Site-specific protein O-glycosylation modulates proprotein processing — Deciphering specific functions of the large polypeptide GalNAc-transferase gene family - Schjoldager, Katrine T.-B.G.; Clausen, Henrik (Biochimica et biophysica acta, 2012)
Keywords: Amino Acid Sequence; biosynthesis; Congenital disorder of glycosylation (CDG); Fibroblast Growth Factor-23; GalNAc-transferase (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase); gene expression regulation; gene targeting; genes; Glycoproteins - metabolism; Glycosylation; human cell lines; human diseases; Humans; lipid metabolism; Molecular Sequence Data; Multigene Family; N-Acetylgalactosaminyltransferases - genetics; N-Acetylgalactosaminyltransferases - metabolism; O-glycosylation; phenotype; Polypeptide N-acetylgalactosaminyltransferase; polypeptides; post-translational modification; Pro-protein convertase (PC) processing; Proprotein Convertases - metabolism; Protein Processing, Post-Translational; proteinases; proteins; proteolysis; zinc finger motif; Zinc finger nuclease gene targeting; Congenital disorder of glycosylation (CDG); O-glycosylation; GalNAc-transferase (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase); Zinc finger nuclease gene targeting; Pro-protein convertase (PC) processing