PARP Power: A Structural Perspective on PARP1, PARP2, and PARP3 in DNA Damage Repair and Nucleosome Remodelling.
Allosteric Regulation
/ drug effects
Carrier Proteins
/ metabolism
Cell Cycle Proteins
/ chemistry
DNA Repair
Humans
Models, Molecular
Nuclear Proteins
/ metabolism
Nucleosomes
/ metabolism
Poly (ADP-Ribose) Polymerase-1
/ chemistry
Poly(ADP-ribose) Polymerase Inhibitors
/ pharmacology
Poly(ADP-ribose) Polymerases
/ chemistry
Protein Domains
/ drug effects
ADP-ribosylation
DNA damage response
PARP activation
PARP-DNA binding
Poly (ADP-ribose) polymerases 1-3
histone PARylation factor 1
nucleosome remodelling
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
12 May 2021
12 May 2021
Historique:
received:
06
04
2021
revised:
04
05
2021
accepted:
06
05
2021
entrez:
2
6
2021
pubmed:
3
6
2021
medline:
11
6
2021
Statut:
epublish
Résumé
Poly (ADP-ribose) polymerases (PARP) 1-3 are well-known multi-domain enzymes, catalysing the covalent modification of proteins, DNA, and themselves. They attach mono- or poly-ADP-ribose to targets using NAD
Identifiants
pubmed: 34066057
pii: ijms22105112
doi: 10.3390/ijms22105112
pmc: PMC8150716
pii:
doi:
Substances chimiques
Carrier Proteins
0
Cell Cycle Proteins
0
HPF1 protein, human
0
Nuclear Proteins
0
Nucleosomes
0
Poly(ADP-ribose) Polymerase Inhibitors
0
PARP1 protein, human
EC 2.4.2.30
PARP2 protein, human
EC 2.4.2.30
PARP3 protein, human
EC 2.4.2.30
Poly (ADP-Ribose) Polymerase-1
EC 2.4.2.30
Poly(ADP-ribose) Polymerases
EC 2.4.2.30
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Déclaration de conflit d'intérêts
L.v.B., S.P., M.S., and T.M.d.O. were employees and shareowners of AstraZeneca at the time of writing this review. E.M. is supported by a BBSRC CASE Studentship in partnership with AstraZeneca. The funders had no role in the design, execution, interpretation, or writing of the study.
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