More than just a focus: The chromatin response to DNA damage and its role in genome integrity maintenance
Abstract
Following the discovery in 1998 of γ-H2AX, the first histone modification induced by DNA damage, interest in the changes to chromatin induced by DNA damage has exploded, and a vast amount of information has been generated. However, there has been a discrepancy between our rapidly advancing knowledge of how chromatin responds to DNA damage and the understanding of why cells mobilize large segments of chromatin to protect the genome against destabilizing effects posed by tiny DNA lesions. Recent research has provided insights into these issues and suggests that chromatin responses induced by DNA damage are not simply the accumulation of 'nuclear foci' but are mechanisms required to guard genome integrity.
Integrity signals
Registry
Cites
Statistics
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?
Failure of the DDR to properly repair DNA results in accumulation of DNA damage and subsequently cellular senescence.
“Failure of the DDR to properly repair DNA results in the accumulation of DNA damage and subsequently cellular senescence, and as such it plays a crucial role in maintaining the genomic integrity and cellular function [92, 121, 168].”
From DNA repair deficiency and senescence in concussed professional athletes involved in contact sports (2019) · cites this paper as [92]
Cites
1 retracted
RETRACTED: DNA Damage, Homology-Directed Repair, and DNA Methylation
Cuozzo, C., Porcellini, A., Angrisano, T., Morano, A., Lee, B., Pardo, A. D., Messina, S., Iuliano, R., Fusco, A., Santillo, M. R., et al. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030110 · Cited by 190 · see citing works
RetractedGlioma stem cells promote radioresistance by preferential activation of the DNA damage response
Bao, S., Wu, Q., McLendon, R. E., Hao, Y., Shi, Q., Hjelmeland, A. B., Dewhirst, M. W., Bigner, D. D., & Rich, J. N. (2006) · Nature · doi:10.1038/nature05236 · Cited by 6,397 · see citing works
DNA double-stranded breaks induce histone H2AX phosphorylation on serine 139
Rogakou, E. P., Pilch, D. R., Orr, A. H., Ivanova, V. S., & Bonner, W. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.10.5858 · Cited by 5,438 · see citing works
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 · see citing works
Inhibition of Poly(ADP-Ribose) Polymerase in Tumors from <i>BRCA</i> Mutation Carriers
Fong, P. C., Boss, D. S., Yap, T. A., Tutt, A., Wu, P., Mergui-Roelvink, M., Mortimer, P., Swaisland, H., Lau, A., O'Connor, M. J., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0900212 · Cited by 3,634 · see citing works
ATM 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 · see citing works
53BP1 Inhibits Homologous Recombination in Brca1-Deficient Cells by Blocking Resection of DNA Breaks
Bunting, S. F., Callén, E., Wong, N., Chen, H.-T., Polato, F., Gunn, A., Bothmer, A., Feldhahn, N., Fernandez-Capetillo, O., Cao, L., et al. (2010) · Cell · doi:10.1016/j.cell.2010.03.012 · Cited by 1,671 · see citing works
A guide to super-resolution fluorescence microscopy
Schermelleh, L., Heintzmann, R., & Leonhardt, H. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201002018 · Cited by 1,258 · 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
Bouwman, P., Aly, A., Escandell, J. M., Pieterse, M., Bartkova, J., van der Gulden, H., Hiddingh, S., Thanasoula, M., Kulkarni, A., Yang, Q., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1831 · Cited by 1,001 · see citing works
Botuyan, M. V., Lee, J., Ward, I. M., Kim, J., Thompson, J. R., Chen, J., & Mer, G. (2006) · Cell · doi:10.1016/j.cell.2006.10.043 · Cited by 973 · see citing works
Systematic Protein Location Mapping Reveals Five Principal Chromatin Types in Drosophila Cells
Filion, G. J. P., van Bemmel, J. G., Braunschweig, U., Talhout, W., Kind, J., Ward, L. D., Brugman, W., de Castro, I. J., Kerkhoven, R. M., Bussemaker, H. J., et al. (2010) · Cell · doi:10.1016/j.cell.2010.09.009 · Cited by 963 · see citing works
Doil, C., Mailand, N., Bekker‐Jensen, S., Ménard, P., Larsen, D. H., Pepperkok, R., Ellenberg, J., Panier, S., Durocher, D., Bártek, J., et al. (2009) · Cell · doi:10.1016/j.cell.2008.12.041 · Cited by 938 · see citing works
Self-citationMethylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
Huyen, Y., Zgheib, O., DiTullio Jr, R. A., Gorgoulis, V. G., Zacharatos, P., Petty, T. J., Sheston, E. A., Mellert, H. S., Stavridi, E. S., & Halazonetis, T. D. (2004) · Nature · doi:10.1038/nature03114 · Cited by 884 · see citing works
The PARP Side of the Nucleus: Molecular Actions, Physiological Outcomes, and Clinical Targets
Krishnakumar, R., & Kraus, W. L. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.017 · Cited by 836 · see citing works
The RIDDLE Syndrome Protein Mediates a Ubiquitin-Dependent Signaling Cascade at Sites of DNA Damage
Stewart, G. S., Panier, S., Townsend, K., Al-Hakim, A., Kolas, N. K., Miller, E. S., Nakada, S., Ylanko, J., Olivarius, S., Mendez, M., et al. (2009) · Cell · doi:10.1016/j.cell.2008.12.042 · Cited by 759 · 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
Chromatin Challenges during DNA Replication and Repair
Groth, A., Rocha, W., Verreault, A., & Almouzni, G. (2007) · Cell · doi:10.1016/j.cell.2007.01.030 · Cited by 733 · see citing works
Lukas, C., Savic, V., Bekker‐Jensen, S., Doil, C., Neumann, B., Pedersen, R. S., Grøfte, M., Chan, K., Hickson, I. D., Bártek, J., et al. (2011) · Nature Cell Biology · doi:10.1038/ncb2201 · Cited by 658 · see citing works
Self-citationHuman HDAC1 and HDAC2 function in the DNA-damage response to promote DNA nonhomologous end-joining
Miller, K. M., Tjeertes, J. V., Coates, J., Legube, G., Polo, S. E., Britton, S., & Jackson, S. P. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1899 · Cited by 629 · see citing works
Replication stress induces sister-chromatid bridging at fragile site loci in mitosis
Chan, K., Palmai‐Pallag, T., Ying, S., & Hickson, I. D. (2009) · Nature Cell Biology · doi:10.1038/ncb1882 · Cited by 614 · see citing works
Poly(ADP-ribose)–Dependent Regulation of DNA Repair by the Chromatin Remodeling Enzyme ALC1
Ahel, D., Hořejší, Z., Wiechens, N., Polo, S. E., Garcia-Wilson, E., Ahel, I., Flynn, H., Skehel, M., West, S. C., Jackson, S. P., et al. (2009) · Science · doi:10.1126/science.1177321 · Cited by 588 · see citing works
CtIP-BRCA1 modulates the choice of DNA double-strand-break repair pathway throughout the cell cycle
Yun, M. H., & Hiom, K. (2009) · Nature · doi:10.1038/nature07955 · Cited by 556 · see citing works
Tyrosine dephosphorylation of H2AX modulates apoptosis and survival decisions
Cook, P. J., Ju, B. G., Telese, F., Wang, X., Glass, C. K., & Rosenfeld, M. G. (2009) · Nature · doi:10.1038/nature07849 · Cited by 534 · see citing works
Chou, D. M., Adamson, B., Dephoure, N. E., Tan, X., Nottke, A. C., Hurov, K. E., Gygi, S. P., Colaiácovo, M. P., & Elledge, S. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012946107 · Cited by 529 · see citing works
Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks
Galanty, Y., Belotserkovskaya, R., Coates, J., Polo, S. E., Miller, K. M., & Jackson, S. P. (2009) · Nature · doi:10.1038/nature08657 · Cited by 523 · see citing works
Chiolo, I., Minoda, A., Colmenares, S. U., Polyzos, A. A., Costes, S. V., & Karpen, G. H. (2011) · Cell · doi:10.1016/j.cell.2011.02.012 · Cited by 516 · see citing works
High‐resolution profiling of γH2AX around DNA double strand breaks in the mammalian genome
Iacovoni, J. S., Caron, P., Lassadi, I., Nicolas, E., Massip, L., Trouche, D., & Legube, G. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.38 · Cited by 515 · see citing works
Positional stability of single double-strand breaks in mammalian cells
Soutoglou, E., Dorn, J. F., Sengupta, K., Jasin, M., Nussenzweig, A., Ried, T., Danuser, G., & Misteli, T. (2007) · Nature Cell Biology · doi:10.1038/ncb1591 · Cited by 515 · see citing works
Roles of ATM and NBS1 in chromatin structure modulation and DNA double-strand break repair
Berkovich, E., Monnat, R. J., & Kastan, M. B. (2007) · Nature Cell Biology · doi:10.1038/ncb1599 · Cited by 477 · see citing works
Histone H3 methylation links DNA damage detection to activation of the tumour suppressor Tip60
Sun, Y., Jiang, X., Xu, Y., Ayrapetov, M. K., Moreau, L. A., Whetstine, J. R., & Price, B. D. (2009) · Nature Cell Biology · doi:10.1038/ncb1982 · Cited by 454 · see citing works
Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction
Fierz, B., Chatterjee, C., McGinty, R. K., Bar‐Dagan, M., Raleigh, D. P., & Muir, T. W. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.501 · Cited by 435 · see citing works
The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress
Morris, J. R., Boutell, C., Epple, M., Densham, R. M., Weekes, D. B., Alamshah, A., Butler, L. R., Galanty, Y., Pangon, L., Kiuchi, T., et al. (2009) · Nature · doi:10.1038/nature08593 · Cited by 434 · see citing works
Poly(ADP-ribose)-binding zinc finger motifs in DNA repair/checkpoint proteins
Ahel, I., Ahel, D., Matsusaka, T., Clark, A. J., Pines, J., Boulton, S. J., & West, S. C. (2008) · Nature · doi:10.1038/nature06420 · Cited by 429 · see citing works
Cell-type-specific replication initiation programs set fragility of the FRA3B fragile site
Letessier, A., Millot, G. A., Koundrioukoff, S., Lachagès, A.-M., Vogt, N., Hansen, R. S., Malfoy, B., Brison, O., & Debatisse, M. (2011) · Nature · doi:10.1038/nature09745 · Cited by 426 · see citing works
WSTF regulates the H2A.X DNA damage response via a novel tyrosine kinase activity
Xiao, A., Li, H., Shechter, D., Ahn, S. H., Fabrizio, L. A., Erdjument‐Bromage, H., Ishibe-Murakami, S., Wang, B., Tempst, P., Hofmann, K., et al. (2008) · Nature · doi:10.1038/nature07668 · Cited by 417 · see citing works
MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites
Pei, H., Zhang, L. M., Luo, K., Qin, Y., Chesi, M., Fei, Y. F., Bergsagel, P. L., Wang, L., You, Z., & Lou, Z. (2011) · Nature · doi:10.1038/nature09658 · Cited by 410 · see citing works
HP1-β mobilization promotes chromatin changes that initiate the DNA damage response
Ayoub, N., Jeyasekharan, A. D. D., Bernal, J. A., & Venkitaraman, A. R. (2008) · Nature · doi:10.1038/nature06875 · Cited by 404 · see citing works
Moyal, L., Lerenthal, Y., Gana‐Weisz, M., Mass, G., So, S., Wang, S., Eppink, B., Chung, Y. M., Shalev, G., Shema, E., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.015 · Cited by 402 · see citing works
O'Hagan, H. M., Mohammad, H. P., & Baylin, S. B. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000155 · Cited by 386 · see citing works
Torres‐Rosell, J., Šunjevarić, I., Piccoli, G. D., Sacher, M., Eckert‐Boulet, N., Reid, R. J. D., Jentsch, S., Rothstein, R. J., Aragón, L., & Lisby, M. (2007) · Nature Cell Biology · doi:10.1038/ncb1619 · Cited by 379 · see citing works
DNA Damage-Dependent Acetylation and Ubiquitination of H2AX Enhances Chromatin Dynamics
Ikura, T., Tashiro, S., Kakino, A., Shima, H., Jacob, N. K., Amunugama, R., Yoder, K. E., Izumi, S., Kuraoka, I., Tanaka, K., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00579-07 · Cited by 376 · see citing works
Polo, S. E., Kaidi, A., Baskcomb, L., Galanty, Y., & Jackson, S. P. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.188 · Cited by 374 · cited 1× · see citing works
“Although binding to PAR chains seems to recruit these complexes to DNA break”
BackgroundPoly(ADP-ribosyl)ation directs recruitment and activation of an ATP-dependent chromatin remodeler
Gottschalk, A. J., Timinszky, G., Kong, S. E., Jin, J., Cai, Y., Swanson, S. K., Washburn, M. P., Florens, L. A., Ladurner, A. G., Conaway, J. W., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906920106 · Cited by 358 · see citing works
Non-canonical inhibition of DNA damage-dependent ubiquitination by OTUB1
Nakada, S., Tai, I., Panier, S., Al-Hakim, A., Iemura, S.-I., Juang, Y.-C., O’Donnell, L., Kumakubo, A., Munro, M., Sicheri, F., et al. (2010) · Nature · doi:10.1038/nature09297 · Cited by 357 · see citing works
Regulation of Homologous Recombination by RNF20-Dependent H2B Ubiquitination
Nakamura, K., Kato, A., Kobayashi, J., Yanagihara, H., Sakamoto, S., Oliveira, D. V. N. P., Shimada, M., Tauchi, H., Suzuki, H., Tashiro, S., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.002 · Cited by 351 · see citing works
Replication stress induces 53BP1-containing OPT domains in G1 cells
Harrigan, J. A., Belotserkovskaya, R., Coates, J., Dimitrova, D. S., Polo, S. E., Bradshaw, C. R., Fraser, P., & Jackson, S. P. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201011083 · Cited by 344 · see citing works
PARP-3 and APLF Function Together to Accelerate Nonhomologous End-Joining
Rulten, S. L., Fisher, A. E. O., Robert, I., Zuma, M. C., Rouleau, M., Ju, L., Poirier, G. G., Reina‐San‐Martin, B., & Caldecott, K. W. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.006 · Cited by 326 · see citing works
RAD18 transmits DNA damage signalling to elicit homologous recombination repair
Huang, J., Huen, M. S. Y., Kim, H., Leung, C. C. Y., Glover, J. N. M., Yu, X., & Chen, J. (2009) · Nature Cell Biology · doi:10.1038/ncb1865 · Cited by 309 · see citing works
Cao, L., Xu, X., Bunting, S. F., Liu, J., Wang, R.-H., Cao, L. L., Wu, J. J., Peng, T.-N., Chen, J., Nussenzweig, A., et al. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.06.037 · Cited by 308 · see citing works
Goodarzi, A. A., Jeggo, P., & Lobrich, M. (2010) · DNA Repair · doi:10.1016/j.dnarep.2010.09.013 · Cited by 305 · see citing works
Epigenetic Instability due to Defective Replication of Structured DNA
Sarkies, P., Reams, C., Simpson, L. J., & Sale, J. E. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.009 · Cited by 302 · see citing works
Bothmer, A., Robbiani, D. F., Feldhahn, N., Gazumyan, A., Nussenzweig, A., & Nussenzweig, M. C. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20100244 · Cited by 283 · see citing works
Replication Stress Interferes with Histone Recycling and Predeposition Marking of New Histones
Jasencakova, Z., Scharf, A. N. D., Ask, K., Corpet, A., Imhof, A., Almouzni, G., & Groth, A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.033 · Cited by 279 · see citing works
HERC2 coordinates ubiquitin-dependent assembly of DNA repair factors on damaged chromosomes
Bekker‐Jensen, S., Danielsen, J. M. R., Fugger, K., Gromova, I., Nerstedt, A., Lukas, C., Bártek, J., Lukas, J., & Mailand, N. (2009) · Nature Cell Biology · doi:10.1038/ncb2008 · Cited by 277 · see citing works
Self-citationFacchino, S., Abdouh, M., Chatoo, W., & Bernier, G. (2010) · Journal of Neuroscience · doi:10.1523/jneurosci.1634-10.2010 · Cited by 275 · see citing works
BMI1-mediated histone ubiquitylation promotes DNA double-strand break repair
Ismail, I. H., Andrin, C., McDonald, D., & Hendzel, M. J. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201003034 · Cited by 270 · see citing works
PARP1 ADP-ribosylates lysine residues of the core histone tails
Messner, S., Altmeyer, M., Zhao, H., Pozivil, A., Roschitzki, B., Gehrig, P., Rutishauser, D., Danzhi Huang, A., Caflisch, A., & Hottiger, M. O. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq463 · Cited by 264 · see citing works
Heterochromatin protein 1 is recruited to various types of DNA damage
Luijsterburg, M. S., Dinant, C., Lans, H., Stap, J., Wiernasz, E., Lagerwerf, S., Warmerdam, D. O., Lindh, M., Brink, M. C., Dobrucki, J. W., et al. (2009) · Journal of Cell Biology · doi:10.1083/jcb.200810035 · Cited by 264 · see citing works
Heterochromatin is refractory to γ-H2AX modification in yeast and mammals
Kim, J., Kruhlak, M. J., Dotiwala, F., Nussenzweig, A., & Haber, J. E. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200612031 · Cited by 260 · see citing works
Goodarzi, A. A., Kurka, T., & Jeggo, P. A. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2077 · Cited by 255 · see citing works
DNA damage triggers nucleotide excision repair-dependent monoubiquitylation of histone H2APreprint
Bergink, S., Salomons, F. A., Hoogstraten, D., Groothuis, T. A., de Waard, H., Wu, J., Li, Y., Citterio, E., Houtsmuller, A. B., Neefjes, J., et al. (2006) · Genes & Development · doi:10.1101/gad.373706 · Cited by 247 · see citing works
Oda, H., Hübner, M. R., Beck, D. B., Vermeulen, M., Hurwitz, J., Spector, D. L., & Reinberg, D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.011 · Cited by 246 · see citing works
Regulation of DNA End Joining, Resection, and Immunoglobulin Class Switch Recombination by 53BP1
Bothmer, A., Robbiani, D. F., Di Virgilio, M., Bunting, S. F., Klein, I. A., Feldhahn, N., Barlow, J., Chen, H.-T., Bosque, D., Callen, E., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.019 · Cited by 244 · see citing works
The NuRD chromatin–remodeling complex regulates signaling and repair of DNA damage
Smeenk, G., Wiegant, W. W., Vrolijk, H., Solari, A. P., Pastink, A., & van Attikum, H. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201001048 · Cited by 243 · see citing works
The chromatin-remodeling factor CHD4 coordinates signaling and repair after DNA damage
Larsen, D. H., Poinsignon, C., Guðjόnsson, Þ., Dinant, C., Payne, M., Hari, F. J., Danielsen, J. M. R., Ménard, P., Sand, J. C., Stucki, M., et al. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.200912135 · Cited by 240 · see citing works
Self-citationGlobal chromatin compaction limits the strength of the DNA damage response
Murga, M., Jaco, I., Fan, Y., Soria, R., Martínez-Pastor, B., Cuadrado, M., Yang, S.-M., Blasco, M. A., Skoultchi, A. I., & Fernández-Capetillo, Ó. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200704140 · Cited by 236 · see citing works
Hu, Y., Scully, R., Sobhian, B., Xie, A., Shestakova, E. A., & Livingston, D. M. (2011) · Genes & Development · doi:10.1101/gad.2011011 · Cited by 232 · see citing works
The BRCA1-RAP80 Complex Regulates DNA Repair Mechanism Utilization by Restricting End Resection
Coleman, K. A., & Greenberg, R. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.213728 · Cited by 224 · see citing works
Shao, G., Lilli, D. R., Patterson-Fortin, J., Coleman, K. A., Morrissey, D. E., & Greenberg, R. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807485106 · Cited by 218 · see citing works
ATM damage response and XLF repair factor are functionally redundant in joining DNA breaks
Zha, S., Guo, C., Boboilă, C., Oksenych, V., Cheng, H.-L., Zhang, Y., Wesemann, D. R., Yuen, G. J., Patel, H., Goff, P. H., et al. (2010) · Nature · doi:10.1038/nature09604 · Cited by 209 · see citing works
Savic, V., Yin, B., Maas, N. L., Bredemeyer, A. L., Carpenter, A. C., Helmink, B. A., Yang-Iott, K. S., Sleckman, B. P., & Bassing, C. H. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.012 · Cited by 204 · see citing works
HP1α recruitment to DNA damage by p150CAF-1 promotes homologous recombination repair
Baldeyron, C., Soria, G., Roche, D., Cook, A. J. L., & Almouzni, G. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201101030 · Cited by 200 · see citing works
The p400 ATPase regulates nucleosome stability and chromatin ubiquitination during DNA repair
Xu, Y., Sun, Y., Jiang, X., Ayrapetov, M. K., Moskwa, P., Yang, S., Weinstock, D. M., & Price, B. D. (2010) · Journal of Cell Biology · doi:10.1083/jcb.201001160 · Cited by 194 · see citing works
MDC1 directs chromosome-wide silencing of the sex chromosomes in male germ cellsPreprint
Ichijima, Y., Ichijima, M., Lou, Z., Nussenzweig, A., Camerini‐Otero, R. D., Chen, J., Andreassen, P. R., & Namekawa, S. H. (2011) · Genes & Development · doi:10.1101/gad.2030811 · Cited by 192 · see citing works
Lazzaro, F., Sapountzi, V., Granata, M., Pellicioli, A., Vaze, M. B., Haber, J. E., Plevani, P., Lydall, D. A., & Muzi-Falconi, M. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.81 · Cited by 190 · see citing works
BRIT1/MCPH1 links chromatin remodelling to DNA damage response
Peng, G., Yim, E.-K., Dai, H., Jackson, A. P., van der Burgt, I., Pan, M., Hu, R., Li, K., & Lin, S. (2009) · Nature Cell Biology · doi:10.1038/ncb1895 · Cited by 186 · see citing works
A viral E3 ligase targets RNF8 and RNF168 to control histone ubiquitination and DNA damage responses
Lilley, C. E., Chaurushiya, M. S., Boutell, C., Landry, S., Suh, J., Panier, S., Everett, R. D., Stewart, G. S., Durocher, D., & Weitzman, M. D. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.400 · Cited by 177 · see citing works
Chromatin dynamics and the repair of DNA double strand breaks
Xu, Y., & Price, B. D. (2011) · Cell Cycle · doi:10.4161/cc.10.2.14543 · Cited by 166 · see citing works
BBAP Monoubiquitylates Histone H4 at Lysine 91 and Selectively Modulates the DNA Damage Response
Yan, Q., Dutt, S., Xu, R., Graves, K., Juszczyński, P., Manis, J. P., & Shipp, M. A. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.08.019 · Cited by 165 · see citing works
DNA Repair Factor APLF Is a Histone Chaperone
Mehrotra, P. V., Ahel, D., Ryan, D., Weston, R., Wiechens, N., Kraehenbuehl, R., Owen‐Hughes, T., & Ahel, I. (2011) · Molecular Cell · doi:10.1016/j.molcel.2010.12.008 · Cited by 161 · see citing works
Iles, N., Rulten, S. L., El‐Khamisy, S. F., & Caldecott, K. W. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02269-06 · Cited by 159 · see citing works
Kanno, S., Kuzuoka, H., Sasao, S., Hong, Z., Lan, L., Nakajima, S., & Yasui, A. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601663 · Cited by 153 · see citing works
Histone Ubiquitination Associates with BRCA1-Dependent DNA Damage Response
Wu, J., Huen, M. S. Y., Lu, L., Lin, Y., Dou, Y., Ljungman, M. E., Chen, J., & Yu, X. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01302-08 · Cited by 146 · see citing works
H2AX prevents CtIP-mediated DNA end resection and aberrant repair in G1-phase lymphocytes
Helmink, B. A., Tubbs, A., Dorsett, Y., Bednarski, J. J., Walker, L. M., Feng, Z., Sharma, G. G., McKinnon, P. J., Zhang, J., Bassing, C. H., et al. (2010) · Nature · doi:10.1038/nature09585 · Cited by 143 · see citing works
MDC1 collaborates with TopBP1 in DNA replication checkpoint control
Wang, J., Gong, Z., & Chen, J. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201010026 · Cited by 118 · see citing works
Bermejo, R., Capra, T., González‐Huici, V., Fachinetti, D., Cocito, A., Natoli, G., Katou, Y., Mori, H., Kurokawa, K., Shirahige, K., et al. (2009) · Cell · doi:10.1016/j.cell.2009.06.022 · Cited by 113 · see citing works
MCPH1 Functions in an H2AX-dependent but MDC1-independent Pathway in Response to DNA Damage
Wood, J. L., Singh, N., Mer, G., & Chen, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m705245200 · Cited by 109 · see citing works
Chfr and RNF8 synergistically regulate ATM activation
Wu, J., Chen, Y., Lu, L., Wu, Y., Paulsen, M. T., Ljungman, M. E., Ferguson, D. O., & Yu, X. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2078 · Cited by 107 · see citing works
The ubiquitin‐ and SUMO‐dependent signaling response to DNA double‐strand breaks
Bekker‐Jensen, S., & Mailand, N. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.056 · Cited by 105 · see citing works
MDC1: The art of keeping things in focus
Jungmichel, S., & Stucki, M. (2010) · Chromosoma · doi:10.1007/s00412-010-0266-9 · Cited by 101 · see citing works
TopBP1 functions with 53BP1 in the G1 DNA damage checkpoint
Cescutti, R., Negrini, S., Kohzaki, M., & Halazonetis, T. D. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.238 · Cited by 92 · see citing works
Wolf–Hirschhorn syndrome candidate 1 is involved in the cellular response to DNA damage
Hajdú, I., Ciccia, A., Lewis, S. M., & Elledge, S. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110081108 · Cited by 91 · see citing works
Devgan, S. S., Sanal, Ö., Doil, C., Nakamura, K., Nahas, S., Pettijohn, K. J., Bártek, J., Lukas, C., Lukáš, J., & Gatti, R. A. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.18 · Cited by 88 · see citing works
Self-citationBohgaki, T., Bohgaki, M., Cardoso, R., Panier, S., Zeegers, D., Li, L., Stewart, G. S., Sanchez, O. H., Hande, M. P., Durocher, D., et al. (2011) · PLoS Genetics · doi:10.1371/journal.pgen.1001381 · Cited by 83 · see citing works
Human Xip1 (C2orf13) Is a Novel Regulator of Cellular Responses to DNA Strand Breaks
Bekker‐Jensen, S., Fugger, K., Danielsen, J. M. R., Gromova, I., Sehested, M., Celis, J. E., Bártek, J., Lukas, J., & Mailand, N. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.c700060200 · Cited by 82 · see citing works
Self-citationRAD18 promotes DNA double-strand break repair during G1 phase through chromatin retention of 53BP1
Watanabe, K., Iwabuchi, K., Sun, J., Tsuji, Y., Tani, T., Tokunaga, K., Date, T., HASHIMOTO, M. W., Yamaizumi, M., & Tateishi, S. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp082 · Cited by 75 · see citing works
Huen, M. S. Y., Huang, J., Leung, J. W. C., Sy, S. M.-H., Leung, K. M., Ching, Y.-P., Tsao, S. W., & Chen, J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2009.12.040 · Cited by 73 · see citing works
DNA-damage response and repair activities at uncapped telomeres depend on RNF8
Peuscher, M. H., & Jacobs, J. J. L. (2011) · Nature Cell Biology · doi:10.1038/ncb2326 · Cited by 69 · see citing works
Moon, S.-H., Nguyen, T., Darlington, Y. F., Lu, X., & Donehower, L. A. (2010) · Cell Cycle · doi:10.4161/cc.9.11.11810 · Cited by 66 · see citing works
Chernikova, S. B., Dorth, J. A., Razorenova, O. V., Game, J. C., & Brown, J. M. (2010) · Radiation Research · doi:10.1667/rr2184.1 · Cited by 59 · see citing works
Assembly of multiprotein complexes that control genome function
Dinant, C., Luijsterburg, M. S., Höfer, T., von Bornstaedt, G., Vermeulen, W., Houtsmuller, A. B., & DRIEL, R. V. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200811080 · Cited by 43 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927 · see citing works
Mechanisms of DNA damage, repair, and mutagenesis
Chatterjee, N., & Walker, G. C. (2017) · Environmental and Molecular Mutagenesis · doi:10.1002/em.22087 · Cited by 2,039 · see citing works
The ATM protein kinase: regulating the cellular response to genotoxic stress, and more
Shiloh, Y., & Ziv, Y. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3546 · Cited by 1,649 · see citing works
Playing the End Game: DNA Double-Strand Break Repair Pathway Choice
Chapman, J. R., Taylor, M. R. G., & Boulton, S. J. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.07.029 · Cited by 1,629 · 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
DNA double-strand break repair-pathway choice in somatic mammalian cells
Scully, R., Panday, A., Elango, R., & Willis, N. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0152-0 · Cited by 1,445 · see citing works
Understanding nucleotide excision repair and its roles in cancer and ageing
Marteijn, J. A., Lans, H., Vermeulen, W., & Hoeijmakers, J. H. J. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3822 · Cited by 1,192 · see citing works
Double-strand break repair: 53BP1 comes into focus
Panier, S., & Boulton, S. J. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3719 · Cited by 1,089 · see citing works
The Global Phosphorylation Landscape of SARS-CoV-2 Infection
Bouhaddou, M., Memon, D., Meyer, B., White, K. M., Rezelj, V. V., Marrero, M. C., Polacco, B. J., Melnyk, J. E., Ulferts, S., Kaake, R. M., et al. (2020) · Cell · doi:10.1016/j.cell.2020.06.034 · Cited by 998 · see citing works
Current state of melanoma diagnosis and treatment
Davis, L. E., Shalin, S. C., & Tackett, A. J. (2019) · Cancer Biology & Therapy · doi:10.1080/15384047.2019.1640032 · Cited by 945 · see citing works
53BP1 is a reader of the DNA-damage-induced H2A Lys 15 ubiquitin mark
Fradet-Turcotte, A., Canny, M. D., Escribano-Díaz, C., Orthwein, A., Leung, C. C. Y., Huang, H., Landry, M.-C., Kitevski-LeBlanc, J., Noordermeer, S. M., Sicheri, F., et al. (2013) · Nature · doi:10.1038/nature12318 · Cited by 686 · see citing works
DNA damage and its links to neurodegeneration
Madabhushi, R., Pan, L., & Tsai, L.-H. (2014) · Neuron · doi:10.1016/j.neuron.2014.06.034 · Cited by 654 · see citing works
Regulation of DNA Damage Responses by Ubiquitin and SUMO
Jackson, S. P., & Durocher, D. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.01.017 · Cited by 601 · see citing works
A Role for Small RNAs in DNA Double-Strand Break Repair
Wei, W., Ba, Z., Gao, M., Wu, Y., Ma, Y., Amiard, S., White, C. I., Danielsen, J. M. R., Yang, Y., & Qi, Y. (2012) · Cell · doi:10.1016/j.cell.2012.03.002 · Cited by 583 · see citing works
Site-specific DICER and DROSHA RNA products control the DNA-damage response
Francia, S., Michelini, F., Saxena, A., Tang, D. T. P., de Hoon, M., Anelli, V., Mione, M., Carninci, P., & di Fagagna, F. D. (2012) · Nature · doi:10.1038/nature11179 · Cited by 533 · see citing works
Phase separation of 53BP1 determines liquid‐like behavior of DNA repair compartments
Kilic, S., Lezaja, A., Gatti, M., Bianco, E., Michelena, J., Imhof, R., & Altmeyer, M. (2019) · The EMBO Journal · doi:10.15252/embj.2018101379 · Cited by 434 · see citing works
Toll-like receptors: Significance, ligands, signaling pathways, and functions in mammals
Vidya, M. K., Kumar, V. G., Sejian, V., Bagath, M., Krishnan, G., & Bhatta, R. (2017) · International Reviews of Immunology · doi:10.1080/08830185.2017.1380200 · Cited by 442 · see citing works
Interaction of FUS and HDAC1 regulates DNA damage response and repair in neurons
Wang, W., Pan, L., Su, S. C., Quinn, E. J., Sasaki, M., Jimenez, J., Mackenzie, I. R., Huang, E. J., & Tsai, L. (2013) · Nature Neuroscience · doi:10.1038/nn.3514 · Cited by 433 · see citing works
Rif1 Prevents Resection of DNA Breaks and Promotes Immunoglobulin Class Switching
Virgilio, M. D., Callén, E., Yamane, A., Zhang, W., Janković, M., Gitlin, A. D., Feldhahn, N., Resch, W., Oliveira, T. Y., Chait, B. T., et al. (2013) · Science · doi:10.1126/science.1230624 · Cited by 401 · see citing works
Histone H4 Lysine 20 methylation: key player in epigenetic regulation of genomic integrity
Jorgensen, S., Schotta, G., & Sørensen, C. S. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt012 · Cited by 399 · see citing works
SIRT6 recruits SNF2H to DNA break sites, preventing genomic instability through chromatin remodeling
Toiber, D., Erdel, F., Bouazoune, K., Silberman, D. M., Zhong, L., Mulligan, P., Sebastian, C., Cosentino, C., Martinez-Pastor, B., Giacosa, S., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.018 · Cited by 381 · see citing works
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 370 · see citing works
Self-citationRegulation of DNA double-strand break repair by ubiquitin and ubiquitin-like modifiers
Schwertman, P., Bekker‐Jensen, S., & Mailand, N. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.58 · Cited by 354 · see citing works
Thompson, L. H. (2012) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2012.06.002 · Cited by 357 · see citing works
Prime, Repair, Restore: The Active Role of Chromatin in the DNA Damage Response
Soria, G., Polo, S. E., & Almouzni, G. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.06.002 · Cited by 342 · see citing works
TRIP12 and UBR5 Suppress Spreading of Chromatin Ubiquitylation at Damaged Chromosomes
Guðjόnsson, Þ., Altmeyer, M., Savic, V., Toledo, L. I., Dinant, C., Grøfte, M., Bártková, J., Poulsen, M., Oka, Y., Bekker‐Jensen, S., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.039 · Cited by 338 · see citing works
Self-citationXu, 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
DNA damage foci: Meaning and significance
Rothkamm, K., Barnard, S. G. R., Moquet, J., Ellender, M., Rana, Z., & Burdak‐Rothkamm, S. (2015) · Environmental and Molecular Mutagenesis · doi:10.1002/em.21944 · Cited by 335 · see citing works
The plasticity of DNA replication forks in response to clinically relevant genotoxic stress
Berti, M., Cortez, D., & Lopes, M. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0257-5 · Cited by 329 · see citing works
BRCA1-associated exclusion of 53BP1 from DNA damage sites underlies temporal control of DNA repair
Chapman, J. R., Sossick, A. J., Boulton, S. J., & Jackson, S. P. (2012) · Journal of Cell Science · doi:10.1242/jcs.105353 · Cited by 327 · see citing works
Chemotherapy induced DNA damage response: Convergence of drugs and pathways
Woods, D., & Turchi, J. J. (2013) · Cancer Biology & Therapy · doi:10.4161/cbt.23761 · Cited by 296 · see citing works
Histone deacetylase inhibitor (HDACI) mechanisms of action: Emerging insights
Bose, P., Dai, Y., & Grant, S. (2014) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2014.04.004 · Cited by 282 · see citing works
The AAA-ATPase VCP/p97 promotes 53BP1 recruitment by removing L3MBTL1 from DNA double-strand breaks
Ács, K., Luijsterburg, M. S., Ackermann, L., Salomons, F. A., Hoppe, T., & Dantuma, N. P. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2188 · Cited by 279 · see citing works
PARP inhibitors in the management of breast cancer: current data and future prospects
Livraghi, L., & Garber, J. E. (2015) · BMC Medicine · doi:10.1186/s12916-015-0425-1 · Cited by 267 · see citing works
SETD2 is required for DNA double-strand break repair and activation of the p53-mediated checkpoint
Carvalho, S., Vítor, A. C., Sridhara, S. R. C., Martins, F. B., Raposo, A. C., Desterro, J. M. P., Ferreira, J. A., & de Almeida, S. F. (2014) · eLife · doi:10.7554/elife.02482 · Cited by 266 · see citing works
Violet, M., Delattre, L., Tardivel, M., Sultan, A., Chauderlier, A., Caillierez, R., Talahari, S., Nesslany, F., Lefebvre, B., Bonnefoy, E., et al. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00084 · Cited by 251 · see citing works
Histone methylation and the DNA damage response
Gong, F., & Miller, K. M. (2017) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2017.09.003 · Cited by 247 · see citing works
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 246 · see citing works
A two-step mechanism for TRF2-mediated chromosome-end protection
Okamoto, K., Bartocci, C., Ouzounov, I., Diedrich, J. K., Yates, J. R., & Denchi, E. L. (2013) · Nature · doi:10.1038/nature11873 · Cited by 240 · see citing works
Histone demethylases in chromatin biology and beyond
Dimitrova, E., Turberfield, A. H., & Klose, R. J. (2015) · EMBO Reports · doi:10.15252/embr.201541113 · Cited by 236 · see citing works
The structural basis of modified nucleosome recognition by 53BP1
Wilson, M. D., Benlekbir, S., Fradet‐Turcotte, A., Sherker, A., Julien, J., McEwan, A., Noordermeer, S. M., Sicheri, F., Rubinstein, J. L., & Durocher, D. (2016) · Nature · doi:10.1038/nature18951 · Cited by 234 · see citing works
Targeting tumour-supportive cellular machineries in anticancer drug development
Dobbelstein, M., & Moll, U. M. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4201 · Cited by 229 · see citing works
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 223 · see citing works
53BP1 fosters fidelity of homology-directed DNA repair
Ochs, F., Somyajit, K., Altmeyer, M., Rask, M., Lukas, J., & Lukas, C. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3251 · Cited by 219 · see citing works
Self-citationEarly neuronal accumulation of DNA double strand breaks in Alzheimer’s disease
Shanbhag, N. M., Evans, M. D., Mao, W., Nana, A. L., Seeley, W. W., Adame, A., Rissman, R. A., Masliah, E., & Mucke, L. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0723-5 · Cited by 214 · see citing works
Local generation of fumarate promotes DNA repair through inhibition of histone H3 demethylation
Jiang, Y., Qian, X., Shen, J., Wang, Y., Li, X., Liu, R., Xia, Y., Chen, Q., Peng, G., Lin, S.-Y., et al. (2015) · Nature Cell Biology · doi:10.1038/ncb3209 · Cited by 208 · see citing works
Spatiotemporal regulation of posttranslational modifications in the DNA damage response
Dantuma, N. P., & van Attikum, H. (2015) · The EMBO Journal · doi:10.15252/embj.201592595 · Cited by 200 · see citing works
Stabilization of chromatin topology safeguards genome integrity
Ochs, F., Karemore, G., Miron, E., Brown, J. M., Polášek-Sedláčková, H., Rask, M., Lampe, M., Buckle, V. J., Schermelleh, L., Lukas, J., et al. (2019) · Nature · doi:10.1038/s41586-019-1659-4 · Cited by 202 · see citing works
Self-citationActivation of DNA Damage Response Signaling by Condensed Chromatin
Burgess, R. C., Burman, B., Kruhlak, M. J., & Misteli, T. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.060 · Cited by 198 · see citing works
OTUB1 Co-opts Lys48-Linked Ubiquitin Recognition to Suppress E2 Enzyme Function
Juang, Y.-C. A., Landry, M.-C., Sanches, M., Vittal, V., Leung, C. C. Y., Ceccarelli, D. F. J., Mateo, A.-R. F., Pruneda, J. N., Mao, D. Y. L., Szilard, R. K., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.011 · Cited by 198 · see citing works
The therapeutic significance of mutational signatures from DNA repair deficiency in cancer
Ma, J., Setton, J. S., Lee, N. Y., Riaz, N., & Powell, S. N. (2018) · Nature Communications · doi:10.1038/s41467-018-05228-y · Cited by 192 · see citing works
A role for reactive oxygen species in JAK2V617F myeloproliferative neoplasm progression
Marty, C., Lacout, C., Droin, N. M., Couedic, J. L., Ribrag, V., Solary, É., Vainchenker, W., Villeval, J., & Plo, I. (2013) · Leukemia · doi:10.1038/leu.2013.102 · Cited by 194 · see citing works
Long non-coding RNA ANRIL (CDKN2B-AS) is induced by the ATM-E2F1 signaling pathway
Wan, G., Mathur, R., Hu, X., Liu, Y., Zhang, X., Peng, G., & Lu, X. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.02.006 · Cited by 193 · see citing works
Ago2 facilitates Rad51 recruitment and DNA double-strand break repair by homologous recombination
Gao, M., Wei, W., Li, M.-M., Wu, Y.-S., Ba, Z., Jin, K.-X., Li, M.-M., Liao, Y.-Q., Adhikari, S., Chong, Z., et al. (2014) · Cell Research · doi:10.1038/cr.2014.36 · Cited by 186 · see citing works
FOXM1 (Forkhead box M1) in Tumorigenesis
Wierstra, I. (2013) · Advances in cancer research · doi:10.1016/b978-0-12-407190-2.00016-2 · Cited by 183 · see citing works
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 182 · see citing works
Kanu, N., Gronroos, E. C., Martinez, P., Burrell, R. A., Goh, X. Y., Bártková, J., Maya‐Mendoza, A., Mistrík, M., Rowan, A., Patel, H., et al. (2015) · Oncogene · doi:10.1038/onc.2015.24 · Cited by 181 · see citing works
Gruosso, T., Mieulet, V., Cardon, M., Bourachot, B., Kieffer, Y., Devun, F., Dubois, T., Dutreix, M., Vincent‐Salomon, A., Miller, K. M., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201505891 · Cited by 179 · see citing works
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 · see citing works
Robu, M., Shah, R. G., Petitclerc, N., Brind’Amour, J., Kandan-Kulangara, F., & Shah, G. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209507110 · Cited by 177 · see citing works
Cao, L., Tian, H., Fang, M., Xu, Z., Tang, D., Chen, J., Yin, J., Xiao, H., Shang, K., Han, H., et al. (2022) · Biomaterials · doi:10.1016/j.biomaterials.2022.121856 · Cited by 176 · see citing works
Molecular and epigenetic mechanisms of Cr(VI)-induced carcinogenesis
Chen, Q. Y., Murphy, A., Sun, H., & Costa, M. (2019) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2019.114636 · Cited by 175 · see citing works
Alkene–Tetrazine Ligation for Imaging Cellular DNA
Rieder, U., & Luedtke, N. W. (2014) · Angewandte Chemie International Edition · doi:10.1002/anie.201403580 · Cited by 171 · see citing works
Non-canonical functions of the RB protein in cancer
Dick, F. A., Goodrich, D. W., Sage, J., & Dyson, N. J. (2018) · Nature reviews. Cancer · doi:10.1038/s41568-018-0008-5 · Cited by 169 · see citing works
DNA Damage Response and Autophagy: A Meaningful Partnership
Eliopoulos, A. G., Havaki, S., & Gorgoulis, V. G. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00204 · Cited by 169 · see citing works
Histone variants: emerging players in cancer biology
Vardabasso, C., Hasson, D., Ratnakumar, K., Chung, C., Duarte, L. F., & Bernstein, E. (2013) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1343-z · Cited by 167 · see citing works
The FHA and BRCT domains recognize ADP-ribosylation during DNA damage responsePreprint
Mo, L., Lu, L., Yang, C., Wang, S., & Yu, X. (2013) · Genes & Development · doi:10.1101/gad.226357.113 · Cited by 164 · see citing works
The biogenesis of chromosome translocations
Roukos, V., & Misteli, T. (2014) · Nature Cell Biology · doi:10.1038/ncb2941 · Cited by 166 · see citing works
Oplustilova, L., Wolanin, K., Mistrík, M., Kořínková, G., Šimková, D., Bouchal, J., Lenobel, R., Bártková, J., Lau, A., O’Connor, M. J., et al. (2012) · Cell Cycle · doi:10.4161/cc.22026 · Cited by 164 · see citing works
Self-citationThe RNA Splicing Response to DNA Damage
Shkreta, L., & Chabot, B. (2015) · Biomolecules · doi:10.3390/biom5042935 · Cited by 154 · see citing works
Mechanisms of FUS mutations in familial amyotrophic lateral sclerosis
Shang, Y., & Huang, E. J. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.036 · Cited by 154 · see citing works
A protein interaction landscape of breast cancer
Kim, M., Park, J., Bouhaddou, M., Kim, K., Rojc, A., Modak, M., Soucheray, M., McGregor, M., O’Leary, P. C., Wolf, D. M., et al. (2021) · Science · doi:10.1126/science.abf3066 · Cited by 154 · see citing works
ATM-Dependent Phosphorylation of All Three Members of the MRN Complex: From Sensor to Adaptor
Lavin, M. F., Kozlov, S., Gatei, M. H., & Kijas, A. W. (2015) · Biomolecules · doi:10.3390/biom5042877 · Cited by 152 · see citing works
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
Davalli, P., Marverti, G., Lauriola, A., & D’Arca, D. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2389523 · Cited by 151 · see citing works
Trial Watch: Targeting ATM–CHK2 and ATR–CHK1 pathways for anticancer therapy
Manic, G., Obrist, F., Sistigu, A., & Vitale, I. (2015) · Molecular & Cellular Oncology · doi:10.1080/23723556.2015.1012976 · Cited by 147 · see citing works
Jiang, J., Lv, W., Ye, X., Wang, L., Zhang, M., Yang, H., Okuka, M., Zhou, C., Zhang, X., Liu, L., et al. (2012) · Cell Research · doi:10.1038/cr.2012.157 · Cited by 146 · see citing works
ATM kinase: Much more than a DNA damage responsive protein
Guleria, A., & Chandna, S. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.12.009 · Cited by 145 · see citing works
Francia, S., Cabrini, M., Matti, V., Oldani, A., & di Fagagna, F. D. (2016) · Journal of Cell Science · doi:10.1242/jcs.182188 · Cited by 139 · see citing works
53BP1: A key player of DNA damage response with critical functions in cancer
Mirza‐Aghazadeh‐Attari, M., Mohammadzadeh, A., Yousefi, B., Mihanfar, A., Karimian, A., & Majidinia, M. (2018) · DNA repair · doi:10.1016/j.dnarep.2018.11.008 · Cited by 142 · see citing works
Protein post-translational modifications in the regulation of cancer hallmarks
Wang, H., Yang, L., Liu, M., & Luo, J. (2022) · Cancer Gene Therapy · doi:10.1038/s41417-022-00464-3 · Cited by 144 · see citing works
Robert, C., & Rassool, F. V. (2012) · Advances in cancer research · doi:10.1016/b978-0-12-394387-3.00003-3 · Cited by 139 · see citing works
Kim, J. J., Lee, S. Y., Gong, F., Battenhouse, A. M., Boutz, D. R., Bashyal, A., Refvik, S. T., Chiang, C., Xhemalçe, B., Paull, T. T., et al. (2019) · Genes & Development · doi:10.1101/gad.331231.119 · Cited by 139 · see citing works
A small RNA response at DNA ends in Drosophila
Michalik, K., Böttcher, R., & Förstemann, K. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks711 · Cited by 134 · see citing works
An ATR‐dependent function for the Ddx19 RNA helicase in nuclear R‐loop metabolism
Hodroj, D., Recolin, B., Serhal, K., Martinez, S. F., Tsanov, N., Merhi, R. A., & Maiorano, D. (2017) · The EMBO Journal · doi:10.15252/embj.201695131 · Cited by 134 · see citing works
Acetylation Reader Proteins: Linking Acetylation Signaling to Genome Maintenance and Cancer
Gong, F., Chiu, L.-Y., & Miller, K. M. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006272 · Cited by 132 · see citing works
The SUV4-20 inhibitor A-196 verifies a role for epigenetics in genomic integrity
Bromberg, K. D., Mitchell, T. R. H., Upadhyay, A. K., Jakob, C. G., Jhala, M. A., Comess, K. M., Lasko, L. M., Li, C., Tuzon, C. T., Dai, Y., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2282 · Cited by 132 · see citing works
Mosbech, A., Lukas, C., Bekker‐Jensen, S., & Mailand, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.459917 · Cited by 131 · see citing works
Self-citationJMJD1C 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 130 · see citing works
Self-citationEngineered proteins detect spontaneous DNA breakage in human and bacterial cells
Shee, C., Cox, B. D., Gu, F., Luengas, E. M., Joshi, M. C., Chiu, L.-Y., Magnan, D. R., Halliday, J. A., Frisch, R. L., Gibson, J. L., et al. (2013) · eLife · doi:10.7554/elife.01222 · Cited by 127 · see citing works
Treacher Collins syndrome TCOF1 protein cooperates with NBS1 in the DNA damage response
Ciccia, A., Huang, J., Izhar, L., Sowa, M. E., Harper, J. W., & Elledge, S. J. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1422488112 · Cited by 126 · see citing works
ISWI chromatin remodeling complexes in the DNA damage response
Aydın, Ö. Z., Vermeulen, W., & Lans, H. (2014) · Cell Cycle · doi:10.4161/15384101.2014.956551 · Cited by 125 · see citing works
Qiao, H., Chen, J. K., Reynolds, A., Höög, C., Paddy, M. R., & Hunter, N. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002790 · Cited by 126 · see citing works
Yan, G., Eller, M. S., Elm, C. M. L., Larocca, C. A., Ryu, B., Panova, I. P., Rabbitts, B. M., Bowers, E. M., Meyers, D. J., Lareau, L., et al. (2013) · Journal of Investigative Dermatology · doi:10.1038/jid.2013.187 · Cited by 122 · see citing works
USP13 regulates the RAP80-BRCA1 complex dependent DNA damage response
Li, Y., Luo, K., Yin, Y., Wu, C., Deng, M., Li, L., Chen, Y., Nowsheen, S., Lou, Z., & Yuan, J. (2017) · Nature Communications · doi:10.1038/ncomms15752 · Cited by 122 · see citing works
Ubiquitin-activating enzyme UBA1 is required for cellular response to DNA damage
Moudrý, P., Lukas, C., Macůrek, L., Hanzlíková, H., Hodný, Z., Lukas, J., & Bártek, J. (2012) · Cell Cycle · doi:10.4161/cc.19978 · Cited by 120 · see citing works
Self-citationNikolova, T., Dvorak, M., Jung, F., Adam, I., Krämer, E., Gerhold‐Ay, A., & Kaina, B. (2014) · Toxicological Sciences · doi:10.1093/toxsci/kfu066 · Cited by 119 · see citing works
CREBBP and p300 lysine acetyl transferases in the DNA damage response
Dutto, I., Scalera, C., & Prosperi, E. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2717-4 · Cited by 118 · see citing works
Systemic DNA damage responses in aging and diseases
Ribezzo, F., Shiloh, Y., & Schumacher, B. (2016) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2015.12.005 · Cited by 116 · see citing works
Patching Broken DNA: Nucleosome Dynamics and the Repair of DNA Breaks
Gürsoy-Yüzügüllü, Ö., House, N. C. M., & Price, B. D. (2015) · Journal of Molecular Biology · doi:10.1016/j.jmb.2015.11.021 · Cited by 110 · see citing works
- Authors
- Lukas, J., Lukas, C., & Bartek, J.
- Affiliations
- Danish Cancer Society (DK)
- Corresponding author
- Lukas, Jiri
- Lukas, Claudia
- ORCID
- Lukas, Claudia
- Venue
- Nature Cell Biology
- Published
- 2011-10
- Volume
- 13
- Issue
- 10
- Pages
- 1161-1169
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W2008185037
- Cited by
- 645
- References
- 102
- Citations by year
- 2026: 11 · 2025: 12 · 2024: 28 · 2023: 23 · 2022: 33 · 2021: 36 · 2020: 36 · 2019: 35 · 2018: 45 · 2017: 45 · 2016: 60 · 2015: 56 · 2014: 71 · 2013: 82 · 2012: 64
- FWCI
- 6.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- genome stability, DNA damage response, γH2AX, histone modifications, nuclear foci, DNA lesions
- MeSH terms
- Animals, Cell Cycle, DNA Damage, DNA Repair, Histones, Humans, Protein Processing, Post-Translational, Chromatin Assembly and Disassembly, Genomic Instability
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