The DOI matches its Crossref record; 57 of the 58 references it cites were found in a registry or an index.
Acetylation limits 53BP1 association with damaged chromatin to promote homologous recombination
Open accessAbstract
The pathogenic sequelae of BRCA1 mutation in human and mouse cells are mitigated by concomitant deletion of 53BP1, which binds histone H4 dimethylated at Lys20 (H4K20me2) to promote nonhomologous end joining, suggesting that a balance between BRCA1 and 53BP1 regulates DNA double strand-break (DSB) repair mechanism choice. Here we document that acetylation is a key determinant of this balance. TIP60 acetyltransferase deficiency reduced BRCA1 at DSB chromatin with commensurate increases in 53BP1, whereas HDAC inhibition yielded the opposite effect. TIP60-dependent H4 acetylation diminished 53BP1 binding to H4K20me2 in part through disruption of a salt bridge between H4K16 and Glu1551 in the 53BP1 Tudor domain. Moreover, TIP60 deficiency impaired homologous recombination and conferred sensitivity to PARP inhibition in a 53BP1-dependent manner. These findings demonstrate that acetylation in cis to H4K20me2 regulates relative BRCA1 and 53BP1 DSB chromatin occupancy to direct DNA repair mechanism.
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.
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
The PyMOL Molecular Graphics System
DeLano, W. L. (2002) · Medical Entomology and Zoology · Cited by 18,147
The Amber biomolecular simulation programs
Case, D. A., Cheatham, T. E., Darden, T., Gohlke, H., Luo, R., Merz, K. M., Onufriev, A., Simmerling, C., Wang, B., & Woods, R. J. (2005) · Journal of Computational Chemistry · doi:10.1002/jcc.20290 · Cited by 9,535
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
Targeting the DNA repair defect in BRCA mutant cells as a therapeutic strategy
Farmer, H., McCabe, N., Lord, C. J., Tutt, A. N. J., Johnson, D. A., Richardson, T. B., Santarosa, M., Dillon, K. J., Hickson, I., Knights, C., et al. (2005) · Nature · doi:10.1038/nature03445 · Cited by 6,683
AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
Laskowski, R., Rullmann, J. A., MacArthur, M., Kaptein, R., & Thornton, J. (1996) · Journal of Biomolecular NMR · doi:10.1007/bf00228148 · Cited by 5,502
Specific killing of BRCA2-deficient tumours with inhibitors of poly(ADP-ribose) polymerase
Bryant, H. E., Schultz, N., Thomas, H. D., Parker, K. M., Flower, D., Lopez, E., Kyle, S., Meuth, M., Curtin, N. J., & Helleday, T. (2005) · Nature · doi:10.1038/nature03443 · Cited by 5,198
Inhibition of Poly(ADP-Ribose) Polymerase in Tumors from BRCA Mutation Carriers
Fong, P. C., Boss, D. S., Yap, T. A., Tutt, A., Wu, P., Mergui-Roelvink, M., Mortimer, P., Swaisland, H., Lau, A., O'Connor, M. J., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0900212 · Cited by 3,634
Histone H4-K16 Acetylation Controls Chromatin Structure and Protein Interactions
Shogren‐Knaak, M. A., Ishii, H., Sun, J.-M., Pazin, M. J., Davie, J., & Peterson, C. L. (2006) · Science · doi:10.1126/science.1124000 · Cited by 1,959
Fraga, M. F., Ballestar, E., Villar‐Garea, A., Boix-Chornet, M., Espada, J., Schotta, G., Bonaldi, T., Haydon, C. E., Ropero, S., Petrie, K. R., et al. (2005) · Nature Genetics · doi:10.1038/ng1531 · Cited by 1,926
The UCSC Genome Browser database: update 2011
Fujita, P. A., Rhead, B., Zweig, A. S., Hinrichs, A. S., Karolchik, D., Cline, M., Goldman, M. J., Barber, G. P., Clawson, H., Coelho, A., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq963 · Cited by 1,843
Cited by
Sorted by citations
Items 201–300 of 522
Moreno, N. S., Liu, J., Haas, K. M., Parker, L. L., Chakraborty, C., Kron, S. J., Hodges, K. B., Miller, L. D., Langefeld, C. D., Robinson, J. P., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz138 · Cited by 44
The two faces of giant cell tumor of bone
di Carlo, F. S., Whyte, M. P., & Gianfrancesco, F. (2020) · Cancer Letters · doi:10.1016/j.canlet.2020.05.031 · Cited by 44
Rezazadeh, S., Yang, D. X., Biashad, S. A., Firsanov, D., Takasugi, M., Gilbert, M. B., Tombline, G., Bhanu, N. V., Garcia, B. A., Seluanov, A., et al. (2020) · Aging · doi:10.18632/aging.103567 · Cited by 42
Helfricht, A., Thijssen, P. E., Rother, M. B., Shah, R. G., Du, L., Takada, S., Rogier, M., Moritz, J., IJspeert, H., Stoepker, C., et al. (2020) · The Journal of Experimental Medicine · doi:10.1084/jem.20191688 · Cited by 45
The Chromatin Landscape Channels DNA Double-Strand Breaks to Distinct Repair Pathways
Chen, Z., & Tyler, J. K. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.909696 · Cited by 44
Screen identifies DYRK1B network as mediator of transcription repression on damaged chromatin
Dong, C., West, K. L., Tan, X. Y., Li, J., Ishibashi, T., Yu, C., Sy, S. M.-H., Leung, J. W. C., & Huen, M. S. Y. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002193117 · Cited by 47
Johnson, D. P., Spitz, G. S., Tharkar, S., Quayle, S. N., Shearstone, J. R., Jones, S. S., McDowell, M. E., Wellman, H., Tyler, J. K., Cairns, B. R., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.3120 · Cited by 43
Ho, T., Sitz, J., Shen, Q., Leblanc-Lacroix, A., Campos, E. I., Borozan, I., Marcon, E., Greenblatt, J. F., Fradet‐Turcotte, A., Jin, D., et al. (2018) · Journal of Virology · doi:10.1128/jvi.00262-18 · Cited by 45
MAD2L2 dimerization and TRIP13 control shieldin activity in DNA repair
de Krijger, I., Föhr, B., Hernández-Pérez, S., Vincendeau, E., Serrat, J., Thouin, A. M., Susvirkar, V., Lescale, C., Paniagua, I., Hoekman, L., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-25724-y · Cited by 42
Poly(ADP-ribose) binding and macroH2A mediate recruitment and functions of KDM5A at DNA lesions
Kumbhar, R., Sanchez, A. R., Perren, J. O., Gong, F., Corujo, D., Medina, F., Devanathan, S. K., Xhemalçe, B., Matouschek, A. T., Buschbeck, M., et al. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202006149 · Cited by 44
Hu, K., Li, Y., Wu, W., Xie, L., Yan, H., Cai, Y., Dong, C., Jiang, Q., Lin, L., Chen, Z. B., et al. (2020) · Advanced Science · doi:10.1002/advs.202000157 · Cited by 39
DNA Damage Response Regulation by Histone Ubiquitination
Sekiguchi, M., & Matsushita, N. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23158187 · Cited by 45
Assembling nuclear domains: Lessons from DNA repair
Schrank, B. R., & Gautier, J. (2019) · The Journal of Cell Biology · doi:10.1083/jcb.201904202 · Cited by 39
Role of Histone Methylation in Maintenance of Genome Integrity
Mushtaq, A., Mir, U. S., Hunt, C. R., Pandita, S., Tantray, W. W., Bhat, A., PANDITA, R. K., Altaf, M., & Pandita, T. K. (2021) · Genes · doi:10.3390/genes12071000 · Cited by 45
PHRF1 promotes genome integrity by modulating non-homologous end-joining
Chang, C.-F., Chu, P.-C., Wu, P.-Y., Yu, M.-Y., Lee, J.-Y., Tsai, M.-D., & Chang, M.-S. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.81 · Cited by 37
Structural Plasticity of Methyllysine Recognition by the Tandem Tudor Domain of 53BP1
Tong, Q., Cui, G., Botuyan, M. V., Rothbart, S. B., Hayashi, R., Musselman, C. A., Singh, N., Appella, E., Strahl, B. D., Mer, G., et al. (2015) · Structure · doi:10.1016/j.str.2014.11.013 · Cited by 39
Self-citationGLP-catalyzed H4K16me1 promotes 53BP1 recruitment to permit DNA damage repair and cell survival
Lu, X., Tang, M., Zhu, Q., Yang, Q., Li, Z., Bao, Y., Liu, G., Hou, T., Lv, Y., Zhao, Y., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz897 · Cited by 39
The Role of Histone Lysine Methylation in the Response of Mammalian Cells to Ionizing Radiation
Nisio, E. D., Lupo, G., Licursi, V., & Negri, R. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.639602 · Cited by 39
Lee, D., Apelt, K., Lee, S.-O., Chan, H., Luijsterburg, M. S., Leung, J. W. C., & Miller, K. M. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac160 · Cited by 35
H3K4 methylation by SETD1A/BOD1L facilitates RIF1-dependent NHEJ
Bayley, R., Borel, V., Moss, R. J., Sweatman, E., Ruis, P., Ormrod, A., Goula, A., Mottram, R. M. A., Stanage, T. H., Hewitt, G., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.030 · Cited by 38
Gürsoy-Yüzügüllü, Ö., Carman, C. L., & Price, B. D. (2017) · Scientific Reports · doi:10.1038/s41598-017-13036-5 · Cited by 38
ADAR1 links R-loop homeostasis to ATR activation in replication stress response
Zhang, B., Li, Y., Zhang, J., Wang, Y., Liang, C., Lü, T., Zhang, C., Liu, L., Qin, Y. F., He, J., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad839 · Cited by 37
Small Cajal body-associated RNA 2 (scaRNA2) regulates DNA repair pathway choice by inhibiting DNA-PK
Bergstrand, S., O’Brien, E. M., Coucoravas, C., Hroššová, D., Peirasmaki, D., Schmidli, S., Dhanjal, S., Pederiva, C., Siggens, L., Mortusewicz, O., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28646-5 · Cited by 40
Brochier, C., & Langley, B. C. (2013) · Neurotherapeutics · doi:10.1007/s13311-013-0210-9 · Cited by 41
Double duty: ZMYND8 in the DNA damage response and cancer
Gong, F., & Miller, K. M. (2018) · Cell Cycle · doi:10.1080/15384101.2017.1376150 · Cited by 36
MOF Suppresses Replication Stress and Contributes to Resolution of Stalled Replication Forks
Singh, D. K., PANDITA, R. K., Singh, M. K., Chakraborty, S., Hambarde, S., Ramnarain, D. B., Charaka, V., Ahmed, K. M., Hunt, C. R., & Pandita, T. K. (2018) · Molecular and Cellular Biology · doi:10.1128/mcb.00484-17 · Cited by 36
The histone acetyltransferase hMOF promotes vascular invasion in hepatocellular carcinoma
Poté, N., Cros, J. F., Laouirem, S., Raffenne, J., Negrão, M., Albuquerque, M., Bédossa, P., Ferreira, M. G., Ait‐Si‐Ali, S., Fior, R., et al. (2020) · Liver International · doi:10.1111/liv.14381 · Cited by 35
Methylation of histone 4’s lysine 20: a critical analysis of the state of the field
Corvalan, A. Z., & Coller, H. A. (2020) · Physiological Genomics · doi:10.1152/physiolgenomics.00128.2020 · Cited by 37
CDKL5 kinase controls transcription‐coupled responses to DNA damage
Khanam, T., Munoz, I. M., Weiland, F., Carroll, T. D., Morgan, M., Borsos, B. N., Pantazi, V., Slean, M. M., Novak, M. J., Toth, R. L., et al. (2021) · The EMBO Journal · doi:10.15252/embj.2021108271 · Cited by 36
Lysine Acetylation, Cancer Hallmarks and Emerging Onco-Therapeutic Opportunities
Hu, M., He, F.-L., Thompson, E. W., Ostrikov, K., & Dai, X. (2022) · Cancers · doi:10.3390/cancers14020346 · Cited by 36
Das, C., Adhikari, S., Bhattacharya, A., Chakraborty, S., Mondal, P., Yadav, S. S., Adhikary, S., Hunt, C. R., Yadav, K. K., Pandita, S., et al. (2023) · Cancer Research · doi:10.1158/0008-5472.can-22-3015 · Cited by 39
Bártová, E., Legartová, S., Dundr, M., & Suchánková, J. (2019) · Aging · doi:10.18632/aging.101917 · Cited by 36
CTCF cooperates with CtIP to drive homologous recombination repair of double-strand breaks
Hwang, S. Y., Kang, M. A., Baik, C. J., Lee, Y., Hang, N. T., Kim, B., Han, J. S., Jeong, J., Park, D., Myung, K., et al. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz639 · Cited by 32
Yang, Y., Yang, G., Yu, L., Lin, L., Liu, L. P., Fang, M., & Xu, Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00484 · Cited by 33
DNA Repair in Space and Time: Safeguarding the Genome with the Cohesin Complex
Phipps, J., & Dubrana, K. (2022) · Genes · doi:10.3390/genes13020198 · Cited by 36
Zhang, H., Sun, L., Wang, K., Wu, D., Trappio, M., Witting, C. S., & Cao, K. (2016) · PLoS ONE · doi:10.1371/journal.pone.0167454 · Cited by 37
Bennetzen, M. V., Larsen, D. H., Dinant, C., Watanabe, S., Bártek, J., Lukas, J., & Andersen, J. (2013) · Cell Cycle · doi:10.4161/cc.24758 · Cited by 33
PHF2 regulates homology-directed DNA repair by controlling the resection of DNA double strand breaks
Vega, I. A., Paz‐Cabrera, M. C., Rother, M. B., Wiegant, W. W., Checa-Rodríguez, C., Hernandez-Fernaud, J. R., Huertas, P., Freire, R., van Attikum, H., & Smits, V. A. J. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa196 · Cited by 35
Mitrentsi, I., Lou, J., Kerjouan, A., Verigos, J., Reina‐San‐Martin, B., Hinde, E., & Soutoglou, E. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.03.033 · Cited by 33
Role of histone acetyltransferases MOF and Tip60 in genome stability
Mir, U. S., Bhat, A., Mushtaq, A., Pandita, S., Altaf, M., & Pandita, T. K. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103205 · Cited by 32
Taming Tricky DSBs: ATM on duty
Clouaire, T., Marnef, A., & Legube, G. (2017) · DNA repair · doi:10.1016/j.dnarep.2017.06.010 · Cited by 37
Targeting protein–protein interactions in the DNA damage response pathways for cancer chemotherapy
McPherson, K. S., & Korzhnev, D. M. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00101a · Cited by 35
Fukuda, T., Wu, W., Okada, M., Maeda, I., Kojima, Y., Hayami, R., Miyoshi, Y., Tsugawa, K., & Ohta, T. (2015) · Cancer Science · doi:10.1111/cas.12717 · Cited by 33
Keep moving and stay in a good shape to find your homologous recombination partner
Bordelet, H., & Dubrana, K. (2018) · Current Genetics · doi:10.1007/s00294-018-0873-1 · Cited by 34
Salamun, S. G., Sitz, J., de la Cruz-Herrera, C. F., Yockteng-Melgar, J., Marcon, E., Greenblatt, J. F., Fradet‐Turcotte, A., & Frappier, L. (2019) · Journal of Virology · doi:10.1128/jvi.01070-19 · Cited by 34
BMI-1 regulates DNA end resection and homologous recombination repair
Fitieh, A. M., Locke, A. J., Mashayekhi, F., Khaliqdina, F., Sharma, A. K., & Ismail, I. H. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110536 · Cited by 35
Sanchez, A. R., de Vivo, A., Tonzi, P., Kim, J., Huang, T. T., & Kee, Y. (2020) · PLoS Genetics · doi:10.1371/journal.pgen.1008524 · Cited by 31
van de Kooij, B., van der Wal, F. J., Rother, M. B., Wiegant, W. W., Creixell, P., Stout, M., Joughin, B. A., Vornberger, J., Altmeyer, M., van Vugt, M. A. T. M., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51090-6 · Cited by 31
Zhu, H., Tian, Y., Chen, H., Qian, Y., Li, J., Niu, D., Zhao, W., Wu, Y., Zhang, X., Tang, T., et al. (2025) · Drug Resistance Updates · doi:10.1016/j.drup.2025.101287 · Cited by 30
Hu, Y., Wang, C., Huang, K., Xia, F., Parvin, J. D., & Mondal, N. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110522 · Cited by 32
Inhibition of histone deacetylases enhances DNA damage repair in SCNT embryos
Bohrer, R. C., Duggavathi, R., & Bordignon, V. (2014) · Cell Cycle · doi:10.4161/cc.29215 · Cited by 31
Mackay, D. R., Howa, A. C., Werner, T. L., & Ullman, K. S. (2017) · Journal of Cell Science · doi:10.1242/jcs.203513 · Cited by 31
Transcription-associated events affecting genomic integrity
Sebastian, R., & Oberdoerffer, P. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0288 · Cited by 28
An Acetyl-Methyl Switch Drives a Conformational Change in p53
Tong, Q., Mazur, S. J., Rincón‐Arano, H., Rothbart, S. B., Kuznetsov, D. M., Cui, G., Liu, W. H., Gete, Y. G., Klein, B. J., Jenkins, L. M. M., et al. (2015) · Structure · doi:10.1016/j.str.2014.12.010 · Cited by 29
Self-citationOrtega, P., Gómez‐González, B., & Aguilera, A. (2019) · Nature Communications · doi:10.1038/s41467-019-13210-5 · Cited by 29
DNA Double-Strand Break Repair: All Roads Lead to HeterochROMAtin Marks
Caron, P., Pobega, E., & Polo, S. E. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.730696 · Cited by 34
RIF1-ASF1-mediated high-order chromatin structure safeguards genome integrity
Feng, S., Ma, S., Li, K., Gao, S., Ning, S., Shang, J., Guo, R., Chen, Y., Blumenfeld, B., Simon, I., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-28588-y · Cited by 29
Tetratricopeptide repeat factor XAB2 mediates the end resection step of homologous recombination
Onyango, D. O., Howard, S. M., Neherin, K., Yanez, D. A., & Stark, J. M. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw275 · Cited by 26
Integrated Proteogenomic Characterization of Human High-Grade Serous Ovarian Cancer
Zhang, H., Liu, T., Zhang, Z., Payne, S., Zhang, B., McDermott, J., Zhou, J., Petyuk, V., Chen, L., Ray, D., et al. (2025) · Cell · doi:10.1016/j.cell.2025.10.043 · Cited by 34
Nardi, I. K., Stark, J. M., Larsen, A. B., Salgia, R., & Raz, D. J. (2019) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0053 · Cited by 28
Genetic and epigenetic alterations in aging and rejuvenation of human
Park, K., Jeon, M. C., Lee, D., Kim, J., & Im, S.-W. (2024) · Molecules and Cells · doi:10.1016/j.mocell.2024.100137 · Cited by 30
The nucleosome: orchestrating DNA damage signaling and repair within chromatin
Agarwal, P., & Miller, K. M. (2016) · Biochemistry and Cell Biology · doi:10.1139/bcb-2016-0017 · Cited by 28
LEDGF/p75 Is Required for an Efficient DNA Damage Response
Liedtke, V., Schröder, C., Roggenbuck, D., Weiss, R., Stohwasser, R., Schierack, P., Rödiger, S., & Schenk, L. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115866 · Cited by 26
PHF8-promoted TOPBP1 demethylation drives ATR activation and preserves genome stability
Ma, S., Cao, C., Che, S., Wang, Y., Su, D., Liu, S., Gong, W., Liu, L., Sun, J., Zhao, J., et al. (2021) · Science Advances · doi:10.1126/sciadv.abf7684 · Cited by 29
TPX2 Impacts Acetylation of Histone H4 at Lysine 16: Implications for DNA Damage Response
Neumayer, G., & Nguyen, M. D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0110994 · Cited by 27
Zhang, H., Devoucoux, M., Song, X., Li, L., Ayaz, G., Cheng, H., Tempel, W., Cheng, D., Loppnau, P., Côté, J., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.03.003 · Cited by 26
Interplay between the DNA damage response and the life cycle of DNA tumor viruses
Studstill, C. J., Mac, M., & Moody, C. A. (2023) · Tumour Virus Research · doi:10.1016/j.tvr.2023.200272 · Cited by 28
Proteome-wide microarray-based screening of PAR-binding proteins
Kang, B. G., Kang, S.-U., Kim, J. J., Kwon, J.-S., Gagné, J., Lee, S. Y., Kim, S., Lee, K. S., Ha, S., Jeong, J. S., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf300 · Cited by 23
RYBP Is a K63-Ubiquitin-Chain-Binding Protein that Inhibits Homologous Recombination Repair
Ali, M. A., Strickfaden, H., Lee, B. L., Spyracopoulos, L., & Hendzel, M. J. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.047 · Cited by 26
Assessing kinetics and recruitment of DNA repair factors using high content screens
Martínez-Pastor, B., da Silveira, G. G., Clarke, T. L., Chung, D., Gu, Y., Cosentino, C., Davidow, L. S., Mata, G., Hassanieh, S., Salsman, J., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.110176 · Cited by 25
Maroschik, B., Gürtler, A., Kraemer, A. I., Rößler, U., Gomolka, M., Hornhardt, S., Mörtl, S., & Friedl, A. A. (2014) · Radiation Oncology · doi:10.1186/1748-717x-9-15 · Cited by 26
Cruz, G. M. S., Kong, X., Silva, B. A., Khatibzadeh, N., Thai, R., Berns, M. W., & Yokomori, K. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv976 · Cited by 29
Metabolic modulation of chromatin: implications for DNA repair and genomic integrity
Liu, J. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00182 · Cited by 26
Overcoming Resistance of Cancer Cells to PARP-1 Inhibitors with Three Different Drug Combinations
Yalon, M., Tuval-Kochen, L., Castel, D., Moshe, I., Mazal, I., Cohen, O., Avivi, C., Rosenblatt, K., Aviel‐Ronen, S., Schiby, G., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0155711 · Cited by 25
Penterling, C., Drexler, G. A., Böhland, C., Stamp, R., Wilke, C., Braselmann, H., Caldwell, R. B., Reindl, J., Girst, S., Greubel, C., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0156599 · Cited by 25
Impact of the DNA Damage Response on Human Papillomavirus Chromatin
Gautam, D., & Moody, C. A. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005613 · Cited by 25
Trakarnphornsombat, W., & Kimurâ, H. (2023) · Journal of Cell Science · doi:10.1242/jcs.260698 · Cited by 31
Giorgio, E. D., Dalla, E., Tolotto, V., D’Este, F., Paluvai, H., Ranzino, L., & Brancolini, C. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae501 · Cited by 26
The nuclear kinesin KIF18B promotes 53BP1-mediated DNA double-strand break repair
Luessing, J., Sakhteh, M., Sarai, N., Frizzell, L., Tsanov, N., Ramberg, K. O., Maretto, S., Crowley, P. B., & Lowndes, N. F. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.109306 · Cited by 24
A di-acetyl-decorated chromatin signature couples liquid condensation to suppress DNA end synapsis
Bao, K., Ma, Y., Li, Y., Shen, X., Zhao, J., Tian, S., Zhang, C., Liang, C., Zhao, Z., Yang, Y., et al. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.02.002 · Cited by 24
H3K36 dimethylation by MMSET promotes classical non-homologous end-joining at unprotected telomeres
de Krijger, I., van der Torre, J., Peuscher, M. H., Eder, M., & Jacobs, J. J. L. (2020) · Oncogene · doi:10.1038/s41388-020-1334-0 · Cited by 26
Campillo‐Marcos, I., Monte-Serrano, E., Navarro-Carrasco, E., García-González, R., & Lazo, P. A. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.715126 · Cited by 24
Interaction of the epigenetic integrator UHRF1 with the MYST domain of TIP60 inside the cell
Ashraf, W., Bronner, C., Zaayter, L., Ahmad, T., Richert, L., Alhosin, M., Ibrahim, A., Hamiche, A., Mély, Y., & Mousli, M. (2017) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-017-0659-1 · Cited by 23
Emerging Perspectives on DNA Double-strand Breaks in Neurodegenerative Diseases
Zhu, L., Wang, D., Cui, K., Liu, D., & Zhu, L. (2019) · Current Neuropharmacology · doi:10.2174/1570159x17666190726115623 · Cited by 24
The modulation of PD-L1 induced by the oncogenic HBXIP for breast cancer growth
Xu, F., Sun, H., Fang, R., Zhang, L., Shi, H., Wang, X., Fu, X., Li, X.-M., Shi, X.-H., Wu, Y., et al. (2021) · Acta Pharmacologica Sinica · doi:10.1038/s41401-021-00631-6 · Cited by 23
Targeting the Interplay between HDACs and DNA Damage Repair for Myeloma Therapy
Gkotzamanidou, M. A., Terpou, E., Kentepozidis, N. K., & Terpos, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910406 · Cited by 24
Glover, L., & Horn, D. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku900 · Cited by 23
Coordinated Regulation of TIP60 and Poly(ADP-Ribose) Polymerase 1 in Damaged-Chromatin Dynamics
Ikura, M., Furuya, K., Fukuto, A., Matsuda, R., Adachi, J., Matsuda, T., Kakizuka, A., & Ikura, T. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.01085-15 · Cited by 23
Coucoravas, C., Dhanjal, S., Henriksson, S., Böhm, S., & Farnebo, M. (2016) · RNA Biology · doi:10.1080/15476286.2016.1243647 · Cited by 23
Functional Roles of Acetylated Histone Marks at Mouse Meiotic Recombination Hot Spots
Getun, I. V., Wu, Z., Fallahi, M., Ouizem, S., Liu, Q., Li, W., Costi, R., Roush, W. R., Cleveland, J. L., & Bois, P. R. J. (2016) · Molecular and Cellular Biology · doi:10.1128/mcb.00942-15 · Cited by 21
Lashgari, A., Fauteux, M., Maréchal, A., & Gaudreau, L. R. (2018) · Scientific Reports · doi:10.1038/s41598-018-32323-3 · Cited by 26
DDX17 is required for efficient DSB repair at DNA:RNA hybrid deficient loci
Bader, A. S., Luessing, J., Hawley, B. R., Skalka, G., Lu, W.-T., Lowndes, N. F., & Bushell, M. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac843 · Cited by 23
HDAC3 in action: Expanding roles in inflammation and inflammatory diseases
He, R., He, Z., Zhang, T., Liu, B., Gao, M., Li, N., & Geng, Q. (2024) · Cell Proliferation · doi:10.1111/cpr.13731 · Cited by 23
β2-spectrin depletion impairs DNA damage repair
Horikoshi, N., PANDITA, R. K., Mujoo, K., Hambarde, S., Sharma, D., Mattoo, A. R., Chakraborty, S., Charaka, V., Hunt, C. R., & Pandita, T. K. (2016) · Oncotarget · doi:10.18632/oncotarget.9677 · Cited by 22
Chromatin context-dependent effects of epigenetic drugs on CRISPR-Cas9 editing
Schep, R., Trauernicht, M., Vergara, X., Friskes, A., Morris, B., Gregoricchio, S., Manzo, S. G., Zwart, W. T., Beijersbergen, R. L., Medema, R. H., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae570 · Cited by 21
Replicated chromatin curtails 53BP1 recruitment in BRCA1-proficient and BRCA1-deficient cells
Michelena, J., Pellegrino, S., Spegg, V., & Altmeyer, M. (2021) · Life Science Alliance · doi:10.26508/lsa.202101023 · Cited by 22
Making Connections: Integrative Signaling Mechanisms Coordinate DNA Break Repair in Chromatin
Sanchez, A. R., Lee, D., Kim, D. I., & Miller, K. M. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.747734 · Cited by 25
SLFN5-mediated chromatin dynamics sculpt higher-order DNA repair topology
Huang, J., Wu, C., Kloeber, J. A., Gao, H., Gao, M., Zhu, Q., Chang, Y., Zhao, F., Guo, G., Luo, K., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.02.004 · Cited by 20
The relationship between histone posttranslational modification and DNA damage signaling and repair
Sharma, A. K., & Hendzel, M. J. (2018) · International Journal of Radiation Biology · doi:10.1080/09553002.2018.1516911 · Cited by 20
Uba, A. İ., & Yelekçi, K. (2018) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2018.10.016 · Cited by 22
Metadata
- Authors
- Tang, J., Cho, N. W., Cui, G., Manion, E. M., Shanbhag, N. M., Botuyan, M. V., Mer, G., & Greenberg, R. A.
- Affiliations
- University of Pennsylvania (US)
- Mayo Clinic (US)
- Corresponding author
- Greenberg, Roger A
- Venue
- Nature Structural & Molecular Biology
- Published
- 2013-02-03
- Volume
- 20
- Issue
- 3
- Pages
- 317-325
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC3594358
- OpenAlex
- W2060247906
- Cited by
- 521
- References
- 58
- Citations by year
- 2026: 20 · 2025: 26 · 2024: 28 · 2023: 29 · 2022: 52 · 2021: 45 · 2020: 48 · 2019: 34 · 2018: 48 · 2017: 49 · 2016: 53 · 2015: 35 · 2014: 33 · 2013: 21
- FWCI
- 21.37
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Cancer Institute (R01CA138835, R01CA132878, R01CA174904, P50CA116201, P30CA016520)
- National Institute of General Medical Sciences (R01GM101149)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- 53BP1, BRCA1, histone H4 acetylation, H4K16 acetylation, Tip60, H4K20me2, homologous recombination, non-homologous end joining, DNA double-strand break repair, DNA repair pathway choice, Tudor domain, histone deacetylase inhibition, chromatin binding
- MeSH terms
- Tumor Suppressor p53-Binding Protein 1, ATPases Associated with Diverse Cellular Activities, Lysine Acetyltransferase 5, Acetylation, Amino Acid Sequence, Carrier Proteins, Cells, Cultured, Chromatin, Chromosomal Proteins, Non-Histone, DNA Helicases, DNA-Binding Proteins, Histone Deacetylases, Histones, Humans, Molecular Sequence Data, Magnetic Resonance Spectroscopy, Protein Conformation, BRCA1 Protein, Intracellular Signaling Peptides and Proteins, Histone Acetyltransferases, DNA Breaks, Double-Stranded, Gene Knockdown Techniques, Homologous Recombination
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