O-linked β-N-actylglucosamine (O-GlcNAc) is a carbohydrate post-translational modification
on hydroxyl groups of serine and/or threonine residues of cytosolic and nuclear proteins. …

Simple Summary O-linked β-N-acetylglucosamine (O-GlcNAc) is a post-translational modification
(PTM) linking nutrient flux through the hexosamine biosynthetic pathway (HBP) to gene …

The covalent attachment of β-DN-acetylglucosamine monosaccharides (O-GlcNAc) to serine/threonine
residues of nuclear and cytoplasmic proteins is a major regulatory mechanism in …

O-GlcNAcylation is a dynamic post-translational modification consisting of the addition of a
single N-acetylglucosamine sugar to serine and threonine residues in proteins by the enzyme …

Simple Summary Dynamic O-GlcNAc modification regulates the functions of proteins in a
broad range of cellular processes. Dysregulation of the sole enzymes responsible for O-…

Increasing glucose consumption is thought to provide an evolutionary advantage to cancer
cells. Alteration of glucose metabolism in cancer influences various important metabolic …

Cancer cells exhibit increased uptake of glucose and glutamine, and rewire the metabolic
flux toward anabolic pathways important for cell growth and proliferation. Understanding how …

O-GlcNAcylation is an O-linked β-N-acetylglucosamine (O-GlcNAc) moiety linked to the
serine or threonine residues in proteins. O-GlcNAcylation is a dynamic post-translational …

A reversible post-translational protein modification which involves addition of N-acetylglucosamine
(GlcNAc) onto hydroxyl groups of serine and/or threonine residues which is known as …

… ), IKB kinase (Kawauchi, Araki et al. 2009), c-Myc (Chou, Dang et al. 1995), and Snail (Park,
Kim et al. 2010) are regulated by O-GlcNAcylation, yet the role of OGlcNAc in cancer biology …