PARP inhibition: PARP1 and beyond

Nat Rev Cancer. 2010 Apr;10(4):293-301. doi: 10.1038/nrc2812. Epub 2010 Mar 4.

Abstract

Recent findings have thrust poly(ADP-ribose) polymerases (PARPs) into the limelight as potential chemotherapeutic targets. To provide a framework for understanding these recent observations, we review what is known about the structures and functions of the family of PARP enzymes, and then outline a series of questions that should be addressed to guide the rational development of PARP inhibitors as anticancer agents.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Antineoplastic Agents / therapeutic use
  • Cell Death
  • DNA Damage
  • DNA, Neoplasm / genetics
  • Dacarbazine / analogs & derivatives
  • Dacarbazine / therapeutic use
  • Deoxycytidine / analogs & derivatives
  • Deoxycytidine / therapeutic use
  • Humans
  • Kinetics
  • Mice
  • Neoplasms / enzymology
  • Neoplasms / pathology
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerase Inhibitors
  • Poly(ADP-ribose) Polymerases / genetics
  • Poly(ADP-ribose) Polymerases / metabolism
  • Poly(ADP-ribose) Polymerases / therapeutic use*
  • Substrate Specificity
  • Temozolomide

Substances

  • Antineoplastic Agents
  • DNA, Neoplasm
  • Poly(ADP-ribose) Polymerase Inhibitors
  • Deoxycytidine
  • Dacarbazine
  • gemcitabine
  • PARP1 protein, human
  • Poly (ADP-Ribose) Polymerase-1
  • Poly(ADP-ribose) Polymerases
  • Temozolomide