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.
- A3958 Veliparib dihydrochlorideTarget: PARPSummary: PARP-1/PARP-2 inhibitor
- A4524 4-HQNSummary: PARP inhibitor
- A4525 BYK 204165Summary: PARP-1 inhibitor,potent and selective
- A4526 BYK 49187Summary: Potent PARP-1/PARP-2 inhibitor
- A4527 DR 2313Summary: PARP inhibitor
- A4528 EB 47Summary: Potent PARP-1 inhibitor
- A4529 JW 55Summary: PARP domain inhibitor
- A4530 NU 1025Summary: PARP inhibitor,potent and novel
- A4531 WIKI4Summary: Inhibitor of Wnt/ß-Catenin signaling and tankyrase
- A1877 XAV-9391 CitationTarget: TNKSSummary: Tankyrase 1/2 inhibitor