An allosteric PRC2 inhibitor targeting the H3K27me3 binding pocket of EED

<i>Coot</i> : model-building tools for molecular graphics

Emsley, P., & Cowtan, K. (2004) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444904019158 · Cited by 30,571 · see citing works

The CCP4 suite: programs for protein crystallography

Number Collaborative Computational Project (1994) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444994003112 · Cited by 17,299 · 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

Epigenetic Regulations of GABAergic Neurotransmission: Relevance for Neurological Disorders and Epigenetic Therapy

Shrestha, S., & Offer, S. M. (2016) · Medical Epigenetics · doi:10.1159/000444713 · Cited by 8,949 · see citing works

REFMAC 5 for the refinement of macromolecular crystal structures

Murshudov, G. N., Skubák, P., Lebedev, A. A., Pannu, N. S., Steiner, R. A., Nicholls, R. A., Winn, M., Long, F., & Vagin, A. A. (2011) · Acta Crystallographica Section D Biological Crystallography · doi:10.1107/s0907444911001314 · Cited by 8,385 · see citing works

EZH2 inhibition as a therapeutic strategy for lymphoma with EZH2-activating mutations

McCabe, M. T., Ott, H. M., Ganji, G., Korenchuk, S., Thompson, C., Van Aller, G. S., Liu, Y., Graves, A. P., III, A. D. P., Diaz, E., et al. (2012) · Nature · doi:10.1038/nature11606 · Cited by 1,786 · see citing works

Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin

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

Lapatinib with trastuzumab for HER2-positive early breast cancer (NeoALTTO): a randomised, open-label, multicentre, phase 3 trial

Baselga, J. M., Bradbury, I., Eidtmann, H., Cosimo, S. D., de Azambuja, E., Aura, C. M., Gómez, H., Dinh, P., Fauria, K., Dooren, V. V., et al. (2012) · The Lancet · doi:10.1016/s0140-6736(11)61847-3 · Cited by 1,317 · see citing works

Role of the polycomb protein EED in the propagation of repressive histone marks

Margueron, R., Justin, N., Ohno, K., Sharpe, M. L., Son, J., Drury, W. J., Voigt, P., Martin, S. R., Taylor, W. R., Marco, V. D., et al. (2009) · Nature · doi:10.1038/nature08398 · Cited by 1,203 · see citing works

EZH2 is downstream of the pRB-E2F pathway, essential for proliferation and amplified in cancer.

Bracken, A. P., Pasini, D., Capra, M., Prosperini, E., Colli, E., & Helin, K. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg542 · Cited by 1,196 · 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

Chromatin Modifications by Methylation and Ubiquitination: Implications in the Regulation of Gene Expression

Shilatifard, A. (2006) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.75.103004.142422 · Cited by 1,099 · see citing works

The functions of E(Z)/EZH2-mediated methylation of lysine 27 in histone H3

Cao, R., & Zhang, Y. (2004) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.02.001 · Cited by 907 · see citing works

SUZ12 Is Required for Both the Histone Methyltransferase Activity and the Silencing Function of the EED-EZH2 Complex

Cao, R., & Zhang, Y. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.06.020 · Cited by 809 · see citing works

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 · 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

Coordinated activities of wild-type plus mutant EZH2 drive tumor-associated hypertrimethylation of lysine 27 on histone H3 (H3K27) in human B-cell lymphomas

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

Structure and function of WD40 domain proteins

Xu, C., & Min, J. (2011) · Protein & Cell · doi:10.1007/s13238-011-1018-1 · Cited by 644 · see citing works

WD40 proteins propel cellular networks

Stirnimann, C. U., Petsalaki, E., Russell, R. B., & Müller, C. W. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.04.003 · Cited by 629 · see citing works

PRC2 is recurrently inactivated through EED or SUZ12 loss in malignant peripheral nerve sheath tumors

Lee, W., Teckie, S., Wiesner, T., Ran, L., Granada, C. N. P., Lin, M., Zhu, S., Cao, Z., Liang, Y., Sboner, A., et al. (2014) · Nature Genetics · doi:10.1038/ng.3095 · Cited by 618 · see citing works

Somatic mutations at EZH2 Y641 act dominantly through a mechanism of selectively altered PRC2 catalytic activity, to increase H3K27 trimethylation

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 609 · see citing works

Selective inhibition of Ezh2 by a small molecule inhibitor blocks tumor cells proliferation

Qi, W., Chan, H., Teng, L., Li, L., Chuai, S., Zhang, R., Zeng, J., Li, M., Fan, H. X., Lin, Y., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1210371110 · Cited by 550 · see citing works

H3K36 Methylation Antagonizes PRC2-mediated H3K27 Methylation

Yuan, W., Xu, M., Huang, C., Liu, N., Chen, S., & Zhu, B. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.194027 · Cited by 537 · see citing works

Selective Inhibition of EZH2 by EPZ-6438 Leads to Potent Antitumor Activity in EZH2 -Mutant Non-Hodgkin Lymphoma

Knutson, S. K., Kawano, S., Minoshima, Y., Warholic, N. M., Huang, K., Xiao, Y., Kadowaki, T., Uesugi, M., Kuznetsov, G., Kumar, N., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0773 · Cited by 529 · 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., et al. (2012) · Nature Medicine · doi:10.1038/nm.2651 · Cited by 528 · see citing works

Mutation of A677 in histone methyltransferase EZH2 in human B-cell lymphoma promotes hypertrimethylation of histone H3 on lysine 27 (H3K27)

McCabe, M. T., Graves, A. P., Ganji, G., Diaz, E., Halsey, W. S., Jiang, Y., Smitheman, K. N., Ott, H. M., Pappalardi, M. B., Allen, K. E., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1116418109 · Cited by 493 · see citing works

PRC2 loss amplifies Ras-driven transcription and confers sensitivity to BRD4-based therapies

Raedt, T. D., Beert, E., Pasmant, É., Luscan, A., Brems, H., Ortonne, N., Helin, K., Hornick, J. L., Mautner, V., Kehrer‐Sawatzki, H., et al. (2014) · Nature · doi:10.1038/nature13561 · Cited by 463 · see citing works

An Orally Bioavailable Chemical Probe of the Lysine Methyltransferases EZH2 and EZH1

Konze, K. D., Ma, A., Li, F., Baršytė-Lovejoy, D., Parton, T., MacNevin, C. J., Liu, F., Gao, C., Huang, X., Kuznetsova, E., et al. (2013) · ACS Chemical Biology · doi:10.1021/cb400133j · Cited by 450 · see citing works

Structural basis of oncogenic histone H3K27M inhibition of human polycomb repressive complex 2

Justin, N., Zhang, Y., Tarricone, C., Martin, S. R., Chen, S., Underwood, E., Marco, V. D., Haire, L. F., Walker, P. A., Reinberg, D., et al. (2016) · Nature Communications · doi:10.1038/ncomms11316 · Cited by 403 · see citing works

Structural basis of histone H3K27 trimethylation by an active polycomb repressive complex 2

Jiao, L., & Liu, X. (2015) · Science · doi:10.1126/science.aac4383 · Cited by 402 · see citing works

Crystal structure of the human PRMT5:MEP50 complex

Antonysamy, S., Bonday, Z., Campbell, R. M., Doyle, B. L., Druzina, Z., Gheyi, T., Han, B., Jungheim, L. N., Qian, Y., Rauch, C. T., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1209814109 · Cited by 373 · see citing works

A Polycomb Repression Signature in Metastatic Prostate Cancer Predicts Cancer Outcome

Yu, J., Yu, J., Rhodes, D. R., Tomlins, S. A., Cao, X., Chen, G., Mehra, R., Wang, X., Ghosh, D., Shah, R. B., et al. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-2498 · Cited by 348 · see citing works

Targeting MLL1 H3K4 Methyltransferase Activity in Mixed-Lineage Leukemia

Cao, F., Townsend, E. C., Karataş, H., Xu, J., Li, L., Lee, S. H. F., Liu, L., Chen, Y., Ouillette, P. D., Zhu, J., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.001 · Cited by 306 · see citing works

Synergistic blockade of mitotic exit by two chemical inhibitors of the APC/C

Sackton, K. L., Dimova, N., Zeng, X., Tian, W., Zhang, M., Sackton, T. B., Meaders, J., Pfaff, K. L., Sigoillot, F., Yu, H., et al. (2014) · Nature · doi:10.1038/nature13660 · Cited by 257 · see citing works

Structural basis for activity regulation of MLL family methyltransferases

Li, Y., Han, J., Zhang, Y., Cao, F., Liu, Z., Li, S., Wu, J., Hu, C., Wang, Y., Jin, S., et al. (2016) · Nature · doi:10.1038/nature16952 · Cited by 244 · see citing works

Relationship between Tumor Biomarkers and Efficacy in EMILIA, a Phase III Study of Trastuzumab Emtansine in HER2-Positive Metastatic Breast Cancer

Baselga, J. M., Phillips, G. D. L., Verma, S., Ro, J., Huober, J., Guardino, A. E., Samant, M. K., Olsen, S., de Haas, S. L., & Pegram, M. D. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-2499 · Cited by 229 · see citing works

Binding of different histone marks differentially regulates the activity and specificity of polycomb repressive complex 2 (PRC2)

Xu, C., Bian, C., Yang, W., Galka, M., Ouyang, H., Chen, C., Qiu, W., Liu, H., Jones, A. E., MacKenzie, F., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008937107 · Cited by 221 · see citing works

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 174 · see citing works

Small-molecule inhibition of MLL activity by disruption of its interaction with WDR5

Senisterra, G. A., Wu, H. Y., Allali‐Hassani, A., Wasney, G. A., Baršytė-Lovejoy, D., Dombrovski, L., Dong, A., Nguyen, K. T., Smil, D. V., Bolshan, Y., et al. (2012) · Biochemical Journal · doi:10.1042/bj20121280 · Cited by 165 · see citing works

Polycomb repressive complex 2 structure with inhibitor reveals a mechanism of activation and drug resistance

Brooun, A., Gajiwala, K. S., Deng, Y., Liu, W., Bolaños, B., Bingham, P., He, Y.-A., Diehl, W. C., Grable, N., Kung, P., et al. (2016) · Nature Communications · doi:10.1038/ncomms11384 · Cited by 164 · see citing works

Identification of EZH2 and EZH1 Small Molecule Inhibitors with Selective Impact on Diffuse Large B Cell Lymphoma Cell Growth

Garapaty, S., Nasveschuk, C. G., Gagnon, A., Chan, E. Y., Sandy, P., Busby, J., Balasubramanian, S., Campbell, R., Zhao, F., Bergeron, L., et al. (2013) · Chemistry & Biology · doi:10.1016/j.chembiol.2013.09.013 · Cited by 154 · see citing works

Structural Basis of EZH2 Recognition by EED

Han, Z., Xing, X., Hu, M., Zhang, Y., Liu, P., & Chai, J. (2007) · Structure · doi:10.1016/j.str.2007.08.007 · Cited by 150 · see citing works

A687V EZH2 is a gain‐of‐function mutation found in lymphoma patients

Majer, C. R., Jin, L., Scott, M. P., Knutson, S. K., Kuntz, K. W., Keilhack, H., Smith, J. J., Moyer, M. P., Richon, V. M., Copeland, R. A., et al. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.07.066 · Cited by 149 · see citing works

Development of secondary mutations in wild-type and mutant EZH2 alleles cooperates to confer resistance to EZH2 inhibitors

Gibaja, V, Shen, F., Harari, J., Korn, J., Ruddy, D., Saenz-Vash, V, Zhai, H., Rejtar, T., Paris, C. G., Yu, Z., et al. (2016) · Oncogene · doi:10.1038/onc.2015.114 · Cited by 149 · see citing works

Structure of the Arginine Methyltransferase PRMT5-MEP50 Reveals a Mechanism for Substrate Specificity

Ho, M.-C., Wilczek, C., Bonanno, J. B., Li, X., Seznec, J., Matsui, T., Carter, L. G., Onikubo, T., Kumar, P. R., Chan, M. K., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0057008 · Cited by 144 · see citing works

Ezh2 loss in hematopoietic stem cells predisposes mice to develop heterogeneous malignancies in an Ezh1-dependent manner

Mochizuki‐Kashio, M., Aoyama, K., Sashida, G., Oshima, M., Tomioka, T., Muto, T., Wang, C., & Iwama, A. (2015) · Blood · doi:10.1182/blood-2015-03-634428 · Cited by 141 · see citing works

EPZ011989, A Potent, Orally-Available EZH2 Inhibitor with Robust in Vivo Activity

Campbell, J. E., Kuntz, K. W., Knutson, S. K., Warholic, N. M., Keilhack, H., Wigle, T. J., Raimondi, A., Klaus, C. R., Rioux, N., Yokoi, A., et al. (2015) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00037 · Cited by 129 · see citing works

Acquisition of a single EZH2 D1 domain mutation confers acquired resistance to EZH2-targeted inhibitors

Baker, T. E., Nerle, S., Pritchard, J. R., Zhao, B., Rivera, V. M., Garner, A. P., & Gonzalvez, F. (2015) · Oncotarget · doi:10.18632/oncotarget.5066 · Cited by 78 · see citing works

Analysis of the Binding of Mixed Lineage Leukemia 1 (MLL1) and Histone 3 Peptides to WD Repeat Domain 5 (WDR5) for the Design of Inhibitors of the MLL1−WDR5 Interaction

Karataş, H., Townsend, E. C., Bernard, D., Dou, Y., & Wang, S. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100139b · Cited by 75 · see citing works

The Multifunctions of WD40 Proteins in Genome Integrity and Cell Cycle Progression

Zhang, C., & Zhang, F. (2015) · Journal of Genomics · doi:10.7150/jgen.11015 · Cited by 74 · see citing works

On WD40 proteins: Propelling our knowledge of transcriptional control?

Migliori, V., Mapelli, M., & Guccione, E. (2012) · Epigenetics · doi:10.4161/epi.21140 · Cited by 70 · see citing works

Discovery and Optimization of Tetramethylpiperidinyl Benzamides as Inhibitors of EZH2

Nasveschuk, C. G., Gagnon, A., Garapaty, S., Balasubramanian, S., Campbell, R., Lee, C., Zhao, F., Bergeron, L., Cummings, R. T., Trojer, P., et al. (2014) · ACS Medicinal Chemistry Letters · doi:10.1021/ml400494b · Cited by 63 · see citing works

Quantitative Profiling of Combinational K27/K36 Modifications on Histone H3 Variants in Mouse Organs

Yu, Y., Chen, J., Gao, Y., Gao, J., Liao, R., Wang, Y., O-Yang, C., Li, E., Zeng, C., Zhou, S., et al. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.5b01164 · Cited by 21 · see citing works

A liquid chromatography/mass spectrometry-based generic detection method for biochemical assay and hit discovery of histone methyltransferases

Li, S., Gu, X., Hao, Q., Fan, H. X., Li, L., Zhou, S., Zhao, K., Chan, H. M., & Wang, Y. (2013) · Analytical Biochemistry · doi:10.1016/j.ab.2013.08.029 · Cited by 13 · see citing works

Small molecules in targeted cancer therapy: advances, challenges, and future perspectives

Zhong, L., Li, Y., Xiong, L., Wang, W., Wu, M., Yuan, T., Yang, W. M., Tian, C., Miao, Z., Wang, T., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00572-w · Cited by 1,735 · see citing works

Targeted protein degradation: expanding the toolbox

Schapira, M., Calabrese, M. F., Bullock, A. N., & Crews, C. M. (2019) · Nature Reviews Drug Discovery · doi:10.1038/s41573-019-0047-y · Cited by 960 · see citing works

EZH2: a novel target for cancer treatment

Duan, R., Du, W., & Guo, W. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00937-8 · Cited by 946 · see citing works

An Evolutionarily Conserved Function of Polycomb Silences the MHC Class I Antigen Presentation Pathway and Enables Immune Evasion in Cancer

Burr, M. L., Sparbier, C. E., Chan, K. L., Chan, Y.-C., Kersbergen, A. J., Lam, E. Y. N., Azidis-Yates, E., Vassiliadis, D., Bell, C. C., Gilan, O., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.08.008 · Cited by 656 · see citing works

PROTACs: An Emerging Therapeutic Modality in Precision Medicine

Nalawansha, D. A., & Crews, C. M. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.07.020 · Cited by 514 · see citing works

Epigenetic tools (The Writers, The Readers and The Erasers) and their implications in cancer therapy

Biswas, S., & Rao, C. M. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.08.021 · Cited by 402 · see citing works

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 382 · see citing works

WD40 repeat domain proteins: a novel target class?

Schapira, M., Tyers, M., Torrent, M., & Arrowsmith, C. H. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.179 · Cited by 335 · see citing works

Inhibitors of Protein Methyltransferases and Demethylases

Kanıskan, H. Ü., Martini, M. L., & Jin, J. J. (2017) · Chemical Reviews · doi:10.1021/acs.chemrev.6b00801 · Cited by 320 · see citing works

Chemical and Biochemical Perspectives of Protein Lysine Methylation

Luo, M. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00008 · Cited by 288 · see citing works

Regulation of Cellular Senescence by Polycomb Chromatin Modifiers through Distinct DNA Damage- and Histone Methylation-Dependent Pathways

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 · see citing works

PRC2 is high maintenancePreprint

Yu, J.-R., Lee, C., Oksuz, O., Stafford, J. M., & Reinberg, D. (2019) · Genes & Development · doi:10.1101/gad.325050.119 · Cited by 248 · see citing works

Recent Advances in Prostate Cancer Treatment and Drug Discovery

Nevedomskaya, E., Baumgart, S. J., & Haendler, B. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051359 · Cited by 257 · see citing works

Epigenetics and beyond: targeting writers of protein lysine methylation to treat disease

Bhat, K. P., Kanıskan, H. Ü., Jin, J. J., & Gozani, O. (2021) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-00108-x · Cited by 243 · see citing works

Targeting EZH2 in cancer therapy

Yamagishi, M., & Uchimaru, K. (2017) · Current Opinion in Oncology · doi:10.1097/cco.0000000000000390 · Cited by 224 · see citing works

EED-Targeted PROTACs Degrade EED, EZH2, and SUZ12 in the PRC2 Complex

Hsu, J. H.-R., Rasmusson, T., Robinson, J., Pachl, F., Read, J., Kawatkar, S., O’ Donovan, D. H., Bagal, S., Code, E., Rawlins, P., et al. (2020) · Cell Chemical Biology · doi:10.1016/j.chembiol.2019.11.004 · Cited by 202 · see citing works

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 196 · see citing works

Dangerous liaisons: interplay between SWI/SNF, NuRD, and Polycomb in chromatin regulation and cancerPreprint

Bracken, A. P., Brien, G. L., & Verrijzer, C. P. (2019) · Genes & Development · doi:10.1101/gad.326066.119 · Cited by 192 · see citing works

Regulation, functions and transmission of bivalent chromatin during mammalian development

Macrae, T. A., Fothergill-Robinson, J., & Ramalho‐Santos, M. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00518-2 · Cited by 186 · see citing works

Polycomb Gene Silencing Mechanisms: PRC2 Chromatin Targeting, H3K27me3 'Readout', and Phase Separation-Based Compaction

Guo, Y., Zhao, S., & Wang, G. G. (2021) · Trends in Genetics · doi:10.1016/j.tig.2020.12.006 · Cited by 184 · see citing works

Recent developments in epigenetic cancer therapeutics: clinical advancement and emerging trends

Nepali, K., & Liou, J. (2021) · Journal of Biomedical Science · doi:10.1186/s12929-021-00721-x · Cited by 185 · see citing works

Degradation of Polycomb Repressive Complex 2 with an EED-Targeted Bivalent Chemical Degrader

Potjewyd, F., Turner, A. W., Beri, J., Rectenwald, J. M., Norris-Drouin, J. L., Cholensky, S. H., Margolis, D. M., Pearce, K. H., Herring, L. E., & James, L. I. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.11.006 · Cited by 179 · see citing works

The long and short non-coding RNAs modulating EZH2 signaling in cancer

Mirzaei, S., Gholami, M. H., Hushmandi, K., Hashemi, F., Zabolian, A., Cañadas, I., Zarrabi, A., Nabavi, N., Aref, A. R., Crea, F., et al. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01235-1 · Cited by 162 · see citing works

RNA-modifying proteins as anticancer drug targets

Boriack‐Sjodin, P. A., Ribich, S. A., & Copeland, R. A. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.71 · Cited by 154 · see citing works

Mechanisms of resistance to EZH2 inhibitors in diffuse large B-cell lymphomas

Bisserier, M., & Wajapeyee, N. (2018) · Blood · doi:10.1182/blood-2017-08-804344 · Cited by 146 · see citing works

The role of histone methylation in the development of digestive cancers: a potential direction for cancer management

Chen, Y., Ren, B., Yang, J., Wang, H., Yang, G., Xu, R., You, L., & Zhao, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-00252-1 · Cited by 143 · see citing works

Distinct Stimulatory Mechanisms Regulate the Catalytic Activity of Polycomb Repressive Complex 2

Lee, C., Holder, M., Grau, D., Saldaña-Meyer, R., Yu, J.-R., Ganai, R. A., Zhang, J., Wang, M., LeRoy, G., Dobenecker, M., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.019 · Cited by 142 · see citing works

Engaging chromatin: PRC2 structure meets function

Chammas, P., Mocavini, I., & Croce, L. D. (2019) · British Journal of Cancer · doi:10.1038/s41416-019-0615-2 · Cited by 138 · see citing works

Optimization of Orally Bioavailable Enhancer of Zeste Homolog 2 (EZH2) Inhibitors Using Ligand and Property-Based Design Strategies: Identification of Development Candidate ( R )-5,8-Dichloro-7-(methoxy(oxetan-3-yl)methyl)-2-((4-methoxy-6-methyl-2-oxo-1,2-dihydropyridin-3-yl)methyl)-3,4-dihydroisoquinolin-1(2 H )-one (PF-06821497)

Kung, P., Bingham, P., Brooun, A., Collins, M. R., Deng, Y., Dinh, D. M., Fan, C., Gajiwala, K. S., Grantner, R., Gukasyan, H. J., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b01375 · Cited by 138 · see citing works

A chemical biology toolbox to study protein methyltransferases and epigenetic signaling

Scheer, S., Ackloo, S. Z., Medina, T. D. S., Schapira, M., Li, F., Ward, J. A., Lewis, A. M., Northrop, J. P., Richardson, P. L., Kanıskan, H. Ü., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-07905-4 · Cited by 136 · see citing works

Allosteric Activation Dictates PRC2 Activity Independent of Its Recruitment to Chromatin

Lee, C., Yu, J.-R., Kumar, S., Jin, Y., LeRoy, G., Bhanu, N. V., Kaneko, S., Garcia, B. A., Hamilton, A. D., & Reinberg, D. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.03.020 · Cited by 135 · see citing works

Shifts in podocyte histone H3K27me3 regulate mouse and human glomerular disease

Majumder, S., Thieme, K., Batchu, S. N., Alghamdi, T. A., Bowskill, B. B., Kabir, M. G., Liu, Y., Advani, S. L., White, K., Geldenhuys, L., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci95946 · Cited by 127 · see citing works

Proteolysis targeting chimeras (PROTACs) are emerging therapeutics for hematologic malignancies

He, Y., Khan, S., Huo, Z., Lv, D., Zhang, X., Liu, X., Yuan, Y., Hromas, R., Xu, M., Zheng, G., et al. (2020) · Journal of Hematology &amp; Oncology · doi:10.1186/s13045-020-00924-z · Cited by 126 · see citing works

Six Years (2012–2018) of Researches on Catalytic EZH2 Inhibitors: The Boom of the 2‐Pyridone Compounds

Fioravanti, R., Stazi, G., Zwergel, C., Valente, S., & Mai, A. (2018) · The Chemical Record · doi:10.1002/tcr.201800091 · Cited by 119 · see citing works

Histone Methyltransferase EZH2: A Therapeutic Target for Ovarian Cancer

Jones, B. A., Varambally, S., & Arend, R. C. (2018) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0437 · Cited by 115 · see citing works

The Promise for Histone Methyltransferase Inhibitors for Epigenetic Therapy in Clinical Oncology: A Narrative Review

Rugo, H. S., Jacobs, I. A., Sharma, S., Scappaticci, F. A., Paul, T. A., Jensen-Pergakes, K., & Malouf, G. G. (2020) · Advances in Therapy · doi:10.1007/s12325-020-01379-x · Cited by 108 · see citing works

EZH2 abnormalities in lymphoid malignancies: underlying mechanisms and therapeutic implications

Li, B., & Chng, W. J. (2019) · Journal of Hematology & Oncology · doi:10.1186/s13045-019-0814-6 · Cited by 99 · see citing works

Mesenchymal and adrenergic cell lineage states in neuroblastoma possess distinct immunogenic phenotypes

Sengupta, S., Das, S., Crespo, Â. C., Cornel, A. M., Patel, A. G., Mahadevan, N. R., Campisi, M., Ali, A. K., Sharma, B., Rowe, J. H., et al. (2022) · Nature Cancer · doi:10.1038/s43018-022-00427-5 · Cited by 94 · see citing works

Epigenetic regulation in cancer therapy: From mechanisms to clinical advances

Tao, L., Zhou, Y., Luo, Y., Qiu, J., Xiao, Y., Zou, J., Zhang, Y., Liu, X., Yang, X., Gou, K., et al. (2024) · MedComm – Oncology · doi:10.1002/mog2.59 · Cited by 93 · see citing works

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 · see citing works

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 79 · see citing works

Long non-coding RNA SNHG15 inhibits P15 and KLF2 expression to promote pancreatic cancer proliferation through EZH2-mediated H3K27me3

Ma, Z., Huang, H., Wang, J., Zhou, Y., Pu, F., Zhao, Q., Peng, P., Hui, B., Ji, H., & Wang, K. (2017) · Oncotarget · doi:10.18632/oncotarget.20359 · Cited by 77 · see citing works

Targeting Histone Methylation in Cancer

McCabe, M. T., Mohammad, H. P., Barbash, O., & Kruger, R. G. (2017) · The Cancer Journal · doi:10.1097/ppo.0000000000000283 · Cited by 73 · see citing works

EZH2-Mediated microRNA-139-5p Regulates Epithelial-Mesenchymal Transition and Lymph Node Metastasis of Pancreatic Cancer.

Ma, J., Zhang, J., Weng, Y., & Wang, J. (2018) · Europe PMC (PubMed Central) · doi:10.14348/molcells.2018.0109 · Cited by 70 · see citing works

Polycomb group proteins EZH2 and EED directly regulate androgen receptor in advanced prostate cancer

Liu, Q., Wang, G., Li, Q., Jiang, W., Kim, J., Wang, R., Zhu, S. L., Wang, X., Lin, Y., Yang, Y., et al. (2019) · International Journal of Cancer · doi:10.1002/ijc.32118 · Cited by 69 · see citing works

VHL-based PROTACs as potential therapeutic agents: Recent progress and perspectives

Wang, C., Zhang, Y., Wang, J., & Xing, D. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113906 · Cited by 71 · see citing works

Fragment-to-Lead Medicinal Chemistry Publications in 2017

Mortenson, P. N., Erlanson, D. A., de Esch, I. J. P., Jahnke, W., & Johnson, C. N. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01472 · Cited by 69 · see citing works

Lineage specification and pluripotency revealed by transcriptome analysis from oocyte to blastocyst in pig

Kong, Q., Xu, Y., Zhang, H., Liu, S., Zhao, J., Zhang, J., Weng, X., Jin, J., & Liu, Z. (2019) · The FASEB Journal · doi:10.1096/fj.201901818rr · Cited by 65 · see citing works

Triazole-fused pyrimidines in target-based anticancer drug discovery

Dai, X., Xue, L.-P., Ji, S., Zhou, Y., Gao, Y., Zheng, Y., Liu, H., & Liu, H. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115101 · Cited by 63 · see citing works

Targeting DCAF5 suppresses SMARCB1-mutant cancer by stabilizing SWI/SNF

Radko-Juettner, S., Yue, H., Myers, J., Carter, R. D., Robertson, A. N., Mittal, P., Zhu, Z., Hansen, B. S., Donovan, K. A., Hunkeler, M., et al. (2024) · Nature · doi:10.1038/s41586-024-07250-1 · Cited by 65 · see citing works

A chemical probe of CARM1 alters epigenetic plasticity against breast cancer cell invasion

Cai, X.-C., Zhang, T., Kim, E., Jiang, M. Z., Wang, K., Wang, J., Chen, S., Zhang, N., Wu, H., Li, F., et al. (2019) · eLife · doi:10.7554/elife.47110 · Cited by 62 · see citing works

Discovery of the Clinical Candidate MAK683: An EED-Directed, Allosteric, and Selective PRC2 Inhibitor for the Treatment of Advanced Malignancies

Huang, Y. R., Sendzik, M., Zhang, J., Gao, Z., Sun, Y., Wang, L., Gu, J., Zhao, K., Yu, Z., Zhang, L., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c02148 · Cited by 62 · see citing works

Polycomb repressive complex 2 shields naïve human pluripotent cells from trophectoderm differentiation

Kumar, B. M., Navarro, C., Winblad, N., Schell, J. P., Zhao, C., Weltner, J., Baqué-Vidal, L., Mantero, A. S., Sophie Petropoulos, A., Lanner, F., et al. (2022) · Nature Cell Biology · doi:10.1038/s41556-022-00916-w · Cited by 62 · see citing works

Small Molecule Approaches for Targeting the Polycomb Repressive Complex 2 (PRC2) in Cancer

Martin, M. C., Zeng, G., Yu, J., & Schiltz, G. E. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01344 · Cited by 62 · see citing works

Discovery and Characterization of a Cellular Potent Positive Allosteric Modulator of the Polycomb Repressive Complex 1 Chromodomain, CBX7

Lamb, K. N., Bsteh, D., Dishman, S. N., Moussa, H. F., Fan, H., Stuckey, J. I., Norris, J. L., Cholensky, S. H., Li, D., Wang, J., et al. (2019) · Cell chemical biology · doi:10.1016/j.chembiol.2019.07.013 · Cited by 60 · see citing works

Targeting epigenetic modulators using PROTAC degraders: Current status and future perspective

Webb, T., Craigon, C., & Ciulli, A. (2022) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2022.128653 · Cited by 59 · see citing works

Genome-Wide Estrogen Receptor Activity in Breast Cancer

Farcas, A. M., Nagarajan, S., Cosulich, S. C., & Carroll, J. S. (2020) · Endocrinology · doi:10.1210/endocr/bqaa224 · Cited by 58 · see citing works

Targeting non-bromodomain chromatin readers

Arrowsmith, C. H., & Schapira, M. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0290-2 · Cited by 58 · see citing works

EZH2 in hepatocellular carcinoma: progression, immunity, and potential targeting therapies

Wang, B., Liu, Y., Liao, Z., Wu, H., Zhang, B., & Zhang, L. (2023) · Experimental Hematology and Oncology · doi:10.1186/s40164-023-00405-2 · Cited by 57 · see citing works

Overcoming Clinical Resistance to EZH2 Inhibition Using Rational Epigenetic Combination Therapy

Kazansky, Y., Cameron, D., Mueller, H. S., Demarest, P., Zaffaroni, N., Arrighetti, N., Zuco, V., Kuwahara, Y., Somwar, R., Ladanyi, M., et al. (2024) · Cancer Discovery · doi:10.1158/2159-8290.cd-23-0110 · Cited by 59 · see citing works

PROTAC Linkerology Leads to an Optimized Bivalent Chemical Degrader of Polycomb Repressive Complex 2 (PRC2) Components

Bashore, F. M., Foley, C. A., Ong, H. W., Rectenwald, J. M., Hanley, R. P., Norris-Drouin, J. L., Cholensky, S. H., Mills, C. A., Pearce, K. H., Herring, L. E., et al. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.2c00804 · Cited by 56 · see citing works

Methyltransferase Inhibitors: Competing with, or Exploiting the Bound Cofactor

de Freitas, R. F., Ivanochko, D., & Schapira, M. (2019) · Molecules · doi:10.3390/molecules24244492 · Cited by 54 · see citing works

An Allosteric PRC2 Inhibitor Targeting EED Suppresses Tumor Progression by Modulating the Immune Response

Dong, H., Liu, S., Zhang, X., Chen, S., Kang, L., Chen, Y., Ma, S., Fu, X., Liu, Y., Zhang, H., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-0428 · Cited by 54 · see citing works

Polycomb Repressive Complex 2 Modulation through the Development of EZH2–EED Interaction Inhibitors and EED Binders

Tomassi, S., Romanelli, A., Zwergel, C., Valente, S., & Mai, A. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00226 · Cited by 56 · see citing works

Discovery and Molecular Basis of a Diverse Set of Polycomb Repressive Complex 2 Inhibitors Recognition by EED

Li, L., Zhang, H., Zhang, M., Zhao, M., Feng, L., Luo, X., Gao, Z., Huang, Y. R., Ardayfio, O., Zhang, J.-H., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169855 · Cited by 53 · see citing works

EZH2 is overexpressed in transitional preplasmablasts and is involved in human plasma cell differentiation

Herviou, L., Jourdan, M., Martinez, A., Cavalli, G., & Moreaux, J. (2019) · Leukemia · doi:10.1038/s41375-019-0392-1 · Cited by 52 · see citing works

Epigenetic small molecule modulators of histone and DNA methylation

Hauser, A., Robaa, D., & Jung, M. (2018) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2018.03.003 · Cited by 50 · see citing works

Drugging histone methyltransferases in cancer

Richart, L., & Margueron, R. (2020) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2019.11.009 · Cited by 49 · see citing works

EZH2 inhibitors: a patent review (2014-2016)

Stazi, G., Zwergel, C., Mai, A., & Valente, S. (2017) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2017.1316976 · Cited by 49 · see citing works

Drug Discovery and Chemical Biology of Cancer Epigenetics

Ribich, S. A., Harvey, D. M., & Copeland, R. A. (2017) · Cell chemical biology · doi:10.1016/j.chembiol.2017.08.020 · Cited by 49 · see citing works

Epigenetic Therapies for Acute Myeloid Leukemia and Their Immune-Related Effects

Gambacorta, V., Gnani, D., Vago, L., & Micco, R. D. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00207 · Cited by 48 · see citing works

Lysine methyltransferase inhibitors: where we are now

Feoli, A., Viviano, M., Cipriano, A., Milite, C., Castellano, S., & Sbardella, G. (2021) · RSC Chemical Biology · doi:10.1039/d1cb00196e · Cited by 48 · see citing works

Chemical modulators for epigenome reader domains as emerging epigenetic therapies for cancer and inflammation

Zaware, N., & Zhou, M. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.06.012 · Cited by 47 · see citing works

Persistent epigenetic reprogramming of sweet taste by diet

Vaziri, A., Khabiri, M., Genaw, B. T., May, C. E., Freddolino, P. L., & Dus, M. (2020) · Science Advances · doi:10.1126/sciadv.abc8492 · Cited by 47 · see citing works

Targeting epigenetic machinery: Emerging novel allosteric inhibitors

Ye, F., Huang, J. L., Wang, H., Luo, C., & Zhao, K. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.107406 · Cited by 45 · see citing works

Targeting PRC2 for the treatment of cancer: an updated patent review (2016 - 2020)

Dockerill, M., Gregson, C. L., & O’Donovan, D. H. (2020) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2021.1841167 · Cited by 46 · see citing works

Disease Association and Druggability of WD40 Repeat Proteins

Song, R., Wang, Z.-D., & Schapira, M. (2017) · Journal of Proteome Research · doi:10.1021/acs.jproteome.7b00451 · Cited by 45 · see citing works

Induction of senescence-associated secretory phenotype underlies the therapeutic efficacy of PRC2 inhibition in cancer

Chu, L., Qu, Y.-X., An, Y., Hou, L., Li, J., Li, W., Fan, G., Song, B., Li, E., Zhang, L., et al. (2022) · Cell Death and Disease · doi:10.1038/s41419-022-04601-6 · Cited by 45 · see citing works

Targeting key proteins involved in transcriptional regulation for cancer therapy: Current strategies and future prospective

Pei, H., Guo, W., Peng, Y., Xiong, H., & Chen, Y. (2022) · Medicinal Research Reviews · doi:10.1002/med.21886 · Cited by 45 · see citing works

Recent progress in developing selective inhibitors of protein methyltransferases

Kanıskan, H. Ü., & Jin, J. J. (2017) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2017.06.013 · Cited by 44 · see citing works

Epigenetic regulatory mutations and epigenetic therapy for multiple myeloma

Dupéré-Richer, D., & Licht, J. D. (2017) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000358 · Cited by 43 · see citing works

Structure-Guided Development of Small-Molecule PRC2 Inhibitors Targeting EZH2–EED Interaction

Du, D., Xu, D., Zhu, L., Stazi, G., Zwergel, C., Liu, Y., Luo, Z., Li, Y., Zhang, Y., Zhu, K., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c02261 · Cited by 44 · see citing works

PRC2, Chromatin Regulation, and Human Disease: Insights From Molecular Structure and Function

Liu, X., & Liu, X. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.894585 · Cited by 44 · see citing works

Exploiting Epigenetic Alterations in Prostate Cancer

Baumgart, S. J., & Haendler, B. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18051017 · Cited by 41 · see citing works

PRC2 engages a bivalent H3K27M-H3K27me3 dinucleosome inhibitor

Diehl, K. L., Ge, E. J., Weinberg, D. N., Jani, K. S., Allis, C. D., & Muir, T. W. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1911775116 · Cited by 40 · see citing works

Polycomb-lamina antagonism partitions heterochromatin at the nuclear periphery

Siegenfeld, A. P., Roseman, S. A., Roh, H., Lue, N. Z., Wagen, C., Zhou, E., Johnstone, S. E., Aryee, M. J., & Liau, B. B. (2022) · Nature Communications · doi:10.1038/s41467-022-31857-5 · Cited by 40 · see citing works

Disruption of mammalian SWI/SNF and polycomb complexes in human sarcomas: mechanisms and therapeutic opportunities

McBride, M. J., & Kadoch, C. (2018) · The Journal of Pathology · doi:10.1002/path.5042 · Cited by 39 · see citing works

The control of polycomb repressive complexes by long noncoding RNAs

Trotman, J. B., Braceros, K. C. A., Cherney, R. E., Murvin, M. M., & Calabrese, J. M. (2021) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1657 · Cited by 37 · see citing works

EZH2: An Accomplice of Gastric Cancer

Yu, W., Liu, N., Song, X., Chen, L., Wang, M., Xiao, G., Li, T., Wang, Z., & Zhang, Y. (2023) · Cancers · doi:10.3390/cancers15020425 · Cited by 37 · see citing works

Targeting protein methylation: from chemical tools to precision medicines

Dilworth, D., & Baršytė-Lovejoy, D. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03147-9 · Cited by 35 · see citing works

A positive feedback loop between EZH2 and NOX4 regulates nucleus pulposus cell senescence in age-related intervertebral disc degeneration

Liu, C., Liu, L., Yang, M., Li, B., Yi, J., Ai, X., Zhang, Y., Huang, B. S., Li, C., Feng, C., et al. (2020) · Cell Division · doi:10.1186/s13008-020-0060-x · Cited by 35 · see citing works

EEDi-5285: An Exceptionally Potent, Efficacious, and Orally Active Small-Molecule Inhibitor of Embryonic Ectoderm Development

Rej, R. K., Wang, C., Lü, J., Wang, M., Petrunak, E. M., Zawacki, K. P., McEachern, D., Fernández‐Salas, E., Yang, C., Wang, L., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00479 · Cited by 35 · see citing works

Pharmacological inhibition of noncanonical EED-EZH2 signaling overcomes chemoresistance in prostate cancer

Li, X., Gera, L., Zhang, S., Chen, Y., Lou, L., Wilson, L. M., Xie, Z., Sautto, G. A., Liu, D., Danaher, A., et al. (2021) · Theranostics · doi:10.7150/thno.49235 · Cited by 35 · see citing works

Chemically induced degradation of epigenetic targets

Kabir, M., Yu, X., Kanıskan, H. Ü., & Jin, J. J. (2023) · Chemical Society Reviews · doi:10.1039/d3cs00100h · Cited by 35 · see citing works

Structure-based view of the druggable genome

Wang, J., Yazdani, S., Han, A., & Schapira, M. (2020) · Drug Discovery Today · doi:10.1016/j.drudis.2020.02.006 · Cited by 34 · see citing works

Discovery of EEDi-5273 as an Exceptionally Potent and Orally Efficacious EED Inhibitor Capable of Achieving Complete and Persistent Tumor Regression

Rej, R. K., Wang, C., Lü, J., Wang, M., Petrunak, E. M., Zawacki, K. P., McEachern, D., Yang, C., Wang, L., Li, R., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01059 · Cited by 34 · see citing works

PRC2-Inactivating Mutations in Cancer Enhance Cytotoxic Response to DNMT1-Targeted Therapy via Enhanced Viral Mimicry

Patel, A. J., Warda, S., Mååg, J. L. V., Misra, R., Miranda-Román, M. A., Pachai, M. R., Lee, C. J., Li, D., Wang, N., Bayshtok, G., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-1671 · Cited by 36 · see citing works

Tackling malignant melanoma epigenetically: histone lysine methylation

Orouji, E., & Utikal, J. S. (2018) · Clinical Epigenetics · doi:10.1186/s13148-018-0583-z · Cited by 33 · see citing works

Histone H1 Mutations in Lymphoma: A Link(er) between Chromatin Organization, Developmental Reprogramming, and Cancer

Soshnev, A. A., Allis, C. D., Cesarman, E., & Melnick, A. M. (2021) · Cancer Research · doi:10.1158/0008-5472.can-21-2619 · Cited by 30 · see citing works

Methyllysine binding domains: Structural insight and small molecule probe development

Teske, K. A., & Hadden, M. K. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.04.047 · Cited by 32 · see citing works

Abstract LB-288: An allosteric PRC2 inhibitor targeting the H3K27me3 binding pocket of EED

Qi, W., Zhao, K., Gu, J., Huang, Y. R., Wang, Y., Zhang, H., Zhang, M., Zhang, J., Yu, Z., Li, L., et al. (2017) · Cancer Research · doi:10.1158/1538-7445.am2017-lb-288 · Cited by 1 · see citing works

Abstract IA19: Targeting the PRC2 complex through EED for anti-cancer therapy

Atadja, P. W. (2017) · Cancer Research · doi:10.1158/1538-7445.newfront17-ia19

Binding Modes of Small‐Molecule Inhibitors to the EED Pocket of PRC2

Huang, D., Tian, S., Qi, Y., & Zhang, J. Z. H. (2019) · ChemPhysChem · doi:10.1002/cphc.201900903 · Cited by 14 · see citing works

Discovery and Molecular Basis of a Diverse Set of Polycomb Repressive Complex 2 Inhibitors Recognition by EED

Li, L., Zhang, H., Zhang, M., Zhao, M., Feng, L., Luo, X., Gao, Z., Huang, Y. R., Ardayfio, O., Zhang, J.-H., et al. (2017) · PLoS ONE · doi:10.1371/journal.pone.0169855 · Cited by 53 · see citing works

Targeting the EED–H3K27me3 Interaction Allosterically Inhibits PRC2

(2017) · Cancer Discovery · doi:10.1158/2159-8290.cd-rw2017-030 · Cited by 2 · see citing works