The DOI matches its Crossref record; 102 of the 102 references it cites were found in a registry or an index.
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.
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
“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]
Citations
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 198
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 6,517
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
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
Inhibition of Poly(ADP-Ribose) Polymerase in Tumors from BRCA 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
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
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
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
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
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 1,023
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
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
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
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 1,728
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
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 1,542
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
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 1,168
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 1,018
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 986
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
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
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
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 575
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 553
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 456
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 459
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 467
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 423
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 414
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
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
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 368
Thompson, L. H. (2012) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2012.06.002 · Cited by 357
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
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 347
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
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 345
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 343
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
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
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 287
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 296
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 272
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 282
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
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 265
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
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 251
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 251
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 246
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 233
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
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 232
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
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
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 209
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 203
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
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
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 203
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
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 198
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 192
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 190
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
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 189
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
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
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
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 179
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 180
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
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 175
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
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 178
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 178
The biogenesis of chromosome translocations
Roukos, V., & Misteli, T. (2014) · Nature Cell Biology · doi:10.1038/ncb2941 · Cited by 174
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 167
Self-citationThe RNA Splicing Response to DNA Damage
Shkreta, L., & Chabot, B. (2015) · Biomolecules · doi:10.3390/biom5042935 · Cited by 156
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 164
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 160
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 164
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
Davalli, P., Marverti, G., Lauriola, A., & D’Arca, D. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2389523 · Cited by 156
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 152
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 147
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 147
Francia, S., Cabrini, M., Matti, V., Oldani, A., & di Fagagna, F. D. (2016) · Journal of Cell Science · doi:10.1242/jcs.182188 · Cited by 145
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 144
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 148
Robert, C., & Rassool, F. V. (2012) · Advances in cancer research · doi:10.1016/b978-0-12-394387-3.00003-3 · Cited by 140
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 138
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
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
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 137
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
Mosbech, A., Lukas, C., Bekker‐Jensen, S., & Mailand, N. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.459917 · Cited by 136
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 139
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 134
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
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
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
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
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 123
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 124
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
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
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
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 118
Metadata
- 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