Dataset Information

Novel modifications of PARP inhibitor veliparib increase PARP1 binding to DNA breaks

ABSTRACT: The project is about studying the dynamics of PARP1 when bound to DNA and veliparib derivatives.

INSTRUMENT(S): Exactive Plus

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Ramya Billur

LAB HEAD: Dr. Ben E. Black

PROVIDER: PXD047072 | Pride | 2024-03-19

REPOSITORIES: Pride

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Novel modifications of PARP inhibitor veliparib increase PARP1 binding to DNA breaks.

Velagapudi Uday Kiran UK Rouleau-Turcotte Élise É Billur Ramya R Shao Xuwei X Patil Manisha M Black Ben E BE Pascal John M JM Talele Tanaji T TT

The Biochemical journal 20240301 6

Catalytic poly(ADP-ribose) production by PARP1 is allosterically activated through interaction with DNA breaks, and PARP inhibitor compounds have the potential to influence PARP1 allostery in addition to preventing catalytic activity. Using the benzimidazole-4-carboxamide pharmacophore present in the first generation PARP1 inhibitor veliparib, a series of 11 derivatives was designed, synthesized, and evaluated as allosteric PARP1 inhibitors, with the premise that bulky substituents would engage ...[more]

PMID: 38372302

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			Action	DRS
	A2_1_PARP1_10e2.raw	Raw
	A2_2_PARP1_10e2.raw	Raw
	A2_3_PARP1_10e2.raw	Raw
	B2_1_PARP1_DNA_10e2.raw	Raw
	B2_2_PARP1_DNA_10e2.raw	Raw