Biochemical and Biophysical Research Communications
Volume 175, Issue 2, 15 March 1991, Pages 668-672
Synthesis of a new inhibitor of the UDP-GalNAc: Polypeptide galactosaminyl transferase
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Cited by (7)
Selective inhibition of glycosyltransferases by bivalent imidazolium salts
2013, Bioorganic and Medicinal ChemistryCitation Excerpt :The activity of purified bovine polypeptide GalNAc-transferase 1, using AQPTPPP as the acceptor peptide,19 was strongly inhibited by 24 (Table 2). A previously described inhibitor of this activity was nucleotide sugar-based and also contained an aliphatic chain.20 In comparison, another O-glycan synthesis inhibitor, GalNAcα-Bn, is a competitive substrate and only blocks the extension of O-glycans after GalNAc has been added to Ser/Thr.
Chemical regulation of glycosylation processes
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Present address: Department of Biomolecular Engineering, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama 227, Japan.
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Present address: Department of Biochemistry and Molecular Biology, University of Arkansas for Medical Sciences, 4301 W. Markham, Little Rock, AR 72205-7199.
Copyright © 1991 Published by Elsevier Inc.