Cancer epigenetics: from mechanism to therapy
Open accessAbstract
The epigenetic regulation of DNA-templated processes has been intensely studied over the last 15 years. DNA methylation, histone modification, nucleosome remodeling, and RNA-mediated targeting regulate many biological processes that are fundamental to the genesis of cancer. Here, we present the basic principles behind these epigenetic pathways and highlight the evidence suggesting that their misregulation can culminate in cancer. This information, along with the promising clinical and preclinical results seen with epigenetic drugs against chromatin regulators, signifies that it is time to embrace the central role of epigenetics in cancer.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Hypomethylation of repetitive elements in cancer cells can lead to activation and transposition of endogenous retroviral sequences, promoting genetic instability and tumour development.
“Nevertheless, hypomethylation of these elements is observed in cancer cells 26,27 and this can lead to activation and transposition of the endogenous retroviral sequences thereby promoting genetic instability and tumour development 1 (Figure 2).”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [1]
Pervasive mutations occur in a range of enzymes that methylate and de-methylate DNA and histones.
“A major finding from the cancer genome efforts has been that pervasive mutations occur in a range of enzymes that methylate and de-methylate DNA and histones 1,89 .”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [1]
Epigenetic alterations play important roles in driving cancer initiation and progression.
“Many reports have demonstrated that epigenetic alterations play important roles in driving cancer initiation and progression [123, 124].”
From Non-viral delivery systems for CRISPR/Cas9-based genome editing: challenges and opportunities (2018) · cites this paper as [124]
Cites
Hallmarks of Cancer: The Next Generation
Hanahan, D., & Weinberg, R. A. (2011) · Cell · doi:10.1016/j.cell.2011.02.013 · Cited by 66,590 · see citing works
Chromatin modifications and their function
Kouzarides, T. (2007) · Cell · doi:10.1016/j.cell.2007.02.005 · Cited by 10,883 · see citing works
Self-citationThe Cancer Cell Line Encyclopedia enables predictive modelling of anticancer drug sensitivity
Barretina, J., Caponigro, G., Stransky, N., Venkatesan, K., Margolin, A. A., Kim, S., Wilson, C. J., Lehár, J., Kryukov, G. V., Sonkin, D., et al. (2012) · Nature · doi:10.1038/nature11003 · Cited by 7,950 · see citing works
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 · see citing works
Okano, M., Bell, D. W., Haber, D. A., & Li, E. (1999) · Cell · doi:10.1016/s0092-8674(00)81656-6 · Cited by 6,143 · see citing works
Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1
Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., et al. (2009) · Science · doi:10.1126/science.1170116 · Cited by 5,836 · see citing works
A bivalent chromatin structure marks key developmental genes in embryonic stem cells
Bernstein, B. E., Mikkelsen, T. S., Xie, X., Kamal, M., Huebert, D. J., Cuff, J., Fry, B., Meissner, A., Wernig, M., Plath, K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.02.041 · Cited by 5,361 · see citing works
Molecular Mechanisms of Long Noncoding RNAs
Wang, K., & Chang, H. Y. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.018 · Cited by 4,390 · see citing works
Selective inhibition of BET bromodomains
Filippakopoulos, P., Qi, J., Picaud, S., Shen, Y., Smith, W. B., Fedorov, O., Morse, E. M., Keates, T., Hickman, T. T., Felletar, I., et al. (2010) · Nature · doi:10.1038/nature09504 · Cited by 4,262 · see citing works
Lysine acetylation targets protein complexes and co-regulates major cellular functions
Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040 · see citing works
Targeted mutation of the DNA methyltransferase gene results in embryonic lethality
Li, E., Bestor, T. H., & Jaenisch, R. (1992) · Cell · doi:10.1016/0092-8674(92)90611-f · Cited by 3,984 · see citing works
Stratton, M. R., Campbell, P. J., & Futreal, P. A. (2009) · Nature · doi:10.1038/nature07943 · Cited by 3,458 · see citing works
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 · cited 2× · see citing works
“Consistent with this, ChIP- Seq analyses have confirmed the distribution of histone acetylation at promoters and enhancers and, in some cases, throughout the transcribed region of active genes (Heintzman et al., 2007; Wang et al., 2008).”
BackgroundThe Polycomb complex PRC2 and its mark in life
Margueron, R., & Reinberg, D. (2011) · Nature · doi:10.1038/nature09784 · Cited by 3,347 · see citing works
Xu, W., Yang, H., Liu, Y., Yang, Y., Wang, P., Kim, S.-H., Ito, S., Yang, C., Wang, P., Xiao, M.-T., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2010.12.014 · Cited by 2,875 · see citing works
A decade of exploring the cancer epigenome—biological and translational implications
Baylin, S. B., & Jones, P. A. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3130 · Cited by 2,871 · see citing works
DNA methylation and human disease
Robertson, K. D. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1655 · Cited by 2,864 · see citing works
BET Bromodomain Inhibition as a Therapeutic Strategy to Target c-Myc
Delmore, J. E., Issa, G. C., Lemieux, M. E., Rahl, P. B., Shi, J., Jacobs, H. M., Kastritis, E., Gilpatrick, T., Paranal, R. M., Qi, J., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.017 · Cited by 2,820 · see citing works
Tumorigenic conversion of primary embryo fibroblasts requires at least two cooperating oncogenes
Land, H., Parada, L. F., & Weinberg, R. A. (1983) · Nature · doi:10.1038/304596a0 · Cited by 2,804 · see citing works
The Nuclear DNA Base 5-Hydroxymethylcytosine Is Present in Purkinje Neurons and the Brain
Kriaucionis, S., & Heintz, N. (2009) · Science · doi:10.1126/science.1169786 · Cited by 2,700 · see citing works
Fenaux, P., Mufti, G. J., Hellstrom-Lindberg, E., Santini, V., Finelli, C., Giagounidis, A., Schoch, R., Gattermann, N., Sanz, G., List, A., et al. (2009) · The Lancet Oncology · doi:10.1016/s1470-2045(09)70003-8 · Cited by 2,663 · see citing works
ACETYLATION AND METHYLATION OF HISTONES AND THEIR POSSIBLE ROLE IN THE REGULATION OF RNA SYNTHESIS
Allfrey, V. G., Faulkner, R. D., & Mirsky, A. E. (1964) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.51.5.786 · Cited by 2,649 · see citing works
Driver mutations in histone H3.3 and chromatin remodelling genes in paediatric glioblastoma
Schwartzentruber, J., Korshunov, A., Liu, X.-Y., Jones, D. T. W., Pfaff, E., Jacob, K., Sturm, D., Fontebasso, A. M., Quang, D.-A. K., Tönjes, M., et al. (2012) · Nature · doi:10.1038/nature10833 · Cited by 2,631 · see citing works
Histone modifications at human enhancers reflect global cell-type-specific gene expression
Heintzman, N. D., Hon, G. C., Hawkins, R. D., Kheradpour, P., Stark, A., Harp, L. F., Ye, Z., Lee, L. K., Stuart, R. K., Ching, C. W., et al. (2009) · Nature · doi:10.1038/nature07829 · Cited by 2,533 · see citing works
Genomic DNA methylation: the mark and its mediators.
Klose, R. J., & Bird, A. P. (2006) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2005.12.008 · Cited by 2,501 · see citing works
Systematic identification of genomic markers of drug sensitivity in cancer cells
Garnett, M. J., Edelman, E. J., Heidorn, S. J., Greenman, C. D., Dastur, A., Lau, K. W., Greninger, P., Thompson, I. R., Luo, X., Soares, J., et al. (2012) · Nature · doi:10.1038/nature11005 · Cited by 2,456 · see citing works
The history of cancer epigenetics
Feinberg, A. P., & Tycko, B. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1279 · Cited by 2,350 · see citing works
Combinatorial patterns of histone acetylations and methylations in the human genome
Wang, Z., Zang, C., Rosenfeld, J. A., Schones, D. E., Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Peng, W., Zhang, M. Q., et al. (2008) · Nature Genetics · doi:10.1038/ng.154 · Cited by 2,331 · see citing works
COSMIC: mining complete cancer genomes in the Catalogue of Somatic Mutations in Cancer
Forbes, S. A., Bindal, N., Bamford, S., Cole, C., Kok, C. Y., Beare, D., Jia, M., Shepherd, R., Leung, K., Menzies, A., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq929 · Cited by 2,278 · see citing works
ChIP–seq: advantages and challenges of a maturing technology
Park, P. J. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2641 · Cited by 2,217 · see citing works
Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
Minucci, S., & Pelicci, P. G. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1779 · Cited by 2,211 · see citing works
<i>DNMT3A</i> Mutations in Acute Myeloid Leukemia
Ley, T. J., Ding, L., Walter, M. J., McLellan, M. D., Lamprecht, T., Larson, D. E., Kandoth, C., Payton, J. E., Baty, J., Welch, J., et al. (2010) · New England Journal of Medicine · doi:10.1056/nejmoa1005143 · Cited by 1,983 · see citing works
Prognostic Relevance of Integrated Genetic Profiling in Acute Myeloid Leukemia
Patel, J. P., Gönen, M., Figueroa, M. E., Fernandez, H. F., Sun, Z., Racevskis, J., Vlierberghe, P. V., Dolgalev, I., Thomas, S., Aminova, O., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1112304 · Cited by 1,936 · see citing works
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 · see citing works
Tan, M., Luo, H., Lee, S., Jin, F., Yang, J. S., Montellier, E., Buchou, T., Cheng, Z., Rousseaux, S., Rajagopal, N., et al. (2011) · Cell · doi:10.1016/j.cell.2011.08.008 · Cited by 1,902 · see citing works
An operational definition of epigenetics: Figure 1.Preprint
Berger, S. L., Kouzarides, T., Shiekhattar, R., & Shilatifard, A. (2009) · Genes & Development · doi:10.1101/gad.1787609 · Cited by 1,889 · see citing works
Self-citationRNAi screen identifies Brd4 as a therapeutic target in acute myeloid leukaemia
Zuber, J., Shi, J., Wang, E., Rappaport, A. R., Herrmann, H., Sison, E. A., Magoon, D., Qi, J., Blatt, K., Wunderlich, M., et al. (2011) · Nature · doi:10.1038/nature10334 · Cited by 1,870 · see citing works
The CBP co-activator is a histone acetyltransferase
Bannister, A. J., & Kouzarides, T. (1996) · Nature · doi:10.1038/384641a0 · Cited by 1,824 · see citing works
Self-citationMutation in <i>TET2</i> in Myeloid Cancers
Delhommeau, F., Dupont, S., Valle, V. D., James, C., Trannoy, S., Massé, A., Kosmider, O., Le Couedic, J.-P., Robert, F., Alberdi, A., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0810069 · Cited by 1,776 · see citing works
Addiction to Oncogenes--the Achilles Heal of Cancer
Weinstein, I. (2002) · Science · doi:10.1126/science.1073096 · Cited by 1,753 · see citing works
St. Jude Children's Research Hospital–Washington University Pediatric Cancer Genome Project (2012) · Nature Genetics · doi:10.1038/ng.1102 · Cited by 1,724 · see citing works
Jiao, Y., Shi, C., Edil, B. H., de Wilde, R. F., Klimstra, D. S., Maitra, A., Schulick, R. D., Tang, L. H., Wolfgang, C. L., Choti, M. A., et al. (2011) · Science · doi:10.1126/science.1200609 · Cited by 1,717 · see citing works
Morin, R. D., Johnson, N. A., Severson, T., Mungall, A. J. J., An, J., Goya, R., Paul, J. E., Boyle, M., Woolcock, B. W., Kuchenbauer, F. C., et al. (2010) · Nature Genetics · doi:10.1038/ng.518 · Cited by 1,670 · see citing works
Frequent mutation of histone-modifying genes in non-Hodgkin lymphoma
Morin, R. D., Mendez-Lago, M., Mungall, A. J., Goya, R., Mungall, K. L., Corbett, R. D., Johnson, N. A., Severson, T. M., Chiu, R., Field, M., et al. (2011) · Nature · doi:10.1038/nature10351 · Cited by 1,614 · see citing works
The genetic basis of early T-cell precursor acute lymphoblastic leukaemia
Zhang, J., Ding, L., Holmfeldt, L., Wu, G., Heatley, S. L., Payne-Turner, D., Easton, J., Chen, X., Wang, J., Rusch, M., et al. (2012) · Nature · doi:10.1038/nature10725 · Cited by 1,596 · cited 3× · see citing works
“, 2010) and T-ALL (Ntziachristos et al., 2012; Zhang et al., 2012), suggesting a tumor-suppressive role for EZH2 in these cell lineages.”
BackgroundReflecting on 25 years with MYC
Meyer, N., & Penn, L. Z. (2008) · Nature Reviews Cancer · doi:10.1038/nrc2231 · Cited by 1,575 · see citing works
Principles and challenges of genome-wide DNA methylation analysis
Laird, P. W. (2010) · Nature Reviews Genetics · doi:10.1038/nrg2732 · Cited by 1,574 · see citing works
Suppression of inflammation by a synthetic histone mimic
Nicodeme, E., Jeffrey, K. L., Schaefer, U., Beinke, S., Dewell, S., Chung, C.-W., Chandwani, R., Marazzi, I., Wilson, P., Coste, H., et al. (2010) · Nature · doi:10.1038/nature09589 · Cited by 1,563 · see citing works
Truncating mutations of hSNF5/INI1 in aggressive paediatric cancer
Versteege, I., Sévenet, N., Lange, J., Rousseau-Merck, M.-F., Ambros, P. F., Handgretinger, R., Aurias, A., & Delattre, O. (1998) · Nature · doi:10.1038/28212 · Cited by 1,552 · see citing works
Inhibition of BET recruitment to chromatin as an effective treatment for MLL-fusion leukaemia
Dawson, M. A., Prinjha, R. K., Dittmann, A., Giotopoulos, G., Bantscheff, M., Chan, W.-I., Robson, S. C., Chung, C., Hopf, C., Savitski, M. M., et al. (2011) · Nature · doi:10.1038/nature10509 · Cited by 1,512 · see citing works
Self-citationInitial genome sequencing and analysis of multiple myeloma
Chapman, M. A., Lawrence, M. S., Keats, J. J., Cibulskis, K., Sougnez, C. L., Schinzel, A. C., Harview, C. L., Brunet, J.-P., Ahmann, G. J., Adli, M., et al. (2011) · Nature · doi:10.1038/nature09837 · Cited by 1,422 · see citing works
Taverna, S. D., Li, H., Ruthenburg, A. J., Allis, C. D., & Patel, D. J. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1338 · Cited by 1,419 · see citing works
Tet2 loss leads to increased hematopoietic stem cell self-renewal and myeloid transformation
Moran-Crusio, K., Reavie, L., Shih, A., Abdel-Wahab, O., Ndiaye-Lobry, D., Lobry, C., Figueroa, M. E., Vasanthakumar, A., Patel, J., Zhao, X., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.06.001 · Cited by 1,339 · see citing works
MLL translocations, histone modifications and leukaemia stem-cell development
Krivtsov, A., & Armstrong, S. (2007) · Nature Reviews. Cancer · doi:10.1038/nrc2253 · Cited by 1,294 · see citing works
SWI/SNF nucleosome remodellers and cancer
Wilson, B. G., & Roberts, C. W. M. (2011) · Nature reviews. Cancer · doi:10.1038/nrc3068 · Cited by 1,286 · see citing works
Exome sequencing identifies frequent mutation of the SWI/SNF complex gene PBRM1 in renal carcinoma
Varela, I., Tarpey, P. S., Raine, K. M., Huang, D., Ong, C. K., Stephens, P., Davies, H. R., Jones, D., Lin, M., Teague, J. W., et al. (2011) · Nature · doi:10.1038/nature09639 · Cited by 1,278 · see citing works
Kogo, R., Shimamura, T., Mimori, K., Kawahara, K., Imoto, S., Sudo, T., Tanaka, F., Shibata, K., Suzuki, A., Komune, S., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-1021 · Cited by 1,238 · see citing works
Frequent Mutations of Chromatin Remodeling Gene ARID1A in Ovarian Clear Cell Carcinoma
Jones, S., Wang, T., Shih, I., Mao, T., Nakayama, K., Roden, R. B. S., Glas, R., Slamon, D. J., Diaz, L. A., Vogelstein, B., et al. (2010) · Science · doi:10.1126/science.1196333 · Cited by 1,218 · see citing works
Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes
Dalgliesh, G. L., Furge, K., Greenman, C., Chen, L., Bignell, G., Butler, A., Davies, H., Edkins, S., Hardy, C., Latimer, C., et al. (2010) · Nature · doi:10.1038/nature08672 · Cited by 1,173 · see citing works
Inactivating mutations of the histone methyltransferase gene EZH2 in myeloid disorders
Ernst, T., Chase, A. J., Score, J., Hidalgo-Curtis, C. E., Bryant, C., Jones, A. V., Waghorn, K., Zoi, K., Ross, F. M., Reiter, A., et al. (2010) · Nature Genetics · doi:10.1038/ng.621 · Cited by 1,139 · see citing works
Ohm, J. E., McGarvey, K. M., Yu, X., Cheng, L., Schuebel, K. E., Cope, L., Mohammad, H. P., Chen, W., Daniel, V. C., Yu, W., et al. (2007) · Nature Genetics · doi:10.1038/ng1972 · Cited by 1,130 · see citing works
Targeting MYC dependence in cancer by inhibiting BET bromodomains
Mertz, J. A., Conery, A. R., Bryant, B. M., Sandy, P., Balasubramanian, S., Mele, D. A., Bergeron, L., & Sims, R. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1108190108 · Cited by 1,118 · see citing works
Stucki, M., Clapperton, J. A., Mohammad, D. H., Yaffe, M. B., Smerdon, S. J., & Jackson, S. P. (2005) · Cell · doi:10.1016/j.cell.2005.09.038 · Cited by 1,103 · see citing works
Global histone modification patterns predict risk of prostate cancer recurrence
Seligson, D. B., Horvath, S., Shi, T., Yu, H., Tze, S., Grunstein, M. R., & Kurdistani, S. K. (2005) · Nature · doi:10.1038/nature03672 · Cited by 1,090 · see citing works
Olsen, E. A., Kim, Y. H., Kuzel, T. M., Pacheco, T. R., Foss, F. M., Parker, S. R. S., Frankel, S. R., Chen, C., Ricker, J. L., Arduino, J. M., et al. (2007) · Journal of Clinical Oncology · doi:10.1200/jco.2006.10.2434 · Cited by 1,057 · see citing works
Inactivating mutations of acetyltransferase genes in B-cell lymphoma
Pasqualucci, L., Dominguez-Sola, D., Chiarenza, A., Fabbri, G., Grunn, A., Trifonov, V., Kasper, L. H., Lerach, S., Tang, H., Ma, J., et al. (2011) · Nature · doi:10.1038/nature09730 · Cited by 949 · see citing works
Selective Killing of Mixed Lineage Leukemia Cells by a Potent Small-Molecule DOT1L Inhibitor
Daigle, S. R., Olhava, E. J., Therkelsen, C. A., Majer, C. R., Sneeringer, C. J., Song, J. J., Johnston, L. D., Scott, M. P., Smith, J. J., Xiao, Y., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.06.009 · Cited by 926 · see citing works
Quivoron, C., Couronné, L., Della Valle, V., Lopez, C. K., Plo, I., Wagner-Ballon, O., Do Cruzeiro, M., Delhommeau, F., Arnulf, B., Stern, M.-H., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.06.003 · Cited by 924 · see citing works
Vermeulen, M., Eberl, H. C., Matarese, F., Marks, H., Denissov, S., Butter, F., Lee, K. K., Olsen, J. V., Hyman, A. A., Stunnenberg, H. G., et al. (2010) · Cell · doi:10.1016/j.cell.2010.08.020 · Cited by 806 · see citing works
Somatic mutations of the histone H3K27 demethylase gene UTX in human cancer
van Haaften, G., Dalgliesh, G. L., Davies, H., Chen, L., Bignell, G., Greenman, C., Edkins, S., Hardy, C., O'Meara, S., Teague, J., et al. (2009) · Nature Genetics · doi:10.1038/ng.349 · Cited by 784 · see citing works
The SET-domain protein superfamily: protein lysine methyltransferases.
Dillon, S. C., Zhang, X. Y., Trievel, R. C., & Cheng, X. (2005) · Genome biology · doi:10.1186/gb-2005-6-8-227 · Cited by 784 · see citing works
Exome sequencing identifies frequent mutation of ARID1A in molecular subtypes of gastric cancer
Wang, K., Kan, J., Yuen, S. T., Shi, S. T., Chu, K., Law, S. Y.-K., Chan, T. L., Kan, Z., Chan, A. S. Y., Tsui, W. Y., et al. (2011) · Nature Genetics · doi:10.1038/ng.982 · Cited by 770 · see citing works
Acquired mutations in TET2 are common in myelodysplastic syndromes
Langemeijer, S. M. C., Kuiper, R. P., Berends, M., Knops, R., Aslanyan, M. G., Massop, M., Stevens-Linders, E., van Hoogen, P., van Kessel, A. G., Raymakers, R. A. P., et al. (2009) · Nature Genetics · doi:10.1038/ng.391 · Cited by 755 · see citing works
Somatic mutations of the histone methyltransferase gene EZH2 in myelodysplastic syndromes
Nikoloski, G., Langemeijer, S. M. C., Kuiper, R. P., Knops, R., Massop, M., Tönnissen, E., van der Heijden, A., Scheele, T. N., Vandenberghe, P., de Witte, T., et al. (2010) · Nature Genetics · doi:10.1038/ng.620 · Cited by 754 · see citing works
Frequent mutations of chromatin remodeling genes in transitional cell carcinoma of the bladder
Gui, Y., Guo, G., Huang, Y., Hu, X., Tang, A., Gao, S., Wu, R., Chen, C., Li, X., Zhou, L., et al. (2011) · Nature Genetics · doi:10.1038/ng.907 · Cited by 748 · see citing works
Piekarz, R., Frye, R., Turner, M. L. C., Wright, J. J., Allen, S. L., Kirschbaum, M. H., Zain, J. M., Prince, H. M., Leonard, J. P., Geskin, L. J., et al. (2009) · Journal of Clinical Oncology · doi:10.1200/jco.2008.21.6150 · Cited by 739 · see citing works
A decade of 3C technologies: insights into nuclear organizationPreprint
de Wit, E., & de Laat, W. L. (2012) · Genes & Development · doi:10.1101/gad.179804.111 · Cited by 701 · see citing works
Huntly, B. J. P., Shigematsu, H., Deguchi, K., Lee, B. H., Mizuno, S., Duclos, N., Rowan, R., Amaral, S., Curley, D., Williams, I. R., et al. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.10.015 · Cited by 697 · see citing works
Sneeringer, C. J., Scott, M. P., Kuntz, K. W., Knutson, S. K., Pollock, R. M., Richon, V. M., & Copeland, R. A. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012525107 · Cited by 691 · see citing works
Schenk, T., Chen, W. C., Göllner, S., Howell, L., Jin, L., Hebestreit, K., Klein, H.-U., Popescu, A. C., Burnett, A., Mills, K., et al. (2012) · Nature Medicine · doi:10.1038/nm.2661 · Cited by 672 · see citing works
Mechanisms and functions of Tet protein-mediated 5-methylcytosine oxidationPreprint
Wu, H., & Zhang, Y. (2011) · Genes & Development · doi:10.17615/800j-yk16 · Cited by 665 · see citing works
Berman, B. P., Weisenberger, D. J., Aman, J. F., Hinoue, T., Ramjan, Z., Liu, Y., Noushmehr, H., Lange, C. P. E., van Dijk, C. M., Tollenaar, R. A. E. M., et al. (2012) · Nature Genetics · doi:10.1038/ng.969 · Cited by 660 · see citing works
Chemoproteomics profiling of HDAC inhibitors reveals selective targeting of HDAC complexes
Bantscheff, M., Hopf, C., Savitski, M. M., Dittmann, A., Grandi, P., Michon, A.-M., Schlegl, J., Abraham, Y., Becher, I., Bergamini, G., et al. (2011) · Nature Biotechnology · doi:10.1038/nbt.1759 · Cited by 659 · see citing works
Tsai, H.-C., Li, H., Neste, L. V., Cai, Y., Robert, C., Rassool, F. V., Shin, J., Harbom, K., Beaty, R. M., Pappou, E. P., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2011.12.029 · Cited by 651 · see citing works
Iyer, N. G., Özdağ, H., & Caldas, C. (2004) · Oncogene · doi:10.1038/sj.onc.1207118 · Cited by 645 · see citing works
JAK2 phosphorylates histone H3Y41 and excludes HP1α from chromatin
Dawson, M. A., Bannister, A. J., Göttgens, B., Foster, S. D., Bartke, T., Green, A. R., & Kouzarides, T. (2009) · Nature · doi:10.1038/nature08448 · Cited by 624 · see citing works
Self-citationThe Eukaryotic Genome as an RNA Machine
Amaral, P., Dinger, M. E., Mercer, T. R., & Mattick, J. S. (2008) · Science · doi:10.1126/science.1155472 · Cited by 621 · see citing works
Encyclopedia of molecular cell biology and molecular medicine
Meyers, R. A. (2004) · Cited by 616 · see citing works
Nucleosome-Interacting Proteins Regulated by DNA and Histone Methylation
Bartke, T., Vermeulen, M., Xhemalce, B., Robson, S. C., Mann, M., & Kouzarides, T. (2010) · Cell · doi:10.1016/j.cell.2010.10.012 · Cited by 611 · see citing works
Self-citationThe Language of Histone Crosstalk
Lee, J., Smith, E. R., & Shilatifard, A. (2010) · Cell · doi:10.1016/j.cell.2010.08.011 · Cited by 598 · see citing works
Reversal of Histone Methylation: Biochemical and Molecular Mechanisms of Histone Demethylases
Mosammaparast, N., & Shi, Y. (2010) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.070907.103946 · Cited by 585 · see citing works
Chesi, M., Nardini, E., Lim, R. S. C., Smith, K. D., Kuehl, W. M., & Bergsagel, P. L. (1998) · Blood · doi:10.1182/blood.v92.9.3025 · Cited by 569 · see citing works
Genetic inactivation of the polycomb repressive complex 2 in T cell acute lymphoblastic leukemia
Ntziachristos, P., Tsirigos, A., Vlierberghe, P. V., Nedjic, J., Trimarchi, T., Flaherty, M. S., Ferrés-Marcó, D., Ros, V. G. D., Tang, Z., Siegle, J. M., et al. (2012) · Nature Medicine · doi:10.1038/nm.2651 · Cited by 525 · see citing works
Insights from genomic profiling of transcription factors
Farnham, P. J. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2636 · Cited by 519 · see citing works
Statistical Issues in cDNA Microarray Data Analysis
Smyth, G. K., Yang, J. Y. H., & Speed, T. P. (2003) · Humana Press eBooks · doi:10.1385/1-59259-364-x:111 · Cited by 463 · see citing works
Spatial Distribution of Di- and Tri-methyl Lysine 36 of Histone H3 at Active Genes
Bannister, A. J., Schneider, R., Myers, F. A., Thorne, A. W., Crane‐Robinson, C., & Kouzarides, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500796200 · Cited by 459 · see citing works
Self-citationHistone deacetylase inhibitors in cancer therapy
Johnstone, R. W., & Licht, J. D. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00165-x · Cited by 450 · see citing works
Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger
Wang, G. G., Song, J., Wang, Z., Dormann, H. L., Casadio, F., Li, H., Luo, J.-L., Patel, D. J., & Allis, C. D. (2009) · Nature · doi:10.1038/nature08036 · Cited by 439 · see citing works
An assessment of histone-modification antibody quality
Egelhofer, T. A., Minoda, A., Klugman, S. A., Lee, K., Kolasinska-Zwierz, P., Alekseyenko, A. A., Cheung, M.-S., Day, D. S., Gadel, S., Gorchakov, A. A., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1972 · Cited by 430 · see citing works
Lorsbach, R. B., Moore, J., Mathew, S., Raimondi, S. C., Mukatira, S. T., & Downing, J. R. (2003) · Leukemia · doi:10.1038/sj.leu.2402834 · Cited by 416 · see citing works
MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites
Pei, H., Zhang, L. M., Luo, K., Qin, Y., Chesi, M., Fei, Y. F., Bergsagel, P. L., Wang, L., You, Z., & Lou, Z. (2011) · Nature · doi:10.1038/nature09658 · Cited by 410 · see citing works
Acetylation inactivates the transcriptional repressor BCL6
Bereshchenko, O., Gu, W. J., & Dalla‐Favera, R. (2002) · Nature Genetics · doi:10.1038/ng1018 · Cited by 394 · see citing works
A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf–Hirschhorn syndrome
Nimura, K., Ura, K., Shiratori, H., Ikawa, M., Okabe, M., Schwartz, R. J., & Kaneda, Y. (2009) · Nature · doi:10.1038/nature08086 · Cited by 376 · see citing works
Signaling Kinase AMPK Activates Stress-Promoted Transcription via Histone H2B Phosphorylation
Bungard, D., Fuerth, B. J., Zeng, P.-Y., Faubert, B., Maas, N. L., Viollet, B., Carling, D., Thompson, C. B., Jones, R. G., & Berger, S. L. (2010) · Science · doi:10.1126/science.1191241 · Cited by 372 · see citing works
Martínez-García, E., Popovic, R., Min, D.-J., Sweet, S. M. M., Thomas, P. M., Zamdborg, L., Heffner, A., Will, C., Lamy, L., Staudt, L. M., et al. (2010) · Blood · doi:10.1182/blood-2010-07-298349 · Cited by 365 · see citing works
The MYST family of histone acetyltransferases and their intimate links to cancer
Avvakumov, N., & Côté, J. (2007) · Oncogene · doi:10.1038/sj.onc.1210608 · Cited by 356 · see citing works
Recognition of a Mononucleosomal Histone Modification Pattern by BPTF via Multivalent Interactions
Ruthenburg, A. J., Li, H., Milne, T. A., Dewell, S. B., McGinty, R. K., Yuen, M. A., Ueberheide, B. M., Dou, Y., Muir, T. W., Patel, D. J., et al. (2011) · Cell · doi:10.1016/j.cell.2011.03.053 · Cited by 353 · see citing works
Genome-Wide Views of Chromatin Structure
Rando, O. J., & Chang, H. Y. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.071107.134639 · Cited by 323 · see citing works
A DNA hypermethylation module for the stem/progenitor cell signature of cancerPreprint
Easwaran, H., Johnstone, S. E., Neste, L. V., Ohm, J. E., Mosbruger, T., Wang, Q., Aryee, M. J., Joyce, P., Ahuja, N., Weisenberger, D., et al. (2012) · Genome Research · doi:10.1101/gr.131169.111 · Cited by 293 · see citing works
Li, Y., Trojer, P., Xu, C., Cheung, P., Kuo, A. J., Drury, W. J., Qiao, Q., Neubert, T. A., Xu, R.-M., Gozani, O., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.034462 · Cited by 292 · see citing works
Cooperative Epigenetic Modulation by Cancer Amplicon Genes
Rui, L., Emre, N. C. T., Kruhlak, M. J., Chung, H., Steidl, C., Slack, G. W., Wright, G. W., Lenz, G., Ngo, V. N., Shaffer, A. L., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.11.013 · Cited by 283 · see citing works
From DNA sequence to transcriptional behaviour: a quantitative approach
Segal, E., & Widom, J. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2591 · Cited by 262 · see citing works
Chromatin remodeling and cancer, part II: ATP-dependent chromatin remodeling
Wang, G. G., Allis, C. D., & Chi, P. (2007) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2007.07.004 · Cited by 254 · see citing works
Chemical probes for histone-modifying enzymes
Cole, P. A. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.111 · Cited by 249 · see citing works
Duns, G., van den Berg, E., van Duivenbode, I., Osinga, J., Hollema, H., Hofstra, R. M. W., & Kok, K. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-0120 · Cited by 236 · see citing works
TET Family Proteins and Their Role in Stem Cell Differentiation and Transformation
Cimmino, L., Abdel-Wahab, O. I., Levine, R. L., & Aifantis, I. (2011) · Cell stem cell · doi:10.1016/j.stem.2011.08.007 · Cited by 229 · see citing works
Deguchi, K., Ayton, P. M., Carapeti, M., Kutok, J. L., Snyder, C. S., Williams, I. R., Cross, N. C. P., Glass, C. K., Cleary, M. L., & Gilliland, D. G. (2003) · Cancer Cell · doi:10.1016/s1535-6108(03)00051-5 · Cited by 224 · see citing works
Marango, J., Shimoyama, M., Nishio, H., Meyer, J. A., Min, D.-J., Sirulnik, A., Martinez-Martinez, Y., Chesi, M., Bergsagel, P. L., Zhou, M., et al. (2007) · Blood · doi:10.1182/blood-2007-06-092122 · Cited by 198 · see citing works
Genetic events in the pathogenesis of multiple myeloma
Chng, W. J., Glebov, O. K., Bergsagel, P. L., & Kuehl, W. M. (2007) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2007.08.004 · Cited by 189 · see citing works
Influence of Combinatorial Histone Modifications on Antibody and Effector Protein Recognition
Fuchs, S. M., Krajewski, K., Baker, R. W., Miller, V. L., & Strahl, B. D. (2010) · Current Biology · doi:10.1016/j.cub.2010.11.058 · Cited by 182 · see citing works
Bell, O., Wirbelauer, C., Hild, M., Scharf, A. N. D., Schwaiger, M., MacAlpine, D. M., Zilbermann, F., van Leeuwen, F., Bell, S. P., Imhof, A., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601926 · Cited by 171 · see citing works
Lauring, J. D., Abukhdeir, A. M., Konishi, H., Garay, J. P., Gustin, J. P., Wang, Q., Arceci, R. J., Matsui, W. H., & Park, B. H. (2007) · Blood · doi:10.1182/blood-2007-05-088674 · Cited by 159 · see citing works
When Signaling Kinases Meet Histones and Histone Modifiers in the Nucleus
Baek, S. H. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.022 · Cited by 149 · see citing works
Linking Heterochromatin Protein 1 (HP1) to cancer progression
Dialynas, G. K., Vitalini, M. W., & Wallrath, L. L. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.09.007 · Cited by 131 · see citing works
Conditional MLL‐CBP targets GMP and models therapy‐related myeloproliferative disease
Wang, J., Iwasaki, H., Krivtsov, A. V., Febbo, P. G., Thorner, A. R., Ernst, P., Anastasiadou, E., Kutok, J. L., Kogan, S. C., Zinkel, S. S., et al. (2005) · The EMBO Journal · doi:10.1038/sj.emboj.7600521 · Cited by 116 · see citing works
Metastasis-Associated Protein 1/Nucleosome Remodeling and Histone Deacetylase Complex in Cancer
Li, D., Pakala, S. B., Nair, S. S., Eswaran, J., & Kumar, R. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-2345 · Cited by 108 · see citing works
The ING gene family in the regulation of cell growth and tumorigenesis
Coles, A. H., & Jones, S. N. (2008) · Journal of Cellular Physiology · doi:10.1002/jcp.21583 · Cited by 102 · see citing works
Epigenome Microarray Platform for Proteome-Wide Dissection of Chromatin-Signaling Networks
Bua, D. J., Kuo, A. J., Cheung, P., Liu, C. L., Migliori, V., Espejo, A. B., Casadio, F., Bassi, C., Amati, B. B., Bedford, M. T., et al. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006789 · Cited by 98 · see citing works
Histone Deacetylase Inhibitors in the Treatment of Hematological Malignancies and Solid Tumors
Federico, M., & Bagella, L. (2010) · BioMed Research International · doi:10.1155/2011/475641 · Cited by 98 · see citing works
Kim, J., Kee, H. J., Choe, N., Kim, S., Eom, G.-H., Baek, H. J., Kook, H., Kook, H., & Seo, S. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02130-07 · Cited by 98 · see citing works
Creusot, R. J., Yaghoubi, S. S., Kodama, K., et al. (2008) · Clinical Immunology · doi:10.1016/j.clim.2007.12.009 · Cited by 69 · see citing works
Targeting 14-3-3zeta in cancer therapy
Yang, X., Cao, W., Zhang, L., Zhang, W., Zhang, X., & Lin, H. (2011) · Cancer Gene Therapy · doi:10.1038/cgt.2011.85 · Cited by 45 · see citing works
Progress in the Discovery of Small-Molecule Inhibitors of Bromodomain–Histone Interactions
Chung, C., & Witherington, J. J. (2011) · SLAS DISCOVERY · doi:10.1177/1087057111421372 · Cited by 44 · see citing works
New Ways to Use DNA Methyltransferase Inhibitors for the Treatment of Myelodysplastic Syndrome
Gore, S. D. (2011) · Hematology · doi:10.1182/asheducation-2011.1.550 · Cited by 28 · see citing works
Stunnenberg, H. G., & Vermeulen, M. (2011) · BioEssays · doi:10.1002/bies.201100044 · Cited by 22 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Selective Inhibition of Tumor Oncogenes by Disruption of Super-Enhancers
Lovén, J., Hoke, H. A., Lin, C. Y., Lau, A., Orlando, D. A., Vakoc, C. R., Bradner, J. E., Lee, T. I., & Young, R. A. (2013) · Cell · doi:10.1016/j.cell.2013.03.036 · Cited by 2,961 · see citing works
The molecular hallmarks of epigenetic control
Allis, C. D., & Jenuwein, T. (2016) · Nature Reviews Genetics · doi:10.1038/nrg.2016.59 · Cited by 2,809 · see citing works
EMT, CSCs, and drug resistance: the mechanistic link and clinical implications
Shibue, T., & Weinberg, R. A. (2017) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2017.44 · Cited by 2,539 · see citing works
Cholangiocarcinoma — evolving concepts and therapeutic strategies
Ilyas, S. I., Khan, S. A., Hallemeier, C. L., Kelley, R. K., & Gores, G. J. (2018) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2017.157 · Cited by 1,626 · see citing works
Histone deacetylases and their inhibitors in cancer, neurological diseases and immune disorders
Falkenberg, K. J., & Johnstone, R. W. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4360 · Cited by 1,564 · see citing works
Transcriptional enhancers: from properties to genome-wide predictions
Shlyueva, D., Stampfel, G., & Stark, A. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3682 · Cited by 1,356 · see citing works
Epigenetic plasticity and the hallmarks of cancer
Flavahan, W. A., Gaskell, E., & Bernstein, B. E. (2017) · Science · doi:10.1126/science.aal2380 · Cited by 1,340 · see citing works
Histone Deacetylase Inhibitors as Anticancer Drugs
Eckschlager, T., Plch, J., Stiborova, M., & Hrabeta, J. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18071414 · Cited by 1,206 · see citing works
Cancer Epigenetics: Tumor Heterogeneity, Plasticity of Stem-like States, and Drug Resistance
Easwaran, H., Tsai, H.-C., & Baylin, S. B. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.05.015 · Cited by 915 · see citing works
Influence of Metabolism on Epigenetics and Disease
Kaelin, W. G., & McKnight, S. L. (2013) · Cell · doi:10.1016/j.cell.2013.03.004 · Cited by 920 · see citing works
Epigenetic reprogramming in cancer
Suvà, M. L., Riggi, N., & Bernstein, B. E. (2013) · Science · doi:10.1126/science.1230184 · Cited by 706 · see citing works
Hou, Y., Guo, H., Cao, C., Li, X., Hu, B., Zhu, P., Wu, X., Wen, L., Tang, F., Huang, Y., et al. (2016) · Cell Research · doi:10.1038/cr.2016.23 · Cited by 647 · see citing works
The roles of DNA, RNA and histone methylation in ageing and cancer
Michalak, E. M., Burr, M. L., Bannister, A. J., & Dawson, M. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0143-1 · Cited by 549 · see citing works
Self-citationQuantitative ChIP-Seq normalization reveals global modulation of the epigenome
Orlando, D. A., Chen, M. W., Brown, V. E., Solanki, S., Choi, Y. J., Olson, E. R., Fritz, C. C., Bradner, J. E., & Guenther, M. G. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.10.018 · Cited by 503 · see citing works
Paediatric and adult glioblastoma: multiform (epi)genomic culprits emerge
Sturm, D., Bender, S., Jones, D. T. W., Lichter, P., Grill, J., Becher, O., Hawkins, C., Majewski, J., Jones, C., Costello, J. F., et al. (2014) · Nature Reviews Cancer · doi:10.1038/nrc3655 · Cited by 555 · see citing works
Akt-dependent metabolic reprogramming regulates tumor cell histone acetylation
Lee, J. V., Carrer, A., Shah, S., Snyder, N. W., Wei, S., Venneti, S., Worth, A. J., Yuan, Z.-F., Lim, H.-W., Liu, S., et al. (2014) · Cell Metabolism · doi:10.1016/j.cmet.2014.06.004 · Cited by 563 · see citing works
BET inhibitor resistance emerges from leukaemia stem cells
Fong, C. Y., Gilan, O., Lam, E. Y. N., Rubin, A. F., Ftouni, S., Tyler, D., Stanley, K., Sinha, D., Yeh, P., Morison, J., et al. (2015) · Nature · doi:10.1038/nature14888 · Cited by 545 · see citing works
Self-citationGain-of-function p53 mutants co-opt chromatin pathways to drive cancer growth
Zhu, J., Sammons, M. A., Donahue, G., Dou, Z., Vedadi, M., Getlik, M., Barsyte-Lovejoy, D., Al-awar, R., Katona, B. W., Shilatifard, A., et al. (2015) · Nature · doi:10.1038/nature15251 · Cited by 493 · see citing works
Differentiation therapy revisited
de Thé, H. (2018) · Nature reviews. Cancer · doi:10.1038/nrc.2017.103 · Cited by 462 · see citing works
Role of SWI/SNF in acute leukemia maintenance and enhancer-mediated <i>Myc</i> regulation
Shi, J., Whyte, W. A., Zepeda-Mendoza, C. J., Milazzo, J. P., Shen, C., Roe, J.-S., Minder, J. L., Mercan, F., Wang, E., Eckersley-Maslin, M. A., et al. (2013) · Genes & Development · doi:10.1101/gad.232710.113 · Cited by 463 · see citing works
The emerging role of epigenetic therapeutics in immuno-oncology
Topper, M. J., Vaz, M., Marrone, K. A., Brahmer, J. R., & Baylin, S. B. (2020) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-019-0266-5 · Cited by 433 · see citing works
Non-viral delivery systems for CRISPR/Cas9-based genome editing: challenges and opportunities
Li, L., Hu, S., & Chen, X. (2018) · Biomaterials · doi:10.1016/j.biomaterials.2018.04.031 · Cited by 415 · see citing works
Absolute quantification of single-base m6A methylation in the mammalian transcriptome using GLORI
Liu, C., Sun, H., Yi, Y., Shen, W., Li, K., Xiao, Y., Li, F., Li, Y., Hou, Y., Lu, B., et al. (2023) · Nature Biotechnology · doi:10.1038/s41587-022-01487-9 · Cited by 386 · see citing works
Gao, Y., Chen, J., Li, K., Wu, T., Huang, B., Liu, W., Kou, X., Zhang, Y., Huang, H., Jiang, Y., et al. (2013) · Cell Stem Cell · doi:10.1016/j.stem.2013.02.005 · Cited by 362 · see citing works
Lin, Y. C., Benner, C., Mansson, R., Heinz, S., Miyazaki, K., Miyazaki, M., Chandra, V., Bossen, C., Glass, C. K., & Murre, C. (2012) · Nature Immunology · doi:10.1038/ni.2432 · Cited by 281 · see citing works
KMT2D Deficiency Impairs Super-Enhancers to Confer a Glycolytic Vulnerability in Lung Cancer
Alam, H., Tang, M., Maitituoheti, M., Dhar, S. S., Kumar, M., Han, C. Y., Ambati, C. R., Amin, S. B., Gu, B., Chen, T.-Y., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.03.005 · Cited by 243 · see citing works
An epigenetic framework for neurodevelopmental disorders: From pathogenesis to potential therapy
Millan, M. J. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2012.11.015 · Cited by 229 · see citing works
Zdzisińska, B., Żurek, A., & Kandefer-Szerszeń, M. (2017) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-016-0406-x · Cited by 221 · see citing works
Stabilization of histone demethylase PHF8 by USP7 promotes breast carcinogenesis.
Wang, Q., Ma, S., Song, N., Li, X., Liu, L., Yang, S., Ding, X., Shan, L., Zhou, X., Su, D., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci85747 · Cited by 206 · see citing works
Marek, M., Kannan, S., Hauser, A.-T., Moraes Mourão, M., Caby, S., Cura, V., Stolfa, D. A., Schmidtkunz, K., Lancelot, J., Andrade, L., et al. (2013) · PLoS Pathogens · doi:10.1371/journal.ppat.1003645 · Cited by 173 · see citing works
The Metabolic Impact on Histone Acetylation and Transcription in Ageing
Peleg, S., Feller, C., Ladurner, A. G., & Imhof, A. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.05.008 · Cited by 178 · see citing works
Unlocking the potential of retinoic acid in anticancer therapy
Schenk, T., Stengel, S., & Zelent, A. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.412 · Cited by 160 · see citing works
Meyer, U. A., Zanger, U. M., & Schwab, M. (2013) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010510-100502 · Cited by 157 · see citing works
Bultman, S. J. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-2483 · Cited by 157 · see citing works
Volinia, S., & Croce, C. M. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1304977110 · Cited by 149 · see citing works
Epigenetic modifications: Key players in cancer heterogeneity and drug resistance
Sadida, H. Q., Abdulla, A., Marzooqi, S. A., Hashem, S., Macha, M. A., Akil, A. S. A.-S., & Bhat, A. A. (2024) · Translational Oncology · doi:10.1016/j.tranon.2023.101821 · Cited by 151 · see citing works
The Multifaceted Role of Heme in Cancer
Fiorito, V., Chiabrando, D., Petrillo, S., Bertino, F., & Tolosano, E. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2019.01540 · Cited by 129 · see citing works
Marek, M., Shaik, T. B., Heimburg, T., Chakrabarti, A., Lancelot, J., Ramos-Morales, E., Da Veiga, C., Kalinin, D., Melesina, J., Robaa, D., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01087 · Cited by 123 · see citing works
Toyokuni, S. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.10.401 · Cited by 102 · see citing works
Drug resistance in colorectal cancer: An epigenetic overview
Luo, M., Yang, X., Chen, H.-N., Nice, E. C., & Huang, C. (2021) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2021.188623 · Cited by 94 · see citing works
HDAC3 regulates DNMT1 expression in multiple myeloma: therapeutic implications
Harada, T., Ohguchi, H., Grondin, Y., Kikuchi, S., Sagawa, M., Tai, Y.-T., Mazitschek, R., Hideshima, T., & Anderson, K. C. (2017) · Leukemia · doi:10.1038/leu.2017.144 · Cited by 89 · see citing works
Han, L., Zi, X., Garmire, L. X., Wu, Y., Weissman, S. M., Pan, X., & Fan, R. (2014) · Scientific Reports · doi:10.1038/srep06485 · Cited by 83 · see citing works
Interactions between epigenetics and metabolism in cancers
Yun, J., Johnson, J. L., Hanigan, C. L., & Locasale, J. W. (2012) · Frontiers in Oncology · doi:10.3389/fonc.2012.00163 · Cited by 82 · see citing works
In vivo reprogramming drives Kras-induced cancer development
Shibata, H., Komura, S., Yamada, Y., Sankoda, N., Tanaka, A., Ukai, T., Kabata, M., Sakurai, S., Kuze, B., Woltjen, K., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04449-5 · Cited by 76 · see citing works
Zhang, Y., Chang, J.-F., Sun, J., Chen, L., Yang, X.-M., Tang, H.-Y., Jing, Y.-Y., Kang, X., He, Z.-M., Wu, J.-Y., et al. (2018) · Journal of Cell Science · doi:10.1242/jcs.215525 · Cited by 45 · see citing works
The role of protein acetylation in carcinogenesis and targeted drug discovery
Yang, J., Song, C., & Zhan, X. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.972312 · Cited by 42 · see citing works
Inhibition of DNA methylation promotes breast tumor sensitivity to netrin‐1 interference
Grandin, M., Mathot, P., Devailly, G., Bidet, Y., Ghantous, A., Favrot, C., Gibert, B., Gadot, N., Puisieux, I., Herceg, Z., et al. (2016) · EMBO Molecular Medicine · doi:10.15252/emmm.201505945 · Cited by 39 · see citing works
Brglez, V., Pucer, A., Pungerčar, J., Lambeau, G., & Petan, T. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.01.182 · Cited by 35 · see citing works
Histone deacetylase 8 is deregulated in urothelial cancer but not a target for efficient treatment
Lehmann, M., Hoffmann, M. J., Koch, A., Ulrich, S. M., Schulz, W. A., & Niegisch, G. (2014) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-014-0059-8 · Cited by 34 · see citing works
Biological Basis for Novel Mesothelioma Therapies
Obacz, J., Yung, H., Shamseddin, M., Linnane, E., Liu, X., Azad, A. A., Rassl, D. M., Fairen-Jimenez, D., Rintoul, R. C., Nikolić, M. Z., et al. (2021) · British Journal of Cancer · doi:10.1038/s41416-021-01462-2 · Cited by 31 · see citing works
Das, A. B., Smith-Díaz, C. C., & Vissers, M. C. M. (2020) · Haematologica · doi:10.3324/haematol.2020.259283 · Cited by 25 · see citing works
Blum, K., Bowirrat, A., Baron, D., Elman, I., Makale, M. T., Cadet, J. L., Thanos, P. K., Hanna, C., Ahmed, R., Gondre-Lewis, M. C., et al. (2024) · Gene & Protein in Disease · doi:10.36922/gpd.1966 · Cited by 14 · see citing works
- Authors
- Dawson, M. A., & Kouzarides, T.
- Affiliations
- University of Cambridge (GB)
- Corresponding author
- Kouzarides, Tony
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2012-07
- Volume
- 150
- Issue
- 1
- Pages
- 12-27
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2117247812
- Cited by
- 3,203
- References
- 135
- Citations by year
- 2026: 150 · 2025: 199 · 2024: 246 · 2023: 258 · 2022: 312 · 2021: 264 · 2020: 204 · 2019: 211 · 2018: 230 · 2017: 239 · 2016: 239 · 2015: 229 · 2014: 213 · 2013: 174 · 2012: 33
- FWCI
- 18.96
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust (092096)
- Cancer Research UK
- Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- cancer epigenetics, DNA methylation, histone modifications, nucleosome remodeling, chromatin regulation, epigenetic drugs, chromatin regulators, epigenetic therapy
- MeSH terms
- Humans, Neoplasms, Gene Expression Regulation, Neoplastic, DNA Methylation, Chromatin Assembly and Disassembly, Histone Code, Epigenesis, Genetic, Epigenomics
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
