By Dr. Felix R. Althaus, Dr. Christoph Richter (auth.)

ISBN-10: 3642830773

ISBN-13: 9783642830778

ISBN-10: 364283079X

ISBN-13: 9783642830792

In 1966, a paper entitled "On the formation of a singular adenylylic compound by means of enzymatic extracts of liver nuclei" from Paul Mandel's laboratory in Strasbourg, France, planted the seed for a quickly growing to be new box of organic learn targeting ADP-ribosylation reactions. the advance of this box over the last 2 a long time displays a great deal a contemporary development of organic examine. As extra precise wisdom accumulates, enigmatic phenomena develop into ideas which create their very own enigmata. This strategy has a tendency to prefer the improvement of a number of, likely disconnected, examine traces till simplicity emerges from chaos and unifying suggestions replacement for controversy. it seems that the sector of ADP-ribosylation reactions has now not but attained this latter level. for instance, with the id of 2 assorted sessions of ADP-ribosylation reactions, i.e., mono-ADP-ribosyla­ tion and poly-ADP-ribosylation reactions, the sphere break up very early into separate branches of analysis. With the current quantity, we've got divided the duty of reviewing those periods of ADP­ ribosylation hence, even though their coexistence in eukaryotes may perhaps contain a better useful linkage than hitherto recognized.

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Additional resources for ADP-Ribosylation of Proteins: Enzymology and Biological Significance

Example text

A large number of inhibitors have become known in the past 2 decades, but real excitement for the use of the "inhibitor approach" was prompted by the report of Purnell and Whish (1980 a) showing that substituted benzamides are potent inhibitors of poly(ADP-ribose) synthetase with a Ki of less than 2 ~M. These authors concluded that 3-aminobenzamide and 3-methoxybenzamide are physiologically specific inhibitors of this enzyme and therefore ... "will be extremely valuable as probes for use as inhibitors ofpoly(ADP-ribose) synthetase in vivo".

B All compounds were tested at a concentration of 2 mM, except for theobromine which was tested at 1 mM. C The inhibition is expressed as percent of the poly(ADP-ribose)polymerase activity of untreated control cells; the values are derived from mean values of duplicate or triplicate assays. Poly(ADP-ribose)polymerase activities were measured in nucleotide-permeable human lymphocytes following 3 days of stimulation with 2 ~g/ml L-phytohemagglutinin. For details of assay conditions see Berger et al.

Nucleic Acid Res 1: 1317-1327 Neuer B, Werner D (1985) Screening of isolated DNA for sequences released from anchorage sites in nuclear matrix. J Mol Bioi 181 :15-25 Niedergang C, Okazaki H, Mandel P (1979) Properties of purified calf thymus poly(adenosine diphosphate ribose) polymerase. Eur J Biochem 102:43-57 Nishikimi M, Ogasawara K, Kameshita I, Taniguchi T, Shizuta Y (1982) Poly(ADP-ribose) synthetase. The DNA binding domain and the automodification domain. J Bioi Chern 257:6102-6105 Nishizuka Y, Veda K, Nakazawa K, Hayaishi 0 (1967) Studies on the polymer of adenosine diphosphate ribose.

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ADP-Ribosylation of Proteins: Enzymology and Biological Significance by Dr. Felix R. Althaus, Dr. Christoph Richter (auth.)


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