HPF1 completes the PARP active site for DNA damage-induced ADP-ribosylation.
ADP-Ribosylation
Allosteric Regulation
Amino Acid Motifs
Amino Acid Sequence
Animals
Biocatalysis
Carrier Proteins
/ chemistry
Catalytic Domain
DNA Damage
HEK293 Cells
Humans
Models, Molecular
Mutation
NAD
/ metabolism
Nuclear Magnetic Resonance, Biomolecular
Nuclear Proteins
/ chemistry
Poly (ADP-Ribose) Polymerase-1
/ chemistry
Poly(ADP-ribose) Polymerase Inhibitors
/ pharmacology
Poly(ADP-ribose) Polymerases
/ chemistry
Sea Anemones
Journal
Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462
Informations de publication
Date de publication:
03 2020
03 2020
Historique:
received:
18
11
2019
accepted:
29
01
2020
pubmed:
7
2
2020
medline:
2
6
2020
entrez:
7
2
2020
Statut:
ppublish
Résumé
The anti-cancer drug target poly(ADP-ribose) polymerase 1 (PARP1) and its close homologue, PARP2, are early responders to DNA damage in human cells
Identifiants
pubmed: 32028527
doi: 10.1038/s41586-020-2013-6
pii: 10.1038/s41586-020-2013-6
pmc: PMC7104379
mid: EMS85649
doi:
Substances chimiques
Carrier Proteins
0
HPF1 protein, human
0
Nuclear Proteins
0
Poly(ADP-ribose) Polymerase Inhibitors
0
NAD
0U46U6E8UK
PARP1 protein, human
EC 2.4.2.30
PARP2 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
Langues
eng
Sous-ensembles de citation
IM
Pagination
598-602Subventions
Organisme : Medical Research Council
ID : MC_U105178934
Pays : United Kingdom
Organisme : Cancer Research UK
ID : A22284
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 210634
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 101794
Pays : United Kingdom
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_U117533887
Pays : United Kingdom
Commentaires et corrections
Type : CommentIn
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