The DOI matches its Crossref record; 101 of the 101 references it cites were found in a registry or an index.
Tip60: Connecting chromatin to DNA damage signaling
Open accessAbstract
Cells are constantly exposed to genotoxic events that can damage DNA. To counter this, cells have evolved a series of highly conserved DNA repair pathways to maintain genomic integrity. The ATM protein kinase is a master regulator of the DNA double-strand break (DSB) repair pathway. DSBs activate ATM's kinase activity, promoting the phosphorylation of proteins involved in both checkpoint activation and DNA repair. Recent work has revealed that two DNA damage response proteins, the Tip60 acetyltransferase and the mre11- rad50-nbs1 (MRN) complex, co-operate in the activation of ATM in response to DSBs. MRN functions to target ATM and the Tip60 acetyltransferase to DSBs. Tip60's chromodomain then interacts with histone H3 trimethylated on lysine 9, activating Tip60's acetyltransferase activity and stimulating the subsequent acetylation and activation of ATM's kinase activity. These results underscore the importance of chromatin structure in regulating DNA damage signaling and emphasize how histone modifications co-ordinate DNA repair. In addition, human tumors frequently exhibit altered patterns of histone methylation. This rewriting of the histone methylation code in tumor cells may impact the efficiency of DSB repair, increasing genomic instability and contributing to the initiation and progression of cancer.
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
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883
High-Resolution Profiling of Histone Methylations in the Human Genome
Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Schones, D. E., Wang, Z., Wei, G., Chepelev, I., & Zhao, K. (2007) · Cell · doi:10.1016/j.cell.2007.05.009 · Cited by 6,845
The DNA-damage response in human biology and disease
Jackson, S. P., & Bartek, J. (2009) · Nature · doi:10.1038/nature08467 · Cited by 6,092
Genome-wide maps of chromatin state in pluripotent and lineage-committed cells
Mikkelsen, T. S., Ku, M., Jaffe, D. B., Issac, B., Lieberman, E., Giannoukos, G., Alvarez, P., Brockman, W., Kim, T.-K., Koche, R. P., et al. (2007) · Nature · doi:10.1038/nature06008 · Cited by 4,129
DNA damage activates ATM through intermolecular autophosphorylation and dimer dissociation
Bakkenist, C. J., & Kastan, M. B. (2003) · Nature · doi:10.1038/nature01368 · Cited by 3,466
Heintzman, N. D., Stuart, R. K., Hon, G., Fu, Y., Ching, C. W., Hawkins, R. D., Barrera, L. O., Van Calcar, S., Qu, C., Ching, K. A., et al. (2007) · Nature Genetics · doi:10.1038/ng1966 · Cited by 3,398
ATM and ATR Substrate Analysis Reveals Extensive Protein Networks Responsive to DNA Damage
Matsuoka, S., Ballif, B. A., Smogorzewska, A., McDonald, E. R., Hurov, K. E., Luo, J., Bakalarski, C. E., Zhao, Z., Solimini, N., Lerenthal, Y., et al. (2007) · Science · doi:10.1126/science.1140321 · Cited by 3,075
Megabase Chromatin Domains Involved in DNA Double-Strand Breaks in Vivo
Rogakou, E. P., Boon, C., Redon, C., & Bonner, W. M. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.5.905 · Cited by 2,422
Bernstein, B. E., Meissner, A., & Lander, E. S. (2007) · Cell · doi:10.1016/j.cell.2007.01.033 · Cited by 2,086
A Chromatin Landmark and Transcription Initiation at Most Promoters in Human Cells
Guenther, M. G., Levine, S. S., Boyer, L. A., Jaenisch, R., & Young, R. A. (2007) · Cell · doi:10.1016/j.cell.2007.05.042 · Cited by 2,002
Cited by
Sorted by citations
The DNA Damage Response: Making It Safe to Play with Knives
Ciccia, A., & Elledge, S. J. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.019 · Cited by 4,368
Chromatin Remodeling at DNA Double-Strand Breaks
Price, B. D., & D’Andrea, A. D. (2013) · Cell · doi:10.1016/j.cell.2013.02.011 · Cited by 588
Self-citationNBS1 lactylation is required for efficient DNA repair and chemotherapy resistance
Chen, H., Li, Y., Li, H., Chen, X., Fu, H., Mao, D., Chen, W., Lan, L., Wang, C., Hu, K., et al. (2024) · Nature · doi:10.1038/s41586-024-07620-9 · Cited by 639
The MRN complex in double‐strand break repair and telomere maintenance
Lamarche, B. J., Orazio, N. I., & Weitzman, M. D. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.07.029 · Cited by 446
Ayrapetov, M. K., Gursoy-Yuzugullu, O., Xu, C., Xu, Y., & Price, B. D. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1403565111 · Cited by 391
Self-citationThompson, L. H. (2012) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2012.06.002 · Cited by 357
PRMTs and Arginine Methylation: Cancer’s Best-Kept Secret?
Jarrold, J., & Davies, C. C. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.05.007 · Cited by 346
Xu, Y., Ayrapetov, M. K., Xu, C., Gursoy-Yuzugullu, O., Hu, Y., & Price, B. D. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.026 · Cited by 336
Self-citationATM-Dependent and -Independent Dynamics of the Nuclear Phosphoproteome After DNA Damage
Bensimon, A., Schmidt, A., Ziv, Y., Elkon, R., Wang, S., Chen, D. J., Aebersold, R. H., & Shiloh, Y. (2010) · Science Signaling · doi:10.1126/scisignal.2001034 · Cited by 290
Li, X., Corsa, C. A. S., Pan, P. W., Wu, L., Ferguson, D. O., Yu, X., Min, J., & Dou, Y. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00350-10 · Cited by 203
Lysine acetylation and cancer: A proteomics perspective
Gil, J., Ramírez-Torres, A., & Encarnación‐Guevara, S. (2016) · Journal of Proteomics · doi:10.1016/j.jprot.2016.10.003 · Cited by 191
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
Johnson, S. M., Torrice, C. D., Bell, J. F., Monahan, K. B., Jiang, Q., Wang, Y., Ramsey, M. R., Jin, J., Wong, K.-K., Su, L., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci41402 · Cited by 168
Chromatin dynamics and the repair of DNA double strand breaks
Xu, Y., & Price, B. D. (2011) · Cell Cycle · doi:10.4161/cc.10.2.14543 · Cited by 172
Self-citationKlingelhutz, A. J., & Roman, A. (2012) · Virology · doi:10.1016/j.virol.2011.12.018 · Cited by 177
ATM-Dependent Phosphorylation of All Three Members of the MRN Complex: From Sensor to Adaptor
Lavin, M. F., Kozlov, S., Gatei, M. H., & Kijas, A. W. (2015) · Biomolecules · doi:10.3390/biom5042877 · Cited by 164
Sirtuin 1 (SIRT1): The Misunderstood HDAC
Stünkel, W., & Campbell, R. M. (2011) · SLAS DISCOVERY · doi:10.1177/1087057111422103 · Cited by 154
ATM kinase: Much more than a DNA damage responsive protein
Guleria, A., & Chandna, S. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.12.009 · Cited by 147
Robert, C., & Rassool, F. V. (2012) · Advances in cancer research · doi:10.1016/b978-0-12-394387-3.00003-3 · Cited by 140
Cann, K. L., & Dellaire, G. (2011) · Biochemistry and Cell Biology · doi:10.1139/o10-113 · Cited by 140
KATs in cancer: functions and therapies
Farria, A. T., Li, W., & Dent, S. (2015) · Oncogene · doi:10.1038/onc.2014.453 · Cited by 134
Acetylation Reader Proteins: Linking Acetylation Signaling to Genome Maintenance and Cancer
Gong, F., Chiu, L.-Y., & Miller, K. M. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1006272 · Cited by 137
Structure and Mechanisms of Lysine Methylation Recognition by the Chromodomain in Gene Transcription
Yap, K. L., & Zhou, M. (2011) · Biochemistry · doi:10.1021/bi101885m · Cited by 126
The multifaceted proteins Reptin and Pontin as major players in cancer
Grigoletto, A., Lestienne, P. P., & Rosenbaum, J. (2010) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2010.11.002 · Cited by 124
The role of protein lactylation: A kaleidoscopic post-translational modification in cancer
Iozzo, M., Pardella, E., Giannoni, E., & Chiarugi, P. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.02.011 · Cited by 126
The tale of a tail: histone H4 acetylation and the repair of DNA breaks
Dhar, S., Gürsoy-Yüzügüllü, Ö., Parasuram, R., & Price, B. D. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0284 · Cited by 123
Self-citationBRCA Mutations in Ovarian and Prostate Cancer: Bench to Bedside
Boussios, S., Rassy, E., Moschetta, M., Ghose, A., Adeleke, S. M., Sanchez, E., Sheriff, M., Chargari, C., & Pavlidis, N. A. (2022) · Cancers · doi:10.3390/cancers14163888 · Cited by 117
Laurberg, J. R., Brems-Eskildsen, A. S., Nordentoft, I., Fristrup, N., Schepeler, T., Ulhøi, B. P., Agerbæk, M., Hartmann, A., Bertz, S., Wittlinger, M., et al. (2012) · British Journal of Urology · doi:10.1111/j.1464-410x.2012.11564.x · Cited by 100
Insight into the mechanisms of action of estrogen receptor β in the breast, prostate, colon, and CNS
Dey, P., Barros, R. P. A., Warner, M. N., Ström, A., & Gustafsson, J.-Α. (2013) · Journal of Molecular Endocrinology · doi:10.1530/jme-13-0150 · Cited by 98
Role of Histone-Modifying Enzymes and Their Complexes in Regulation of Chromatin Biology
DesJarlais, R. L., & Tummino, P. J. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01210 · Cited by 100
Liu, C., Srihari, S., Cao, K. L., Chenevix‐Trench, G., Simpson, P. T., Ragan, M. A., & Khanna, K. K. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku284 · Cited by 91
Participation of Chromatin-Remodeling Proteins in the Repair of Ultraviolet-B-Damaged DNA
Campi, M., D’Andrea, L., Emiliani, J., & Casati, P. (2011) · PLANT PHYSIOLOGY · doi:10.1104/pp.111.191452 · Cited by 91
Russo, G., Landi, R., Pezone, A., Morano, A., Zuchegna, C., Romano, A., Muller, M. T., Gottesman, M. E., Porcellini, A., & Avvedimento, E. V. (2016) · Scientific Reports · doi:10.1038/srep33222 · Cited by 86
Kari, V., Shchebet, A., Neumann, H., & Johnsen, S. A. (2011) · Cell Cycle · doi:10.4161/cc.10.20.17769 · Cited by 90
Deubiquitination of Tip60 by USP7 determines the activity of the p53-dependent apoptotic pathway.
Dar, A., Shibata, E., & Dutta, A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00358-13 · Cited by 83
SUMOylation and de‐SUMOylation in response to DNA damage
Dou, H., Huang, C., Nguyen, T. V., Lu, L., & Yeh, E. T. H. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.04.002 · Cited by 88
Zhao, Y. J., Brickner, J. R., Majid, M. C., & Mosammaparast, N. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.01.005 · Cited by 79
Wang, Q., & Goldstein, M. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-2334 · Cited by 78
Li, F., Xu, Y., Liu, B., Singh, P. K., Zhao, W., Jin, J., Han, G., Scott, A. W., Dong, X., Huo, L., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-18-1029 · Cited by 78
Immediate-Early, Early, and Late Responses to DNA Double Stranded Breaks
Kieffer, S. R., & Lowndes, N. F. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.793884 · Cited by 76
DNA damage regulation and its role in drug-related phenotypes in the malaria parasites
Gupta, D. K., Patra, A. T., Zhu, L., Gupta, A. P., & Bozdech, Z. (2016) · Scientific Reports · doi:10.1038/srep23603 · Cited by 68
BRCA1 in the DNA damage response and at telomeres
Rosen, E. M. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00085 · Cited by 68
NOTCH1 Inhibits Activation of ATM by Impairing the Formation of an ATM-FOXO3a-KAT5/Tip60 Complex
Adamowicz, M., Vermezovic, J., & di Fagagna, F. D. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.07.038 · Cited by 69
Ikura, M., Furuya, K., Matsuda, S., Matsuda, R., Shima, H., Adachi, J., Matsuda, T., Shiraki, T., & Ikura, T. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00757-15 · Cited by 70
E3 ligase EDD1/UBR5 is utilized by the HPV E6 oncogene to destabilize tumor suppressor TIP60
Subbaiah, V. K., Zhang, Y., Rajagopalan, D., Abdullah, L. N., Yeo-Teh, N. S. L., Tomaić, V., Banks, L., Myers, M. P., Chow, E. K., & Jha, S. (2015) · Oncogene · doi:10.1038/onc.2015.268 · Cited by 66
Targeting cancer using KAT inhibitors to mimic lethal knockouts
Brown, J. A. L., Bourke, E., Eriksson, L. A., & Kerin, M. J. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160081 · Cited by 66
Histone acetylation dynamics in repair of DNA double-strand breaks
Aricthota, S., Rana, P. P., & Haldar, D. (2022) · Frontiers in Genetics · doi:10.3389/fgene.2022.926577 · Cited by 67
Crafting the Brain – Role of Histone Acetyltransferases in Neural Development and Disease
Sheikh, B. N. (2014) · Cell and Tissue Research · doi:10.1007/s00441-014-1835-7 · Cited by 59
Cellular functions of programmed cell death 5
Li, G., Ma, D., & Chen, Y. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2015.12.021 · Cited by 59
Radhakrishnan, R., Li, Y., Xiang, S., Yuan, F., Yuan, Z., Telles, E., Fang, J., Coppola, D., Shibata, D., Lane, W. S., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.612945 · Cited by 59
O’Hagan, H. M. (2013) · Environmental and Molecular Mutagenesis · doi:10.1002/em.21830 · Cited by 62
Bromodomain coactivators in cancer, obesity, type 2 diabetes, and inflammation.
Denis, G. V. (2010) · PubMed · Cited by 57
KMT Set7/9 affects genotoxic stress response via the Mdm2 axis
Lezina, L., Aksenova, V., Fedorova, O., Kriger, D. V., Shuvalov, O. Y., Antonov, A. V., Tentler, D., Garabadgiu, A. V., Melino, G., & Barlev, N. A. (2015) · Oncotarget · doi:10.18632/oncotarget.4584 · Cited by 55
Microarray Analysis Uncovers a Role for Tip60 in Nervous System Function and General Metabolism
Lorbeck, M. T., Pirooznia, K., Sarthi, J. B., Zhu, X., & Elefant, F. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018412 · Cited by 57
Su, Q., Jing, J., Li, W., Ma, J., Zhang, X., Wang, Z., Zhou, Z., Dai, L., & Shao, L. (2019) · Journal of Autoimmunity · doi:10.1016/j.jaut.2019.02.007 · Cited by 52
Role of primary aging hallmarks in Alzheimer´s disease
Zhao, J., & Huai, J. (2022) · Theranostics · doi:10.7150/thno.79535 · Cited by 55
MYC in Germinal Center‐derived lymphomas: Mechanisms and therapeutic opportunities
Bisso, A., Sabò, A., & Amati, B. B. (2019) · Immunological Reviews · doi:10.1111/imr.12734 · Cited by 51
Overview for the Histone Codes for DNA Repair
Williamson, E. A., Wray, J. W., Bansal, P., & Hromas, R. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-387665-2.00008-0 · Cited by 50
Clinical potential of ATM inhibitors
Lavin, M. F., & Yeo, A. J. (2020) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2020.111695 · Cited by 51
To spread or not to spread—chromatin modifications in response to DNA damage
Altmeyer, M., & Lukas, J. (2013) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2012.11.001 · Cited by 53
Dynamics of double strand breaks and chromosomal translocations
Iarovaia, O. V., Rubtsov, M. A., Ioudinkova, E. S., Tsfasman, T., Razin, S. V., & Vassetzky, Y. S. (2014) · Molecular Cancer · doi:10.1186/1476-4598-13-249 · Cited by 52
Lario, L. D., Ramírez-Parra, E., Gutiérrez, C., Spampinato, C. P., & Casati, P. (2013) · PLANT PHYSIOLOGY · doi:10.1104/pp.112.212837 · Cited by 52
RVBs Are Required for Assembling a Functional TIP60 Complex
Jha, S., Gupta, A. K., Dar, A., & Dutta, A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01567-12 · Cited by 54
VRK1 Phosphorylates Tip60/KAT5 and Is Required for H4K16 Acetylation in Response to DNA Damage
García-González, R., Morejón‐García, P., Campillo‐Marcos, I., Salzano, M., & Lazo, P. A. (2020) · Cancers · doi:10.3390/cancers12102986 · Cited by 47
Bromodomain proteins: repairing DNA damage within chromatin
Chiu, L.-Y., Gong, F., & Miller, K. M. (2017) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2016.0286 · Cited by 49
Ghobashi, A. H., & Kamel, M. A. E.-N. (2018) · Journal of Applied Genetics · doi:10.1007/s13353-018-0432-y · Cited by 47
RNA Splicing: A New Player in the DNA Damage Response
Lenzken, S. C., Loffreda, A., & Barabino, S. M. L. (2013) · International Journal of Cell Biology · doi:10.1155/2013/153634 · Cited by 48
Histone modifications in DNA damage response
Cao, L., Shen, C., & Zhu, W. (2016) · Science China Life Sciences · doi:10.1007/s11427-016-5011-z · Cited by 47
ATM Mediates pRB Function To Control DNMT1 Protein Stability and DNA Methylation
Shamma, A., Suzuki, M., Hayashi, N., Kobayashi, M., Sasaki, N., Nishiuchi, T., Doki, Y., Okamoto, T., Kohno, S., Muranaka, H., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01597-12 · Cited by 45
Hong, S., Dutta, A., & Laimins, L. A. (2015) · Journal of Virology · doi:10.1128/jvi.03455-14 · Cited by 44
Belle, J. I., & Nijnik, A. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.03.004 · Cited by 46
Huo, D., Chen, H., Cheng, Y., Song, X., Zhang, K., Li, M. J., & Xuan, C. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0397-3 · Cited by 42
Plant programmed cell death from a chromatin point of view
Latrasse, D., Benhamed, M., Catherine Bergounioux, A., Raynaud, C., & Delarue, M. (2016) · Journal of Experimental Botany · doi:10.1093/jxb/erw329 · Cited by 43
ATP Hydrolysis by RAD50 Protein Switches MRE11 Enzyme from Endonuclease to Exonuclease
Majka, J., Alford, B. D., Ausió, J., Finn, R. M., & McMurray, C. T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.307041 · Cited by 40
Antoch, M. P., & Kondratov, R. V. (2013) · Handbook of experimental pharmacology · doi:10.1007/978-3-642-25950-0_12 · Cited by 41
Mechanism of Histone H3K4me3 Recognition by the Plant Homeodomain of Inhibitor of Growth 3
Kim, S., Natesan, S., Cornilescu, G., Carlson, S., Tonelli, M., McClurg, U. L., Binda, O., Robson, C. N., Markley, J. L., Baláž, Š., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.690651 · Cited by 39
HIV-1 Tat impairs cell cycle control by targeting the Tip60, Plk1 and cyclin B1 ternary complex
Zhang, S., Song, M., Yang, T., Fan, R., Liu, X., & Zhou, P. (2012) · Cell Cycle · doi:10.4161/cc.11.6.19664 · Cited by 35
Regulation of Histone Acetyltransferase TIP60 Function by Histone Deacetylase 3
Yi, J., Huang, X., Yang, Y., Zhu, W., Gu, W. J., & Luo, J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.575266 · Cited by 38
CHFR: a key checkpoint component implicated in a wide range of cancers
Sanbhnani, S., & Yeong, F. M. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0892-2 · Cited by 37
Mutual regulation of TGFβ-induced oncogenic EMT, cell cycle progression and the DDR
Schuhwerk, H., & Brabletz, T. (2023) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2023.11.009 · Cited by 35
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
McKenzie, J., López‐Giráldez, F., Delecluse, H., Walsh, A., & El-Guindy, A. S. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1006008 · Cited by 35
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
Xu, J., Li, C., & Kang, X. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1267456 · Cited by 32
MDR1 mediated chemoresistance: BMI1 and TIP60 in action
Mustafi, S. B., Chakraborty, P. K., Naz, S., Dwivedi, S. K. D., Street, M., Basak, R., Yang, D., Ding, K., Mukherjee, P., & Bhattacharya, R. (2016) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2016.06.002 · Cited by 32
Quantifying Tip60 (Kat5) stratifies breast cancer
McGuire, A., Casey, M., Shalaby, A., Kalinina, O., Curran, C. E., Webber, M., Callagy, G. M., Holian, E., Bourke, E., Kerin, M. J., et al. (2019) · Scientific Reports · doi:10.1038/s41598-019-40221-5 · Cited by 34
Du, J., Fu, L., Ji, F., Wang, C., Liu, S., & Qiu, X. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118374 · Cited by 31
KAT5 promotes invasion and metastasis through C-MYC stabilization in ATC
Wei, X., Cai, S., Boohaker, R. J., Fried, J. S., Li, Y., Hu, L., Pan, Y., Cheng, R., Zhang, S., Tian, Y., et al. (2018) · Endocrine Related Cancer · doi:10.1530/erc-18-0193 · Cited by 29
Naik, N. G., Nguyen, T. H., Roberts, L., Fischer, L. T., Glickman, K., Golas, G., Papp, B., & Tóth, Z. (2020) · PLoS Pathogens · doi:10.1371/journal.ppat.1008268 · Cited by 28
Modulation of Nuclear Receptor Function by Chromatin Modifying Factor TIP60
Jaiswal, B., & Gupta, A. K. (2018) · Endocrinology · doi:10.1210/en.2017-03190 · Cited by 32
Coordinated methyl readers: Functional communications in cancer
Park, I.-G., Jeon, M., Kim, H.-K., & Lee, J. M. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.03.015 · Cited by 29
Pal, D., Raj, K., Nandi, S. S., Sinha, S., Mishra, A., Mondal, A., Lagoa, R., Burcher, J. T., & Bishayee, A. (2023) · Cancers · doi:10.3390/cancers15102808 · Cited by 29
AtPDCD5 Plays a Role in Programmed Cell Death after UV-B Exposure in Arabidopsis
Ferreyra, M. L. F., Casadevall, R., D’Andrea, L., AbdElgawad, H., Beemster, G. T. S., & Casati, P. (2016) · PLANT PHYSIOLOGY · doi:10.1104/pp.16.00033 · Cited by 29
Palmieri, D., Scarpa, M., Tessari, A., Uka, R., Amari, F., Lee, C., Richmond, T. K., Foray, C., Sheetz, T. J., Braddom, A. E., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.7813 · Cited by 29
Nuclear Remodeling as a Mechanism for Genomic Instability in Cancer
Gadji, M., Vallente, R. U., Klewes, L., Righolt, C. H., Wark, L., Kongruttanachok, N., Knecht, H., & Mai, S. (2011) · Advances in cancer research · doi:10.1016/b978-0-12-387688-1.00004-1 · Cited by 28
Increased Pontin expression is a potential predictor for outcome in sporadic colorectal carcinoma
Lauscher, J. C., Elezkurtaj, S., Dullat, S., Lipka, S., Gröne, J., Buhr, H. J., Huber, O., & Kruschewski, M. (2012) · Oncology Reports · doi:10.3892/or.2012.1968 · Cited by 28
Critical DNA damaging pathways in tumorigenesis
Kloeber, J. A., & Lou, Z. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.04.012 · Cited by 30
Integration of DNA damage responses with dynamic spatial genome organization
Stanić, M., & Mekhail, K. (2021) · Trends in Genetics · doi:10.1016/j.tig.2021.08.016 · Cited by 28
Nucleotide excision repair efficiency in quiescent human fibroblasts is modulated by circadian clock
Bee, L., Marini, S., Pontarin, G., Ferraro, P., Costa, R., Albrecht, U., & Celotti, L. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv081 · Cited by 27
García-González, R., Monte-Serrano, E., Morejón‐García, P., Navarro-Carrasco, E., & Lazo, P. A. (2022) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2022.194887 · Cited by 26
Metadata
- Authors
- Sun, Y., Jiang, X., & Price, B. D.
- Affiliations
- Harvard University (US)
- Corresponding author
- Price, Brendan D.
- Venue
- Cell Cycle
- Publisher
- Informa UK Limited
- Published
- 2010-03
- Volume
- 9
- Issue
- 5
- Pages
- 930-936
- ISSN
- 1538-4101 (ISSN-L)
- 1551-4005
- PMC
- PMC2901859
- OpenAlex
- W2072607093
- Cited by
- 230
- References
- 85
- Citations by year
- 2026: 8 · 2025: 16 · 2024: 11 · 2023: 9 · 2022: 14 · 2021: 13 · 2020: 10 · 2019: 8 · 2018: 8 · 2017: 5 · 2016: 28 · 2015: 19 · 2014: 18 · 2013: 18 · 2012: 18
- FWCI
- 1.77
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Cell Cycle (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- U.S. Department of Defense
- National Cancer Institute (T32 CA09078, R01CA064585, R01CA093602, CA09078, CA64585, T32CA009078, CA93602)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- Tip60, ATM kinase, DNA double-strand break repair, DNA damage response, MRN complex, histone H3 lysine 9 trimethylation, chromodomain, chromatin structure, histone modifications, genomic instability, cancer
- MeSH terms
- Lysine Acetyltransferase 5, MRE11 Homologue Protein, Chromatin, DNA Repair, DNA-Binding Proteins, Histones, Humans, Signal Transduction, Protein Serine-Threonine Kinases, Cell Cycle Proteins, Tumor Suppressor Proteins, Histone Acetyltransferases, DNA Breaks, Double-Stranded, Ataxia Telangiectasia Mutated Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review