Ubiquitin-Binding Protein RAP80 Mediates BRCA1-Dependent DNA Damage Response

The DNA damage response: putting checkpoints in perspective

Zhou, B.-B. S., & Elledge, S. J. (2000) · Nature · doi:10.1038/35044005 · Cited by 3,213 · see citing works

Genetic heterogeneity and penetrance analysis of the BRCA1 and BRCA2 genes in breast cancer families. The Breast Cancer Linkage Consortium.

Ford, D., Easton, D., Stratton, M. R., Narod, S., Goldgar, D., Devilee, P., Bishop, D., Weber, B., Lenoir, G., Chang-Claude, J., et al. (1998) · American Journal of Human Genetics · doi:10.1086/301749 · Cited by 2,766 · see citing works

Chk1 is an essential kinase that is regulated by Atr and required for the G ₂ /M DNA damage checkpoint

Liu, Q., Guntuku, S., Cui, X.-S., Matsuoka, S., Cortez, D., Tamai, K., Luo, G., Carattini-Rivera, S., DeMayo, F., Bradley, A., et al. (2000) · Genes & Development · doi:10.1101/gad.14.12.1448 · Cited by 1,625 · see citing works

Rules for Making Human Tumor Cells

Hahn, W. C., & Weinberg, R. A. (2002) · New England Journal of Medicine · doi:10.1056/nejmra021902 · Cited by 951 · see citing works

BRCA1 mutations in women attending clinics that evaluate the risk of breast cancer.

Couch, F., DeShano, M. L., Blackwood, M., Calzone, K., Stopfer, J., Campeau, L., Ganguly, A., Rebbeck, T., Weber, B., Jablon, L., et al. (1997) · New England Journal of Medicine · doi:10.1056/nejm199705153362002 · Cited by 715 · see citing works

Interfaces Between the Detection, Signaling, and Repair of DNA Damage

Rouse, J. W., & Jackson, S. P. (2002) · Science · doi:10.1126/science.1074740 · Cited by 688 · see citing works

BACH1, a Novel Helicase-like Protein, Interacts Directly with BRCA1 and Contributes to Its DNA Repair Function

Cantor, S. B., Bell, D. W., Ganesan, S., Kass, E. M., Drapkin, R., Grossman, S., Wahrer, D. C. R., Sgroi, D. C., Lane, W. S., Haber, D. A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00304-x · Cited by 674 · see citing works

The RING heterodimer BRCA1-BARD1 is a ubiquitin ligase inactivated by a breast cancer-derived mutation

Hashizume, R., Fukuda, M., Maeda, I., Nishikawa, H., Oyake, D., Yabuki, Y., Ogata, H., & Ohta, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c000881200 · Cited by 634 · see citing works

Involvement of Brca1 in S-Phase and G 2 -Phase Checkpoints after Ionizing Irradiation

Xu, B., Kim, S., & Kastan, M. B. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.10.3445-3450.2001 · Cited by 540 · see citing works

BRCA1 regulates the G2/M checkpoint by activating Chk1 kinase upon DNA damage

Yarden, R. I., Pardo-Reoyo, S., Sgagias, M. K., Cowan, K. H., & Brody, L. C. (2002) · Nature Genetics · doi:10.1038/ng837 · Cited by 483 · see citing works

Aberrant cell cycle checkpoint function and early embryonic death in Chk1−/− micePreprint

Takai, H., Tominaga, K., Motoyama, N., Minamishima, Y. A., Nagahama, H., Tsukiyama, T., Ikeda, K., Nakayama, K., Nakanishi, M., & Nakayama, K. (2000) · Genes & Development · doi:10.1101/gad.14.12.1439 · Cited by 478 · see citing works

DNA Damage-Induced Cell Cycle Checkpoint Control Requires CtIP, a Phosphorylation-Dependent Binding Partner of BRCA1 C-Terminal Domains

Yu, X., & Chen, J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9478-9486.2004 · Cited by 410 · see citing works

Functional Interaction of Monoubiquitinated FANCD2 and BRCA2/FANCD1 in Chromatin

Wang, X., Andreassen, P. R., & D’Andrea, A. D. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.13.5850-5862.2004 · Cited by 332 · see citing works

BRCA1 ubiquitinates its phosphorylation-dependent binding partner CtIPPreprint

Yu, X., Fu, S., Lai, M., Baer, R. J., & Chen, J. (2006) · Genes & Development · doi:10.1101/gad.1431006 · Cited by 283 · see citing works

Cellular Responses to DNA Damage: One Signal, Multiple Choices

Su, T. T. (2006) · Annual Review of Genetics · doi:10.1146/annurev.genet.40.110405.090428 · Cited by 227 · see citing works

Autoubiquitination of the BRCA1·BARD1 RING Ubiquitin Ligase

Chen, A., Kleiman, F. E., Manley, J. L., Ouchi, T., & Pan, Z. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201252200 · Cited by 218 · see citing works

The human decatenation checkpoint

Deming, P. B., Cistulli, C. A., Zhao, H., Graves, P. R., Piwnica-Worms, H. M., Paules, R. S., Downes, C. S., & Kaufmann, W. K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221430898 · Cited by 181 · see citing works

Double-sided ubiquitin binding of Hrs-UIM in endosomal protein sorting

Hirano, S., Kawasaki, M., Ura, H., Kato, R., Raiborg, C., Stenmark, H., & Soichi Wakatsuki, A. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1051 · Cited by 178 · see citing works

Regulated interaction of the Fanconi anemia protein, FANCD2, with chromatin

Oca, R. M. D., Andreassen, P. R., Margossian, S. P., Gregory, R. C., Taniguchi, T., Wang, X., Houghtaling, S. R., Grompe, M., & D’Andrea, A. D. (2004) · Blood · doi:10.1182/blood-2003-11-3997 · Cited by 132 · see citing works

Environmental signals and cell fate specification in premigratory neural crest

Dorsky, R. I., Moon, R. T., & Raible, D. W. (2000) · BioEssays · doi:10.1002/1521-1878(200008)22:8 · Cited by 111 · see citing works

RAP80, a Novel Nuclear Protein That Interacts with the Retinoid-related Testis-associated Receptor

Yan, Z., Kim, Y. S., & Jetten, A. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203475200 · Cited by 50 · see citing works

DNA Damage Sensing by the ATM and ATR Kinases

Marechal, A., & Zou, L. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012716 · Cited by 1,514 · see citing works

Regulation of DNA repair throughout the cell cycle

Branzei, D., & Foiani, M. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2351 · Cited by 1,228 · see citing works

Dynamics of DNA damage response proteins at DNA breaks: a focus on protein modifications

Polo, S. E., & Jackson, S. P. (2011) · Genes & Development · doi:10.1101/gad.2021311 · Cited by 1,092 · see citing works

Homologous Recombination and Human Health: The Roles of BRCA1, BRCA2, and Associated Proteins

Prakash, R., Zhang, Y., Feng, W., & Jasin, M. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a016600 · Cited by 869 · see citing works

ATM-Dependent Chromatin Changes Silence Transcription In cis to DNA Double-Strand Breaks

Shanbhag, N. M., Rafalska-Metcalf, I. U., Balane-Bolivar, C., Janicki, S. M., & Greenberg, R. A. (2010) · Cell · doi:10.1016/j.cell.2010.04.038 · Cited by 737 · see citing works

Emergence of a DNA-damage response network consisting of Fanconi anaemia and BRCA proteins

Wang, W. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2159 · Cited by 663 · see citing works

Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination

Tang, J., Cho, N. W., Cui, G., Manion, E. M., Shanbhag, N. M., Botuyan, M. V., Mer, G., & Greenberg, R. A. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2499 · Cited by 521 · see citing works

Proteogenomics of Non-smoking Lung Cancer in East Asia Delineates Molecular Signatures of Pathogenesis and Progression

Chen, Y.-J., Roumeliotis, T. I., Chang, Y.-H., Chen, C.-T., Han, C.-L., Lin, M.-H., Chen, H.-W., Chang, G.-C., Chang, Y.-L., Wu, C.-T., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.012 · Cited by 382 · see citing works

Recognition, signaling, and repair of DNA double-strand breaks produced by ionizing radiation in mammalian cells: the molecular choreography

Thompson, L. H. (2012) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2012.06.002 · Cited by 357 · see citing works

Principles of Ubiquitin-Dependent Signaling

Oh, E., Akopian, D., & Rape, M. (2018) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100617-062802 · Cited by 339 · see citing works

Assembly and function of DNA double-strand break repair foci in mammalian cells

Bekker-Jensen, S., & Mailand, N. (2010) · DNA Repair · doi:10.1016/j.dnarep.2010.09.010 · Cited by 338 · see citing works

Histone H2A.Z Controls a Critical Chromatin Remodeling Step Required for DNA Double-Strand Break Repair

Xu, Y., Ayrapetov, M. K., Xu, C., Gursoy-Yuzugullu, O., Hu, Y., & Price, B. D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.026 · Cited by 336 · see citing works

53BP1, BRCA1, and the Choice between Recombination and End Joining at DNA Double-Strand Breaks

Daley, J. M., & Sung, P. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01639-13 · Cited by 318 · see citing works

DNA Damage Response: Three Levels of DNA Repair Regulation

Sirbu, B. M., & Cortez, D. (2013) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012724 · Cited by 272 · see citing works

The role of BRCA1 in DNA damage response

Wu, J., Lu, L.-Y., & Yu, X. (2010) · Protein & Cell · doi:10.1007/s13238-010-0010-5 · Cited by 235 · see citing works

CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response

Kim, H., Huang, J., & Chen, J. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1277 · Cited by 212 · see citing works

Nucleotide excision repair-induced H2A ubiquitination is dependent on MDC1 and RNF8 and reveals a universal DNA damage response

Marteijn, J. A., Bekker-Jensen, S., Mailand, N., Lans, H., Schwertman, P., Gourdin, A. M., Dantuma, N. P., Lukas, J., & Vermeulen, W. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200902150 · Cited by 184 · see citing works

NBA1, a new player in the Brca1 A complex, is required for DNA damage resistance and checkpoint control

Wang, B., Hurov, K., Hofmann, K., & Elledge, S. J. (2009) · Genes & Development · doi:10.1101/gad.1770309 · Cited by 172 · see citing works

Mechanisms of BRCA1 Tumor Suppression

Silver, D. P., & Livingston, D. M. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0221 · Cited by 159 · see citing works

Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks.

Panier, S., Ichijima, Y., Fradet-Turcotte, A., Leung, C. C. Y., Kaustov, L., Arrowsmith, C. H., & Durocher, D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.045 · Cited by 152 · see citing works

CCDC98 targets BRCA1 to DNA damage sites

Liu, Z., Wu, J., & Yu, X. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1279 · Cited by 148 · see citing works

Human RNF169 is a negative regulator of the ubiquitin-dependent response to DNA double-strand breaks.

Poulsen, M., Lukas, C., Lukas, J., Bekker-Jensen, S., & Mailand, N. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201109100 · Cited by 146 · see citing works

Regulation of DNA Repair Mechanisms: How the Chromatin Environment Regulates the DNA Damage Response

Stadler, J., & Richly, H. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18081715 · Cited by 110 · see citing works

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

Caestecker, K. W., & Van de Walle, G. R. (2013) · Experimental Cell Research · doi:10.1016/j.yexcr.2012.11.013 · Cited by 108 · see citing works

The deubiquitylating enzyme USP15 regulates homologous recombination repair and cancer cell response to PARP inhibitors

Peng, Y., Liao, Q., Tan, W., Peng, C., Hu, Z., Chen, Y., Li, Z., Li, J., Zhen, B., Zhu, W., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09232-8 · Cited by 104 · see citing works

Differential regulation of JAMM domain deubiquitinating enzyme activity within the RAP80 complex

Patterson-Fortin, J., Shao, G., Bretscher, H., Messick, T. E., & Greenberg, R. A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.135319 · Cited by 85 · see citing works

Metabolic control of BRISC-SHMT2 assembly regulates immune signalling

Walden, M., Tian, L., Ross, R. L., Sykora, U. M., Byrne, D. P., Hesketh, E. L., Masandi, S. K., Cassel, J., George, R., Ault, J. R., et al. (2019) · Nature · doi:10.1038/s41586-019-1232-1 · Cited by 85 · see citing works

Structural basis of BRCC36 function in DNA repair and immune regulation

Rabl, J., Bunker, R. D., Schenk, A. D., Cavadini, S., Gill, M. E., Abdulrahman, W., Andrés-Pons, A., Luijsterburg, M. S., Ibrahim, A. F. M., Branigan, E., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.06.002 · Cited by 84 · see citing works

BRCA1 tumor suppressor network: focusing on its tail

Wang, B. (2012) · Cell & Bioscience · doi:10.1186/2045-3701-2-6 · Cited by 78 · see citing works

Familial breast cancer screening reveals an alteration in the RAP80 UIM domain that impairs DNA damage response function

Nikkilä, J., Coleman, K. A., Morrissey, D., Pylkäs, K., Erkko, H., Messick, T. E., Karppinen, S.-M., Amelina, A., Winqvist, R., & Greenberg, R. A. (2009) · Oncogene · doi:10.1038/onc.2009.33 · Cited by 63 · see citing works

Breast Cancer–Associated <i>Abraxas</i> Mutation Disrupts Nuclear Localization and DNA Damage Response Functions

Solyom, S., Aressy, B., Pylkäs, K., Patterson-Fortin, J., Hartikainen, J. M., Kallioniemi, A., Kauppila, S., Nikkilä, J., Kosma, V.-M., Mannermaa, A., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003223 · Cited by 59 · see citing works

NFBD1/MDC1, 53BP1 and BRCA1 have both redundant and unique roles in the ATM pathway

Wilson, K. A., & Stern, D. F. (2008) · Cell Cycle · doi:10.4161/cc.7.22.7102 · Cited by 43 · see citing works

BRCA1-A and BRISC: multifunctional molecular machines for ubiquitin signaling

Rabl, J. (2020) · Biomolecules · doi:10.3390/biom10111503 · Cited by 31 · see citing works

Distinct selective forces and Neanderthal introgression shaped genetic diversity at genes involved in neurodevelopmental disorders

Mozzi, A., Forni, D., Cagliani, R., Pozzoli, U., Clerici, M., & Sironi, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-06440-4 · Cited by 19 · see citing works

RAP80 regulates epithelial–mesenchymal transition related with metastasis and malignancy of cancer

Park, S. Y., Korm, S., Chung, H. J., Choi, S. J., Jang, J., Cho, S., Lim, Y. T., Kim, H., & Lee, J. (2016) · Cancer Science · doi:10.1111/cas.12877 · Cited by 12 · see citing works

The poxvirus encoded ubiquitin ligase, p28, is regulated by proteasomal degradation and autoubiquitination

Mottet, K., Bareiss, B., Milne, C. D., et al. (2014) · Virology · doi:10.1016/j.virol.2014.08.028 · Cited by 10 · see citing works

Ubiquitination and Degradation of Mutant p53

Lukashchuk, N., & Vousden, K. H. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00050-07 · Cited by 223 · see citing works

Promiscuous Interactions of gp78 E3 Ligase CUE Domain with Polyubiquitin Chains

Liu, S., Chen, Y., Li, J., Huang, T., Tarasov, S. G., King, A., Weissman, A. M., Byrd, R. A., & Das, R. (2012) · Structure · doi:10.1016/j.str.2012.09.020 · Cited by 31 · see citing works

The Antibiotic Treatment Index: A Novel Tool to Improve Antibiotic Resistance Monitoring

Manomayitthikan, T., Kessomboon, N., & Borlace, G. N. (2014) · Research in Social and Administrative Pharmacy · doi:10.1016/j.sapharm.2014.07.138

The Ubiquitin E3 Ligase MaLUL2 Is Involved in High Temperature-Induced Green Ripening in Banana Fruit

Wei, W., Chen, J., Zeng, Z.-X., et al. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249386 · Cited by 24 · see citing works