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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
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
Samples were analyzed using a Maxis II QTOF instrument (Bruker Daltonik GmbH, Bremen, Germany) equipped with CaptiveSpray nanoBooster ion source coupled to a Dionex UltiMate 3000 RSLCnano system (Sunnyvale, CA, USA). Peptides were separated on an Acquity M-Class BEH130 C18 analytical column using gr...
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2021-04-28 | MSV000087329 | MassIVE
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 |
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 |
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
Protein N-glycosylation plays a crucial role in the human liver, impacting key functions like hepatocyte lipid metabolism hepatocyte apoptosis, and inflammatory response. Despite its significance, the site-specific N-glycosylation patterns and their variations of liver biosy samples between healthy ...
ORGANISM(S): Homo Sapiens 
2024-07-04 | PXD053626 |
A novel chemoenzymatic method termed solid phase extraction of N-linked Glycans And Glycosite-containing peptides (NGAG) for the simultaneous analysis of N-glycans, glycosite-containing peptides, and intact N-glycopeptides with site-specific glycosylation information.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2017-03-31 | MSV000080840 | MassIVE
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
Glycosylation is a critical determinant of the efficacy, stability, and pharmacological behavior of therapeutic proteins. R27T, an engineered variant of interferon-β1a, contains two N-glycosylation sites (Asn25 and Asn80), increasing its structural complexity and analytical requirements. In this stu...
ORGANISM(S): Homo sapiens (Human) 
2026-09-21 | PXD077477 | Pride
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