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PARP-2: Structure-Function Relationship

Authors :
Patrick Stiegler
Valérie Schreiber
Vincent Favaudon
Laure Sabatier
Véronique Meder
Jean-Christophe Amé
Françoise Dantzer
Gilbert de Murcia
Michelle Ricoul
Claude Niedergang
Catherine Spenlehauer
Josiane Ménissier-de Murcia
Source :
Poly(ADP-Ribosyl)ation ISBN: 9780387333717
Publication Year :
2006
Publisher :
Springer US, 2006.

Abstract

Poly(ADP-ribosyl)ation is an immediate DNA damage-dependent posttranslational modification of histones and other nuclear proteins that contributes to the survival of injured proliferating cells. Poly(ADP-ribose) polymerases (PARPs) now constitute a large family of 18 proteins, encoded by different genes and displaying a conserved catalytic domain in which PARP-1 (113 kDa), the founding member, and PARP-2 (62 kDa) are so far the sole enzymes whose catalytic activity is immediately stimulated by DNA strand-breaks. This review summarizes our present knowledge of the structure and function of PARP-2, the closest relative to PARP-1.

Details

ISBN :
978-0-387-33371-7
ISBNs :
9780387333717
Database :
OpenAIRE
Journal :
Poly(ADP-Ribosyl)ation ISBN: 9780387333717
Accession number :
edsair.doi...........573c919db1a8b931f944f3be5931dc12
Full Text :
https://doi.org/10.1007/0-387-36005-0_2