Glycans are involved in numerous biological recognition events. Being secondary gene
products, their labeling by genetic methods–comparable to GFP labeling of proteins–is not …

Despite advances in genetic and proteomic techniques, a complete portrait of the proteome
and its complement of dynamic interactions and modifications remains a lofty, and as of yet …

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

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

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 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 …

The surging development of bioorthogonal chemistry has profoundly transformed chemical
biology over the last two decades. Involving chemical partners that specifically react together …

Cellular carbohydrates or glycans are critical mediators of biological function. Their
remarkably diverse structures and varied activities present exciting opportunities for …

The unexpected, non‐enzymatic S‐glycosylation of cysteine residues in various proteins by
per‐O‐acetylated monosaccharides is described. This artificial S‐glycosylation greatly …

Protein glycosylation is a heterogeneous post-translational modification (PTM) that plays an
essential role in biological regulation. However, the diversity found in glycoproteins has …