The DOI matches its Crossref record; 21 of the 21 references it cites were found in a registry or an index.
The breast cancer tumor suppressor BRCA2 promotes the specific targeting of RAD51 to single-stranded DNA
Open accessAbstract
Individuals with BRCA2 mutations are predisposed to breast cancers owing to genome instability. To determine the functions of BRCA2, the human protein was purified. It was found to bind selectively to single-stranded DNA (ssDNA), and to ssDNA in tailed duplexes and replication fork structures. Monomeric and dimeric forms of BRCA2 were observed by EM. BRCA2 directed the binding of RAD51 recombinase to ssDNA, reduced the binding of RAD51 to duplex DNA and stimulated RAD51-mediated DNA strand exchange. These observations provide a molecular basis for the role of BRCA2 in the maintenance of genome stability.
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Cites
Mitotic homologous recombination maintains genomic stability and suppresses tumorigenesis
Moynahan, M. E., & Jasin, M. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2851 · Cited by 930
BRCA2 Function in DNA Binding and Recombination from a BRCA2-DSS1-ssDNA Structure
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PALB2 is an integral component of the BRCA complex required for homologous recombination repair
Sy, S. M. H., Huen, M. S. Y., & Chen, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811159106 · Cited by 614
CDK-dependent phosphorylation of BRCA2 as a regulatory mechanism for recombinational repair
Esashi, F., Christ, N., Gannon, J., Liu, Y., Hunt, T., Jasin, M., & West, S. C. (2005) · Nature · doi:10.1038/nature03404 · Cited by 479
Self-citationPurification and characterization of the human Rad51 protein, an analogue of E. coli RecA.
Benson, F. E., Stasiak, A., & West, S. C. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06914.x · Cited by 455
Self-citationThe BRCA2 homologue Brh2 nucleates RAD51 filament formation at a dsDNA–ssDNA junction
Yang, H., Li, Q., Fan, J., Holloman, W. K., & Pavletich, N. P. (2005) · Nature · doi:10.1038/nature03234 · Cited by 336
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Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2
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The BRC Repeats of BRCA2 Modulate the DNA-Binding Selectivity of RAD51
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Cited by
DNA double-strand break repair-pathway choice in somatic mammalian cells
Scully, R., Panday, A., Elango, R., & Willis, N. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0152-0 · Cited by 1,457
Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications
Polo, S. E., & Jackson, S. P. (2011) · Genes & Development · doi:10.1101/gad.2021311 · Cited by 1,092
Homologous Recombination and Human Health: The Roles of BRCA1, BRCA2, and Associated Proteins
Prakash, R., Zhang, Y., Feng, W., & Jasin, M. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016600 · Cited by 869
Homologous recombination and the repair of DNA double-strand breaks
Wright, W. D., Shah, S. S., & Heyer, W.-D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.000372 · Cited by 713
Hereditary breast and ovarian cancer: new genes in confined pathways
Nielsen, F. C., van Overeem Hansen, T., & Sørensen, C. S. (2016) · Nature Reviews Cancer · doi:10.1038/nrc.2016.72 · Cited by 367
Metadata
- Authors
- Thorslund, T., McIlwraith, M. J., Compton, S. A., Lekomtsev, S., Petronczki, M., Griffith, J. D., & West, S. C.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2010-08-22
- Volume
- 17
- Issue
- 10
- Pages
- 1263-1265
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2055761018
- Cited by
- 262
- References
- 21
- FWCI
- 8.03
- Type
- journal article
- Language
- en
- Open access
- green
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- Thorslund, T., McIlwraith, M. J., Compton, S. A., Lekomtsev, S., Petronczki, M., Griffith, J. D., & West, S. C. (2010). The breast cancer tumor suppressor BRCA2 promotes the specific targeting of RAD51 to single-stranded DNA. Nature Structural & Molecular Biology. https://doi.org/10.1038/nsmb.1905
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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