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 …

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 …

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

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 addition of the monosaccharide β-N-acetyl-d-glucosamine to proteins (O-GlcNAc
glycosylation) is an intracellular, post-translational modification that shares features with …

O-GlcNAc is a widespread dynamic carbohydrate modification of cytosolic and nuclear
proteins with features analogous to phosphorylation. O-GlcNAc acts critically in many …

Abstract Skeletal muscle makes up 30–40% of the total body mass. It is of great significance
in maintaining digestion, inhaling and exhaling, sustaining body posture, exercising …

The covalent modification of intracellular proteins by O-linked β-N-acetylglucosamine (O-
GlcNAc) is emerging as a crucial regulatory posttranslational modification akin to …

Increased nuclear protein O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation)
mediated by high glucose treatment or the hyperglycemia of diabetes mellitus contributes to …

Meat quality plays an important role in the purchase decision of consumers, affecting
producers and retailers. The formation mechanisms determining meat quality are intricate …