Promotion of BRCA2-Dependent Homologous Recombination by DSS1 via RPA Targeting and DNA Mimicry
Open accessAbstract
The tumor suppressor BRCA2 is thought to facilitate the handoff of ssDNA from replication protein A (RPA) to the RAD51 recombinase during DNA break and replication fork repair by homologous recombination. However, we find that RPA-RAD51 exchange requires the BRCA2 partner DSS1. Biochemical, structural, and in vivo analyses reveal that DSS1 allows the BRCA2-DSS1 complex to physically and functionally interact with RPA. Mechanistically, DSS1 acts as a DNA mimic to attenuate the affinity of RPA for ssDNA. A mutation in the solvent-exposed acidic domain of DSS1 compromises the efficacy of RPA-RAD51 exchange. Thus, by targeting RPA and mimicking DNA, DSS1 functions with BRCA2 in a two-component homologous recombination mediator complex in genome maintenance and tumor suppression. Our findings may provide a paradigm for understanding the roles of DSS1 in other biological processes.
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Unlike BRCA2-DSS1, BRCA1-BARD1 fails to promote assembly of RAD51 presynaptic filaments on RPA-coated ssDNA.
“while, as reported previously36,38, the BRCA2-DSS1 complex promotes RAD51 presynaptic filament assembly on RPA-coated ssDNA, BRCA1-BARD1 does not possess such an attribute”
From BRCA1–BARD1 promotes RAD51-mediated homologous DNA pairing (2017) · cites this paper as [36]
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Cites
Identification of the breast cancer susceptibility gene BRCA2
Wooster, R., Bignell, G. R., Lancaster, J., Swift, S., Seal, S., Mangion, J., Collins, N., Gregory, S. G., Gumbs, C. E., Micklem, G., et al. (1995) · Nature · doi:10.1038/378789a0 · Cited by 3,645 · see citing works
Genomic instability — an evolving hallmark of cancer
Negrini, S., Gorgoulis, V. G., & Halazonetis, T. D. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2858 · Cited by 2,397 · see citing works
Hoeijmakers, J. H. J. (2009) · New England Journal of Medicine · doi:10.1056/nejmra0804615 · Cited by 2,239 · see citing works
Mechanism of Eukaryotic Homologous Recombination
Filippo, J. S., Sung, P., & Klein, H. L. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061306.125255 · Cited by 1,686 · see citing works
Self-citationDouble-Strand Break End Resection and Repair Pathway Choice
Symington, L. S., & Gautier, J. (2011) · Annual Review of Genetics · doi:10.1146/annurev-genet-110410-132435 · Cited by 1,482 · see citing works
Schlacher, K., Christ, N., Siaud, N., Egashira, A., Wu, H., & Jasin, M. (2011) · Cell · doi:10.1016/j.cell.2011.03.041 · Cited by 1,258 · see citing works
Embryonic lethality and radiation hypersensitivity mediated by Rad51 in mice lacking Brca2
Sharan, S. K., Morimatsu, M., Albrecht, U., Lim, D., Regel, E., Dinh, C. Q., Sands, A., Gregor Eichele, C., Hasty, P., & Bradley, A. (1997) · Nature · doi:10.1038/386804a0 · Cited by 1,071 · see citing works
Role of RAD52 Epistasis Group Genes in Homologous Recombination and Double-Strand Break Repair
Symington, L. S. (2002) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.66.4.630-670.2002 · Cited by 965 · see citing works
Control of BRCA2 Cellular and Clinical Functions by a Nuclear Partner, PALB2
Xia, B., Sheng, Q., Nakanishi, K., Ohashi, A., Wu, J., Christ, N., Liu, X., Jasin, M., Couch, F. J., & Livingston, D. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.022 · Cited by 861 · see citing works
Purified human BRCA2 stimulates RAD51-mediated recombination
Jensen, R. B., Carreira, A., & Kowalczykowski, S. C. (2010) · Nature · doi:10.1038/nature09399 · Cited by 715 · see citing works
Self-citationBRCA2 Function in DNA Binding and Recombination from a BRCA2-DSS1-ssDNA Structure
Yang, H., Jeffrey, P. D., Miller, J. J., Kinnucan, E., Sun, Y., Thomä, N. H., Zheng, N., Chen, P., Lee, W., & Pavletich, N. P. (2002) · Science · doi:10.1126/science.297.5588.1837 · Cited by 705 · see citing works
Wong, A. K. C., Pero, R. S., Ormonde, P. A., Tavtigian, S. V., & Bartel, P. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.51.31941 · Cited by 539 · see citing works
Rad51 protects nascent DNA from Mre11-dependent degradation and promotes continuous DNA synthesis
Hashimoto, Y., Chaudhuri, A. R., Lopes, M., & Costanzo, V. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1927 · Cited by 537 · see citing works
Genetic Steps of Mammalian Homologous Repair with Distinct Mutagenic Consequences
Stark, J. M., Pierce, A. J., Oh, J., Pastink, A., & Jasin, M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9305-9316.2004 · Cited by 501 · see citing works
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 473 · see citing works
DNA strand annealing is promoted by the yeast Rad52 protein.
Mortensen, U. H., Bendixen, C., Šunjevarić, I., & Rothstein, R. J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.20.10729 · Cited by 472 · see citing works
Maréchal, A., & Zou, L. (2015) · Cell Research · doi:10.1038/cr.2014.147 · Cited by 465 · see citing works
Gayther, S. A., Mangion, J., Russell, P. A., Seal, S., Barfoot, R., Ponder, B. A. J., Stratton, M. R., & Easton, D. F. (1997) · Nature Genetics · doi:10.1038/ng0197-103 · Cited by 442 · see citing works
Adamson, B., Smogorzewska, A., Sigoillot, F. D., King, R. W., & Elledge, S. J. (2012) · Nature Cell Biology · doi:10.1038/ncb2426 · Cited by 433 · see citing works
Tutt, A. N. J., Bertwistle, D., Valentine, J., Gabriel, A., Swift, S., Ross, G., Griffin, C. S., Thacker, J., & Ashworth, A. (2001) · The EMBO Journal · doi:10.1093/emboj/20.17.4704 · Cited by 429 · see citing works
Clarifying the mechanics of DNA strand exchange in meiotic recombination
Neale, M. J., & Keeney, S. (2006) · Nature · doi:10.1038/nature04885 · Cited by 417 · see citing works
Human BRCA2 protein promotes RAD51 filament formation on RPA-covered single-stranded DNA
Liu, J., Doty, T., Gibson, B. A., & Heyer, W. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1904 · Cited by 396 · see citing works
Human Fanconi anemia monoubiquitination pathway promotes homologous DNA repair
Nakanishi, K., Yang, Y.-G., Pierce, A. J., Taniguchi, T., Digweed, M., D'Andrea, A. D., Wang, Z.-Q., & Jasin, M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407796102 · Cited by 384 · see citing works
Rad52 inactivation is synthetically lethal with BRCA2 deficiency
Feng, Z., Scott, S. P., Bussen, W., Sharma, G. G., Guo, G., Pandita, T. K., & Powell, S. N. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010959107 · Cited by 342 · see citing works
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 335 · see citing works
The BRC Repeats of BRCA2 Modulate the DNA-Binding Selectivity of RAD51
Carreira, A., Hilario, J., Amitani, I., Baskin, R. J., Shivji, M. K. K., Venkitaraman, A. R., & Kowalczykowski, S. C. (2009) · Cell · doi:10.1016/j.cell.2009.02.019 · Cited by 268 · see citing works
Wilmes, G. M., Bergkessel, M., Bandyopadhyay, S., Shales, M., Braberg, H., Cagney, G., Collins, S. R., Whitworth, G. B., Kress, T. L., Weissman, J. S., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.012 · Cited by 265 · see citing works
Thorslund, T., McIlwraith, M. J., Compton, S. A., Lekomtsev, S., Petronczki, M. P., Griffith, J. D., & West, S. C. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1905 · Cited by 262 · see citing works
Crackower, M. A. (1996) · Human Molecular Genetics · doi:10.1093/hmg/5.5.571 · Cited by 207 · see citing works
Marston, N. J., Richards, W. J., Hughes, D. A., Bertwistle, D., Marshall, C. J., & Ashworth, A. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.7.4633 · Cited by 186 · see citing works
Carreira, A., & Kowalczykowski, S. C. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1106971108 · Cited by 185 · see citing works
Human meiotic recombinase Dmc1 promotes ATP-dependent homologous DNA strand exchange
Sehorn, M. G., Sigurðsson, S., Bussen, W., Unger, V. M., & Sung, P. (2004) · Nature · doi:10.1038/nature02563 · Cited by 179 · see citing works
Self-citationBrca2 is involved in meiosis in Arabidopsis thaliana as suggested by its interaction with Dmc1
Siaud, N., Dray, E. V., Gy, I., Gérard, E., Takvorian, N., & Doutriaux, M.-P. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600146 · Cited by 178 · see citing works
Kojić, M., Kostrub, C. F., Buchman, A. R., & Holloman, W. K. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00632-9 · Cited by 168 · see citing works
DSS1 is required for the stability of BRCA2
Li, J., Zou, C., Bai, Y., Wazer, D. E., Band, V., & Gao, Q. (2005) · Oncogene · doi:10.1038/sj.onc.1209153 · Cited by 136 · see citing works
Recombination Mediator and Rad51 Targeting Activities of a Human BRCA2 Polypeptide
Filippo, J. S., Chi, P., Sehorn, M. G., Etchin, J., Krejci, L., & Sung, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m601249200 · Cited by 134 · see citing works
Self-citationInteractions between human BRCA2 protein and the meiosis‐specific recombinase DMC1
Thorslund, T., Esashi, F., & West, S. C. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601739 · Cited by 123 · see citing works
PCI Complexes: Beyond the Proteasome, CSN, and eIF3 Troika
Pick, E., Hofmann, K., & Glickman, M. H. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.009 · Cited by 121 · see citing works
Rad52 Promotes Postinvasion Steps of Meiotic Double-Strand-Break Repair
Lao, J. P., Oh, S. D., Shinohara, M., Shinohara, A., & Hunter, N. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.014 · Cited by 117 · see citing works
Interaction with Rad51 Is Indispensable for Recombination Mediator Function of Rad52
Krejčí, L., Song, B., Bussen, W., Rothstein, R. J., Mortensen, U. H., & Sung, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206511200 · Cited by 117 · see citing works
Self-citationDSS1 is required for RAD51 focus formation and genomic stability in mammalian cells
Gudmundsdottir, K. K., Lord, C. J., Witt, E., Tutt, A. N. J., & Ashworth, A. (2004) · EMBO Reports · doi:10.1038/sj.embor.7400255 · Cited by 116 · see citing works
Kojić, M., Yang, H., Kostrub, C. F., Pavletich, N. P., & Holloman, W. K. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00367-8 · Cited by 115 · see citing works
Rad52‐mediated DNA annealing after Rad51‐mediated DNA strand exchange promotes second ssDNA capture
Sugiyama, T., Kantake, N., Wu, Y., & Kowalczykowski, S. C. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601412 · Cited by 112 · see citing works
A cancer-associated BRCA2 mutation reveals masked nuclear export signals controlling localization
Jeyasekharan, A. D. D., Liu, Y., Hattori, H., Pisupati, V., Jonsdottir, A. B., Rajendra, E., Lee, M.-Y., Sundaramoorthy, E., Schlachter, S. C., Kaminski, C. F., et al. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2666 · Cited by 109 · see citing works
Dss1 Is a 26S Proteasome Ubiquitin Receptor
Paraskevopoulos, K., Kriegenburg, F., Tatham, M. H., Rösner, H. I., Medina, B., Larsen, I. B., Morrish, R. B., Hardwick, K., Hay, R. T., Kragelund, B. B., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.09.008 · Cited by 93 · see citing works
Structural Mechanisms of DNA Replication, Repair, and Recombination
Stauffer, M. E., & Chazin, W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.r400015200 · Cited by 87 · see citing works
Self-citationSiaud, N., Barbera, M. A., Egashira, A., Lam, I., Christ, N., Schlacher, K., Xia, B., & Jasin, M. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1002409 · Cited by 86 · see citing works
Interaction with RPA Is Necessary for Rad52 Repair Center Formation and for Its Mediator Activity
Plate, I., Hallwyl, S. C. L., Shi, I. Y., Krejčí, L., Müller, C. R., Albertsen, L., Sung, P., & Mortensen, U. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804881200 · Cited by 84 · see citing works
Self-citationBRCA2 is a mediator of RAD51‐ and DMC1‐facilitated homologous recombination in Arabidopsis thaliana
Seeliger, K., Dukowic‐Schulze, S., Wurz‐Wildersinn, R., Pacher, M., & Puchta, H. (2011) · New Phytologist · doi:10.1111/j.1469-8137.2011.03947.x · Cited by 80 · see citing works
Shivji, M. K. K., Mukund, S. R., Rajendra, E., Chen, S., Short, J. M., Savill, J. M., Klenerman, D., & Venkitaraman, A. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906208106 · Cited by 73 · see citing works
Tomko, R. J., & Hochstrasser, M. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.009 · Cited by 72 · see citing works
A high-throughput screen to identify enhancers of ADAR-mediated RNA-editing
Garncarz, W., Tariq, A., Handl, C., Pusch, O., & Jantsch, M. F. (2013) · RNA Biology · doi:10.4161/rna.23208 · Cited by 72 · see citing works
Molecular Anatomy of the Recombination Mediator Function of Saccharomyces cerevisiae Rad52
Seong, C., Sehorn, M. G., Plate, I., Shi, I. Y., Song, B., Chi, P., Mortensen, U. H., Sung, P., & Krejčí, L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800763200 · Cited by 59 · see citing works
Self-citationThe homologous recombination system of Ustilago maydis
Holloman, W. K., Schirawski, J., & Holliday, R. (2008) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2008.04.006 · Cited by 52 · see citing works
Depletion of DSS1 protein disables homologous recombinational repair in human cells
Kristensen, C. N., Bystol, K., Li, B., Serrano, L., & Brenneman, M. A. (2010) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2010.08.007 · Cited by 43 · see citing works
Ignatius, J., Knuutila, S., Scherer, S. W., Trask, B. J., & Kere, J. (1996) · Journal of Medical Genetics · doi:10.1136/jmg.33.6.507 · Cited by 42 · see citing works
C. elegans dss-1is functionally conserved and required for oogenesis and larval growth
Pispa, J., Palmén, S., Holmberg, C. I., & Jäntti, J. (2008) · BMC Developmental Biology · doi:10.1186/1471-213x-8-51 · Cited by 37 · see citing works
Wei, S., Trempus, C. S., Cannon, R. E., Bortner, C. D., & Tennant, R. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206328200 · Cited by 35 · see citing works
Zhou, Q., Kojić, M., & Holloman, W. K. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m809226200 · Cited by 30 · see citing works
Abo, M. A., Dejsuphong, D., Hirota, K., Yonetani, Y., Yamazoe, M., Kurumizaka, H., & Takeda, S. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-1443 · Cited by 25 · see citing works
Rezano, A., Kuwahara, K., Yamamoto‐Ibusuki, M., Kitabatake, M., Moolthiya, P., Phimsen, S., Suda, T., Toné, S., Yamamoto, Y., Iwase, H., et al. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-562 · Cited by 22 · see citing works
Dss1 Regulates Interaction of Brh2 with DNA
Zhou, Q., Mazloum, N. A., Mao, N., Kojić, M., & Holloman, W. K. (2009) · Biochemistry · doi:10.1021/bi901775j · Cited by 21 · see citing works
Ma, Y.-Y., Lin, H., Chang, F.-M., Chang, T., Trieu, T., Pridgen, H. I., Zhang, Y., Huang, J., Patiño-Guzman, K., Diab, N., et al. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs279 · Cited by 16 · see citing works
Dss1 Release Activates DNA Binding Potential in Brh2
Zhou, Q., Kojić, M., & Holloman, W. K. (2012) · Biochemistry · doi:10.1021/bi3011187 · Cited by 12 · see citing works
Flagged first, then by citations
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Nuclear cGAS suppresses DNA repair and promotes tumorigenesis
Liu, H., Zhang, H., Wu, X., Ma, D., Wu, J., Wang, L., Jiang, Y., Fei, Y., Zhu, C., Tan, R., et al. (2018) · Nature · doi:10.1038/s41586-018-0629-6 · Cited by 651 · see citing works
DNA Repair Pathway Choices in CRISPR-Cas9-Mediated Genome Editing
Xue, C., & Greene, E. C. (2021) · Trends in Genetics · doi:10.1016/j.tig.2021.02.008 · Cited by 431 · see citing works
BRCA1–BARD1 promotes RAD51-mediated homologous DNA pairing
Zhao, W., Steinfeld, J. B., Liang, F., Chen, X., Maranon, D. G., Jian Ma, C., Kwon, Y., Rao, T., Wang, W., Sheng, C., et al. (2017) · Nature · doi:10.1038/nature24060 · Cited by 393 · see citing works
Self-citationThe antitumorigenic roles of BRCA1–BARD1 in DNA repair and replication
Tarsounas, M., & Sung, P. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0218-z · Cited by 366 · see citing works
Self-citationRanjha, L., Howard, S. M., & Ćejka, P. (2018) · Chromosoma · doi:10.1007/s00412-017-0658-1 · Cited by 324 · see citing works
BRCA Genes: The Role in Genome Stability, Cancer Stemness and Therapy Resistance
Gorodetska, I., Kozeretska, I. A., & Dubrovska, A. (2019) · Journal of Cancer · doi:10.7150/jca.30410 · Cited by 279 · see citing works
Alternative Lengthening of Telomeres through Two Distinct Break-Induced Replication Pathways
Zhang, J., Yadav, T., Ouyang, J., Lan, L., & Zou, L. (2019) · Cell Reports · doi:10.1016/j.celrep.2018.12.102 · Cited by 252 · see citing works
53BP1 fosters fidelity of homology-directed DNA repair
Ochs, F., Somyajit, K., Altmeyer, M., Rask, M., Lukas, J., & Lukas, C. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3251 · Cited by 219 · see citing works
DNA repair defects in cancer and therapeutic opportunitiesPreprint
Hopkins, J. L., Lan, L., & Zou, L. (2022) · Genes & Development · doi:10.1101/gad.349431.122 · Cited by 204 · see citing works
Inano, S., Sato, K., Katsuki, Y., Kobayashi, W., Tanaka, H., Nakajima, K., Nakada, S., Miyoshi, H., Knies, K., Takaori‐Kondo, A., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.04.022 · Cited by 171 · see citing works
Preserving replication fork integrity and competence via the homologous recombination pathway
Saada, A. A., Lambert, S., & Carr, A. M. (2018) · DNA repair · doi:10.1016/j.dnarep.2018.08.017 · Cited by 169 · see citing works
The BRCA Tumor Suppressor Network in Chromosome Damage Repair by Homologous Recombination
Zhao, W., Wiese, C., Kwon, Y., Hromas, R., & Sung, P. (2019) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-013118-111058 · Cited by 161 · see citing works
Self-citationStructural basis of homologous recombination
Sun, Y., McCorvie, T. J., Yates, L. A., & Zhang, X. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03365-1 · Cited by 160 · see citing works
DNA end resection and its role in DNA replication and DSB repair choice in mammalian cells
Zhao, F., Kim, W., Kloeber, J. A., & Lou, Z. (2020) · Experimental & Molecular Medicine · doi:10.1038/s12276-020-00519-1 · Cited by 148 · see citing works
Replication protein A: a multifunctional protein with roles in DNA replication, repair and beyond
Dueva, R., & Iliakis, G. E. (2020) · NAR Cancer · doi:10.1093/narcan/zcaa022 · Cited by 130 · see citing works
Role of Rad51 and DNA repair in cancer: A molecular perspective
Laurini, E., Marson, D., Fermeglia, A., Aulić, S., Fermeglia, M., & Pricl, S. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107492 · Cited by 128 · see citing works
The complementarity of DDR, nucleic acids and anti-tumour immunity
Kornepati, A. V. R., Rogers, C. M., Sung, P., & Curiel, T. J. (2023) · Nature · doi:10.1038/s41586-023-06069-6 · Cited by 115 · see citing works
Self-citationBanerjee, D., Langberg, K. A., Abbas, S., Odermatt, E., Yerramothu, P., Volaric, M. P., Reidenbach, M. A., Krentz, K. J., Rubinstein, C. D., Brautigan, D. L., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26240-9 · Cited by 84 · see citing works
BRCA2 functions: from DNA repair to replication fork stabilization
Fradet‐Turcotte, A., Sitz, J., Grapton, D., & Orthwein, A. (2016) · Endocrine Related Cancer · doi:10.1530/erc-16-0297 · Cited by 82 · see citing works
Zhang, J., Fujiwara, Y., Yamamoto, S., & Shibuya, H. (2019) · Nature Communications · doi:10.1038/s41467-019-08676-2 · Cited by 81 · see citing works
CTCF facilitates DNA double-strand break repair by enhancing homologous recombination repair
Hilmi, K., Jangal, M., Marques, M., Zhao, T., Saad, A., Zhang, C., Luo, V. M., Syme, A., Rejon, C. A., Yu, Z., et al. (2017) · Science Advances · doi:10.1126/sciadv.1601898 · Cited by 79 · see citing works
Mechanics and Single-Molecule Interrogation of DNA Recombination
Bell, J. C., & Kowalczykowski, S. C. (2016) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034352 · Cited by 78 · see citing works
Beláň, O., Barroso, C., Kaczmarczyk, A. P., Anand, R., Federico, S., O’Reilly, N., Newton, M. D., Mäeots, M.-E., Enchev, R. I., Martínez-Pérez, E., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.12.020 · Cited by 74 · see citing works
Human RecQ Helicases in DNA Double-Strand Break Repair
Lu, H., & Davis, A. J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.640755 · Cited by 74 · see citing works
Takemoto, K., Tani, N., Takada-Horisawa, Y., Fujimura, S., Tanno, N., Yamane, M., Okamura, K., Sugimoto, M., Araki, K., & Ishiguro, K. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107686 · Cited by 72 · see citing works
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Lee, C.-Y., Su, G.-C., Huang, W., Ko, M.-Y., Yeh, H., Chang, G., Lin, S., & Chi, P. (2019) · Nature Communications · doi:10.1038/s41467-018-08011-1 · Cited by 72 · see citing works
Kwon, Y., Rösner, H. I., Zhao, W., Selemenakis, P., He, Z., Kawale, A. S., Katz, J. N., Rogers, C. M., Neal, F. E., Shabestari, A. B., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36211-x · Cited by 65 · see citing works
Self-citationDistinct binding of BRCA2 BRC repeats to RAD51 generates differential DNA damage sensitivity
Chatterjee, G., Jiménez-Sáinz, J., Presti, T., Nguyen, T. T. M., & Jensen, R. B. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw242 · Cited by 63 · see citing works
Self-citationUbiquitin-specific protease 21 stabilizes BRCA2 to control DNA repair and tumor growth
Liu, J., Kruswick, A., Dang, H. T., Tran, A. D., Kwon, S. M., Wang, X. W., & Oberdoerffer, P. (2017) · Nature Communications · doi:10.1038/s41467-017-00206-2 · Cited by 59 · see citing works
Role of RAD51AP1 in homologous recombination DNA repair and carcinogenesis
Pires, E., Sung, P., & Wiese, C. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.09.008 · Cited by 57 · see citing works
Self-citationZhang, J., Gurusaran, M., Fujiwara, Y., Zhang, K., Echbarthi, M., Vorontsov, E. A., Guo, R., Pendlebury, D. F., Alam, I., Livera, G., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15954-x · Cited by 57 · see citing works
RAD52: Paradigm of Synthetic Lethality and New Developments
Rossi, M. J., DiDomenico, S. F., Patel, M., & Mazin, A. V. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.780293 · Cited by 55 · see citing works
Structural insights into BCDX2 complex function in homologous recombination
Rawal, Y., Jia, L., Meir, A., Zhou, S., Kaur, H., Ruben, E. A., Kwon, Y., Bernstein, K. A., Jasin, M., Taylor, A. B., et al. (2023) · Nature · doi:10.1038/s41586-023-06219-w · Cited by 55 · see citing works
Self-citationNon-catalytic Roles for XPG with BRCA1 and BRCA2 in Homologous Recombination and Genome Stability
Trego, K. S., Groesser, T., Davalos, A. R., Parplys, A. C., Zhao, W., Nelson, M. R., Hlaing, A. S., Shih, B., Rydberg, B., Pluth, J. M., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2015.12.026 · Cited by 55 · see citing works
Self-citationA second DNA binding site in human BRCA2 promotes homologous recombination
Nicolai, C. V., Ehlén, Å., Martin, C. A., Zhang, X., & Carreira, A. (2016) · Nature Communications · doi:10.1038/ncomms12813 · Cited by 55 · see citing works
Mechanisms that drive telomere maintenance and recombination in human cancers
Sobinoff, A. P., & Pickett, H. A. (2020) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2020.02.006 · Cited by 55 · see citing works
Guardians of the Genome: BRCA2 and Its Partners
Le, H. P., Heyer, W., & Liu, J. (2021) · Genes · doi:10.3390/genes12081229 · Cited by 52 · see citing works
Mladenov, E., Staudt, C., Soni, A., Murmann-Konda, T., Siemann, M., & Iliakis, G. E. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1167 · Cited by 52 · see citing works
Andreassen, P. R., Seo, J., Wiek, C., & Hanenberg, H. (2021) · Genes · doi:10.3390/genes12071034 · Cited by 49 · see citing works
DSS1/Sem1, a Multifunctional and Intrinsically Disordered Protein
Kragelund, B. B., Schenstrøm, S. M., Rebula, C. A., Panse, V. G., & Hartmann‐Petersen, R. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.02.004 · Cited by 49 · see citing works
Felipe-Medina, N., Caburet, S., Sánchez-Sáez, F., Condezo, Y. B., de Rooij, D. G., Gómez-H, L., Garcia-Valiente, R., Todeschini, A. L., Duque, P., Sánchez-Martin, M. A., et al. (2020) · eLife · doi:10.7554/elife.56996 · Cited by 45 · see citing works
Untangling the crosstalk between BRCA1 and R-loops during DNA repair
Alonso, M. S. M., & Noordermeer, S. M. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab178 · Cited by 45 · see citing works
Deihimi, S., Lev, A., Slifker, M. J., Shagisultanova, E. I., Xu, Q., Jung, K., Vijayvergia, N., Ross, E. A., Xiu, J., Swensen, J. J., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.18098 · Cited by 41 · see citing works
Positive and negative regulators of RAD51/DMC1 in homologous recombination and DNA replication
Ito, M., Fujita, Y., & Shinohara, A. (2023) · DNA repair · doi:10.1016/j.dnarep.2023.103613 · Cited by 40 · see citing works
DSS1 and ssDNA regulate oligomerization of BRCA2
Le, H. P., Ma, X., Vaquero, J., Brinkmeyer, M. K., Guo, F., Heyer, W., & Liu, J. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa555 · Cited by 36 · see citing works
Haas, K. T., Lee, M.-Y., Esposito, A., & Venkitaraman, A. R. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx1303 · Cited by 35 · see citing works
BRCA2 chaperones RAD51 to single molecules of RPA-coated ssDNA
Bell, J. C., Dombrowski, C., Plank, J. L., Jensen, R. B., & Kowalczykowski, S. C. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2221971120 · Cited by 35 · see citing works
Self-citationDSS1 interacts with and stimulates RAD52 to promote the repair of DSBs
Štefanovie, B., Hengel, S. R., Mlčoušková, J., Prochazkova, J., Špı́rek, M., Nikulenkov, F., Němeček, D., Koch, B. G., Bain, F. E., Yu, L. P., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1052 · Cited by 34 · see citing works
Homologous Recombination in Protozoan Parasites and Recombinase Inhibitors
Kelso, A. A., Waldvogel, S. M., Luthman, A. J., & Sehorn, M. G. (2017) · Frontiers in Microbiology · doi:10.3389/fmicb.2017.01716 · Cited by 33 · see citing works
Mechanism and significance of chromosome damage repair by homologous recombination
Kawale, A. S., & Sung, P. (2020) · Essays in Biochemistry · doi:10.1042/ebc20190093 · Cited by 33 · see citing works
Self-citationUbiquitin and ubiquitin-like molecules in DNA double strand break repair
Yu, J., Qin, B., & Lou, Z. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-0380-1 · Cited by 33 · see citing works
Molding BRCA2 function through its interacting partners
Martinez, J. S., Baldeyron, C., & Carreira, A. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1093702 · Cited by 32 · see citing works
DNA double-strand break repair pathway choice: the fork in the road
Han, J., & Huang, J. (2019) · Genome Instability & Disease · doi:10.1007/s42764-019-00002-w · Cited by 32 · see citing works
Trypanosoma brucei TIF2 and TRF Suppress VSG Switching Using Overlapping and Independent Mechanisms
Jehi, S. E., Nanavaty, V., & Li, B. (2016) · PLoS ONE · doi:10.1371/journal.pone.0156746 · Cited by 32 · see citing works
Awate, S., & Brosh, R. M. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061233 · Cited by 32 · see citing works
Ma, É., Pauline, D., Maloisel, L., Guérois, R., Cam, É. L., & Coı̈c, E. (2018) · eLife · doi:10.7554/elife.32744 · Cited by 32 · see citing works
Page, C. L., Amuzu, S., Rahimi, K., Gotlieb, W. H., Ragoussis, J., & Tonin, P. N. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.08.005 · Cited by 30 · see citing works
NUCKS1 promotes RAD54 activity in homologous recombination DNA repair
Maranon, D. G., Sharma, N., Huang, Y., Selemenakis, P., Wang, M., Altina, N. H., Zhao, W., & Wiese, C. (2020) · The Journal of Cell Biology · doi:10.1083/jcb.201911049 · Cited by 30 · see citing works
Self-citationDefects in homologous recombination repair behind the human diseases: FA and HBOC
Katsuki, Y., & Takata, M. (2016) · Endocrine Related Cancer · doi:10.1530/erc-16-0221 · Cited by 30 · see citing works
Biochemical attributes of mitotic and meiotic presynaptic complexes
Crickard, J. B., & Greene, E. C. (2018) · DNA repair · doi:10.1016/j.dnarep.2018.08.018 · Cited by 29 · see citing works
Lee, M.-Y., Shorthouse, D., Mahen, R., Hall, B. A., & Venkitaraman, A. R. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab308 · Cited by 29 · see citing works
Selemenakis, P., Sharma, N., Uhrig, M. E., Katz, J., Kwon, Y., Sung, P., & Wiese, C. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.866601 · Cited by 29 · see citing works
Self-citationYuan, S., Huang, T., Bao, Z., Wang, S., Wu, X., Liu, J., Liu, H., & Chen, Z. (2022) · Genome biology · doi:10.1186/s13059-022-02758-z · Cited by 28 · see citing works
Role of BRCA2 DNA-binding and C-terminal domain in its mobility and conformation in DNA repair
Paul, M. W., Sidhu, A., Liang, Y., van Rossum-Fikkert, S. E., Odijk, H., Zelensky, A. N., Kanaar, R., & Wyman, C. (2021) · eLife · doi:10.7554/elife.67926 · Cited by 27 · see citing works
Visualization of direct and diffusion-assisted RAD51 nucleation by full-length human BRCA2 protein
Beláň, O., Greenhough, L. A., Kuhlen, L., Anand, R., Kaczmarczyk, A. P., Gruszka, D. T., Yardimci, H., Zhang, X., Rueda, D., West, S. C., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.031 · Cited by 27 · see citing works
Wang, W., Daley, J. M., Kwon, Y., Xue, X., Krasner, D. S., Miller, A. S., Nguyen, K. A., Williamson, E. A., Shim, E. Y., Lee, S. E., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.004769 · Cited by 26 · see citing works
Self-citationPharmacologically targeting protein lactylation to overcome cancer drug resistance
Wang, Y., Chen, J., Wang, Y., Zhao, J., Zhang, J., & Wang, H. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117905 · Cited by 25 · see citing works
Mishra, A. P., Hartford, S. A., Sahu, S., Klarmann, K. D., Chittela, R. K., Biswas, K., Jeon, A. B., Martin, B. K., Burkett, S. S., Southon, E. A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-29409-y · Cited by 25 · see citing works
Xu, Z., Xie, H., Song, L., Huang, Y., & Huang, J. (2025) · DNA repair · doi:10.1016/j.dnarep.2025.103847 · Cited by 24 · see citing works
Molecular flexibility of DNA as a key determinant of RAD51 recruitment
Paoletti, F., El-Sagheer, A. H., Allard, J. F., Brown, T. P., Dushek, O., & Esashi, F. (2020) · The EMBO Journal · doi:10.15252/embj.2019103002 · Cited by 23 · see citing works
Ubiquitylation in DNA double-strand break repair
Tang, M., Li, S., & Chen, J. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103129 · Cited by 22 · see citing works
Lee, J., Sung, K., Joo, S. Y., Jeong, J.-H., Kim, S. K., & Lee, H. (2022) · Nature Communications · doi:10.1038/s41467-022-31156-z · Cited by 22 · see citing works
Deveryshetty, J., Ryzhikov, M., Brahati, N., Peterlini, T., Dellaire, G., Masson, J., & Korolev, S. (2019) · eLife · doi:10.7554/elife.44063 · Cited by 22 · see citing works
Nasheuer, H., Meaney, A. M., Hulshoff, T., Thiele, I., & Onwubiko, N. O. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25010588 · Cited by 21 · see citing works
Advances in structural studies of recombination mediator proteins
Korolev, S. (2016) · Biophysical Chemistry · doi:10.1016/j.bpc.2016.12.001 · Cited by 21 · see citing works
Disparate requirements for RAD54L in replication fork reversal
Uhrig, M. E., Sharma, N., Maxwell, P., Gómez, J., Selemenakis, P., Mazin, A. V., & Wiese, C. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae828 · Cited by 20 · see citing works
Self-citationCrosstalk between CST and RPA regulates RAD51 activity during replication stress
Lei, K.-H., Yang, H.-L., Chang, H.-Y., Yeh, H.-Y., Nguyen, D.-D., Lee, T.-Y., Lyu, X., Chastain, M., Chai, W.-H., Li, H.-W., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26624-x · Cited by 22 · see citing works
Expression of Rad51 and the histo-morphological evaluation of testis of the sterile male cattle-yak
Niayale, R., Yan, C., Yu, S., Bo, L., He, H., Zhao, P., Hong-wei, X., Zhang, J., Li, S., & Zhang, Q. (2021) · Theriogenology · doi:10.1016/j.theriogenology.2021.06.018 · Cited by 20 · see citing works
Bianco, P. R. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.784451 · Cited by 21 · see citing works
Kelso, A. A., Goodson, S. D., Watts, L. E., Ledford, L. L., Waldvogel, S. M., Diehl, J. N., Shah, S. B., Say, A. F., White, J. D., & Sehorn, M. G. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw877 · Cited by 19 · see citing works
Jiménez-Sáinz, J., & Jensen, R. B. (2021) · Genes · doi:10.3390/genes12050780 · Cited by 19 · see citing works
Self-citationShailani, A., Kaur, R. P., & Munshi, A. (2018) · Medical Oncology · doi:10.1007/s12032-018-1085-8 · Cited by 19 · see citing works
Double-Stranded Break Repair in Mammalian Cells and Precise Genome Editing
Ali, A., Xiao, W., Babar, M. E., & Bi, Y. (2022) · Genes · doi:10.3390/genes13050737 · Cited by 17 · see citing works
Therapeutic disruption of RAD52–ssDNA complexation via novel drug-like inhibitors
Bhat, D. S., Malacaria, E., Biagi, L. D., Razzaghi, M., Honda, M., Hobbs, K., Hengel, S. R., Pichierri, P., Spies, M., & Spies, M. (2023) · NAR Cancer · doi:10.1093/narcan/zcad018 · Cited by 16 · see citing works
Role of the RAD51–SWI5–SFR1 Ensemble in homologous recombination
Su, G.-C., Yeh, H., Lin, S., Chung, C.-I., Huang, Y.-S., Liu, Y., Lyu, P. C., & Chi, P. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw375 · Cited by 16 · see citing works
Papageorgiou, A. C., Pospíšilová, M., Cibulka, J., Ashraf, R., Waudby, C. A., Kadeřávek, P., Maroz, V., Kubíček, K., Prokop, Z., Krejčí, L., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-42503-z · Cited by 15 · see citing works
Allosteric effects of SSB C-terminal tail on assembly ofE. coliRecOR proteins
Shinn, M. K., Kozlov, A. G., & Lohman, T. M. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1291 · Cited by 15 · see citing works
Histone chaperone ASF1 acts with RIF1 to promote DNA end joining in BRCA1-deficient cells
Tang, M., Chen, Z., Wang, C., Feng, X., Lee, N., Huang, M., Zhang, H., Li, S., Xiong, Y., & Chen, J. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101979 · Cited by 15 · see citing works
Zhou, Z., Yang, H., Liang, X., Zhou, T., Zhang, T., Yang, Y., Wang, J., & Wang, W. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112907 · Cited by 14 · see citing works
Expanded Interactome of the Intrinsically Disordered Protein Dss1
Schenstrøm, S. M., Rebula, C. A., Tatham, M. H., Hendus-Altenburger, R., Jourdain, I., Hay, R. T., Kragelund, B. B., & Hartmann‐Petersen, R. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.09.080 · Cited by 14 · see citing works
Essential Roles for Polymerase Theta-Mediated End Joining in Repair of Chromosome Breaks
Wyatt, D. W. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/5jdw-e446 · Cited by 13 · see citing works
A Newly Assigned Role of CTCF in Cellular Response to Broken DNAs
Kang, M. A., & Lee, J.-S. (2021) · Biomolecules · doi:10.3390/biom11030363 · Cited by 13 · see citing works
RAD51AP1 mediates RAD51 activity through nucleosome interaction
Pires, E., Sharma, N., Selemenakis, P., Wu, B., Huang, Y., Alimbetov, D. S., Zhao, W., & Wiese, C. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100844 · Cited by 13 · see citing works
Self-citationJulien, M., Ghouil, R., Petitalot, A., Caputo, S., Carreira, A., & Zinn-Justin, S. (2021) · Biomolecules · doi:10.3390/biom11071060 · Cited by 11 · see citing works
Falco, M. D., & Felice, M. D. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms222413296 · Cited by 13 · see citing works
An Aurora B-RPA signaling axis secures chromosome segregation fidelity
Roshan, P., Kuppa, S., Mattice, J. R., Kaushik, V., Chadda, R., Pokhrel, N., Tumala, B., Biswas, A., Bothner, B. B., Antony, E., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-38711-2 · Cited by 13 · see citing works
Elucidating Recombination Mediator Function Using Biophysical Tools
Henry, C., & Henrikus, S. S. (2021) · Biology · doi:10.3390/biology10040288 · Cited by 12 · see citing works
Ghouil, R., Miron, S. M., Koornneef, L., Veerman, J., Paul, M. W., Du, M. L., Sleddens–Linkels, E., van Rossum-Fikkert, S. E., van Loon, Y., Felipe‐Medina, N., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24871-6 · Cited by 12 · see citing works
Sgs1 Binding to Rad51 Stimulates Homology-Directed DNA Repair in Saccharomyces cerevisiae
Doerfler, L., Syed, S., & Schmidt, K. H. (2017) · Genetics · doi:10.1534/genetics.117.300545 · Cited by 12 · see citing works
Microcephaly family protein MCPH1 stabilizes RAD51 filaments
Chang, H.-Y., Lee, C., Lu, C., Lee, W., Yang, H., Yeh, H., Li, H., & Chi, P. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa636 · Cited by 12 · see citing works
- Authors
- Zhao, W., Vaithiyalingam, S., San Filippo, J., Maranon, D. G., Jimenez-Sainz, J., Fontenay, G. V., Kwon, Y., Leung, S. G., Lu, L., Jensen, R. B., Chazin, W. J., Wiese, C., & Sung, P.
- Affiliations
- Yale University (US)
- Vanderbilt University (US)
- Colorado State University (US)
- Lawrence Berkeley National Laboratory (US)
- Corresponding author
- Chazin, Walter J.
- Sung, Patrick
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2015-07
- Volume
- 59
- Issue
- 2
- Pages
- 176-187
- ISSN
- 1097-2765 (ISSN-L)
- PMC
- PMC4506714
- OpenAlex
- W1521943738
- Cited by
- 177
- References
- 64
- Citations by year
- 2026: 11 · 2025: 6 · 2024: 14 · 2023: 19 · 2022: 20 · 2021: 29 · 2020: 20 · 2019: 14 · 2018: 14 · 2017: 15 · 2016: 14 · 2015: 1
- FWCI
- 6.37
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health (GM65484, P30 CA068485, P30 ES00267, CA92584, CA168635, ES015252, ES007061, ES021454, S10 RR025677)
- Vanderbilt University
- National Science Foundation (0922862)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › BRCA gene mutations in cancer
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Keywords
- BRCA2, DSS1, RPA, RAD51, homologous recombination, single-stranded DNA binding, DNA repair, replication fork repair, genome maintenance, tumor suppression, acidic domain, protein complexes
- MeSH terms
- Breast Neoplasms, Cell Line, Female, HeLa Cells, Humans, Models, Biological, Recombinant Proteins, Mutagenesis, Site-Directed, Molecular Mimicry, Nuclear Magnetic Resonance, Biomolecular, Amino Acid Substitution, Protein Subunits, BRCA2 Protein, Proteasome Endopeptidase Complex, Rad51 Recombinase, Replication Protein A, Homologous Recombination
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