O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) catalyze the dynamic cycling of
intracellular, post-translational O-GlcNAc modification on thousands of Ser/Thr residues of …

O-GlcNAcylation—the attachment of O-linked N-acetylglucosamine (O-GlcNAc) moieties to
cytoplasmic, nuclear and mitochondrial proteins—is a post-translational modification that …

O-GlcNAcylation is an important posttranslational modification governed by a single pair of
enzymes–O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). These two enzymes …

O-GlcNAcylation is a protein posttranslational modification that results in the addition of O-
GlcNAc to Ser/Thr residues. Since its discovery in the 1980s, it has been shown to play an …

Unlike the complex glycans decorating the cell surface, the O-linked β-N-acetyl glucosamine
(O-GlcNAc) modification is a simple intracellular Ser/Thr-linked monosaccharide that is …

Protein O-GlcNAcylation is a dynamic post-translational modification involving the
attachment of N-acetylglucosamine (GlcNAc) to the hydroxyl groups of Ser/Thr residues on …

The addition of N-acetylglucosamine (GlcNAc) O-linked to serine and threonine residues of
proteins is known as O-GlcNAc. This post-translational modification is found within …

O-GlcNAc is an abundant post-translational modification found on nuclear and cytoplasmic
proteins in all metazoans. This modification regulates a wide variety of cellular processes …

Modifications of nuclear and cytoplasmic proteins with a single sugar, N‐acetylglucosamine
(GlcNAc), play roles in a wide variety of fundamental cellular processes, and aberrant O …

The O-linked N-acetylglucosamine (O-GlcNAc) post-translational modification (O-
GlcNAcylation) is the dynamic and reversible attachment of N-acetylglucosamine to serine …