Mucin type O‐glycosylation is one of the most diverse types of glycosylation, playing
essential roles in tissue development and homeostasis. In complex organisms, O‐GalNAc …

O-glycosylation is a highly frequent post-translation modification of proteins, with important
functional implications in both physiological and disease contexts. The biosynthesis of O …

Proteins and lipids decorated with glycans are found throughout biological entities, playing
roles in biological functions and dysfunctions. Current analytical strategies for these glycan …

Glycosylation of proteins is an essential process in all eukaryotes and a great diversity in
types of protein glycosylation exists in animals, plants and microorganisms. Mucin-type O …

The structural diversity of glycans on cells—the glycome—is vast and complex to decipher.
Glycan arrays display oligosaccharides and are used to report glycan hapten binding …

Glycosylation is one of the most prevalent posttranslational modifications that profoundly
affects the structure and functions of proteins in a wide variety of biological recognition …

N-acetylgalactosaminyl-transferases (GalNAc-Ts) initiate mucin-type O-glycosylation, an
abundant and complex posttranslational modification that regulates host-microbe …

Mucins are a large family of heavily O-glycosylated proteins that cover all mucosal surfaces
and constitute the major macromolecules in most body fluids. Mucins are primarily defined …

Glycosylation is a very common modification of protein and lipid, and most glycosylation
reactions occur in the Golgi. Although the transfer of initial sugar (s) to glycoproteins or …

Glycoconjugates constitute a major class of biomolecules which include glycoproteins,
glycosphingolipids and proteoglycans. Glycans are involved in several physiological and …