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DNA Double-stranded Breaks Induce Histone H2AX Phosphorylation on Serine 139
Open accessAbstract
When mammalian cell cultures or mice are exposed to ionizing radiation in survivable or lethal amounts, novel mass components are found in the histone H2A region of two-dimensional gels. Collectively referred to as gamma, these components are formed in vivo by several procedures that introduce double-stranded breaks into DNA. gamma-Components, which appeared to be the only major novel components detected by mass or 32PO4 incorporation on acetic acid-urea-Triton X-100-acetic acid-urea-cetyltrimethylammonium bromide or SDS-acetic acid-urea-cetyltrimethylammonium bromide gels after exposure of cells to ionizing radiation, are shown to be histone H2AX species that have been phosphorylated specifically at serine 139. gamma-H2AX appears rapidly after exposure of cell cultures to ionizing radiation; half-maximal amounts are reached by 1 min and maximal amounts by 10 min. At the maximum, approximately 1% of the H2AX becomes gamma-phosphorylated per gray of ionizing radiation, a finding that indicates that 35 DNA double-stranded breaks, the number introduced by each gray into the 6 x 10(9) base pairs of a mammalian G1 genome, leads to the gamma-phosphorylation of H2AX distributed over 1% of the chromatin. Thus, about 0.03% of the chromatin appears to be involved per DNA double-stranded break. This value, which corresponds to about 2 x 10(6) base pairs of DNA per double-stranded break, indicates that large amounts of chromatin are involved with each DNA double-stranded break. Thus, gamma-H2AX formation is a rapid and sensitive cellular response to the presence of DNA double-stranded breaks, a response that may provide insight into higher order chromatin structures.
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In the citing paper
“The variant histone H2AX is phosphorylated at serine 139 (forming ␥H2AX) in the vicinity of single-stranded DNA (ssDNA), DNA single-or double-strand breaks (SSBs and DSBs, respectively) [38][39][40].”
From Gap-filling and bypass at the replication fork are both active mechanisms for tolerance of low-dose ultraviolet-induced DNA damage in the human genome (2014) · cites this paper as [38]
Experimental — accuracy not yet measuredIn the citing paper
“phosphoS139 H2AX, a well-established marker for double-stranded DNA breaks”
From Aggrecan, link protein and tenascin-R are essential components of the perineuronal net to protect neurons against iron-induced oxidative stress (2014) · cites this paper as [58]
In the citing paper
“aged HSCs and muscle stem cells (also called satellite cells) show an increased number of nuclear foci that stain for the phosphorylated form of the variant histone H2A.X (γH2A.X)36–38, which serves as a marker of DNA double-strand breaks39.”
From Stem cell aging: mechanisms, regulators and therapeutic opportunities (2014) · cites this paper as [39]
In the citing paper
“Experimental results have indicated that γ-H2AX foci colocalize with DSB repair factors (such as Rad51, BRCA1, Mre11, Rad50, and Nbs1) [86, 91] and participate the repair of DSBs [85, 89, 90].”
From Markers of cellular senescence. Telomere shortening as a marker of cellular senescence (2016) · cites this paper as [90]
In the citing paper
“Thus, γ-H2AX foci reflect – not only age-dependent irreversible DSBs (including telomere shortening) – but also temporal accumulation of DSBs, which may be a result of massive ionizing radiation (1 Gy of ionizing radiation, about 2 × 106 bp of DDBs, triggers phosphorylation of about 1% of the H2AX) [90].”
From Markers of cellular senescence. Telomere shortening as a marker of cellular senescence (2016) · cites this paper as [90]
In the citing paper
“As an ATM substrate, histone H2AX is phosphorylated at Serine 139, which is referred to γ-H2AX and prevents DSBs from processing into chromosomal translocations [58, 59].”
From Functional interplay between ATM/ATR-mediated DNA damage response and DNA repair pathways in oxidative stress (2014) · cites this paper as [58]
In the citing paper
“Phosphorylation of H2AX and S/T-Q sites, both of which are targets of ATM, occurs rapidly after DNA breaks.9,37,38”
From Mdmx promotes genomic instability independent of p53 and Mdm2 (2015) · cites this paper as [37]
In the citing paper
“WB analyses on postmortem human samples correlate those results with a significant increase in a phosphorylated form of the histone variant H2AX (γ-H2AX), a commonly used marker of cell senescence that indicates double-stranded DNA breaks [94] (Additional file 1: Fig. S8).”
From Senescence-related impairment of autophagy induces toxic intraneuronal amyloid-β accumulation in a mouse model of amyloid pathology (2023) · cites this paper as [94]
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Citations
Cites
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466
Friedberg, E. C., Walker, G. C., Siede, W., Wood, R. D., Schultz, R. A., & Ellenberger, T. (2005) · doi:10.1128/9781555816704 · Cited by 5,683
A Single Ataxia Telangiectasia Gene with a Product Similar to PI-3 Kinase
Savitsky, K., Bar-Shira, A., Gilad, S., Rotman, G., Ziv, Y., Vanagaite, L., Tagle, D. A., Smith, S., Uziel, T., Sfez, S., et al. (1995) · Science · doi:10.1126/science.7792600 · Cited by 2,785
Bootsma, D., & Hoeijmakers, J. H. J. (1996) · Trends in Genetics · doi:10.1016/0168-9525(96)81408-9 · Cited by 2,285
Brownell, J. E., Zhou, J., Ranalli, T. A., Kobayashi, R., Edmondson, D. G., Dent, S., & Allis, C. D. (1996) · Cell · doi:10.1016/s0092-8674(00)81063-6 · Cited by 1,636
Requirement for Ku80 in growth and immunoglobulin V(D)J recombination
Nussenzweig, A., Chen, C., Soares, V. D. C., Sanchez, M., Sokol, K. A., Nussenzweig, M. C., & Li, G. C. (1996) · Nature · doi:10.1038/382551a0 · Cited by 662
The Complexity of DNA Damage: Relevance to Biological Consequences
Ward, J. F. (1994) · International Journal of Radiation Biology · doi:10.1080/09553009414551401 · Cited by 633
DNA-Dependent Kinase (p350) as a Candidate Gene for the Murine SCID Defect
Kirchgessner, C. U., Patil, C. K., Evans, J., Cuomo, C. A., Fried, L. M., Carter, T., Oettinger, M. A., & Brown, J. M. (1995) · Science · doi:10.1126/science.7855601 · Cited by 609
Histone Phosphorylation and Chromatin Structure during Mitosis in Chinese Hamster Cells
Gurley, L. R., D'Anna, J. A., Barham, S. S., Deaven, L. L., & Tobey, R. A. (1978) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1978.tb12135.x · Cited by 534
Absence of p350 Subunit of DNA-Activated Protein Kinase from a Radiosensitive Human Cell Line
Lees‐Miller, S. P., Godbout, R., Chan, D. W., Weinfeld, M., Day, R. S., Barron, G. M., & Allalunis‐Turner, J. (1995) · Science · doi:10.1126/science.7855602 · Cited by 529
Research works printed but not linked: 1
- West, 1981, Nucleic Acids Res., 20, 4671
Cited by
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Items 401–500 of 1,034
Downregulation of XPF–ERCC1 enhances cisplatin efficacy in cancer cells☆
Arora, S., Kothandapani, A., Tillison, K., Kalman‐Maltese, V., & Patrick, S. M. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.03.010 · Cited by 182
Therapeutic targeting of Chk1 in NSCLC stem cells during chemotherapy
Bartucci, M., Svensson, S., Romania, P., Dattilo, R., Patrizii, M., Signore, M., Navarra, S., Lotti, F., Biffoni, M., Pilozzi, E., et al. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.170 · Cited by 181
Derijck, A. A. H. A., van der Heijden, G. W., Giele, M., Philippens, M. E. P., & de Boer, P. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn090 · Cited by 182
Mus81-mediated DNA cleavage resolves replication forks stalled by topoisomerase I–DNA complexes
Regairaz, M., Zhang, Y., Fu, H., Agama, K., Tata, N., Agrawal, S., Aladjem, M. I., & Pommier, Y. G. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201104003 · Cited by 181
Lloyd, R. L., Wijnhoven, P. W. G., Ramos‐Montoya, A., Wilson, Z., Illuzzi, G., Falenta, K., Jones, G. N., James, N. H., Chabbert, C. D., Stott, J., et al. (2020) · Oncogene · doi:10.1038/s41388-020-1328-y · Cited by 185
Chromatin compartmentalization regulates the response to DNA damage
Arnould, C., Rocher, V., Saur, F., Bader, A. S., Muzzopappa, F., Collins, S., Lesage, E., Bozec, B. L., Puget, N., Clouaire, T., et al. (2023) · Nature · doi:10.1038/s41586-023-06635-y · Cited by 187
Telomeres and meiosis in health and disease
Scherthan, H. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6463-2 · Cited by 176
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
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 181
A Current Overview of the Biological and Cellular Effects of Nanosilver
Cameron, S. J., Hosseinian, F. S., & Willmore, W. G. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19072030 · Cited by 186
Maidarti, M., Anderson, R. A., & Telfer, E. E. (2020) · Cells · doi:10.3390/cells9010200 · Cited by 184
Histone H3 and the Histone Acetyltransferase Hat1p Contribute to DNA Double-Strand Break Repair
Qin, S., & Parthun, M. R. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.23.8353-8365.2002 · Cited by 177
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
Pogribny, I. P., Koturbash, I., Tryndyak, V., Hudson, D., Stevenson, S. M. L., Sedelnikova, O. A., Bonner, W. M., & Kovalchuk, O. (2005) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-05-0074 · Cited by 181
Self-citationRolleston, H. D. (2009) · Cambridge University Press eBooks · doi:10.1017/cbo9780511693632.005 · Cited by 179
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Wang, C., Wang, D., Dai, T., Xu, P., Wu, P., Zou, Y., Yang, P., Hu, J., Li, Y., & Cheng, Y. (2018) · Advanced Functional Materials · doi:10.1002/adfm.201802127 · Cited by 178
Radiation-induced DNA damage and delayed induced genomic instability
Suzuki, K., Ojima, M., Kodama, S., & Watanabe, M. (2003) · Oncogene · doi:10.1038/sj.onc.1206881 · Cited by 184
Synthetic RNA-Based Immunomodulatory Gene Circuits for Cancer Immunotherapy
Nissim, L., Wu, M.-R., Pery, E., Binder-Nissim, A., Suzuki, H. I., Stupp, D., Wehrspaun, C. C., Tabach, Y., Sharp, P. A., & Lu, T. K. (2017) · Cell · doi:10.1016/j.cell.2017.09.049 · Cited by 179
Hypoxia induced LUCAT1/PTBP1 axis modulates cancer cell viability and chemotherapy response
Huan, L., Guo, T., Wu, Y., Xu, L., Huang, S., Xu, Y., Liang, L., & He, X. (2020) · Molecular Cancer · doi:10.1186/s12943-019-1122-z · Cited by 177
Telomerase insufficiency in rheumatoid arthritis
Fujii, H., Shao, L., Colmegna, I., Goronzy, J. J., & Weyand, C. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811332106 · Cited by 172
PARP-2 sustains erythropoiesis in mice by limiting replicative stress in erythroid progenitors
Farrés, J., Llacuna, L., Martín‐Caballero, J., Martínez, C. M., Lozano, J. J., Ampurdanés, C., Lopez-Contreras, A. J., Florensa, L., Navarro, J., Ottina, E., et al. (2014) · Cell Death and Differentiation · doi:10.1038/cdd.2014.202 · Cited by 186
Epigenetic Modifications in Double-Strand Break DNA Damage Signaling and Repair
Rossetto, D., Truman, A. W., Kron, S. J., & Côté, J. (2010) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-0513 · Cited by 183
Candidate protein biodosimeters of human exposure to ionizing radiation
Marchetti, F., Coleman, M. A., Jones, I. M., & Wyrobek, A. J. (2006) · International Journal of Radiation Biology · doi:10.1080/09553000600930103 · Cited by 176
Histone H2A variants and the inactive X chromosome: identification of a second macroH2A variant
Chadwick, B. P. (2001) · Human Molecular Genetics · doi:10.1093/hmg/10.10.1101 · Cited by 174
Genomic integrity and the ageing brain
Chow, H.-M., & Herrup, K. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn4020 · Cited by 174
DNA Damage Response in Plants: Conserved and Variable Response Compared to Animals
Yoshiyama, K., Sakaguchi, K., & Kimura, S. (2013) · Biology · doi:10.3390/biology2041338 · Cited by 182
Arya, G., Mallaredy, V., Acharya, S., & Sahoo, S. K. (2011) · Nanomedicine Nanotechnology Biology and Medicine · doi:10.1016/j.nano.2011.03.009 · Cited by 174
Greater Than the Sum of Parts: Complexity of the Dynamic Epigenome
Soshnev, A. A., Josefowicz, S. Z., & Allis, C. D. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.05.004 · Cited by 181
Checkpoint Responses to DNA Double-Strand Breaks
Waterman, D. P., Haber, J. E., & Smolka, M. B. (2020) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-011520-104722 · Cited by 184
Reduced Mcm2 Expression Results in Severe Stem/Progenitor Cell Deficiency and Cancer
Pruitt, S. C., Bailey, K. J., & Freeland, A. L. (2007) · Stem Cells · doi:10.1634/stemcells.2007-0483 · Cited by 175
DNA Damage Responses in Human Induced Pluripotent Stem Cells and Embryonic Stem Cells
Momčilović, O., Knobloch, L., Fornsaglio, J. L., Varum, S., Easley, C. A., & Schatten, G. P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013410 · Cited by 182
Preclinical Evaluation of the WEE1 Inhibitor MK-1775 as Single-Agent Anticancer Therapy
Guertin, A. D., Li, J., Liu, Y., Hurd, M. S., Schuller, A., Long, B., Hirsch, H., Feldman, I., Benita, Y., Toniatti, C., et al. (2013) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0025 · Cited by 171
CRISPR-Cas9D10A nickase-based genotypic and phenotypic screening to enhance genome editing
Chiang, T.-W. W., le Sage, C., Larrieu, D., Demir, M., & Jackson, S. P. (2016) · Scientific Reports · doi:10.1038/srep24356 · Cited by 171
Suttkus, A., Rohn, S., Weigel, S., Glöckner, P., Arendt, T., & Morawski, M. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.25 · Cited by 168
Systematic identification of fragile sites via genome-wide location analysis of γ-H2AX
Szilard, R. K., Jacques, P., Laramée, L., Cheng, B., Galicia, S., Bataille, A. R., Yeung, M., Mendez, M., Bergeron, M., Robert, F., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1754 · Cited by 167
Mammalian DNA repair: HATs and HDACs make their mark through histone acetylation
Gong, F., & Miller, K. M. (2013) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2013.07.002 · Cited by 175
Rassool, F. V., Gaymes, T. J., Omidvar, N., Brady, N., Beurlet, S., Pla, M., Reboul, M., Lea, N. C., Chomienne, C., Thomas, N. S. B., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-4807 · Cited by 171
Mechanisms and measurements of nanomaterial-induced oxidative damage to DNA
Petersen, E. J., & Nelson, B. C. (2010) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-010-3881-7 · Cited by 175
Use of the γ-H2AX Assay to Investigate DNA Repair Dynamics Following Multiple Radiation Exposures
Mariotti, L., Pirovano, G., Savage, K. I., Ghita, M., Ottolenghi, A., Prise, K. M., & Schettino, G. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079541 · Cited by 186
Complex DNA Damage: A Route to Radiation-Induced Genomic Instability and Carcinogenesis
Mavragani, I. V., Nikitaki, Z., Souli, M., Aziz, A., Nowsheen, S., Aziz, K., Rogakou, E. P., & Georgakilas, A. G. (2017) · Cancers · doi:10.3390/cancers9070091 · Cited by 184
Self-citationLow-dose radiation: Thresholds, bystander effects, and adaptive responses
Bonner, W. M. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1031538100 · Cited by 171
Self-citationEvidence of DNA damage in Alzheimer disease: phosphorylation of histone H2AX in astrocytes
Myung, N.-H., Zhu, X., Kruman, I. I., Castellani, R. J., Petersen, R. B., Siedlak, S. L., Perry, G., Smith, M. A., & Lee, H.-G. (2008) · AGE · doi:10.1007/s11357-008-9050-7 · Cited by 170
H2AX Is Required for Cell Cycle Arrest via the p53/p21 Pathway
Fragkos, M., Jurvansuu, J., & Beard, P. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01830-08 · Cited by 176
Chen, T., & Wong, Y. S. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8329-2 · Cited by 170
Three steps to the immortality of cancer cells: senescence, polyploidy and self-renewal
Erenpreisa, J. A., & Cragg, M. S. (2013) · Cancer Cell International · doi:10.1186/1475-2867-13-92 · Cited by 177
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Prabhu, K. S., Kuttikrishnan, S., Ahmad, N., Habeeba, U., Mariyam, Z., Suleman, M., Bhat, A. A., & Shahab Uddin, M. S. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.116663 · Cited by 186
Toduka, Y., Toyooka, T., & Ibuki, Y. (2012) · Environmental Science & Technology · doi:10.1021/es300433x · Cited by 170
Nuclear Localization of p38 MAPK in Response to DNA Damage
Wood, C. D., Thornton, T. M., Sabio, G., Davis, R. J., & Rincón, M. (2009) · International Journal of Biological Sciences · doi:10.7150/ijbs.5.428 · Cited by 177
γ-H2AX Foci as a Biomarker for Patient X-Ray Exposure in Pediatric Cardiac Catheterization
Beels, L., Bacher, K., Wolf, D. D., Werbrouck, J., & Thierens, H. M. (2009) · Circulation · doi:10.1161/circulationaha.109.880385 · Cited by 169
The RAG Recombinase Dictates Functional Heterogeneity and Cellular Fitness in Natural Killer Cells
Karo, J. M., Schatz, D. G., & Sun, J. C.-Y. (2014) · Cell · doi:10.1016/j.cell.2014.08.026 · Cited by 171
Both telomeric and non-telomeric DNA damage are determinants of mammalian cellular senescence
Nakamura, A. J., Chiang, Y. J., Hathcock, K. S., Horikawa, I., Sedelnikova, O. A., Hodes, R. J., & Bonner, W. M. (2008) · Epigenetics & Chromatin · doi:10.1186/1756-8935-1-6 · Cited by 168
Self-citationLe, O. N. L., Rodier, F., Fontaine, F., Coppe, J., Campisi, J., DeGregori, J., Laverdière, C., Kokta, V., Haddad, E., & Beauséjour, C. M. (2010) · Aging Cell · doi:10.1111/j.1474-9726.2010.00567.x · Cited by 168
Syljuåsen, R. G., Jensen, S., Bártek, J., & Lukas, J. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-2144 · Cited by 174
Increased frequency of homologous recombination and T‐DNA integration in Arabidopsis CAF‐1 mutants
Endo, M., Ishikawa, Y., Osakabe, K., Nakayama, S., Kaya, H., Araki, T., Shibahara, K., Abe, K., Ichikawa, H., Valentine, L., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601434 · Cited by 168
Riches, L. C., Trinidad, A. G., Hughes, G., Jones, G. N., Hughes, A. M., Thomason, A. G., Gavine, P. R., Cui, A., Ling, S., Stott, J., et al. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-18-1394 · Cited by 168
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Expression and purification of recombinant human histones
Tanaka, Y., Tawaramoto-Sasanuma, M., Kawaguchi, S., Ohta, T., Yoda, K., Kurumizaka, H., & Yokoyama, S. (2004) · Methods · doi:10.1016/j.ymeth.2003.10.024 · Cited by 165
Li, S., Song, Y., Quach, C., Guo, H., Jang, G.-B., Maazi, H., Zhao, S., Sands, N. A., Liu, Q., In, G. K., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09634-8 · Cited by 173
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Nitta, M., Kobayashi, O., Honda, S., Hirota, T., Kuninaka, S., Marumoto, T., Ushio, Y., & Saya, H. (2004) · Oncogene · doi:10.1038/sj.onc.1207873 · Cited by 166
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Gruhne, B., Sompallae, R. R., & Masucci, M. G. (2009) · Oncogene · doi:10.1038/onc.2009.258 · Cited by 172
Sensenig, R. L., Kalghatgi, S. R., Cerchar, E., Fridman, G., Shereshevsky, A., Torabi, B., Arjunan, K. P., Podolsky, E. R., Fridman, A., Friedman, G., et al. (2010) · Annals of Biomedical Engineering · doi:10.1007/s10439-010-0197-x · Cited by 170
RetractedFarg, M. A., Konopka, A., Soo, K. Y., Ito, D., & Atkin, J. D. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx170 · Cited by 173
Chou, D. M., & Elledge, S. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609251103 · Cited by 166
Alpatov, R., Lesch, B. J., Nakamoto-Kinoshita, M., Blanco, M. A., Chen, S., Stützer, A., Armache, K., Simon, M. D., Xu, C., Ali, M., et al. (2014) · Cell · doi:10.1016/j.cell.2014.03.040 · Cited by 175
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miR-17 and miR-20a temper an E2F1-induced G1 checkpoint to regulate cell cycle progression
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Horn, S., Barnard, S. G. R., & Rothkamm, K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025113 · Cited by 164
Jarvis, I. W. H., Dreij, K., Mattsson, Å., Jernström, B., & Stenius, U. (2014) · Toxicology · doi:10.1016/j.tox.2014.03.012 · Cited by 163
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Ritzel, R. M., Doran, S. J., Glaser, E. P., Meadows, V. E., Faden, A. I., Stoica, B. A., & Loane, D. J. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.02.010 · Cited by 156
An, J., Huang, Y.-C., Xu, Q.-Z., Zhou, L.-J., Shang, Z., Huang, B., Wang, Y., Liu, X.-D., Wu, D.-C., & Zhou, P. (2010) · BMC Molecular Biology · doi:10.1186/1471-2199-11-18 · Cited by 177
Geng, L., Cuneo, K. C., Fu, A., Tu, T., Atadja, P. W., & Hallahan, D. E. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-0049 · Cited by 163
Histone variants--the structure behind the function
Ausió, J. (2006) · Briefings in Functional Genomics and Proteomics · doi:10.1093/bfgp/ell020 · Cited by 163
Identification and functional analysis of TopBP1 and its homologs
Garcia, V., Furuya, K., & Carr, A. M. (2005) · DNA Repair · doi:10.1016/j.dnarep.2005.04.001 · Cited by 158
Hou, J., Han, Z.-P., Jing, Y.-Y., Yang, X., Zhang, S.-S., Sun, K., Hao, C., Meng, Y., Yu, F.-H., Liu, X.-Q., et al. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.338 · Cited by 163
Biological Effects of Proton Radiation: What We Know and Don't Know
Girdhani, S., Sachs, R. K., & Hlatky, L. (2013) · Radiation Research · doi:10.1667/rr2839.1 · Cited by 162
Brar, S. S., Watson, M., & Diaz, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403503200 · Cited by 161
Inhibition of Hsp90 Compromises the DNA Damage Response to Radiation
Dote, H., Burgan, W. E., Camphausen, K. A., & Tofilon, P. J. (2006) · Cancer Research · doi:10.1158/0008-5472.can-06-2181 · Cited by 161
Georgoulis, A., Vorgias, C. E., Chrousos, G. P., & Rogakou, E. P. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18091979 · Cited by 172
Self-citationMetabolic control of regulatory T cell (Treg) survival and function by Lkb1
He, N., Fan, W., Henriquez, B., Yu, R. T., Atkins, A. R., Liddle, C., Zheng, Y., Downes, M., & Evans, R. M. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1715363114 · Cited by 166
SPOCD1 is an essential executor of piRNA-directed de novo DNA methylation
Zoch, A., Auchynnikava, T., Berrens, R. V., Kabayama, Y., Schöpp, T., Heep, M., Vasiliauskaitė, L., Perez-Rico, Y. A., Cook, A. G., Shkumatava, A., et al. (2020) · Nature · doi:10.1038/s41586-020-2557-5 · Cited by 164
Rübe, C. E., Grudzenski, S., Kühne, M., Dong, X., Rief, N., Löbrich, M., & Rübe, C. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-5147 · Cited by 158
Olier, M., Marcq, I., Salvador–Cartier, C., Sécher, T., Dobrindt, U., Boury, M., Bacquie, V., Pénary, M., Gaultier, E., Nougayrède, J., et al. (2012) · Gut Microbes · doi:10.4161/gmic.21737 · Cited by 173
Repair of HZE-Particle-Induced DNA Double-Strand Breaks in Normal Human Fibroblasts
Asaithamby, A., Uematsu, N., Chatterjee, A., Story, M. D., Burma, S., & Chen, D. J. (2008) · Radiation Research · doi:10.1667/rr1165.1 · Cited by 159
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
MiR-106b induces cell radioresistance via the PTEN/PI3K/AKT pathways and p21 in colorectal cancer
Zheng, L., Zhang, Y., Liu, Y., Zhou, M., Lu, Y., Li, Y., Zhang, C., Hong, M., Wang, S., & Li, X. (2015) · Journal of Translational Medicine · doi:10.1186/s12967-015-0592-z · Cited by 159
Couëdel, C., Mills, K. D., Barchi, M., Shen, L., Olshen, A. B., Johnson, R. D., Nussenzweig, A., Essers, J., Kanaar, R., Li, G. C., et al. (2004) · Genes & Development · doi:10.1101/gad.1209204 · Cited by 159
Sampson, N., Kozieł, R., Zenzmaier, C., Bubendorf, L., Plas, E., Jansen‐Dürr, P., & Berger, P. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0340 · Cited by 163
Multi-phenotype CRISPR-Cas9 Screen Identifies p38 Kinase as a Target for Adoptive Immunotherapies
Gurusamy, D., Henning, A. N., Yamamoto, T. N., Yu, Z., Zacharakis, N., Krishna, S., Kishton, R. J., Vodnala, S. K., Eidizadeh, A., Jia, L., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.05.004 · Cited by 159
Ronen, A., & Glickman, B. W. (2001) · Environmental and Molecular Mutagenesis · doi:10.1002/em.1033 · Cited by 161
Biological Imaging of Heavy Charged-Particle Tracks
Jakob, B., Scholz, M., & Taucher-Scholz, G. (2003) · Radiation Research · doi:10.1667/0033-7587(2003)159[0676:biohct]2.0.co;2 · Cited by 156
Hexavalent Chromium-Induced DNA Damage and Repair Mechanisms
Wise, S. S., Holmes, A. L., & Wise, J. P. (2008) · Reviews on Environmental Health · doi:10.1515/reveh.2008.23.1.39 · Cited by 157
Highly Multiplexed Immunohistochemical MALDI-MS Imaging of Biomarkers in Tissues
Yagnik, G. B., Liu, Z., Rothschild, K. J., & Lim, M. J. (2021) · Journal of the American Society for Mass Spectrometry · doi:10.1021/jasms.0c00473 · Cited by 167
γH2AX as a molecular marker of aging and disease
Mah, L.-J., El‐Osta, A., & Karagiannis, T. C. (2010) · Epigenetics · doi:10.4161/epi.5.2.11080 · Cited by 156
Gwak, H., Kim, T. H., Jo, G. H., Kim, Y., Kwak, H., Kim, J. H., Yin, J., Yoo, H., Lee, S. H., & Park, J. B. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047449 · Cited by 160
53BP1, an activator of ATM in response to DNA damage
Mochan, T. A., Venere, M., DiTullio, R. A., & Halazonetis, T. D. (2004) · DNA repair · doi:10.1016/j.dnarep.2004.03.017 · Cited by 162
Characterization of the Stability and Folding of H2A.Z Chromatin Particles
Abbott, D. W., Ivanova, V. S., Wang, X., Bonner, W. M., & Ausió, J. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m108217200 · Cited by 155
Self-citationMechanisms of ATP dependent chromatin remodeling
Gangaraju, V. K., & Bartholomew, B. (2007) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2006.08.015 · Cited by 154
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
Metadata
- Authors
- Rogakou, E. P., Pilch, D. R., Orr, A. H., Ivanova, V. S., & Bonner, W. M.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Bonner, William M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-03
- Volume
- 273
- Issue
- 10
- Pages
- 5858-5868
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1985775217
- Cited by
- 5,438
- References
- 41
- Citations by year
- 2026: 150 · 2025: 169 · 2024: 202 · 2023: 214 · 2022: 202 · 2021: 256 · 2020: 283 · 2019: 240 · 2018: 249 · 2017: 257 · 2016: 272 · 2015: 295 · 2014: 261 · 2013: 278 · 2012: 292
- FWCI
- 5.94
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Effects of Radiation Exposure
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- DNA double-strand breaks, histone H2AX, γH2AX, ionizing radiation, chromatin structure, DNA damage response, phosphorylation kinetics
- MeSH terms
- Amino Acid Sequence, Animals, Cells, Cultured, Chromatin, DNA, Gamma Rays, Histones, Mice, Inbred Strains, Molecular Sequence Data, Nuclear Proteins, Peptide Fragments, Phosphorylation, Phosphoserine, Protein Kinases, Recombinant Proteins, Whole-Body Irradiation, Electrophoresis, Gel, Two-Dimensional, Mice
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