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Alterations of protein abundance and post-translational modifications in patients with Alzheimer’s disease (AD), such as glycosylation, phosphorylation, and ubiquitination, and their roles in disease progression and treatment outcome are areas of intense study. Little is known, however, about...
ORGANISM(S): Homo sapiens (Human) 
2022-10-31 | PXD032219 | Pride
To understand the cellular functions of glycans and to exploit them as clinical targets it is essential to acquire information on their cell surface exposure. Here, we developed a sensitive and specific mass spectrometry method to globally study the N-glycoforms displayed at individual protein sites...
ORGANISM(S): Homo sapiens (Human) 
2024-01-26 | PXD042172 | Pride
Glycoproteomics analysis of triple wild-type lung adenocarcinoma tissue samples for the publication of the same name.
ORGANISM(S): Homo Sapiens (ncbitaxon:9606) 
2024-11-18 | MSV000096450 | MassIVE
In the biological systems, several genes are involved in protein glycosylation and deglycosylation pathways. Congenital disorders of deglycosylation (CDDG) are a set of disorders which occur due to the defect in genes involved in deglycosylation pathways. The only known CDDG so far is the defect in ...
ORGANISM(S): Homo sapiens (Human) 
2023-05-10 | PXD034364 | Pride
GalNAc-T2 was identified as a novel antiviral factor that promotes viral clearance and contributes to reduced disease severity.This project aimed to investigate the impact of GalNAc-T2 overexpression on proteomics and glycoproteomics in lung cell. We employ SILAC labeling, lectin-based affinity enri...
ORGANISM(S): Homo sapiens (Human) 
2026-01-12 | PXD051101 | Pride
A bacterial antigen (Ag85B) was recombinantly expressed in Expi293 cells in which non-native N-glycosylation occured. We used glycoproteomics to characterize site-specific glycosylation across the surface of Ag85B as informed by glycomics data.
ORGANISM(S): Homo sapiens (Human) 
2026-05-25 | PXD077483 | Pride
Reanalysis of submissions PXD011533 and PXD009476 using MSFragger-Glyco mode. Processed MSFragger results files (pepXML) and PSM tables (psm.tsv) supporting MSFragger-Glyco manuscript (Fast and Comprehensive N- and O-glycoproteomics analysis with MSFragger-Glyco. Recent advances in methods for enric...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2020-10-06 | PXD021196 | Pride
We performed N-glycomics and glycoproteomics on a LARGE1dTM protein recombinantly expressed in HEK cells.
ORGANISM(S): Homo sapiens (Human) 
2025-08-21 | PXD060053 | Pride
Critical role for high multiplicity of protein N-linked glycans in neuron adhesion
ORGANISM(S): Mus musculus (Mouse) 
2018-10-16 | PXD009906 | Pride
Recent advances in software-driven glycopeptide identification in LC-MS/MS-based N-glycoproteomics have facilitated biochemical studies reporting thousands of intact N-glycopeptides, i.e. N-glycan-conjugated peptides, but the automated identification process remains to be scrutinized. Herein, we exp...
ORGANISM(S): Homo sapiens (Human) 
2016-08-17 | PXD004243 | Pride
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