Glycosylation is catalyzed by various glycosyltransferase enzymes which are mostly located
in the Golgi apparatus in cells. These enzymes glycosylate various complex carbohydrates …

Glycosylation is one of the most common post‐translational modification reactions and
nearly half of all known proteins in eukaryotes are glycosylated. In fact, changes in …

Removal of the fucose residue from the N‐glycans of the Fc portion of immunoglobulin G
(IgG) results in a dramatic enhancement of antibody‐dependent cellular cytotoxicity (ADCC) …

The β‐site amyloid precursor protein cleaving enzyme‐1 (BACE 1), an essential protease for
the generation of amyloid‐β (Aβ) peptide, is a major drug target for Alzheimer's disease …

Chronic liver diseases are a serious health problem worldwide. The current gold standard to
assess structural liver damage is through a liver biopsy which has several disadvantages. A …

Among the various posttranslational modification reactions, glycosylation is the most
common, and nearly 50% of all known proteins are thought to be glycosylated. In particular …

Glycosylation is one of the most common post‐translational modifications, and
approximately 50% of all proteins are presumed to be glycosylated in eukaryotes. Branched …

Glycan structures covalently attached to proteins and lipids play numerous roles in
mammalian cells, including protein folding, targeting, recognition, and adhesion at the …

BACKGROUND: Cell migration is an essential process in organ homeostasis, in
inflammation, and also in metastasis, the main cause of death from cancer. The extracellular …

Glycosylation changes are key molecular events in tumorigenesis, progression and
glycosyltransferases play a vital role in the this process. FUT8 belongs to the …