Cryo-EM structures of human RAD51 recombinase filaments during catalysis of DNA-strand exchange-Reference-Cited by-同舟云学术

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Cryo-EM structures of human RAD51 recombinase filaments during catalysis of DNA-strand exchange

Published:2016-12-12 Issue:1 Volume:24 Page:40-46
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Xu Jingfei,Zhao Lingyun,Xu Yuanyuan,Zhao Weixing,Sung Patrick,Wang Hong-Wei

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb.3336.pdf

Reference64 articles.

1. Wang, A.T. et al. A dominant mutation in human RAD51 reveals its function in DNA interstrand crosslink repair independent of homologous recombination. Mol. Cell 59, 478–490 (2015).

2. Mazón, G., Mimitou, E.P. & Symington, L.S. SnapShot: homologous recombination in DNA double-strand break repair. Cell 142, 648.e1–648.e2 (2010).

3. Lambert, S. et al. Homologous recombination restarts blocked replication forks at the expense of genome rearrangements by template exchange. Mol. Cell 39, 346–359 (2010).

4. van den Bosch, M., Lohman, P.H.M. & Pastink, A. DNA double-strand break repair by homologous recombination. Biol. Chem. 383, 873–892 (2002).

5. 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).

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