The addition of O-linked-β-DN-acetylglucosamine (O-GlcNAc) onto serine and threonine
residues of nuclear and cytoplasmic proteins is an abundant, unique post-translational …

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 …

Abstract Over the past 35 years,~ 1700 articles have characterized protein O-GlcNAcylation.
Found in almost all living organisms, this post-translational modification of serine and …

Cellular response to environmental, physiological, or chemical stress is key to survival
following injury or disease. Here we describe a unique signaling mechanism by which cells …

From the extracellular matrix to the cytoskeleton, a network of molecular links connects cells
to their environment. Molecules in this network transmit and detect mechanical forces, which …

A dynamic cycle of addition and removal of O-linked N-acetylglucosamine (O-GlcNAc) at
serine and threonine residues is emerging as a key regulator of nuclear and cytoplasmic …

Myriad nuclear and cytoplasmic proteins in metazoans are modified on Ser and Thr residues
by the monosaccharide O-linked β-N-acetylglucosamine (O-GlcNAc). The rapid and …

An increasing body of evidence points to a central regulatory role for glucose in mediating
cellular processes and expands the role of glucose well beyond its traditional role (s) in …

The abundant and dynamic post-translational modification of nuclear and cytosolic proteins
by β-O-linked N-acetylglucosamine (O-GlcNAc) is catalyzed by O-GlcNAc-transferase (OGT) …

Both phosphorylation and O-GlcNAc glycosylation posttranslationally modify microtubule-
associated Tau proteins. Whereas the hyperphosphorylation of these proteins that occurs in …