- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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1 Online-Ressource.
- Language
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Englisch
- Bibliographic citation
-
Structural basis for stabilisation of the RAD51 nucleoprotein filament by BRCA2 ; volume:14 ; number:1 ; day:2 ; month:11 ; year:2023 ; pages:1-12 ; date:12.2023
Nature Communications ; 14, Heft 1 (2.11.2023), 1-12, 12.2023
- Creator
-
Appleby, Robert
Joudeh, Luay
Cobbett, Katie
Pellegrini, Luca
- Contributor
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SpringerLink (Online service)
- DOI
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10.1038/s41467-023-42830-1
- URN
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urn:nbn:de:101:1-2024012210561202755441
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:35 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Appleby, Robert
- Joudeh, Luay
- Cobbett, Katie
- Pellegrini, Luca
- SpringerLink (Online service)
Other Objects (12)
Structural and torsional properties of the RAD51-dsDNA nucleoprotein filament
Human RAD51 paralogue SWSAP1 fosters RAD51 filament by regulating the anti-recombinase FIGNL1 AAA+ ATPase
A RAD51–ADP double filament structure unveils the mechanism of filament dynamics in homologous recombination
BRCA2 stabilises RAD51 and DMC1 nucleoprotein filaments through a conserved interaction mode
Yeast Rad52 is a homodecamer and possesses BRCA2-like bipartite Rad51 binding modes
Addendum: BRCA2 stabilises RAD51 and DMC1 nucleoprotein filaments through a conserved interaction mode
Sister chromatid exchanges induced by perturbed replication can form independently of BRCA1, BRCA2 and RAD51
FoxM1-dependent RAD51 and BRCA2 signaling protects idiopathic pulmonary fibrosis fibroblasts from radiation-induced cell death
Structural basis of actin filament assembly and aging
Heterophase materials for fused filament fabrication of structural electronics
Structural basis for cofilin binding and actin filament disassembly
Human Rad51 mediated DNA unwinding is facilitated by conditions that favour Rad51-dsDNA aggregation
Structural and torsional properties of the RAD51-dsDNA nucleoprotein filament
Human RAD51 paralogue SWSAP1 fosters RAD51 filament by regulating the anti-recombinase FIGNL1 AAA+ ATPase
A RAD51–ADP double filament structure unveils the mechanism of filament dynamics in homologous recombination
BRCA2 stabilises RAD51 and DMC1 nucleoprotein filaments through a conserved interaction mode
Yeast Rad52 is a homodecamer and possesses BRCA2-like bipartite Rad51 binding modes
Addendum: BRCA2 stabilises RAD51 and DMC1 nucleoprotein filaments through a conserved interaction mode
Sister chromatid exchanges induced by perturbed replication can form independently of BRCA1, BRCA2 and RAD51
FoxM1-dependent RAD51 and BRCA2 signaling protects idiopathic pulmonary fibrosis fibroblasts from radiation-induced cell death
Structural basis of actin filament assembly and aging
Heterophase materials for fused filament fabrication of structural electronics
Structural basis for cofilin binding and actin filament disassembly
Human Rad51 mediated DNA unwinding is facilitated by conditions that favour Rad51-dsDNA aggregation
Structural and torsional properties of the RAD51-dsDNA nucleoprotein filament
Human RAD51 paralogue SWSAP1 fosters RAD51 filament by regulating the anti-recombinase FIGNL1 AAA+ ATPase
A RAD51–ADP double filament structure unveils the mechanism of filament dynamics in homologous recombination
BRCA2 stabilises RAD51 and DMC1 nucleoprotein filaments through a conserved interaction mode
Yeast Rad52 is a homodecamer and possesses BRCA2-like bipartite Rad51 binding modes
Addendum: BRCA2 stabilises RAD51 and DMC1 nucleoprotein filaments through a conserved interaction mode
Sister chromatid exchanges induced by perturbed replication can form independently of BRCA1, BRCA2 and RAD51
FoxM1-dependent RAD51 and BRCA2 signaling protects idiopathic pulmonary fibrosis fibroblasts from radiation-induced cell death
Structural basis of actin filament assembly and aging
Heterophase materials for fused filament fabrication of structural electronics
Structural basis for cofilin binding and actin filament disassembly