PARP
Poly (ADP-ribose) polymerases (PARPs) is a large family of proteins with a conserved catalytic domain that catalyze an immediate DNA-damage-dependent post-translational modification of histones and other nuclear proteins leading to the survival of injured proliferating cells. So far, a total number of 18 human PARP proteins encoded by different genes have been identified, including PARP-1 to PARP-4, PARP-5a, PARP-5b, PARP-5c and PARP-6 to PARP-16. The general structural of PARP proteins has been revealed through the extensive study of the founding family member PARP-1, which is characterized by the presence of four functional domains, including a DNA-binding domain, a caspase-cleaved domain, an automodification domain and a catalytic domain.
- A8893 Rucaparib (free base)Target: PARPSummary: Potent PARP inhibitor
- A3002 ABT-888 (Veliparib)6 CitationSummary: Potent PARP inhibitor
- A4153 BMN 673Summary: Potent PARP inhibitor
- A4154 Olaparib (AZD2281, Ku-0059436)12 CitationSummary: Potent PARP1/PARP2 inhibitor
- A4156 Rucaparib (AG-014699,PF-01367338)Summary: Potent PARP inhibitor
- A4157 Iniparib (BSI-201)Summary: PARP1 inhibitor,intravenously adminsitered
- A4158 AG-143611 CitationSummary: Potent PARP1 inhibitor
- A4159 PJ34 hydrochlorideSummary: PARP inhibitor,potent and cell-permeable
- A4160 A-966492Target: PARPSummary: PARP-1/-2 inhibitor, highly potent
- A4161 3-aminobenzamide1 CitationSummary: Potent PARP inhibitor