Glycosylation, and especially O-linked glycosylation, remains a critical blind spot in the
understanding of post-translational modifications. Due to their nature as proteins defined by …

Natural biopolymers have inspired the development of synthetic analogues that can adopt
defined conformations and assemble into 3D architectures. These compounds are mainly …

Sugar nucleotides are essential glycosylation donors in the carbohydrate metabolism.
Naturally, most sugar nucleotides are derived from a limited number of common sugar …

Sugar nucleotide-dependent glycosyltransferases (GTs) are key enzymes that catalyze the
formation of glycosidic bonds in nature. They have been increasingly applied in the …

Core fucosylation and O-GlcNAcylation are the two most famous protein glycosylation
modifications that regulate diverse physiological and pathological processes in living …

Chemical synthesis of insulin superfamily proteins (ISPs) has recently been widely studied
to develop next‐generation drugs. Separate synthesis of multiple peptide fragments and …

Glycosylation of proteins is a complicated post-translational modification. Despite the
significant progress in glycoproteomics, accurate functions of glycoproteins are still …

Highlights•Automated platform for chemoenzymatic synthesis enables rapid preparation of
glycans and glycopeptides with diverse carbohydrate structures.•Synthetic glycoproteins …

Glycosylation is catalyzed by glycosyltransferases using sugar nucleotides or occasionally
lipid‐linked phosphosugars as donors. However, only very few common sugar nucleotides …

The synthesis of defined oligosaccharides is a complex task. Several enabling technologies
have been introduced in the last two decades to facilitate synthetic access to these valuable …