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

Control of the Hippo Pathway by Set7-Dependent Methylation of Yap

Oudhoff, M. J., Freeman, S. A., Couzens, A. L., Antignano, F., Kuznetsova, E., Min, P. H., Northrop, J. P., Lehnertz, B., Baršytė-Lovejoy, D., Vedadi, M., et al. (2013) · Developmental Cell · doi:10.1016/j.devcel.2013.05.025 · Cited by 173

The Structure of NSD1 Reveals an Autoregulatory Mechanism Underlying Histone H3K36 Methylation

Qiao, Q., Li, Y., Chen, Z., Wang, M., Reinberg, D., & Xu, R.-M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.204115 · Cited by 172

Negative Regulation of Hypoxic Responses via Induced Reptin Methylation

Lee, J. S., Kim, Y.-H., Kim, I. S., Kim, B., Choi, H. J., Lee, J. M., Shin, H. R., Kim, J. H., Kim, J.-Y., Seo, S., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.06.008 · Cited by 172

ZNF274 Recruits the Histone Methyltransferase SETDB1 to the 3′ Ends of ZNF Genes

Frietze, S. E., O’Geen, H., Blahnik, K. R., Jin, V. X., & Farnham, P. (2010) · PLoS ONE · doi:10.1371/journal.pone.0015082 · Cited by 171

Smyd2 controls cytoplasmic lysine methylation of Hsp90 and myofilament organizationPreprint

Donlin, L. T., Andresen, C., Just, S., Rudensky, E., Pappas, C. T., Krüger, M., Jacobs, E. Y., Unger, A., Zieseniß, A., Dobenecker, M., et al. (2012) · Genes & Development · doi:10.1101/gad.177758.111 · Cited by 169

TwoC. eleganshistone methyltransferases represslin-3EGF transcription to inhibit vulval development

Andersen, E. C., & Horvitz, H. R. (2007) · Development · doi:10.1242/dev.009373 · Cited by 166

The Evil proto-oncogene is required at midgestation for neural, heart, and paraxial mesenchyme development

Hoyt, P. R., Bartholomew, C., Davis, A. J., Yutzey, K. E., Gamer, L. W., Potter, S. S., Ihle, J. N., & Mucenski, M. L. (1997) · Mechanisms of Development · doi:10.1016/s0925-4773(97)00057-9 · Cited by 164

MPP8 mediates the interactions between DNA methyltransferase Dnmt3a and H3K9 methyltransferase GLP/G9a

Chang, Y., Sun, L., Kokura, K., Horton, J. R., Fukuda, M., Espejo, A. B., Izumi, V., Koomen, J. M., Bedford, M. T., Zhang, X., et al. (2011) · Nature Communications · doi:10.1038/ncomms1549 · Cited by 163

G9a selectively represses a class of late-replicating genes at the nuclear periphery

Yokochi, T., Poduch, K., Ryba, T., Lu, J., Hiratani, I., Tachibana, M., Shinkai, Y., & Gilbert, D. M. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906142106 · Cited by 162

Phosphorylation of MLL by ATR is required for execution of mammalian S-phase checkpoint

Liu, H., Takeda, S., Kumar, R., Westergard, T. D., Brown, E. J., Pandita, T. K., Cheng, E. H. Y., & Hsieh, J. J.-D. (2010) · Nature · doi:10.1038/nature09350 · Cited by 161

Histone H3 Lysine 36 Dimethylation (H3K36me2) Is Sufficient to Recruit the Rpd3s Histone Deacetylase Complex and to Repress Spurious Transcription

Li, B., Jackson, J., Simon, M. D., Fleharty, B., Gogol, M., Seidel, C. W., Workman, J. L., & Shilatifard, A. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808220200 · Cited by 160

ASH1, a Drosophila trithorax group protein, is required for methylation of lysine 4 residues on histone H3

Byrd, K. N., & Shearn, A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1933593100 · Cited by 159

Histone H4 lysine 20 monomethylation promotes transcriptional repression by L3MBTL1

Kalakonda, N., Fischle, W., Boccuni, P., Gurvich, N., Hoya-Arias, R., Zhao, X., Miyata, Y., MacGrogan, D., Zhang, J., Sims, J. K., et al. (2008) · Oncogene · doi:10.1038/onc.2008.67 · Cited by 156

Catalytic Function of the PR-Set7 Histone H4 Lysine 20 Monomethyltransferase Is Essential for Mitotic Entry and Genomic Stability

Houston, S. I., McManus, K. J., Adams, M. M., Sims, J. K., Carpenter, P. B., Hendzel, M. J., & Rice, J. C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710579200 · Cited by 154

The Set1 Methyltransferase Opposes Ipl1 Aurora Kinase Functions in Chromosome Segregation

Zhang, K., Lin, W., Latham, J. A., Riefler, G. M., Schumacher, J. M., Chan, C. S. M., Tatchell, K., Hawke, D. H., Kobayashi, R., & Dent, S. (2005) · Cell · doi:10.1016/j.cell.2005.06.021 · Cited by 151

Hypoxic silencing of tumor suppressor RUNX3 by histone modification in gastric cancer cells

Lee, S. H., Kim, J., Kim, W.-H., & Lee, Y. M. (2008) · Oncogene · doi:10.1038/onc.2008.377 · Cited by 151

The SET domain protein Metnase mediates foreign DNA integration and links integration to nonhomologous end-joining repair

Lee, S., Oshige, M., Durant, S. T., Rasila, K. K., Williamson, E. A., Ramsey, H. E., Corwin, L. K., Nickoloff, J. A., & Hromas, R. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0503676102 · Cited by 150

Functional Interplay between Acetylation and Methylation of the RelA Subunit of NF-κB

Yang, X., Tajkhorshid, E., & Chen, L. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01343-09 · Cited by 149

Prdm16 is a physiologic regulator of hematopoietic stem cells

Aguiló, F., Avagyan, S., Labar, A., Sevilla, A., Lee, D., Kumar, P., Lemischka, I. R., Zhou, B. Y., & Snoeck, H. (2011) · Blood · doi:10.1182/blood-2010-08-300145 · Cited by 148

Cyclin-dependent Kinase 1 (CDK1)-mediated Phosphorylation of Enhancer of Zeste 2 (Ezh2) Regulates Its Stability

Wu, S. C., & Zhang, Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.240515 · Cited by 147

Histone Methyltransferase NSD2/MMSET Mediates Constitutive NF-κB Signaling for Cancer Cell Proliferation, Survival, and Tumor Growth via a Feed-Forward Loop

Yang, P. X., Guo, L., Duan, Z., Tepper, C. G., Xue, L., Chen, X., Kung, H., Gao, A. C., Zou, J. X., & Chen, H.-W. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00204-12 · Cited by 145

Transcriptional Repression and Heterochromatin Formation by MBD1 and MCAF/AM Family Proteins

Ichimura, T., Watanabe, S., Sakamoto, Y., Aoto, T., Fujita, N., & Nakao, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m413654200 · Cited by 145

Structural analysis of the core COMPASS family of histone H3K4 methylases from yeast to human

Takahashi, Y.-H., Westfield, G., Oleskie, A. N., Trievel, R. C., Shilatifard, A., & Skiniotis, G. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109360108 · Cited by 144

Role for the nuclear receptor-binding SET domain protein 1 (NSD1) methyltransferase in coordinating lysine 36 methylation at histone 3 with RNA polymerase II function

Lucio-Eterovic, A. K., Singh, M. M., Gardner, J. E., Veerappan, C. S., Rice, J. C., & Carpenter, P. B. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1002653107 · Cited by 143

CDYL Bridges REST and Histone Methyltransferases for Gene Repression and Suppression of Cellular Transformation

Mulligan, P., Westbrook, T. F., Ottinger, M., Pavlova, N. N., Chang, B., Macia, E., Shi, Y.-J., Barretina, J. G., Liu, J., Howley, P. M., et al. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.10.025 · Cited by 143

Reduced exploration, increased anxiety, and altered social behavior: Autistic-like features of euchromatin histone methyltransferase 1 heterozygous knockout mice

Balemans, M. C. M., Huibers, M. M. H., Eikelenboom, N., Kuipers, A. J., van Summeren, R. C. J., Pijpers, M. M. C. A., Tachibana, M., Shinkai, Y., van Bokhoven, H., & der Zee, C. E. E. M. V. (2009) · Behavioural Brain Research · doi:10.1016/j.bbr.2009.11.008 · Cited by 142

Preferential Dimethylation of Histone H4 Lysine 20 by Suv4-20

Yang, H., Pesavento, J. J., Starnes, T. W., Cryderman, D. E., Wallrath, L. L., Kelleher, N. L., & Mizzen, C. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707974200 · Cited by 140

Zinc Finger Protein Wiz Links G9a/GLP Histone Methyltransferases to the Co-repressor Molecule CtBP

Ueda, J., Tachibana, M., Ikura, T., & Shinkai, Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603087200 · Cited by 140

Crystal Structure of the Human Histone Methyltransferase ASH1L Catalytic Domain and Its Implications for the Regulatory Mechanism

An, S., Yeo, K. J., Jeon, Y. H., & Song, J. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.203380 · Cited by 139

Stabilization of Suv39H1 by SirT1 is part of oxidative stress response and ensures genome protection.

Bosch-Presegué, L., Raurell-Vila, H., Marazuela-Duque, A., Kane-Goldsmith, N., Valle, A., Oliver, J., Serrano, L., & Vaquero, A. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.034 · Cited by 138

Methyltransferase Set7/9 regulates p53 activity by interacting with Sirtuin 1 (SIRT1)

Liu, X., Wang, D., Zhao, Y., Tu, B., Zheng, Z., Wang, L., Wang, H., Gu, W. J., Roeder, R. G., & Zhu, W. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1019619108 · Cited by 137

hamlet , a Binary Genetic Switch Between Single- and Multiple- Dendrite Neuron Morphology

Moore, A. W., Jan, L. Y., & Jan, Y. N. (2002) · Science · doi:10.1126/science.1072387 · Cited by 137

Substrate and product specificities of SET domain methyltransferases

Rizzo, P. A. D., & Trievel, R. C. (2011) · Epigenetics · doi:10.4161/epi.6.9.16069 · Cited by 136

Dynamic regulation of the PR-Set7 histone methyltransferase is required for normal cell cycle progressionPreprint

Wu, S., Wang, W., Kong, X., Congdon, L. M., Yokomori, K., Kirschner, M. W., & Rice, J. C. (2010) · Genes & Development · doi:10.1101/gad.1984210 · Cited by 135

Histone H3 Lysine 56 Methylation Regulates DNA Replication through Its Interaction with PCNA

Yu, Y., Song, C., Zhang, Q., DiMaggio, P. A., Garcia, B. A., York, A. G., Carey, M., & Grunstein, M. R. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.01.019 · Cited by 132

Histone methyltransferase G9a contributes to H3K27 methylation in vivo

Wu, H., Chen, X., Xiong, J., Li, Y., Li, H., Ding, X., Liu, S., Chen, S., Gao, S., & Zhu, B. (2010) · Cell Research · doi:10.1038/cr.2010.157 · Cited by 131

Direct Interaction between SET8 and Proliferating Cell Nuclear Antigen Couples H4-K20 Methylation with DNA Replication

Huen, M. S. Y., Sy, S. M.-H., van Deursen, J. M., & Chen, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.c700242200 · Cited by 129

SET8 is degraded via PCNA-coupled CRL4(CDT2) ubiquitylation in S phase and after UV irradiation

Jørgensen, S., Eskildsen, M., Fugger, K., Hansen, L., Larsen, M. S. Y., Kousholt, A. N., Syljuåsen, R. G., Trelle, M. B., Jensen, O. N., Helin, K., et al. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201009076 · Cited by 128

Structural and Functional Profiling of the Human Histone Methyltransferase SMYD3

Foreman, K. W., Brown, M., Park, F., Emtage, S., Harriss, J. V., Das, C., Zhu, L., Crew, A., Arnold, L. D., Shaaban, S. A., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022290 · Cited by 128

MLL5, a trithorax homolog, indirectly regulates H3K4 methylation, represses cyclin A2 expression, and promotes myogenic differentiation

Sebastian, S., Sreenivas, P., Sambasivan, R., Cheedipudi, S. M., Kandalla, P. K., Pavlath, G. K., & Dhawan, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0807136106 · Cited by 127

Automethylation of G9a and its implication in wider substrate specificity and HP1 binding

Chin, H. G., Estève, P., Pradhan, M., Benner, J. S., Patnaik, D., Carey, M., & Pradhan, S. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm726 · Cited by 127

Regulation of the androgen receptor by SET9-mediated methylation.

Gaughan, L., Stockley, J., Wang, N., McCracken, S. R. C., Treumann, A., Armstrong, K., Shaheen, F., Watt, K., McEwan, I. J., Wang, C., et al. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkq861 · Cited by 127

MES-4: an autosome-associated histone methyltransferase that participates in silencing the X chromosomes in theC. elegansgerm line

Bender, L. B., Suh, J., Carroll, C. R., Fong, Y., Fingerman, I. M., Briggs, S. D., Cao, R., Zhang, Y., Reinke, V., & Strome, S. (2006) · Development · doi:10.1242/dev.02584 · Cited by 125

Lysine methylation regulates the pRb tumour suppressor protein

Munro, S., Khaire, N., Inche, A. G., Carr, S. M., & Thangue, N. B. L. (2010) · Oncogene · doi:10.1038/onc.2009.511 · Cited by 124

The role of PR-Set7 in replication licensing depends on Suv4-20hPreprint

Beck, D. B., Burton, A., Oda, H., Ziegler-Birling, C., Torres‐Padilla, M., & Reinberg, D. (2012) · Genes & Development · doi:10.1101/gad.195636.112 · Cited by 124

Dynamic Methylation of Numb by Set8 Regulates Its Binding to p53 and Apoptosis

Dhami, G. K., Liu, H., Galka, M., Voss, C., Wei, R., Muranko, K., Kaneko, T., Cregan, S. P., Li, L., & Li, S. S. ‐. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.04.028 · Cited by 123

Prdm Proto-Oncogene Transcription Factor Family Expression and Interaction with the Notch-Hes Pathway in Mouse Neurogenesis

Kinameri, E., Inoue, T., Aruga, J., Imayoshi, I., Kageyama, R., Shimogori, T., & Moore, A. W. (2008) · PLoS ONE · doi:10.1371/journal.pone.0003859 · Cited by 122

The plasticity of WDR5 peptide-binding cleft enables the binding of the SET1 family of histone methyltransferases

Zhang, P., Lee, H., Brunzelle, J. S., & Couture, J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gkr1235 · Cited by 122

Lysine-specific Demethylase 2B (KDM2B)-let-7-Enhancer of Zester Homolog 2 (EZH2) Pathway Regulates Cell Cycle Progression and Senescence in Primary Cells

Tzatsos, A., Paskaleva, P., Lymperi, S., Contino, G., Stoykova, S., Chen, Z., Wong, K., & Bardeesy, N. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.257667 · Cited by 119

Characterization of a Novel WDR5-binding Site That Recruits RbBP5 through a Conserved Motif to Enhance Methylation of Histone H3 Lysine 4 by Mixed Lineage Leukemia Protein-1*

Odho, Z., Southall, S. M., & Wilson, J. R. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.159921 · Cited by 117

Structural and Biochemical Insights into MLL1 Core Complex Assembly

Avdic, V., Zhang, P., Lanouette, S., Groulx, A. F., Tremblay, V., Brunzelle, J. S., & Couture, J. (2011) · Structure · doi:10.1016/j.str.2010.09.022 · Cited by 117

Ubiquitylation of the COMPASS component Swd2 links H2B ubiquitylation to H3K4 trimethylation

Vitaliano-Prunier, A., Menant, A., Hobeika, M., Géli, V., Gwizdek, C., & Dargemont, C. (2008) · Nature Cell Biology · doi:10.1038/ncb1796 · Cited by 117

Proteomic analyses of the SMYD family interactomes identify HSP90 as a novel target for SMYD2

Abu‐Farha, M., Lanouette, S., Elisma, F., Tremblay, V., Butson, J., Figeys, D., & Couture, J. (2011) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjr025 · Cited by 117

The H3K27me3 Demethylase dUTX Is a Suppressor of Notch- and Rb-Dependent Tumors in Drosophila

Herz, H., Madden, L. D., Chen, Z., Bolduc, C., Buff, E. M., Gupta, R., Davuluri, R. V., Shilatifard, A., Hariharan, I. K., & Bergmann, A. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01633-09 · Cited by 116

p21WAF1 gene promoter is epigenetically silenced by CTIP2 and SUV39H1

Cherrier, T., Suzanne, S., Redel, L., Calao, M., Marban, C., Samah, B., Mukerjee, R., Schwartz, C., Gras, G. S., Sawaya, B. E., et al. (2009) · Oncogene · doi:10.1038/onc.2009.193 · Cited by 115

Interplay between lysine methylation and Cdk phosphorylation in growth control by the retinoblastoma protein

Carr, S. M., Munro, S., Kessler, B. M., Oppermann, U. C. T., & Thangue, N. B. L. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.311 · Cited by 115

huASH1 protein, a putative transcription factor encoded by a human homologue of the Drosophila ash1 gene, localizes to both nuclei and cell–cell tight junctions

Nakamura, T., Blechman, J., Tada, S., Rozovskaia, T., Itoyama, T., Bullrich, F., Mazo, A., Croce, C. M., Geiger, B., & Canaani, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.13.7284 · Cited by 114

The Cellular Lysine Methyltransferase Set7/9-KMT7 Binds HIV-1 TAR RNA, Monomethylates the Viral Transactivator Tat, and Enhances HIV Transcription

Pagans, S., Kauder, S. E., Kaehlcke, K., Sakane, N., Schroeder, S., Dormeyer, W., Trievel, R. C., Verdin, E. M., Schnölzer, M., & Ott, M. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.02.005 · Cited by 113

An Ash2L/RbBP5 Heterodimer Stimulates the MLL1 Methyltransferase Activity through Coordinated Substrate Interactions with the MLL1 SET Domain

Cao, F., Chen, Y., Cierpicki, T., Liu, Y., Basrur, V., Lei, M., & Dou, Y. (2010) · PLoS ONE · doi:10.1371/journal.pone.0014102 · Cited by 112

Four enzymes cooperate to displace histone H1 during the first minute of hormonal gene activationPreprint

Vicent, G. P., Nacht, A. S., Font-Mateu, J., Castellano, G., Gaveglia, L., Ballaré, C., & Beato, M. (2011) · Genes & Development · doi:10.1101/gad.621811 · Cited by 109

Drosophila SETDB1 Is Required for Chromosome 4 Silencing

Seum, C., Reo, E., Peng, H., Rauscher, F. J., Spierer, P., & Bontron, S. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030076 · Cited by 109

Trans-generational epigenetic regulation of C. elegans primordial germ cells

Furuhashi, H., Takasaki, T., Rechtsteiner, A., Li, T., Kimura, H., Checchi, P. M., Strome, S., & Kelly, W. G. (2010) · Epigenetics & Chromatin · doi:10.1186/1756-8935-3-15 · Cited by 107

G9a-mediated Lysine Methylation Alters the Function of CCAAT/Enhancer-binding Protein-β

Pleß, O., Kowenz‐Leutz, E., Knoblich, M., Lausen, J., Beyermann, M., Walsh, M. J., & Leutz, A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802132200 · Cited by 107

Histone H1 variant-specific lysine methylation by G9a/KMT1C and Glp1/KMT1D

Weiss, T., Hergeth, S., Zeißler, U., Izzo, A., Tropberger, P., Zee, B. M., Dundr, M., Garcia, B. A., Daujat, S., & Schneider, R. (2010) · Epigenetics & Chromatin · doi:10.1186/1756-8935-3-7 · Cited by 107

Lysine Methylation and Functional Modulation of Androgen Receptor by Set9 Methyltransferase

Ko, S., Ahn, J., Song, C. S., Kim, S.-Y., Knapczyk‐Stwora, K., & Chatterjee, B. (2011) · Molecular Endocrinology · doi:10.1210/me.2010-0482 · Cited by 102

dSet1 Is the Main H3K4 Di- and Tri-Methyltransferase ThroughoutDrosophilaDevelopment

Hallson, G., Hollebakken, R. E., Li, T., Syrzycka, M., Kim, I., Cotsworth, S., Fitzpatrick, K. A., Sinclair, D. A. R., & Honda, B. M. (2011) · Genetics · doi:10.1534/genetics.111.135863 · Cited by 102

Global identification of MLL2-targeted loci reveals MLL2’s role in diverse signaling pathways

Guo, C., Chang, C.-C., Wortham, M., Chen, L. H., Kernagis, D., Qin, X., Cho, Y., Chi, J., Grant, G. A., McLendon, R. E., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208807109 · Cited by 101

Methylation by Set9 modulates FoxO3 stability and transcriptional activity

Calnan, D. R., Webb, A. E., White, J. L., Stowe, T. R., Goswami, T., Shi, X., Espejo, A. B., Bedford, M. T., Gozani, O., Gygi, S. P., et al. (2012) · Aging · doi:10.18632/aging.100471 · Cited by 101

Identification of a PRMT5-dependent repressor complex linked to silencing of human fetal globin gene expression

Rank, G., Cerruti, L., Simpson, R. J., Moritz, R. L., Jane, S. M., & Zhao, Q. (2010) · Blood · doi:10.1182/blood-2009-10-251116 · Cited by 94

The MBT Repeats of L3MBTL1 Link SET8-mediated p53 Methylation at Lysine 382 to Target Gene Repression

West, L. E., Roy, S., Weiner, K., Hayashi, R., Shi, X., Appella, E., Kutateladze, T. G., & Gozani, O. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.139527 · Cited by 94

SUV420H2-Mediated H4K20 Trimethylation Enforces RNA Polymerase II Promoter-Proximal Pausing by Blocking hMOF-Dependent H4K16 Acetylation

Kapoor-Vazirani, P., Kagey, J. D., & Vertino, P. M. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.00524-10 · Cited by 94

Wolf–Hirschhorn syndrome candidate 1 is involved in the cellular response to DNA damage

Hajdú, I., Ciccia, A., Lewis, S. M., & Elledge, S. J. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1110081108 · Cited by 92

Chromatin modification of Notch targets in olfactory receptor neuron diversification

Endo, K., Karim, M. R., Taniguchi, H., Krejčı́, A., Kinameri, E., Siebert, M., Ito, K., Bray, S. J., & Moore, A. W. (2011) · Nature Neuroscience · doi:10.1038/nn.2998 · Cited by 90

The Methyltransferase Set7/9 (Setd7) Is Dispensable for the p53-Mediated DNA Damage Response In Vivo

Campaner, S., Spreafico, F., Burgold, T., Doni, M., Rosato, U., Amati, B. B., & Testa, G. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.007 · Cited by 88

Post-translational modifications in the large subunit of ribulose bisphosphate carboxylase/oxygenase.

Houtz, R. L., Stults, J. T., Mulligan, R. M., & Tolbert, N. E. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.6.1855 · Cited by 88

PR‐Set7‐mediated monomethylation of histone H4 lysine 20 at specific genomic regions induces transcriptional repression

Congdon, L. M., Houston, S. I., Veerappan, C. S., Spektor, T. M., & Rice, J. C. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22570 · Cited by 87

Multiple SET Methyltransferases Are Required to Maintain Normal Heterochromatin Domains in the Genome of Drosophila melanogaster

Brower-Toland, B., Riddle, N. C., Jiang, H., Huisinga, K. L., & Elgin, S. C. R. (2009) · Genetics · doi:10.1534/genetics.108.100271 · Cited by 86

Lysine methylation of HIV-1 Tat regulates transcriptional activity of the viral LTR

Duyne, R. V., Easley, R. L., Wu, W., Berro, R., Pedati, C., Klase, Z. A., Kehn‐Hall, K., Flynn, E. K., Symer, D. E., & Kashanchi, F. (2008) · Retrovirology · doi:10.1186/1742-4690-5-40 · Cited by 86

A Distinct Mechanism for Coactivator versus Corepressor Function by Histone Methyltransferase G9a in Transcriptional Regulation

Purcell, D. J., Jeong, K. W., Bittencourt, D., Gerke, D. S., & Stallcup, M. R. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.298463 · Cited by 85

Epigenetic regulation of the Drosophila chromosome 4 by the histone H3K9 methyltransferase dSETDB1

Tzeng, T., Lee, C., Chan, L.-W., & Shen, C. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705534104 · Cited by 84

Inhibition of SUV39H1 Methyltransferase Activity by DBC1

Li, Z., Chen, L., Kabra, N., Wang, C., Fang, J., & Chen, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m900956200 · Cited by 84

Recruitment ofDrosophilaPolycomb-group proteins by Polycomblike, a component of a novel protein complex in larvae

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CLLD8/KMT1F Is a Lysine Methyltransferase That Is Important for Chromosome Segregation

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EVI-1 interacts with histone methyltransferases SUV39H1 and G9a for transcriptional repression and bone marrow immortalization

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H4K20me1 Contributes to Downregulation of X-Linked Genes for C. elegans Dosage Compensation

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Structural basis of SETD6-mediated regulation of the NF-kB network via methyl-lysine signaling

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Polycomb Repressive Complex 2-Dependent and -Independent Functions of Jarid2 in Transcriptional Regulation in Drosophila

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Aberrant monomethylation of histone H4 lysine 20 activates the DNA damage checkpoint in Drosophila melanogaster

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p53-Dependent Transcription and Tumor Suppression Are Not Affected in Set7/9-Deficient Mice

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Chromatin Signaling to Kinetochores: Transregulation of Dam1 Methylation by Histone H2B Ubiquitination

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H3 K36 Methylation Helps Determine the Timing of Cdc45 Association with Replication Origins

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Set2-Catalyzed Methylation of Histone H3 Represses Basal Expression of GAL4 in Saccharomyces cerevisiae

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Structure of Human SMYD2 Protein Reveals the Basis of p53 Tumor Suppressor Methylation

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Metnase mediates chromosome decatenation in acute leukemia cells

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Ecdysone- and NO-Mediated Gene Regulation by Competing EcR/Usp and E75A Nuclear Receptors during Drosophila Development

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The JARID2–PRC2 duality: Figure 1.Preprint

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MDM2 recruitment of lysine methyltransferases regulates p53 transcriptional output

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Identification of three histone methyltransferases in Drosophila: dG9a is a suppressor of PEV and is required for gene silencing

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The SET and transposase domain protein Metnase enhances chromosome decatenation: regulation by automethylation

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UpSET Recruits HDAC Complexes and Restricts Chromatin Accessibility and Acetylation at Promoter Regions

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SET8 plays a role in controlling G1/S transition by blocking lysine acetylation in histone through binding to H4 N-terminal tail

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Polycomb CBX7 Directly Controls Trimethylation of Histone H3 at Lysine 9 at the p16 Locus

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Yeast Swd2 Is Essential Because of Antagonism between Set1 Histone Methyltransferase Complex and APT (Associated with Pta1) Termination Factor

Soares, L. M. M., & Buratowski, S. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.341412 · Cited by 59

The Polycomb Group Mutant esc Leads to Augmented Levels of Paused Pol II in the Drosophila Embryo

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Direct methylation of FXR by Set7/9, a lysine methyltransferase, regulates the expression of FXR target genes

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EVI1 recruits the histone methyltransferase SUV39H1 for transcription repression

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A novel interaction between the proto‐oncogene Evi1 and histone methyltransferases, SUV39H1 and G9a

Spensberger, D., & Delwel, R. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.06.056 · Cited by 54

Dual Function of Histone H3 Lysine 36 Methyltransferase ASH1 in Regulation of Hox Gene Expression

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A Novel SET Domain Methyltransferase in Yeast

Porras-Yakushi, T. R., Whitelegge, J. P., & Clarke, S. G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606578200 · Cited by 53

The bromodomain protein LIN-49 and trithorax-related protein LIN-59 affect development and gene expression in Caenorhabditis elegans

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A Role for Chd1 and Set2 in Negatively Regulating DNA Replication in Saccharomyces cerevisiae

Biswas, D., Takahata, S., Hua, X., Dutta-Biswas, R., Yu, Y., Formosa, T., & Stillman, D. J. (2008) · Genetics · doi:10.1534/genetics.107.084202 · Cited by 50

Crystal structure of the N‐terminal region of human Ash2L shows a winged‐helix motif involved in DNA binding

Chen, Y., Wan, B., Wang, K., Cao, F., Yang, Y., Protacio, A., Dou, Y., Chang, H. Y., & Lei, M. (2011) · EMBO Reports · doi:10.1038/embor.2011.101 · Cited by 50

Crucial Roles for Interactions between MLL3/4 and INI1 in Nuclear Receptor Transactivation

Lee, S., Kim, D., Goo, Y. H., Lee, Y. C., Lee, S., & Lee, J. W. (2009) · Molecular Endocrinology · doi:10.1210/me.2008-0455 · Cited by 49

A Novel SET Domain Methyltransferase Modifies Ribosomal Protein Rpl23ab in Yeast

Porras-Yakushi, T. R., Whitelegge, J. P., Miranda, T. B., & Clarke, S. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507672200 · Cited by 49

Charge-based Interaction Conserved within Histone H3 Lysine 4 (H3K4) Methyltransferase Complexes Is Needed for Protein Stability, Histone Methylation, and Gene Expression

Mersman, D. P., Du, H., Fingerman, I. M., South, P. F., & Briggs, S. D. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.280867 · Cited by 48

Multiple lysine methylation of PCAF by Set9 methyltransferase

Masatsugu, T., & Yamamoto, K. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.01.185 · Cited by 48

ASCOM Controls Farnesoid X Receptor Transactivation through Its Associated Histone H3 Lysine 4 Methyltransferase Activity

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Novel trans-Tail Regulation of H2B Ubiquitylation and H3K4 Methylation by the N Terminus of Histone H2A

Zheng, S., Wyrick, J. J., & Reese, J. C. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00324-10 · Cited by 47

Functional Characterization of the Drosophila Hmt4-20/Suv4-20 Histone Methyltransferase

Sakaguchi, A., Karachentsev, D., Seth‐Pasricha, M., Druzhinina, M. K., & Steward, R. (2008) · Genetics · doi:10.1534/genetics.108.087650 · Cited by 46

Epigenetic Regulation of Surfactant Protein A Gene (SP-A) Expression in Fetal Lung Reveals a Critical Role for Suv39h Methyltransferases during Development and Hypoxia

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Crystal structure of the trithorax group protein ASH2L reveals a forkhead-like DNA binding domain

Sarvan, S., Avdic, V., Tremblay, V., Chaturvedi, C.-P., Zhang, P., Lanouette, S., Blais, A., Brunzelle, J. S., Brand, M., & Couture, J. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2093 · Cited by 44

Drosophila G9a Is a Nonessential Gene

Seum, C., Bontron, S., Reo, E., Delattre, M., & Spierer, P. (2007) · Genetics · doi:10.1534/genetics.107.078220 · Cited by 43

Identification of Two SET Domain Proteins Required for Methylation of Lysine Residues in Yeast Ribosomal Protein Rpl42ab

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Molecular genetic analysis of the Drosophila trithorax-related gene which encodes a novel SET domain protein

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Comparative Analyses of SUV420H1 Isoforms and SUV420H2 Reveal Differences in Their Cellular Localization and Effects on Myogenic Differentiation

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Histone recognition and nuclear receptor co-activator functions ofDrosophilaCara Mitad, a homolog of the N-terminal portion of mammalian MLL2 and MLL3

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Structure of human lysine methyltransferase Smyd2 reveals insights into the substrate divergence in Smyd proteins

Xu, S., Zhong, C., Zhang, T., & Ding, J. (2011) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjr015 · Cited by 36

Yeast Ribosomal/Cytochrome c SET Domain Methyltransferase Subfamily

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GRIP1-associated SET-domain methyltransferase in glucocorticoid receptor target gene expression

Chinenov, Y. V., Sacta, M. A., Cruz, A. R., & Rogatsky, I. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810863105 · Cited by 30

Methylations of histone H3 lysine 9 and lysine 36 are functionally linked to DNA replication checkpoint control in fission yeast

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PR-Set7 Establishes a Repressive trans-Tail Histone Code That Regulates Differentiation

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Organization and characterization of the ribulose-1,5-bisphosphate carboxylase/oxygenase large subunit % MathType!MTEF!2!1!+-% feaafiart1ev1aaatCvAUfeBSjuyZL2yd9gzLbvyNv2CaerbuLwBLn% hiov2DGi1BTfMBaeXafv3ySLgzGmvETj2BSbqef0uAJj3BZ9Mz0bYu% H52CGmvzYLMzaerbd9wDYLwzYbItLDharqqr1ngBPrgifHhDYfgasa% acOqpw0xe9v8qqaqFD0xXdHaVhbbf9v8qqaqFr0xc9pk0xbba9q8Wq% Ffea0-yr0RYxir-Jbba9q8aq0-yq-He9q8qqQ8frFve9Fve9Ff0dme% GabaqaaiGacaGaamqadaabaeaafiaakeaadaahbaWcbeqaaiabgIGi% odaakiaad6eaaaa!465E!\[{}^ \in N\]-methyltransferase gene in tobacco

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Epigenetic modifications of histones in cancer

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Unsafe SETs: histone lysine methyltransferases and cancer

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SET domains and histone methylation

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Structures of SET Domain Proteins

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