In the early 1980s, while using purified glycosyltransferases to probe glycan structures on
surfaces of living cells in the murine immune system, we discovered a novel form of …

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 …

Protein O-linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) is a
unique monosaccharide modification discovered in the early 1980s. With the technological …

Post-translational modification with O-linked β-N-acetylglucosamine (O-GlcNAc), a process
referred to as O-GlcNAcylation, occurs on a vast variety of proteins. Mounting evidence in …

Diabetes mellitus increases the risk of heart failure independent of co-existing hypertension
and coronary artery disease. Although several molecular mechanisms for the development …

Alterations in glucose and glutamine utilizing pathways and in fatty acid metabolism are
currently considered the most significant and prevalent metabolic changes observed in …

O-linked β-N-acetylglucosamine (O-GlcNAc) is a post-translational modification (ie, O-
GlcNAcylation) on the serine/threonine residues of proteins. As a unique intracellular …

O-GlcNAcylation, a dynamic nutrient and stress sensitive post-translational modification,
occurs on myriad proteins in the cell nucleus, cytoplasm and mitochondria. O-GlcNAcylation …

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

Background: Heart failure is a leading cause of death worldwide and is associated with the
rising prevalence of obesity, hypertension, and diabetes. O-GlcNAcylation (the attachment of …