Brca1 Controls Homology-Directed DNA Repair

The double-strand-break repair model for recombination

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Association of BRCA1 with Rad51 in Mitotic and Meiotic Cells

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XRCC3 promotes homology-directed repair of DNA damage in mammalian cellsPreprint

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Gatekeepers and caretakers

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The Genetic Basis of Human Cancer

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Embryonic lethality and radiation hypersensitivity mediated by Rad51 in mice lacking Brca2

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Centrosome Amplification and a Defective G2–M Cell Cycle Checkpoint Induce Genetic Instability in BRCA1 Exon 11 Isoform–Deficient Cells

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DNA double-strand break repair and chromosome translocations

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BARD1 Participates with BRCA1 in Homology-Directed Repair of Chromosome Breaks

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PML Colocalizes with and Stabilizes the DNA Damage Response Protein TopBP1

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BRCA1 : mechanisms of inactivation and implications for management of patients

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CtIP-mediated resection is essential for viability and can operate independently of BRCA1

Polato, F., Callén, E., Wong, N., Faryabi, R. B., Bunting, S. F., Chen, H. T., Kozak, M., Kruhlak, M. J., Reczek, C. R., Lee, W., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20131939 · Cited by 123

Checkpoint Kinase 2–Mediated Phosphorylation of BRCA1 Regulates the Fidelity of Nonhomologous End-Joining

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New complexities for BRCA1 and BRCA2

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BRCA1 methylation: a significant role in tumour development?

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BRCA1-deficient mammary tumor cells are dependent on EZH2 expression and sensitive to Polycomb Repressive Complex 2-inhibitor 3-deazaneplanocin A

Puppe, J., Drost, R., Liu, X., Joosse, S. A., Evers, B., Cornelissen‐Steijger, P., Nederlof, P. M., Yu, Q., Jonkers, J., van Lohuizen, M., et al. (2009) · Breast Cancer Research · doi:10.1186/bcr2354 · Cited by 117

Role of homologous recombination in carcinogenesis

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The PARP inhibitor AZD2281 (Olaparib) induces autophagy/mitophagy in BRCA1 and BRCA2 mutant breast cancer cells

Arun, B., Akar, U., Gutierrez‐Barrera, A. M., Hortobágyi, G. N., & Özpolat, B. (2015) · International Journal of Oncology · doi:10.3892/ijo.2015.3003 · Cited by 115

Targeting homologous recombination repair defects in cancer

Evers, B., Helleday, T., & Jonkers, J. (2010) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.06.001 · Cited by 115

The cancer connection: BRCA1 and BRCA2 tumor suppression in mice and humans

Moynahan, M. E. (2002) · Oncogene · doi:10.1038/sj.onc.1206177 · Cited by 114

Predictive biomarkers for cancer therapy with PARP inhibitors

Michels, J., Vitale, I., Saparbaev, M. K., Castedo, M., & Kroemer, G. (2013) · Oncogene · doi:10.1038/onc.2013.352 · Cited by 117

Impaired DNA Damage Response in Cells Expressing an Exon 11-Deleted Murine Brca1 Variant That Localizes to Nuclear Foci

Huber, L. J., Yang, T. W., Sarkisian, C. J., Master, S. R., Deng, C., & Chodosh, L. A. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.12.4005-4015.2001 · Cited by 112

Activation of BRCA1/BRCA2-Associated Helicase BACH1 Is Required for Timely Progression through S Phase

Kumaraswamy, E., & Shiekhattar, R. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00961-07 · Cited by 110

DNA double-strand break repair signalling: The case of RAD51 post-translational regulation

Daboussi, F., Dumay, A., Delacôte, F., & López, B. S. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(02)00052-9 · Cited by 107

Checking in on Cds1 (Chk2): A checkpoint kinase and tumor suppressor

McGowan, C. H. (2002) · BioEssays · doi:10.1002/bies.10101 · Cited by 109

The role of BRCA1 in DNA double-strand repair: Past and present

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Double-strand break repair by homologous recombination in primary mouse somatic cells requires BRCA1 but not the ATM kinase

Kass, E. M., Helgadottir, H. R., Chen, C.-C., Barbera, M. A., Wang, R., Westermark, U., Ludwig, T., Moynahan, M. E., & Jasin, M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1216824110 · Cited by 110

BRCA1, PARP, and 53BP1: conditional synthetic lethality and synthetic viability

Aly, A., & Ganesan, S. (2011) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjq055 · Cited by 116

Cell-cycle responses to DNA damage in G2

Cuddihy, A. R., & O'Connell, M. J. (2003) · International Review of Cytology · doi:10.1016/s0074-7696(02)22013-6 · Cited by 89

BRCA1 Inhibits Membrane Estrogen and Growth Factor Receptor Signaling to Cell Proliferation in Breast Cancer

Razandi, M., Pedram, A., Rosen, E. M., & Levin, E. R. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.13.5900-5913.2004 · Cited by 108

Making the best of PARP inhibitors in ovarian cancer

Banerjee, S. N., Kaye, S. B., & Ashworth, A. (2010) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2010.116 · Cited by 107

BRCA1 establishes DNA damage signaling and pericentric heterochromatin of the X chromosome in male meiosis

Broering, T. J., Alavattam, K. G., Sadreyev, R. I., Ichijima, Y., Kato, Y., Hasegawa, K., Camerini‐Otero, R. D., Lee, J. T., Andreassen, P. R., & Namekawa, S. H. (2014) · The Journal of Cell Biology · doi:10.1083/jcb.201311050 · Cited by 100

RING domain–deficient BRCA1 promotes PARP inhibitor and platinum resistance

Wang, Y., Krais, J. J., Bernhardy, A. J., Nicolas, É., Cai, K. Q., Harrell, M. I., Kim, H. H., George, E. M., Swisher, E. M., Simpkins, F. A., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci87033 · Cited by 110

Nanoparticle-mediated delivery of siRNA targeting Parp1 extends survival of mice bearing tumors derived from Brca1-deficient ovarian cancer cells

Goldberg, M. S., Xing, D., Ren, Y., Oršulić, S., Bhatia, S. N., & Sharp, P. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016538108 · Cited by 107

BRCA1 Regulates RAD51 Function in Response to DNA Damage and Suppresses Spontaneous Sister Chromatid Replication Slippage: Implications for Sister Chromatid Cohesion, Genome Stability, and Carcinogenesis

Cousineau, I., Abaji, C., & Belmaaza, A. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-2156 · Cited by 108

HP1 promotes tumor suppressor BRCA1 functions during the DNA damage response

Lee, Y.-H., Kuo, C., Stark, J. M., Shih, H., & Ann, D. K. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt231 · Cited by 116

Assessment of functional effects of unclassified genetic variants

Couch, F. J., Rasmussen, L. J., Hofstra, R. M. W., Monteiro, Á. N. A., Greenblatt, M. S., de Wind, N., & for the IARC Unclassified Genetic Variants Working Group (2008) · Human Mutation · doi:10.1002/humu.20899 · Cited by 111

Ataxia Telangiectasia Mutated and Checkpoint Kinase 2 Regulate BRCA1 to Promote the Fidelity of DNA End-Joining

Wang, H., Chou, W., Shieh, S.-Y., & Shen, C. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3270 · Cited by 109

Phase I study of olaparib in combination with liposomal doxorubicin in patients with advanced solid tumours

Conte, G. D., Sessa, C., von Moos, R., Viganò, L., Digena, T., Locatelli, A., Gallerani, E., Fasolo, A., Tessari, A., Cathomas, R. L., et al. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.345 · Cited by 104

Minding the gap: The underground functions of BRCA1 and BRCA2 at stalled replication forks

Nagaraju, G., & Scully, R. (2007) · DNA repair · doi:10.1016/j.dnarep.2007.02.020 · Cited by 103

Tumor Suppressor p53 Is Required To Modulate BRCA1 Expression

Arizti, P., Li, F., Park, I., Yin, Y., Solomon, E., Ouchi, T., Aaronson, S. A., & Lee, S. W. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.20.7450-7459.2000 · Cited by 102

DNA damage accumulates and responses are engaged in human ALS brain and spinal motor neurons and DNA repair is activatable in iPSC-derived motor neurons with SOD1 mutations

Kim, B., Jeong, Y. E., Wong, M., & Martin, L. J. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0874-4 · Cited by 109

Inactivation of human SRBC, located within the 11p15.5-p15.4 tumor suppressor region, in breast and lung cancers.

Xu, X. L., Wu, L. C., Du, F., Davis, A., Peyton, M., Tomizawa, Y., Maitra, A., Tomlinson, G. E., Gazdar, A. F., Weissman, B. E., et al. (2001) · PubMed · Cited by 103

Overexpression of a protein fragment of RNA helicase A causes inhibition of endogenous BRCA1 function and defects in ploidy and cytokinesis in mammary epithelial cells

Schlegel, B. P., Starita, L. M., & Parvin, J. D. (2003) · Oncogene · doi:10.1038/sj.onc.1206195 · Cited by 102

The BRCA1 suppressor hypothesis: An explanation for the tissue-specific tumor development in BRCA1 patients

Elledge, S. J., & Amon, A. (2002) · Cancer Cell · doi:10.1016/s1535-6108(02)00041-7 · Cited by 100

BRCA1 Promotes Induction of ssDNA by Ionizing Radiation

Schlegel, B. P., Jodelka, F. M., & Núñez, R. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3209 · Cited by 107

How do mutations affecting the breast cancer genes BRCA1 and BRCA2 cause cancer susceptibility?

Venkitaraman, A. R. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.102668 · Cited by 111

Triple Negative Breast Cancer: A Mountain Yet to Be Scaled Despite the Triumphs

Wu, Q., Siddharth, S., & Sharma, D. (2021) · Cancers · doi:10.3390/cancers13153697 · Cited by 110

The Fanconi road to cancer: Figure 1.Preprint

D’Andrea, A. D. (2003) · Genes & Development · doi:10.1101/gad.1128303 · Cited by 99

Serine-linked PARP1 auto-modification controls PARP inhibitor response

Prokhorova, E. A., Zobel, F., Smith, R., Zentout, S., Gibbs‐Seymour, I., Schützenhofer, K., Peters, A., Groslambert, J., Zorzini, V., Agnew, T., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24361-9 · Cited by 102

XRCC2 Is a Nuclear RAD51-like Protein Required for Damage-dependent RAD51 Focus Formation without the Need for ATP Binding

O’Regan, P., Wilson, C. R., Townsend, S., & Thacker, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102396200 · Cited by 99

A single mutated BRCA1 allele leads to impaired fidelity of double strand break end-joining

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BRCA1 Is a Selective Co-activator of 14-3-3ς Gene Transcription in Mouse Embryonic Stem Cells

Aprelikova, O. N., Pace, A. J., Fang, B. S., Koller, B. H., & Liu, E. T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100265200 · Cited by 99

BRCA1 Mutation-Specific Responses to 53BP1 Loss-Induced Homologous Recombination and PARP Inhibitor Resistance

Nacson, J., Krais, J. J., Bernhardy, A. J., Clausen, E., Feng, W., Wang, Y., Nicolas, É., Cai, K. Q., Tricarico, R., Hua, X., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.08.086 · Cited by 99

PARP Inhibitors and Prostate Cancer: To Infinity and BeyondBRCA

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DNA damage responses and their many interactions with the replication fork

Andreassen, P. R., Ho, G. P. H., & D’Andrea, A. D. (2006) · Carcinogenesis · doi:10.1093/carcin/bgi319 · Cited by 99

Reduced Proficiency in Homologous Recombination Underlies the High Sensitivity of Embryonal Carcinoma Testicular Germ Cell Tumors to Cisplatin and Poly (ADP-Ribose) Polymerase Inhibition

Cavallo, F., Graziani, G., Antinozzi, C., Feldman, D. R., Houldsworth, J., Bosl, G. J., Chaganti, R. S. K., Moynahan, M. E., Jasin, M., & Barchi, M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0051563 · Cited by 98

Collaboration of Werner syndrome protein and BRCA1 in cellular responses to DNA interstrand cross-links

Cheng, W.-H., Kusumoto, R., Opresko, P. L., Sui, X., Huang, S., Nicolette, M. L., Paull, T. T., Campisi, J., Seidman, M. M., & Bohr, V. A. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl362 · Cited by 98

BLM helicase regulates DNA repair by counteracting RAD51 loading at DNA double-strand break sites

Patel, D. S., Misenko, S. M., Her, J., & Bunting, S. F. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201703144 · Cited by 98

Negative Cell Cycle Regulation and DNA Damage-inducible Phosphorylation of the BRCT Protein 53BP1

Xia, Z., Morales, J. C., Dunphy, W. G., & Carpenter, P. B. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007665200 · Cited by 96

Targeting poly(ADP-ribosyl)ation: a promising approach in cancer therapy

Haince, J.-F., Rouleau, M., Hendzel, M. J., Masson, J., & Poirier, G. G. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.08.003 · Cited by 98

Polymorphisms in DNA double-strand break repair genes and breast cancer risk in the Nurses' Health Study

Han, J. (2003) · Carcinogenesis · doi:10.1093/carcin/bgh002 · Cited by 96

BRCA1 and BRCA2 mutations and the risk for colorectal cancer

Sopik, V., Phelan, C., Cybulski, C., & Narod, S. A. (2014) · Clinical Genetics · doi:10.1111/cge.12497 · Cited by 95

Homologous recombination deficiency leads to profound genetic instability in cells derived from Xrcc2-knockout mice.

Deans, B., Griffin, C. S., O’Regan, P., Jasin, M., & Thacker, J. (2003) · PubMed · Cited by 95

BRC‐1 acts in the inter‐sister pathway of meiotic double‐strand break repair

Adamo, A., Montemauri, P., Silva, N., Ward, J. D., Boulton, S. J., & Volpe, A. L. (2008) · EMBO Reports · doi:10.1038/sj.embor.7401167 · Cited by 92

BRCA2 Hypomorphic Missense Variants Confer Moderate Risks of Breast Cancer

Shimelis, H., Mesman, R. L. S., Nicolai, C. V., Ehlén, Å., Guidugli, L., Martin, C. A., Calléja, F. M. G. R., Meeks, H., Hallberg, E., Hinton, J., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2568 · Cited by 96

DNA repair and damage pathways in breast cancer development and therapy

Majidinia, M., & Yousefi, B. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.03.009 · Cited by 92

Cyclin D1 Antagonizes BRCA1 Repression of Estrogen Receptor α Activity

Wang, C., Fan, S., Li, Z., Fu, M., Rao, M., Ma, Y., Lisanti, M. P., Albanese, C., Katzenellenbogen, B. S., Kushner, P. J., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0486 · Cited by 93

The role of the DNA double-strand break response network in meiosis

Richardson, C. A., Horikoshi, N., & Pandita, T. K. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.05.007 · Cited by 94

Homologous recombination proficiency in ovarian and breast cancer patients

Creeden, J. F., Nanavaty, N. S., Einloth, K. R., Gillman, C. E., Stanbery, L., Hamouda, D., Dworkin, L. D., & Nemunaitis, J. J. (2021) · BMC Cancer · doi:10.1186/s12885-021-08863-9 · Cited by 96

BRCA1 Inhibition of Telomerase Activity in Cultured Cells

Xiong, J., Fan, S., Meng, Q., Schramm, L., Wang, C., Bouzahza, B., Zhou, J., Zafonte, B. T., Goldberg, I. D., Haddad, B. R., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.23.8668-8690.2003 · Cited by 96

DNA cross-link-dependent RAD50/MRE11/NBS1 subnuclear assembly requires the Fanconi anemia C protein

Pichierri, P. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.21.2531 · Cited by 90

Replication and recombination intersect

Marians, K. J. (2000) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(00)00059-9 · Cited by 91

Transcriptional Regulation of the Base Excision Repair Pathway by BRCA1

Saha, T., Rih, J. K., Roy, R., Ballal, R. D., & Rosen, E. M. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.104430 · Cited by 93

Opposing roles for 53BP1 during homologous recombination

Kakarougkas, A., Ismail, A., Klement, K., Goodarzi, A. A., Conrad, S., Freire, R., Shibata, A., Löbrich, M., & Jeggo, P. A. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt729 · Cited by 98

Targeting the DNA damage response for cancer therapy

Powell, S. N., & Bindra, R. S. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.04.011 · Cited by 86

Germline de novo mutation clusters arise during oocyte aging in genomic regions with high double-strand-break incidence

Goldmann, J. M., Seplyarskiy, V. B., Wong, W. S. W., Vilboux, T., Neerincx, P. B. T., Bodian, D. L., Solomon, B. D., Veltman, J. A., Deeken, J. F., Gilissen, C., et al. (2018) · Nature Genetics · doi:10.1038/s41588-018-0071-6 · Cited by 89

Recombination: a frank view of exchanges and vice versa

Haber, J. E. (2000) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00090-9 · Cited by 89

BACH1 is a DNA repair protein supporting BRCA1 damage response

Peng, M., Litman, R., Jin, Z., Fong, G., & Cantor, S. B. (2006) · Oncogene · doi:10.1038/sj.onc.1209257 · Cited by 88

BRCA1 and cell signaling

Wang, Q., Zhang, H., Fishel, R. A., & Greene, M. I. (2000) · Oncogene · doi:10.1038/sj.onc.1203974 · Cited by 87

Distinct functions of BRCA1 and BRCA2 in double-strand break repair

Liu, Y., & West, S. C. (2001) · Breast Cancer Research · doi:10.1186/bcr417 · Cited by 87

Modeling Therapy Resistance in BRCA1/2 -Mutant Cancers

Dréan, A., Williamson, C. T., Brough, R., Brandsma, I., Menon, M. R., Konde, A., García-Murillas, I., Pemberton, H. N., Frankum, J. R., Rafiq, R., et al. (2017) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0098 · Cited by 84

Homologous recombination as a mechanism for genome rearrangements: environmental and genetic effects

Bishop, A. J. R. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.16.2427 · Cited by 86

BRCA1: exploring the links to transcription

Monteiro, Á. N. A. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01632-7 · Cited by 87

Distinct Roles of FANCO/RAD51C Protein in DNA Damage Signaling and Repair

Somyajit, K., Subramanya, S., & Nagaraju, G. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.311241 · Cited by 88

Molecular Functions of BRCA1 in the DNA Damage Response

Scully, R., Xie, A., & Nagaraju, G. (2004) · Cancer Biology & Therapy · doi:10.4161/cbt.3.6.842 · Cited by 85

Mutant BRCA1 genes antagonize phenotype of wild-type BRCA1

Fan, S., Yuan, R., Ma, Y. X., Meng, Q., Goldberg, I. D., & Rosen, E. M. (2001) · Oncogene · doi:10.1038/sj.onc.1205033 · Cited by 85

When Genome Maintenance Goes Badly Awry

Kass, E. M., Moynahan, M. E., & Jasin, M. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.021 · Cited by 84

Cellular senescence and DNA repair

Lou, Z., & Chen, J. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2006.06.009 · Cited by 82

DNA double-strand break signaling and human disorders

Bohgaki, T., Bohgaki, M., & Hakem, R. (2010) · Genome Integrity · doi:10.1186/2041-9414-1-15 · Cited by 95

Making the best of the loose ends: Mre11/Rad50 complexes and Sae2 promote DNA double-strand break resection

Paull, T. T. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.09.015 · Cited by 90

BRCA1 loss activates cathepsin L–mediated degradation of 53BP1 in breast cancer cells

Grotsky, D. A., González-Suárez, I., Novell, A., Neumann, M. A., Yaddanapudi, S. C., Croke, M., Martínez‐Alonso, M., Redwood, A. B., Ortega‐Martínez, S., Feng, Z., et al. (2013) · The Journal of Cell Biology · doi:10.1083/jcb.201204053 · Cited by 89

DNA Damage Induces p53-dependent BRCA1 Nuclear Export

Feng, Z., Kachnic, L. A., Zhang, J., Powell, S. N., & Xia, F. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m404137200 · Cited by 85

The BRCT Domains of the BRCA1 and BARD1 Tumor Suppressors Differentially Regulate Homology-Directed Repair and Stalled Fork Protection

Billing, D. L., Horiguchi, M., Wu-Baer, F., Taglialatela, A., Leuzzi, G., Nanez, S. A., Jiang, W., Zha, S., Szabolcs, M. J., Lin, C., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.08.016 · Cited by 86

NFBD1, a Novel Nuclear Protein with Signature Motifs of FHA and BRCT, and an Internal 41-Amino Acid Repeat Sequence, Is an Early Participant in DNA Damage Response

Shang, Y. L., Bodero, A. J., & Chen, P. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210749200 · Cited by 82

BRCC36 Is Essential for Ionizing Radiation–Induced BRCA1 Phosphorylation and Nuclear Foci Formation

Chen, X., Arciero, C. A., Wang, C., Broccoli, D., & Godwin, A. K. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-4194 · Cited by 82

Programmable DNA repair with CRISPRa/i enhanced homology-directed repair efficiency with a single Cas9

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The interaction between CtIP and BRCA1 is not essential for resection-mediated DNA repair or tumor suppression

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