The addition and removal of O-linked N-acetylglucosamine (O-GlcNAc) to and from the Ser
and Thr residues of proteins is an emerging post-translational modification. Unlike …

Despite the long held view that protein glycosylation occurs exclusively on extracellular or
lumenal polypeptides (1), it is clear that many nuclear and cytoplasmic proteins are multiply …

The posttranslational modification of serine and threonine residues of nuclear and
cytoplasmic proteins by the O-linked attachment of the monosaccharide β-N …

O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is
dynamically regulated in response to various environmental and biological stimuli. O …

O-GlcNAcylation is a common posttranslational modification of nucleocytoplasmic proteins
by β-N-acetylglucosamine (GlcNAc). The dynamic addition and removal of O-GlcNAc groups …

O-GlcNAcylation is a conserved post-translational modification that attaches N-acetyl
glucosamine (GlcNAc) to myriad cellular proteins. In response to nutritional and hormonal …

Post‐translational modification of protein serines/threonines with N‐acetylglucosamine (O‐
GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by …

Recent advances in the understanding of the molecular mechanisms underlying cancer
progression have led to the development of novel therapeutic targeting strategies. Aberrant …

O-GlcNAcylation is a posttranslational modification ruled by the activity of a single pair of
enzymes, O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA). These two enzymes carry …

β-O-linked N-acetylglucosamine (O-GlcNAc) is an abundant modification of cytosolic and
nuclear proteins that occurs in metazoans. O-GlcNAc is dynamically processed by a unique …