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Multifactorial contributions to an acute DNA damage response by BRCA1/BARD1-containing complexes
Open accessAbstract
The BRCA1 gene product and its stoichiometric binding partner, BARD1, play a vital role in the cellular response to DNA damage. However, how they acquire specific biochemical functions after DNA damage is poorly understood. Following exposure to genotoxic stress, DNA damage-specific interactions were observed between BRCA1/BARD1 and the DNA damage-response proteins, TopBP1 and Mre11/Rad50/NBS1. Two distinct DNA damage-dependent super complexes emerged; their activation was dependent, in part, on the actions of specific checkpoint kinases, and each super complex contributed to a distinctive aspect of the DNA damage response. The results support a new, multifactorial model that describes how genotoxic stress enables BRCA1 to execute a diverse set of DNA damage-response functions.
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“Three proteins, Abraxas (also known as Abra1, FAM175A, CCDC98), Bach1 (also known as Brip1, FancJ) and CtIP (also known as RBBP8), directly interact with the BRCA1 BRCT domains through the pSPxF motif in a phosphorylation-dependent manner forming mutually exclusive complexes, which were thus named as the A, B and C complexes of BRCA1 (Greenberg et al., 2006; Kim et al., 2007; Liu et al., 2007;”
From The BRCA1-Interacting Protein Abraxas Is Required for Genomic Stability and Tumor Suppression (2014) · cites this paper as Greenberg et al., 2006
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“FANCJ helicase activity induced in S phase is also required for FANCJ to promote S phase progression and possibly intra-S phase checkpoints [71,72].”
From Hereditary Breast Cancer and the BRCA1-Associated FANCJ/BACH1/BRIP1 (2011) · cites this paper as [72]
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Citations
Cites
Genetic instabilities in human cancers
Lengauer, C., Kinzler, K. W., & Vogelstein, B. (1998) · Nature · doi:10.1038/25292 · Cited by 4,168 · cited 1×
“Testament to this relationship is the observation that a significant fraction of inherited cancer syndromes stem from germline mutations in DNA repair and checkpoint control genes (Lengauer et al. 1998; Vessey et al. 1999).”
BackgroundThe DNA damage response: putting checkpoints in perspective
Zhou, B.-B. S., & Elledge, S. J. (2000) · Nature · doi:10.1038/35044005 · Cited by 3,213
DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis
Bartkova, J., Hořejší, Z., Koed, K., Krämer, A., Tort, F., Zieger, K., Guldberg, P., Sehested, M., Nesland, J. M., Lukas, C., et al. (2005) · Nature · doi:10.1038/nature03482 · Cited by 2,688
Megabase Chromatin Domains Involved in DNA Double-Strand Breaks in Vivo
Rogakou, E. P., Boon, C., Redon, C., & Bonner, W. M. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.5.905 · Cited by 2,422
Breast and Ovarian Cancer Risks Due to Inherited Mutations in BRCA1 and BRCA2
King, M.-C., Marks, J. H., & Mandell, J. B. (2003) · Science · doi:10.1126/science.1088759 · Cited by 2,229
Activation of the DNA damage checkpoint and genomic instability in human precancerous lesions
Gorgoulis, V. G., Vassiliou, L.-V. F., Karakaidos, P., Zacharatos, P., Kotsinas, A., Liloglou, T., Venere, M., DiTullio, R. A., Kastrinakis, N. G., Levy, B., et al. (2005) · Nature · doi:10.1038/nature03485 · Cited by 2,009
Cancer Susceptibility and the Functions of BRCA1 and BRCA2
Venkitaraman, A. R. (2002) · Cell · doi:10.1016/s0092-8674(02)00615-3 · Cited by 1,713
Chk1 and Chk2 kinases in checkpoint control and cancer
Bartek, J., & Lukas, J. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00110-7 · Cited by 1,513
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
Self-citationBrca1 Controls Homology-Directed DNA Repair
Moynahan, M. E., Chiu, J. W., Koller, B. H., & Jasin, M. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80202-6 · Cited by 1,245
Research works printed but not linked: 5
- 1998, Cancer Res., 58, 4375
- 1999, Cancer Res., 59, 4375
- 2002, Cancer Res., 62, 4588
- 2003, Cancer Res., 63, 3049
- 2002, Nat. Genet., 11, 11
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Park, D., Bergin, S. M., Jones, D. M., Ru, P., Koivisto, C. S., Jeon, Y.-J., Sizemore, G. M., Kladney, R. D., Hadjis, A. D., Shakya, R., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-0486 · Cited by 21
The MRN-CtIP Pathway Is Required for Metaphase Chromosome Alignment
Rozier, L., Guo, Y., Peterson, S., Sato, M., Baer, R. J., Gautier, J., & Mao, Y. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.023 · Cited by 19
Xu, Z., Xie, H., Song, L., Huang, Y., & Huang, J. (2025) · DNA repair · doi:10.1016/j.dnarep.2025.103847 · Cited by 25
Autologous K63 deubiquitylation within the BRCA1-A complex licenses DNA damage recognition
Jiang, Q., Foglizzo, M., Morozov, Y. I., Yang, X., Datta, A., Tian, L., Thada, V., Li, W., Zeqiraj, E., & Greenberg, R. A. (2022) · The Journal of Cell Biology · doi:10.1083/jcb.202111050 · Cited by 18
Self-citationNath, S., Somyajit, K., Mishra, A., Scully, R., & Nagaraju, G. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx586 · Cited by 17
Xu, Y., Wu, X., & Her, C. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.642884 · Cited by 19
Livingston, D. M. (2009) · Science · doi:10.1126/science.1174839 · Cited by 16
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Bergstrand, S., O’Brien, E. M., & Farnebo, M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00051 · Cited by 17
HP1 regulates the localization of FANCJ at sites of DNA double‐strand breaks
Wu, W., Togashi, Y., Johmura, Y., Miyoshi, Y., Nobuoka, S., Nakanishi, M., & Ohta, T. (2016) · Cancer Science · doi:10.1111/cas.13008 · Cited by 16
BRCA1 ubiquitylation of CtIP: Just the tIP of the iceberg?
Barber, L. J., & Boulton, S. J. (2006) · DNA repair · doi:10.1016/j.dnarep.2006.08.009 · Cited by 16
Approaches for Assessing and Discovering Protein Interactions in Cancer
Mohammed, H., & Carroll, J. S. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0454 · Cited by 15
Regulation of BRCA1 stability through the tandem UBX domains of isoleucyl-tRNA synthetase 1
CHUNG, S. ‐., Kang, M.-S., Alimbetov, D. S., Mun, G., Yunn, N.-O., Kim, Y., Kim, B., Wie, M., Lee, E. A., Ra, J. S., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34612-y · Cited by 15
Singh, A., Busacca, S., Gaba, A., Sheaff, M. T., Poile, C., Nakas, A., Działo, J., Bzura, A., Dawson, A. G., Fennell, D. A., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02577-3 · Cited by 15
Tantos, Á., Kalmár, L., & Tompa, P. (2015) · Expert Review of Proteomics · doi:10.1586/14789450.2015.1042866 · Cited by 16
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Nicolo, A. D., Parisini, E., Zhong, Q., Palma, M. D., Stoeckert, K. A., Domchek, S. M., Nathanson, K. L., Caligo, M. A., Vidal, M., Cusick, M. E., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-1440 · Cited by 15
Structural aspects of multi-domain RING/Ubox E3 ligases in DNA repair
Hibbert, R. G., Mattiroli, F., & Sixma, T. K. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.01.014 · Cited by 15
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Verma, P., & Greenberg, R. A. (2021) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2021.05.006 · Cited by 15
Self-citationDNA damage response and repair in the development and treatment of brain tumors
Dana, P. M., Sadoughi, F., Mirzaei, H., Asemi, Z., & Yousefi, B. (2022) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2022.174957 · Cited by 15
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Rigon, M., Mutti, L., & Campanella, M. (2024) · Molecular Oncology · doi:10.1002/1878-0261.13591 · Cited by 13
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Tu, Z., Aird, K. M., & Zhang, R. (2012) · Small GTPases · doi:10.4161/sgtp.19884 · Cited by 12
Cantor, S. B., & Nayak, S. U. (2016) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2016.02.003 · Cited by 13
Self-citationPrime Editing: Mechanistic Insights and DNA Repair Modulation
Mentani, A., Maresca, M., & Shiriaeva, A. (2025) · Cells · doi:10.3390/cells14040277 · Cited by 13
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Dhar, S., & Brosh, R. M. (2018) · Cell Cycle · doi:10.1080/15384101.2018.1520567 · Cited by 13
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Bian, C., WU, R. T., Cho, K. R., & Yu, X. (2012) · PLoS ONE · doi:10.1371/journal.pone.0040406 · Cited by 12
Orr, K. S., & Savage, K. I. (2015) · InTech eBooks · doi:10.5772/59996 · Cited by 14
Liang, S., Esswein, S. R., Ochi, T., Wu, Q., Ascher, D. B., Chirgadze, D. Y., Sibanda, B. L., & Blundell, T. L. (2016) · Structural Chemistry · doi:10.1007/s11224-016-0841-7 · Cited by 12
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Cusin, I., Teixeira, D., Zahn‐Zabal, M., de Laval, V. R., Gleizes, A., Viassolo, V., Chappuis, P. O., Hutter, P., Bairoch, A., & Gaudet, P. (2018) · Human Genomics · doi:10.1186/s40246-018-0168-0 · Cited by 11
Cdk1 and BRCA1 target γ-tubulin to microtubule domains
Hubert, T., Vandekerckhove, J. S., & Gettemans, J. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.09.064 · Cited by 12
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Guénolé, A., Velilla, F., Chartier, A., Rich, A., Carvunis, A., Sardet, C., Simonelig, M., & Sobhian, B. (2022) · Scientific Reports · doi:10.1038/s41598-022-13309-8 · Cited by 13
Self-citationBreast cancer gene variants: separating the harmful from the harmless
Domchek, S. M., & Greenberg, R. A. (2009) · Journal of Clinical Investigation · doi:10.1172/jci40577 · Cited by 11
Self-citationAlexander, K. L., Jenkins, Y., Alomari, M., Mirzaei, M., Best, G., Pascovici, D., Mactier, S., Mulligan, S. P., Haynes, P. A., & Christopherson, R. I. (2015) · Oncotarget · doi:10.18632/oncotarget.5715 · Cited by 11
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Maas, E. J., Betz‐Stablein, B., Aoude, L. G., Soyer, H. P., & McInerney-Leo, A. M. (2022) · Trends in Genetics · doi:10.1016/j.tig.2022.06.007 · Cited by 11
Contemplating chemosensitivity of basal-like breast cancer based on BRCA1 dysfunction
Ohta, T., Wu, W., Koike, A., Asakawa, H., Koizumi, H., & Fukuda, M. (2009) · Breast Cancer · doi:10.1007/s12282-009-0115-y · Cited by 11
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Karppinen, S. (2009) · Cited by 11
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Li, S., Tang, M., Xiong, Y., Feng, X., Wang, C., Nie, L., Huang, M., Zhang, H., Yin, L., Zhu, D., et al. (2024) · Oncogene · doi:10.1038/s41388-024-03108-y · Cited by 10
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Antoccia, A., Sakamoto, S., Matsuura, S., Tauchi, H., & Komatsu, K. (2008) · Radiation Research · doi:10.1667/rr1357.1 · Cited by 9
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Elkholi, I. E., Foulkes, W. D., & Rivera, B. (2021) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-1509 · Cited by 9
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Chen, H., Shan, J., Chen, D., Wang, R., Qi, W., Wang, H., Ke, Y., Liu, W., & Zeng, X. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27824 · Cited by 10
Park, D., Gharghabi, M., Schrock, M. S., Plow, R., Druck, T., Yungvirt, C., Aldaz, C. M., & Huebner, K. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103264 · Cited by 8
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Hillukkala, T. (2006) · Cited by 8
PALB2 as a potential prognostic biomarker for colorectal cancer
Pan, W., Lu, K., Wang, W., Yao, J., & Hou, Y. (2020) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2020.107289 · Cited by 7
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Liu, Y., & Smolka, M. B. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201601028 · Cited by 7
The ORFIUS complex regulates ORC2 localization at replication origins
Yang, Z., Mogre, S., He, R., Berdan, E. L., Sui, S. J. H., & Hill, S. J. (2024) · NAR Cancer · doi:10.1093/narcan/zcae003 · Cited by 6
Sakasai, R., Sakai, A., Iimori, M., Kiyonari, S., Matsuoka, K., Kakeji, Y., Kitao, H., & Maehara, Y. (2012) · Genes to Cells · doi:10.1111/gtc.12011 · Cited by 6
Cheng, J., Tsuda, M., Okolotowicz, K. J., Dwyer, M., Bushway, P., Colas, A. R., Lancman, J. J., Schade, D., Perea‐Gil, I., Bruyneel, A. A. N., et al. (2021) · Cell chemical biology · doi:10.1016/j.chembiol.2021.01.001 · Cited by 7
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Greenberg, R. A. (2006) · Cancer Biology & Therapy · doi:10.4161/cbt.5.9.3370 · Cited by 5
Self-citationChoudhary, R. K., Siddiqui, M. Q., Gadewal, N., Kumar, N. S., Kuligina, E. S., & Varma, A. K. (2018) · RSC Advances · doi:10.1039/c8ra06524a · Cited by 5
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Chen, T., Yeh, H., Chen, P.-P., Huang, W.-T., Wu, C.-Y., Liao, T.-C., Lin, S.-L., Chen, Y.-Y., Lin, K., Hsu, S. D., et al. (2022) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2022.130099 · Cited by 5
Jiao, Y., Zhang, Y., & Zhu, Y. (2016) · Science China Life Sciences · doi:10.1007/s11427-016-5086-6 · Cited by 3
Thanh, N. T. N., Tram, P. B., Tuyet, N. H. H., Uyen, N. H. P., Tien, L. T. M., Anh, D. N., Van, L. T. T., Luan, H. H., & Huế, N. T. (2021) · Cytology and Genetics · doi:10.3103/s0095452721040101 · Cited by 3
The BRCA1-A complex restricts replication fork reversal-dependent DNA repair in ATM deficient cells
Datta, A., Jackson, J., Morozov, Y. I., Qiu, J., Vindigni, A., & Greenberg, R. A. (2026) · Nature Communications · doi:10.1038/s41467-026-75271-7 · Cited by 2
Self-citationPyrimidine base damage is increased in women with BRCA mutations
Budzinski, E. E., Patrzyc, H. B., Dawidzik, J. B., Freund, H. G., Frederick, P. J., Godoy, H. E., Voian, N. C., Odunsi, K. O., & Box, H. C. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.04.001 · Cited by 2
BRCA1 and BRCA2: Role in the DNA Damage Response, Cancer Formation and Treatment
Savage, K. I., & Harkin, D. P. (2009) · Springer eBooks · doi:10.1007/978-90-481-2561-6_18 · Cited by 3
What can yeast tell us about breast cancer?
Golubeva, V. A., & Monteiro, Á. N. A. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1230376 · Cited by 2
Baralić, K., Božović, P., & Đukić-Ćosić, D. (2024) · Archives of Industrial Hygiene and Toxicology · doi:10.2478/aiht-2024-75-3817 · Cited by 1
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Xie, J. (2009) · eScholarship@UMassChan · doi:10.13028/95cm-wn54 · Cited by 1
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Jiao, Y., Xu, X., & Hao, Y. (2012) · The Chinese-German Journal of Clinical Oncology · doi:10.1007/s10330-012-1088-4 · Cited by 1
Ramaekers, C. H. M. A., van den Beucken, T., Bristow, R. G., Chiu, R. K., Durocher, D., & Wouters, B. G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0089997 · Cited by 1
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Ramsay, J., Al-Zeer, K., & Jacob, Z. (2011) · InTech eBooks · doi:10.5772/19995 · Cited by 1
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Solomon, E., & Morris, J. R. (2009) · Springer eBooks · doi:10.1007/978-1-4419-0477-5_4 · Cited by 2
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Velkova, A. (2009) · Defense Technical Information Center (DTIC) · doi:10.21236/ada511277
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Bennett, C. B. (2005) · Defense Technical Information Center (DTIC) · doi:10.21236/ada437737
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Gu, Y. (2015) · Työväentutkimus Vuosikirja
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Flynn, R. L. (2007) · The Journal of the American Medical Association (JAMA) Network (American Medical Association) · doi:10.13028/ad72-xg56
Morgese, F. (2009) · OpenstarTs (Univeristy of Trieste https://www.units.it/)
Signaling at Stalled Replication Forks
Mordes, D. A., & Cortez, D. (2009) · Springer eBooks · doi:10.1007/978-90-481-2561-6_2
Molecular Analysis of Breast Cancer Transcriptomes, Genomes, and Circulating Tumor DNA
Olsson, E. (2015) · Lund University Publications (Lund University)
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Wiltshire, T. D. (2007) · doi:10.33915/etd.2601
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Nelson, N. C. (2015) · ThinkIR: The University of Louisville's Institutional Repository (University of Louisville) · doi:10.18297/etd/2336
A New Cell-Free System to Study BRCA1 Function
Walter, J. C., & Diamond, B. (2014) · Defense Technical Information Center (DTIC) · doi:10.21236/ada608618
DEVELOPMENT OF A FUNCTIONAL ASSAY FOR DETERMINATION OF BRCA1 CARRIER STATUS
Bathurst, L. (2014) · QSpace (Queen's University Library)
Modulating DNA Damage Responses for Improved Breast Cancer Therapy
Ilcheva, M. (2015)
Epigenetic Instability Induced by DNA Base Lesion via DNA Base Excision Repair
Jiang, Z. (2017) · FIU - Digital Commons (Florida International University) · doi:10.25148/etd.fidc003999
Genes Involved in the Cisplatin Response of BRCA2 Cancers
Rose, J. M. (2012) · Digital WPI
In silico BRCA1 pathway analysis in breast invasive carcinoma
Shah, Z. A., Nouroz, F., & Tayyeb, A. (2021) · MGM Journal of Medical Sciences · doi:10.4103/mgmj.mgmj_88_20
POGZ modulates the DNA damage response in a HP1-dependent mannerPreprint
Heath, J., Simo‐Cheyou, E. R., Findlay, S., Luo, V. M., Carpio, E. P., Lee, J., Djerir, B., Chen, X., Morin, T., Lebeau, B., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.06.28.447216
Characterization of homologous recombination proteins in telomere processing and t-circle formation
Stockton, P. D. Q. (2009) · eScholarship (California Digital Library)
Vollebregt, C. (2012)
(2013) · CRC Press eBooks · doi:10.1201/b14587-15
Cantor, S. B., & Xie, J. (2011) · Springer eBooks · doi:10.1007/978-3-642-16483-5_513
Self-citationFaculty Opinions recommendation of Human CtIP promotes DNA end resection.
Comai, L. (2007) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1093988.548939
Weißhaar, B. (2008) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.1097593.553679
(2006) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1863
Cantor, S. B., & Xie, J. (2008) · Springer eBooks · doi:10.1007/978-3-540-47648-1_513
Self-citationCauses and consequences of mitotic DNA damage
Kok, Y. P. (2022) · doi:10.33612/diss.222465462
Data from BRCA1 Ubiquitinates RPB8 in Response to DNA Damage
Wu, W., Nishikawa, H., Hayami, R., Sato, K., Honda, A., Aratani, S., Nakajima, T., Fukuda, M., & Ohta, T. (2023) · doi:10.1158/0008-5472.c.6494961
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Wu, W., Nishikawa, H., Hayami, R., Sato, K., Honda, A., Aratani, S., Nakajima, T., Fukuda, M., & Ohta, T. (2023) · doi:10.1158/0008-5472.c.6494961.v1
Rebbeck, T. R., Mitra, N., Domchek, S. M., Wan, F., Chuai, S., Friebel, T. M., Panossian, S., Spurdle, A. B., Chenevix‐Trench, G., Singer, C. F., et al. (2023) · doi:10.1158/0008-5472.c.6499160.v1
Self-citationGeorge, J., Alsop, K., Etemadmoghadam, D., Hondow, H., Mikeska, T., Dobrovic, A., DeFazio, A., Smyth, G. K., Levine, D. A., Mitchell, G., et al. (2023) · doi:10.1158/1078-0432.c.6522258.v1
Hu, Y., Petit, S. A., Ficarro, S. B., Toomire, K. J., Xie, A., Lim, E., Cao, S. A., Park, E. Y., Eck, M. J., Scully, R., et al. (2023) · doi:10.1158/2159-8290.22530476.v1
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Sànchez, G. M. (2012) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)
Metadata
- Authors
- Greenberg, R. A., Sobhian, B., Pathania, S., Cantor, S. B., Nakatani, Y., & Livingston, D. M.
- Affiliations
- Harvard University (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2006-01-01
- Volume
- 20
- Issue
- 1
- Pages
- 34-46
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC1356099
- OpenAlex
- W2164458581
- Cited by
- 308
- References
- 61
- Citations by year
- 2026: 2 · 2025: 3 · 2024: 4 · 2023: 9 · 2022: 12 · 2021: 17 · 2020: 13 · 2019: 4 · 2018: 14 · 2017: 12 · 2016: 10 · 2015: 19 · 2014: 21 · 2013: 19 · 2012: 22
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- eScholarship@UMassChan (submittedVersion)
- Funders
- Leukemia Research Foundation
- Broad Institute
- Österreichischen Akademie der Wissenschaften
- National Cancer Institute
- 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
- BRCA1, BARD1, DNA damage response, TopBP1, Mre11-Rad50-Nbs1, checkpoint kinase, genotoxic stress
- MeSH terms
- MRE11 Homologue Protein, Carrier Proteins, Cell Cycle, DNA Damage, DNA Repair, DNA-Binding Proteins, Humans, Nuclear Proteins, Protein Binding, Acid Anhydride Hydrolases, Cell Cycle Proteins, BRCA1 Protein, Tumor Suppressor Proteins, Ubiquitin-Protein Ligases, DNA Repair Enzymes, Cell Line, Tumor
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