Glycosylation is the most ubiquitous post-translational modification in eukaryotes. N-glycan
is attached to nascent glycoproteins and is processed and matured by various glycosidases …

L-Fucose-containing glycoconjugates are essential for a myriad of physiological and
pathological activities, such as inflammation, bacterial and viral infections, tumor metastasis …

Protein O-fucosylation is an essential post-translational modification, involved in the folding
of target proteins and in the role of these target proteins during embryonic development and …

Bacterial glycosyltransferases (GT) often synthesize the same glycan linkages as
mammalian GT; yet, they usually have very little sequence identity. Nevertheless, enzymatic …

Mammalian Asn-linked glycans are extensively processed as they transit the secretory
pathway to generate diverse glycans on cell surface and secreted glycoproteins. Additional …

Protein O‐fucosylation is a post‐translational modification found on serine/threonine
residues of thrombospondin type 1 repeats (TSR). The fucose transfer is catalysed by the …

Several in the field—and many outside—consider that solving the three-dimensional
structures of more glycoside hydrolases (GHs) and glycosyltransferases (GTs) confines to …

The plant cell wall is a complex and dynamic network made mostly of cellulose,
hemicelluloses, and pectins. Xyloglucan, the major hemicellulosic component in …

Escherichia coli O86 possesses high human blood group B activity because of its O-antigen
structure, sharing the human blood group B epitope. In this study, the wbwK gene of E. coli …

Lewis x (Lex) and sialyl Lewis x (SLex)-containing glycans play important roles in numerous
physiological and pathological processes. The key enzyme for the final step formation of …