The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
A genome-wide homologous recombination screen identifies the RNA-binding protein RBMX as a component of the DNA-damage response
Open accessAbstract
Repair of DNA double-strand breaks is critical to genomic stability and the prevention of developmental disorders and cancer. A central pathway for this repair is homologous recombination (HR). Most knowledge of HR is derived from work in prokaryotic and eukaryotic model organisms. We carried out a genome-wide siRNA-based screen in human cells. Among positive regulators of HR we identified networks of DNA-damage-response and pre-mRNA-processing proteins, and among negative regulators we identified a phosphatase network. Three candidate proteins localized to DNA lesions, including RBMX, a heterogeneous nuclear ribonucleoprotein that has a role in alternative splicing. RBMX accumulated at DNA lesions through multiple domains in a poly(ADP-ribose) polymerase 1-dependent manner and promoted HR by facilitating proper BRCA2 expression. Our screen also revealed that off-target depletion of RAD51 is a common source of RNAi false positives, raising a cautionary note for siRNA screens and RNAi-based studies of HR.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“CRISPRi represents an important advance over RNAi, since it lacks the pervasive off-target effects (Gilbert et al., 2014) inherent to RNAi-based screening approaches (Adamson et al., 2012; Jackson et al., 2003; Kaelin, 2012).”
From CRISPR Interference-Based Platform for Multimodal Genetic Screens in Human iPSC-Derived Neurons (2019) · cites this paper as Adamson et al., 2012
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
1 retracted
RETRACTED: hnRNP K: An HDM2 Target and Transcriptional Coactivator of p53 in Response to DNA Damage
Moumen, A., Masterson, P., O'Connor, M. J., & Jackson, S. P. (2005) · Cell · doi:10.1016/j.cell.2005.09.032 · Cited by 350
RetractedMicroRNAs: Target Recognition and Regulatory Functions
Bartel, D. P. (2009) · Cell · doi:10.1016/j.cell.2009.01.002 · Cited by 20,068
The DNA Damage Response: Making It Safe to Play with Knives
Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368
Self-citationATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage
Matsuoka, S., Ballif, B. A., Smogorzewska, A., McDonald, E. R., Hurov, K. E., Luo, J., Bakalarski, C. E., Zhao, Z., Solimini, N., Lerenthal, Y., et al. (2007) · Science · doi:10.1126/science.1140321 · Cited by 3,075
Self-citationMechanism of Eukaryotic Homologous Recombination
Filippo, J. S., Sung, P., & Klein, H. L. (2008) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.061306.125255 · Cited by 1,766
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
Human CtIP promotes DNA end resection
Sartori, A. A., Lukas, C., Coates, J., Mistrik, M., Fu, S., Bartek, J., Baer, R., Lukas, J., & Jackson, S. P. (2007) · Nature · doi:10.1038/nature06337 · Cited by 1,362
Molecular views of recombination proteins and their control
West, S. C. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1127 · Cited by 977
Control of BRCA2 Cellular and Clinical Functions by a Nuclear Partner, PALB2
Xia, B., Sheng, Q., Nakanishi, K., Ohashi, A., Wu, J., Christ, N., Liu, X., Jasin, M., Couch, F. J., & Livingston, D. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.022 · Cited by 861
Identification of the FANCI Protein, a Monoubiquitinated FANCD2 Paralog Required for DNA Repair
Smogorzewska, A., Matsuoka, S., Vinciguerra, P., McDonald, E. R., Hurov, K. E., Luo, J., Ballif, B. A., Gygi, S. P., Hofmann, K., D’Andrea, A. D., et al. (2007) · Cell · doi:10.1016/j.cell.2007.03.009 · Cited by 718
Self-citation
Cited by
Sorted by citations
Genome-Scale CRISPR-Mediated Control of Gene Repression and Activation
Gilbert, L. A., Horlbeck, M. A., Adamson, B., Villalta, J. E., Chen, Y., Whitehead, E. H., Guimaraes, C., Panning, B., Ploegh, H. L., Bassik, M. C., et al. (2014) · Cell · doi:10.1016/j.cell.2014.09.029 · Cited by 2,728
Self-citationDNA 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
Davoli, T., Xu, A. W., Mengwasser, K. E., Sack, L. M., Yoon, J. C., Park, P. J., & Elledge, S. J. (2013) · Cell · doi:10.1016/j.cell.2013.10.011 · Cited by 815
Self-citationNoncoding RNA NORAD Regulates Genomic Stability by Sequestering PUMILIO Proteins
Lee, S., Kopp, F. B., Chang, T.-C., Sataluri, A., Chen, B., Sivakumar, S., Yu, H., Xie, Y., & Mendell, J. T. (2015) · Cell · doi:10.1016/j.cell.2015.12.017 · Cited by 892
N 6-methyladenosine alters RNA structure to regulate binding of a low-complexity protein
Liu, N., Zhou, K. I., Parisien, M., Dai, Q., Diatchenko, L. B., & Pan, T. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx141 · Cited by 786
CRISPRi-based genome-scale identification of functional long noncoding RNA loci in human cells
Liu, S. J., Horlbeck, M. A., Cho, S. W., Birk, H. S., Malatesta, M., He, D. X., Attenello, F. J., Villalta, J. E., Cho, M. Y., Chen, Y., et al. (2016) · Science · doi:10.1126/science.aah7111 · Cited by 756
CRISPR Interference-Based Platform for Multimodal Genetic Screens in Human iPSC-Derived Neurons
Tian, R., Gachechiladze, M. A., Ludwig, C. H., Laurie, M. T., Hong, J. Y., Nathaniel, D., Prabhu, A. V., Fernandopulle, M. S., Patel, R., Abshari, M., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.07.014 · Cited by 543
Pfister, S. X., Ahrabi, S., Zalmas, L., Sarkar, S., Aymard, F., Bachrati, C. Z., Helleday, T., Legube, G., Thangue, N. B. L., Porter, A. C. G., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.05.026 · Cited by 496
Yazinski, S. A., Comaills, V., Buisson, R., Genois, M., Nguyen, H. D., Ho, C. K., Kwan, T. T., Morris, R. T., Lauffer, S., Nussenzweig, A., et al. (2017) · Genes & Development · doi:10.1101/gad.290957.116 · Cited by 405
The NORAD lncRNA assembles a topoisomerase complex critical for genome stability
Munschauer, M., Nguyen, C. T., Sirokman, K., Hartigan, C. R., Hogstrom, L. J., Engreitz, J., Ulirsch, J. C., Fulco, C. P., Subramanian, V., Chen, J., et al. (2018) · Nature · doi:10.1038/s41586-018-0453-z · Cited by 386
RNA-binding proteins in tumor progression
Qin, H., Ni, H., Liu, Y., Yuan, Y., Xi, T., Li, X., & Zheng, L. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00927-w · Cited by 387
Jungmichel, S., Rosenthal, F., Altmeyer, M., Lukas, J., Hottiger, M. O., & Nielsen, M. L. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.026 · Cited by 393
CRISPRi and CRISPRa Screens in Mammalian Cells for Precision Biology and Medicine
Kampmann, M. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.7b00657 · Cited by 387
A library of TAL effector nucleases spanning the human genome
Kim, Y., Kweon, J., Kim, A., Chon, J. K., Yoo, J. Y., Kim, H. J., Kim, S., Lee, C., Jeong, E., Chung, E., et al. (2013) · Nature Biotechnology · doi:10.1038/nbt.2517 · Cited by 379
Mechanisms of nuclear content loading to exosomes
Yokoi, A., Villar‐Prados, A., Oliphint, P. A., Zhang, J., Song, X., Hoff, P. L. D., Morey, R. E., Liu, J., Roszik, J., Clise-Dwyer, K., et al. (2019) · Science Advances · doi:10.1126/sciadv.aax8849 · Cited by 299
Adam, S., Polo, S. E., & Almouzni, G. (2013) · Cell · doi:10.1016/j.cell.2013.08.029 · Cited by 309
Mastrocola, A. S., Kim, S. H., Trinh, A. T., Rodenkirch, L. A., & Tibbetts, R. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.497974 · Cited by 280
PCAT-1 , a Long Noncoding RNA, Regulates BRCA2 and Controls Homologous Recombination in Cancer
Prensner, J. R., Chen, W., Iyer, M. K., Cao, Q., Ma, T., Han, S., Sahu, A., Malik, R., Wilder-Romans, K., Navone, N. M., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-3159 · Cited by 255
Readers of poly(ADP-ribose): designed to be fit for purpose
Teloni, F., & Altmeyer, M. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1383 · Cited by 269
Maréchal, A., Li, J.-M., Ji, X. Y., Wu, C.-S. P., Yazinski, S. A., Nguyen, H. D., Liu, S., Jiménez, A. E., Jin, J., & Zou, L. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.11.002 · Cited by 258
Dissecting the expression landscape of RNA-binding proteins in human cancers
Kechavarzi, B., & Janga, S. C. (2014) · Genome biology · doi:10.1186/gb-2014-15-1-r14 · Cited by 243
Genome-wide transcriptome profiling of homologous recombination DNA repair
Peng, G., Lin, C. C.-J., Mo, W., Dai, H., Park, Y., Kim, S. M., Peng, Y., Mo, Q., Siwko, S. K., Hu, R., et al. (2014) · Nature Communications · doi:10.1038/ncomms4361 · Cited by 231
The new (dis)order in RNA regulation
Järvelin, A. I., Noerenberg, M., Davis, I., & Castelló, A. (2016) · Cell Communication and Signaling · doi:10.1186/s12964-016-0132-3 · Cited by 232
A Macrohistone Variant Links Dynamic Chromatin Compaction to BRCA1-Dependent Genome Maintenance
Khurana, S., Kruhlak, M. J., Kim, J., Tran, A. D., Liu, J., Nyswaner, K., Shi, L., Jailwala, P., Sung, M.-H., Hakim, O., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.024 · Cited by 220
Drosha drives the formation of DNA:RNA hybrids around DNA break sites to facilitate DNA repair
Lu, W.-T., Hawley, B. R., Skalka, G., Baldock, R. A., Smith, E. M., Bader, A. S., Malewicz, M., Watts, F. Z., Wilczynska, A., & Bushell, M. (2018) · Nature Communications · doi:10.1038/s41467-018-02893-x · Cited by 229
STING enhances cell death through regulation of reactive oxygen species and DNA damage
Hayman, T. J., Baro, M., MacNeil, T., Phoomak, C., Aung, T. N., Cui, W., Leach, K., Iyer, R. P., Challa, S., Sandoval-Schaefer, T., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-22572-8 · Cited by 219
DNA repair defects in cancer and therapeutic opportunitiesPreprint
Hopkins, J. L., Lan, L., & Zou, L. (2022) · Genes & Development · doi:10.1101/gad.349431.122 · Cited by 212
Genetic Screens Reveal FEN1 and APEX2 as BRCA2 Synthetic Lethal Targets
Mengwasser, K. E., Adeyemi, R. O., Leng, Y., Choi, M. Y., Clairmont, C. S., D’Andrea, A. D., & Elledge, S. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.12.008 · Cited by 203
Self-citationMapping the genetic landscape of DNA double-strand break repair
Hussmann, J. A., Jia, L., Ravisankar, P., Yan, J., Cirincione, A., Xu, A., Simpson, D., Yang, D., Bothmer, A., Cotta‐Ramusino, C., et al. (2021) · Cell · doi:10.1016/j.cell.2021.10.002 · Cited by 188
Self-citationRulten, S. L., Rotheray, A., Green, R. L., Grundy, G. J., Moore, D. A. Q., Gómez-Herreros, F., Hafezparast, M., & Caldecott, K. W. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt835 · Cited by 190
Britton, S., Dernoncourt, E., Delteil, C., Froment, C., Burlet‐Schiltz, O., Salles, B., Frit, P., & Calsou, P. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku601 · Cited by 185
Mersaoui, S. Y., Yu, Z., Coulombe, Y., Karam, M., Busatto, F. F., Masson, J., & Richard, S. (2019) · The EMBO Journal · doi:10.15252/embj.2018100986 · Cited by 186
Coupling of Homologous Recombination and the Checkpoint by ATR
Buisson, R., Joshi, N., Rodrigue, A., Ho, C. K., Kreuzer, J., Foo, T. K., Hardy, É. J.-L., Dellaire, G., Haas, W., Xia, B., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2016.12.007 · Cited by 186
Histone demethylase KDM5A regulates the ZMYND8–NuRD chromatin remodeler to promote DNA repair
Gong, F., Clouaire, T., Aguirrebengoa, M., Legube, G., & Miller, K. M. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201611135 · Cited by 192
Izhar, L., Adamson, B., Ciccia, A., Lewis, J., Vaites, L. P., Leng, Y., Liang, A. C. T., Westbrook, T. F., Harper, J. W., & Elledge, S. J. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.053 · Cited by 178
Self-citationPromotion of BRCA2-Dependent Homologous Recombination by DSS1 via RPA Targeting and DNA Mimicry
Zhao, W., Vaithiyalingam, S., San Filippo, J., Maranon, D. G., Jimenez-Sainz, J., Fontenay, G. V., Kwon, Y., Leung, S. G., Lu, L., Jensen, R. B., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.05.032 · Cited by 177
Functions, Regulation, and Therapeutic Implications of the ATR Checkpoint Pathway
Yazinski, S. A., & Zou, L. (2016) · Annual Review of Genetics · doi:10.1146/annurev-genet-121415-121658 · Cited by 178
Linking RNA biology to lncRNAsPreprint
Goff, L. A., & Rinn, J. L. (2015) · Genome Research · doi:10.1101/gr.191122.115 · Cited by 173
Reprogramming cellular events by poly(ADP-ribose)-binding proteins
Krietsch, J., Rouleau, M., Pic, É., Ethier, C., Dawson, T. M., Dawson, V. L., Masson, J., Poirier, G. G., & Gagné, J. (2012) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2012.12.005 · Cited by 185
Defining and Modulating ‘BRCAness’
Byrum, A. K., Vindigni, A., & Mosammaparast, N. (2019) · Trends in Cell Biology · doi:10.1016/j.tcb.2019.06.005 · Cited by 164
Krietsch, J., Caron, M., Gagné, J., Ethier, C., Vignard, J., Vincent, M., Rouleau, M., Hendzel, M. J., Poirier, G. G., & Masson, J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks798 · Cited by 166
A bioinformatics method identifies prominent off-targeted transcripts in RNAi screens
Sigoillot, F. D., Lyman, S. K., Huckins, J. F., Adamson, B., Chung, E., Quattrochi, B., & King, R. W. (2012) · Nature Methods · doi:10.1038/nmeth.1898 · Cited by 162
Self-citationLiu, Y., Cao, Z., Wang, Y., Guo, Y., Xu, P., Yuan, P., Liu, Z., He, Y. M., & Wei, W. (2018) · Nature Biotechnology · doi:10.1038/nbt.4283 · Cited by 154
TGF-β Inhibition Rescues Hematopoietic Stem Cell Defects and Bone Marrow Failure in Fanconi Anemia
Zhang, H., Kozono, D., O’Connor, K. W., Vidal-Cardenas, S. L., Rousseau, A., Hamilton, A., Moreau, L. A., Gaudiano, E. F., Greenberger, J. S., Bagby, G. C., et al. (2016) · Cell stem cell · doi:10.1016/j.stem.2016.03.002 · Cited by 158
A BRCA1‐interacting lncRNA regulates homologous recombination
Sharma, V., Khurana, S., Kubben, N., Abdelmohsen, K., Oberdoerffer, P., Gorospe, M., & Misteli, T. (2015) · EMBO Reports · doi:10.15252/embr.201540437 · Cited by 151
The RNA Splicing Response to DNA Damage
Shkreta, L., & Chabot, B. (2015) · Biomolecules · doi:10.3390/biom5042935 · Cited by 156
DEAD Box 1 Facilitates Removal of RNA and Homologous Recombination at DNA Double-Strand Breaks
Li, L., Germain, D. R., Poon, H.-Y., Hildebrandt, M. R., Monckton, E. A., McDonald, D., Hendzel, M. J., & Godbout, R. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00415-16 · Cited by 159
Khoury-Haddad, H., Guttmann‐Raviv, N., Ipenberg, I., Huggins, D. J., Jeyasekharan, A. D. D., & Ayoub, N. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317585111 · Cited by 148
Cell fitness screens reveal a conflict between LINE-1 retrotransposition and DNA replication
Ardeljan, D., Steranka, J. P., Liu, C., Li, Z., Taylor, M. S., Payer, L. M., Gorbounov, M., Sarnecki, J. S., Deshpande, V., Hruban, R. H., et al. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0372-1 · Cited by 135
Self-citationHoward, S. M., Yanez, D. A., & Stark, J. M. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1004943 · Cited by 148
Lin, A., Giuliano, C. J., Sayles, N. M., & Sheltzer, J. M. (2017) · eLife · doi:10.7554/elife.24179 · Cited by 147
Chromatin dynamics after DNA damage: The legacy of the access–repair–restore model
Polo, S. E., & Almouzni, G. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.09.014 · Cited by 142
Two familial ALS proteins function in prevention/repair of transcription-associated DNA damage
Hill, S. J., Mordes, D. A., Cameron, L., Neuberg, D. S., Landini, S., Eggan, K. C., & Livingston, D. M. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1611673113 · Cited by 136
Charity begins at home: non-coding RNA functions in DNA repair
Chowdhury, D., Choi, Y. E., & Brault, M. E. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3523 · Cited by 140
RFWD3-Dependent Ubiquitination of RPA Regulates Repair at Stalled Replication Forks
Elia, A. E. H., Wang, D. C., Willis, N. A., Boardman, A. P., Hajdú, I., Adeyemi, R. O., Lowry, E. L., Gygi, S. P., Scully, R., & Elledge, S. J. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.011 · Cited by 132
Self-citationSpecificity of RNAi, LNA and CRISPRi as loss-of-function methods in transcriptional analysis
Stojic, L., Lun, A. T. L., Mangei, J., Mascalchi, P., Quarantotti, V., Barr, A. R., Bakal, C., Marioni, J. C., Gergely, F. V., & Odom, D. T. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky437 · Cited by 132
JMJD1C demethylates MDC1 to regulate the RNF8 and BRCA1–mediated chromatin response to DNA breaks
Watanabe, S., Watanabe, K., Akimov, V., Bártková, J., Blagoev, B., Lukas, J., & Bártek, J. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2702 · Cited by 139
Jubin, T., Kadam, A. A., Jariwala, M., Bhatt, S., Sutariya, S., Gani, A. R., Gautam, S., & Begum, R. (2016) · Cell Proliferation · doi:10.1111/cpr.12268 · Cited by 136
Targeting PFKFB3 radiosensitizes cancer cells and suppresses homologous recombination
Gustafsson, N., Färnegårdh, K., Bonagas, N., Ninou, A. H., Groth, P., Wiita, E., Jönsson, M., Hallberg, K., Lehto, J., Pennisi, R., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-06287-x · Cited by 128
Kampmann, M., Bassik, M. C., & Weissman, J. S. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1307002110 · Cited by 123
Systematic E2 screening reveals a UBE2D–RNF138–CtIP axis promoting DNA repair
Schmidt, C. K., Galanty, Y., Sczaniecka-Clift, M., Coates, J., Jhujh, S. S., Demir, M., Cornwell, M., Beli, P., & Jackson, S. P. (2015) · Nature Cell Biology · doi:10.1038/ncb3260 · Cited by 123
DNA damage: RNA-binding proteins protect from near and far
Dutertre, M., Lambert, S., Carreira, A., Amor-Guéret, M., & Vagner, S. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.01.003 · Cited by 127
The role of hnRNPs in frontotemporal dementia and amyotrophic lateral sclerosis
Bampton, A., Gittings, L. M., Fratta, P., Lashley, T., & Gatt, A. P. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02203-0 · Cited by 116
BRCA2 promotes DNA‐RNA hybrid resolution by DDX5 helicase at DNA breaks to facilitate their repair‡
Sessa, G., Gómez‐González, B., Silva, S. D. R., Calero, C. P., Beaurepere, R., Barroso, S. I., Martineau, S., Martin, C. A., Ehlén, Å., Martínez, J. S., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2020106018 · Cited by 118
Roles of RNA-Binding Proteins in DNA Damage Response
Kai, M. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17030310 · Cited by 112
BRCA1 Haploinsufficiency Is Masked by RNF168-Mediated Chromatin Ubiquitylation
Zong, D., Adam, S., Wang, Y., Sasanuma, H., Callén, E., Murga, M., Day, A., Kruhlak, M. J., Wong, N., Munro, M., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.12.010 · Cited by 110
Yang, X., Li, L., Liang, J., Shi, L., Yang, J., Yi, X., Zhang, D., Han, X., Yu, N., & Shang, Y. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.473199 · Cited by 112
RNA Processing and Genome Stability: Cause and Consequence
Wickramasinghe, V. O., & Venkitaraman, A. R. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.001 · Cited by 110
The roles of RNA in DNA double-strand break repair
Bader, A. S., Hawley, B. R., Wilczynska, A., & Bushell, M. (2020) · British Journal of Cancer · doi:10.1038/s41416-019-0624-1 · Cited by 121
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
High-Throughput Imaging for the Discovery of Cellular Mechanisms of Disease
Pegoraro, G., & Misteli, T. (2017) · Trends in Genetics · doi:10.1016/j.tig.2017.06.005 · Cited by 106
DEAD-Box RNA Helicases and Genome Stability
Cargill, M. J., Venkataraman, R., & Lee, S. C.-W. (2021) · Genes · doi:10.3390/genes12101471 · Cited by 105
Biomolecular condensates at sites of DNA damage: More than just a phase
Spegg, V., & Altmeyer, M. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103179 · Cited by 101
Fine-Tuning of DNA Damage-Dependent Ubiquitination by OTUB2 Supports the DNA Repair Pathway Choice
Kato, K., Nakajima, K., Ui, A., Terao-Muto, Y., Ogiwara, H., & Nakada, S. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.01.030 · Cited by 102
CRISPR/Cas System and Factors Affecting Its Precision and Efficiency
Javaid, N., & Choi, S. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.761709 · Cited by 106
DNA Repair and Therapeutic Strategies in Cancer Stem Cells
Gillespie, M. S., Ward, C. M., & Davies, C. C. (2023) · Cancers · doi:10.3390/cancers15061897 · Cited by 101
Mechanisms of genome instability induced by RNA-processing defects
Chan, Y. A., Hieter, P., & Stirling, P. C. (2014) · Trends in Genetics · doi:10.1016/j.tig.2014.03.005 · Cited by 96
From “Cellular” RNA to “Smart” RNA: Multiple Roles of RNA in Genome Stability and Beyond
Michelini, F., Jalihal, A. P., Francia, S., Meers, C., Neeb, Z. T., Rossiello, F., Gioia, U., Aguado, J., Jones-Weinert, C., Luke, B., et al. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.7b00487 · Cited by 85
ZMYM3 regulates BRCA1 localization at damaged chromatin to promote DNA repairPreprint
Leung, J. W. C., Makharashvili, N., Agarwal, P., Chiu, L.-Y., Pourpre, R., Cammarata, M. B., Cannon, J. R., Sherker, A., Durocher, D., Brodbelt, J. S., et al. (2017) · Genes & Development · doi:10.1101/gad.292516.116 · Cited by 92
Revolutionizing DNA repair research and cancer therapy with CRISPR–Cas screens
Awwad, S. W., Serrano-Benítez, A., Thomas, J. C., Gupta, V., & Jackson, S. P. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00571-x · Cited by 93
The impact of SF3B1 mutations in CLL on the DNA-damage response
Raa, G. D. T., Derks, I. A. M., Navrkalová, V., Skowrońska, A., Moerland, P. D., van Laar, J., Oldreive, C., Monsuur, H. N., Trbušek, M., Malčíková, J., et al. (2014) · Leukemia · doi:10.1038/leu.2014.318 · Cited by 86
Shkreta, L., Toutant, J., Durand, M., Manley, J. L., & Chabot, B. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.10.071 · Cited by 87
Yu, Z., Mersaoui, S. Y., Guitton-Sert, L., Coulombe, Y., Song, J., Masson, J., & Richard, S. (2020) · NAR Cancer · doi:10.1093/narcan/zcaa028 · Cited by 86
Naro, C., Bielli, P., Pagliarini, V., & Sette, C. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00142 · Cited by 84
Yan, Q., Zeng, P., Zhou, X., Zhao, X., Chen, R., Qiao, J., Ling, F., Zhu, Z., Zhang, G., & Chen, C. (2021) · Oncogene · doi:10.1038/s41388-021-01666-z · Cited by 86
Lang, F., Li, X., Zheng, W., Li, Z., Lu, D., Chen, G., Gong, D., Yang, L., Fu, J., Shi, P., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1704076114 · Cited by 83
Non‐coding RNAs in DNA damage and repair
Sharma, V., & Misteli, T. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.05.006 · Cited by 86
Elguindy, M. M., Kopp, F. B., Goodarzi, M., Rehfeld, F., Thomas, A. A., Chang, T.-C., & Mendell, J. T. (2019) · eLife · doi:10.7554/elife.48625 · Cited by 81
Wickramasinghe, V. O., Savill, J. M., Chavali, S., Jonsdottir, A. B., Rajendra, E., Grüner, T., Laskey, R. A., Babu, M. M., & Venkitaraman, A. R. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.031 · Cited by 80
Ke, Y., Han, Y., Guo, X., Wen, J., Wang, K., Jiang, X. Y., Tian, X., Ba, X., Boldogh, I. R., & Zeng, X. (2017) · Nature Communications · doi:10.1038/ncomms14632 · Cited by 84
Regulators of homologous recombination repair as novel targets for cancer treatment
Krajewska, M., Fehrmann, R. S. N., de Vries, E. G. E., & van Vugt, M. A. T. M. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00096 · Cited by 81
Poly-ADP ribosylation in DNA damage response and cancer therapy
Hou, W., Chen, S.-H., & Yu, X. (2017) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2017.09.004 · Cited by 82
Reshaping Chromatin after DNA Damage: The Choreography of Histone Proteins
Polo, S. E. (2014) · Journal of Molecular Biology · doi:10.1016/j.jmb.2014.05.025 · Cited by 84
A high‐throughput, flow cytometry‐based method to quantify DNA‐end resection in mammalian cells
Forment, J. V., Walker, R. V., & Jackson, S. P. (2012) · Cytometry Part A · doi:10.1002/cyto.a.22155 · Cited by 74
BRCA1 and CtIP suppress long-tract gene conversion between sister chromatids
Chandramouly, G., Kwok, A., Huang, B., Willis, N. A., Xie, A., & Scully, R. (2013) · Nature Communications · doi:10.1038/ncomms3404 · Cited by 70
Post-transcriptional control of gene expression following stress: the role of RNA-binding proteins
Harvey, R. F., Dezi, V., Pizzinga, M., & Willis, A. E. (2017) · Biochemical Society Transactions · doi:10.1042/bst20160364 · Cited by 77
DNA damage, chromatin, and transcription: the trinity of aging
Burgess, R. C., Misteli, T., & Oberdoerffer, P. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.07.005 · Cited by 72
Musiani, D., Giambruno, R., Massignani, E., Ippolito, M. R., Maniaci, M., Jammula, S., Manganaro, D., Cuomo, A., Nicosia, L., Pasini, D., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2019.12.061 · Cited by 73
Tumor protein D52 (TPD52) and cancer—oncogene understudy or understudied oncogene?
Byrne, J. A., Frost, S., Chen, Y., & Bright, R. K. (2014) · Tumor Biology · doi:10.1007/s13277-014-2006-x · Cited by 71
Chen, Y., Zhang, H., Xu, Z., Tang, H., Geng, A., Cai, B., Su, T., Shi, J., Jiang, C., Tian, X., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz592 · Cited by 75
Metadata
- Authors
- Adamson, B., Smogorzewska, A., Sigoillot, F. D., King, R. W., & Elledge, S. J.
- Affiliations
- Brigham and Women's Hospital (US)
- Harvard University (US)
- Corresponding author
- Elledge, Stephen J.
- Venue
- Nature Cell Biology
- Published
- 2012-02-19
- Volume
- 14
- Issue
- 3
- Pages
- 318-328
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- PMC
- PMC3290715
- OpenAlex
- W2052973047
- Cited by
- 433
- References
- 36
- Citations by year
- 2026: 10 · 2025: 19 · 2024: 25 · 2023: 34 · 2022: 28 · 2021: 43 · 2020: 40 · 2019: 33 · 2018: 30 · 2017: 30 · 2016: 30 · 2015: 33 · 2014: 34 · 2013: 35 · 2012: 8
- FWCI
- 14.15
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Cancer Institute (T32CA09216, T32CA009216)
- National Institute of General Medical Sciences (R37GM044664, R01GM044664)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Keywords
- homologous recombination, RBMX, DNA damage response, DNA double-strand break repair, siRNA screen, off-target effects, RAD51, PARP1, BRCA2, pre-mRNA processing, RNA-binding proteins, alternative splicing, heterogeneous nuclear ribonucleoproteins
- MeSH terms
- DNA Damage, DNA Repair, Humans, Microscopy, Fluorescence, Models, Genetic, Nuclear Proteins, Poly(ADP-ribose) Polymerases, RNA Precursors, Transcription Factors, Immunoblotting, Genome, Human, RNA-Binding Proteins, Cell Cycle Proteins, Reverse Transcriptase Polymerase Chain Reaction, BRCA2 Protein, Nuclear Pore Complex Proteins, Heterogeneous-Nuclear Ribonucleoproteins, RNA Interference, RNA, Small Interfering, Cell Line, Tumor, Green Fluorescent Proteins, Rad51 Recombinase, Gene Regulatory Networks, Histone Chaperones, Homologous Recombination
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review