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

Glycosylation is a prevalent, yet heterogeneous modification with a broad range of
implications in molecular biology. This heterogeneity precludes enrichment strategies that …

Altered metabolism and deregulated cellular energetics are now considered a hallmark of
all cancers. Glucose, glutamine, fatty acids, and amino acids are the primary drivers of tumor …

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

Streptavidin and its homologs (together referred to as streptavidin) are widely used in
molecular science owing to their highly selective and stable interaction with biotin. Other …

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 …

Several mechanisms have been proposed for histone marks to exert their functions,
including altering the physical properties of nucleosomes by neutralization of charge via …

Accurate quantification of protein expression in biological systems is an increasingly
important part of proteomics research. Incorporation of differential stable isotopes in samples …

Chemical tools have accelerated progress in glycoscience, reducing experimental barriers
to studying protein glycosylation, the most widespread and complex form of posttranslational …

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