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 …

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

Glycoproteins with O-glycosidically linked carbohydrate chains of complex structures and
functions are found in secretions and on the cell surfaces of cancer cells. The structures of O …

Mucin-type linkages (GalNAcα1-O-Ser/Thr) are initiated by a family of glycosyltransferases
known as the UDP-N-acetylgalactosamine: polypeptide N-acetylgalactosaminyltransferases …

Mutations in the gene encoding the glycosyltransferase polypeptide GalNAc-T3, which is
involved in initiation of O-glycosylation, were recently identified as a cause of the rare …

BACKGROUND: Posttranslational modifications (PTMs) greatly expand the function and
regulation of proteins, and glycosylation is the most abundant and diverse PTM. Of the many …

Mucin-type O-linked glycosylation is a fundamental post-translational modification that is
involved in a variety of important biological processes. However, the lack of chemical tools to …

Mucin-type O-glycans are found on mucins as well as many other glycoproteins. The
initiation step in synthesis is catalyzed by a large family of polypeptide GalNAc-transferases …

Background While the underlying causes of cancer are genetic modifications, changes in
cellular states mediate cancer development. Tumor cells display markedly changed …

The MUC1 mucin represents a prime target antigen for cancer immunotherapy because it is
abundantly expressed and aberrantly glycosylated in carcinomas. Attempts to generate …