The Polycomb complex PRC2 and its mark in life

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

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

Functional Demarcation of Active and Silent Chromatin Domains in Human HOX Loci by Noncoding RNAs

Rinn, J. L., Kertesz, M., Wang, J. K., Squazzo, S. L., Xu, X. H., Brugmann, S. A., Goodnough, L. H., Helms, J. A., Farnham, P., Segal, E., et al. (2007) · Cell · doi:10.1016/j.cell.2007.05.022 · Cited by 4,246

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

A gene complex controlling segmentation in Drosophila

Lewis, E. B. (1978) · Nature · doi:10.1038/276565a0 · Cited by 3,813

Long Noncoding RNA as Modular Scaffold of Histone Modification Complexes

Tsai, M.-C., Manor, O., Wan, Y., Mosammaparast, N., Wang, J. K., Lan, F., Shi, Y., Segal, E., & Chang, H. Y. (2010) · Science · doi:10.1126/science.1192002 · Cited by 3,290 · cited 1×

Many human large intergenic noncoding RNAs associate with chromatin-modifying complexes and affect gene expression

Khalil, A. M., Guttman, M., Huarte, M., Garber, M., Raj, A., Rivea Morales, D., Thomas, K., Presser, A., Bernstein, B. E., van Oudenaarden, A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0904715106 · Cited by 2,872

The 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

Genome-scale DNA methylation maps of pluripotent and differentiated cells

Meissner, A., Mikkelsen, T. S., Gu, H., Wernig, M., Hanna, J., Sivachenko, A., Zhang, X., Bernstein, B. E., Nusbaum, C., Jaffe, D. B., et al. (2008) · Nature · doi:10.1038/nature07107 · Cited by 2,536

Enhancer of zeste homolog 2 (Ezh2) controls bone formation and cell cycle progression during osteogenesis in mice

Dudakovic, A., Camilleri, E. T., Paradise, C. R., Samsonraj, R. M., Gluscevic, M., Paggi, C. A., Begun, D. L., Khani, F., Pichurin, O., Ahmed, F. S., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.002983 · Cited by 88

EZH2 regulates PD-L1 expression via HIF-1α in non-small cell lung cancer cells

Zhao, Y., Wang, X., Wu, W., Long, H., Huang, J., Wang, Z., Li, T., Tang, S., Zhu, B., & Chen, D. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.07.039 · Cited by 91

Middle‐down hybrid chromatography/tandem mass spectrometry workflow for characterization of combinatorial post‐translational modifications in histones

Sidoli, S., Schwämmle, V., Ruminowicz, C., Hansen, T. A., Wu, X., Helin, K., & Jensen, O. N. (2014) · PROTEOMICS · doi:10.1002/pmic.201400084 · Cited by 87

Age-Related Dopaminergic Innervation Augments T Helper 2-Type Allergic Inflammation in the Postnatal Lung

Wang, W., Cohen, J. A., Wallrapp, A., Trieu, K. G., Barrios, J., Shao, F., Krishnamoorthy, N., Kuchroo, V. K., Jones, M. R., Fine, A., et al. (2019) · Immunity · doi:10.1016/j.immuni.2019.10.002 · Cited by 86

Overcoming Immune Checkpoint Blockade Resistance via EZH2 Inhibition

Kim, H. J., Cantor, H., & Cosmopoulos, K. (2020) · Trends in Immunology · doi:10.1016/j.it.2020.08.010 · Cited by 88

Epigenetic alterations and advancement of treatment in peripheral T-cell lymphoma

Zhang, P., & Zhang, M. (2020) · Clinical Epigenetics · doi:10.1186/s13148-020-00962-x · Cited by 91

Recruitment and Biological Consequences of Histone Modification of H3K27me3 and H3K9me3

Kim, J. H., & Kim, H. (2012) · ILAR Journal · doi:10.1093/ilar.53.3-4.232 · Cited by 94

Post-translational modifications of EZH2 in cancer

Li, Z., Li, M., Wang, D., Hou, P., Chen, X., Chu, S., Chai, D., Zheng, J., & Bai, J. (2020) · Cell & Bioscience · doi:10.1186/s13578-020-00505-0 · Cited by 87

Meta‐analysis of genome‐wide DNA methylation and integrative omics of age in human skeletal muscle

Voisin, S. A. C., Jacques, M., Landen, S., Harvey, N. R., Haupt, L. M., Griffiths, L. R., Gancheva, S., Ouni, M., Jähnert, M., Ashton, K. J., et al. (2021) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.12741 · Cited by 93

Targeting the enhancer of zeste homologue 2 in medulloblastoma

Alimova, I. N., Venkataraman, S., Harris, P. S., Márquez, V. E., Northcott, P. A., Dubuc, A. M., Taylor, M. D., Foreman, N. K., & Vibhakar, R. (2012) · International Journal of Cancer · doi:10.1002/ijc.27455 · Cited by 87

Inactivation of Ezh2 Upregulates Gfi1 and Drives Aggressive Myc-Driven Group 3 Medulloblastoma

Vo, B. T., Li, C., Morgan, M. A., Theurillat, I., Finkelstein, D., Wright, S., Hyle, J. W., Smith, S. M. C., Fan, Y., Wang, Y., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.02.073 · Cited by 86

Histone Deacetylase 3 Coordinates Deacetylase-independent Epigenetic Silencing of Transforming Growth Factor-β1 (TGF-β1) to Orchestrate Second Heart Field Development

Lewandowski, S. L., Janardhan, H. P., & Trivedi, C. M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.684753 · Cited by 85

Inhibitors of DNA Methylation, Histone Deacetylation, and Histone Demethylation

Zahnow, C. A., Topper, M. J., Stone, M. L., Stewart, T. M., Li, H., Baylin, S. B., & Casero, R. A. (2016) · Advances in cancer research · doi:10.1016/bs.acr.2016.01.007 · Cited by 88

Corepressor Protein CDYL Functions as a Molecular Bridge between Polycomb Repressor Complex 2 and Repressive Chromatin Mark Trimethylated Histone Lysine 27

Zhang, Y., Yang, X., Gui, B., Xie, G., Zhang, D., Shang, Y., & Liang, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.271064 · Cited by 89

Nanoscale chromatin profiling of gastric adenocarcinoma reveals cancer-associated cryptic promoters and somatically acquired regulatory elements

Muratani, M., Deng, N., Ooi, W. F., Lin, S. J., Xing, M., Xu, C., Qamra, A., Tay, S. T., Malik, S., Wu, J., et al. (2014) · Nature Communications · doi:10.1038/ncomms5361 · Cited by 84

PRDM14: a unique regulator for pluripotency and epigenetic reprogramming

Nakaki, F., & Saitou, M. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.04.003 · Cited by 87

Digging deep into “dirty” drugs – modulation of the methylation machinery

Pleyer, L., & Greil, R. (2015) · Drug Metabolism Reviews · doi:10.3109/03602532.2014.995379 · Cited by 84

Multifaceted role of EZH2 in breast and prostate tumorigenesis

Deb, G., Thakur, V. S., & Gupta, S. (2013) · Epigenetics · doi:10.4161/epi.24532 · Cited by 92

Jmjd3 Controls Mesodermal and Cardiovascular Differentiation of Embryonic Stem Cells

Ohtani, K., Zhao, C., Dobreva, G. D., Manavski, Y., Kluge, B., Braun, T. W., Rieger, M. A., Zeiher, A. M., & Dimmeler, S. (2013) · Circulation Research · doi:10.1161/circresaha.113.302035 · Cited by 87

The Human Immunodeficiency Virus 1 ASP RNA promotes viral latency by recruiting the Polycomb Repressor Complex 2 and promoting nucleosome assembly

Zapata, J. C., Campilongo, F., Barclay, R. A., DeMarino, C., Iglesias-Ussel, M. D., Kashanchi, F., & Romerio, F. (2017) · Virology · doi:10.1016/j.virol.2017.03.002 · Cited by 84

Using antagonistic pleiotropy to design a chemotherapy-induced evolutionary trap to target drug resistance in cancer

Lin, K., Rutter, J. C., Xie, A., Pardieu, B., Winn, E. T., Bello, R. D., Forget, A., Itzykson, R., Ahn, Y.-R., Dai, Z., et al. (2020) · Nature Genetics · doi:10.1038/s41588-020-0590-9 · Cited by 88

Multiomic analysis of malignant pleural mesothelioma identifies molecular axes and specialized tumor profiles driving intertumor heterogeneity

Mangiante, L., Alcala, N., Sexton‐Oates, A., Genova, A. D., González-Pérez, A., Khandekar, A., Bergstrom, E. N., Kim, J., Liu, X., Blázquez‐Encinas, R., et al. (2023) · Nature Genetics · doi:10.1038/s41588-023-01321-1 · Cited by 89

Lineage-specific canonical and non-canonical activity of EZH2 in advanced prostate cancer subtypes

Venkadakrishnan, V. B., Presser, A. G., Singh, R., Booker, M. A., Traphagen, N. A., Weng, K., Voss, N. C. E., Mahadevan, N. R., Mizuno, K., Puca, L., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-51156-5 · Cited by 84

Posttranslational modifications of human histone H3: An update

Xu, Y., Du, J.-Y., & Lau, A. T. Y. (2014) · PROTEOMICS · doi:10.1002/pmic.201300435 · Cited by 89

Cutting Edge: EZH2 Promotes Osteoclastogenesis by Epigenetic Silencing of the Negative Regulator IRF8

Fang, C., Qiao, Y., Mun, S. H., Lee, M. J., Murata, K., Bae, S., Zhao, B., Park‐Min, K., & Ivashkiv, L. B. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1501466 · Cited by 85

Long noncoding RNA H19 regulates EZH2 expression by interacting with miR-630 and promotes cell invasion in nasopharyngeal carcinoma

Li, X., Lin, Y., Yang, X., Wu, X., & He, X. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.03.150 · Cited by 83

Targeting EZH2 reactivates a breast cancer subtype-specific anti-metastatic transcriptional program

Hirukawa, A., Smith, H. W., Zuo, D., Dufour, C. R., Savage, P., Bertos, N., Johnson, R. M., Bui, T., Bourque, G., Basik, M., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04864-8 · Cited by 85

Histone variants H2A.Z and H3.3 coordinately regulate PRC2-dependent H3K27me3 deposition and gene expression regulation in mES cells

Wang, Y., Long, H., Yu, J., Dong, L., Wassef, M. A., Zhuo, B., Li, X., Zhao, J., Wang, M., Liu, C., et al. (2018) · BMC Biology · doi:10.1186/s12915-018-0568-6 · Cited by 81

LncRNAs as Chromatin Regulators in Cancer: From Molecular Function to Clinical Potential

Begolli, R., Sideris, N., & Giakountis, A. (2019) · Cancers · doi:10.3390/cancers11101524 · Cited by 90

Overview of epigenetic degraders based on PROTAC, molecular glue, and hydrophobic tagging technologies

Peng, X., Hu, Z., Zeng, L., Zhang, M., Xu, C., Lu, B., Tao, C., Chen, W., Hou, W., Cheng, K., et al. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.09.003 · Cited by 87

The Properties of Long Noncoding RNAs That Regulate Chromatin

Rutenberg-Schoenberg, M., Sexton, A. N., & Simon, M. D. (2016) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-090314-024939 · Cited by 86

IFN-γ Induces Histone 3 Lysine 27 Trimethylation in a Small Subset of Promoters to Stably Silence Gene Expression in Human Macrophages

Qiao, Y., Kang, K., Γιαννοπούλου, Ε., Fang, C., & Ivashkiv, L. B. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.08.051 · Cited by 83

A non‐canonical function of Ezh2 preserves immune homeostasis

Vasanthakumar, A., Xu, D., Lun, A. T. L., Kueh, A. J., van Gisbergen, K. P. J. M., Iannarella, N., Li, X., Yu, L., Wang, D., Williams, B. R. G., et al. (2017) · EMBO Reports · doi:10.15252/embr.201643237 · Cited by 86

Inhibitors of the Histone Methyltransferases EZH2/1 Induce a Potent Antiviral State and Suppress Infection by Diverse Viral Pathogens

Arbuckle, J. H., Gardina, P. J., Gordon, D. N., Hickman, H. D., Yewdell, J. W., Pierson, T. C., Myers, T. G., & Kristie, T. M. (2017) · mBio · doi:10.1128/mbio.01141-17 · Cited by 83

Targeting histone methyltransferase EZH2 as cancer treatment

Kondo, Y. (2014) · The Journal of Biochemistry · doi:10.1093/jb/mvu054 · Cited by 82

TRIM28 interacts with EZH2 and SWI/SNF to activate genes that promote mammosphere formation

Li, J.-D., Xi, Y., Li, W., McCarthy, R. L., Stratton, S. A., Zou, W., Li, W., Dent, S., Jain, A. K., & Barton, M. C. (2017) · Oncogene · doi:10.1038/onc.2016.453 · Cited by 81

A Chemical Genetics Approach for the Functional Assessment of Novel Cancer Genes

Zhou, Q., Derti, A., Ruddy, D. A., Rakiec, D. P., Kao, I., Lira, M., Gibaja, V., Chan, H., Yang, Y., Min, J., et al. (2015) · Cancer Research · doi:10.1158/0008-5472.can-14-2930 · Cited by 85

SIRT6 promotes transcription of a subset of NRF2 targets by mono-ADP-ribosylating BAF170

Rezazadeh, S., Yang, D. X., Tombline, G., Simon, M. A., Regan, S. P., Seluanov, A., & Gorbunova, V. A. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz528 · Cited by 82

Histone target selection within chromatin: an exemplary case of teamworkPreprint

Lalonde, M., Cheng, X., & Côté, J. (2014) · Genes & Development · doi:10.1101/gad.236331.113 · Cited by 85

Targeting activating mutations of EZH2 leads to potent cell growth inhibition in human melanoma by derepression of tumor suppressor genes

Tiffen, J. C., Gunatilake, D., Gallagher, S. J., Gowrishankar, K., Heinemann, A., Cullinane, C. M., Dutton‐Regester, K., Pupo, G. M., Strbenac, D., Yang, J. Y. H., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.4809 · Cited by 81

An Evolutionary Conserved Epigenetic Mark of Polycomb Response Elements Implemented by Trx/MLL/COMPASS

Rickels, R. A., Hu, D., Collings, C. K., Woodfin, A. R., Piunti, A., Mohan, M., Herz, H., Kvon, E. Z., & Shilatifard, A. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.06.018 · Cited by 82

Landscape of histone modifications in a sponge reveals the origin of animal cis-regulatory complexity

Gaiti, F., Jindrich, K., Fernández-Valverde, S. L., Roper, K. E., Degnan, B. M., & Tanurdžić, M. (2017) · eLife · doi:10.7554/elife.22194 · Cited by 84

Ubiquitination-Independent Repression of PRC1 Targets during Neuronal Fate Restriction in the Developing Mouse Neocortex

Tsuboi, M., Kishi, Y., Yokozeki, W., Koseki, H., Hirabayashi, Y., & Gotoh, Y. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.11.018 · Cited by 86

DNA methylation clocks for dogs and humans

Horvath, S., Lu, A. T.-H., Haghani, A., Zoller, J. A., Li, C. Z., Lim, A. R., Brooke, R. T., Raj, K., Armero, A. S., Dreger, D. L., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2120887119 · Cited by 85

Regulation of T Cell Differentiation and Function by EZH2

Karantanos, T., Chistofides, A., Barhdan, K., Li, L., & Boussiotis, V. A. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00172 · Cited by 81

Roles of H3K27me2 and H3K27me3 Examined during Fate Specification of Embryonic Stem Cells

Juan, A. H., Wang, S., Ko, K. D., Zare, H., Tsai, P.-F., Feng, X., Vivanco, K. O., Ascoli, A. M., Gutierrez-Cruz, G., Krebs, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.087 · Cited by 77

Live-cell imaging reveals the dynamics of PRC2 and recruitment to chromatin by SUZ12-associated subunitsPreprint

Youmans, D. T., Schmidt, J. C., & Cech, T. R. (2018) · Genes & Development · doi:10.1101/gad.311936.118 · Cited by 85

PRC 1 is taking the lead in P c G repression

Merini, W., & Calonje, M. (2015) · The Plant Journal · doi:10.1111/tpj.12818 · Cited by 83

Chromatin signature of widespread monoallelic expression

Nag, A., Savova, V., Fung, H.-L., Miron, A., Yuan, G., Zhang, K., & Gimelbrant, A. A. (2013) · eLife · doi:10.7554/elife.01256 · Cited by 78

Loss of H3K27me3 in meningiomas

Nassiri, F., Wang, J. Z., Singh, O., Karimi, S., Dalcourt, T., Ijad, N., Pirouzmand, N., Ng, H., Saladino, A., Pollo, B., et al. (2021) · Neuro-Oncology · doi:10.1093/neuonc/noab036 · Cited by 80

Uncovering the role of genomic “dark matter” in human disease

Martin, L., & Chang, H. Y. (2012) · Journal of Clinical Investigation · doi:10.1172/jci60020 · Cited by 80

Cutting Edge: Smad2 and Smad4 Regulate TGF-β–Mediated Il9 Gene Expression via EZH2 Displacement

Wang, A., Pan, D., Lee, Y., Martínez, G., Feng, X., & Dong, C. (2013) · The Journal of Immunology · doi:10.4049/jimmunol.1300433 · Cited by 87

Complementary Activities of TELOMERE REPEAT BINDING Proteins and Polycomb Group Complexes in Transcriptional Regulation of Target Genes

Zhou, Y., Hartwig, B., James, G. V., Schneeberger, K., & Turck, F. (2015) · The Plant Cell · doi:10.1105/tpc.15.00787 · Cited by 77

Systems Level Analysis of Histone H3 Post-translational Modifications (PTMs) Reveals Features of PTM Crosstalk in Chromatin Regulation

Schwämmle, V., Sidoli, S., Ruminowicz, C., Wu, X., Lee, C.-F., Helin, K., & Jensen, O. N. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.054460 · Cited by 80

LANA-Mediated Recruitment of Host Polycomb Repressive Complexes onto the KSHV Genome during De Novo Infection

Tóth, Z., Papp, B., Brulois, K., Choi, Y. J., Gao, S., & Jung, J. U. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005878 · Cited by 80

Transcriptional Regulation of Arabidopsis Polycomb Repressive Complex 2 Coordinates Cell-Type Proliferation and Differentiation

de Lucas, M., Pu, L., Turco, G. M., Gaudinier, A., Morao, A. K., Harashima, H., Kim, D., Ron, M., Sugimoto, K., Roudier, F., et al. (2016) · The Plant Cell · doi:10.1105/tpc.15.00744 · Cited by 84

Cancer: pathological nuclear reprogramming?

Goding, C. R., Pei, D., & Lü, X. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3781 · Cited by 82

Large Scale Analysis of Co-existing Post-translational Modifications in Histone Tails Reveals Global Fine Structure of Cross-talk

Schwämmle, V., Aspalter, C.-M., Sidoli, S., & Jensen, O. N. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.o113.036335 · Cited by 79

A late-lineage murine neutrophil precursor population exhibits dynamic changes during demand-adapted granulopoiesis

Kim, M., Yang, D., Kim, M., Kim, S., Kim, D., & Kang, S. (2017) · Scientific Reports · doi:10.1038/srep39804 · Cited by 82

Ezh2 programs TFH differentiation by integrating phosphorylation-dependent activation of Bcl6 and polycomb-dependent repression of p19Arf

Li, F., Zeng, Z., Xing, S., Gullicksrud, J. A., Shan, Q., Choi, J., Badovinac, V. P., Crotty, S., Peng, W., & Xue, H. (2018) · Nature Communications · doi:10.1038/s41467-018-07853-z · Cited by 79

Polycomb repressive 2 complex—Molecular mechanisms of function

Kouznetsova, V. L., Tchekanov, A., Li, X., Yan, X., & Tsigelny, I. F. (2019) · Protein Science · doi:10.1002/pro.3647 · Cited by 82

LncRNA HOTAIR: A Potential Prognostic Factor and Therapeutic Target in Human Cancers

Xin, X., Li, Q., Fang, J., & Zhao, T. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.679244 · Cited by 79

Ctbp2 Modulates NuRD-Mediated Deacetylation of H3K27 and Facilitates PRC2-Mediated H3K27me3 in Active Embryonic Stem Cell Genes During Exit from Pluripotency

Kim, T. W., Kang, B.-H., Jang, H., Kwak, S., Shin, J., Kim, H., Lee, S.-E., Lee, S.-M., Lee, J., Kim, J.-H., et al. (2015) · Stem Cells · doi:10.1002/stem.2046 · Cited by 79

Local Effect of Enhancer of Zeste-Like Reveals Cooperation of Epigenetic and cis-Acting Determinants for Zygotic Genome Rearrangements

Lhuillier‐Akakpo, M., Frapporti, A., Wilkes, C. D., Matelot, M., Vervoort, M., Sperling, L., & Duharcourt, S. (2014) · PLoS Genetics · doi:10.1371/journal.pgen.1004665 · Cited by 86

Centromeric and ectopic assembly of CENP-A chromatin in health and cancer: old marks and new tracks

Sharma, A. B., Dimitrov, S. I., Hamiche, A., & Dyck, E. V. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky1298 · Cited by 82

Structure, mechanism, and regulation of polycomb-repressive complex 2

Moritz, L., & Trievel, R. C. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.r117.800367 · Cited by 84

PRC2‐complex related dysfunction in overgrowth syndromes: A review of EZH2 , EED , and SUZ12 and their syndromic phenotypes

Cyrus, S., Burkardt, D. D., Weaver, D. D., & Gibson, W. T. (2019) · American Journal of Medical Genetics Part C Seminars in Medical Genetics · doi:10.1002/ajmg.c.31754 · Cited by 78

The Functions of Hepatitis B Virus Encoding Proteins: Viral Persistence and Liver Pathogenesis

Zhao, F., Xie, X., Tan, X., Yu, H., Tian, M., Lv, H., Qin, C., Qi, J., & Zhu, Q. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.691766 · Cited by 86

Non‐coding RNAs and EZH2 interactions in cancer: Long and short tales from the transcriptome

Benetatos, L., Voulgaris, E., Vartholomatos, G., & Hatzimichael, E. C. (2012) · International Journal of Cancer · doi:10.1002/ijc.27859 · Cited by 78

The polycomb group protein EZH2 is a novel therapeutic target in tongue cancer

Li, Z., Wang, Y., Qiu, J., Li, Q., Yuan, C., Zhang, W., Wang, D., Ye, J., Jiang, H., Yang, J., et al. (2013) · Oncotarget · doi:10.18632/oncotarget.1503 · Cited by 79

Deciphering the Epigenetic Code of Cardiac Myocyte Transcription

Preißl, S., Schwaderer, M., Raulf, A., Hesse, M., Grüning, B. A., Köbele, C., Backofen, R., Fleischmann, B. K., Hein, L., & Gilsbach, R. (2015) · Circulation Research · doi:10.1161/circresaha.115.306337 · Cited by 75

Epigenetic Control of the Bone-master Runx2 Gene during Osteoblast-lineage Commitment by the Histone Demethylase JARID1B/KDM5B

Rojas, A. P., Aguilar, R., Henríquez, B., Lian, J. B., Stein, J. L., Stein, G. S., van Wijnen, A. J., van Zundert, B., Allende, M. L., & Montecino, M. A. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.657825 · Cited by 78

Dynamic Protein Interactions of the Polycomb Repressive Complex 2 during Differentiation of Pluripotent Cells

Oliviero, G., Brien, G. L., Waston, A., Streubel, G., Jerman, E., Andrews, D. C., Doyle, B., Munawar, N., Wynne, K. J., Crean, J. K. G., et al. (2016) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.062240 · Cited by 89

EZH2 cooperates with gain‐of‐function p53 mutants to promote cancer growth and metastasis

Zhao, Y., Ding, L., Wang, D., Ye, Z., He, Y., Ma, L., Zhu, R., Pan, Y., Wu, Q., Pang, K., et al. (2019) · The EMBO Journal · doi:10.15252/embj.201899599 · Cited by 81

Non-canonical functions of the DNA methylome in gene regulation

Reddington, J. P., Pennings, S., & Meehan, R. R. (2013) · Biochemical Journal · doi:10.1042/bj20121585 · Cited by 81

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