O-linked N-acetyl-β-d-glucosamine (O-GlcNAc) is a ubiquitous and dynamic post-
translational modification known to modify over 3,000 nuclear, cytoplasmic, and …

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

In the mid-1980s, the identification of serine and threonine residues on nuclear and
cytoplasmic proteins modified by a N-acetylglucosamine moiety (O-GlcNAc) via an O …

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 modification of nuclear, mitochondrial, and cytosolic proteins by O-linked βN-
acetylglucosamine (O-GlcNAc) has emerged as a dynamic and essential post-translational …

This chapter presents an overview of the dynamic modification of serine or threonine
hydroxyl moieties on nuclear, mitochondrial, and cytoplasmic proteins by O-linked β-N …

O-GlcNAcylation is the addition of β-DN-acetylglucosamine to serine or threonine residues
of nuclear and cytoplasmic proteins. O-linked N-acetylglucosamine (O-GlcNAc) was not …

In the 30 years, since the discovery of nucleocytoplasmic glycosylation, O-GlcNAc has been
implicated in regulating cellular processes as diverse as protein folding, localization …

Hundreds of nuclear, cytoplasmic, and mitochondrial proteins within multicellular eukaryotes
have hydroxyl groups of specific serine and threonine residues modified by the …

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 …