Structural insights into BCDX2 complex function in homologous recombination.
Humans
Cryoelectron Microscopy
DNA Replication
DNA, Single-Stranded
/ chemistry
DNA-Binding Proteins
/ chemistry
Homologous Recombination
Multiprotein Complexes
/ chemistry
Neoplasms
/ genetics
Nucleoproteins
/ metabolism
Protein Subunits
/ chemistry
Rad51 Recombinase
/ chemistry
Substrate Specificity
Journal
Nature
ISSN: 1476-4687
Titre abrégé: Nature
Pays: England
ID NLM: 0410462
Informations de publication
Date de publication:
Jul 2023
Jul 2023
Historique:
received:
23
01
2023
accepted:
15
05
2023
pmc-release:
01
07
2024
medline:
21
7
2023
pubmed:
22
6
2023
entrez:
21
6
2023
Statut:
ppublish
Résumé
Homologous recombination (HR) fulfils a pivotal role in the repair of DNA double-strand breaks and collapsed replication forks
Identifiants
pubmed: 37344589
doi: 10.1038/s41586-023-06219-w
pii: 10.1038/s41586-023-06219-w
pmc: PMC10712684
mid: NIHMS1947754
doi:
Substances chimiques
DNA, Single-Stranded
0
DNA-Binding Proteins
0
Multiprotein Complexes
0
Nucleoproteins
0
Protein Subunits
0
Rad51 Recombinase
EC 2.7.7.-
RAD51B protein, human
0
RAD51C protein, human
0
RAD51D protein, human
0
XRCC2 protein, human
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
640-649Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM141091
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM115568
Pays : United States
Organisme : NIEHS NIH HHS
ID : P30 ES013508
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM128731
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM136717
Pays : United States
Organisme : NCI NIH HHS
ID : R01 CA188347
Pays : United States
Informations de copyright
© 2023. The Author(s), under exclusive licence to Springer Nature Limited.
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