The DOI matches its Crossref record; 53 of the 53 references it cites were found in a registry or an index.
ATM-Dependent Chromatin Changes Silence Transcription In cis to DNA Double-Strand Breaks
Open accessAbstract
DNA double-strand breaks (DSBs) initiate extensive local and global alterations in chromatin structure, many of which depend on the ATM kinase. Histone H2A ubiquitylation (uH2A) on chromatin surrounding DSBs is one example, thought to be important for recruitment of repair proteins. uH2A is also implicated in transcriptional repression; an intriguing yet untested hypothesis is that this function is conserved in the context of DSBs. Using a novel reporter that allows for visualization of repair protein recruitment and local transcription in single cells, we describe an ATM-dependent transcriptional silencing program in cis to DSBs. ATM prevents RNA polymerase II elongation-dependent chromatin decondensation at regions distal to DSBs. Silencing is partially dependent on E3 ubiquitin ligases RNF8 and RNF168, whereas reversal of silencing relies on the uH2A deubiquitylating enzyme USP16. These findings give insight into the role of posttranslational modifications in mediating crosstalk between diverse processes occurring on chromatin.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“DSBs were previously shown to interfere with the expression of break-proximal genes in tumor cell lines (11–13,42).”
From Controlled DNA double-strand break induction in mice reveals post-damage transcriptome stability (2016) · cites this paper as [13]
In the citing paper
“Consistent with this, recent findings demonstrate transcriptional repression in cis to DSBs, which depends on DNA damage signaling and ceases after DSB repair is complete (10–13).”
From Controlled DNA double-strand break induction in mice reveals post-damage transcriptome stability (2016) · cites this paper as [13]
In the citing paper
“This work is, however, limited to highly proliferative tumor cell lines, and its implications for animal tissues, which often exhibit little or no proliferation, remain unclear.”
From Controlled DNA double-strand break induction in mice reveals post-damage transcriptome stability (2016) · cites this paper as [13]
In the citing paper
“DSBs are known to promote a dynamic reorganization of break-proximal chromatin, with the potential to affect the expression of both break-proximal and ostensibly undamaged genes (10,13,19,45,48–50).”
From Controlled DNA double-strand break induction in mice reveals post-damage transcriptome stability (2016) · cites this paper as [13]
In the citing paper
“our findings, thus, suggest that most tissues have the potential to restore DSB-induced gene deregulation, although the kinetics of DSB repair and DNA damage-associated gene silencing may differ depending on cell type and/or cell cycle state.”
From Controlled DNA double-strand break induction in mice reveals post-damage transcriptome stability (2016) · cites this paper as [13]
In the citing paper
“The latter is in agreement with several reports implicating the DDR mediators ATM and DNA-PK in DSB-proximal repressive chromatin formation as well as transcriptional silencing (9–13,50).”
From Controlled DNA double-strand break induction in mice reveals post-damage transcriptome stability (2016) · cites this paper as [13]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
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
DNA damage response as a candidate anti-cancer barrier in early human tumorigenesis
Bartkova, J., Hořejší, Z., Koed, K., Krämer, A., Tort, F., Zieger, K., Guldberg, P., Sehested, M., Nesland, J. M., Lukas, C., et al. (2005) · Nature · doi:10.1038/nature03482 · Cited by 2,688
Hypomethylation distinguishes genes of some human cancers from their normal counterparts
Feinberg, A. P., & Vogelstein, B. (1983) · Nature · doi:10.1038/301089a0 · Cited by 2,430
Megabase Chromatin Domains Involved in DNA Double-Strand Breaks in Vivo
Rogakou, E. P., Boon, C., Redon, C., & Bonner, W. M. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.5.905 · Cited by 2,422
Activation of the DNA damage checkpoint and genomic instability in human precancerous lesions
Gorgoulis, V. G., Vassiliou, L.-V. F., Karakaidos, P., Zacharatos, P., Kotsinas, A., Liloglou, T., Venere, M., DiTullio, R. A., Kastrinakis, N. G., Levy, B., et al. (2005) · Nature · doi:10.1038/nature03485 · Cited by 2,009
Role of histone H2A ubiquitination in Polycomb silencing
Wang, H., Wang, L., Erdjument‐Bromage, H., Vidal, M., Tempst, P., Jones, R. S., & Zhang, Y. (2004) · Nature · doi:10.1038/nature02985 · Cited by 1,856
Position effect at S. cerevisiae telomeres: Reversible repression of Pol II transcription
Gottschling, D. E., Aparicio, O. M., Billington, B. L., & Zakian, V. A. (1990) · Cell · doi:10.1016/0092-8674(90)90141-z · Cited by 1,325
Hickson, I., Zhao, Y., Richardson, C. J., Green, S. J., Martin, N. M. B., Orr, A. I., Reaper, P. M., Jackson, S. P., Curtin, N. J., & Smith, G. C. M. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-2727 · Cited by 1,220
RNF8 Ubiquitylates Histones at DNA Double-Strand Breaks and Promotes Assembly of Repair Proteins
Mailand, N., Bekker‐Jensen, S., Kildegaard, H. F., Melander, F., Bártek, J., Lukas, C., & Lukas, J. (2007) · Cell · doi:10.1016/j.cell.2007.09.040 · Cited by 1,193
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–300 of 741
The emerging role of Polycomb repressors in the response to DNA damage
Vissers, J. H. A., van Lohuizen, M., & Citterio, E. (2012) · Journal of Cell Science · doi:10.1242/jcs.107375 · Cited by 81
Zhang, Z., Yang, H., & Wang, H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.599605 · Cited by 79
Bahrami, E., Witzel, M., Racek, T., Puchałka, J., Hollizeck, S., Kohistani, N., Kotlarz, D., Horny, H., Feederle, R., Schmidt, H., et al. (2017) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2016.10.053 · Cited by 74
RNF20–RNF40: A ubiquitin‐driven link between gene expression and the DNA damage response
Shiloh, Y., Shema, E., Moyal, L., & Oren, M. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.07.034 · Cited by 77
RNF8- and Ube2S-Dependent Ubiquitin Lysine 11-Linkage Modification in Response to DNA Damage
Paul, A., & Wang, B. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.04.013 · Cited by 75
ATM and CDK2 control chromatin remodeler CSB to inhibit RIF1 in DSB repair pathway choice
Batenburg, N. L., Walker, J. R., Noordermeer, S. M., Moatti, N., Durocher, D., & Zhu, X. (2017) · Nature Communications · doi:10.1038/s41467-017-02114-x · Cited by 73
DNA damage, chromatin, and transcription: the trinity of aging
Burgess, R. C., Misteli, T., & Oberdoerffer, P. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.07.005 · Cited by 72
Chen, J., Feng, W., Jiang, J., Deng, Y., & Huen, M. S. Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.373530 · Cited by 72
Nucleotide Pool Depletion Induces G-Quadruplex-Dependent Perturbation of Gene Expression
Papadopoulou, C., Guilbaud, G., Schiavone, D., & Sale, J. E. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.039 · Cited by 71
Meiotic DSB patterning: A multifaceted process
Cooper, T. J., Garcia, V., & Neale, M. J. (2016) · Cell Cycle · doi:10.1080/15384101.2015.1093709 · Cited by 79
A Novel Aspect of Tumorigenesis—BMI1 Functions in Regulating DNA Damage Response
Lin, X., Ojo, D., Wei, F., Wong, N., Gu, Y. J., & Tang, D. (2015) · Biomolecules · doi:10.3390/biom5043396 · Cited by 72
Analysis of NHEJ-Based DNA Repair after CRISPR-Mediated DNA Cleavage
Song, B., Yang, S., Hwang, G., Yu, J., & Bae, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22126397 · Cited by 75
ADAR-mediated RNA editing of DNA:RNA hybrids is required for DNA double strand break repair
Jimeno, S., Prados‐Carvajal, R., Fernández-Ávila, M. J., Silva, S. D. R., Silvestris, D. A., Endara-Coll, M., Rodríguez‐Real, G., Domingo‐Prim, J., Mejías-Navarro, F., Romero-Franco, A., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25790-2 · Cited by 73
DNA double-strand break–capturing nuclear envelope tubules drive DNA repair
Shokrollahi, M., Stanić, M., Hundal, A. K., Chan, J. N. Y., Urman, D., Jordan, C. A., Hakem, A., Espín, R., Hao, J., Krishnan, R., et al. (2024) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01286-7 · Cited by 71
Transcription and DNA Damage: Holding Hands or Crossing Swords?
D’Alessandro, G., & di Fagagna, F. D. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.11.002 · Cited by 72
ATM Deficiency Results in Accumulation of DNA-Topoisomerase I Covalent Intermediates in Neural Cells
Alagöz, M., Chiang, S., Sharma, A. B., & El‐Khamisy, S. F. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058239 · Cited by 71
Transcriptional Regulation at DSBs: Mechanisms and Consequences
Machour, F. E., & Ayoub, N. (2020) · Trends in Genetics · doi:10.1016/j.tig.2020.01.001 · Cited by 68
Sharma, S., Anand, R., Zhang, X., Francia, S., Michelini, F., Galbiati, A., Williams, H., Ronato, D. A., Masson, J., Rothenberg, E., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2020.108565 · Cited by 69
Bon voyage: A transcriptional journey around DNA breaks
Caron, P., van der Linden, J., & van Attikum, H. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.102686 · Cited by 68
The CIP2A-TOPBP1 complex safeguards chromosomal stability during mitosis
Zompit, M. D. M., Esteban, M. T., Mooser, C., Adam, S., Rossi, S. E., Jeanrenaud, A., Leimbacher, P.-A., Fink, D. A., Shorrocks, A.-M. K., Blackford, A. N., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31865-5 · Cited by 66
The ubiquitin specific protease USP34 promotes ubiquitin signaling at DNA double-strand breaks
Sy, S. M.-H., Jiang, J., O, W. S., Deng, Y., & Huen, M. S. Y. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt622 · Cited by 68
Chromatin dynamics in DNA double-strand break repair
Shi, L., & Oberdoerffer, P. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.01.002 · Cited by 72
Wip1 Controls Global Heterochromatin Silencing via ATM/BRCA1-Dependent DNA Methylation
Filipponi, D., Müller, J., Emelyanov, A., & Bulavin, D. V. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.08.022 · Cited by 70
DNA Nicks Promote Efficient and Safe Targeted Gene Correction
Davis, L. J., & Maizels, N. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023981 · Cited by 67
Nuclear dynamics of radiation-induced foci in euchromatin and heterochromatin
Chiolo, I., Tang, J., Georgescu, W., & Costes, S. V. (2013) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2013.08.001 · Cited by 67
BMI1–UBR5 axis regulates transcriptional repression at damaged chromatin
Sanchez, A. R., de Vivo, A., Uprety, N., Kim, J., Stevens, S. M., & Kee, Y. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1610735113 · Cited by 66
Abu‐Zhayia, E. R., Awwad, S. W., Ben‐Oz, B. M., Khoury-Haddad, H., & Ayoub, N. (2017) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjx050 · Cited by 71
Alexander, A., & Walker, C. L. (2010) · Cell Cycle · doi:10.4161/cc.9.18.13253 · Cited by 65
ATM-dependent pathways of chromatin remodelling and oxidative DNA damage responses
Berger, N. D., Stanley, F. K. T., Moore, S., & Goodarzi, A. A. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0283 · Cited by 65
USP11 Is a Negative Regulator to γH2AX Ubiquitylation by RNF8/RNF168
Yu, M., Liu, K., Mao, Z., Luo, J., Gu, W. J., & Zhao, W. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.624478 · Cited by 64
Controlled DNA double-strand break induction in mice reveals post-damage transcriptome stability
Kim, J., Sturgill, D., Tran, A. D., Sinclair, D. A., & Oberdoerffer, P. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkv1482 · Cited by 62
The dark side of RNA:DNA hybrids
Brambati, A., Zardoni, L., Nardini, E., Pellicioli, A., & Liberi, G. (2020) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2020.108300 · Cited by 65
Antecedent chromatin organization determines cGAS recruitment to ruptured micronuclei
MacDonald, K. M., Nicholson-Puthenveedu, S., Tageldein, M. M., Khasnis, S., Arrowsmith, C. H., & Harding, S. M. (2023) · Nature Communications · doi:10.1038/s41467-023-36195-8 · Cited by 66
Chromatin perturbations during the DNA damage response in higher eukaryotes
Bakkenist, C. J., & Kastan, M. B. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.09.002 · Cited by 64
Kulashreshtha, M., Mehta, I. S., Kumar, P., & Rao, B. J. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw573 · Cited by 67
DNA:RNA hybrids form at DNA double-strand breaks in transcriptionally active loci
Bader, A. S., & Bushell, M. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2464-6 · Cited by 62
Xie, A., Odate, S., Chandramouly, G., & Scully, R. A. (2010) · Cell Cycle · doi:10.4161/cc.9.17.12884 · Cited by 59
Bhatia, N., Xiao, T. Z., Rosenthal, K. A., Siddiqui, I. A., Thiyagarajan, S., Smart, B., Meng, Q., Zuleger, C., Mukhtar, H., Kenney, S. C., et al. (2012) · Journal of Investigative Dermatology · doi:10.1038/jid.2012.355 · Cited by 59
C‐Jun N‐terminal kinase signalling pathway in response to cisplatin
Yan, D., An, G., & Kuo, M. T. (2016) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12908 · Cited by 61
Structural basis of specific H2A K13/K15 ubiquitination by RNF168
Horn, V., Uckelmann, M., Zhang, H., Eerland, J., Aarsman, I., le Paige, U. B., Davidovich, C., Sixma, T. K., & van Ingen, H. (2019) · Nature Communications · doi:10.1038/s41467-019-09756-z · Cited by 60
Helfricht, A., Wiegant, W. W., Thijssen, P., Vertegaal, A. C. O., Luijsterburg, M. S., & van Attikum, H. (2013) · Cell Cycle · doi:10.4161/cc.26033 · Cited by 66
Single-molecule imaging of transcription at damaged chromatin
Vítor, A. C., Sridhara, S. R. C., Sabino, J. C., Afonso, A., Grosso, A. R., Martin, R. M., & de Almeida, S. F. (2019) · Science Advances · doi:10.1126/sciadv.aau1249 · Cited by 56
Cas9 deactivation with photocleavable guide RNAs
Zou, R. S., Liu, Y., Wu, B., & Ha, T. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.02.007 · Cited by 61
Solyom, S., Aressy, B., Pylkäs, K., Patterson-Fortin, J., Hartikainen, J. M., Kallioniemi, A., Kauppila, S., Nikkilä, J., Kosma, V.-M., Mannermaa, A., et al. (2012) · Science Translational Medicine · doi:10.1126/scitranslmed.3003223 · Cited by 59
Self-citationA critical role for topoisomerase IIb and DNA double strand breaks in transcription
Calderwood, S. K. (2016) · Transcription · doi:10.1080/21541264.2016.1181142 · Cited by 61
Tanikawa, M., Sanjiv, K., Helleday, T., Herr, P., & Mortusewicz, O. (2016) · Oncogenesis · doi:10.1038/oncsis.2016.70 · Cited by 59
Control of the chromatin response to DNA damage: Histone proteins pull the strings
Ferrand, J., Plessier, A., & Polo, S. E. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.07.002 · Cited by 61
Spatiotemporal dynamics of 53BP1 dimer recruitment to a DNA double strand break
Lou, J., Priest, D. G., Solano, A. N., Kerjouan, A., & Hinde, E. (2020) · Nature Communications · doi:10.1038/s41467-020-19504-3 · Cited by 62
BAP1 as a guardian of genome stability: implications in human cancer
Kwon, J., Lee, D., & Lee, S.-A. (2023) · Experimental & Molecular Medicine · doi:10.1038/s12276-023-00979-1 · Cited by 63
O’Hagan, H. M. (2013) · Environmental and Molecular Mutagenesis · doi:10.1002/em.21830 · Cited by 62
Seiler, D. M., Rouquette, J., Schmid, V. J., Strickfaden, H., Ottmann, C., Drexler, G. A., Mazurek, B., Greubel, C., Hable, V., Dollinger, G., et al. (2011) · Chromosome Research · doi:10.1007/s10577-011-9244-1 · Cited by 64
The RNA Response to DNA Damage
Giono, L. E., Moreno, N. N., Botto, A. E. C., Dujardin, G., Muñoz, M. J., & Kornblihtt, A. R. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.03.004 · Cited by 59
Reading chromatin signatures after DNA double-strand breaks
Wilson, M. D., & Durocher, D. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0280 · Cited by 60
Mikolaskova, B., Jurcik, M., Čipáková, I., Kretová, M., Chovanec, M., & Cipak, L. (2018) · Current Genetics · doi:10.1007/s00294-018-0819-7 · Cited by 60
Ka, N., Lim, G. Y., Hwang, S., Kim, S.-S., & Lee, M. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110138 · Cited by 61
Epigenomics and the Regulation of Aging
Boyd-Kirkup, J. D., Green, C. D., Wu, G., Wang, D., & Han, J. J. (2013) · Epigenomics · doi:10.2217/epi.13.5 · Cited by 57
The epigenetics of tumour initiation: cancer stem cells and their chromatin
Avgustinova, A., & Benitah, S. A. (2016) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2016.01.003 · Cited by 58
Burger, K., Ketley, R. F., & Gullerová, M. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00061 · Cited by 58
A licensing step links AID to transcription elongation for mutagenesis in B cells
Methot, S. P., Litzler, L. C., Subramani, P. G., Eranki, A. K., Fifield, H., Patenaude, A., Gilmore, J. C., Santiago, G. E., Bagci, H., Côté, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-03387-6 · Cited by 59
Róna, G., Roberti, D., Yin, Y., Pagan, J. K., Homer, H., Sassani, E., Zeke, A., Busino, L., Rothenberg, E., & Pagano, M. (2018) · eLife · doi:10.7554/elife.38771 · Cited by 61
Topoisomerase IIα represses transcription by enforcing promoter-proximal pausing
Herrero-Ruíz, A., Martínez-García, P. M., Terrón-Bautista, J., Millán-Zambrano, G., Lieberman, J., Jimeno-González, S., & Cortés-Ledesma, F. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108977 · Cited by 44
Hang, Q., Zeng, L., Wang, L., Nie, L., Yao, F., Teng, H., Deng, Y., Yap, S., Sun, Y., Frank, S. J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24298-z · Cited by 57
Lloyd, R. L., Urban, V., Muñoz‐Martínez, F., Ayestaran, I., Thomas, J. C., de Renty, C., O’Connor, M. J., Forment, J. V., Galanty, Y., & Jackson, S. P. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab628 · Cited by 56
Regulation of stem cell function by protein ubiquitylation
Strikoudis, A., Guillamot, M., & Aifantis, I. (2014) · EMBO Reports · doi:10.1002/embr.201338373 · Cited by 55
The BRCA1 Ubiquitin ligase function sets a new trend for remodelling in DNA repair
Densham, R. M., & Morris, J. R. (2016) · Nucleus · doi:10.1080/19491034.2016.1267092 · Cited by 55
Bouwman, B. A. M., & Crosetto, N. (2018) · Genes · doi:10.3390/genes9120632 · Cited by 65
Chen, Y., & Zhu, W. (2016) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmw050 · Cited by 57
Regulation of DNA Double Strand Breaks Processing: Focus on Barriers
Marini, F., Rawal, C. C., Liberi, G., & Pellicioli, A. (2019) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00055 · Cited by 55
Jia, N., Guo, C., Nakazawa, Y., van den Heuvel, D., Luijsterburg, M. S., & Ogi, T. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103192 · Cited by 50
Hao, S., Wang, Y., Zhao, Y., Gao, W. Y., Cui, W., Li, Y., Cui, J. G., Liu, Y., Lin, L., Xu, X., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac734 · Cited by 55
TRIP12 as a mediator of human papillomavirus/p16-related radiation enhancement effects
Wang, L., Zhang, P., Molkentine, D. P., Chen, C., Molkentine, J. M., Piao, H., Raju, U., Zhang, J., Valdecanas, D. R., Tailor, R. C., et al. (2016) · Oncogene · doi:10.1038/onc.2016.250 · Cited by 50
Ka, N., Na, T., Na, H., Lee, M. H., Park, H., Hwang, S., Kim, I. Y., Seong, J. K., & Lee, M. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2099 · Cited by 53
Experimental approaches to identify cellular G-quadruplex structures and functions
Antonio, M. D., Rodriguez, R., & Balasubramanian, S. (2012) · Methods · doi:10.1016/j.ymeth.2012.01.008 · Cited by 53
Single cell analysis of Daxx and ATRX-dependent transcriptional repression
Newhart, A., Rafalska-Metcalf, I. U., Yang, T., Negorev, D. G., & Janicki, S. M. (2012) · Journal of Cell Science · doi:10.1242/jcs.110148 · Cited by 53
Self-citationMorales, J. C., Richard, P., Rommel, A., Fattah, F. J., Motea, E. A., Patidar, P. L., Xiao, L., Leskov, K., Wu, S.-Y., Hittelman, W. N., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku160 · Cited by 50
Hepatoma-derived growth factor-related protein 2 promotes DNA repair by homologous recombination
Baude, A., Aaes, T. L., Zhai, B., Al-Nakouzi, N., Oo, H. Z., Daugaard, M., Rohde, M., & Jäättelä, M. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1526 · Cited by 46
The abscopal effect: a sense of DNA damage is in the air
Lippert, T. P., & Greenberg, R. A. (2021) · Journal of Clinical Investigation · doi:10.1172/jci148274 · Cited by 53
Self-citationAberrant RNA methylation triggers recruitment of an alkylation repair complex
Tsao, N., Brickner, J. R., Rodell, R., Ganguly, A., Wood, M., Oyeniran, C., Ahmad, T., Sun, H., Bacolla, A., Zhang, L., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.09.024 · Cited by 46
To spread or not to spread—chromatin modifications in response to DNA damage
Altmeyer, M., & Lukas, J. (2013) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2012.11.001 · Cited by 53
TRAIP/RNF206 is required for recruitment of RAP80 to sites of DNA damage
Lee, N. S., Chung, H. J., Kim, H.-J., Lee, S. Y., Ji, J.-H., Seo, Y., Han, S. H., Choi, M., Yun, M., Lee, S., et al. (2016) · Nature Communications · doi:10.1038/ncomms10463 · Cited by 46
Writers, Readers, and Erasers of Histone Ubiquitylation in DNA Double-Strand Break Repair
Smeenk, G., & Mailand, N. (2016) · Frontiers in Genetics · doi:10.3389/fgene.2016.00122 · Cited by 52
As a Nucleus Enters a Small Pore, Chromatin Stretches and Maintains Integrity, Even with DNA Breaks
Irianto, J., Xia, Y., Pfeifer, C. R., Greenberg, R. A., & Discher, D. E. (2016) · Biophysical Journal · doi:10.1016/j.bpj.2016.09.047 · Cited by 49
Self-citationPellino1 regulates reversible ATM activation via NBS1 ubiquitination at DNA double-strand breaks
Ha, G., Ji, J., Chae, S., Park, J., Kim, S., Lee, J., Kim, Y., Min, S., Park, J., Kang, T., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09641-9 · Cited by 47
DNA double-strand breaks: a potential therapeutic target for neurodegenerative diseases
Thadathil, N., Hori, R. T., Xiao, J., & Khan, M. M. (2019) · Chromosome Research · doi:10.1007/s10577-019-09617-x · Cited by 51
Bartocci, C., & Denchi, E. L. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00128 · Cited by 50
Velichko, A. K., Petrova, N. V., Luzhin, A. V., Strelkova, O. S., Ovsiannikova, N. L., Kireev, I. I., Petrova, N. V., Razin, S. V., & Kantidze, O. L. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz436 · Cited by 48
RNA Splicing: A New Player in the DNA Damage Response
Lenzken, S. C., Loffreda, A., & Barabino, S. M. L. (2013) · International Journal of Cell Biology · doi:10.1155/2013/153634 · Cited by 48
Aquarius is required for proper CtIP expression and homologous recombination repair
Sakasai, R., Isono, M., Wakasugi, M., HASHIMOTO, M. W., Sunatani, Y., Matsui, T., Shibata, A., Matsunaga, T., & Iwabuchi, K. (2017) · Scientific Reports · doi:10.1038/s41598-017-13695-4 · Cited by 45
RNF8-dependent histone ubiquitination during DNA damage response and spermatogenesis
Ma, T., Keller, J. A., & Yu, X. (2011) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmr016 · Cited by 50
Zhao, J., Tian, S., Guo, Q., Bao, K., Yu, G., Wang, X., Shen, X., Zhang, J., Chen, J., Yang, Y., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.031 · Cited by 49
Double-strand break repair on sex chromosomes: challenges during male meiotic prophase
Lu, L., & Yu, X. (2015) · Cell Cycle · doi:10.1080/15384101.2014.998070 · Cited by 48
ATM mediated phosphorylation of CHD4 contributes to genome maintenance
Urquhart, A. J., Gatei, M. H., Richard, D. J., & Khanna, K. K. (2011) · Genome Integrity · doi:10.1186/2041-9414-2-1 · Cited by 45
Histone modifications in DNA damage response
Cao, L., Shen, C., & Zhu, W. (2016) · Science China Life Sciences · doi:10.1007/s11427-016-5011-z · Cited by 47
Untangling the crosstalk between BRCA1 and R-loops during DNA repair
Alonso, M. S. M., & Noordermeer, S. M. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab178 · Cited by 45
Klaric, J. A., Wüst, S., & Panier, S. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.668821 · Cited by 46
Fijen, C., & Rothenberg, E. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103170 · Cited by 43
The Role of hnRPUL1 Involved in DNA Damage Response Is Related to PARP1
Hong, Z., Jiang, J., Ma, J., Dai, S., Xu, T., Li, H. Z., & Yasui, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060208 · Cited by 45
ATRX and the replication of structured DNA
Clynes, D., & Gibbons, R. J. (2013) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2013.01.005 · Cited by 48
Dub3 controls DNA damage signalling by direct deubiquitination of H2AX
Delgado‐Diaz, M. R., Martín, Y., Berg, A., Freire, R., & Smits, V. A. J. (2014) · Molecular Oncology · doi:10.1016/j.molonc.2014.03.003 · Cited by 44
Nucleolar DNA Double-Strand Break Responses Underpinning rDNA Genomic Stability
van Sluis, M., & McStay, B. (2019) · Trends in Genetics · doi:10.1016/j.tig.2019.07.001 · Cited by 43
Metadata
- Authors
- Shanbhag, N. M., Rafalska-Metcalf, I. U., Balane-Bolivar, C., Janicki, S. M., & Greenberg, R. A.
- Affiliations
- Abramson Cancer Center (US)
- The Wistar Institute (US)
- Corresponding author
- Greenberg, Roger A.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 141
- Issue
- 6
- Pages
- 970-981
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC2920610
- OpenAlex
- W2135144687
- Cited by
- 737
- References
- 53
- Citations by year
- 2026: 30 · 2025: 28 · 2024: 45 · 2023: 45 · 2022: 49 · 2021: 71 · 2020: 51 · 2019: 45 · 2018: 38 · 2017: 49 · 2016: 45 · 2015: 44 · 2014: 46 · 2013: 54 · 2012: 42
- FWCI
- 19.66
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 1142 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Genentech
- National Cancer Institute (K08CA106597, T32CA115299, R01CA138835, 1-T32-CA-115299-01A2)
- 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
- ATM kinase, DNA double-strand breaks, transcriptional silencing, chromatin decondensation, RNA polymerase II elongation, RNF8, RNF168, USP16, E3 ubiquitin ligase, post-translational modification
- MeSH terms
- Chromatin, DNA Damage, DNA-Binding Proteins, Histones, Humans, Transcription, Genetic, Protein Serine-Threonine Kinases, Cell Cycle Proteins, Gene Silencing, Tumor Suppressor Proteins, Ubiquitin Thiolesterase, Cell Line, Tumor, DNA Breaks, Double-Stranded, Ubiquitination, 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
