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ProteomicsA “Two birds One Stone” Strategy for Site-specific Analysis of the Core Fucosylation and O-GlcNAcylation
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 |
ProteomicsA “One-step” Strategy for the Global Characterization of Core-Fucosylated Glycoproteome
Core fucosylation, a special type of N-linked glycosylation, is important in tumor proliferation, invasion, metastatic potential, and therapy resistance. However, the core-fucosylated glycoproteome has not been extensively profiled due to the low abundance and poor ionization efficiency of glycosyla...
ORGANISM(S): Homo Sapiens 
PXD051139 |
ProteomicsA Sensitive and Reversible Labeling Strategy Enables Global Mapping of the Core-Fucosylated Glycoproteome on Cell Surfaces
Core fucosylation, the attachment of α1,6-fucose to the innermost GlcNAc residue of N-glycans, is a unique protein glycosylation in living organisms. It plays significant roles in diverse physiological and pathological processes, and its upregulation has been observed in many cancers. Core fucosylat...
ORGANISM(S): Homo Sapiens 
2022-08-13 | PXD036051 |
ProteomicsDecoding protein glycosylation by an integrative mass spectrometry-based de novo sequencing strategy
Glycoprotein is one of the most complex biomacromolecule，accounting for over 50% of total human proteins and the majority of biopharmaceuticals, exerting profound influences on various essential biological processes. With multiple N-glycosylation sites and O- glycosylation sites on the protein backb...
ORGANISM(S): Homo Sapiens Bos Taurus 
PXD055221 |
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 |
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