Protein glycosylation involves the co-translational or post-translational addition of glycans to
proteins and is a crucial protein modification in health and disease. The aim of …

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 …

RNA modification is a dynamic and reversible process regulated by a series of writers,
erasers and readers (WERs). Abnormal changes of WERs will disrupt the RNA modification …

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 …

Itaconate has been recently recognized as an anti-inflammatory metabolite involved in the
pathogen–macrophage interface. Due to its weak electrophilicity, itaconate could modify …

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 …

Liquid–liquid phase separation (LLPS) of SynGAP and PSD-95, two abundant proteins that
interact in the postsynaptic density (PSD) of neurons, has been implicated in modulating …

Dysregulated translation is a common feature of cancer. Uncovering its governing factors
and underlying mechanism are important for cancer therapy. Here, we report that enhancer …

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

Unnatural monosaccharides such as azidosugars that can be metabolically incorporated
into cellular glycans are currently used as a major tool for glycan imaging and …