The DOI matches its Crossref record; 37 of the 37 references it cites were found in a registry or an index.
Sensing DNA Damage Through ATRIP Recognition of RPA-ssDNA Complexes
Abstract
The function of the ATR (ataxia-telangiectasia mutated– and Rad3-related)–ATRIP (ATR-interacting protein) protein kinase complex is crucial for the cellular response to replication stress and DNA damage. Here, we show that replication protein A (RPA), a protein complex that associates with single-stranded DNA (ssDNA), is required for the recruitment of ATR to sites of DNA damage and for ATR-mediated Chk1 activation in human cells. In vitro, RPA stimulates the binding of ATRIP to ssDNA. The binding of ATRIP to RPA-coated ssDNA enables the ATR-ATRIP complex to associate with DNA and stimulates phosphorylation of the Rad17 protein that is bound to DNA. Furthermore, Ddc2, the budding yeast homolog of ATRIP, is specifically recruited to double-strand DNA breaks in an RPA-dependent manner. A checkpoint-deficient mutant of RPA, rfa1-t11 , is defective for recruiting Ddc2 to ssDNA both in vivo and in vitro. Our data suggest that RPA-coated ssDNA is the critical structure at sites of DNA damage that recruits the ATR-ATRIP complex and facilitates its recognition of substrates for phosphorylation and the initiation of checkpoint signaling.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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
“ATR in complex with its nuclear binding partner ATR-interacting protein (ATRIP) binds to this RPA-coated ssDNA via an ATRIP-RPA interaction. ATRIP also serves to activate the checkpoint kinase activity of ATR 4, 27–30.”
From Xeroderma Pigmentosa Group A (XPA), Nucleotide Excision Repair and Regulation by ATR in Response to Ultraviolet Irradiation (2017) · cites this paper as [29]
In the citing paper
“In addition, during S phase, replication forks encounter the CPD and 6-4PP lesions that provoke stalling of the replication forks at the single-strand breaks (SSBs).”
From ATR- and ATM-Mediated DNA Damage Response Is Dependent on Excision Repair Assembly during G1 but Not in S Phase of Cell Cycle (2016) · cites this paper as [18]
In the citing paper
“These breaks are processed to long ssDNA, where RPA binds and initiates the recruitment of a complex array of DNA damage response (DDR) proteins, including ATRIP-ATR complex, TopBP1, MRE11, Rad50, Rad17, and 9-1-1 complex [17–19].”
From ATR- and ATM-Mediated DNA Damage Response Is Dependent on Excision Repair Assembly during G1 but Not in S Phase of Cell Cycle (2016) · cites this paper as [18]
In the citing paper
“ATR is the primary sensor of single-stranded (ssDNA) breaks (SSB) caused by UV damage and replication stress.”
From NER initiation factors, DDB2 and XPC, regulate UV radiation response by recruiting ATR and ATM kinases to DNA damage sites (2013) · cites this paper as [16]
In the citing paper
“It has been shown that DNA damage and replication intermediates increase the unwinding of DNA, leading to the accumulation of RPA-coated ss-DNA, which recruits ATR [15, 16].”
From NER initiation factors, DDB2 and XPC, regulate UV radiation response by recruiting ATR and ATM kinases to DNA damage sites (2013) · cites this paper as [16]
In the citing paper
“It has been shown that in response to UV irradiation, RPA-coated single-stranded DNA (ssDNA) recruits ATR to the UV damage site [15, 16].”
From NER initiation factors, DDB2 and XPC, regulate UV radiation response by recruiting ATR and ATM kinases to DNA damage sites (2013) · cites this paper as [16]
In the citing paper
“Given the variety of DNA lesions the cell has to deal with, it was hypothesized that the first responders, among checkpoint factors, had to be recruited to a common DNA intermediate, which was later identified as long regions of ssDNA covered by RPA [44].”
From Mind the gap: keeping UV lesions in check (2011) · cites this paper as [44]
In the citing paper
“While ATRIP and Ddc2 directly bind RPA-covered ssDNA [44], loading of the 9-1-1 complex requires the activity of an RFC-like complex, that places it at the junction between dsDNA and 5′ ssDNA [45].”
From Mind the gap: keeping UV lesions in check (2011) · cites this paper as [44]
In the citing paper
“ATR-interacting protein ATRIP is recruited to ssDNA via direct interaction between RPA and ATRIP, thereby recruiting ATR to RPA-ssDNA [100, 101].”
From Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress (2014) · cites this paper as [100]
Citations
Cites
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
Self-citationCell cycle checkpoint signaling through the ATM and ATR kinases
Abraham, R. T. (2001) · Genes & Development · doi:10.1101/gad.914401 · Cited by 1,966
Wood, R., Mitchell, M., Sgouros, J., & Lindahl, T. (2001) · Science · doi:10.1126/science.1056154 · Cited by 1,719
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
Self-citationWold, M. S. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.61 · Cited by 1,445
ATR and ATRIP: Partners in Checkpoint Signaling
Cortez, D., Guntuku, S., Qin, J., & Elledge, S. J. (2001) · Science · doi:10.1126/science.1065521 · Cited by 985
Self-citationFork Reversal and ssDNA Accumulation at Stalled Replication Forks Owing to Checkpoint Defects
Sogo, J. M., Lopes, M., & Foiani, M. (2002) · Science · doi:10.1126/science.1074023 · Cited by 824
Loss of a yeast telomere: Arrest, recovery, and chromosome loss
Sandell, L. J. (1993) · Cell · doi:10.1016/0092-8674(93)90493-a · Cited by 792
Recombinant replication protein A: expression, complex formation, and functional characterization
Henricksen, L. A., Umbricht, C. B., & Wold, M. S. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)78100-9 · Cited by 597
Functional interactions between BRCA1 and the checkpoint kinase ATR during genotoxic stress
Tibbetts, R. S., Cortez, D., Brumbaugh, K. M., Scully, R., Livingston, D., Elledge, S. J., & Abraham, R. T. (2000) · Genes & Development · doi:10.1101/gad.851000 · Cited by 512
Self-citation
Flagged first, then by citations
Cited by
Sorted by citations
Items 401–500 of 1,014
Recruitment of the Cell Cycle Checkpoint Kinase ATR to Chromatin during S-phase
Dart, D. A., Adams, K. E., Akerman, I., & Lakin, N. D. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314212200 · Cited by 124
Yajima, H., Lee, K.-J., Zhang, S., Kobayashi, J., & Chen, B. P. C. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2008.11.036 · Cited by 124
ATM Acts Downstream of ATR in the DNA Damage Response Signaling of Bystander Cells
Burdak‐Rothkamm, S., Rothkamm, K., & Prise, K. M. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0545 · Cited by 124
Leung‐Pineda, V., Huh, J., & Piwnica-Worms, H. M. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-3382 · Cited by 130
Replication stress impairs chromosome segregation and preimplantation development in human embryos
Palmerola, K. L., Amrane, S., Angeles, A. D. L., Xu, S., Wang, N., de Pinho, J., Zuccaro, M. V., Taglialatela, A., Massey, D. J., Turocy, J. M., et al. (2022) · Cell · doi:10.1016/j.cell.2022.06.028 · Cited by 127
Drosophila ATM and ATR have distinct activities in the regulation of meiotic DNA damage and repair
Joyce, E. F., Pedersen, M., Tiong, S. Y. K., White-Brown, S. K., Paul, A., Campbell, S. D., & McKim, K. S. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201104121 · Cited by 132
A Maternal Functional Module in the Mammalian Oocyte-To-Embryo Transition
Lu, X., Gao, Z., Qin, D., & Li, L. (2017) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2017.09.004 · Cited by 123
Early events in the mammalian response to DNA double-strand breaks
Riches, L. C., Lynch, A. M., & Gooderham, N. J. (2008) · Mutagenesis · doi:10.1093/mutage/gen039 · Cited by 124
TopBP1 assembles nuclear condensates to switch on ATR signaling
Frattini, C., Promonet, A., Alghoul, E., Vidal-Eychenié, S., Lamarque, M., Blanchard, M., Urbach, S., Basbous, J., & Constantinou, A. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.12.049 · Cited by 126
O'Connell, B. C., Adamson, B., Lydeard, J. R., Sowa, M. E., Ciccia, A., Bredemeyer, A. L., Schlabach, M., Gygi, S. P., Elledge, S. J., & Harper, J. W. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.022 · Cited by 122
Self-citationYeast DNA replication protein Dpb11 activates the Mec1/ATR checkpoint kinase
Navadgi-Patil, V. M., & Burgers, P. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m807435200 · Cited by 121
Giannattasio, M., Follonier, C., Tourrière, H., Puddu, F., Lazzaro, F., Pasero, P., Lopes, M., Plevani, P., & Muzi-Falconi, M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.004 · Cited by 121
Dpb11 activates the Mec1-Ddc2 complex
Mordes, D. A., Nam, E. A., & Cortez, D. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806621105 · Cited by 121
Yang, G., Liu, C., Chen, S.-H., Kassab, M. A., Hoff, J. D., Walter, N. G., & Yu, X. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky088 · Cited by 129
The Initial Response of a Eukaryotic Replisome to DNA Damage
Taylor, M. R. G., & Yeeles, J. T. P. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.04.022 · Cited by 121
BRCA1 Is Required for Postreplication Repair after UV-Induced DNA Damage
Pathania, S., Nguyen, J., Hill, S. J., Scully, R., Adelmant, G., Marto, J. A., Feunteun, J., & Livingston, D. M. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.09.002 · Cited by 125
Nucleases Acting at Stalled Forks: How to Reboot the Replication Program with a Few Shortcuts
Pasero, P., & Vindigni, A. (2017) · Annual Review of Genetics · doi:10.1146/annurev-genet-120116-024745 · Cited by 130
UV stalled replication forks restart by re-priming in human fibroblasts
Elvers, I., Johansson, F., Groth, P., Erixon, K., & Helleday, T. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr420 · Cited by 124
Kemp, M. G., Akan, Z., Yilmaz, S., Grillo, M., Smith‐Roe, S. L., Kang, T., Cordeiro‐Stone, M., Kaufmann, W. K., Abraham, R. T., Sancar, A., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110304 · Cited by 129
Mutations in DONSON disrupt replication fork stability and cause microcephalic dwarfism
Reynolds, J. J., Bicknell, L. S., Carroll, P., Higgs, M. R., Shaheen, R., Murray, J., Papadopoulos, D. K., Leitch, A., Murina, O., Tarnauskaitė, Ž., et al. (2017) · Nature Genetics · doi:10.1038/ng.3790 · Cited by 123
Inactivating intracellular antiviral responses during adenovirus infection
Weitzman, M. D., & Ornelles, D. A. (2005) · Oncogene · doi:10.1038/sj.onc.1209063 · Cited by 123
Zimmerman, E. S., Chen, J., Andersen, J. L., Ardon, O., DeHart, J. L., Blackett, J. L., Choudhary, S. K., Camerini, D., Nghiem, P., & Planelles, V. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9286-9294.2004 · Cited by 124
Ha, K., Lee, G. E., Palii, S. S., Brown, K. D., Takeda, Y., Liu, K., Bhalla, K. N., & Robertson, K. D. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq451 · Cited by 127
Zhang, Y., Zhou, J., & Lim, C. U. (2006) · Cell Research · doi:10.1038/sj.cr.7310007 · Cited by 118
Choreography of recombination proteins during the DNA damage response
Lisby, M., & Rothstein, R. J. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.04.007 · Cited by 126
SMARCA4: Current status and future perspectives in non-small-cell lung cancer
Tian, Y., Xu, L., Li, X., Li, H., & Zhao, M. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.216022 · Cited by 123
Kanagaraj, R., Saydam, N., Garcia, P. L., Zheng, L., & Janščák, P. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl677 · Cited by 118
Yoo, H. Y., Kumagai, A., Shevchenko, A., Shevchenko, A., & Dunphy, W. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701770200 · Cited by 118
Mechanisms of Dealing with DNA Damage-Induced Replication Problems
Budzowska, M., & Kanaar, R. (2008) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-008-9039-y · Cited by 122
Dual role for Saccharomyces cerevisiae Tel1 in the checkpoint response to double‐strand breaks
Mantiero, D., Clerici, M., Lucchini, G., & Longhese, M. P. (2007) · EMBO Reports · doi:10.1038/sj.embor.7400911 · Cited by 118
Proximal tubule ATR regulates DNA repair to prevent maladaptive renal injury responses
Kishi, S., Brooks, C. R., Taguchi, K., Ichimura, T., Mori, Y., Akinfolarin, A., Gupta, N., Galichon, P., Elias, B. C., Suzuki, T., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci122313 · Cited by 117
Ogi, T., Walker, S., Stiff, T., Hobson, E., Limsirichaikul, S., Carpenter, G., Prescott, K., Suri, M., Byrd, P. J., Matsuse, M., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002945 · Cited by 120
Karp, J. E., Thomas, B. M., Greer, J. M., Sorge, C. L., Gore, S. D., Pratz, K. W., Smith, B. D., Flatten, K. S., Peterson, K., Schneider, P. A., et al. (2012) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-12-2442 · Cited by 117
Fanconi Anemia Signaling and Cancer
Nepal, M. K., Che, R., Zhang, J., Ma, C., & Fei, P. (2017) · Trends in cancer · doi:10.1016/j.trecan.2017.10.005 · Cited by 125
ATR, Claspin and the Rad9-Rad1-Hus1 Complex Regulate Chk1 and Cdc25A in the Absence of DNA Damage
Sørensen, C. S., Syljuåsen, R. G., Lukas, J., & Bártek, J. (2004) · Cell Cycle · doi:10.4161/cc.3.7.972 · Cited by 117
Plasticity of the Mre11–Rad50–Xrs2–Sae2 nuclease ensemble in the processing of DNA-bound obstaclesPreprint
Wang, W., Daley, J. M., Kwon, Y., Krasner, D. S., & Sung, P. (2017) · Genes & Development · doi:10.1101/gad.307900.117 · Cited by 121
ATM protein kinase: the linchpin of cellular defenses to stress
Bhatti, S., Kozlov, S., Farooqi, A. A., Naqi, A., Lavin, M., & Khanna, K. K. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0683-9 · Cited by 116
Leung, J. W. C., Ghosal, G., Wang, W., Shen, X. H., Wang, J., Li, L., & Chen, J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.411603 · Cited by 123
Assembly of checkpoint and repair machineries at DNA damage sites
Huen, M. S. Y., & Chen, J. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.09.001 · Cited by 118
Zhang, X., Succi, J., Feng, Z., Prithivirajsingh, S., Story, M. D., & Legerski, R. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.9207-9220.2004 · Cited by 119
Puddu, F., Granata, M., Di Nola, L., Balestrini, A., Piergiovanni, G., Lazzaro, F., Giannattasio, M., Plevani, P., & Muzi-Falconi, M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00330-08 · Cited by 115
Moreno, N. N., Olthof, A. M., & Svejstrup, J. Q. (2023) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052621-091205 · Cited by 119
DNA damage control: regulation and functions of checkpoint kinase 1
Smits, V. A. J., & Gillespie, D. A. (2015) · FEBS Journal · doi:10.1111/febs.13387 · Cited by 120
Zubko, M. K., Guillard, S., & Lydall, D. A. (2004) · Genetics · doi:10.1534/genetics.104.027904 · Cited by 118
Full-term Pregnancy Induces a Specific Genomic Signature in the Human Breast
Russo, J., Balogh, G., & Russo, I. H. (2008) · Cancer Epidemiology Biomarkers & Prevention · doi:10.1158/1055-9965.epi-07-0678 · Cited by 115
Vélez-Cruz, R., Manickavinayaham, S., Biswas, A., Clary, R. W., Premkumar, T., Cole, F., & Johnson, D. G. (2016) · Genes & Development · doi:10.1101/gad.288282.116 · Cited by 122
DNA nucleotide excision repair-dependent signaling to checkpoint activation
Marini, F., Nardo, T., Giannattasio, M., Minuzzo, M., Stefanini, M., Plevani, P., & Falconi, M. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0605446103 · Cited by 114
RPA and ATR link transcriptional stress to p53
Derheimer, F. A., O’Hagan, H. M., Krueger, H., Hanasoge, S., Paulsen, M. T., & Ljungman, M. E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705317104 · Cited by 119
Li, L., & Zou, L. (2004) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20355 · Cited by 117
Self-citationPhysical and functional interactions between nucleotide excision repair and DNA damage checkpoint
Giannattasio, M., Lazzaro, F., Longhese, M. P., Plevani, P., & Muzi‐Falconi, M. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600051 · Cited by 113
Wu, X., Shell, S. M., & Zou, Y. (2005) · Oncogene · doi:10.1038/sj.onc.1208674 · Cited by 113
Requirement of the Mre11 complex and exonuclease 1 for activation of the Mec1 signaling pathway
Nakada, D., Hirano, Y., & Sugimoto, K. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.22.10016-10025.2004 · Cited by 113
Dealing with DNA damage: Relationships between checkpoint and repair pathways
Warmerdam, D. O., & Kanaar, R. (2009) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2009.12.001 · Cited by 122
Common Chemical Inductors of Replication Stress: Focus on Cell‐Based Studies
Veselá, E., Chromá, K., Turi, Z., & Mistrík, M. (2017) · Biomolecules · doi:10.3390/biom7010019 · Cited by 128
The Retinoblastoma (RB) Tumor Suppressor: Pushing Back against Genome Instability on Multiple Fronts
Vélez-Cruz, R., & Johnson, D. G. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18081776 · Cited by 121
Dpb11 coordinates Mec1 kinase activation with cell cycle‐regulated Rad9 recruitment
Pfander, B., & Diffley, J. F. X. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.345 · Cited by 120
Human single-stranded DNA binding proteins are essential for maintaining genomic stability
Ashton, N. W., Bolderson, E., Cubeddu, L., O'Byrne, K. J., & Richard, D. J. (2013) · BMC Molecular Biology · doi:10.1186/1471-2199-14-9 · Cited by 118
HIV-1 Vpr: Mechanisms of G2 arrest and apoptosis
Andersen, J. L., Rouzic, E. L., & Planelles, V. (2008) · Experimental and Molecular Pathology · doi:10.1016/j.yexmp.2008.03.015 · Cited by 120
MCM8-9 complex promotes resection of double-strand break ends by MRE11-RAD50-NBS1 complex
Lee, K. Y., Im, J.-S., Shibata, E., Park, J.-H., Handa, N., Kowalczykowski, S. C., & Dutta, A. (2015) · Nature Communications · doi:10.1038/ncomms8744 · Cited by 116
Serrano, M. A., Li, Z., Dangeti, M., Musich, P. R., Patrick, S., Roginskaya, M., Cartwright, B., & Zou, Y. (2012) · Oncogene · doi:10.1038/onc.2012.257 · Cited by 124
The Intra-S Checkpoint Responses to DNA Damage
Iyer, D., & Rhind, N. (2017) · Genes · doi:10.3390/genes8020074 · Cited by 131
Deciphering UV‐induced DNA Damage Responses to Prevent and Treat Skin Cancer
Lee, J. W., Ratnakumar, K., Hung, K., Rokunohe, D., & Kawasumi, M. (2020) · Photochemistry and Photobiology · doi:10.1111/php.13245 · Cited by 121
HCLK2 is essential for the mammalian S-phase checkpoint and impacts on Chk1 stability
Collis, S. J., Barber, L. J., Clark, A. J., Martin, J. S., Ward, J. D., & Boulton, S. J. (2007) · Nature Cell Biology · doi:10.1038/ncb1555 · Cited by 112
Cellular Functions of Human RPA1
Haring, S. J., Mason, A. C., Binz, S. K., & Wold, M. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m800881200 · Cited by 112
Identification of SMARCAL1 as a Component of the DNA Damage Response
Postow, L., Woo, E. M., Chait, B. T., & Funabiki, H. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.048330 · Cited by 112
Johnson, N., & Shapiro, G. I. (2010) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2010.525221 · Cited by 113
γH2Ax: Biomarker of Damage or Functional Participant in DNA Repair “All that Glitters Is not Gold!”
Cleaver, J. E. (2011) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.2011.00995.x · Cited by 112
Mcm10 Plays a Role in Functioning of the Eukaryotic Replicative DNA Helicase, Cdc45-Mcm-GINS
Watase, G. J., Takisawa, H., & Kanemaki, M. T. (2012) · Current Biology · doi:10.1016/j.cub.2012.01.023 · Cited by 111
Cyclin‐dependent kinase 9–cyclin K functions in the replication stress response
Yu, D. S., Zhao, R., Hsu, E., Cayer, J., Ye, F., Guo, Y. P., Shyr, Y., & Cortez, D. (2010) · EMBO Reports · doi:10.1038/embor.2010.153 · Cited by 114
CARM1 regulates replication fork speed and stress response by stimulating PARP1
Genois, M., Gagné, J., Yasuhara, T., Jackson, J., Saxena, S., Langelier, M.-F., Ahel, I., Bedford, M. T., Pascal, J. M., Vindigni, A., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2020.12.010 · Cited by 114
Self-citationMRE11-RAD50-NBS1 Complex Dictates DNA Repair Independent of H2AX
Yuan, J., & Chen, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.078436 · Cited by 117
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
Docking onto chromatin via the Saccharomyces cerevisiae Rad9 Tudor domain
Grenon, M., Costelloe, T., Jimeno, S., O'Shaughnessy, A. M., Fitzgerald, J., Zgheib, O., Degerth, L., & Lowndes, N. F. (2007) · Yeast · doi:10.1002/yea.1441 · Cited by 110
The FANCM family of DNA helicases/translocases
Whitby, M. C. (2010) · DNA repair · doi:10.1016/j.dnarep.2009.12.012 · Cited by 109
Targeting Hypoxic Cells through the DNA Damage Response
Olcina, M. M., Lecane, P. S., & Hammond, E. M. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-0286 · Cited by 112
Block, W. D. (2004) · Nucleic Acids Research · doi:10.1093/nar/gkh265 · Cited by 115
Lopes, M., Cotta‐Ramusino, C., Liberi, G., & Foiani, M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00473-8 · Cited by 109
Doksani, Y., Bermejo, R., Fiorani, S., Haber, J. E., & Foiani, M. (2009) · Cell · doi:10.1016/j.cell.2009.02.016 · Cited by 114
Joshi, N., Brown, M. S., Bishop, D. K., & Börner, G. V. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.027 · Cited by 108
Mechanisms and regulation of DNA end resection
Longhese, M. P., Bonetti, D., Manfrini, N., & Clerici, M. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.165 · Cited by 117
Life or Death after a Break: What Determines the Choice?
Krenning, L., van den Berg, J., & Medema, R. H. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.08.023 · Cited by 113
Inhibitors of the Proteasome Suppress Homologous DNA Recombination in Mammalian Cells
Murakawa, Y., Sonoda, E., Barber, L. J., Zeng, W., Yokomori, K., Kimurâ, H., Niimi, A., Lehmann, A. R., Zhao, G., Hochegger, H., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1166 · Cited by 108
TopBP1 and DNA polymerase-α directly recruit the 9-1-1 complex to stalled DNA replication forks
Yan, S., & Michael, W. M. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200810185 · Cited by 107
Methods for Studying the DNA Damage Response in the Caenorhabdatis elegans Germ Line
Craig, A. L., Moser, S. C., Bailly, A., & Gartner, A. (2012) · Methods in cell biology · doi:10.1016/b978-0-12-394620-1.00011-4 · Cited by 107
DNA double strand break repair, chromosome synapsis and transcriptional silencing in meiosis
Inagaki, A., Schoenmakers, S., & Baarends, W. M. (2010) · Epigenetics · doi:10.4161/epi.5.4.11518 · Cited by 110
ATRIP associates with replication protein A-coated ssDNA through multiple interactions
Namiki, Y., & Zou, L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510223103 · Cited by 111
Self-citationKumar, S., & Burgers, P. (2013) · Genes & Development · doi:10.1101/gad.204750.112 · Cited by 114
Mre11 Assembles Linear DNA Fragments into DNA Damage Signaling Complexes
Costanzo, V., Paull, T., Gottesman, M., & Gautier, J. (2004) · PLoS Biology · doi:10.1371/journal.pbio.0020110 · Cited by 106
Campos, A., & Clemente‐Blanco, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21020446 · Cited by 114
Shelterin-Like Proteins and Yku Inhibit Nucleolytic Processing of Saccharomyces cerevisiae Telomeres
Bonetti, D., Clerici, M., Anbalagan, S., Martina, M., Lucchini, G., & Longhese, M. P. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000966 · Cited by 106
Richard, D. J., Bolderson, E., & Khanna, K. K. (2009) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230902849180 · Cited by 108
Targeting DNA repair in cancer: current state and novel approaches
Klinakis, A., Karagiannis, D., & Rampias, T. N. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03299-8 · Cited by 108
Following the Path of the Virus: The Exploitation of Host DNA Repair Mechanisms by Retroviruses
Smith, J. A., & Daniel, R. (2006) · ACS Chemical Biology · doi:10.1021/cb600131q · Cited by 113
Human UPF1 interacts with TPP1 and telomerase and sustains telomere leading‐strand replication
Chawla, R., Redon, S., Raftopoulou, C., Wischnewski, H., Gagos, S., & Azzalin, C. M. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.280 · Cited by 112
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
A consensus set of genetic vulnerabilities to ATR inhibition
Hustedt, N., Álvarez-Quilón, A., McEwan, A., Yuan, J. Y., Cho, T., Koob, L., Hart, T., & Durocher, D. (2019) · Open Biology · doi:10.1098/rsob.190156 · Cited by 107
Cryo-EM structure of human ATR-ATRIP complex
Rao, Q., Liu, M., Tian, Y., Wu, Z., Hao, Y., Song, L., Qin, Z., Ding, C., Wang, H., Wang, J., et al. (2017) · Cell Research · doi:10.1038/cr.2017.158 · Cited by 106
The DNA damage response during mitosis
Heijink, A. M., Krajewska, M., & van Vugt, M. A. T. M. (2013) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2013.07.003 · Cited by 107
The MRE11 GAR motif regulates DNA double-strand break processing and ATR activation
Yu, Z., Vogel, G., Coulombe, Y., Dubeau, D., Spehalski, E. I., Hébert, J., Ferguson, D. O., Masson, J., & Richard, S. (2011) · Cell Research · doi:10.1038/cr.2011.128 · Cited by 107
Loo, Y., & Melendy, T. (2004) · Journal of Virology · doi:10.1128/jvi.78.4.1605-1615.2004 · Cited by 104
Metadata
- Authors
- Zou, L., & Elledge, S. J.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Elledge, Stephen J.
- Venue
- Science
- Published
- 2003-06-06
- Volume
- 300
- Issue
- 5625
- Pages
- 1542-1548
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2043895957
- Cited by
- 2,693
- References
- 37
- Citations by year
- 2026: 64 · 2025: 65 · 2024: 114 · 2023: 98 · 2022: 112 · 2021: 136 · 2020: 111 · 2019: 116 · 2018: 106 · 2017: 114 · 2016: 130 · 2015: 139 · 2014: 117 · 2013: 144 · 2012: 121
- FWCI
- 41.94
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM-44664)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- replication protein A, single-stranded DNA, DNA damage recognition, DNA damage checkpoint, Chk1 activation, DNA double-strand breaks, replication stress
- MeSH terms
- Checkpoint Kinase 1, Cell Nucleus, DNA Damage, DNA Repair, DNA Replication, DNA-Binding Proteins, DNA, Fungal, DNA, Single-Stranded, Enzyme Activation, Exodeoxyribonucleases, HeLa Cells, Humans, Mutation, Phosphoproteins, Phosphorylation, Protein Binding, Protein Kinases, Radiation, Ionizing, Recombination, Genetic, Saccharomyces cerevisiae, Transcription Factors, Transfection, Tumor Cells, Cultured, Ultraviolet Rays, Signal Transduction, Protein Serine-Threonine Kinases, Cell Cycle Proteins, Saccharomyces cerevisiae Proteins, RNA, Small Interfering, Adaptor Proteins, Signal Transducing, Replication Protein A, Ataxia Telangiectasia Mutated Proteins
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
