SET for life: biochemical activities and biological functions of SET domain-containing proteins

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

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

Distinct and predictive chromatin signatures of transcriptional promoters and enhancers in the human genome

Heintzman, N. D., Stuart, R. K., Hon, G., Fu, Y., Ching, C. W., Hawkins, R. D., Barrera, L. O., Van Calcar, S., Qu, C., Ching, K. A., et al. (2007) · Nature Genetics · doi:10.1038/ng1966 · Cited by 3,398

The Polycomb complex PRC2 and its mark in life

Margueron, R., & Reinberg, D. (2011) · Nature · doi:10.1038/nature09784 · Cited by 3,347

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

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

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

Histone modifications at human enhancers reflect global cell-type-specific gene expression

Heintzman, N. D., Hon, G. C., Hawkins, R. D., Kheradpour, P., Stark, A., Harp, L. F., Ye, Z., Lee, L. K., Stuart, R. K., Ching, C. W., et al. (2009) · Nature · doi:10.1038/nature07829 · Cited by 2,533

Combinatorial patterns of histone acetylations and methylations in the human genome

Wang, Z., Zang, C., Rosenfeld, J. A., Schones, D. E., Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Peng, W., Zhang, M. Q., et al. (2008) · Nature Genetics · doi:10.1038/ng.154 · Cited by 2,331

Histone methylation: a dynamic mark in health, disease and inheritance

Greer, E. L., & Shi, Y. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3173 · Cited by 2,241

Domain organization of human chromosomes revealed by mapping of nuclear lamina interactions

Guelen, L., Pagie, L., Brasset, É., Meuleman, W. R. A., Faza, M. B., Talhout, W., Eussen, B. H. J., de Klein, A., Wessels, L. F. A., de Laat, W. L., et al. (2008) · Nature · doi:10.1038/nature06947 · Cited by 2,042

A long noncoding RNA maintains active chromatin to coordinate homeotic gene expression

Wang, K., Yang, Y. W., Liu, B., Sanyal, A., Corces, M. R., Chen, Y., Lajoie, B. R., Protacio, A., Flynn, R. A., Gupta, R. A., et al. (2011) · Nature · doi:10.1038/nature09819 · Cited by 2,005

Loss of the Suv39h Histone Methyltransferases Impairs Mammalian Heterochromatin and Genome Stability

Peters, A. H. F. M., O'Carroll, D., Scherthan, H., Mechtler, K., Sauer, S., Schöfer, C., Weipoltshammer, K., Pagani, M., Lachner, M., Kohlmaier, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00542-6 · Cited by 1,766

Polycomb Proteins Targeted by a Short Repeat RNA to the Mouse X Chromosome

Zhao, J. C., Sun, B. K., Erwin, J. A., Song, J., & Lee, J. T. (2008) · Science · doi:10.1126/science.1163045 · Cited by 1,580

Histone Lysine Methylation Dynamics: Establishment, Regulation, and Biological Impact

Black, J. C., Rechem, C. V., & Whetstine, J. R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.006 · Cited by 1,391

Mechanisms of Polycomb gene silencing: knowns and unknowns

Simon, J. A., & Kingston, R. E. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2763 · Cited by 1,360

SETDB1: a novel KAP-1-associated histone H3, lysine 9-specific methyltransferase that contributes to HP1-mediated silencing of euchromatic genes by KRAB zinc-finger proteins

Schultz, D. C., Ayyanathan, K., Negorev, D., Maul, G. G., & Rauscher, F. J. (2002) · Genes & Development · doi:10.1101/gad.973302 · Cited by 1,313

G9a histone methyltransferase plays a dominant role in euchromatic histone H3 lysine 9 methylation and is essential for early embryogenesisPreprint

Tachibana, M., Sugimoto, K., Nozaki, M., Ueda, J., Ohta, T., Ohki, M., Fukuda, M., Takeda, N., Niida, H., Kato, H., et al. (2002) · Genes & Development · doi:10.1101/gad.989402 · Cited by 1,294

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 1,281

Partitioning and Plasticity of Repressive Histone Methylation States in Mammalian Chromatin

Peters, A. H. F. M., Kubicek, S., Mechtler, K., O’Sullivan, R. J., Derijck, A. A. H. A., Perez-Burgos, L., Kohlmaier, A., Opravil, S., Tachibana, M., Shinkai, Y., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00477-5 · Cited by 1,208

Regulation of Alternative Splicing by Histone Modifications

Luco, R. F., Pan, Q., Tominaga, K., Blencowe, B. J., Pereira‐Smith, O. M., & Misteli, T. (2010) · Science · doi:10.1126/science.1184208 · Cited by 1,099

The COMPASS Family of Histone H3K4 Methylases: Mechanisms of Regulation in Development and Disease Pathogenesis

Shilatifard, A. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051710-134100 · Cited by 1,091

A silencing pathway to induce H3-K9 and H4-K20 trimethylation at constitutive heterochromatin

Schotta, G., Lachner, M., Sarma, K., Ebert, A., Sengupta, R., Reuter, G., Reinberg, D., & Jenuwein, T. (2004) · Genes & Development · doi:10.1101/gad.300704 · Cited by 1,031

EZH1 mediates methylation on histone H3 lysine 27 and complements EZH2 in maintaining stem cell identity and executing pluripotency

Shen, X., Liu, Y., Hsu, Y.-J., Fujiwara, Y., Kim, J., Mao, X., Yuan, G.-C., & Orkin, S. H. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.10.016 · Cited by 1,021

Genome-wide Identification of Polycomb-Associated RNAs by RIP-seq

Zhao, J. C., Ohsumi, T. K., Kung, J. T., Ogawa, Y., Grau, D., Sarma, K., Song, J. J., Kingston, R. E., Borowsky, M. L., & Lee, J. T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.12.011 · Cited by 1,008

Understanding the language of Lys36 methylation at histone H3

Wagner, E. J., & Carpenter, P. B. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3274 · Cited by 974

Ezh1 and Ezh2 Maintain Repressive Chromatin through Different Mechanisms

Margueron, R., Li, G., Sarma, K., Blais, A., Zavadil, J., Woodcock, C. L. F., Dynlacht, B. D., & Reinberg, D. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.11.004 · Cited by 930

The Polycomb-Group GeneEzh2 Is Required for Early Mouse Development

O’Carroll, D., Erhardt, S., Pagani, M., Barton, S. C., Surani, M. A., & Jenuwein, T. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.13.4330-4336.2001 · Cited by 908

EZH2 Oncogenic Activity in Castration-Resistant Prostate Cancer Cells Is Polycomb-Independent

Xu, K., Wu, Z. J., Groner, A. C., He, H. H., Cai, C., Lis, R. T., Wu, X., Stack, E. C., Loda, M. F., Liu, T., et al. (2012) · Science · doi:10.1126/science.1227604 · Cited by 901

Altered Hox expression and segmental identity in Mll-mutant mice

Yu, B., Hess, J. L., Horning, S. E., Brown, G. A. J., & Korsmeyer, S. J. (1995) · Nature · doi:10.1038/378505a0 · Cited by 872

Histone methyltransferases G9a and GLP form heteromeric complexes and are both crucial for methylation of euchromatin at H3-K9Preprint

Tachibana, M., Ueda, J., Fukuda, M., Takeda, N., Ohta, T., Iwanari, H., Sakihama, T., Kodama, T., Hamakubo, T., & Shinkai, Y. (2005) · Genes & Development · doi:10.1101/gad.1284005 · Cited by 868

Regulation of p53 activity through lysine methylation

Chuikov, S., Kurash, J. K., Wilson, J. R., Xiao, B., Justin, N., Ivanov, G. S., McKinney, K. M., Tempst, P., Prives, C. L., Gamblin, S. J., et al. (2004) · Nature · doi:10.1038/nature03117 · Cited by 846

Phosphorylation of EZH2 Activates STAT3 Signaling via STAT3 Methylation and Promotes Tumorigenicity of Glioblastoma Stem-like Cells

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

The lysine demethylase LSD1 (KDM1) is required for maintenance of global DNA methylation

Wang, J., Hevi, S., Kurash, J. K., Lei, H., Gay, F., Bajko, J., Su, H., Sun, W., Chang, H., Xu, G., et al. (2008) · Nature Genetics · doi:10.1038/ng.268 · Cited by 827

Distinct epigenomic landscapes of pluripotent and lineage-committed human cells

Hawkins, R. D., Hon, G. C., Lee, L. K., Ngo, Q., Lister, R., Pelizzola, M., Edsall, L. E., Kuan, S., Luu, Y., Klugman, S., et al. (2010) · Cell stem cell · doi:10.1016/j.stem.2010.03.018 · Cited by 806

Histone Methylation by PRC2 Is Inhibited by Active Chromatin Marks

Schmitges, F. W., Prusty, A. B., Faty, M., Stützer, A., Lingaraju, G. M., Aiwazian, J., Sack, R., Heß, D., Li, L., Zhou, S., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.025 · Cited by 772

SMYD3 encodes a histone methyltransferase involved in the proliferation of cancer cells

Hamamoto, R., Furukawa, Y., Morita, M., Iimura, Y., Pittella-Silva, F., Li, M., Yagyu, R., & Nakamura, Y. (2004) · Nature Cell Biology · doi:10.1038/ncb1151 · Cited by 752

The Polycomb Group Protein Suz12 Is Required for Embryonic Stem Cell Differentiation

Pasini, D., Bracken, A. P., Hansen, J. B., Capillo, M., & Helin, K. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01432-06 · Cited by 714

Central role of Drosophila SU(VAR)3–9 in histone H3‐K9 methylation and heterochromatic gene silencing

Schotta, G., Ebert, A., Krauss, V., Fischer, A., Hoffmann, J., Rea, S., Jenuwein, T., Dorn, R., & Reuter, G. (2002) · The EMBO Journal · doi:10.1093/emboj/21.5.1121 · Cited by 714

Differential chromatin marking of introns and expressed exons by H3K36me3

Kolasinska-Zwierz, P., Down, T. A., Latorre, I. J., Liu, T., Liu, X. S., & Ahringer, J. (2009) · Nature Genetics · doi:10.1038/ng.322 · Cited by 699

Methylation of Histone H3 by Set2 in Saccharomyces cerevisiae Is Linked to Transcriptional Elongation by RNA Polymerase II

Krogan, N. J., Kim, M., Tong, A. H. Y., Golshani, A., Cagney, G., Canadien, V., Richards, D. P., Beattie, B. K., Emili, A., Boone, C. M., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.12.4207-4218.2003 · Cited by 699

Essential Role of the Histone Methyltransferase G9a in Cocaine-Induced Plasticity

Maze, I., Covington, H. E., Dietz, D. M., LaPlant, Q., Renthal, W., Russo, S. J., Mechanic, M., Mouzon, E., Neve, R. L., Haggarty, S. J., et al. (2010) · Science · doi:10.1126/science.1179438 · Cited by 665

Chromatin Signatures in Multipotent Human Hematopoietic Stem Cells Indicate the Fate of Bivalent Genes during Differentiation

Cui, K., Zang, C., Roh, T., Schones, D. E., Childs, R. W., Peng, W., & Zhao, K. (2009) · Cell stem cell · doi:10.1016/j.stem.2008.11.011 · Cited by 646

Chromatin organization marks exon-intron structure

Schwartz, S., Meshorer, E., & Ast, G. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1659 · Cited by 638

Large histone H3 lysine 9 dimethylated chromatin blocks distinguish differentiated from embryonic stem cells

Wen, B., Wu, H., Shinkai, Y., Irizarry, R. A., & Feinberg, A. P. (2009) · Nature Genetics · doi:10.1038/ng.297 · Cited by 634

Repression of p53 activity by Smyd2-mediated methylation

Huang, J. L., Perez-Burgos, L., Placek, B. J., Sengupta, R., Richter, M., Dorsey, J. A., Kubicek, S., Opravil, S., Jenuwein, T., & Berger, S. L. (2006) · Nature · doi:10.1038/nature05287 · Cited by 626

CpG islands influence chromatin structure via the CpG-binding protein Cfp1

Thomson, J. P., Skene, P. J., Selfridge, J., Clouaire, T., Guy, J., Webb, S., Kerr, A. R. W., Deaton, A., Andrews, R., James, K. D., et al. (2010) · Nature · doi:10.1038/nature08924 · Cited by 625

CBP-mediated acetylation of histone H3 lysine 27 antagonizesDrosophilaPolycomb silencing

Tie, F., Banerjee, R., Stratton, C. A., Prasad-Sinha, J., Stepanik, V. A., Zlobin, A., Dı́az, M. O., Scacheri, P. C., & Harte, P. J. (2009) · Development · doi:10.1242/dev.037127 · Cited by 612

ncRNA- and Pc2 methylation-dependent gene relocation between nuclear structures mediates gene activation programs

Yang, L., Lin, C., Liu, W., Zhang, J., Ohgi, K. A., Grinstein, J. D., Dorrestein, P. C., & Rosenfeld, M. G. (2011) · Cell · doi:10.1016/j.cell.2011.08.054 · Cited by 612

Step-wise methylation of histone H3K9 positions heterochromatin at the nuclear periphery

Towbin, B. D., González-Aguilera, C., Sack, R., Gaidatzis, D., Kalck, V., Meister, P., Askjaer, P., & Gasser, S. M. (2012) · Cell · doi:10.1016/j.cell.2012.06.051 · Cited by 597

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 574

H3K9 methyltransferase G9a and the related molecule GLPPreprint

Shinkai, Y., & Tachibana, M. (2011) · Genes & Development · doi:10.1101/gad.2027411 · Cited by 571

Set2 Is a Nucleosomal Histone H3-Selective Methyltransferase That Mediates Transcriptional Repression

Strahl, B. D., Grant, P. A., Briggs, S. D., Sun, Z., Bone, J. R., Caldwell, J., Mollah, S., Cook, R. G., Shabanowitz, J., Hunt, D. F., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.5.1298-1306.2002 · Cited by 564

Akt-Mediated Phosphorylation of EZH2 Suppresses Methylation of Lysine 27 in Histone H3

Cha, T., Zhou, B. P., Xia, W., Wu, Y., Yang, C., Chen, C., Ping, B., Otte, A. P., & Hung, M. (2005) · Science · doi:10.1126/science.1118947 · Cited by 563

Epigenetic regulation of telomere length in mammalian cells by the Suv39h1 and Suv39h2 histone methyltransferases

García‐Cao, M., O’Sullivan, R. J., Peters, A. H. F. M., Jenuwein, T., & Blasco, M. A. (2003) · Nature Genetics · doi:10.1038/ng1278 · Cited by 557

Dynamic histone H3 methylation during gene induction: HYPB/Setd2 mediates all H3K36 trimethylation

Edmunds, J. W., Mahadevan, L. C., & Clayton, A. L. (2008) · The EMBO Journal · doi:10.1038/sj.emboj.7601967 · Cited by 547

The Brd4 Extraterminal Domain Confers Transcription Activation Independent of pTEFb by Recruiting Multiple Proteins, Including NSD3

Rahman, S., Sowa, M. E., Ottinger, M., Smith, J. A., Shi, Y., Harper, J. W., & Howley, P. M. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01341-10 · Cited by 532

Bre1, an E3 Ubiquitin Ligase Required for Recruitment and Substrate Selection of Rad6 at a Promoter

Wood, A., Krogan, N. J., Dover, J., Schneider, J., Heidt, J. W., Boateng, M. A., Dean, K., Golshani, A., Zhang, Y., Greenblatt, J., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(02)00802-x · Cited by 530

Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive

Guccione, E., Bassi, C., Casadio, F., Martinato, F., Cesaroni, M., Schuchlautz, H., Lüscher, B., & Amati, B. B. (2007) · Nature · doi:10.1038/nature06166 · Cited by 495

Asymmetrically Modified Nucleosomes

Voigt, P., LeRoy, G., Drury, W. J., Zee, B. M., Son, J., Beck, D. B., Young, N. L., Garcia, B. A., & Reinberg, D. (2012) · Cell · doi:10.1016/j.cell.2012.09.002 · Cited by 488

Trithorax group proteins: switching genes on and keeping them active

Schuettengruber, B., Martinez, A., Iovino, N., & Cavalli, G. (2011) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3230 · Cited by 478

A chromatin-wide transition to H4K20 monomethylation impairs genome integrity and programmed DNA rearrangements in the mousePreprint

Schotta, G., Sengupta, R., Kubicek, S., Malin, S., Kauer, M., Callén, E., Celeste, A., Pagani, M., Opravil, S., Rosa-Velázquez, I. A. D. L., et al. (2008) · Genes & Development · doi:10.1101/gad.476008 · Cited by 478

Different Ezh2-Containing Complexes Target Methylation of Histone H1 or Nucleosomal Histone H3

Kuzmichev, A., Jenuwein, T., Tempst, P., & Reinberg, D. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00185-6 · Cited by 467

Histone Crosstalk between H2B Monoubiquitination and H3 Methylation Mediated by COMPASS

Lee, J., Shukla, A., Schneider, J., Swanson, S. K., Washburn, M. P., Florens, L. A., Bhaumik, S. R., & Shilatifard, A. (2007) · Cell · doi:10.1016/j.cell.2007.09.046 · Cited by 465

Modulation of p53 Function by SET8-Mediated Methylation at Lysine 382

Shi, X., Kachirskaia, I., Yamaguchi, H., West, L. E., Wen, H., Wang, E. W., Dutta, S. M., Appella, E., & Gozani, O. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.012 · Cited by 463

NSD2 Links Dimethylation of Histone H3 at Lysine 36 to Oncogenic Programming

Kuo, A. J., Cheung, P., Chen, K., Zee, B. M., Kioi, M., Lauring, J. D., Xi, Y., Park, B. H., Shi, X., Garcia, B. A., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.042 · Cited by 458

Polycomb/Trithorax response elements and epigenetic memory of cell identity

Ringrose, L., & Paro, R. (2006) · Development · doi:10.1242/dev.02723 · Cited by 458

SIRT1 regulates the histone methyl-transferase SUV39H1 during heterochromatin formation.

Vaquero, A., Scher, M., Erdjument-Bromage, H., Tempst, P., Serrano, L., & Reinberg, D. (2007) · Nature · doi:10.1038/nature06268 · Cited by 439

PHD Domain-Mediated E3 Ligase Activity Directs Intramolecular Sumoylation of an Adjacent Bromodomain Required for Gene Silencing

Ivanov, A. V., Peng, H., Yurchenko, V., Yap, K. L., Negorev, D. G., Schultz, D. C., Psulkowski, E., Fredericks, W. J., White, D. E., Maul, G. G., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.11.012 · Cited by 432

MMSET regulates histone H4K20 methylation and 53BP1 accumulation at DNA damage sites

Pei, H., Zhang, L. M., Luo, K., Qin, Y., Chesi, M., Fei, Y. F., Bergsagel, P. L., Wang, L., You, Z., & Lou, Z. (2011) · Nature · doi:10.1038/nature09658 · Cited by 425

G9a and Glp Methylate Lysine 373 in the Tumor Suppressor p53

Huang, J. L., Dorsey, J. A., Chuikov, S., Perez-Burgos, L., Zhang, X., Jenuwein, T., Reinberg, D., & Berger, S. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.062588 · Cited by 417

Characterization of an antagonistic switch between histone H3 lysine 27 methylation and acetylation in the transcriptional regulation of Polycomb group target genes

Pasini, D., Malatesta, M., Jung, H. R., Walfridsson, J., Willer, A., Olsson, L., Skotte, J., Wutz, A., Porse, B. T., Jensen, O. N., et al. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq244 · Cited by 413

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

The Paf1 Complex Is Essential for Histone Monoubiquitination by the Rad6-Bre1 Complex, Which Signals for Histone Methylation by COMPASS and Dot1p

Wood, A., Schneider, J., Dover, J., Johnston, M., & Shilatifard, A. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c300269200 · Cited by 404

Histone H3 lysine 4 trimethylation marks meiotic recombination initiation sites

Borde, V., Robine, N., Lin, W., Bonfils, S., Géli, V., & Nicolas, A. G. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.257 · Cited by 403

A Long ncRNA Links Copy Number Variation to a Polycomb/Trithorax Epigenetic Switch in FSHD Muscular Dystrophy

Cabianca, D. S., Casà, V., Bodega, B., Xynos, A., Ginelli, E., Tanaka, Y., & Gabellini, D. (2012) · Cell · doi:10.1016/j.cell.2012.03.035 · Cited by 402

Histone H3-K9 Methyltransferase ESET Is Essential for Early Development

Dodge, J. E., Kang, Y., Beppu, H., Lei, H., & Li, E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.6.2478-2486.2004 · Cited by 400

Phosphorylation of the PRC2 component Ezh2 is cell cycle-regulated and up-regulates its binding to ncRNAPreprint

Kaneko, S., Li, G., Son, J., Xu, C., Margueron, R., Neubert, T. A., & Reinberg, D. (2010) · Genes & Development · doi:10.1101/gad.1983810 · Cited by 399

TNF/p38α/Polycomb Signaling to Pax7 Locus in Satellite Cells Links Inflammation to the Epigenetic Control of Muscle Regeneration

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

Biased chromatin signatures around polyadenylation sites and exons

Nielsen, C. B., Padgett, R. A., Spies, N., & Burge, C. B. (2009) · DSpace@MIT (Massachusetts Institute of Technology) · Cited by 390

CDK1-dependent phosphorylation of EZH2 suppresses methylation of H3K27 and promotes osteogenic differentiation of human mesenchymal stem cells

Wei, Y., Chen, Y.-H., Li, L., Lang, J., Yeh, S., Shi, B., Yang, C., Yang, J.-Y., Lin, C.-Y., Lai, C., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2139 · Cited by 388

Enhancer-associated H3K4 monomethylation by Trithorax-related, the Drosophila homolog of mammalian Mll3/Mll4

Herz, H.-M., Mohan, M., Garruss, A. S., Liang, K., Takahashi, Y.-H., Mickey, K., Voets, O., Verrijzer, C. P., & Shilatifard, A. (2012) · Genes & Development · doi:10.1101/gad.201327.112 · Cited by 388

Short RNAs Are Transcribed from Repressed Polycomb Target Genes and Interact with Polycomb Repressive Complex-2

Kanhere, A., Viiri, K. M., Araújo, C. C., Rasaiyaah, J., Bouwman, R. D., Whyte, W. A., Pereira, C., Brookes, E., Walker, K., Bell, G. W., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.03.019 · Cited by 386

Biased Chromatin Signatures around Polyadenylation Sites and Exons

Spies, N., Nielsen, C. B., Padgett, R. A., & Burge, C. B. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.008 · Cited by 385

A histone H3 lysine 36 trimethyltransferase links Nkx2-5 to Wolf–Hirschhorn syndrome

Nimura, K., Ura, K., Shiratori, H., Ikawa, M., Okabe, M., Schwartz, R. J., & Kaneda, Y. (2009) · Nature · doi:10.1038/nature08086 · Cited by 379

Lysine Methylation Regulates E2F1-Induced Cell Death

Kontaki, H., & Talianidis, I. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.006 · Cited by 374

Arginine methylation at histone H3R2 controls deposition of H3K4 trimethylation

Kirmizis, A., Santos-Rosa, H., Penkett, C. J., Singer, M. A., Vermeulen, M., Mann, M., Bähler, J., Green, R. D., & Kouzarides, T. (2007) · Nature · doi:10.1038/nature06160 · Cited by 367

Polycomb Group Protein Ezh2 Controls Actin Polymerization and Cell Signaling

Su, I.-H., Dobenecker, M.-W., Dickinson, E., Oser, M., Basavaraj, A., Marqueron, R., Viale, A., Reinberg, D., Wülfing, C., & Tarakhovsky, A. (2005) · Cell · doi:10.1016/j.cell.2005.02.029 · Cited by 365

Global Analysis of H3K4 Methylation Defines MLL Family Member Targets and Points to a Role for MLL1-Mediated H3K4 Methylation in the Regulation of Transcriptional Initiation by RNA Polymerase II

Wang, P., Lin, C., Smith, E. R., Guo, H. W., Sanderson, B. W., Wu, M., Gogol, M., Alexander, T. B., Seidel, C. W., Wiedemann, L. M., et al. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00924-09 · Cited by 360

Mir-214-Dependent Regulation of the Polycomb Protein Ezh2 in Skeletal Muscle and Embryonic Stem Cells

Juan, A. H., Kumar, R., Marx, J. G., Young, R. A., & Sartorelli, V. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.08.008 · Cited by 359

Regulated recruitment of HP1 to a euchromatic gene induces mitotically heritable, epigenetic gene silencing: a mammalian cell culture model of gene variegationPreprint

Ayyanathan, K., Lechner, M. S., Bell, P., Maul, G. G., Schultz, D., Yamada, Y., Tanaka, K., Torigoe, K., & Rauscher, F. J. (2003) · Genes & Development · doi:10.1101/gad.1102803 · Cited by 356

mAM Facilitates Conversion by ESET of Dimethyl to Trimethyl Lysine 9 of Histone H3 to Cause Transcriptional Repression

Wang, H., An, W., Cao, R., Li, X., Erdjument‐Bromage, H., Chatton, B., Tempst, P., Roeder, R. G., & Zhang, Y. (2003) · Molecular Cell · doi:10.1016/j.molcel.2003.08.007 · Cited by 355

Integration of Estrogen and Wnt Signaling Circuits by the Polycomb Group Protein EZH2 in Breast Cancer Cells

Shi, B., Liang, J., Yang, X., Wang, Y., Zhao, Y., Wu, H., Sun, L., Zhang, Y., Chen, Y., Li, R., et al. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00162-07 · Cited by 355

Role of the Histone H3 Lysine 4 Methyltransferase, SET7/9, in the Regulation of NF-κB-dependent Inflammatory Genes

Li, Y., Reddy, M. A., Miao, F., Shanmugam, N., Yee, J.-K., Hawkins, D., Ren, B., & Natarajan, R. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802800200 · Cited by 353

Protein lysine methyltransferase G9a acts on non-histone targets

Rathert, P., Dhayalan, A., Murakami, M., Zhang, X., Tamas, R., Jurkowska, R., Komatsu, Y., Shinkai, Y., Cheng, X., & Jeltsch, A. (2008) · Nature Chemical Biology · doi:10.1038/nchembio.88 · Cited by 347

Reversible methylation of promoter-bound STAT3 by histone-modifying enzymes

Yang, J., Huang, J., Dasgupta, M., Sears, N., Miyagi, M., Wang, B., Chance, M. R., Chen, X., Du, Y., Wang, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016147107 · Cited by 340

Prdm3 and Prdm16 are H3K9me1 Methyltransferases Required for Mammalian Heterochromatin Integrity

Pinheiro, I., Margueron, R., Shukeir, N., Eisold, M., Fritzsch, C., Richter, F. M., Mittler, G., Genoud, C., Goyama, S., Kurokawa, M., et al. (2012) · Cell · doi:10.1016/j.cell.2012.06.048 · Cited by 340

A Region of the Human HOXD Cluster that Confers Polycomb-Group Responsiveness

Woo, C. J., Kharchenko, P. V., Daheron, L. M., Park, P. J., & Kingston, R. E. (2010) · Cell · doi:10.1016/j.cell.2009.12.022 · Cited by 333

Regulation of DNMT1 stability through SET7-mediated lysine methylation in mammalian cells

Estève, P., Chin, H. G., Benner, J. S., Feehery, G. R., Samaranayake, M., Horwitz, G. A., Jacobsen, S. E., & Pradhan, S. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810362106 · Cited by 328

Molecular Regulation of H3K4 Trimethylation by Wdr82, a Component of Human Set1/COMPASS

Wu, M., Wang, P. F., Lee, J. S., Martin‐Brown, S., Florens, L. A., Washburn, M. P., & Shilatifard, A. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00976-08 · Cited by 324

A Subset of the Histone H3 Lysine 9 Methyltransferases Suv39h1, G9a, GLP, and SETDB1 Participate in a Multimeric Complex

Fritsch, L., Robin, P., Mathieu, J. R. R., Souidi, M., Hinaux, H., Rougeulle, C., Harel-Bellan, A., Ameyar-Zazoua, M., & Ait-Si-Ali, S. (2010) · Molecular Cell · doi:10.1016/j.molcel.2009.12.017 · Cited by 321

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

Set2 methylation of histone H3 lysine 36 suppresses histone exchange on transcribed genes

Venkatesh, S., Smolle, M. M., Li, H., Gogol, M., Saint, M., Kumar, S. A., Natarajan, K., & Workman, J. L. (2012) · Nature · doi:10.1038/nature11326 · Cited by 319

Monomethylation of Histone H4-Lysine 20 Is Involved in Chromosome Structure and Stability and Is Essential for Mouse Development

Oda, H., Okamoto, I., Murphy, N., Chu, J., Price, S. M., Shen, M. M., Torres-Padilla, M. E., Heard, É., & Reinberg, D. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01768-08 · Cited by 319

Control of Cognition and Adaptive Behavior by the GLP/G9a Epigenetic Suppressor Complex

Schaefer, A., Sampath, S. C., Intrator, A., Min, A., Gertler, T. S., Surmeier, D. J., Tarakhovsky, A., & Greengard, P. (2009) · Neuron · doi:10.1016/j.neuron.2009.11.019 · Cited by 317

ChIP-seq analysis reveals distinct H3K27me3 profiles that correlate with transcriptional activity

Young, M. D., Willson, T. A., Wakefield, M. J., Trounson, E., Hilton, D. J., Blewitt, M. E., Oshlack, A., & Majewski, I. J. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr416 · Cited by 312

Molecular Regulation of Histone H3 Trimethylation by COMPASS and the Regulation of Gene Expression

Schneider, J., Wood, A., Lee, J., Schuster, R. M., Dueker, J., Maguire, C., Swanson, S. K., Florens, L. A., Washburn, M. P., & Shilatifard, A. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.07.024 · Cited by 311

Combined Action of PHD and Chromo Domains Directs the Rpd3S HDAC to Transcribed Chromatin

Li, B., Gogol, M., Carey, M., Lee, D., Seidel, C. W., & Workman, J. L. (2007) · Science · doi:10.1126/science.1139004 · Cited by 309

PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylationPreprint

Hyllus, D. M., Stein, C., Schnabel, K., Schiltz, E., Imhof, A., Dou, Y., Hsieh, J. J.-D., & Bauer, U. (2007) · Genes & Development · doi:10.1101/gad.447007 · Cited by 308

Ten different Polycomb group genes are required for spatial control of the abdA and AbdB homeotic products

Simon, J. A., Chiang, A., & Bender, W. W. (1992) · Development · doi:10.1242/dev.114.2.493 · Cited by 304

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

Dense Chromatin Activates Polycomb Repressive Complex 2 to Regulate H3 Lysine 27 Methylation

Yuan, W., Wu, T., Fu, H., Dai, C., Wu, H., Liu, N., Li, X., Xu, M., Zhang, Z., Niu, T., et al. (2012) · Science · doi:10.1126/science.1225237 · Cited by 304

Pcl‐PRC2 is needed to generate high levels of H3‐K27 trimethylation at Polycomb target genes

Nekrasov, M., Klymenko, T., Fraterman, S., Papp, B., Oktaba, K., Köcher, T., Cohen, A., Stunnenberg, H. G., Wilm, M. S., & Müller, J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601837 · Cited by 303

Ezh2 Requires PHF1 To Efficiently Catalyze H3 Lysine 27 Trimethylation In Vivo

Sarma, K., Margueron, R., Ivanov, A. V., Pirrotta, V., & Reinberg, D. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02017-07 · Cited by 303

Methylation of histone H3 lysine 36 enhances DNA repair by nonhomologous end-joining

Fnu, S., Williamson, E. A., Haro, L. P. D., Brenneman, M. A., Wray, J. W., Shaheen, M. F., Radhakrishnan, K., Lee, S., Nickoloff, J. A., & Hromas, R. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1013571108 · Cited by 300

The Target of the NSD Family of Histone Lysine Methyltransferases Depends on the Nature of the Substrate

Li, Y., Trojer, P., Xu, C., Cheung, P., Kuo, A. J., Drury, W. J., Qiao, Q., Neubert, T. A., Xu, R.-M., Gozani, O., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.034462 · Cited by 300

Multiple epigenetic maintenance factors implicated by the loss of Mll2 in mouse development

Glaser, S. P., Schaft, J., Lubitz, S., Vintersten, K., van der Hoeven, F., Tufteland, K. R., Aasland, R., Anastassiadis, K., Ang, S., & Stewart, A. F. (2006) · Development · doi:10.1242/dev.02302 · Cited by 294

Cyclin-dependent kinases regulate epigenetic gene silencing through phosphorylation of EZH2

Chen, D., Bohrer, L. R., Rai, A. N., Pan, Y., Gan, L., Zhou, X., Bagchi, A., Simon, J. A., & Huang, H. (2010) · Nature Cell Biology · doi:10.1038/ncb2116 · Cited by 292

Cfp1 integrates both CpG content and gene activity for accurate H3K4me3 deposition in embryonic stem cellsPreprint

Clouaire, T., Webb, S., Skene, P., Illingworth, R. S., Kerr, A. R. W., Andrews, R., Lee, J., Skalnik, D. G., & Bird, A. P. (2012) · Genes & Development · doi:10.1101/gad.194209.112 · Cited by 292

Su(var) genes regulate the balance between euchromatin and heterochromatin in DrosophilaPreprint

Ebert, A., Schotta, G., Lein, S., Kubicek, S., Krauß, V., Jenuwein, T., & Reuter, G. (2004) · Genes & Development · doi:10.1101/gad.323004 · Cited by 292

Regulation of Estrogen Receptor α by the SET7 Lysine Methyltransferase

Subramanian, K., Jia, D., Kapoor-Vazirani, P., Powell, D. R., Collins, R. E., Sharma, D., Peng, J., Cheng, X., & Vertino, P. M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.03.022 · Cited by 291

A Role for Repressive Histone Methylation in Cocaine-Induced Vulnerability to Stress

Covington, H. E., Maze, I., Sun, H., Bomze, H. M., DeMaio, K. D., Wu, E. Y., Dietz, D. M., Lobo, M. K., Ghose, S., Mouzon, E., et al. (2011) · Neuron · doi:10.1016/j.neuron.2011.06.007 · Cited by 289

The histone H4 Lys 20 methyltransferase PR-Set7 regulates replication origins in mammalian cells

Tardat, M., Brustel, J., Kirsh, O., Lefevbre, C., Callanan, M. B., Sardet, C., & Julien, E. (2010) · Nature Cell Biology · doi:10.1038/ncb2113 · Cited by 289

The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules

Collins, R. E., Northrop, J. P., Horton, J. R., Lee, D. Y., Zhang, X., Stallcup, M. R., & Cheng, X. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1384 · Cited by 288

Regulation of NF-κB by NSD1/FBXL11-dependent reversible lysine methylation of p65

Lu, T., Jackson, M. W., Wang, B., Yang, M., Chance, M. R., Miyagi, M., Gudkov, A. V., & Stark, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912493107 · Cited by 286

CRL4Cdt2 Regulates Cell Proliferation and Histone Gene Expression by Targeting PR-Set7/Set8 for Degradation

Abbas, T., Shibata, E., Park, J.-H., Jha, S., Karnani, N., & Dutta, A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.014 · Cited by 280

SET8 promotes epithelial–mesenchymal transition and confers TWIST dual transcriptional activities

Yang, F., Sun, L., Li, Q., Han, X., Lei, L., Zhang, H., & Shang, Y. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.364 · Cited by 275

Polycomb response elements and targeting of Polycomb group proteins in Drosophila

Müller, J., & Kassis, J. A. (2006) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2006.08.005 · Cited by 273

MLL2 Is Required in Oocytes for Bulk Histone 3 Lysine 4 Trimethylation and Transcriptional Silencing

Andreu‐Vieyra, C., Chen, R., Agno, J. E., Glaser, S. P., Anastassiadis, K., Stewart, A. F., & Matzuk, M. M. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000453 · Cited by 272

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

Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb activity

Ballaré, C., Lange, M., Lapinaitė, A., Martín, G. M., Morey, L., Pascual, G., Liefke, R., Simon, B., Shi, Y., Gozani, O., et al. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2434 · Cited by 268

Lysine methylation of the NF-κB subunit RelA by SETD6 couples activity of the histone methyltransferase GLP at chromatin to tonic repression of NF-κB signaling

Levy, D., Kuo, A. J., Chang, Y., Schaefer, U., Kitson, C., Cheung, P., Espejo, A. B., Zee, B. M., Liu, C. L., Tangsombatvisit, S., et al. (2010) · Nature Immunology · doi:10.1038/ni.1968 · Cited by 266

The prdm family: expanding roles in stem cells and development

Hohenauer, T., & Moore, A. W. (2012) · Development · doi:10.1242/dev.070110 · Cited by 265

Human LSD2/KDM1b/AOF1 Regulates Gene Transcription by Modulating Intragenic H3K4me2 Methylation

Fang, R., Barbera, A. J., Xu, Y., Rutenberg, M. S., Leonor, T., Bi, Q., Lan, F., Mei, P., Yuan, G., Lian, C. G., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.008 · Cited by 264

Molecular architecture of human polycomb repressive complex 2

Ciferri, C., Lander, G. C., Maiolica, A., Herzog, F., Aebersold, R. H., & Nogales, E. (2012) · eLife · doi:10.7554/elife.00005 · Cited by 263

Gene-Specific Modulation of TAF10 Function by SET9-Mediated Methylation

Kouskouti, A., Scheer, E., Staub, A., Tora, L., & Talianidis, I. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00182-0 · Cited by 255

2-D Structure of the A Region of Xist RNA and Its Implication for PRC2 Association

Maenner, S., Blaud, M., Fouillen, L., Savoye, A., Marchand, V., Dubois, A., Cianférani, S., DORSSELAER, A. V., Clerc, P., Avner, P. R., et al. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000276 · Cited by 254

Regulation of the Histone H4 Monomethylase PR-Set7 by CRL4Cdt2-Mediated PCNA-Dependent Degradation during DNA Damage

Oda, H., Hübner, M. R., Beck, D. B., Vermeulen, M., Hurwitz, J., Spector, D. L., & Reinberg, D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.011 · Cited by 253

A Vertebrate Polycomb Response Element Governs Segmentation of the Posterior Hindbrain

Sing, A., Pannell, D., Karaiskakis, A., Sturgeon, K., Djabali, M., Ellis, J., Lipshitz, H. D., & Cordes, S. P. (2009) · Cell · doi:10.1016/j.cell.2009.08.020 · Cited by 250

Methylation of a Histone Mimic within the Histone Methyltransferase G9a Regulates Protein Complex Assembly

Sampath, S. C., Marazzi, I., Yap, K. L., Sampath, S. C., Krutchinsky, A. N., Mecklenbräuker, I., Viale, A. J., Rudensky, E., Zhou, M., Chait, B. T., et al. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.026 · Cited by 249

MLL-AF9-Induced Leukemogenesis Requires Coexpression of the Wild-Type Mll Allele

Thiel, A. T., Blessington, P., Zou, T., Feather, D., Wu, X., Yan, J., Zhang, H., Liu, Z., Ernst, P., Koretzky, G. A., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.12.034 · Cited by 249

Splicing enhances recruitment of methyltransferase HYPB/Setd2 and methylation of histone H3 Lys36

de Almeida, S. F., Grosso, A. R., Koch, F., Fenouil, R., Carvalho, S., Andrade, J., Levezinho, H. I. D. S. P., Gut, M., Eick, D., Gut, I. G., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2123 · Cited by 247

The HP1α–CAF1–SetDB1‐containing complex provides H3K9me1 for Suv39‐mediated K9me3 in pericentric heterochromatin

Loyola, A., Tagami, H., Bonaldi, T., Roche, D. M. J., Quivy, J., Imhof, A., Nakatani, Y., Dent, S., & Almouzni, G. (2009) · EMBO Reports · doi:10.1038/embor.2009.90 · Cited by 243

Regulation of NF-κB activity through lysine monomethylation of p65

Ea, C.-K., & Baltimore, D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0910439106 · Cited by 239

Mediator Links Epigenetic Silencing of Neuronal Gene Expression with X-Linked Mental Retardation

Ding, N., Zhou, H., Estève, P., Chin, H. G., Kim, S., Xu, X., Joseph, S., Friez, M. J., Schwartz, C. E., Pradhan, S., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.023 · Cited by 238

Multiple Interactions Recruit MLL1 and MLL1 Fusion Proteins to the HOXA9 Locus in Leukemogenesis

Milne, T. A., Kim, J., Wang, G. G., Stadler, S. C., Basrur, V., Whitcomb, S. J., Wang, Z., Ruthenburg, A. J., Elenitoba‐Johnson, K. S. J., Roeder, R. G., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.011 · Cited by 238

The COMPASS Family of H3K4 Methylases in Drosophila

Mohan, M., Herz, H., Smith, E. R., Zhang, Y., Jackson, J., Washburn, M. P., Florens, L. A., Eissenberg, J. C., & Shilatifard, A. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.06092-11 · Cited by 237

The PAF Complex Synergizes with MLL Fusion Proteins at HOX Loci to Promote Leukemogenesis

Muntean, A. G., Tan, J., Sitwala, K. V., Huang, Y., Bronstein, J. C., Connelly, J. A., Basrur, V., Elenitoba‐Johnson, K. S. J., & Hess, J. L. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.04.012 · Cited by 236

Structural Basis for the Requirement of Additional Factors for MLL1 SET Domain Activity and Recognition of Epigenetic Marks

Southall, S. M., Wong, P. S., Odho, Z., Roe, S. M., & Wilson, J. R. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.029 · Cited by 233

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 232

Spp1, a Member of the Set1 Complex, Promotes Meiotic DSB Formation in Promoters by Tethering Histone H3K4 Methylation Sites to Chromosome Axes

Sommermeyer, V., Béneut, C., Chaplais, E., Serrentino, M. E., & Borde, V. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.11.008 · Cited by 232

FGF-2 Regulates Cell Proliferation, Migration, and Angiogenesis through an NDY1/KDM2B-miR-101-EZH2 Pathway

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

Methylation of the Retinoblastoma Tumor Suppressor by SMYD2

Saddic, L., West, L. E., Aslanian, A., Yates, J. R., Rubin, S. M., Gozani, O., & Sage, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.137612 · Cited by 226

The histone methyltransferase SET8 is required for S-phase progression

Jørgensen, S., Elvers, I., Trelle, M. B., Menzel, T., Eskildsen, M., Jensen, O. N., Helleday, T., Helin, K., & Sørensen, C. S. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200706150 · Cited by 225

Genetic analysis of the enhancer of zeste locus and its role in gene regulation in Drosophila melanogaster.

Jones, R. S., & Gelbart, W. M. (1990) · Genetics · doi:10.1093/genetics/126.1.185 · Cited by 225

Structural and functional analysis of SET8, a histone H4 Lys-20 methyltransferasePreprint

Couture, J., Collazo, E., Brunzelle, J. S., & Trievel, R. C. (2005) · Genes & Development · doi:10.1101/gad.1318405 · Cited by 222

A methylation and phosphorylation switch between an adjacent lysine and serine determines human DNMT1 stability

Estève, P., Chang, Y., Samaranayake, M., Upadhyay, A. K., Horton, J. R., Feehery, G. R., Cheng, X., & Pradhan, S. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1939 · Cited by 220

MSL Complex Is Attracted to Genes Marked by H3K36 Trimethylation Using a Sequence-Independent Mechanism

Larschan, E., Alekseyenko, A. A., Gorchakov, A. A., Peng, S., Li, B., Yang, P. K., Workman, J. L., Park, P. J., & Kuroda, M. I. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.08.011 · Cited by 220

Methylation of p53 by Set7/9 Mediates p53 Acetylation and Activity In Vivo

Kurash, J. K., Lei, H., Shen, Q. “., Marston, W. L., Granda, B. W., Fan, H. X., Wall, D., Li, E., & Gaudet, F. (2008) · Molecular Cell · doi:10.1016/j.molcel.2007.12.025 · Cited by 219

Negative regulation of NF‐κB action by Set9‐mediated lysine methylation of the RelA subunit

Yang, X., Huang, B., Li, M., Lamb, A., Kelleher, N. L., & Chen, L. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.55 · Cited by 218

Histone Lysine Methyltransferase SETD8 Promotes Carcinogenesis by Deregulating PCNA Expression

Takawa, M., Cho, H., Hayami, S., Toyokawa, G., Kogure, M., Yamane, Y., Iwai, Y., Maejima, K., Ueda, K., Masuda, A., et al. (2012) · Cancer Research · doi:10.1158/0008-5472.can-11-3701 · Cited by 217

CRL4Cdt2-Mediated Destruction of the Histone Methyltransferase Set8 Prevents Premature Chromatin Compaction in S Phase

Centore, R. C., Havens, C. G., Manning, A. L., Li, J.-M., Flynn, R. L., Tse, A., Jin, J., Dyson, N. J., Walter, J. C., & Zou, L. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.015 · Cited by 216

Epigenetic inactivation of the Sotos overgrowth syndrome gene histone methyltransferase NSD1 in human neuroblastoma and glioma

Berdasco, M., Ropero, S., Setién, F., Fraga, M. F., Lapunzina, P. D., Losson, R., Alaminos, M., Cheung, N. V., Rahman, N., & Esteller, M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906831106 · Cited by 216

A tumor suppressive coactivator complex of p53 containing ASC-2 and histone H3-lysine-4 methyltransferase MLL3 or its paralogue MLL4

Lee, J., Kim, D., Lee, S., Yang, Q.-H., Lee, D. K., Lee, S., Roeder, R. G., & Lee, J. W. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902873106 · Cited by 215

AEBP2 as a potential targeting protein for Polycomb Repression Complex PRC2

Kim, H., Kang, K., & Kim, J. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkp149 · Cited by 214

Histone and DNA methylation defects at Hox genes in mice expressing a SET domain-truncated form of Mll

Terranova, R., Agherbi, H., Boned, A., Méresse, S., & Djabali, M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0507425103 · Cited by 214

The COMPASS Subunit Spp1 Links Histone Methylation to Initiation of Meiotic Recombination

Acquaviva, L., Székvölgyi, L., Dichtl, B., Dichtl, B. S., Saint-André, C. D. L. R., Nicolas, A. G., & Géli, V. (2012) · Science · doi:10.1126/science.1225739 · Cited by 213

Methylation-Acetylation Interplay Activates p53 in Response to DNA Damage

Ivanov, G. S., Ivanova, T., Kurash, J. K., Ivanov, A. V., Chuikov, S., Gizatullin, F., Herrera-Medina, E. M., Rauscher, F. J., Reinberg, D., & Barlev, N. A. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.00460-07 · Cited by 210

UHRF1 binds G9a and participates in p21 transcriptional regulation in mammalian cells

Kim, J. K., Estève, P., Jacobsen, S. E., & Pradhan, S. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn961 · Cited by 210

RB1 Methylation by SMYD2 Enhances Cell Cycle Progression through an Increase of RB1 Phosphorylation

Cho, H., Hayami, S., Toyokawa, G., Maejima, K., Yamane, Y., Suzuki, T., Dohmae, N., Kogure, M., Kang, D., Neal, D. E., et al. (2012) · Neoplasia · doi:10.1593/neo.12656 · Cited by 209

Dynamic Histone H1 Isotype 4 Methylation and Demethylation by Histone Lysine Methyltransferase G9a/KMT1C and the Jumonji Domain-containing JMJD2/KDM4 Proteins

Trojer, P., Zhang, J., Yonezawa, M., Schmidt, A., Zheng, H., Jenuwein, T., & Reinberg, D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807818200 · Cited by 208

Alternative Epigenetic Chromatin States of Polycomb Target Genes

Schwartz, Y. B., Kahn, T. G., Stenberg, P., Ohno, K., Bourgon, R., & Pirrotta, V. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000805 · Cited by 205

Drosophila Set1 is the major histone H3 lysine 4 trimethyltransferase with role in transcription

Ardehali, M. B., Mei, A., Zobeck, K. L., Caron, M. J., Lis, J. T., & Kusch, T. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.194 · Cited by 204

Epigenetic Regulation of Learning and Memory by Drosophila EHMT/G9a

Kramer, J. M., Kochinke, K., Oortveld, M. A. W., Marks, H., Kramer, D., de Jong, E. K., Asztalos, Z., Westwood, J. T., Stunnenberg, H. G., Sokolowski, M. B., et al. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000569 · Cited by 204

Polycomb-like 2 Associates with PRC2 and Regulates Transcriptional Networks during Mouse Embryonic Stem Cell Self-Renewal and Differentiation

Walker, E. M., Chang, W. Y., Hunkapiller, J., Cagney, G., Garcha, K., Torchia, J., Krogan, N. J., Reiter, J. F., & Stanford, W. L. (2010) · Cell stem cell · doi:10.1016/j.stem.2009.12.014 · Cited by 203

Structural Basis of Substrate Methylation and Inhibition of SMYD2

Ferguson, A. D., Larsen, N. A., Howard, T., Pollard, H., Green, I., Grande, C., Cheung, T., Garcia-Arenas, R., Cowen, S., Wu, J., et al. (2011) · Structure · doi:10.1016/j.str.2011.06.011 · Cited by 203

A Conserved Arginine-containing Motif Crucial for the Assembly and Enzymatic Activity of the Mixed Lineage Leukemia Protein-1 Core Complex

Patel, A. B., Vought, V. E., Dharmarajan, V., & Cosgrove, M. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806317200 · Cited by 202

PRDM proteins: important players in differentiation and disease

Fog, C. K., Galli, G. G., & Lund, A. H. (2012) · BioEssays · doi:10.1002/bies.201100107 · Cited by 201

Pre-mRNA splicing is a determinant of histone H3K36 methylation

Kim, S., Kim, H., Fong, N., Erickson, B., & Bentley, D. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109475108 · Cited by 198

Polycomb Group Protein Displacement and Gene Activation through MSK-Dependent H3K27me3S28 Phosphorylation

Gehani, S. S., Singh, S. A., Dietrich, N., Christophersen, N. S., Helin, K., & Hansen, K. H. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.020 · Cited by 195

The trithorax gene, a trans-acting regulator of the bithorax complex in Drosophila, encodes a protein with zinc-binding domains.

Mazo, A., Huang, D. H., Mozer, B. A., & Dawid, I. B. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.6.2112 · Cited by 194

A Reconfigured Pattern of MLL Occupancy within Mitotic Chromatin Promotes Rapid Transcriptional Reactivation Following Mitotic Exit

Blobel, G. A., Kadauke, S., Wang, E., Lau, A. W., Zuber, J. A., Chou, M. M., & Vakoc, C. R. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.12.001 · Cited by 194

The Histone H3K36 Methyltransferase MES-4 Acts Epigenetically to Transmit the Memory of Germline Gene Expression to Progeny

Rechtsteiner, A., Ercan, S., Takasaki, T., Phippen, T., Egelhofer, T. A., Wang, W., Kimurâ, H., Lieb, J. D., & Strome, S. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001091 · Cited by 193

Histone code pathway involving H3 S28 phosphorylation and K27 acetylation activates transcription and antagonizes polycomb silencing

Lau, P. N. I., & Cheung, P. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012798108 · Cited by 191

PR-Set7-dependent methylation of histone H4 Lys 20 functions in repression of gene expression and is essential for mitosisPreprint

Karachentsev, D., Sarma, K., Reinberg, D., & Steward, R. (2005) · Genes & Development · doi:10.1101/gad.1263005 · Cited by 191

WDR5 Interacts with Mixed Lineage Leukemia (MLL) Protein via the Histone H3-binding Pocket

Song, J., & Kingston, R. E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m806900200 · Cited by 189

Histone H4 Lys 20 monomethylation by histone methylase SET8 mediates Wnt target gene activation

Li, Z., Nie, F., Wang, S., & Li, L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1009353108 · Cited by 187

Specificity and mechanism of the histone methyltransferase Pr-Set7Preprint

Xiao, B., Jing, C., Kelly, G. P., Walker, P. A., Muskett, F. W., Frenkiel, T. A., Martin, S. R., Sarma, K., Reinberg, D., Gamblin, S. J., et al. (2005) · Genes & Development · doi:10.1101/gad.1315905 · Cited by 185

Polycomb Protein Ezh1 Promotes RNA Polymerase II Elongation

Mousavi, K., Zare, H., Wang, A. H., & Sartorelli, V. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.11.019 · Cited by 184

Heterochromatic Genome Stability Requires Regulators of Histone H3 K9 Methylation

Peng, J. C., & Karpen, G. H. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000435 · Cited by 183

The Lysine 831 of Vascular Endothelial Growth Factor Receptor 1 Is a Novel Target of Methylation by SMYD3

Kunizaki, M., Hamamoto, R., Pittella-Silva, F., Yamaguchi, K., Nagayasu, T., Shibuya, M., Nakamura, Y., & Furukawa, Y. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-1132 · Cited by 181

Trithorax-group protein ASH1 methylates histone H3 lysine 36

Tanaka, Y., Katagiri, Z.-I., Kawahashi, K., Kioussis, D., & Kitajima, S. (2007) · Gene · doi:10.1016/j.gene.2007.04.027 · Cited by 181

Localized H3K36 methylation states define histone H4K16 acetylation during transcriptional elongation in Drosophila

Bell, O., Wirbelauer, C., Hild, M., Scharf, A. N. D., Schwaiger, M., MacAlpine, D. M., Zilbermann, F., van Leeuwen, F., Bell, S. P., Imhof, A., et al. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601926 · Cited by 177

Methylated H3K4, a Transcription-Associated Histone Modification, Is Involved in the DNA Damage Response Pathway

Faucher, D., & Wellinger, R. J. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001082 · Cited by 176

Activation of RNA Polymerase I Transcription by Cockayne Syndrome Group B Protein and Histone Methyltransferase G9a

Yuan, X., Feng, W., Imhof, A., Grummt, I., & Zhou, Y. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.021 · Cited by 175

Smyd3 regulates cancer cell phenotypes and catalyzes histone H4 lysine 5 methylation

Aller, G. S. V., Reynoird, N., Barbash, O., Huddleston, M. J., Liu, S., Zmoos, A., McDevitt, P. J., Sinnamon, R. H., Le, B., Martín, G. M., et al. (2012) · Epigenetics · doi:10.4161/epi.19506 · Cited by 174

Epigenetic modifications of histones in cancer

Zhao, Z., & Shilatifard, A. (2019) · Genome biology · doi:10.1186/s13059-019-1870-5 · Cited by 591

Comprehensive Catalog of Currently Documented Histone ModificationsPreprint

Zhao, Y., & Garcia, B. A. (2015) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a025064 · Cited by 484

Targeting 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

An inhibitor of KDM5 demethylases reduces survival of drug-tolerant cancer cells

Vinogradova, M. V., Gehling, V. S., Gustafson, A. E., Arora, S., Tindell, C., WILSON, C. A., Williamson, K. E., Guler, G. D., Gangurde, P., Manieri, W., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2085 · Cited by 363

Reevaluating the roles of histone-modifying enzymes and their associated chromatin modifications in transcriptional regulation

Morgan, M. A., & Shilatifard, A. (2020) · Nature Genetics · doi:10.1038/s41588-020-00736-4 · Cited by 374

Structure of SET domain proteins: a new twist on histone methylation

Marmorstein, R. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00007-0 · Cited by 113

Unsafe SETs: histone lysine methyltransferases and cancer

Schneider, R., Bannister, A. J., & Kouzarides, T. (2002) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)02141-2 · Cited by 287

SET domains and histone methylation

Xiao, B., Wilson, J. R., & Gamblin, S. J. (2003) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2003.10.003 · Cited by 172

Structures of SET Domain Proteins

Yeates, T. O. (2002) · Cell · doi:10.1016/s0092-8674(02)01010-3 · Cited by 87

SET domain protein lysine methyltransferases: Structure, specificity and catalysis

Qian, C., & Zhou, M. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6274-5 · Cited by 331