Brca1 Controls Homology-Directed DNA Repair

The double-strand-break repair model for recombination

Szostak, J. W., Orr-Weaver, T. L., Rothstein, R. J., & Stahl, F. W. (1983) · Cell · doi:10.1016/0092-8674(83)90331-8 · Cited by 2,437

Association of BRCA1 with Rad51 in Mitotic and Meiotic Cells

Scully, R., Chen, J., Plug, A., Xiao, Y., Weaver, D., Feunteun, J., Ashley, T., & Livingston, D. M. (1997) · Cell · doi:10.1016/s0092-8674(00)81847-4 · Cited by 1,459

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

Pierce, A. J., Johnson, R. D., Thompson, L. H., & Jasin, M. (1999) · Genes & Development · doi:10.1101/gad.13.20.2633 · Cited by 1,384

Gatekeepers and caretakers

Kinzler, K. W., & Vogelstein, B. (1997) · Nature · doi:10.1038/386761a0 · Cited by 1,240

The Genetic Basis of Human Cancer

Vogelstein, B., & Kinzler, K. W. (1997) · Cited by 1,120

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 1,087

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

Xu, X., Ohler, Z. W., Linke, S. P., Li, C., Gotay, J., Wang, X. W., Harris, C. C., Ried, T., & Deng, C. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80466-9 · Cited by 819

Olaparib in the management of ovarian cancer

Bixel, K. L., & Hays, J. L. (2015) · Pharmacogenomics and Personalized Medicine · doi:10.2147/pgpm.s62809 · Cited by 58

Identification of Filamin A as a BRCA1-interacting protein required for efficient DNA repair

Velkova, A., Carvalho, M. A., Johnson, J., Tavtigian, S. V., & Monteiro, Á. N. A. (2010) · Cell Cycle · doi:10.4161/cc.9.7.11256 · Cited by 55

Chromatin structure in double strand break repair

Gospodinov, A. G., & Herceg, Z. (2013) · DNA repair · doi:10.1016/j.dnarep.2013.07.006 · Cited by 56

p38γ Mitogen-Activated Protein Kinase Contributes to Oncogenic Properties Maintenance and Resistance to Poly (ADP-Ribose)-Polymerase-1 Inhibition in Breast Cancer

Meng, F., Zhang, H., Liu, G., Kreike, B., Chen, W., Sethi, S. N., Miller, F. R., & Wu, G. (2011) · Neoplasia · doi:10.1593/neo.101748 · Cited by 53

The role of BRCA1 in homologous recombination repair in response to replication stress: significance in tumorigenesis and cancer therapy

Zhang, J. (2013) · Cell & Bioscience · doi:10.1186/2045-3701-3-11 · Cited by 58

Targeting DNA repair in breast cancer: A clinical and translational update

Amir, E., Šeruga, B., Serrano, R., & Ocaña, A. (2010) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2010.03.006 · Cited by 52

Prediction of BRCA2-association in hereditary breast carcinomas using array-CGH

Joosse, S. A., Brandwijk, K. I. M., Devilee, P., Wesseling, J., Hogervorst, F. B. L., Verhoef, S., & Nederlof, P. M. (2010) · Breast Cancer Research and Treatment · doi:10.1007/s10549-010-1016-7 · Cited by 53

Hypersensitivity of Brca1-deficient MEF to the DNA interstrand crosslinking agent mitomycin C is associated with defect in homologous recombination repair and aberrant S-phase arrest

Yun, J., Zhong, Q., Kwak, J., & Lee, W. (2005) · Oncogene · doi:10.1038/sj.onc.1208575 · Cited by 53

Clinical Considerations ofBRCA1- andBRCA2-Mutation Carriers: A Review

Bougie, O., & Weberpals, J. I. (2011) · International Journal of Surgical Oncology · doi:10.1155/2011/374012 · Cited by 54

Crucial roles of the BRCA1-BARD1 E3 ubiquitin ligase activity in homology-directed DNA repair

Wang, M., Li, W., Tomimatsu, N., Yu, C. H., Ji, J., Alejo, S., Witus, S. R., Alimbetov, D. S., Fitzgerald, O. R., Wu, B., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.09.015 · Cited by 50

The BRCA1 ubiquitin ligase and homologous recombination repair

Ohta, T., Sato, K., & Wu, W. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.005 · Cited by 53

A role for XRCC2 gene polymorphisms in breast cancer risk and survival

Lin, W., Camp, N. J., Cannon‐Albright, L., Allen‐Brady, K., Balasubramanian, S. P., Reed, M., Hopper, J. L., Apicella, C., Giles, G. G., Southey, M. C., et al. (2011) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2011-100018 · Cited by 52

Genomic instability in pancreatic adenocarcinoma: a new step towards precision medicine and novel therapeutic approaches

Şahin, İ. H., Lowery, M. A., Stadler, Z. K., Salo‐Mullen, E. E., Iacobuzio–Donahue, C. A., Kelsen, D. P., & O'Reilly, E. M. (2016) · Expert Review of Gastroenterology & Hepatology · doi:10.1586/17474124.2016.1153424 · Cited by 56

Kinase-dead ATM protein is highly oncogenic and can be preferentially targeted by Topo-isomerase I inhibitors

Yamamoto, K., Wang, J., Sprinzen, L., Xu, J., Haddock, C. J., Li, C., Lee, B. J., Loredan, D. G., Jiang, W., Vindigni, A., et al. (2016) · eLife · doi:10.7554/elife.14709 · Cited by 53

Homologous recombination deficiency in breast cancer: Implications for risk, cancer development, and therapy

Ali, R., McIntosh, S., & Savage, K. I. (2020) · Genes Chromosomes and Cancer · doi:10.1002/gcc.22921 · Cited by 52

Decision for cell fate: deubiquitinating enzymes in cell cycle checkpoint

Lim, K., Song, M.-H., & Baek, K. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2129-2 · Cited by 52

Lack of the Matricellular Protein SPARC (Secreted Protein, Acidic and Rich in Cysteine) Attenuates Liver Fibrogenesis in Mice

Atorrasagasti, C., Peixoto, E., Aquino, J. B., Kippes, N., Malvicini, M., Alaniz, L. D., García, M. G., Piccioni, F., Fiore, E. J., Bayo, J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054962 · Cited by 54

Estrogen receptor beta decreases survival of p53-defective cancer cells after DNA damage by impairing G2/M checkpoint signaling

Thomas, C. G., Ström, A., Lindberg, K., & Gustafsson, J.-Α. (2010) · Breast Cancer Research and Treatment · doi:10.1007/s10549-010-1011-z · Cited by 52

Genome‐wide analysis reveals a role for BRCA1 and PALB2 in transcriptional co‐activation

Gardini, A., Baillat, D., Cesaroni, M., & Shiekhattar, R. (2014) · The EMBO Journal · doi:10.1002/embj.201385567 · Cited by 51

TRIP12 as a mediator of human papillomavirus/p16-related radiation enhancement effects

Wang, L., Zhang, P., Molkentine, D. P., Chen, C., Molkentine, J. M., Piao, H., Raju, U., Zhang, J., Valdecanas, D. R., Tailor, R. C., et al. (2016) · Oncogene · doi:10.1038/onc.2016.250 · Cited by 50

Breast Cancer Susceptibility and the DNA Damage Response

Đapic, V., Carvalho, M. A., & Monteiro, Á. N. A. (2005) · Cancer Control · doi:10.1177/107327480501200210 · Cited by 49

BRCA1- and BRCA2-related mutations: therapeutic implications in ovarian cancer

Pothuri, B. (2013) · Annals of Oncology · doi:10.1093/annonc/mdt307 · Cited by 50

An ex vivo assay of XRT-induced Rad51 foci formation predicts response to PARP-inhibition in ovarian cancer

Shah, M. M., Dobbin, Z. C., Nowsheen, S., Wielgos, M. E., Katre, A. A., Alvarez, R. D., Konstantinopoulos, P. A., Yang, E. S.-H., & Landen, C. N. (2014) · Gynecologic Oncology · doi:10.1016/j.ygyno.2014.05.009 · Cited by 50

High XIST and Low 53BP1 Expression Predict Poor Outcome after High-Dose Alkylating Chemotherapy in Patients with a BRCA1 -like Breast Cancer

Schouten, P. C., Vollebergh, M. A., Opdam, M., Jonkers, M., Lodén, M., Wesseling, J., Hauptmann, M., & Linn, S. C. (2015) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-15-0470 · Cited by 50

Should platinum-based chemotherapy be preferred for germline BReast CAncer genes (BRCA) 1 and 2-mutated pancreatic ductal adenocarcinoma (PDAC) patients? A systematic review and meta-analysis

Rebelatto, T. F., Falavigna, M., Pozzari, M., Spada, F., Cella, C. A., Laffi, A., Pellicori, S., & Fazio, N. (2019) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2019.101895 · Cited by 50

Spontaneous mitotic homologous recombination at an enhanced yellow fluorescent protein (EYFP) cDNA direct repeat in transgenic mice

Hendricks, C. A., Almeida, K. H., Stitt, M. S., Jonnalagadda, V. S., Rugo, R. E., Kerrison, G. F., & Engelward, B. P. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1232231100 · Cited by 50

Knockout mouse models and mammary tumorigenesis

Deng, C., & Brodie, S. G. (2001) · Seminars in Cancer Biology · doi:10.1006/scbi.2001.0394 · Cited by 50

BRCA1 and Prostate Cancer

Rosen, E. M., Fan, S., & Goldberg, I. D. (2001) · Cancer Investigation · doi:10.1081/cnv-100103134 · Cited by 50

Current treatment options in triple negative breast cancer

Rodler, E. T., Korde, L. A., & Gralow, J. R. (2011) · Breast Disease · doi:10.3233/bd-2010-0304 · Cited by 49

Replication stress triggers microsatellite destabilization and hypermutation leading to clonal expansion in vitro

Matsuno, Y., Atsumi, Y., Shimizu, A., Katayama, K., Fujimori, H., Hyodo, M., Minakawa, Y., Nakatsu, Y., Kaneko, S., Hamamoto, R., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11760-2 · Cited by 49

Bax and Bid, two proapoptotic Bcl-2 family members, inhibit homologous recombination, independently of apoptosis regulation

Dumay, A., Laulier, C., Bertrand, P., Saintigny, Y., Lebrun, F., Vayssière, J.-L., & López, B. S. (2005) · Oncogene · doi:10.1038/sj.onc.1209344 · Cited by 49

A Genetic Screen For DNA Double-Strand Break Repair Mutations in Drosophila

Wei, D., & Rong, Y. S. (2007) · Genetics · doi:10.1534/genetics.107.077693 · Cited by 49

Mutations in the BRCT binding site of BRCA1 result in hyper-recombination

Dever, S. M., Golding, S. E., Rosenberg, E., Adams, B. R., Idowu, M. O., Quillin, J. M., Valerie, N. C. K., Xu, B., Povirk, L. F., & Valerie, K. C. (2011) · Aging · doi:10.18632/aging.100325 · Cited by 50

Involvement of a specificity proteins-binding element in regulation of basal and estrogen-induced transcription activity of the BRCA1gene

Hockings, J. K., Degner, S. C., Morgan, S. S., Kemp, M. Q., & Romagnolo, D. F. (2008) · Breast Cancer Research · doi:10.1186/bcr1987 · Cited by 48

The relative efficiency of homology-directed repair has distinct effects on proper anaphase chromosome separation

Laulier, C., Cheng, A., & Stark, J. M. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr187 · Cited by 52

Sensitization of tamoxifen-resistant breast cancer cells by Z-ligustilide through inhibiting autophagy and accumulating DNA damages

Qi, H., Jiang, Z., Wang, C., Yang, Y., Li, L., He, H., & Yu, Z. (2017) · Oncotarget · doi:10.18632/oncotarget.16832 · Cited by 49

Early Events in the DNA Damage Response

Ward, I. M., & Chen, J. (2004) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/s0070-2153(04)63001-8 · Cited by 50

Fanconi Anemia Proteins, DNA Interstrand Crosslink Repair Pathways, and Cancer Therapy

Andreassen, P. R., & Ren, K. (2009) · Current Cancer Drug Targets · doi:10.2174/156800909787314011 · Cited by 50

Integrator3, a Partner of Single-stranded DNA-binding Protein 1, Participates in the DNA Damage Response

Zhang, F., Wu, J., & Yu, X. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.039404 · Cited by 51

BRCA1 promotes the ubiquitination of PCNA and recruitment of translesion polymerases in response to replication blockade

Tian, F., Sharma, S., Zou, J., Lin, S., Wang, B., Rezvani, K. S., Wang, H., Parvin, J. D., Ludwig, T., Canman, C. E., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1306534110 · Cited by 48

Put a RING on it: regulation and inhibition of RNF8 and RNF168 RING finger E3 ligases at DNA damage sites

Bartocci, C., & Denchi, E. L. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00128 · Cited by 50

Breast Cancers with a BRCA1 -like DNA Copy Number Profile Recur Less Often Than Expected after High-Dose Alkylating Chemotherapy

Schouten, P. C., Marmé, F., Aulmann, S., Sinn, H., Essen, H. F. H. V., Ylstra, B., Hauptmann, M., Schneeweiß, A., & Linn, S. C. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-14-1894 · Cited by 47

Predictors and Modulators of Synthetic Lethality: An Update on PARP Inhibitors and Personalized Medicine

Murata, S., Zhang, C., Finch, N., Zhang, K., Campo, L., & Breuer, E.-K. Y. (2016) · BioMed Research International · doi:10.1155/2016/2346585 · Cited by 47

Understanding the Histone DNA Repair Code: H4K20me2 Makes Its Mark

Paquin, K. L., & Howlett, N. G. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-17-0688 · Cited by 48

Preclinical mouse models for BRCA1-associated breast cancer

Drost, R., & Jonkers, J. (2009) · British Journal of Cancer · doi:10.1038/sj.bjc.6605350 · Cited by 48

BRCA1 interacts with FHL2 and enhances FHL2 transactivation function

Yan, J., Zhu, J., Zhong, H.-J., Lu, Q., Huang, C., & Ye, Q. (2003) · FEBS Letters · doi:10.1016/s0014-5793(03)00978-5 · Cited by 46

Regeneration in the metazoans: why does it happen?

Alvarado, A. S. (2000) · BioEssays · doi:10.1002/(sici)1521-1878(200006)22:6 · Cited by 342

Identification of gene fusion transcripts by transcriptome sequencing in BRCA1-mutated breast cancers and cell lines

Ha, K., Lalonde, E., Li, L., Cavallone, L., Natrajan, R., Lambros, M. B. K., Mitsopoulos, C., Hakas, J., Kozarewa, I., Fenwick, K., et al. (2011) · BMC Medical Genomics · doi:10.1186/1755-8794-4-75 · Cited by 46

AKT regulates BRCA1 stability in response to hormone signaling

Nelson, A., Lyons, T. R., Young, C. D., Hansen, K. C., Anderson, S. M., & Holt, J. T. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.01.019 · Cited by 46

BRCA1 Pathway Function in Basal-Like Breast Cancer Cells

Hill, S. J., Clark, A. P., Silver, D. P., & Livingston, D. M. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01646-13 · Cited by 44

Regulating BRCA1 protein stability by cathepsin S-mediated ubiquitin degradation

Kim, S., Jin, H. K., Seo, H. R., Lee, H. J., & Lee, Y. (2018) · Cell Death and Differentiation · doi:10.1038/s41418-018-0153-0 · Cited by 47

Targeting BRCA Deficiency in Breast Cancer: What are the Clinical Evidences and the Next Perspectives?

Nicolas, E., Bertucci, F., Sabatier, R., & Gonçalvès, A. (2018) · Cancers · doi:10.3390/cancers10120506 · Cited by 47

Understanding the functions of BRCA1 in the DNA-damage response

Yun, M. H., & Hiom, K. J. (2009) · Biochemical Society Transactions · doi:10.1042/bst0370597 · Cited by 49

The Epstein-Barr Virus Replication Protein BBLF2/3 Provides an Origin-Tethering Function through Interaction with the Zinc Finger DNA Binding Protein ZBRK1 and the KAP-1 Corepressor

Liao, G., Huang, J., Fixman, E. D., & Hayward, S. D. (2004) · Journal of Virology · doi:10.1128/jvi.79.1.245-256.2005 · Cited by 46

PARP inhibition: targeting the Achilles' heel of DNA repair to treat germline and sporadic ovarian cancers

Carden, C. P., Yap, T. A., & Kaye, S. B. (2010) · Current Opinion in Oncology · doi:10.1097/cco.0b013e32833b5126 · Cited by 43

53BP1 ablation rescues genomic instability in mice expressing ‘RING‐less’ BRCA1

Li, M., Cole, F., Patel, D. S., Misenko, S. M., Her, J., Malhowski, A. J., Alhamza, A., Zheng, H., Baer, R. J., Ludwig, T., et al. (2016) · EMBO Reports · doi:10.15252/embr.201642497 · Cited by 47

Targeting DNA repair: the genome as a potential biomarker

Nesic, K., Wakefield, M. J., Kondrashova, O., Scott, C. L., & McNeish, I. A. (2017) · The Journal of Pathology · doi:10.1002/path.5025 · Cited by 47

Exploring the Role of Fallopian Ciliated Cells in the Pathogenesis of High-Grade Serous Ovarian Cancer

Coan, M., Vinciguerra, G. L. R., Cesaratto, L., Gardenal, E., Bianchet, R., Dassi, E., Vecchione, A. M., Baldassarre, G., Spizzo, R., & Nicoloso, M. S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092512 · Cited by 46

FANCD2 associated with sporadic breast cancer risk

Barroso, E. (2006) · Carcinogenesis · doi:10.1093/carcin/bgl062 · Cited by 45

A novel time-course cDNA microarray analysis method identifies genes associated with the development of cisplatin resistance

Whiteside, M. A., Chen, D., Desmond, R. A., Abdulkadir, S. A., & Johanning, G. L. (2004) · Oncogene · doi:10.1038/sj.onc.1207164 · Cited by 44

Pharmacokinetic Study of Rucaparib in Patients With Advanced Solid Tumors

Shapiro, G. I., Kristeleit, R. S., Burris, H. A., LoRusso, P. M., Patel, M. R., Drew, Y., Giordano, H., Maloney, L., Watkins, S. P., Goble, S. M., et al. (2018) · Clinical Pharmacology in Drug Development · doi:10.1002/cpdd.575 · Cited by 47

DNA Repair and Ovarian Carcinogenesis: Impact on Risk, Prognosis and Therapy Outcome

Tomášová, K., Čumová, A., Šeborová, K., Horak, J., Koucká, K., Vodičková, Ľ., Václavíková, R., & Vodička, P. (2020) · Cancers · doi:10.3390/cancers12071713 · Cited by 47

Loss of Brca2 and p53 synergistically promotes genomic instability and deregulation of T-cell apoptosis.

Cheung, A., Hande, M. P., Jalali, F., Tsao, M., Skinnider, B., Hirao, A., McPherson, J. P., Karásková, J., Suzuki, A., Wakeham, A. C., et al. (2002) · PubMed · Cited by 44

Synchrotron photoactivation of cisplatin elicits an extra number of DNA breaks that stimulate RAD51-mediated repair pathways.

Corde, S., Balosso, J., Elleaume, H., Renier, M., Joubert, A., Biston, M., Adam, J., Charvet, A., Brochard, T., Bas, J. L., et al. (2003) · PubMed · Cited by 44

BRCA1 Interacts with and Is Required for Paclitaxel-Induced Activation of Mitogen-Activated Protein Kinase Kinase Kinase 3

Gilmore, P. M., McCabe, N., Quinn, J. E., Kennedy, R. D., Gorski, J. J., Andrews, H. N., McWilliams, S., Carty, M., Mullan, P. B., Duprex, W. P., et al. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-4080 · Cited by 45

Pir51, a Rad51-interacting protein with high expression in aggressive lymphoma, controls mitomycin C sensitivity and prevents chromosomal breaks

Henson, S. E., Tsai, S.-C., Malone, C. S., Soghomonian, S. V., Ouyang, Y., Wall, R., Marahrens, Y., & Teitell, M. A. (2006) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2006.06.016 · Cited by 40

Genetic analysis of homologous DNA recombination in vertebrate somatic cells

Morrison, C. G., & Takeda, S. (2000) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(00)00033-9 · Cited by 43

Genome-Wide Loss of Heterozygosity and Uniparental Disomy in BRCA1/2-Associated Ovarian Carcinomas

Walsh, C., Ogawa, S., Scoles, D. R., Miller, C. W., Kawamata, N., Narod, S. A., Koeffler, H. P., & Karlan, B. Y. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-1291 · Cited by 43

Methylation of O 6-methylguanine-DNA methyltransferase (MGMT) promoter gene in triple-negative breast cancer patients

Fumagalli, C., Pruneri, G., Possanzini, P., Manzotti, M., Barile, M., Feroce, I., Colleoni, M. A., Bonanni, B., Maisonneuve, P., Radice, P., et al. (2012) · Breast Cancer Research and Treatment · doi:10.1007/s10549-011-1945-9 · Cited by 42

Association of BRCA1 with the inactive X chromosome and XIST RNA

Ganesan, S., Silver, D. P., Drapkin, R., Greenberg, R. A., Feunteun, J., & Livingston, D. M. (2004) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2003.1371 · Cited by 43

Bcl-2 Inhibits Nuclear Homologous Recombination by Localizing BRCA1 to the Endomembranes

Laulier, C., Barascu, A., Guirouilh‐Barbat, J., Pennarun, G., Chalony, C. L., Chevalier, F., Palierne, G., Bertrand, P., Verbavatz, J., & López, B. S. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3119 · Cited by 49

Polo-like kinase 1 mediates BRCA1 phosphorylation and recruitment at DNA double-strand breaks

Chabalier-Taste, C., Brichese, L., Racca, C., Canitrot, Y., Calsou, P., & Larminat, F. (2016) · Oncotarget · doi:10.18632/oncotarget.6825 · Cited by 42

SMC1α Substitutes for Many Meiotic Functions of SMC1β but Cannot Protect Telomeres from Damage

Biswas, U., Stevense, M., & Jessberger, R. (2018) · Current Biology · doi:10.1016/j.cub.2017.12.020 · Cited by 42

Homologous Recombination as a Fundamental Genome Surveillance Mechanism during DNA Replication

Spies, J., Polášek-Sedláčková, H., Lukas, J., & Somyajit, K. (2021) · Genes · doi:10.3390/genes12121960 · Cited by 47

Characterization of a Novel Trans-Activation Domain of BRCA1 That Functions in Concert with the BRCA1 C-terminal (BRCT) Domain

Hu, Y., Miyake, T., Ye, Q., & Li, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.c000607200 · Cited by 42

Structural Determinants of Human FANCF Protein That Function in the Assembly of a DNA Damage Signaling Complex

Kowal, P., Gurtan, A. M., Stuckert, P., D’Andrea, A. D., & Ellenberger, T. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m608356200 · Cited by 41

Gene conversion and deletion frequencies during double-strand break repair in human cells are controlled by the distance between direct repeats

Schildkraut, E. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki295 · Cited by 42

BRCA1 modulates ionizing radiation‐induced nuclear focus formation by the replication protein A p34 subunit

Choudhary, S. K., & Li, R. (2002) · Journal of Cellular Biochemistry · doi:10.1002/jcb.10081 · Cited by 42

Functional Dissection of Transcription Factor ZBRK1 Reveals Zinc Fingers with Dual Roles in DNA-binding and BRCA1-dependent Transcriptional Repression

Tan, W., Zheng, L., Lee, W., & Boyer, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312270200 · Cited by 42

Synthetic Lethality in Ovarian Cancer

Chandrasekaran, A., & Elias, K. M. (2021) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0500 · Cited by 41

BRCA1 16 years later: DNA damage‐induced BRCA1 shuttling

Yang, E. S.-H., & Xia, F. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07734.x · Cited by 41

Mutator Phenotype ofCaenorhabditis elegansDNA Damage Checkpoint Mutants

Harris, J., Lowden, M. R., Clejan, I., Tzoneva, M., Thomas, J. H., Hodgkin, J., & Ahmed, S. C. (2006) · Genetics · doi:10.1534/genetics.106.058701 · Cited by 41

Clinical and biological significance of RAD51 expression in breast cancer: a key DNA damage response protein

Alshareeda, A. T., Negm, O. H., Aleskandarany, M. A., Green, A. R., Nolan, C. C., TigHhe, P. J., Madhusudan, S., Ellis, I. O., & Rakha, E. A. (2016) · Breast Cancer Research and Treatment · doi:10.1007/s10549-016-3915-8 · Cited by 41

Chemopreventive Effects of ROS Targeting in a Murine Model of BRCA1-Deficient Breast Cancer

Li, M., Chen, Q., & Yu, X. (2016) · Cancer Research · doi:10.1158/0008-5472.can-16-2350 · Cited by 41

Factors forming the BRCA1-A complex orchestrate BRCA1 recruitment to the sites of DNA damage

Her, J., Lee, N. S., Kim, Y., & Kim, H. (2016) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmw047 · Cited by 43

FANCJ: Solving problems in DNA replication

Hiom, K. J. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.01.005 · Cited by 41

BRCC36A is epistatic to BRCA1 in DNA crosslink repair and homologous recombination in Arabidopsis thaliana

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