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  4. Poly-ADP ribosylation in DNA damage response and cancer therapy
 
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Poly-ADP ribosylation in DNA damage response and cancer therapy

Journal
Mutation Research-Reviews in Mutation Research
Journal Volume
780
Pages
82-91
Date Issued
2019
Author(s)
W. H. Hou, S. H. Chen and X. C. Yu
SHIH-HSUN CHEN  
DOI
10.1016/j.mrrev.2017.09.004
URI
https://scholars.lib.ntu.edu.tw/handle/123456789/513986
https://www.scopus.com/inward/record.uri?eid=2-s2.0-85029789533&doi=10.1016%2fj.mrrev.2017.09.004&partnerID=40&md5=a12834b74bf96f6384d4bd8640bd6774
Abstract
Poly(ADP-ribosyl)ation (aka PARylation) is a unique protein post-translational modification (PTM) first described over 50 years ago. PARylation regulates a number of biological processes including chromatin remodeling, the DNA damage response (DDR), transcription, apoptosis, and mitosis. The subsequent discovery of poly(ADP-ribose) polymerase-1 (PARP-1) catalyzing DNA-dependent PARylation spearheaded the field of DDR. The expanding knowledge about the poly ADP-ribose (PAR) recognition domains prompted the discovery of novel DDR factors and revealed crosstalk with other protein PTMs including phosphorylation, ubiquitination, methylation and acetylation. In this review, we highlight the current knowledge on PAR-regulated DDR, PAR recognition domain, and PARP inhibition in cancer therapy. © 2017 Elsevier B.V.
Subjects
BRCT domain; De-PARylation; DNA damage response; PAR recognition domain; PARP inhibitor; PARP inhibitor resistance; PARylation; Poly(ADP-ribosyl)ation; Poly(ADP-ribosyl)lation polymerase
SDGs

[SDGs]SDG3

Other Subjects
DNA; poly(adenosine diphosphate ribose); poly(adenosine diphosphate ribose) binding zinc finger protein; unclassified drug; zinc finger protein; nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase; nicotinamide adenine dinucleotide adenosine diphosphate ribosyltransferase inhibitor; poly(adenosine diphosphate ribose); cancer therapy; DNA damage response; metabolism; poly(adenosine diphosphate) ribosylation; priority journal; protein domain; protein structure; Review; RNA recognition motif; animal; DNA damage; DNA repair; drug effect; genetics; human; neoplasm; poly(adenosine diphosphate) ribosylation; Animals; DNA Damage; DNA Repair; Humans; Neoplasms; Poly Adenosine Diphosphate Ribose; Poly ADP Ribosylation; Poly(ADP-ribose) Polymerase Inhibitors; Poly(ADP-ribose) Polymerases
Type
review

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