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

The Fanconi anemia pathway and the DNA interstrand cross-links repair

Rosselli, F. (2003) · Biochimie · doi:10.1016/j.biochi.2003.11.002 · Cited by 28

BRCA1 interacts with dominant negative SWI/SNF enzymes without affecting homologous recombination or radiation‐induced gene activation of p21 or Mdm2

Hill, D. A., de la Serna, I. L., Veal, T. M., & Imbalzano, A. N. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20003 · Cited by 27

PARP1 suppresses homologous recombination events in mice in vivo

Claybon, A. B., Karia, B., Bruce, C., & Bishop, A. J. R. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq624 · Cited by 28

No evidence of involvement of germline BACH1 mutations in Finnish breast and ovarian cancer families

Karppinen, S., Vuosku, J., Heikkinen, K., Allinen, M., & Winqvist, R. (2003) · European Journal of Cancer · doi:10.1016/s0959-8049(02)00498-7 · Cited by 28

Mutation of the BRCA1 SQ-cluster results in aberrant mitosis, reduced homologous recombination, and a compensatory increase in non-homologous end joining

Beckta, J. M., Dever, S. M., Gnawali, N., Khalil, A. A., Sule, A. D., Golding, S. E., Rosenberg, E., Narayanan, A., Kehn‐Hall, K., Xu, B., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4876 · Cited by 26

RNF168-Mediated Ubiquitin Signaling Inhibits the Viability of BRCA1 -Null Cancers

Krais, J. J., Wang, Y., Bernhardy, A. J., Clausen, E., Miller, J. A., Cai, K. Q., Scott, C. L., & Johnson, N. (2020) · Cancer Research · doi:10.1158/0008-5472.can-19-3033 · Cited by 27

Synthetic lethality on drug discovery: an update on cancer therapy

Yar, M. S., Haider, K., Gohel, V., Siddiqui, N. A., & Kamal, Ä. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2020.1744560 · Cited by 27

L ARP7 Is a BRCA1 Ubiquitinase Substrate and Regulates Genome Stability and Tumorigenesis

Zhang, F., Yan, P., Yu, H., Le, H., Li, Z., Chen, J., Liang, X., Wang, S., Wei, W., Liu, L., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107974 · Cited by 28

Effects of germline and somatic events in candidate BRCA-like genes on breast-tumor signatures

Bodily, W. R., Shirts, B. H., Walsh, T., Gülsüner, S., King, M., Parker, A., Roosan, M. R., & Piccolo, S. (2020) · PLoS ONE · doi:10.1371/journal.pone.0239197 · Cited by 27

Activation of DNA damage response signaling in mammalian cells by ionizing radiation

Ghosh, S., & Ghosh, A. (2021) · Free Radical Research · doi:10.1080/10715762.2021.1876853 · Cited by 28

The roles of E3 ligases in Hepatocellular carcinoma.

Yu, Z., Li, H., Zhu, J., Wang, H., & Jin, X. (2022) · PubMed · Cited by 27

Protein expression and methylation of DNA repair genes hMLH1, hMSH2, MGMT and BRCA1 and their correlation with clinicopathological parameters and prognosis in basal‐like breast cancer

Yimit, A., Mitomi, H., Nakai, K., Himuro, T., Saito, T., Takahashi, M., Arakawa, A., Yao, T., & Saito, M. (2013) · Histopathology · doi:10.1111/his.12220 · Cited by 27

Differences in the association of p53 phosphorylated on serine 15 and key enzymes of homologous recombination

Restle, A., Janz, C., & Wiesmüller, L. (2005) · Oncogene · doi:10.1038/sj.onc.1208639 · Cited by 27

Loss of Ubr2, an E3 ubiquitin ligase, leads to chromosome fragility and impaired homologous recombinational repair

Ouyang, Y., Kwon, Y. T., An, J. Y., Eller, D., Tsai, S.-C., Diaz-Perez, S. V., Troke, J. J., Teitell, M. A., & Marahrens, Y. (2006) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2005.12.016 · Cited by 28

BRCA1 downregulates the kinase activity of Polo-like kinase 1 in response to replication stress

Zou, J., Rezvani, K. S., Wang, H., Lee, K. S., & Zhang, D. (2013) · Cell Cycle · doi:10.4161/cc.25349 · Cited by 28

A small ubiquitin binding domain inhibits ubiquitin-dependent protein recruitment to DNA repair foci

Helchowski, C. M., Skow, L., Roberts, K. H., Chute, C. L., & Canman, C. E. (2013) · Cell Cycle · doi:10.4161/cc.26640 · Cited by 28

Chromatin remodeling and repair of DNA double-strand breaks

Wong, L.-Y., Recht, J., & Laurent, B. C. (2006) · Journal of Molecular Histology · doi:10.1007/s10735-006-9047-4 · Cited by 27

Homologous Recombination Is a Primary Pathway to Repair DNA Double-Strand Breaks Generated during DNA Rereplication

Truong, L. N., Li, Y., Sun, E., Ang, K., Hwang, P. Y.-H., & Wu, X. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.576488 · Cited by 29

Hereditary cancer syndromes: utilizing DNA repair deficiency as therapeutic target

Goyal, G., Fan, T., & Silberstein, P. T. (2016) · Familial Cancer · doi:10.1007/s10689-016-9883-7 · Cited by 28

Reviewing the characteristics of BRCA and PALB2-related cancers in the precision medicine era

Macedo, G. S., Alemar, B., & Ashton‐Prolla, P. (2019) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2018-0104 · Cited by 28

BRCA mutations and gastrointestinal cancers: When to expect the unexpected?

Maccaroni, E., Giampieri, R., Lenci, E., Scortichini, L., Bianchi, F., Belvederesi, L., Brugiati, C., Pagliaretta, S., Ambrosini, E., & Berardi, R. (2021) · World Journal of Clinical Oncology · doi:10.5306/wjco.v12.i7.565 · Cited by 26

Widespread chromatin context-dependencies of DNA double-strand break repair proteins

Vergara, X., Manjón, A. G., de Haas, M., Morris, B., Schep, R., Leemans, C., Friskes, A., Beijersbergen, R. L., Sanders, M. A., Medema, R. H., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49232-x · Cited by 26

Promoter methylation of cancer-related genes in gastric carcinoma.

Popławski, T., Tomaszewska, K., Galicki, M., Morawiec, Z., & Błasiak, J. (2008) · PubMed · Cited by 26

The mutagenic potential of a single DNA double-strand break in a mammalian chromosome is not influenced by transcription

Allen, C. (2003) · DNA repair · doi:10.1016/s1568-7864(03)00139-3 · Cited by 25

BRCA-FA Pathway as a Target for Anti-Tumor Drugs

Flynn, R. L., Gupta, R., Brosh, R. M., & Cantor, S. B. (2008) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152008784220285 · Cited by 25

Clonal chromosome aberrations secondary to chromosome instability in an elastofibroma

Batstone, P. J., Forsyth, L., & Goodlad, J. R. (2001) · Cancer Genetics and Cytogenetics · doi:10.1016/s0165-4608(01)00394-6 · Cited by 26

3R coordination by Fanconi anemia proteins

Macé‐Aimé, G., Bogliolo, M., Guervilly, J.-H., du Villard, J.-A. D., & Rosselli, F. (2005) · Biochimie · doi:10.1016/j.biochi.2005.05.003 · Cited by 26

Dhh1 regulates the G1/S-checkpoint following DNA damage or BRCA1 expression in yeast1

Westmoreland, T. J., Olson, J. A., Saito, W. Y., Hüper, G., Marks, J. R., & Bennett, C. B. (2003) · Journal of Surgical Research · doi:10.1016/s0022-4804(03)00155-0 · Cited by 26

BRCA1 in breast and ovarian cancer predisposition

Billack, B., & Monteiro, Á. N. A. (2004) · Cancer Letters · doi:10.1016/j.canlet.2004.11.006 · Cited by 26

MERIT40 cooperates with BRCA2 to resolve DNA interstrand cross-linksPreprint

Jiang, Q., Paramasivam, M., Aressy, B., Wu, J., Bellani, M. A., Tong, W., Seidman, M. M., & Greenberg, R. A. (2015) · Genes & Development · doi:10.1101/gad.264192.115 · Cited by 27

Differential requirements for DNA repair proteins in immortalized cell lines using alternative lengthening of telomere mechanisms

Martinez, A. R., Kaul, Z., Parvin, J. D., & Groden, J. L. (2017) · Genes Chromosomes and Cancer · doi:10.1002/gcc.22465 · Cited by 24

Inactive PARP1 causes embryonic lethality and genome instability in a dominant-negative manner

Shao, Z., Lee, B. J., Zhang, H., Lin, X., Li, C., Jiang, W., Chirathivat, N., Gershik, S., Shen, M. M., Baer, R. J., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2301972120 · Cited by 25

Aberrant expression of LMO4 induces centrosome amplification and mitotic spindle abnormalities in breast cancer cells

Montanez-Wiscovich, M. E., Shelton, M. D., Seachrist, D. D., Lozada, K. L., Johnson, E., Miedler, J. D., Abdul‐Karim, F. W., Visvader, J. E., & Keri, R. A. (2010) · The Journal of Pathology · doi:10.1002/path.2762 · Cited by 25

Breast cancer 1 (BRCA1)-deficient embryos develop normally but are more susceptible to ethanol-initiated DNA damage and embryopathies

Shapiro, A. M., Miller‐Pinsler, L., & Wells, P. G. (2015) · Redox Biology · doi:10.1016/j.redox.2015.11.005 · Cited by 25

Novel splice‐switching oligonucleotide promotes BRCA1 aberrant splicing and susceptibility to PARP inhibitor action

Smith, L., de Calais, F. L., Raponi, M., Mellone, M., Buratti, E., Blaydes, J. P., & Baralle, D. (2016) · International Journal of Cancer · doi:10.1002/ijc.30574 · Cited by 25

Molecular basis for the inhibition of the methyl-lysine binding function of 53BP1 by TIRR

Wang, J., Yuan, Z., Cui, Y., Xie, R., Yang, G., Kassab, M. A., Wang, M., Ma, Y., Wu, C., Yu, X., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05174-9 · Cited by 24

The relevance of BRCA genetics to prostate cancer pathogenesis and treatment.

Sundararajan, S., Ahmed, A. K., & Goodman, O. B. (2011) · PubMed · Cited by 25

Mapping and conformational characterization of the DNA-binding region of the breast cancer susceptibility protein BRCA1

Naseem, R., Sturdy, A., Finch, D., Jowitt, T. A., & Webb, M. (2006) · Biochemical Journal · doi:10.1042/bj20051646 · Cited by 23

Ensuring the Stability of the Genome: DNA Damage Checkpoints

Latif, C., Harvey, S. H., & O'Connell, S. J. (2001) · The Scientific World JOURNAL · doi:10.1100/tsw.2001.297 · Cited by 26

Role of DNA Methylation in Genome Stability

Zhou, D., & Robertson, K. D. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-803309-8.00024-0 · Cited by 25

Role of Next-Generation Sequencing Technologies in Personalized Medicine

Morganti, S., Tarantino, P., Ferraro, E., D’Amico, P., Viale, G., Trapani, D., Duso, B. A., & Curigliano, G. (2019) · Springer eBooks · doi:10.1007/978-3-030-27994-3_8 · Cited by 30

Ovarian Cancer–Specific BRCA -like Copy-Number Aberration Classifiers Detect Mutations Associated with Homologous Recombination Deficiency in the AGO-TR1 Trial

Schouten, P. C., Richters, L., Vis, D. J., Kommoss, S., van Dijk, E., Ernst, C., Kluin, R. J. C., Marmé, F., Lips, E. H., Schmidt, S., et al. (2021) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-1673 · Cited by 24

The BRCA1 alternative splicing variant Δ14-15 with an in-frame deletion of part of the regulatory serine-containing domain (SCD) impairs the DNA repair capacity in MCF-7 cells

Sevcik, J., Falk, M., Kleiblová, P., Lhota, F., Štefančíková, L., Janatová, M., Weiterová, L., Lukášová, E., Kozubek, S., Pohlreich, P., et al. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2011.12.023 · Cited by 24

BRCA1/2 genetic background-based therapeutic tailoring of human ovarian cancer: hope or reality?

Tagliaferri, P., Ventura, M., Baudi, F., Cucinotto, I., Arbitrio, M., Martino, M. T. D., & Tassone, P. (2009) · Journal of Ovarian Research · doi:10.1186/1757-2215-2-14 · Cited by 24

Brca1 in immunoglobulin gene conversion and somatic hypermutation

Longerich, S., Orelli, B. J., Martin, R. W., Bishop, D. K., & Storb, U. (2007) · DNA repair · doi:10.1016/j.dnarep.2007.10.002 · Cited by 24

Identification of a novel transcriptional repressor element located in the first intron of the human BRCA1 gene

Suen, T.-C., & Goss, P. E. (2001) · Oncogene · doi:10.1038/sj.onc.1204078 · Cited by 25

Hypermethylation of theBreast Cancer–Associated Gene 1Promoter Does Not Predict Cytologic Atypia or Correlate with Surrogate End Points of Breast Cancer Risk

Bean, G. R., Ibarra-Drendall, C., Goldenberg, V. K., Baker, J. C., Troch, M. M., Paisie, C. A., Wilke, L. G., Yee, L., Marcom, P. K., Kimler, B. F., et al. (2007) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-06-0598 · Cited by 24

Recombinational DNA Repair in Cancer and Normal Cells: The Challenge of Functional Analysis

Willers, H., Xia, F., & Powell, S. N. (2002) · BioMed Research International · doi:10.1155/s1110724302204027 · Cited by 24

Of mice and (wo)men: genotype-phenotype correlations in BRCA1

Hohenstein, P., & Fodde, R. (2003) · Human Molecular Genetics · doi:10.1093/hmg/ddg258 · Cited by 24

TopBP1-mediated DNA processing during mitosis

Gallina, I., Christiansen, S. K., Pedersen, R. T., Lisby, M., & Oestergaard, V. H. (2015) · Cell Cycle · doi:10.1080/15384101.2015.1128595 · Cited by 22

RNF8 and RNF168 but not HERC2 are required for DNA damage-induced ubiquitylation in chicken DT40 cells

Oestergaard, V. H., Pentzold, C., Pedersen, R. T., Iosif, S., Alpi, A. F., Bekker‐Jensen, S., Mailand, N., & Lisby, M. (2012) · DNA repair · doi:10.1016/j.dnarep.2012.08.005 · Cited by 23

Therapeutic potential of PARP inhibitors for metastatic breast cancer

Irshad, S., Ashworth, A., & Tutt, A. N. J. (2011) · Expert Review of Anticancer Therapy · doi:10.1586/era.11.52 · Cited by 23

Discovery of a novel dual-target inhibitor against RSK1 and MSK2 to suppress growth of human colon cancer

Jin, G., Yan, M., Liu, K., Yao, K., Chen, H., Zhang, C., Yi, Y., Reddy, K., Gorja, D. R., Laster, K. V., et al. (2020) · Oncogene · doi:10.1038/s41388-020-01467-w · Cited by 22

Genomic Scar Score: A robust model predicting homologous recombination deficiency based on genomic instability

Yuan, W., Ni, J., Wen, H., Shi, W., Chen, X., Huang, H., Zhang, X., Lu, X., Zhu, C., Dong, H., et al. (2022) · BJOG An International Journal of Obstetrics & Gynaecology · doi:10.1111/1471-0528.17324 · Cited by 24

The fidelity of transcription in human cells

Chung, C., Verheijen, B. M., Zhang, X., Huang, B., Coakley, A. J., McGann, E. G., Wade, E., Dinep-Schneider, O., LaGosh, J., Anagnostou, M., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2210038120 · Cited by 23

Targeting Chk2 improves gastric cancer chemotherapy by impairing DNA damage repair

Gutiérrez‐González, A., Belda-Iniesta, C., Bargiela-Iparraguirre, J., Domínguez, G., Alfonso, P., Perona, R., & Sánchez‐Pérez, I. (2012) · APOPTOSIS · doi:10.1007/s10495-012-0794-2 · Cited by 22

Novel roles of 1α,25(OH)2D3 on DNA repair provide new strategies for breast cancer treatment

Gonzalo, S. (2013) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2013.09.009 · Cited by 23

The DNA damage response at dysfunctional telomeres, and at interstitial and subtelomeric DNA double-strand breaks

Muraki, K., & Murnane, J. P. (2017) · Genes & Genetic Systems · doi:10.1266/ggs.17-00014 · Cited by 25

Genetic and molecular biology of breast cancer among Iranian patients

Moghbeli, M. (2019) · Journal of Translational Medicine · doi:10.1186/s12967-019-1968-2 · Cited by 25

Insights Into the Impacts of BRCA Mutations on Clinicopathology and Management of Early-Onset Triple-Negative Breast Cancer

Ye, F., He, M. Y., Huang, L., Lang, G., Hu, X., Shao, Z., Di, G., & Cao, A. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2020.574813 · Cited by 23

Oligo/Polynucleotide-Based Gene Modification: Strategies and Therapeutic Potential

Sargent, R. G., Kim, S., & Gruenert, D. C. (2011) · Oligonucleotides · doi:10.1089/oli.2010.0273 · Cited by 23

PARP inhibition during alkylation-induced genotoxic stress signals a cell cycle checkpoint response mediated by ATM

Carrozza, M. J., Stefanick, D. F., Horton, J. K., Kedar, P. S., & Wilson, S. H. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.07.010 · Cited by 24

Deoxycholate, an Endogenous Tumor Promoter and DNA Damaging Agent, Modulates BRCA-1 Expression in Apoptosis-Sensitive Epithelial Cells: Loss of BRCA-1 Expression in Colonic Adenocarcinomas

Romagnolo, D. F., Chirnomas, R. B., Ku, J., Jeffy, B. D., Payne, C. M., Holubec, H., Ramsey, L., Bernstein, H., Bernstein, C., Kunke, K., et al. (2003) · Nutrition and Cancer · doi:10.1207/s15327914nc4601_11 · Cited by 23

Efficient Incorporation of Large (>2 kb) Heterologies Into Heteroduplex DNA: Pms1/Msh2-Dependent and -Independent Large Loop Mismatch Repair in Saccharomyces cerevisiae

Clikeman, J. A., Wheeler, S. L., & Nickoloff, J. A. (2001) · Genetics · doi:10.1093/genetics/157.4.1481 · Cited by 23

Structural basis to characterise transactivation domain of BRCA1

Yadav, L. R., Biswal, M. N., Hosur, M. V., Kumar, N. S., & Varma, A. K. (2016) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2015.1136896 · Cited by 22

BLM and RAD51 Genes Polymorphism and Susceptibility to Breast Cancer

Sassi, A., Popielarski, M., Synowiec, E., Morawiec, Z., & Woźniak, K. (2013) · Pathology & Oncology Research · doi:10.1007/s12253-013-9602-8 · Cited by 22

BRCA1 Haploinsufficiency Leads to Altered Expression of Genes Involved in Cellular Proliferation and Development

Feilotter, H. E., Michel, C. S., Uy, P., Bathurst, L., & Davey, S. K. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100068 · Cited by 23

Haploinsufficiency in mouse models of DNA repair deficiency: modifiers of penetrance

Cabelof, D. C. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0839-7 · Cited by 21

Role of DNA damage response pathways in preventing carcinogenesis caused by intrinsic replication stress

Wallace, M. D., Southard, T. L., Schimenti, K. J., & Schimenti, J. C. (2013) · Oncogene · doi:10.1038/onc.2013.339 · Cited by 23

Radiosensitivity of lymphoblastoid cell lines with a heterozygous BRCA1 mutation is not detected by the comet assay and pulsed field gel electrophoresis

Trenz, K., Schütz, P., & Speit, G. (2005) · Mutagenesis · doi:10.1093/mutage/gei018 · Cited by 22

Atm Heterozygosity Cooperates with Loss of Brca1 to Increase the Severity of Mammary Gland Cancer and Reduce Ductal Branching

Bowen, T. J., Yakushiji, H., Montagna, C., Jain, S., Ried, T., & Wynshaw-Boris, A. J. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1598 · Cited by 22

Strong preference of BRCA1 protein to topologically constrained non-B DNA structures

Brázda, V., Hároníková, L., Liao, J. C. C., Fridrichová, H., & Jagelská, E. B. (2016) · BMC Molecular Biology · doi:10.1186/s12867-016-0068-6 · Cited by 22

Evaluation of unclassified variants in the breast cancer susceptibility genes BRCA1 and BRCA2using five methods: results from a population-based study of young breast cancer patients

Lee, E., McKean‐Cowdin, R., Ma, H., Chen, Z., Berg, D. V. D., Henderson, B. E., Bernstein, L., & Ursin, G. (2008) · Breast Cancer Research · doi:10.1186/bcr1865 · Cited by 22

The Fanconi anemia protein interaction network: Casting a wide net

Rego, M. A., Kolling, F. W., & Howlett, N. G. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.11.018 · Cited by 22

Independence of R/M/N Focus Formation and the Presence of Intact BRCA1

Wu, X., Petrini, J. H. J., Heine, W. F., Weaver, D. T., Livingston, D. M., & Chen, J. (2000) · Science · doi:10.1126/science.289.5476.11 · Cited by 23

Physiological modulation of endogenous BRCA1 p220 abundance suppresses DNA damage during the cell cyclePreprint

Dimitrov, S. D., Lu, D., Naetar, N., Hu, Y., Pathania, S., Kanellopoulou, C., & Livingston, D. M. (2013) · Genes & Development · doi:10.1101/gad.225045.113 · Cited by 22

Inactivation of Apoptosis Antagonizing Transcription Factor in tubular epithelial cells induces accumulation of DNA damage and nephronophthisis

Jain, M., Kaiser, R. W. J., Bohl, K., Hoehne, M., Göbel, H., Bartram, M. P., Habbig, S., Müller, R., Fogo, A. B., Benzing, T. R., et al. (2019) · Kidney International · doi:10.1016/j.kint.2018.10.034 · Cited by 24

Global View of Candidate Therapeutic Target Genes in Hormone-Responsive Breast Cancer

Salvati, A., Gigantino, V., Nassa, G., Cappa, V. M., Ventola, G. M., Cracas, D. G. C., Mastrocinque, R., Rizzo, F. M., Tarallo, R., Weisz, A., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21114068 · Cited by 21

Fangchinoline suppresses conjunctival melanoma by directly binding FUBP2 and inhibiting the homologous recombination pathway

Bao, K., Li, Y., Wei, J., Li, R., Yang, J., Shi, J., Li, B., Zhu, J., Mao, F., Jia, R., et al. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03653-4 · Cited by 21

The downregulation of BAP1 expression by BCR-ABL reduces the stability of BRCA1 in chronic myeloid leukemia

Dkhissi, F., Aggoune, D., Pontis, J., Sorel, N., Piccirilli, N., Corf, A. L., Guilhot, F., Chomel, J., Ait‐Si‐Ali, S., & Turhan, A. G. (2015) · Experimental Hematology · doi:10.1016/j.exphem.2015.04.013 · Cited by 21

Synergistic Interaction of Rnf8 and p53 in the Protection against Genomic Instability and Tumorigenesis

Halaby, M., Hakem, A., Li, L., Ghamrasni, S. E., Venkatesan, S., Hande, M. P., Sanchez, O. H., & Hakem, R. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003259 · Cited by 21

Recombination at chromosomal sequences involved in leukaemogenic rearrangements is differentially regulated by p53

Boehden, G. S. (2004) · Carcinogenesis · doi:10.1093/carcin/bgh092 · Cited by 21

An update on genetic risk assessment and prevention: the role of genetic testing panels in breast cancer

Piccinin, C., Panchal, S., Watkins, N., & Kim, R. H. (2019) · Expert Review of Anticancer Therapy · doi:10.1080/14737140.2019.1659730 · Cited by 21

A critical evaluation of methods to interpret drug combinations

Twarog, N. R., Connelly, M., & Shelat, A. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-61923-1 · Cited by 21

BRCA and Breast Cancer-Related High-Penetrance Genes

Han, S., & Kim, S. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9620-6_25 · Cited by 22

RecQ Helicase Somatic Alterations in Cancer

Thakkar, M. K., Lee, J., Meyer, S., & Chang, V. Y. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.887758 · Cited by 22

Clinical Pharmacokinetics and Pharmacodynamics of Rucaparib

Liao, M., Beltman, J., Giordano, H., Harding, T. C., Maloney, L., Simmons, A. D., & Xiao, J. J. (2022) · Clinical Pharmacokinetics · doi:10.1007/s40262-022-01157-8 · Cited by 20

Estrogen therapy induces receptor-dependent DNA damage enhanced by PARP inhibition in ER+ breast cancer

Traphagen, N. A., Schwartz, G. N., Tau, S., Roberts, A. M., Jiang, A., Hosford, S. R., Marotti, J. D., Goen, A. E., Romo, B. A., Johnson, A. L., et al. (2023) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-23-0488 · Cited by 20

BRCA1 Control of Steroid Receptor Ubiquitination

Heine, G. F., & Parvin, J. D. (2007) · Science s STKE · doi:10.1126/stke.3912007pe34 · Cited by 20

Actin disruption agents induce phosphorylation of histone H2AX in human breast adenocarcinoma MCF-7 cells

An (2011) · Oncology Reports · doi:10.3892/or.2011.1214 · Cited by 20

Checkpoint and Coordinated Cellular Responses to DNA Damage

Yang, X. H., & Zou, L. (2006) · Springer eBooks · doi:10.1007/b136684 · Cited by 20

The Importance of Satellite Sequence Repression for Genome StabilityPreprint

Zeller, P. J., & Gasser, S. M. (2017) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2017.82.033662 · Cited by 22

BRCA1/2 Haploinsufficiency: Exploring the Impact of Losing one Allele

Minello, A., & Carreira, A. (2023) · Journal of Molecular Biology · doi:10.1016/j.jmb.2023.168277 · Cited by 20

BLM and BRCA1-BARD1 coordinate complementary mechanisms of joint DNA molecule resolution

Tsukada, K., Jones, S. E., Bannister, J. V., Durin, M.-A., Vendrell, I., Fawkes, M., Fischer, R., Kessler, B. M., Chapman, J. R., & Blackford, A. N. (2024) · Molecular Cell · doi:10.1016/j.molcel.2023.12.040 · Cited by 18

The Future of Targeted Therapy for Leiomyosarcoma

Denu, R. A., Dann, A. M., Keung, E. Z.-Y., Nakazawa, M. S., & Nassif, E. F. (2024) · Cancers · doi:10.3390/cancers16050938 · Cited by 19

Biomimetic “nano-spears” for CAFs-targeting: splintered three “shields” with enhanced cisplatin anti-TNBC efficiency

Wu, Y., Chen, R., Ni, S., & Hu, K. (2024) · Journal of Controlled Release · doi:10.1016/j.jconrel.2024.04.053 · Cited by 19

Whole‐exome DNA sequence analysis of Brca2‐ and Trp53‐deficient mouse mammary gland tumours

Francis, J. C., Melchor, L., Campbell, J., Kendrick, H. D., Wei, W., Garrido, J. A., Assiotis, I., Chen, L., Kozarewa, I., Fenwick, K., et al. (2015) · The Journal of Pathology · doi:10.1002/path.4517 · Cited by 19

Conservation and Losses of Non-Coding RNAs in Avian Genomes

Gardner, P. P., Fasold, M., Burge, S., Ninova, M., Jana Hertel, A., Kehr, S., Steeves, T. E., Griffiths‐Jones, S., & Stadler, P. F. (2015) · PLoS ONE · doi:10.1371/journal.pone.0121797 · Cited by 22

DNA Damage Tolerance Mechanisms Revealed from the Analysis of Immunoglobulin V Gene Diversification in Avian DT40 Cells

Abe, T., Branzei, D., & Hirota, K. (2018) · Genes · doi:10.3390/genes9120614 · Cited by 20

Role played by BRCA1 in regulating the cellular response to stress

Gilmore, P. M., Quinn, J. E., Mullan, P. B., Andrews, H. N., McCabe, N., Carty, M., Kennedy, R. D., & Harkin, D. P. (2003) · Biochemical Society Transactions · doi:10.1042/bst0310257 · Cited by 19

Caretaker Brca1: keeping the genome in the straight and narrow

Yu, V. P. C. C. (2000) · Breast Cancer Research · doi:10.1186/bcr37 · Cited by 17

Commentary Caretaker Brca1: keeping the genome in the straight and narrow

Yu, V. (2000)

BRCA1 deficient embryonic stem cells display a decreased homologous recombination frequency and an increased frequency of non-homologous recombination that is corrected by expression of a Brca1 transgene

Snouwaert, J. N., Gowen, L. C., Latour, A. M., Mohn, A. R., Xiao, A., DiBiase, L., & Koller, B. H. (1999) · Oncogene · doi:10.1038/sj.onc.1203334 · Cited by 197

BRCA1: a key player at multiple stages of homologous recombination in DNA double-strand break repair

Liu, Y., & Lu, L. (2021) · Genome Instability & Disease · doi:10.1007/s42764-021-00042-1 · Cited by 11

The Role of the BRCA1 Tumor Suppressor in DNA Double-Strand Break Repair

Zhang, J., & Powell, S. N. (2005) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-05-0192 · Cited by 213