BACKGROUND: Since its discovery in the early 1980s, O-linked-β-N-acetylglucosamine (O-
GlcNAc), a single sugar modification on the hydroxyl group of serine or threonine residues …

The enzymes of O-GlcNAc cycling couple the nutrient-dependent synthesis of UDP-GlcNAc
to O-GlcNAc modification of Ser/Thr residues of key nuclear and cytoplasmic targets. This …

O-linked β-N-acetylglucosamine (O-GlcNAc) is a sugar attachment to serine or threonine
hydroxyl moieties on nuclear and cytoplasmic proteins. In many ways, O-GlcNAcylation is …

O-linked beta-N-acetylglucosamine (O-GlcNAc) modification of nuclear and cytoplasmic
proteins is important for many cellular processes, and the number of proteins that contain …

O-GlcNAc glycosylation (O-GlcNAcylation) corresponds to the addition of N-
acetylglucosamine on serine and threonine residues of cytosolic and nuclear proteins. O …

Cardiovascular function is regulated at multiple levels. Some of the most important aspects
of such regulation involve alterations in an ever-growing list of posttranslational …

Excess flux through the hexosamine biosynthesis pathway in adipocytes is a fundamental
cause of “glucose toxicity” and the development of insulin resistance that leads to type II …

OBJECTIVE O-linked β-N-acetylglucosamine (O-GlcNAc) plays an important role in the
development of insulin resistance and glucose toxicity. O-GlcNAcylation is regulated by O …

The post-translational modification of serine and threonine residues of nuclear and
cytoplasmic proteins by the O-linked attachment of the monosaccharide ß-N-acetyl …

A dynamic cycle of O-linked GlcNAc (O-GlcNAc) addition and removal is catalyzed by O-
GlcNAc transferase and O-GlcNAcase, respectively, in a process that serves as the final step …