines are frequently used to study these (glyco)biological changes and their mechanisms. However, differences between CRC cell lines with regard to their glycosylation have hitherto bee...
2017-02-03 | MTBLS227 | MetaboLights
ProteomicsAnalysis of N-Glycosylation for SARS-CoV-2 expressed receptor-binding domain VOCs and membrane protein with LC-MS.
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can infect human cells by first attaching to the ACE-2 receptor via its receptor-binding domain (RBD) in the spike protein. We investigated the influence of N-glycosylation sites of the RBD and the membrane (M) protein on IgG antibody bind...
ORGANISM(S): Severe Acute Respiratory Syndrome Coronavirus 2 
2024-04-29 | PXD048930 | panorama
ProteomicsProtein N-glycosylation is sex-related in Nilaparvata lugens adults
Nilaparvata lugens, or the brown planthopper, is one of the most notorious pest insects of cultured rice, and a model for hemimetabolous development. Recently, the N-glycome of N. lugens was explored throughout post-embryonic development and reproductive stages, which revealed differential protein N...
ORGANISM(S): Nilaparvata lugens 
2020-01-16 | PXD013657 | Pride
Nilaparvata lugens Pest insect N-glycosylation sites N-linked glycosylation 
ProteomicsSite-specific analysis of CD16a and CD32a N-glycosylation from monocytes display donor variability which modulate affinity to IgG1 Fc
Glycopeptide mass spectra of CD16a and CD32a from isolated monocytes display donor and site variability. CD16a N-glycosylation composition affects the affinity of IgG1 Fc. Peptide coverage of CD16a was ~85% while CD32a was ~61%.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2019-06-26 | MSV000084012 | MassIVE
ProteomicsIdentification of N-glycosylation sites on HHV glycoprotein B trimers
Mass spectrometry data for the identification and characterization of N-glycosylation sites on herpesvirus glycoprotein B (gB) trimers. gB proteins were analyzed by LC-MS/MS following proteolytic digestion, with PNGase F-treated and untreated samples analyzed to identify N-glycosylated peptides and ...
ORGANISM(S): Homo sapiens 
2026-10-22 | PXD086038 | Pride
Glycoprotein b (gb) Herpesvirus N-glycosylation 
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 
ProteomicsVEGFR N-glycosylation
Vascular endothelial growth factor receptor-2 (VEGFR2) is a highly N-glycosylated receptor tyrosine kinase involved in pro-angiogenic signaling in physiological and pathological contexts, including cancer. VEGFR2 post-translational modifications (PTMs) and their roles in receptor function and signal...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2021-09-08 | PXD012629 | Pride
Vegfr2 Rtk N-glycosylation Nlc-ms/ms Mouse Glycopeptides 
ProteomicsEndoglycosidases- treated N-glycosylation site identification
Glycoproteins, representing over 50% of human proteins and most biopharmaceuticals, are crucial for regulating various biological processes. The complexity of multiple glycosylation sites often leads to incomplete sequence coverage and ambiguous glycan modification profiles. Here, we developed an in...
ORGANISM(S): Homo Sapiens 
2024-12-30 | PXD059329 |
ProteomicsN-Glycosylation profiling in rice
As a ubiquitous and essential posttranslational modification occurred in both plants and animals, protein N-linked glycosylation regulates various important biological processes. Unlike the well studied animal N-glycoproteomes, the landscape of rice N-glycoproteome remains largely unexplored. Here, ...
ORGANISM(S): Oryza sativa (Rice) 
2025-05-07 | PXD054828 | Pride
N-glycosylation Rice 
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 
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