The DOI matches its Crossref record; 64 of the 68 references it cites were found in a registry or an index.
Pharmacologic disruption of Polycomb-repressive complex 2-mediated gene repression selectively induces apoptosis in cancer cells
Open accessAbstract
Polycomb-repressive complex 2 (PRC2)-mediated histone methylation plays an important role in aberrant cancer gene silencing and is a potential target for cancer therapy. Here we show that S-adenosylhomocysteine hydrolase inhibitor 3-Deazaneplanocin A (DZNep) induces efficient apoptotic cell death in cancer cells but not in normal cells. We found that DZNep effectively depleted cellular levels of PRC2 components EZH2, SUZ12, and EED and inhibited associated histone H3 Lys 27 methylation (but not H3 Lys 9 methylation). By integrating RNA interference (RNAi), genome-wide expression analysis, and chromatin immunoprecipitation (ChIP) studies, we have identified a prominent set of genes selectively repressed by PRC2 in breast cancer that can be reactivated by DZNep. We further demonstrate that the preferential reactivation of a set of these genes by DZNep, including a novel apoptosis affector, FBXO32 , contributes to DZNep-induced apoptosis in breast cancer cells. Our results demonstrate the unique feature of DZNep as a novel chromatin remodeling compound and suggest that pharmacologic reversal of PRC2-mediated gene repression by DZNep may constitute a novel approach for cancer therapy.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“The discovery of deazaneplanocin A (DZNep) is the first attempt to inhibit EZH2 function, which could effectively deplete EZH2, SUZ12, and EED at cellular levels [156].”
From Proteolysis targeting chimeras (PROTACs) are emerging therapeutics for hematologic malignancies (2020) · cites this paper as [156]
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
1 retracted
Histone methylation by the Drosophila epigenetic transcriptional regulator Ash1
Beisel, C., Imhof, A., Greene, J., Kremmer, E., & Sauer, F. (2002) · Nature · doi:10.1038/nature01126 · Cited by 310
RetractedThe fundamental role of epigenetic events in cancer
Jones, P. A., & Baylin, S. B. (2002) · Nature Reviews Genetics · doi:10.1038/nrg816 · Cited by 5,648
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
Role of Histone H3 Lysine 27 Methylation in Polycomb-Group Silencing
Cao, R., Wang, L., Wang, H., Xia, L., Erdjument-Bromage, H., Tempst, P., Jones, R. S., & Zhang, Y. (2002) · Science · doi:10.1126/science.1076997 · Cited by 3,775
Regulation of chromatin structure by site-specific histone H3 methyltransferases
Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845 · cited 1×
“In contrast, histone H3 trimethylation at Lys 9 (H3-K9me3)—which is mediated by another histone MTase, Suv39h1 (Rea et al. 2000; Peters et al. 2001; Lehnertz et al. 2003)—was not affected by DZNep treatment.”
BackgroundThe polycomb group protein EZH2 is involved in progression of prostate cancer
Varambally, S., Dhanasekaran, S. M., Zhou, M., Barrette, T. R., Kumar-Sinha, C., Sanda, M. G., Ghosh, D., Pienta, K. J., Sewalt, R. G. A. B., Otte, A. P., et al. (2002) · Nature · doi:10.1038/nature01075 · Cited by 2,717
Polycomb complexes repress developmental regulators in murine embryonic stem cells
Boyer, L. A., Plath, K., Zeitlinger, J., Brambrink, T., Medeiros, L. A., Lee, T. I., Levine, S. S., Wernig, M., Tajonar, A., Ray, M. K., et al. (2006) · Nature · doi:10.1038/nature04733 · Cited by 2,568
The history of cancer epigenetics
Feinberg, A. P., & Tycko, B. (2004) · Nature reviews. Cancer · doi:10.1038/nrc1279 · Cited by 2,404
Control of Developmental Regulators by Polycomb in Human Embryonic Stem Cells
Lee, T. I., Jenner, R. G., Boyer, L. A., Guenther, M. G., Levine, S. S., Kumar, R., Chevalier, B. S., Johnstone, S. E., Cole, M. F., Isono, K., et al. (2006) · Cell · doi:10.1016/j.cell.2006.02.043 · Cited by 2,296
The Polycomb group protein EZH2 directly controls DNA methylation
Viré, E., Brenner, C., Deplus, R., Blanchon, L., Fraga, M., Didelot, C., Morey, L., Van Eynde, A., Bernard, D., Vanderwinden, J.-M., et al. (2006) · Nature · doi:10.1038/nature04431 · Cited by 2,204
Cited by
Sorted by citations
Long non-coding RNA HOTAIR reprograms chromatin state to promote cancer metastasis
Gupta, R. A., Shah, N., Wang, K., Kim, J., Horlings, H. M., Wong, D. J., Tsai, M.-C., Hung, T., Argani, P., Rinn, J. L., et al. (2010) · Nature · doi:10.1038/nature08975 · Cited by 5,205
Sharma, S., Kelly, T. K., & Jones, P. A. (2010) · Carcinogenesis · doi:10.1093/carcin/bgp220 · Cited by 2,637
Zou, W., Wolchok, J. D., & Chen, L. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aad7118 · Cited by 2,400
Chemokines in the cancer microenvironment and their relevance in cancer immunotherapy
Nagarsheth, N., Wicha, M. S., & Zou, W. (2017) · Nature reviews. Immunology · doi:10.1038/nri.2017.49 · Cited by 2,251
Kim, K. H., & Roberts, C. W. M. (2016) · Nature Medicine · doi:10.1038/nm.4036 · Cited by 1,471
Pluripotent stem cells induced from mouse somatic cells by small-molecule compounds.
Hou, P., Li, Y., Zhang, X., Liu, C., Guan, J., Li, H., Zhao, T., Ye, J., Yang, W., Liu, K., et al. (2013) · Science · doi:10.1126/science.1239278 · Cited by 1,402
Cancer epigenetics reaches mainstream oncology
Rodríguez‐Paredes, M., & Esteller, M. (2011) · Nature Medicine · doi:10.1038/nm.2305 · Cited by 1,252
Epigenetic silencing of TH1-type chemokines shapes tumour immunity and immunotherapy
Peng, D., Kryczek, I., Nagarsheth, N., Zhao, L., Wei, S., Wang, W., Sun, Y., Zhao, E., Vatan, L., Szeliga, W., et al. (2015) · Nature · doi:10.1038/nature15520 · Cited by 1,201
Roles of the EZH2 histone methyltransferase in cancer epigenetics
Simon, J. A., & Lange, C. A. (2008) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2008.07.010 · Cited by 880
The promise and peril of chemical probes
Arrowsmith, C. H., Audia, J. E., Austin, C., Baell, J., Bennett, J., Blagg, J., Bountra, C., Brennan, P. E., Brown, P. J., Bunnage, M. E., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1867 · Cited by 839
Kim, E. H., Kim, M., Woo, D., Shin, Y., Shin, J., Chang, N., Oh, Y. T., Kim, H., Rheey, J., Nakano, I., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.04.008 · Cited by 846
Epigenetic modifications as therapeutic targets
Kelly, T. K., Carvalho, D. D. D., & Jones, P. A. (2010) · Nature Biotechnology · doi:10.1038/nbt.1678 · Cited by 822
A selective inhibitor of EZH2 blocks H3K27 methylation and kills mutant lymphoma cells
Knutson, S. K., Wigle, T. J., Warholic, N. M., Sneeringer, C. J., Allain, C. J., Klaus, C. R., Sacks, J. D., Raimondi, A., Majer, C. R., Song, J., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1084 · Cited by 776
Yap, D., Chu, J., Berg, T., Schapira, M., Cheng, S., Moradian, A., Morin, R. D., Mungall, A. J. J., Meissner, B., Boyle, M., et al. (2010) · Blood · doi:10.1182/blood-2010-11-321208 · Cited by 633
Epigenomic alterations define lethal CIMP-positive ependymomas of infancy
Mack, S. C., Witt, H., Piro, R. M., Gu, L., Zuyderduyn, S., Stütz, A. M., Wang, X., Gallo, M., Garzia, L., Zayne, K., et al. (2014) · Nature · doi:10.1038/nature13108 · Cited by 607
Miranda, T. B., Cortez, C. C., Yoo, C. B., Liang, G., Abe, M., Kelly, T. K., Márquez, V. E., & Jones, P. A. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0013 · Cited by 609
Repression of E-cadherin by the polycomb group protein EZH2 in cancer
Cao, Q., Yu, J., Dhanasekaran, S. M., Kim, J. H., Mani, R. S., Tomlins, S. A., Mehra, R., Laxman, B., Cao, X., Yu, J., et al. (2008) · Oncogene · doi:10.1038/onc.2008.333 · Cited by 592
Ong, L.-T., Lee, W. C., Ma, S., Oguz, G., Niu, Z., Bao, Y., Yusuf, M., Lee, P. L., Goh, J. Y., Wang, P., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2201376119 · Cited by 572
Self-citationChase, A., & Cross, N. C. P. (2011) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-10-2156 · Cited by 563
Roles of F-box proteins in cancer
Wang, Z. P., Liu, P., Inuzuka, H., & Wei, W. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3700 · Cited by 522
EMT as the ultimate survival mechanism of cancer cells
Tiwari, N., Gheldof, A., Tatari, M. N., & Christofori, G. (2012) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2012.02.013 · Cited by 526
Epigenetics in cancer: Targeting chromatin modifications
Ellis, L., Atadja, P. W., & Johnstone, R. W. (2009) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-08-0860 · Cited by 488
EZH2 Is Essential for Glioblastoma Cancer Stem Cell Maintenance
Suvà, M.-L., Riggi, N., Janiszewska, M., Radovanovic, I., Provero, P., Stehle, J., Baumer, K., Bitoux, M. L., Marino, D., Cironi, L., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-1622 · Cited by 466
NNMT promotes epigenetic remodeling in cancer by creating a metabolic methylation sink
Ulanovskaya, O. A., Zuhl, A. M., & Cravatt, B. F. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1204 · Cited by 454
Chromatin proteins and modifications as drug targets
Helin, K., & Dhanak, D. (2013) · Nature · doi:10.1038/nature12751 · Cited by 448
Epigenetics in cancer stem cells
Toh, T. B., Lim, J. J., & Chow, E. K. (2017) · Molecular Cancer · doi:10.1186/s12943-017-0596-9 · Cited by 439
Methionine is a metabolic dependency of tumor-initiating cells
Wang, Z., Yip, L. Y., Lee, J. H. J., Wu, Z., Chew, H. Y., Chong, P. K. W., Teo, C. C., Ang, H. Y.-K., Peh, K. L. E., Yuan, J. X., et al. (2019) · Nature Medicine · doi:10.1038/s41591-019-0423-5 · Cited by 431
Self-citationZhao, E., Maj, T., Kryczek, I., Li, W., Wu, K., Zhao, L., Wei, S., Crespo, J., Wan, S., Vatan, L., et al. (2016) · Nature Immunology · doi:10.1038/ni.3313 · Cited by 405
MeCP2 Controls an Epigenetic Pathway That Promotes Myofibroblast Transdifferentiation and Fibrosis
Mann, J., Chu, D. C. K., Maxwell, A., Oakley, F., Zhu, N., Tsukamoto, H., & Mann, D. A. (2010) · Gastroenterology · doi:10.1053/j.gastro.2009.10.002 · Cited by 397
Context-Specific Regulation of NF-κB Target Gene Expression by EZH2 in Breast Cancers
Lee, S. T., Li, Z., Wu, Z., Aau, M., Guan, P., Karuturi, R. K. M., Liou, Y. C., & Yu, Q. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.011 · Cited by 412
Self-citationTargeting histone methyltransferases and demethylases in clinical trials for cancer therapy
Morera, L., Lübbert, M., & Jung, M. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0223-4 · Cited by 412
Palacios, D., Mozzetta, C., Consalvi, S., Caretti, G., Saccone, V., Proserpio, V., Marquez, V. E., Valente, S., Mai, A., Forcales, S. V., et al. (2010) · Cell Stem Cell · doi:10.1016/j.stem.2010.08.013 · Cited by 392
Cancer Development, Progression, and Therapy: An Epigenetic Overview
Sarkar, S., Horn, G., Moulton, K. L., Oza, A. U., Byler, S., Kokolus, S., & Longacre, M. M. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms141021087 · Cited by 425
The roles of Polycomb repressive complexes in mammalian development and cancer
Piunti, A., & Shilatifard, A. (2021) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00341-1 · Cited by 420
Histone demethylase JMJD3 contributes to epigenetic control of INK4a/ARF by oncogenic RAS
Barradas, M., Anderton, E., Acosta, J. C., Li, S., Banito, A., Rodriguez-Niedenführ, M., Maertens, G., Banck, M., Zhou, M.-M., Walsh, M. J., et al. (2009) · Genes & Development · doi:10.1101/gad.511109 · Cited by 352
Fiskus, W. C., Wang, Y., Sreekumar, A., Buckley, K. M., Shi, H., Jillella, A., Üstün, C., Rao, R., Fernandez, P., Chen, J., et al. (2009) · Blood · doi:10.1182/blood-2009-03-213496 · Cited by 372
Targeted disruption of the EZH2–EED complex inhibits EZH2-dependent cancer
Kim, W., Bird, G. H., Neff, T., Guo, G., Kerenyi, M. A., Walensky, L. D., & Orkin, S. H. (2013) · Nature Chemical Biology · doi:10.1038/nchembio.1331 · Cited by 351
Histone lysine methylation and demethylation pathways in cancer
Varier, R. A., & Timmers, H. T. M. (2010) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2010.10.002 · Cited by 351
Sandovici, I., Smith, N. H., Nitert, M. D., Ackers-Johnson, M., Uribe-Lewis, S., Ito, Y., Jones, R. H., Marquez, V. E., Cairns, W., Tadayyon, M., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019007108 · Cited by 326
Targeting DNA methylation for epigenetic therapy
Yang, X., Lay, F. D., Han, H., & Jones, P. A. (2010) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2010.08.001 · Cited by 333
Self-citationLeukaemogenesis: more than mutant genes
Chen, J., Odenike, O. M., & Rowley, J. D. (2009) · Nature reviews. Cancer · doi:10.1038/nrc2765 · Cited by 314
Molecular subtypes of breast cancer are associated with characteristic DNA methylation patterns
Holm, K., Hegardt, C., Staaf, J., Vallon‐Christersson, J., Jonsson, G. G., Olsson, H. L., Borg, Å., & Ringnér, M. (2010) · Breast Cancer Research · doi:10.1186/bcr2590 · Cited by 312
Histone methyltransferases in cancer
Albert, M., & Helin, K. (2009) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2009.10.007 · Cited by 320
PRC2 directly methylates GATA4 and represses its transcriptional activityPreprint
He, A., Shen, X., Ma, Q., Cao, J., von Gise, A., Zhou, P., Wang, G., Márquez, V. E., Orkin, S. H., & Pu, W. T. (2012) · Genes & Development · doi:10.1101/gad.173930.111 · Cited by 304
PML-RARα/RXR Alters the Epigenetic Landscape in Acute Promyelocytic Leukemia
Martens, J. H. A., Brinkman, A. B., Simmer, F., Françoijs, K., Nebbioso, A., Ferrara, F., Altucci, L., & Stunnenberg, H. G. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.12.042 · Cited by 293
Tumes, D. J., Onodera, A., Suzuki, A., Shinoda, K., Endo, Y., Iwamura, C., Hosokawa, H., Koseki, H., Tokoyoda, K., Suzuki, Y., et al. (2013) · Immunity · doi:10.1016/j.immuni.2013.09.012 · Cited by 291
Regulation and Role of EZH2 in Cancer
Yamaguchi, H., & Hung, M. (2014) · Cancer Research and Treatment · doi:10.4143/crt.2014.46.3.209 · Cited by 291
Au, S. L., Wong, C. C., Lee, J. M., Fan, D. N.-Y., Tsang, F. H., Ng, I. O., & Wong, C. (2012) · Hepatology · doi:10.1002/hep.25679 · Cited by 287
Ito, T., Teo, Y. V., Evans, S. A., Neretti, N., & Sedivy, J. M. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.03.002 · Cited by 265
Nagarsheth, N., Peng, D., Kryczek, I., Wu, K., Li, W., Zhao, E., Zhao, L., Wei, S., Frankel, T. L., Vatan, L., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-1938 · Cited by 277
Cancer Epigenetics: Modifications, Screening, and Therapy
Gal‐Yam, E. N., Saito, Y., Egger, G., & Jones, P. A. (2007) · Annual Review of Medicine · doi:10.1146/annurev.med.59.061606.095816 · Cited by 270
Cancer DNA Methylation: Molecular Mechanisms and Clinical Implications
McCabe, M. T., Brandes, J. C., & Vertino, P. M. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-2784 · Cited by 273
EZH2 inhibition sensitizes BRG1 and EGFR mutant lung tumours to TopoII inhibitors
Brainson, C. F., Xu, C., Desai, P. T., Berry, J. M., Rowbotham, S. P., Lin, Y.-J., Zhang, H., Márquez, V. E., Hammerman, P. S., Wong, K., et al. (2015) · Nature · doi:10.1038/nature14122 · Cited by 254
Cao, P. D., Deng, Z., Wan, M., Huang, W., Cramer, S. D., Xu, J., Lei, M., & Sui, G. (2010) · Molecular Cancer · doi:10.1186/1476-4598-9-108 · Cited by 253
EZH2 Generates a Methyl Degron that Is Recognized by the DCAF1/DDB1/CUL4 E3 Ubiquitin Ligase Complex
Lee, J. M., Lee, J. S., Kim, H.-K., Kim, K., Park, H., Kim, J.-Y., Lee, S. H., Kim, I. S., Kim, J., Lee, M., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.09.004 · Cited by 268
Targeting Epigenetics in Cancer
Bennett, R. L., & Licht, J. D. (2017) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010716-105106 · Cited by 254
Yang, X., Feng, M., Jiang, X., Wu, Z., Li, Z., Aau, M., & Yu, Q. (2009) · Genes & Development · doi:10.1101/gad.1819009 · Cited by 256
Self-citationThrowing the cancer switch: reciprocal roles of polycomb and trithorax proteins
Mills, A. A. (2010) · Nature reviews. Cancer · doi:10.1038/nrc2931 · Cited by 256
Epigenetic Analysis of KSHV Latent and Lytic Genomes
Tóth, Z., Maglinte, D. T., Lee, S. H., Lee, H.-R., Wong, L.-Y., Brulois, K., Lee, S., Buckley, J. D., Laird, P. W., Márquez, V. E., et al. (2010) · PLoS Pathogens · doi:10.1371/journal.ppat.1001013 · Cited by 235
Discovery of a first-in-class EZH2 selective degrader
Ma, A., Στρατικόπουλος, Η., Park, K., Wei, J., Martin, T. C., Yang, X., Schwarz, M. C., Leshchenko, V. V., Rialdi, A., Dale, B., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0421-4 · Cited by 245
Self-citationSmits, M., Nilsson, J. A., Mir, S. E., van der Stoop, P. M., Hulleman, E., Niers, J. M., Hamer, P. C. D. W., Márquez, V. E., Cloos, J. J., Krichevsky, A. M., et al. (2010) · Oncotarget · doi:10.18632/oncotarget.205 · Cited by 242
EZH2: biology, disease, and structure-based drug discovery
Tan, J., Yan, Y., Wang, X., Jiang, Y., & Xu, H. E. (2013) · Acta Pharmacologica Sinica · doi:10.1038/aps.2013.161 · Cited by 248
Self-citationJiang, X., Tan, J. Y., Li, J., Kivimäe, S., Yang, X., Zhuang, L., Lee, P. L., Chan, M. T. W., Stanton, L. W., Liu, E. T., et al. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.04.019 · Cited by 241
Self-citationXu, B., On, D. M., Ma, A., Parton, T., Konze, K. D., Pattenden, S. G., Allison, D. F., Cai, L., Rockowitz, S., Liu, S., et al. (2014) · Blood · doi:10.1182/blood-2014-06-581082 · Cited by 231
Epigenetics in Prostate Cancer: Biologic and Clinical Relevance
Jerónimo, C., Bastian, P. J., Bjartell, A. S., Carbone, G. M., Catto, J. W. F., Clark, S. J., Henrique, R., Nelson, W. G., & Shariat, S. F. (2011) · European Urology · doi:10.1016/j.eururo.2011.06.035 · Cited by 231
Kottakis, F., Polytarchou, C., Foltopoulou, P. F., Sanidas, I., Kampranis, S. C., & Tsichlis, P. N. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.020 · Cited by 226
Yu, J., Cao, Q., Mehra, R., Laxman, B., Yu, J., Tomlins, S. A., Creighton, C. J., Dhanasekaran, S. M., Shen, R., Chen, G., et al. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.10.016 · Cited by 227
Zhou, J., Bi, C., Cheong, L.-L., Mahara, S., Liu, S.-C., Tay, K.-G., Koh, T.-L., Yu, Q., & Chng, W. J. (2011) · Blood · doi:10.1182/blood-2010-07-294827 · Cited by 216
Self-citationDelivery of CRISPR/Cas systems for cancer gene therapy and immunotherapy
Song, X., Liu, C., Wang, N., Huang, H., He, S., Gong, C., & Wei, Y. (2020) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2020.04.010 · Cited by 217
Epigenetic regulation of heterochromatic DNA stability
Peng, J. C., & Karpen, G. H. (2008) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2008.01.021 · Cited by 214
Cheng, A. S. L., Lau, S. S., Chen, Y., Kondo, Y., Li, M. S. M., Feng, H., Ching, A. K.-K., Cheung, K. F., Wong, H. K., TONG, J. H. M., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-3342 · Cited by 212
Concise Review: Roles of Polycomb Group Proteins in Development and Disease: A Stem Cell Perspective
Rajasekhar, V. K., & Begemann, M. (2007) · Stem Cells · doi:10.1634/stemcells.2006-0608 · Cited by 210
Rizzo, S., Hersey, J. M., Mellor, P., Dai, W., Santos‐Silva, A., Liber, D., Luk, L., Titley, I., Carden, C. P., Box, G., et al. (2011) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-10-0788 · Cited by 203
Coordinated Regulation of Polycomb Group Complexes through microRNAs in Cancer
Cao, Q., Mani, R. S., Ateeq, B., Dhanasekaran, S. M., Asangani, I. A., Prensner, J. R., Kim, J. H., Brenner, J. C., Jing, X., Cao, X., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.06.016 · Cited by 208
Therapeutic targeting of tumor suppressor genes
Morris, L. G. T., & Chan, T. A.-T. (2014) · Cancer · doi:10.1002/cncr.29140 · Cited by 209
Enhancer of zeste homolog 2 (EZH2) inhibitors
Gulati, N., Béguelin, W., & Giulino-Roth, L. G. (2018) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2018.1430795 · Cited by 205
der Meulen, J. V., Sanghvi, V. R., Mavrakis, K. J., Durinck, K., Fang, F., Matthijssens, F., Rondou, P., Rosen, M., Pieters, T., Vandenberghe, P., et al. (2014) · Blood · doi:10.1182/blood-2014-05-577270 · Cited by 203
Epi-drugs to fight cancer: From chemistry to cancer treatment, the road ahead
Mai, A., & Altucci, L. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.08.020 · Cited by 192
Targeting histone lysine methylation in cancer
McGrath, J. P., & Trojer, P. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.01.002 · Cited by 190
Zhou, X., Zang, X., Ponnusamy, M., Masucci, M. V., Tolbert, E. M., Gong, R., Zhao, T. C., Liu, N., Bayliss, G. P., Dworkin, L. D., et al. (2015) · Journal of the American Society of Nephrology · doi:10.1681/asn.2015040457 · Cited by 191
CRL4B Catalyzes H2AK119 Monoubiquitination and Coordinates with PRC2 to Promote Tumorigenesis
Hu, H., Yang, Y., Ji, Q., Zhao, W., Jiang, B., Liu, R., Yuan, J., Liu, Q., Li, X., Zou, Y., et al. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.10.024 · Cited by 185
Ning, X., Shi, Z., Liu, X., Zhang, A., Han, L., Jiang, K., Kang, C., & Zhang, Q. (2015) · Cancer Letters · doi:10.1016/j.canlet.2015.01.005 · Cited by 189
STAT3 signaling drives EZH2 transcriptional activation and mediates poor prognosis in gastric cancer
Pan, Y., Wang, C., Zhu, M., Xing, R., Cui, J., Li, W.-M., Yu, D.-D., Wang, S., Zhu, W., Wu, Y., et al. (2016) · Molecular Cancer · doi:10.1186/s12943-016-0561-z · Cited by 188
MYC—Master Regulator of the Cancer Epigenome and Transcriptome
Poole, C. J., & van Riggelen, J. (2017) · Genes · doi:10.3390/genes8050142 · Cited by 180
ANRIL: A Regulator of VEGF in Diabetic Retinopathy
Thomas, A. A., Feng, B., & Chakrabarti, S. (2017) · Investigative Ophthalmology & Visual Science · doi:10.1167/iovs.16-20569 · Cited by 182
EZH2 negatively regulates PD-L1 expression in hepatocellular carcinoma
Xiao, G., Jin, L.-L., Liu, C., Wang, Y., Meng, Y.-M., Zhou, Z., Chen, J., Yu, X.-J., Zhang, Y., Xu, J., et al. (2019) · Journal for ImmunoTherapy of Cancer · doi:10.1186/s40425-019-0784-9 · Cited by 186
Sato, T., Kaneda, A., Tsuji, S., Isagawa, T., Yamamoto, S., Fujita, T., Yamanaka, R., Tanaka, Y., Nukiwa, T., Márquez, V. E., et al. (2013) · Scientific Reports · doi:10.1038/srep01911 · Cited by 181
EZH2 in normal and malignant hematopoiesis
Lund, K., Adams, P. D., & Copland, M. (2013) · Leukemia · doi:10.1038/leu.2013.288 · Cited by 181
Epigenetic mechanisms in glioblastoma multiforme
Nagarajan, R. P., & Costello, J. F. (2009) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2009.02.005 · Cited by 176
The Impact of Chromatin Dynamics on Cas9-Mediated Genome Editing in Human Cells
Daer, R., Cutts, J., Brafman, D. A., & Haynes, K. A. (2016) · ACS Synthetic Biology · doi:10.1021/acssynbio.5b00299 · Cited by 184
Modeling medulloblastoma in vivo and with human cerebellar organoids
Ballabio, C., Anderle, M., Gianesello, M., Lago, C., Miele, E., Cardano, M., Aiello, G., Piazza, S., Caron, D., Gianno, F., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13989-3 · Cited by 181
Early life stress in fathers improves behavioural flexibility in their offspring
Gapp, K., Soldado-Magraner, S., Álvarez-Sánchez, M., Bohacek, J., Vernaz, G., Shu, H., Franklin, T. B., Wolfer, D. P., & Mansuy, I. M. (2014) · Nature Communications · doi:10.1038/ncomms6466 · Cited by 170
EZH2 Mediates Epigenetic Silencing of Neuroblastoma Suppressor Genes CASZ1 , CLU , RUNX3 , and NGFR
Wang, C., Liu, Z., Woo, C., Li, Z., Wang, L., Wei, J. S., Márquez, V. E., Bates, S. E., Jin, Q., Khan, J. I., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-0961 · Cited by 178
Crea, F., Hurt, E. M., Mathews, L., Cabarcas‐Petroski, S., Sun, L., Márquez, V. E., Danesi, R., & Farrar, W. L. (2011) · Molecular Cancer · doi:10.1186/1476-4598-10-40 · Cited by 178
The emerging role of PI3K/AKT-mediated epigenetic regulation in cancer
Spangle, J. M., Roberts, T. M., & Zhao, J. J. (2017) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2017.03.002 · Cited by 170
Polycomb-dependent epigenetic landscape in adult T-cell leukemia
Fujikawa, D., Nakagawa, S., Hori, M., Kurokawa, N., Soejima, A., Nakano, K., Yamochi, T., Nakashima, M., Kobayashi, S., Tanaka, Y., et al. (2016) · Blood · doi:10.1182/blood-2015-08-662593 · Cited by 176
Oxidative Stress and DNA Methylation in Prostate Cancer
Donkena, K. V., Young, C. Y. F., & Tindall, D. J. (2010) · Obstetrics and Gynecology International · doi:10.1155/2010/302051 · Cited by 172
Epigenetic aberrations during oncogenesis
Hatziapostolou, M., & Iliopoulos, D. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0624-z · Cited by 173
Roles of thioredoxin binding protein (TXNIP) in oxidative stress, apoptosis and cancer
Zhou, J., & Chng, W. J. (2012) · Mitochondrion · doi:10.1016/j.mito.2012.06.004 · Cited by 172
FOXQ1 Regulates Epithelial-Mesenchymal Transition in Human Cancers
Qiao, Y., Jiang, X., Lee, S. T., Karuturi, R. K. M., Hooi, S. C., & Yu, Q. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-2787 · Cited by 169
Self-citation
Metadata
- Authors
- Tan, J., Yang, X., Zhuang, L., Jiang, X., Chen, W., Lee, P. L., Karuturi, R. K. M., Tan, P. B. O., Liu, E. T., & Yu, Q.
- Affiliations
- Genome Institute of Singapore (SG)
- Chinese Academy of Medical Sciences & Peking Union Medical College (CN)
- Duke-NUS Medical School (SG)
- ORCID
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2007-04-16
- Volume
- 21
- Issue
- 9
- Pages
- 1050-1063
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC1855231
- OpenAlex
- W2113634596
- Cited by
- 895
- References
- 68
- Citations by year
- 2026: 12 · 2025: 16 · 2024: 18 · 2023: 35 · 2022: 21 · 2021: 35 · 2020: 39 · 2019: 37 · 2018: 44 · 2017: 65 · 2016: 55 · 2015: 65 · 2014: 98 · 2013: 77 · 2012: 70
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- National University of Singapore (submittedVersion)
- Funders
- Agency for Science, Technology and Research
- National Cancer Institute
- 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
- polycomb repressive complex 2, DZNep, EZH2, SUZ12, EED, histone H3 lysine 27 methylation, gene silencing, apoptosis, breast cancer, atrogin-1, chromatin remodeling, cancer therapy
- MeSH terms
- Adenosine, Base Sequence, Breast Neoplasms, Enzyme Inhibitors, Female, Histones, Humans, Methylation, Promoter Regions, Genetic, Repressor Proteins, RNA Polymerase II, Apoptosis, RNA Interference, RNA, Small Interfering, Chromatin Assembly and Disassembly, Adenosylhomocysteinase, Epigenesis, Genetic, Cell Line, Tumor, Chromatin Immunoprecipitation, Polycomb-Group 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