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

Metabolic rewiring and epigenetic remodeling, which are closely linked and reciprocally
regulate each other, are among the well-known cancer hallmarks. Recent evidence …

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 …

The physiological identity of every cell is maintained by highly specific transcriptional
networks that establish a coherent molecular program that is in tune with nutritional …

Unlike the complex glycans decorating the cell surface, the O-linked β-N-acetyl glucosamine
(O-GlcNAc) modification is a simple intracellular Ser/Thr-linked monosaccharide that is …

A major mechanism regulating the accessibility and function of eukaryotic genomes are the
covalent modifications to DNA and histone proteins that dependably package our genetic …

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 …

The smallest viable unit of life is the cell. From bacteria to mammals, all cells use the same
nucleic acid-based universal code for the maintenance and inheritance of genetic …