Sort   by:  
 Page size 
MetabolomicsSerum protein N-glycosylation changes in multiple myeloma

BACKGROUND: Multiple myeloma is characterized by clonal proliferation of malignant plasma cells in the bone marrow that produce monoclonal immunoglobulins. N-glycosylation changes of these monoclonal immunoglobulins have been reported in multiple myeloma, but previous studies on...

2022-04-27 | MTBLS676 | MetaboLights
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
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
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
ProteomicsSite-specific glycosylation mapping of Fc gamma receptor IIIb from neutrophils of individual healthy donors
The uploaded dateset corresponds to MS1 and MS2 spectra obtained for Fc gamma receptor IIIb isolated from neutrophils of individual healthy donors. They represent NA1/NA2, NA2/NA2, NA2/NA2 allotype respectively. Based on the data, the targeted analysis of the N-glycosylation has been performed for t...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-08-05 | MSV000085913 | MassIVE
ProteomicsMiddle-up analysis of polyclonal IgG-Fc
Middle-up strategy for the analysis of the fragment crystallizable (Fc) region of human plasma immunoglobulins G (IgGs). The use of hydrophilic interaction liquid chromatography (HILIC) and capillary electrophoresis (CE) coupled to mass spectrometry (MS) allowed to get a comprenhesive view of the N-...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2020-05-08 | MSV000085388 | MassIVE
ProteomicsHuman IgG subclasses differ in structural elements of their N-glycosylation
We tested tryptic plasma samples using HILIC-LC-MS/MS, which included mixed human plasma as well as plasma from two healthy individuals collected at three different time points, approximately one month apart. Our focus was on the glycan structure of the Fc domain of IGG subclasses. The results indic...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-06-13 | MSV000095017 | MassIVE
TranscriptomicsH. pylori G27 HP0518 mutant showed greater motility
Helicobacter pylori is a human gastric pathogen associated with gastric and duodenal ulcers as well as specific gastric cancers. It is well-evidenced that motility is essential for this pathogen to colonize human gastric tissues. We found that the H. pylori G27 HP0518 mutant showed greater motility ...
ORGANISM(S): Helicobacter pylori 
2010-12-22 | E-GEOD-14752 | biostudies-arrayexpress
ProteomicsComprehensive N-glycoproteomic profiling of humanized antibody expressed in transgenic mouse serum
This dataset reports a comprehensive N-glycoproteomic profiling of serum-derived humanized antibodies expressed in transgenic mice using an intact glycopeptide (IGP)–based LC–MS/MS workflow. The study aimed to identify and characterize site-specific N-glycosylation modifications of mouse serum prote...
ORGANISM(S): Mus musculus (Mouse) 
2025-12-08 | PXD070488 | Pride
Antibody Transgenic mouse Post-translational modification Glycoproteomics Orbitrap astral N-glycosylation Intact glycopeptides Dda Lc–ms/ms 
ProteomicsDecreased Fc fucosylation aligns with enhanced RSV-specific antibody functionality in adults compared to young children
Respiratory syncytial virus (RSV) is a major cause of severe respiratory tract infections in infants and older adults. While vaccines have recently been approved for older adults and pregnant women, vaccine development for infants remains challenging due to the risk of vaccine-enhanced disease. Unde...
ORGANISM(S): Homo sapiens (Human) 
2025-11-05 | PXD069590 | Pride
Fc-glycosylation Antibody maturation Respiratory virus Fc-functionality 
Sort   by:  
 Page size