Core fucosylation, the attachment of α1, 6‐fucose to the innermost N‐acetylglucosamine
(GlcNAc) residue of N‐glycans, has a strong relationship with tumor growth, invasion …

Core fucosylation of N-linked glycoproteins has been linked to the functions of glycoproteins
in physiological and pathological processes. However, quantitative characterization of core …

Dysregulation of protein core-fucosylation plays a pivotal role in the onset, progression, and
immunosuppression of cancer. However, analyzing core-fucosylation, especially the …

Glycosylation modifications of proteins have been attracting increasing attention due to their
roles in the physiological and pathological processes of the cell. Core fucosylation (CF), one …

Abstract Alpha-1, 6 fucosylation of N-glycans (core fucosylation, CF) represents a unique
form of N-glycans and is widely involved in disease progression. In order to accurately …

Core fucosylation and O-GlcNAcylation are the two most famous protein glycosylation
modifications that regulate diverse physiological and pathological processes in living …

Core fucosylation, a special type of N-linked glycosylation, is important in tumor proliferation,
invasion, metastatic potential, and therapy resistance. However, the core-fucosylated …

The core fucosylation (CF) of N-glycoproteins plays important roles in regulating protein
functions during biological development, and it has also been shown to be up-regulated in …

In cancers, increased fucosylation (attachment of fucose sugar residues) on cell-surface
glycans, resulting from the abnormal upregulation of the expression of specific …

Fucosylation is an important feature of protein N-glycosylation as it has been reported to
influence the efficacy of therapeutic proteins and as a potential disease biomarker. A …