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Human PARP1 substrates and regulators of its catalytic activity: An updated overview

Affiliation
Department of Pharmacy ,The Second Affiliated Hospital ,Zhejiang University School of Medicine ,Hangzhou ,China
Zhu, Tao;
Affiliation
Institute of Clinical Pharmacology ,Xiangya Hospital ,Central South University ,Changsha ,China
Zheng, Ju-Yan;
Affiliation
Department of Pharmacy ,The Second Affiliated Hospital ,Zhejiang University School of Medicine ,Hangzhou ,China
Huang, Ling-Ling;
Affiliation
Department of Pharmacy ,The Second Affiliated Hospital ,Zhejiang University School of Medicine ,Hangzhou ,China
Wang, Yan-Hong;
Affiliation
Department of Pharmacy ,The Second Affiliated Hospital ,Zhejiang University School of Medicine ,Hangzhou ,China
Yao, Di-Fei;
Affiliation
Department of Pharmacy ,The Second Affiliated Hospital ,Zhejiang University School of Medicine ,Hangzhou ,China
Dai, Hai-Bin

Poly (ADP-ribose) polymerase 1 (PARP1) is a key DNA damage sensor that is recruited to damaged sites after DNA strand breaks to initiate DNA repair. This is achieved by catalyzing attachment of ADP-ribose moieties, which are donated from NAD + , on the amino acid residues of itself or other acceptor proteins. PARP inhibitors (PARPi) that inhibit PARP catalytic activity and induce PARP trapping are commonly used for treating BRCA1/2 -deficient breast and ovarian cancers through synergistic lethality. Unfortunately, resistance to PARPi frequently occurs. In this review, we present the novel substrates and regulators of the PARP1-catalyzed poly (ADP-ribosyl)ation (PARylatison) that have been identified in the last 3 years. The overall aim is the presentation of protein interactions of potential therapeutic intervention for overcoming the resistance to PARPi.

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License Holder: Copyright © 2023 Zhu, Zheng, Huang, Wang, Yao and Dai.

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