Protein O-linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) is a
unique monosaccharide modification discovered in the early 1980s. With the technological …

Glycosylation is catalyzed by various glycosyltransferase enzymes which are mostly located
in the Golgi apparatus in cells. These enzymes glycosylate various complex carbohydrates …

Glycoproteins are decorated with complex glycans for protein functions. However, regulation
mechanisms of complex glycan biosynthesis are largely unclear. Here we found that …

N-glycan, a fundamental and versatile protein modification in mammals, plays critical roles
in various physiological and pathological events including cancer progression. The …

Mucosal T lymphocytes from patients with ulcerative colitis (UC) were previously shown to
display a deficiency in branched N-glycosylation associated with disease severity. However …

Cancer stem cells (CSCs) represent a small subpopulation of self-renewing oncogenic cells.
As in many other stem cells, metabolic reprogramming has been implicated to be a key …

Fucosylation is a glycan modification critically involved in cancer and inflammation. Although
potent fucosylation inhibitors are useful for basic and clinical research, only a few inhibitors …

Synthetic sugar analogs are widely applied in metabolic oligosaccharide engineering (MOE)
and as novel drugs to interfere with glycoconjugate biosynthesis. However, mechanistic …

Mannose in N-glycans is derived from glucose through phosphomannose isomerase (MPI,
Fru-6-P↔ Man-6-P) whose deficiency causes a congenital disorder of glycosylation (CDG) …

Elevated O-GlcNAcylation is emerging as a general characteristic of most cancers. Although
O-GlcNAcylation can regulate many cell biological pathways, recent evidence suggests that …