Inhibitors and activators of ADP-ribosylation reactions |
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Authors: | Marek Banasik Kunihiro Ueda |
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Affiliation: | (1) Department of Clinical Science and Laboratory Medicine, Kyoto University Faculty of Medicine, Shogoin, Sakyo-ku, 606-01 Kyoto, Japan |
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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 in hibitors, 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. |
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Keywords: | inhibitor activator poly(ADP-ribose) synthetase mono(ADP-ribosyl)transferase |
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