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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 701–800 of 1,034
The phosphorylation status of PAS‐B distinguishes HIF‐1α from HIF‐2α in NBS1 repression
To, K. K. W., Sedelnikova, O. A., Samons, M., Bonner, W. M., & Huang, E. L. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601369 · Cited by 121
Self-citationPontarin, G., Ferraro, P., Bee, L., Reichard, P. A., & Bianchi, V. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1211289109 · Cited by 117
C14ORF39/SIX6OS1 is a constituent of the synaptonemal complex and is essential for mouse fertility
Gómez-H, L., Felipe‐Medina, N., Sánchez‐Martín, M., Davies, O. R., Ramos, I., García‐Tuñón, I., de Rooij, D. G., Dereli, I., Tóth, A., Barbero, J. L., et al. (2016) · Nature Communications · doi:10.1038/ncomms13298 · Cited by 121
Morrison, A. J., Kim, J., Person, M. D., Highland, J., Xiao, J., Wehr, T. S., Hensley, S. C., Bao, Y., Shen, J., Collins, S. R., et al. (2007) · Cell · doi:10.1016/j.cell.2007.06.010 · Cited by 119
Uracil DNA Glycosylase Activity Is Dispensable for Immunoglobulin Class Switch
Begum, N. A., Kinoshita, K., Kakazu, N., Muramatsu, M., Nagaoka, H., Shinkura, R., Biniszkiewicz, D., Boyer, L. A., Jaenisch, R., & Honjo, T. (2004) · Science · doi:10.1126/science.1098444 · Cited by 116
Koturbash, I., Loree, J. M., Kutanzi, K. R., Koganow, C., Pogribny, I. P., & Kovalchuk, O. (2008) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2007.09.039 · Cited by 118
de Vries, J. F., Zwaan, C. M., de Bie, M., Voerman, J. S. A., den Boer, M. L., van Dongen, J. J. M., & van der Velden, V. H. J. (2011) · Leukemia · doi:10.1038/leu.2011.206 · Cited by 116
Wang, Z. H., Kang, K. A., Zhang, R., Piao, M. J., Jo, S. H., Kim, J. S., Kang, S. S., Lee, J. S., Park, D. H., & Hyun, J. W. (2009) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2009.08.007 · Cited by 115
RNF4 is required for DNA double-strand break repair in vivo
Vyas, R., Kumar, R., Clermont, F. F., Helfricht, A., Kalev, P., Sotiropoulou, P., Hendriks, I. A., Radaelli, E., Hochepied, T., Blanpain, C., et al. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.145 · Cited by 120
Common Chemical Inductors of Replication Stress: Focus on Cell‐Based Studies
Veselá, E., Chromá, K., Turi, Z., & Mistrík, M. (2017) · Biomolecules · doi:10.3390/biom7010019 · Cited by 128
NFBD1/KIAA0170 Is a Chromatin-associated Protein Involved in DNA Damage Signaling Pathways
Xu, X., & Stern, D. F. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211392200 · Cited by 116
RETRACTION: XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage
Lévy, N., Martz, A., Bresson, A., Spenlehauer, C., de MURCIA, G., & Murcia, J. M. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj409 · Cited by 119
RetractedUse of γH2AX and Other Biomarkers of Double-Strand Breaks During Radiotherapy
Sak, A., & Stuschke, M. (2010) · Seminars in Radiation Oncology · doi:10.1016/j.semradonc.2010.05.004 · Cited by 113
Sak, A., Grehl, S., Erichsen, P., Engelhard, M., Grannaß, A., Levegrün, S., Pöttgen, C., Groneberg, M., & Stuschke, M. (2007) · International Journal of Radiation Biology · doi:10.1080/09553000701596118 · Cited by 113
Dose-controlled irradiation of cancer cells with laser-accelerated proton pulses
Zeil, K., Baumann, M. A., Beyreuther, E., Burris-Mog, T., Cowan, T. E., Enghardt, W., Karsch, L., Kraft, S., Laschinsky, L., Metzkes-Ng, J., et al. (2012) · Applied Physics B · doi:10.1007/s00340-012-5275-3 · Cited by 114
Proteome-wide prediction of acetylation substrates
Basu, A. B., Rose, K. L., Zhang, J., Beavis, R. C., Ueberheide, B. M., Garcia, B. A., Chait, B. T., Zhao, Y., Hunt, D. F., Segal, E., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906801106 · Cited by 115
Xiao, W., Liu, L., Guo, X., Wang, Y., Zhao, J., & Zhou, S. (2018) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.8b04163 · Cited by 114
G-quadruplex dynamics contribute to regulation of mitochondrial gene expression
Falabella, M., Kolesar, J. E., Wallace, C. T., de Jesus, D. S., Sun, L., Taguchi, Y. V., Wang, C., Wang, T., Xiang, I. M., Alder, J. K., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-41464-y · Cited by 114
Complete loss of H3K9 methylation dissolves mouse heterochromatin organization
Montavon, T., Shukeir, N., Erikson, G. A., Engist, B., Onishi‐Seebacher, M., Ryan, D. P., Musa, Y., Mittler, G., Meyer, A. G., Genoud, C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24532-8 · Cited by 115
Campylobacter jejuniCytolethal Distending Toxin Promotes DNA Repair Responses in Normal Human Cells
Hassane, D. C., Lee, R. B., & Pickett, C. L. (2002) · Infection and Immunity · doi:10.1128/iai.71.1.541-545.2003 · Cited by 113
RNF4 and PLK1 are required for replication fork collapse in ATR-deficient cellsPreprint
Ragland, R. L., Patel, S., Rivard, R. S., Smith, K. D., Peters, A. A., Bielinsky, A., & Brown, E. J. (2013) · Genes & Development · doi:10.1101/gad.223180.113 · Cited by 120
Pharmacological Ascorbate Radiosensitizes Pancreatic Cancer
Du, J., Cieslak, J. A., Welsh, J. L., Sibenaller, Z. A., Allen, B. G., Wagner, B. A., Kalen, A. L., Doskey, C. M., Strother, R. K., Button, A. M., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-1707 · Cited by 112
Adams, B. R., Golding, S. E., Rao, R. R., & Valerie, K. C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0010001 · Cited by 115
Dissection of the unusual structural and functional properties of the variant H2A.Bbd nucleosome
Doyen, C.-M., Montel, F., Gautier, T., Menoni, H., Claudet, C., Delacour‐Larose, M., Angelov, D., Hamiche, A., Bednář, J., Faivre-Moskalenko, C., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601310 · Cited by 113
DNA Double Strand Break Repair: A Radiation Perspective
Kavanagh, J. N., Redmond, K. M., Schettino, G., & Prise, K. M. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.5151 · Cited by 122
Magnetic resonance imaging (MRI): A review of genetic damage investigations
Vijayalaxmi, V., Fatahi, M., & Speck, O. (2015) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2015.02.002 · Cited by 112
Gelatin-Based Laser Direct-Write Technique for the Precise Spatial Patterning of Cells
Schiele, N. R., Chrisey, D. B., & Corr, D. T. (2010) · Tissue Engineering Part C Methods · doi:10.1089/ten.tec.2010.0442 · Cited by 112
Effects of DNA Damage in Smooth Muscle Cells in Atherosclerosis
Gray, K., Kumar, S., Figg, N. L., Harrison, J. E., Baker, L. L., Mercer, J. R., Littlewood, T. D., & Bennett, M. R. (2014) · Circulation Research · doi:10.1161/circresaha.116.304921 · Cited by 113
Liu, Y., Zheng, J., Zhang, Y., Wang, Z., Yang, Y., Bai, M., & Dai, Y. (2016) · Neurochemical Research · doi:10.1007/s11064-016-1989-7 · Cited by 114
Emerging Therapeutics to Overcome Chemoresistance in Epithelial Ovarian Cancer: A Mini-Review
Cornelison, R., Llaneza, D. C., & Landen, C. N. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102171 · Cited by 117
Li, H., Wang, M., Huang, B., Zhu, S., Zhou, J., Chen, D., Cui, R., Zhang, M., & Sun, Z. (2021) · Nature Communications · doi:10.1038/s41467-021-27485-0 · Cited by 113
Oxidative stress induces H2AX phosphorylation in human spermatozoa
Li, Z., Yang, J. J., & Huang, H. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.10.016 · Cited by 114
BRCA2 is required for neurogenesis and suppression of medulloblastoma
Frappart, P., Lee, Y., Lamont, J. M., & McKinnon, P. J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601703 · Cited by 114
Critical role of lysine 134 methylation on histone H2AX for γ-H2AX production and DNA repair
Sone, K., Piao, L., Nakakido, M., Ueda, K., Jenuwein, T., Nakamura, Y., & Hamamoto, R. (2014) · Nature Communications · doi:10.1038/ncomms6691 · Cited by 109
The emerging role of ROS-generating NADPH oxidase NOX4 in DNA-damage responses
Weyemi, U., & Dupuy, C. (2012) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2012.04.002 · Cited by 114
The nuclear γ-H2AX apoptotic ring: implications for cancers and autoimmune diseases
Solier, S., & Pommier, Y. G. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-013-1555-2 · Cited by 114
In vitro and In vivo Radiosensitization Induced by the DNA Methylating Agent Temozolomide
Kil, W. J., Cerna, D., Burgan, W. E., Beam, K., Carter, D., Steeg, P. S., Tofilon, P. J., & Camphausen, K. A. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-07-1856 · Cited by 112
Nair, N., Shoaib, M., & Sørensen, C. S. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071486 · Cited by 117
RECQL, a Member of the RecQ Family of DNA Helicases, Suppresses Chromosomal Instability
Sharma, S., Stumpo, D. J., Balajee, A. S., Bock, C. B., Lansdorp, P. M., Brosh, R. M., & Blackshear, P. J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01620-06 · Cited by 111
Immunofluorescence Detection of Clustered γ-H2AX Foci Induced by HZE-Particle Radiation
Desai, N., Davis, E. J., O'Neill, P., Durante, M., Cucinotta, F. A., & Wu, H. (2005) · Radiation Research · doi:10.1667/rr3431.1 · Cited by 111
Solier, S., Sordet, O., Kohn, K. W., & Pommier, Y. G. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00581-08 · Cited by 112
G2 arrest in response to topoisomerase II inhibitors: the role of p53.
Clifford, B., Beljin, M., Stark, G. R., & Taylor, W. R. (2003) · PubMed · Cited by 109
Chemical proteomics reveals a γH2AX-53BP1 interaction in the DNA damage response
Kleiner, R. E., Verma, P., Molloy, K. R., Chait, B. T., & Kapoor, T. M. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1908 · Cited by 112
Conjugation of vitamin E analog α-TOS to Pt(iv) complexes for dual-targeting anticancer therapy
Suntharalingam, K., Song, Y., & Lippard, S. J. (2013) · Chemical Communications · doi:10.1039/c3cc48740g · Cited by 112
Hanot, M., Tubeuf, E., Guilbert, A., Bado‐Nilles, A., Vigneron, P., Trouiller, B., Braun, A., & Lacroix, G. (2016) · Toxicology in Vitro · doi:10.1016/j.tiv.2016.01.013 · Cited by 110
Li, L., Ma, N., Zhou, H. W., Wang, Q., Zhang, H., Wang, P., Hou, H., Wen, H., & Gao, F. (2016) · International Journal of Nanomedicine · doi:10.2147/ijn.s107021 · Cited by 109
Parp1 promotes sleep, which enhances DNA repair in neurons
Zada, D., Sela, Y., Matosevich, N., Monsonego, A., Lerer‐Goldshtein, T., Nir, Y., & Appelbaum, L. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.10.026 · Cited by 117
Franchitto, A., Pichierri, P., Piergentili, R., Crescenzi, M., Bignami, M., & Palitti, F. (2003) · Oncogene · doi:10.1038/sj.onc.1206254 · Cited by 102
Oocyte differentiation is genetically dissociable from meiosis in mice
Dokshin, G. A., Baltus, A. E., Eppig, J. J., & Page, D. C. (2013) · Nature Genetics · doi:10.1038/ng.2672 · Cited by 109
Impaired NHEJ repair in amyotrophic lateral sclerosis is associated with TDP-43 mutations
Konopka, A., Whelan, D. R., Jamali, M. S., Perri, E. R., Shahheydari, H., Toth, R. P., Parakh, S., Robinson, T., Cheong, A., Mehta, P. M., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00386-4 · Cited by 117
Histone modifications in response to DNA damage
Altaf, M., Saksouk, N., & Côté, J. (2007) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2006.09.009 · Cited by 109
DNA lesions sequestered in micronuclei induce a local defective-damage response
Terradas, M., Martín, M., Tusell, L., & Genescà, A. (2009) · DNA repair · doi:10.1016/j.dnarep.2009.07.004 · Cited by 110
Yi, H., Sardesai, N., Fujinuma, T., Chan, C.-W., Veena, & Gelvin, S. B. (2006) · The Plant Cell · doi:10.1105/tpc.105.039719 · Cited by 108
Rezaeian, A.-H., Li, C., Wu, C., Zhang, X., Delacerda, J., You, M. J., Han, F., Cai, Z., Jeong, Y. S., Jin, G., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3445 · Cited by 112
Rb inactivation leads to E2F1-mediated DNA double-strand break accumulation
Pickering, M. T., & Kowalik, T. F. (2006) · Oncogene · doi:10.1038/sj.onc.1209103 · Cited by 108
Seo, J., Kim, S. C., Lee, H.-S., Kim, J. K., Shon, H. J., Salleh, N. L. M., Desai, K. V., Lee, J. H., Kang, E.-S., Kim, J. S., et al. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks287 · Cited by 112
Zhang, Y., Zheng, L., Ding, Y., Li, Q., Wang, R., Liu, T., Sun, Q., Yang, H., Peng, S., Wang, W., et al. (2015) · International Journal of Radiation Oncology*Biology*Physics · doi:10.1016/j.ijrobp.2015.04.007 · Cited by 108
Song, J., & Bent, A. F. (2014) · PLoS Pathogens · doi:10.1371/journal.ppat.1004030 · Cited by 113
Lithocholic acid phenocopies anti-ageing effects of calorie restriction
Qu, Q., Chen, Y., Wang, Y., Long, S., Wang, W., Yang, H.-Y., Li, M., Tian, X., Wei, X., Liu, Y., et al. (2024) · Nature · doi:10.1038/s41586-024-08329-5 · Cited by 123
The γ‐H2A.X: Is it just a surrogate marker of double‐strand breaks or much more?
Ismail, I. H., & Hendzel, M. J. (2007) · Environmental and Molecular Mutagenesis · doi:10.1002/em.20358 · Cited by 114
A novel plant gene essential for meiosis is related to the human CtIP and the yeast COM1/SAE2 gene
Uanschou, C., Siwiec, T., Pedrosa‐Harand, A., Kerzendorfer, C., Sánchez‐Morán, E., Novatchkova, M., Akimcheva, S., Woglar, A., Klein, F., & Schlögelhofer, P. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601913 · Cited by 107
Nashun, B., Yukawa, M., Liu, H., Akiyama, T., & Aoki, F. (2010) · Development · doi:10.1242/dev.051805 · Cited by 108
Zhao, R., Xiang, N., Domann, F. E., & Zhong, W. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-2216 · Cited by 106
Gaymes, T. J., Padua, R. A., Pla, M., Orr, S. J., Omidvar, N., Chomienne, C., Mufti, G. J., & Rassool, F. V. (2006) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0111 · Cited by 108
Andrievski, A., & Wilkins, R. C. (2009) · International Journal of Radiation Biology · doi:10.1080/09553000902781147 · Cited by 107
Telomere shortening reduces Alzheimer’s disease amyloid pathology in mice
Rolyan, H., Scheffold, A., Heinrich, A., Begus-Nahrmann, Y., Langkopf, B. H., Hölter, S. M., Vogt-Weisenhorn, D. M., Liss, B., Wurst, W., Lie, D. C., et al. (2011) · Brain · doi:10.1093/brain/awr133 · Cited by 106
Female Meiotic Sex Chromosome Inactivation in Chicken
Schoenmakers, S., Wassenaar, E., Hoogerbrugge, J. W., Laven, J. S. E., Grootegoed, J. A., & Baarends, W. M. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000466 · Cited by 107
Beyond transcription factors: how oncogenic signalling reshapes the epigenetic landscape
Liu, F., Wang, L., Perna, F., & Nimer, S. D. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.41 · Cited by 109
gamma-H2AX: Can it be established as a classical cancer prognostic factor?
Palla, V., Karaolanis, G., Katafigiotis, I., Anastasiou, I. P., Patapis, P., Dimitroulis, D., & Perrea, D. N. (2017) · Tumor Biology · doi:10.1177/1010428317695931 · Cited by 114
A comparison of mechanism‐inspired models for particle relative biological effectiveness (RBE)
Stewart, R. D., Carlson, D. J., Butkus, M. P., Hawkins, R. B., Friedrich, T., & Scholz, M. (2018) · Medical Physics · doi:10.1002/mp.13207 · Cited by 107
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Wang, S., Griffiths, G., Midgley, C., Barnett, A. L., Cooper, M. R., Grabarek, J., Ingram, L., Jackson, W., Kontopidis, G. A., McClue, S. J., et al. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.07.016 · Cited by 107
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Wang, S., Zhong, Z., Wan, J., Tan, W., Wu, G., Chen, M., & Wang, Y. (2013) · The American Journal of Chinese Medicine · doi:10.1142/s0192415x13500134 · Cited by 107
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Audebert, M., Riu, A., Jacques, C., Hillenweck, A., Jamin, E. L., Zalko, D., & Cravedi, J. (2010) · Toxicology Letters · doi:10.1016/j.toxlet.2010.08.022 · Cited by 112
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Scott, S. P., & Pandita, T. K. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.21067 · Cited by 106
Alagpulinsa, D. A., Ayyadevara, S., & Reis, R. J. S. (2014) · Frontiers in Oncology · doi:10.3389/fonc.2014.00289 · Cited by 105
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Dote, H., Cerna, D., Burgan, W. E., Carter, D. J., Cerra, M. A., Hollingshead, M. G., Camphausen, K. A., & Tofilon, P. J. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-05-0050 · Cited by 105
Honda, Y., Tojo, M., Matsuzaki, K., Anan, T., Matsumoto, M., Ando, M., Saya, H., & Nakao, M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m104347200 · Cited by 105
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Zhou, J., Ahmad, F., Parikh, S. S., Hoffman, N. E., Rajan, S., Verma, V. K., Song, J., Yuan, A., Shanmughapriya, S., Guo, Y., et al. (2016) · Circulation Research · doi:10.1161/circresaha.116.308544 · Cited by 105
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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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