In Silico design and characterization of RAD51 protein inhibitors targeting homologous recombination repair for cancer therapy
Author:
Funder
Department of Science Technology-Science and Engineering Research Board (DST-SERB), Govt. of India
Publisher
Springer Science and Business Media LLC
Subject
General Medicine
Link
https://link.springer.com/content/pdf/10.1007/s42764-023-00106-4.pdf
Reference56 articles.
1. Amunugama, R., & Fishel, R. (2011). Subunit interface residues F129 and H294 of human RAD51 are essential for recombinase function. PLoS ONE, 6(8), e23071. https://doi.org/10.1371/journal.pone.0023071.
2. Aparicio, T., Baer, R., & Gautier, J. (2014). DNA double-strand break repair pathway choice and cancer. DNA Repair, 19, 169–175. https://doi.org/10.1016/j.dnarep.2014.03.014.
3. Bahassi, E. M., Ovesen, J. L., Riesenberg, A. L., Bernstein, W. Z., Hasty, P. E., & Stambrook, P. J. (2008). The checkpoint kinases Chk1 and Chk2 regulate the functional associations between hBRCA2 and Rad51 in response to DNA damage. Oncogene, 27(28), 3977–3985. https://doi.org/10.1038/onc.2008.17.
4. Begg, A. C., Stewart, F. A., & Vens, C. (2011). Strategies to improve radiotherapy with targeted drugs. Nature Reviews Cancer, 11(4), 239–253. https://doi.org/10.1038/nrc3007.
5. Chen, C. F., Chen, P. L., Zhong, Q., Sharp, Z. D., & Lee, W. H. (1999a). Expression of BRC repeats in breast cancer cells disrupts the BRCA2-Rad51 complex and leads to radiation hypersensitivity and loss of G(2)/M checkpoint control. The Journal of Biological Chemistry, 274(46), 32931–32935. https://doi.org/10.1074/jbc.274.46.32931.
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