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Inhibitors and activators of ADP-ribosylation reactions

  • Chapter
ADP-Ribosylation: Metabolic Effects and Regulatory Functions

Part of the book series: Developments in Molecular and Cellular Biochemistry ((DMCB,volume 12))

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Abstract

ADP-ribosylation reaction, that is the transfer of the ADP-ribose moiety of NAD+ to acceptor protein, is catalyzed by two classes of ADP-ribosyltransferases, i.e., poly(ADP-ribose) synthetase and mono(ADP-ribosyl)transferases. These two types differ not only in the number of transferring ADP-ribose units but also in the acceptor amino acid(s) and protein. Their inhibitors, particularly those of poly(ADP-ribose) synthetase, have been successfully employed in studies on biological functions of the enzymes and other related fields of research. Recently, we found many potent and specific inhibitors of poly(ADP-ribose) synthetase, and broadened their chemical as well as biochemical variety. More recently, we found several potent inhibitors of arginine-specific mono(ADP-ribosyl)transferases and activators of poly(ADP-ribose) synthetase. (Mol Cell Biochem 138: 185–197, 1994)

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Authors and Affiliations

  1. Department of Clinical Science and Laboratory Medicine, Kyoto University Faculty of Medicine, Shogoin, Sakyo-ku, Kyoto, 606-01, Japan

    Marek Banasik & Kunihiro Ueda

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  1. Marek Banasik
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  2. Kunihiro Ueda
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Editors and Affiliations

  1. Laboratory of Cellular Metabolism, National Heart, Lung and Blood Institute, NIH, Building 10, Room 5N-307, Bethesda, MD, 20892, USA

    Joel Moss

  2. Division of Cardiovascular Sciences, St. Boniface General Hospital Research Center, 351 Tache Avenue, Winnipeg, MB, R2H 2A6, Canada

    Peter Zahradka

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© 1994 Springer Science+Business Media Dordrecht

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Banasik, M., Ueda, K. (1994). Inhibitors and activators of ADP-ribosylation reactions. In: Moss, J., Zahradka, P. (eds) ADP-Ribosylation: Metabolic Effects and Regulatory Functions. Developments in Molecular and Cellular Biochemistry, vol 12. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2614-8_25

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  • DOI: https://doi.org/10.1007/978-1-4615-2614-8_25

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