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.
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A4163 UPF 1069Target: PARPSummary: Selective PARP2 inhibitor
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A4164 AZD2461Target: PARPSummary: Novel PARP inhibitor
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A3246 BMN-673 8R,9S1 CitationSummary: Inactive form of BMN 673, used as negative control
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A8600 Tankyrase Inhibitors (TNKS) 22Summary: Tankyrase inhibitor
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A8601 Tankyrase Inhibitors (TNKS) 49Target: TankyrasesSummary: Tankyrase inhibitor
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A8808 ME0328Target: PARPSummary: PARP inhibitor,potent and selective
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A3002 ABT-888 (Veliparib)6 CitationSummary: Potent PARP inhibitor
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B1163 MK-4827 hydrochlorideSummary: PARP1/PARP2 inhibitor
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B1164 MK-4827 tosylateSummary: PARP1/PARP2 inhibitor
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A3958 Veliparib dihydrochlorideTarget: PARPSummary: PARP-1/PARP-2 inhibitor