Functional Regulation of p53 by Covalent Poly ADP-Ribosyl ation

There is no question that the biochemical and enzymatic characterization of p53-(PARP-l) protein complexes as well as the unequivocal identification of the amino acid acceptor sites for p53-poly(ADP-ribosyl)ation with, for example, deoxy analogs of PNAD under standard reaction conditions of poly(ADP-ribosyl)ation, should help clarify the intricacies of the molecular interactions between these two primordial DNA-damage sensors. [Pg.64]

Further studies with PARP-1 and p53 mutant forms, as well as PARP-2, should fully unveil the molecular details of the role of p53-poly(ADP-ribosyl)ation in genomic stability as well as their functional relationship and interdependence in health and disease (oncogenesis). [Pg.65]

Vogelstein B, Lane D, Levine AJ. Surfing the p53 network. Nature 2000 408 307-310. [Pg.65]

Hainaut P, Hollstein M. p53 and human cancer The first ten thousand mutations. Adv Cancer Res 2000 77 81-137. [Pg.65]

Reed M, Woelker B, Wang P et al. The C-terminal domain of p53 recognizes DNA damaged by ionizii radiation. Ptoc Natl Acad Sci USA 1995 92 9455-9459. [Pg.65]

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