The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.
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.
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
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]
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
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
Sorted by citations
Items 601–700 of 1,034
Therapeutic Implications for the Induced Levels of Chk1 in Myc-Expressing Cancer Cells
Höglund, A., Nilsson, L. M., Muralidharan, S. V., Hasvold, L. A., Merta, P. J., Rudelius, M., Nikolova, V. D., Keller, U. B., & Nilsson, J. A. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-11-1198 · Cited by 133
Sécher, T., Samba‐Louaka, A., Oswald, É., & Nougayrède, J. (2013) · PLoS ONE · doi:10.1371/journal.pone.0077157 · Cited by 146
Higher-order chromatin structure in DSB induction, repair and misrepair
Falk, M., Lukášová, E., & Kozubek, S. (2010) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2010.01.013 · Cited by 137
Wang, L., Balasubramanian, P., Chen, A. P., Kummar, S., Evrard, Y. A., & Kinders, R. J. (2016) · Seminars in Oncology · doi:10.1053/j.seminoncol.2016.06.004 · Cited by 132
Ionizing Radiation-Induced Epigenetic Modifications and Their Relevance to Radiation Protection
Belli, M., & Tabocchini, M. A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21175993 · Cited by 138
Detection of DNA Damage in Individual Cells by Analysis of Histone H2AX Phosphorylation
Olive, P. L. (2004) · Methods in cell biology · doi:10.1016/s0091-679x(04)75014-1 · Cited by 133
Chronic hypoxia compromises repair of DNA double-strand breaks to drive genetic instability
Kumareswaran, R., Ludkovski, O., Meng, A. X., Sykes, J. R., Pintilie, M., & Bristow, R. G. (2012) · Journal of Cell Science · doi:10.1242/jcs.092262 · Cited by 130
p53: The Attractive Tumor Suppressor in the Cancer Research Field
Ozaki, T., & Nakagawara, A. (2010) · BioMed Research International · doi:10.1155/2011/603925 · Cited by 138
Ouyang, G., Yao, L., Ruan, K., Song, G., Mao, Y., & Bao, S. (2009) · Cell Biology International · doi:10.1016/j.cellbi.2009.08.011 · Cited by 131
Antony, S., Agama, K., Miao, Z., Takagi, K., Wright, M. H., Robles, A. I., Varticovski, L., Nagarajan, M., Morrell, A. E., Cushman, M., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0938 · Cited by 132
ATR and H2AX cooperate in maintaining genome stability under replication stress
Chanoux, R. A., Yin, B., Urtishak, K. A., Asare, A., Bassing, C. H., & Brown, E. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m806739200 · Cited by 130
Histone modifications dictate specific biological readouts
Munshi, A., Shafi, G., Aliya, N., & Jyothy, A. (2009) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/s1673-8527(08)60094-6 · Cited by 136
Biochemical Kinetics Model of DSB Repair and Induction of γ-H2AX Foci by Non-homologous End Joining
Cucinotta, F. A., Pluth, J. M., Anderson, J. A., Harper, J. V., & O’Neill, P. (2008) · Radiation Research · doi:10.1667/rr1035.1 · Cited by 130
Chemoproteomic discovery of a covalent allosteric inhibitor of WRN helicase
Baltgalvis, K. A., Lamb, K. N., Symons, K. T., Wu, C.-C., Hoffman, M. A., Snead, A. N., Song, X., Glaza, T., Kikuchi, S., Green, J. C., et al. (2024) · Nature · doi:10.1038/s41586-024-07318-y · Cited by 134
Cytometric Assessment of Histone H2AX Phosphorylation
Huang, X., & Darżynkiewicz, Z. (2008) · Methods in molecular biology · doi:10.1385/1-59259-973-7:073 · Cited by 131
Atrx deficiency induces telomere dysfunction, endocrine defects, and reduced life span
Watson, L. A., Solomon, L. A., Li, J. R., Jiang, Y. Y., Edwards, M., Shin‐ya, K., Beier, F., & Bérubé, N. G. (2013) · Journal of Clinical Investigation · doi:10.1172/jci65634 · Cited by 133
Kang, J., Ferguson, D. O., Song, H., Bassing, C. H., Eckersdorff, M., Alt, F. W., & Xu, Y. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.2.661-670.2005 · Cited by 133
Many faces of NF-κB signaling induced by genotoxic stress
Wu, Z., & Miyamoto, S. (2007) · Journal of Molecular Medicine · doi:10.1007/s00109-007-0227-9 · Cited by 131
DNA repair: Spot(light)s on chromatin
Modesti, M., & Kanaar, R. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00112-9 · Cited by 130
Mutation of cancer driver MLL2 results in transcription stress and genome instabilityPreprint
Kantidakis, T., Saponaro, M., Mitter, R., Horswell, S. D., Kranz, A., Boeing, S., Aygün, O., Kelly, G. P., Matthews, N., Stewart, A., et al. (2016) · Genes & Development · doi:10.1101/gad.275453.115 · Cited by 130
Mechanisms of eukaryotic DNA double strand break repair
Cahill, D. (2006) · Frontiers in bioscience · doi:10.2741/1938 · Cited by 129
Chromatin modifications and DNA repair: beyond double-strand breaks
House, N. C. M., Koch, M. R., & Freudenreich, C. H. (2014) · Frontiers in Genetics · doi:10.3389/fgene.2014.00296 · Cited by 132
Woodbine, L. J., Brunton, H., Goodarzi, A. A., Shibata, A., & Jeggo, P. A. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr331 · Cited by 139
SET8 is degraded via PCNA-coupled CRL4(CDT2) ubiquitylation in S phase and after UV irradiation
Jørgensen, S., Eskildsen, M., Fugger, K., Hansen, L., Larsen, M. S. Y., Kousholt, A. N., Syljuåsen, R. G., Trelle, M. B., Jensen, O. N., Helin, K., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201009076 · Cited by 128
Vasko, M. R., Guo, C., & Kelley, M. R. (2005) · DNA repair · doi:10.1016/j.dnarep.2004.11.006 · Cited by 130
PANDITA, R. K., Sharma, G. G., Laszlo, A., Hopkins, K. M., Davey, S. K., Chakhparonian, M., Gupta, A. K. D., Wellinger, R. J., Zhang, J., Powell, S. N., et al. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.5.1850-1864.2006 · Cited by 130
The DNA Damage Response in Neurons: Die by Apoptosis or Survive in a Senescence-Like State?
Fielder, E., von Zglinicki, T., & Jurk, D. (2017) · Journal of Alzheimer's Disease · doi:10.3233/jad-161221 · Cited by 126
Role of Histone Modification in Chromatin Dynamics
Ito, T. (2007) · The Journal of Biochemistry · doi:10.1093/jb/mvm091 · Cited by 132
MEIOB Targets Single-Strand DNA and Is Necessary for Meiotic Recombination
Souquet, B., Abby, E., Hervé, R., Finsterbusch, F., Tourpin, S., Bouffant, R. L., Duquenne, C., Messiaen, S., Martini, E. M.-D., Bernardino-Sgherri, J., et al. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003784 · Cited by 137
Repair of DNA damage induced by accelerated heavy ions—A mini review
Okayasu, R. (2011) · International Journal of Cancer · doi:10.1002/ijc.26445 · Cited by 128
Heat Stress-Induced DNA Damage
Kantidze, O. L., Velichko, A. K., Luzhin, A. V., & Razin, S. V. (2016) · Acta Naturae · doi:10.32607/20758251-2016-8-2-75-78 · Cited by 128
Srougi, M. C., Reinicke, K. E., Bey, E. A., Spitz, D. R., & Boothman, D. A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603678200 · Cited by 128
Schwartz, M., Zlotorynski, E., Goldberg, M., Ozeri, E., Rahat, A., le Sage, C., Chen, B. P. C., Chen, D. J., Agami, R., & Kerem, B. (2005) · Genes & Development · doi:10.1101/gad.340905 · Cited by 134
Eukaryotic DNA damage checkpoint activation in response to double-strand breaks
Finn, K., Lowndes, N. F., & Grenon, M. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0875-3 · Cited by 127
Bellini, M., Mazzucchelli, S., Galbiati, E., Sommaruga, S., Fiandra, L., Truffi, M., Rizzuto, M. A., Colombo, M., Tortora, P., Corsi, F., et al. (2014) · Journal of Controlled Release · doi:10.1016/j.jconrel.2014.10.002 · Cited by 127
Lilley, C. E., Chaurushiya, M. S., Boutell, C., Everett, R. D., & Weitzman, M. D. (2011) · PLoS Pathogens · doi:10.1371/journal.ppat.1002084 · Cited by 129
Epigenetic mechanisms and genome stability
Putiri, E. L., & Robertson, K. D. (2010) · Clinical Epigenetics · doi:10.1007/s13148-010-0017-z · Cited by 133
Hein, J., Boichuk, S., Wu, J., Cheng, Y., Freire, R., Jat, P., Roberts, T. M., & Gjoerup, O. V. (2008) · Journal of Virology · doi:10.1128/jvi.01515-08 · Cited by 125
Role of novel histone modifications in cancer
Shanmugam, M. K., Arfuso, F., Arumugam, S., Chinnathambi, A., Jinsong, B., Warrier, S. R., Wang, L. Z., Kumar, A. P., Ahn, K. S., Sethi, G., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.23356 · Cited by 132
Yin, L., Liu, Y., Peng, Y., Peng, Y., Yu, X., Gao, Y., Yuan, B., Zhu, Q., Cao, T., He, L., et al. (2018) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-018-0810-7 · Cited by 129
P53 aggregation, interactions with tau, and impaired DNA damage response in Alzheimer’s disease
Farmer, K. M., Ghag, G., Puangmalai, N., Montalbano, M., Bhatt, N. N., & Kayed, R. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-01012-6 · Cited by 130
Pryde, F. E., Khalili, S., Robertson, K., Selfridge, J., Ritchie, A., Melton, D. W., Jullien, D., & Adachi, Y. (2005) · Journal of Cell Science · doi:10.1242/jcs.02336 · Cited by 131
Chromatin structure and DNA damage repair
Dinant, C., Houtsmuller, A. B., & Vermeulen, W. (2008) · Epigenetics & Chromatin · doi:10.1186/1756-8935-1-9 · Cited by 127
The in vitro genotoxicity of orthopaedic ceramic (Al2O3) and metal (CoCr alloy) particles
Tsaousi, A., Jones, E., & Case, C. P. (2010) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2010.01.012 · Cited by 126
XRN2 Links Transcription Termination to DNA Damage and Replication Stress
Morales, J. C., Richard, P., Patidar, P. L., Motea, E. A., Dang, T. T., Manley, J. L., & Boothman, D. A. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006107 · Cited by 131
DNA-PK Promotes the Mitochondrial, Metabolic, and Physical Decline that Occurs During Aging
Park, S. J., Gavrilova, O., Brown, A. L., Soto, J. E., Bremner, S. N., Kim, J., Xu, X., Yang, S., Um, J.-H., Koch, L. G., et al. (2017) · Cell Metabolism · doi:10.1016/j.cmet.2017.04.008 · Cited by 123
Retroviral DNA integration and the DNA damage response
Skalka, A. M., & Katz, R. A. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401573 · Cited by 126
Sidoli, S., Cheng, L., & Jensen, O. N. (2012) · Journal of Proteomics · doi:10.1016/j.jprot.2011.12.029 · Cited by 131
Kim, H.-J., Kim, J. H., Chie, E. K., DaYoung, P., Kim, I.-A., & Kim, I. (2012) · Radiation Oncology · doi:10.1186/1748-717x-7-39 · Cited by 125
Combination Therapy Targeting the Chk1 and Wee1 Kinases Shows Therapeutic Efficacy in Neuroblastoma
Russell, M. R., Levin, K., Rader, J., Belcastro, L. T., Li, Y., Martínez, D., Pawel, B., Shumway, S. D., Maris, J. M., & Cole, K. A. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-2669 · Cited by 127
Luo, M. H., Rosenke, K., Czornak, K., & Fortunato, E. A. (2006) · Journal of Virology · doi:10.1128/jvi.01670-06 · Cited by 129
Piya, S., Kornblau, S. M., Ruvolo, V. R., Mu, H. H., Ruvolo, P. P., McQueen, T. J., Davis, R. E., Hail, N., Kantarjian, H. M., Andreeff, M., et al. (2016) · Blood · doi:10.1182/blood-2016-01-692244 · Cited by 125
Rashid, M. B. M. A., Toh, T. B., Hooi, L., Silva, A., Zhang, Y., Tan, P. F., Teh, A. L., Karnani, N., Jha, S., Ho, C., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aan0941 · Cited by 127
Golding, S. E., Rosenberg, E., Khalil, A. A., McEwen, A., Holmes, M., Neill, S. J., Povirk, L. F., & Valerie, K. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314191200 · Cited by 124
Bouquet, F., Muller, C., & Salles, B. (2006) · Cell Cycle · doi:10.4161/cc.5.10.2799 · Cited by 132
Cell cycle control and beyond: emerging roles for the retinoblastoma gene family
Genovese, C., Trani, D., Caputi, M., & Claudio, P. P. (2006) · Oncogene · doi:10.1038/sj.onc.1209652 · Cited by 125
Daughtry, B. L., Rosenkrantz, J. L., Lazar, N. H., Fei, S. S., Redmayne, N., Torkenczy, K. A., Adey, A., Yan, M. Y., Gao, L., Park, B. S., et al. (2019) · Genome Research · doi:10.1101/gr.239830.118 · Cited by 122
DNA damage evaluated by γH2AX foci formation by a selective group of chemical/physical stressors
Zhou, C., Li, Z., Diao, H., Yu, Y., Zhu, W., Dai, Y., Chen, F. F., & Yang, J. J. (2006) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2005.12.004 · Cited by 124
ATM Acts Downstream of ATR in the DNA Damage Response Signaling of Bystander Cells
Burdak‐Rothkamm, S., Rothkamm, K., & Prise, K. M. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0545 · Cited by 124
Organotypic slice cultures of human glioblastoma reveal different susceptibilities to treatments
Merz, F., Gaunitz, F., Dehghani, F., Renner, C., Meixensberger, J., Gutenberg, A., Giese, A., Schopow, K., Hellwig, C. T., Schäfer, M., et al. (2013) · Neuro-Oncology · doi:10.1093/neuonc/not003 · Cited by 123
Bourton, E. C., Plowman, P. N., Smith, D., Arlett, C. F., & Parris, C. N. (2011) · International Journal of Cancer · doi:10.1002/ijc.25953 · Cited by 124
Su, C., Li, W., Tsao, L.-C., Wang, L.-C., Hsu, Y.-P., Wang, W., Liao, M.-C., Lee, C.-L., & Yeh, C. (2019) · ACS Nano · doi:10.1021/acsnano.8b09417 · Cited by 125
Zhang, Y., Gostissa, M., Hildebrand, D. G., Becker, M. S., Boboilă, C., Chiarle, R., Lewis, S. M., & Alt, F. W. (2010) · Advances in immunology · doi:10.1016/s0065-2776(10)06004-9 · Cited by 135
Oocytes Progress beyond Prophase in the Presence of DNA Damage
Marangos, P., & Carroll, J. (2012) · Current Biology · doi:10.1016/j.cub.2012.03.063 · Cited by 123
Early events in the mammalian response to DNA double-strand breaks
Riches, L. C., Lynch, A. M., & Gooderham, N. J. (2008) · Mutagenesis · doi:10.1093/mutage/gen039 · Cited by 124
Granzotto, A., Benadjaoud, M. A., Vogin, G., Devic, C., Ferlazzo, M. L., Bodgi, L., Pereira, S., Sonzogni, L., Forcheron, F., Viau, M., et al. (2015) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2015.11.013 · Cited by 138
Carter, R. J., Nickson, C. M., Thompson, J. M., Kacperek, A., Hill, M. A., & Parsons, J. L. (2017) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2017.11.012 · Cited by 123
An optimized method for measurement of gamma-H2AX in blood mononuclear and cultured cells
Muslimović, A., Ismail, I. H., Gao, Y., & Hammarsten, O. (2008) · Nature Protocols · doi:10.1038/nprot.2008.93 · Cited by 122
Piao, M. J., Kang, K. A., Zhang, R., Ko, D. O., Wang, Z. H., You, H. J., Kim, H. S., Kim, J. S., Kang, S. S., & Hyun, J. W. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.07.012 · Cited by 122
Chromatin remodeling finds its place in the DNA double-strand break response
Pandita, T. K., & Richardson, C. A. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn1071 · Cited by 128
Proximal tubule ATR regulates DNA repair to prevent maladaptive renal injury responses
Kishi, S., Brooks, C. R., Taguchi, K., Ichimura, T., Mori, Y., Akinfolarin, A., Gupta, N., Galichon, P., Elias, B. C., Suzuki, T., et al. (2019) · Journal of Clinical Investigation · doi:10.1172/jci122313 · Cited by 117
Valdiglesias, V., Costa, C., Sharma, V., Kılıç, G., Pásaro, E., Teixeira, J. P., Dhawan, A., & Laffón, B. (2013) · Food and Chemical Toxicology · doi:10.1016/j.fct.2013.04.010 · Cited by 121
Non-redundant Functions of ATM and DNA-PKcs in Response to DNA Double-Strand Breaks
Caron, P., Choudjaye, J., Clouaire, T., Bugler, B., Daburon, V., Aguirrebengoa, M., Mangeat, T., Iacovoni, J. S., Álvarez-Quilón, A., Cortés‐Ledesma, F., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.024 · Cited by 144
Karimian, A., Majidinia, M., Baghi, H. B., & Yousefi, B. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.01.003 · Cited by 125
ZEB1 confers chemotherapeutic resistance to breast cancer by activating ATM
Zhang, X., Zhang, Z., Zhang, Q., Zhang, Q., Sun, P., Xiang, R., Ren, G., & Yang, S. (2018) · Cell Death and Disease · doi:10.1038/s41419-017-0087-3 · Cited by 130
Structure and function of the histone chaperone FACT – Resolving FACTual issues
Gurova, K. V., Chang, H.-W., Valieva, M. E., Sandlesh, P., & Studitsky, V. M. (2018) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2018.07.008 · Cited by 121
Smart, D. J., Halicka, H. D., Schmuck, G., Traganos, F., Darżynkiewicz, Z., & Williams, G. M. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.03.005 · Cited by 121
Nabatiyan, A., & Krude, T. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.7.2853-2862.2004 · Cited by 121
Targeting DNA repair mechanisms in cancer
Furgason, J. M., & Bahassi, E. M. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.10.009 · Cited by 122
Choreography of recombination proteins during the DNA damage response
Lisby, M., & Rothstein, R. J. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.04.007 · Cited by 126
In vitro and in vivo genotoxicity of radiofrequency fields
Verschaeve, L., Juutilainen, J., Lagroye, I., Miyakoshi, J., Saunders, R. A., de Sèze, R., Tenforde, T., van Rongen, E., Veyret, B., & Xu, Z. (2010) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2010.10.001 · Cited by 121
H2AX chromatin structures and their response to DNA damage revealed by 4Pi microscopy
Bewersdorf, J., Bennett, B. T., & Knight, K. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0608709103 · Cited by 125
Roos, W. P., Baumgärtner, M., & Kaina, B. (2004) · Oncogene · doi:10.1038/sj.onc.1207080 · Cited by 122
Conserved and Nonconserved Proteins for Meiotic DNA Breakage and Repair in Yeasts
Young, J. A., Hyppa, R. W., & Smith, G. R. (2004) · Genetics · doi:10.1534/genetics.103.023762 · Cited by 120
Kim, S.-H., Kang, K.-A., Zhang, R., Piao, M.-J., Ko, D. O., Wang, Z., Chae, S., Kang, S.-S., Lee, K.-H., Kang, H., et al. (2008) · Acta Pharmacologica Sinica · doi:10.1111/j.1745-7254.2008.00878.x · Cited by 119
Rajendran, P., Kidane, A. I., Yu, T., Dashwood, W., Bisson, W. H., Löhr, C. V., Ho, E., Williams, D. E., & Dashwood, R. H. (2013) · Epigenetics · doi:10.4161/epi.24710 · Cited by 120
Nikolova, 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
Loss of the Epigenetic Tumor Suppressor SNF5 Leads to Cancer without Genomic Instability
McKenna, E. S., Sansam, C. G., Cho, Y., Greulich, H. E., Evans, J. A., Thom, C. S., Moreau, L. A., Biegel, J. A., Pomeroy, S. L., & Roberts, C. W. M. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00658-08 · Cited by 121
Gupta, A. K. D., Yang, Q., PANDITA, R. K., Hunt, C. R., Tao, X., Misri, S., Zeng, S., Pagan, J. K., Jeffery, J., Puc, J., et al. (2009) · Cell Cycle · doi:10.4161/cc.8.14.8947 · Cited by 118
Dmitrieva, N. I., Cai, Q., & Burg, M. B. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308463100 · Cited by 119
Zimmerman, E. S., Chen, J., Andersen, J. L., Ardon, O., DeHart, J. L., Blackett, J. L., Choudhary, S. K., Camerini, D., Nghiem, P., & Planelles, V. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.21.9286-9294.2004 · Cited by 124
γH2AX foci as a measure of DNA damage: A computational approach to automatic analysis
Ivashkevich, A. N., Martin, O. A., Smith, A. J., Redon, C. E., Bonner, W. M., Martin, R. F., & Lobachevsky, P. N. (2011) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2010.12.015 · Cited by 124
Self-citationThe genesis of cerebellar interneurons and the prevention of neural DNA damage require XRCC1
Lee, Y., Katyal, S., Li, Y., El‐Khamisy, S. F., Russell, H. R., Caldecott, K. W., & McKinnon, P. J. (2009) · Nature Neuroscience · doi:10.1038/nn.2375 · Cited by 115
Zhang, X., Succi, J., Feng, Z., Prithivirajsingh, S., Story, M. D., & Legerski, R. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.9207-9220.2004 · Cited by 119
Ha, K., Lee, G. E., Palii, S. S., Brown, K. D., Takeda, Y., Liu, K., Bhalla, K. N., & Robertson, K. D. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq451 · Cited by 127
DDR-mediated crosstalk between DNA-damaged cells and their microenvironment
Malaquin, N., Carrier-Leclerc, A., Dessureault, M., & Rodier, F. (2015) · Frontiers in Genetics · doi:10.3389/fgene.2015.00094 · Cited by 124
MiR-124 Radiosensitizes Human Colorectal Cancer Cells by Targeting PRRX1
Zhang, Y., Zheng, L., Huang, J., Gao, F., Lin, X., He, L., Li, D., Li, Z., Ding, Y., & Chen, L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093917 · Cited by 119
Sensing core histone phosphorylation — A matter of perfect timing
Sawicka, A., & Seiser, C. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.04.013 · Cited by 129
The Hippo Pathway Prevents YAP/TAZ-Driven Hypertranscription and Controls Neural Progenitor Number
Lavado, A., Park, J. Y., Paré, J., Finkelstein, D., Pan, H., Xu, B., Fan, Y., Kumar, R. P., Neale, G. A. M., Kwak, Y. D., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.09.021 · Cited by 119
MORC2 regulates DNA damage response through a PARP1-dependent pathway
Zhang, L., & Li, D. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz545 · Cited by 119
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
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
