DOI: 10.1038/19560. Binding of double-strand breaks in DNA by human Rad52 protein

Binding of double-strand breaks in DNA by human Rad52 protein

10.1038/19560

Crossref journal-article

Springer Science and Business Media LLC

Nature (297)

Bibliography

Dyck, E. V., Stasiak, A. Z., Stasiak, A., & West, S. C. (1999). Binding of double-strand breaks in DNA by human Rad52 protein. Nature, 398(6729), 728â731.

Authors 4

Eric Van Dyck (first)
Alicja Z. Stasiak (additional)
Andrzej Stasiak (additional)
Stephen C. West (additional)

References 30 Referenced 220

Friedberg, E. C., Walker, G. C. & Siede, W. DNA Repair and Mutagenesis (American Society for Microbiology, Washington, 1995). / DNA Repair and Mutagenesis by EC Friedberg (1995)
Kanaar, R., Hoeijmakers, J. H. J. & van Gent, D. C. Molecular mechanisms of DNA double-strand break repair. Trends Cell Biol. 8, 483–489 (1998). (10.1016/S0962-8924(98)01383-X) / Trends Cell Biol. by R Kanaar (1998)
Liang, F., Han, M. G., Romanienko, P. J. & Jasin, M. Homology-directed repair is a major double-strand break repair pathway in mammalian cells. Proc. Natl Acad. Sci. USA 95, 5172–5177 (1998). (10.1073/pnas.95.9.5172) / Proc. Natl Acad. Sci. USA by F Liang (1998)
Takata, M. et al. Homologous recombination and non-homologous end-joining pathways of DNA double-strand break repair have overlapping roles in the maintenance of chromosomal integrity in vertebrate cells. EMBO J. 17, 5497–5508 (1998). (10.1093/emboj/17.18.5497) / EMBO J. by M Takata (1998)
Critchlow, S. E. & Jackson, S. P. DNA end-joining: from yeast to man. Trends Biochem. Sci. 23, 394–398 (1998). (10.1016/S0968-0004(98)01284-5) / Trends Biochem. Sci. by SE Critchlow (1998)
Sun, H., Treco, D. & Szostak, J. W. Extensive 3′-overhanging, single-stranded DNA associated with the meiosis-specific double-strand breaks at the ARG4 recombination initiation site. Cell 64, 1155–1162 (1991). (10.1016/0092-8674(91)90270-9) / Cell by H Sun (1991)
Sugawara, N. & Haber, J. E. Characterization of double-strand break-induced recombination: homology requirements and single-stranded DNA formation. Mol. Cell. Biol. 12, 563–575 (1992). (10.1128/MCB.12.2.563) / Mol. Cell. Biol. by N Sugawara (1992)
Shen, Z. et al. Self-association of human Rad52 protein. Mutat. Res. 364, 81–89 (1996). (10.1016/0921-8777(96)00025-0) / Mutat. Res. by Z Shen (1996)
Shinohara, A., Shinohara, M., Ohta, T., Matsuda, S. & Ogawa, T. Rad52 forms ring structures and cooperates with RPA in single-strand DNA annealing. Genes to Cells 3, 145–156 (1998). (10.1046/j.1365-2443.1998.00176.x) / Genes to Cells by A Shinohara (1998)
Van Dyck, E., Hajibagheri, N. M. A., Stasiak, A. & West, S. C. Visualization of human Rad52 protein and its complexes with hRad51 and DNA. J. Mol. Biol. 284, 1027–1038 (1998). (10.1006/jmbi.1998.2203) / J. Mol. Biol. by E Van Dyck (1998)
Benson, F. E., Baumann, P. & West, S. C. Synergistic actions of Rad51 and Rad52 in genetic recombination and DNA repair. Nature 391, 401–404 (1998). (10.1038/34937) / Nature by FE Benson (1998)
Baumann, P., Benson, F. E. & West, S. C. Human Rad51 protein promotes ATP-dependent homologous pairing and strand transfer reactions in vitro. Cell 87, 757–766 (1996). (10.1016/S0092-8674(00)81394-X) / Cell by P Baumann (1996)
Nussenzweig, A. et al. Requirement for Ku80 in growth and immunoglobulin V(D)J recombination. Nature 382, 551–555 (1996). (10.1038/382551a0) / Nature by A Nussenzweig (1996)
Nussenzweig, A., Sokol, K., Burgman, P., Li, L. G. & Li, G. C. Hypersensitivity of Ku80-deficient cell lines and mice to DNA damage: the effects of ionizing radiation on growth, survival, and development. Proc. Natl Acad. Sci. USA 94, 13588–13593 (1997). (10.1073/pnas.94.25.13588) / Proc. Natl Acad. Sci. USA by A Nussenzweig (1997)
Anderson, C. W. & Carter, T. H. in Molecular Analysis of DNA Rearrangements in the Immune System (eds Jessberger, R. & Lieber, M. R.) 91–112 (Springer, Heidelberg, 1996). (10.1007/978-3-642-50140-1_7) / Molecular Analysis of DNA Rearrangements in the Immune System by CW Anderson (1996)
Rijkers, T. et al. Targeted inactivation of MmRAD52 reduces homologous recombination but not resistance to ionizing radiation. Mol. Cell. Biol. 18, 6423–6429 (1998). (10.1128/MCB.18.11.6423) / Mol. Cell. Biol. by T Rijkers (1998)
Yamaguchi-Iwai, Y. et al. Homologous recombination, but not DNA repair, is reduced in vertebrate cells deficient in RAD52. Mol. Cell Biol. 18, 6430–6435 (1998). (10.1128/MCB.18.11.6430) / Mol. Cell Biol. by Y Yamaguchi-Iwai (1998)
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Mortensen, U. H., Bendixen, C., Sunjevaric, I. & Rothstein, R. DNA strand annealing is promoted by the yeast Rad52 protein. Proc. Natl Acad. Sci. USA 93, 10729–10734 (1996). (10.1073/pnas.93.20.10729) / Proc. Natl Acad. Sci. USA by UH Mortensen (1996)
Reddy, G., Golub, E. I. & Radding, C. M. Human Rad52 protein promotes single-strand DNA annealing followed by branch migration. Mutat. Res. 377, 53–59 (1997). (10.1016/S0027-5107(97)00057-2) / Mutat. Res. by G Reddy (1997)
Sugiyama, T., New, J. H. & Kowalczykowski, S. C. DNA annealing by Rad52 protein is stimulated by specific interaction with the complex of replication protein A and single-stranded DNA. Proc. Natl Acad. Sci. USA 95, 6049–6054 (1998). (10.1073/pnas.95.11.6049) / Proc. Natl Acad. Sci. USA by T Sugiyama (1998)
New, J. H., Sugiyama, T., Zaitseva, E. & Kowalczykowski, S. C. Rad52 protein stimulates DNA strand exchange by Rad51 and replication protein-A. Nature 391, 407–410 (1998). (10.1038/34950) / Nature by JH New (1998)
Shinohara, A. & Ogawa, T. Stimulation by Rad52 of yeast Rad51-mediated recombination. Nature 391, 404–407 (1998). (10.1038/34943) / Nature by A Shinohara (1998)
Sung, P. Function of yeast Rad52 protein as a mediator between replication protein-A and the Rad51 recombinase. J. Biol. Chem. 272, 28194–28197 (1997). (10.1074/jbc.272.45.28194) / J. Biol. Chem. by P Sung (1997)
Gasior, S. L., Wong, A. K., Kora, Y., Shinohara, A. & Bishop, D. K. Rad52 associates with RP-A and functions with Rad55 and Rad57 to assemble meiotic recombination complexes. Genes Dev. 12, 2208–2221 (1998). (10.1101/gad.12.14.2208) / Genes Dev. by SL Gasior (1998)
Sung, P. Yeast Rad55 and Rad57 proteins form a heterodimer that functions with replication protein-A to promote DNA strand exchange by Rad51 recombinase. Genes Dev. 11, 1111–1121 (1997). (10.1101/gad.11.9.1111) / Genes Dev. by P Sung (1997)
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Dates

Type	When
Created	23 years, 1 month ago (July 26, 2002, 4:39 a.m.)
Deposited	3 years, 9 months ago (Dec. 1, 2021, 4:41 p.m.)
Indexed	1 month, 1 week ago (July 24, 2025, 6:59 a.m.)
Issued	26 years, 5 months ago (April 1, 1999)
Published	26 years, 5 months ago (April 1, 1999)
Published Print	26 years, 5 months ago (April 1, 1999)

Funders 0

None

BibTeX

@article{Dyck_1999, title={Binding of double-strand breaks in DNA by human Rad52 protein}, volume={398}, ISSN={1476-4687}, url={http://dx.doi.org/10.1038/19560}, DOI={10.1038/19560}, number={6729}, journal={Nature}, publisher={Springer Science and Business Media LLC}, author={Dyck, Eric Van and Stasiak, Alicja Z. and Stasiak, Andrzej and West, Stephen C.}, year={1999}, month=apr, pages={728–731} }

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