The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
Human BRCA2 protein promotes RAD51 filament formation on RPA-covered single-stranded DNA
Open accessAbstract
BRCA2 is a tumor suppressor that functions in homologous recombination, a key genomic integrity pathway. BRCA2 interacts with RAD51, the central protein of recombination, which forms filaments on single-stranded DNA (ssDNA) to perform homology search and DNA strand invasion. We report the purification of full-length human BRCA2 and show that it binds to ∼6 RAD51 molecules and promotes RAD51 binding to ssDNA coated by replication protein A (RPA), in a manner that is stimulated by DSS1.
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Cites
Identification of the breast cancer susceptibility gene BRCA2
Wooster, R., Bignell, G., Lancaster, J., Swift, S., Seal, S., Mangion, J., Collins, N., Gregory, S., Gumbs, C., Micklem, G., et al. (1995) · Nature · doi:10.1038/378789a0 · Cited by 3,645
BRCA2 Is Required for Homology-Directed Repair of Chromosomal Breaks
Moynahan, M. E., Pierce, A. J., & Jasin, M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00174-5 · Cited by 1,006
Role of BRCA2 in Control of the RAD51 Recombination and DNA Repair Protein
Davies, A. A., Masson, J.-Y., McIlwraith, M. J., Stasiak, A. Z., Stasiak, A., Venkitaraman, A. R., & West, S. C. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00175-7 · Cited by 718
Purified human BRCA2 stimulates RAD51-mediated recombination
Jensen, R. B., Carreira, A., & Kowalczykowski, S. C. (2010) · Nature · doi:10.1038/nature09399 · Cited by 715
BRCA2 Function in DNA Binding and Recombination from a BRCA2-DSS1-ssDNA Structure
Yang, H., Jeffrey, P. D., Miller, J., Kinnucan, E., Sun, Y., Thomä, N. H., Zheng, N., Chen, P.-L., Lee, W.-H., & Pavletich, N. P. (2002) · Science · doi:10.1126/science.297.5588.1837 · Cited by 705
Wong, A. K. C., Pero, R., Ormonde, P. A., Tavtigian, S. V., & Bartel, P. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.31941 · Cited by 539
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
BRCA2 is required for ionizing radiation-induced assembly of Rad51 complex in vivo.
Yuan, S. F., Lee, S. Y., Chen, G., Song, M., Tomlinson, G. E., & Lee, E. Y.-H. P. (1999) · PubMed · Cited by 404
The 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
Stabilization of RAD51 nucleoprotein filaments by the C-terminal region of BRCA2
Esashi, F., Galkin, V. E., Yu, X., Egelman, E. H., & West, S. C. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1245 · Cited by 280
Cited by
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
Purified human BRCA2 stimulates RAD51-mediated recombination
Jensen, R. B., Carreira, A., & Kowalczykowski, S. C. (2010) · Nature · doi:10.1038/nature09399 · Cited by 715
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
Self-citationHereditary 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
- Liu, J., Doty, T., Gibson, B., & Heyer, W.-D.
- Venue
- Nature Structural & Molecular Biology
- Published
- 2010-08-22
- Volume
- 17
- Issue
- 10
- Pages
- 1260-1262
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2084034209
- Cited by
- 401
- References
- 20
- FWCI
- 10.28
- Type
- journal article
- Language
- en
- Open access
- green
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