Polypeptide N-acetylgalactosaminyltransferase 2

[1]. Monica Zilmer, et al. Novel congenital disorder of O-linked glycosylation caused by GALNT2 loss of function. Brain. 2020 Apr 1;143(4):1114-1126. [Content Brief]

[2]. Sumeet A Khetarpal, et al. Loss of Function of GALNT2 Lowers High-Density Lipoproteins in Humans, Nonhuman Primates, and Rodents. Cell Metab. 2016 Aug 9;24(2):234-45. [Content Brief]

[3]. Erandi Lira-Navarrete, et al. Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation. Nat Commun. 2015 May 5;6:6937. [Content Brief]

[4]. T White, et al. Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. J Biol Chem. 1995 Oct 13;270(41):24156-65. [Content Brief]

[5]. Timothy A Fritz, et al. Dynamic association between the catalytic and lectin domains of human UDP-GalNAc:polypeptide alpha-N-acetylgalactosaminyltransferase-2. J Biol Chem. 2006 Mar 31;281(13):8613-9. [Content Brief]

[6]. H H Wandall, et al. Substrate specificities of three members of the human UDP-N-acetyl-alpha-D-galactosamine:Polypeptide N-acetylgalactosaminyltransferase family, GalNAc-T1, -T2, and -T3. J Biol Chem. 1997 Sep 19;272(38):23503-14. [Content Brief]

[7]. Hiroko Iwasaki, et al. Initiation of O-glycan synthesis in IgA1 hinge region is determined by a single enzyme, UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 2. J Biol Chem. 2003 Feb 21;278(8):5613-21. [Content Brief]