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

High-Resolution Profiling of Histone Methylations in the Human Genome

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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

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

Enhancer biology and enhanceropathies

Smith, E. R., & Shilatifard, A. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2784 · Cited by 326

The role of histone modifications: from neurodevelopment to neurodiseases

Park, J., Lee, K., Kim, K., & Yi, S.-J. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01078-9 · Cited by 333

From 1957 to Nowadays: A Brief History of Epigenetics

Peixoto, P., Cartron, P., Sérandour, A. A., & Hervouet, É. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21207571 · Cited by 250

Assessing sufficiency and necessity of enhancer activities for gene expression and the mechanisms of transcription activationPreprint

Catarino, R. R., & Stark, A. (2018) · Genes & Development · doi:10.1101/gad.310367.117 · Cited by 215

The Role of Nuclear Receptor–Binding SET Domain Family Histone Lysine Methyltransferases in CancerPreprint

Bennett, R. L., Swaroop, A., Troche, C., & Licht, J. D. (2017) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026708 · Cited by 203

Histone modifications in epigenetic regulation of cancer: Perspectives and achieved progress

Неганова, М. Е., Klochkov, S. G., Aleksandrova, Y. R., & Aliev, G. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.07.015 · Cited by 211

Histone H3 lysine-to-methionine mutants as a paradigm to study chromatin signaling

Herz, H.-M., Morgan, M., Gao, X., Jackson, J., Rickels, R., Swanson, S. K., Florens, L., Washburn, M. P., Eissenberg, J. C., & Shilatifard, A. (2014) · Science · doi:10.1126/science.1255104 · Cited by 199

Sound of silence: the properties and functions of repressive Lys methyltransferases

Mozzetta, C., Boyarchuk, E., Pontis, J., & Ait‐Si‐Ali, S. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4029 · Cited by 217

The winding path of protein methylation research: milestones and new frontiers

Murn, J., & Shi, Y. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.35 · Cited by 205

Targeting histone lysine methylation in cancer

McGrath, J. P., & Trojer, P. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.01.002 · Cited by 190

A Histone Methylation Network Regulates Transgenerational Epigenetic Memory in C. elegans

Greer, E. L., Beese‐Sims, S. E., Brookes, E., Spadafora, R., Zhu, Y., Rothbart, S. B., Aristizábal-Corrales, D., Chen, S., Badeaux, A. I., Jin, Q., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.02.044 · Cited by 192

Genetic alterations of histone lysine methyltransferases and their significance in breast cancer

Liu, L., Kimball, S., Liu, H., Holowatyj, A., & Yang, Z.-Q. (2014) · Oncotarget · doi:10.18632/oncotarget.2967 · Cited by 178

Recurrent evolution of vertebrate transcription factors by transposase capture

Cosby, R. L., Judd, J., Zhang, R., Zhong, A., Garry, N., Pritham, E. J., & Feschotte, C. (2021) · Science · doi:10.1126/science.abc6405 · Cited by 173

The cancer COMPASS: navigating the functions of MLL complexes in cancer

Ford, D. J., & Dingwall, A. K. (2015) · Cancer Genetics · doi:10.1016/j.cancergen.2015.01.005 · Cited by 169

Histone Methylation by SET Domain Proteins in Fungi

Freitag, M. (2017) · Annual Review of Microbiology · doi:10.1146/annurev-micro-102215-095757 · Cited by 169

MLL3/MLL4/COMPASS Family on Epigenetic Regulation of Enhancer Function and Cancer

Sze, C. C., & Shilatifard, A. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026427 · Cited by 164

Structures and biological functions of zinc finger proteins and their roles in hepatocellular carcinoma

Li, X., Han, M., Zhang, H., Liu, F., Pan, Y., Zhu, J., Liao, Z., Chen, X., & Zhang, B. (2022) · Biomarker Research · doi:10.1186/s40364-021-00345-1 · Cited by 158

The SUV4-20 inhibitor A-196 verifies a role for epigenetics in genomic integrity

Bromberg, K. D., Mitchell, T. R. H., Upadhyay, A. K., Jakob, C. G., Jhala, M. A., Comess, K. M., Lasko, L. M., Li, C., Tuzon, C. T., Dai, Y., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2282 · Cited by 132

Nonhistone Lysine Methylation in the Regulation of Cancer PathwaysPreprint

Carlson, S. M., & Gozani, O. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026435 · Cited by 133

Helitrons , the Eukaryotic Rolling-circle Transposable Elements

Thomas, J., & Pritham, E. J. (2015) · Microbiology Spectrum · doi:10.1128/microbiolspec.mdna3-0049-2014 · Cited by 121

An Mtb-Human Protein-Protein Interaction Map Identifies a Switch between Host Antiviral and Antibacterial Responses

Penn, B. H., Netter, Z., Johnson, J. R., Dollen, J. V., Jang, G. Μ., Johnson, T. L., Ohol, Y. M., Maher, C., Bell, S. L., Geiger, K. M., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.07.010 · Cited by 118

SETD3 protein is the actin-specific histidine N-methyltransferase

Kwiatkowski, S., Seliga, A. K., Vertommen, D., Terreri, M., Ishikawa, T., Grabowska, I., Tiebe, M., Teleman, A. A., Jagielski, A. K., Veiga‐da‐Cunha, M., et al. (2018) · eLife · doi:10.7554/elife.37921 · Cited by 114

Enhancer deregulation in cancer and other diseases

Herz, H. (2016) · BioEssays · doi:10.1002/bies.201600106 · Cited by 110

SETD7 Controls Intestinal Regeneration and Tumorigenesis by Regulating Wnt/β-Catenin and Hippo/YAP Signaling

Oudhoff, M. J., Braam, M. J. S., Freeman, S. A., Wong, D., Rattray, D., Wang, J., Antignano, F., Snyder, K., Refaeli, I., Hughes, M. R., et al. (2016) · Developmental Cell · doi:10.1016/j.devcel.2016.03.002 · Cited by 114

Targeting post-translational histone modifying enzymes in glioblastoma

Kunadis, E., Lakiotaki, E., Korkolopoulou, P. A., & Piperi, C. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107721 · Cited by 113

The methyltransferase METTL9 mediates pervasive 1-methylhistidine modification in mammalian proteomes

Davydova, E., Shimazu, T., Schuhmacher, M. K., Jakobsson, M. E., Willemen, H. L. D. M., Liu, T., Moen, A. R., Ho, A. Y. Y., Małecki, J., Schroer, L., et al. (2021) · Nature Communications · doi:10.1038/s41467-020-20670-7 · Cited by 108

Structural Basis for KDM5A Histone Lysine Demethylase Inhibition by Diverse Compounds

Horton, J. R., Liu, X., Gale, M., Wu, L., Shanks, J. R., Zhang, X., Webber, P. J., Bell, J. S. K., Kales, S. C., Mott, B. T., et al. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2016.06.006 · Cited by 105

Role of Epigenetic Modifications in Inhibitory Immune Checkpoints in Cancer Development and Progression

Saleh, R., Toor, S. M., Nair, V. S., & Elkord, E. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01469 · Cited by 107

Pluripotency and Epigenetic Factors in Mouse Embryonic Stem Cell Fate Regulation

Morey, L., Santanach, A., & Croce, L. D. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00266-15 · Cited by 101

Macromolecular transport between the nucleus and the cytoplasm: Advances in mechanism and emerging links to disease

Tran, E. J., King, M. C., & Corbett, A. H. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.08.003 · Cited by 101

Protein lysine methylation by seven-β-strand methyltransferases

Falnes, P. Ø., Jakobsson, M. E., Davydova, E., Ho, A. Y. Y., & Małecki, J. (2016) · Biochemical Journal · doi:10.1042/bcj20160117 · Cited by 100

KMT2C/D COMPASS complex-associated diseases [KCDCOM-ADs]: an emerging class of congenital regulopathies

Lavery, W. J., Barski, A., Wiley, S., Schorry, E. K., & Lindsley, A. (2020) · Clinical Epigenetics · doi:10.1186/s13148-019-0802-2 · Cited by 99

Histone methyltransferases EHMT1 and EHMT2 (GLP/G9A) maintain PARP inhibitor resistance in high-grade serous ovarian carcinoma

Watson, Z. L., Yamamoto, T. M., McMellen, A., Kim, H., Hughes, C. J., Wheeler, L., Post, M., Behbakht, K., & Bitler, B. (2019) · Clinical Epigenetics · doi:10.1186/s13148-019-0758-2 · Cited by 80

An Overview of Chromatin-Regulating Proteins in Cells

Zhang, P., Torres, K. E., Liu, X., Liu, C.-G., & Pollock, R. E. (2016) · Current Protein and Peptide Science · doi:10.2174/1389203717666160122120310 · Cited by 91

Gene regulation by histone-modifying enzymes under hypoxic conditions: a focus on histone methylation and acetylation

Kim, J., Lee, H.-R., Yi, S.-J., & Kim, K. (2022) · Experimental & Molecular Medicine · doi:10.1038/s12276-022-00812-1 · Cited by 98

Global histone modification profiling reveals the epigenomic dynamics during malignant transformation in a four-stage breast cancer model

Zhao, Q., Lei, P., Zhang, X., Zheng, J., Wang, H.-Y., Zhao, J., Li, Y., Ye, M., Li, L., Wei, G., et al. (2016) · Clinical Epigenetics · doi:10.1186/s13148-016-0201-x · Cited by 93

MLL2, not MLL1, Plays a Major Role in Sustaining MLL-rearranged Acute Myeloid Leukemia

Chen, Y.-F., Anastassiadis, K., Kranz, A., Stewart, A., Arndt, K., Waskow, C., Yokoyama, A., Jones, K. L., Neff, T., Lee, Y., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.05.002 · Cited by 83

Computational prediction of methylation types of covalently modified lysine and arginine residues in proteins

Deng, W., Wang, Y., Ma, L., Zhang, Y. W., Ullah, S., & Xue, Y. (2016) · Briefings in Bioinformatics · doi:10.1093/bib/bbw041 · Cited by 86

Diverse functions of PHD fingers of the MLL/KMT2 subfamily

Ali, M., Hom, R. A., Blakeslee, W. W., Ikenouye, L., & Kutateladze, T. G. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.11.016 · Cited by 85

The novel lysine specific methyltransferase METTL21B affects mRNA translation through inducible and dynamic methylation of Lys-165 in human eukaryotic elongation factor 1 alpha (eEF1A)

Małecki, J., Aileni, V. K., Ho, A. Y. Y., Schwarz, J., Moen, A. R., Sørensen, V., Nilges, B. S., Jakobsson, M. E., Leidel, S. A., & Falnes, P. Ø. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx002 · Cited by 82

Histone target selection within chromatin: an exemplary case of teamworkPreprint

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

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

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

A methylation-phosphorylation switch determines Plk1 kinase activity and function in DNA damage repair

Li, W., Wang, H., Zhao, X., Duan, H., Cheng, B., Liu, Y., Zhao, M., Shu, W., Mei, Y.-C., Wen, Z., et al. (2019) · Science Advances · doi:10.1126/sciadv.aau7566 · Cited by 77

Regulated nuclear accumulation of a histone methyltransferase times the onset of heterochromatin formation in C. elegans embryos

Mutlu, B., Chen, H.-M., Moresco, J. J., Orelo, B. D., Yang, B., Gaspar, J. M., Keppler‐Ross, S., Yates, J. R., Hall, D. H., Maine, E. M., et al. (2018) · Science Advances · doi:10.1126/sciadv.aat6224 · Cited by 77

Emerging role of SETDB1 as a therapeutic target

Karanth, A. V., Maniswami, R. R., Prashanth, S., Govindaraj, H., Padmavathy, R., Jegatheesan, S. K., Mullangi, R., & Rajagopal, S. (2017) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2017.1279604 · Cited by 69

Mechanisms underlying epigenetic and transcriptional heterogeneity in Chinese hamster ovary (CHO) cell lines

Veith, N., Ziehr, H., MacLeod, R. A. F., & Reamon-Buettner, S. M. (2016) · BMC Biotechnology · doi:10.1186/s12896-016-0238-0 · Cited by 69

Chromatin dysregulation associated with NSD1 mutation in head and neck squamous cell carcinoma

Farhangdoost, N., Horth, C., Hu, B., Bareke, E., Chen, X., Li, Y., Coradin, M., Garcia, B. A., Lü, C., & Majewski, J. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108769 · Cited by 67

Epigenetic moonlighting: Catalytic-independent functions of histone modifiers in regulating transcription

Morgan, M. A., & Shilatifard, A. (2023) · Science Advances · doi:10.1126/sciadv.adg6593 · Cited by 71

Epigenome environment interactions accelerate epigenomic aging and unlock metabolically restricted epigenetic reprogramming in adulthood

Treviño, L. S., Dong, J., Kaushal, A., Katz, T. A., Jangid, R. K., Robertson, M. J., Grimm, S. L., Ambati, C. R., Putluri, V., Cox, A. R., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15847-z · Cited by 70

Epigenomics of macrophages

Gosselin, D., & Glass, C. K. (2014) · Immunological Reviews · doi:10.1111/imr.12213 · Cited by 66

SET Domain–Containing Protein 4 Epigenetically Controls Breast Cancer Stem Cell Quiescence

Ye, S., Ding, Y.-F., Jia, W.-H., Liu, X., Feng, J., Zhu, Q., Cai, S.-L., Yang, Y.-S., Lu, Q.-Y., Huang, X.-T., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-19-1084 · Cited by 63

Histone Methyltransferases as Therapeutic Targets for Kidney Diseases

Yu, C., & Zhuang, S. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01393 · Cited by 62

Molecular basis for substrate recognition by lysine methyltransferases and demethylases

Rizzo, P. A. D., & Trievel, R. C. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.06.008 · Cited by 61

Role of Epigenetic Regulation in Plasticity of Tumor Immune Microenvironment

Yang, Y., & Wang, Y. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.640369 · Cited by 64

An atypical 12q24.31 microdeletion implicates six genes including a histone demethylase KDM2B and a histone methyltransferase SETD1B in syndromic intellectual disability

Labonne, J. D. J., Lee, K.-H., Iwase, S., Kong, I.-K., Diamond, M. P., Layman, L. C., Kim, C.-H., & Kim, H.-G. (2016) · Human Genetics · doi:10.1007/s00439-016-1668-4 · Cited by 61

Human METTL18 is a histidine-specific methyltransferase that targets RPL3 and affects ribosome biogenesis and function

Małecki, J. M., Odonohue, M.-F., Kim, Y., Jakobsson, M. E., Gessa, L., Pinto, R., Wu, J., Davydova, E., Moen, A., Olsen, J. V., et al. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab088 · Cited by 59

Regulation of eukaryotic elongation factor 1 alpha (eEF1A) by dynamic lysine methylation

Jakobsson, M. E., Małecki, J., & Falnes, P. Ø. (2018) · RNA Biology · doi:10.1080/15476286.2018.1440875 · Cited by 59

Protein methylation in mitochondria

Małecki, J., Davydova, E., & Falnes, P. Ø. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101791 · Cited by 57

Cell cycle-dependent degradation of the methyltransferase SETD3 attenuates cell proliferation and liver tumorigenesis

Cheng, X., Yuan, H., Shu, W., Zhao, M., Zhao, C. N., Wu, Y., Peng, X.-D., Yao, P.-F., Xiao, D., Qing, G., et al. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.778001 · Cited by 54

Chromatin Assembly Factor 1 (CAF-1) facilitates the establishment of facultative heterochromatin during pluripotency exit

Cheng, L., Zhang, X., Wang, Y., Gan, H., Xu, X., Lv, X., Hua, X., Que, J., Ördög, T., & Zhang, Z. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz858 · Cited by 52

Histone methylation in the freeze-tolerant wood frog (Rana sylvatica)

Hawkins, L. J., & Storey, K. B. (2017) · Journal of Comparative Physiology B · doi:10.1007/s00360-017-1112-7 · Cited by 54

METTL21B Is a Novel Human Lysine Methyltransferase of Translation Elongation Factor 1A: Discovery by CRISPR/Cas9 Knockout

Hamey, J. J., Wienert, B., Quinlan, K. G. R., & Wilkins, M. R. (2017) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m116.066308 · Cited by 51

Gastric Cancer in the Era of Epigenetics

Christodoulidis, G., Koumarelas, K., Kouliou, M., Thodou, E., & Samara, M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063381 · Cited by 49

Histone methyltransferases: novel targets for tumor and developmental defects.

Yi, X., Jiang, X., Li, X., & Jiang, D. (2015) · PubMed Central · Cited by 49

Kinetics of Xist -induced gene silencing can be predicted from combinations of epigenetic and genomic featuresPreprint

Sousa, L. B. D. A. E., Jonkers, I. H., Syx, L., Dunkel, I., Chaumeil, J., Picard, C., Forêt, B., Chen, C., Lis, J. T., Heard, É., et al. (2019) · Genome Research · doi:10.1101/gr.245027.118 · Cited by 44

Genome-wide analysis of gene expression and protein secretion of Babesia canis during virulent infection identifies potential pathogenicity factors

Eichenberger, R. M., Ramakrishnan, C., Russo, G., Deplazes, P., & Hehl, A. B. (2017) · Scientific Reports · doi:10.1038/s41598-017-03445-x · Cited by 47

Transcriptional Activity of the Islet β Cell Factor Pdx1 Is Augmented by Lysine Methylation Catalyzed by the Methyltransferase Set7/9

Maganti, A. V., Maier, B., Tersey, S. A., Sampley, M. L., Mosley, A. L., Özcan, S., Pachaiyappan, B., Woster, P. M., Hunter, C. S., Stein, R. W., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.616219 · Cited by 47

A histone H3K9M mutation traps histone methyltransferase Clr4 to prevent heterochromatin spreading

Shan, C., Wang, J., Xu, K., Chen, H., Yue, J., Andrews, S. J., Moresco, J. J., Yates, J. R., Nagy, P. L., Tong, L., et al. (2016) · eLife · doi:10.7554/elife.17903 · Cited by 48

Small-molecule Inhibitors of Lysine Methyltransferases SMYD2 and SMYD3: Current Trends

Fabini, E., Manoni, E., Ferroni, C., Río, A. D., & Bartolini, M. (2019) · Future Medicinal Chemistry · doi:10.4155/fmc-2018-0380 · Cited by 46

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 46

Epigenetic regulation of HIV-1 latency: focus on polycomb group (PcG) proteins

Khan, S., Iqbal, M., Tariq, M., Baig, S. M., & Abbas, W. (2018) · Clinical Epigenetics · doi:10.1186/s13148-018-0441-z · Cited by 46

SDG2-Mediated H3K4me3 Is Crucial for Chromatin Condensation and Mitotic Division during Male Gametogenesis in Arabidopsis

Pinon, V., Yao, X., Dong, A., & Shen, W. (2017) · PLANT PHYSIOLOGY · doi:10.1104/pp.17.00306 · Cited by 42

Dynamic regulation of six histone H3 lysine (K) methyltransferases in response to prolonged anoxia exposure in a freshwater turtle

Wijenayake, S., Hawkins, L. J., & Storey, K. B. (2018) · Gene · doi:10.1016/j.gene.2018.01.086 · Cited by 46

Structural basis for the target specificity of actin histidine methyltransferase SETD3

Dai, S., Horton, J. R., Woodcock, C. B., Wilkinson, A. W., Zhang, X., Gozani, O., & Cheng, X. (2019) · Nature Communications · doi:10.1038/s41467-019-11554-6 · Cited by 42

SET1/MLL family of proteins: functions beyond histone methylation

Sugeedha, J., Gautam, J., & Tyagi, S. (2020) · Epigenetics · doi:10.1080/15592294.2020.1809873 · Cited by 46

Drug Discovery Targeting Nuclear Receptor Binding SET Domain Protein 2 (NSD2)

Ma, Z., Bolinger, A. A., Chen, H., & Zhou, J. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00948 · Cited by 42

A Role for Widely Interspaced Zinc Finger (WIZ) in Retention of the G9a Methyltransferase on Chromatin

Simon, J. M., Parker, J. S., Liu, F., Rothbart, S. B., Ait‐Si‐Ali, S., Strahl, B. D., Jin, J. J., Davis, I. J., Mosley, A. L., & Pattenden, S. G. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.654459 · Cited by 42

Regulation of cell differentiation and function by the euchromatin histone methyltranserfases G9a and GLP

Kramer, J. M. (2015) · Biochemistry and Cell Biology · doi:10.1139/bcb-2015-0017 · Cited by 40

Protein Histidine Methylation

Kwiatkowski, S., & Drożak, J. (2020) · Current Protein and Peptide Science · doi:10.2174/1389203721666200318161330 · Cited by 41

Post-translational modifications are key players of the Legionella pneumophila infection strategy

Michard, C., & Doublet, P. (2015) · Frontiers in Microbiology · doi:10.3389/fmicb.2015.00087 · Cited by 39

SETDB-1: A Potential Epigenetic Regulator in Breast Cancer Metastasis

Batham, J., Lim, P. S., & Rao, S. (2019) · Cancers · doi:10.3390/cancers11081143 · Cited by 39

The lysine methyltransferase Ehmt2/G9a is dispensable for skeletal muscle development and regeneration

Zhang, R., Judson, R. N., Liu, D. Y., Kast, J., & Rossi, F. M. V. (2016) · Skeletal Muscle · doi:10.1186/s13395-016-0093-7 · Cited by 38

Epigenetic regulation and therapeutic targets in the tumor microenvironment

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Saccharomyces cerevisiae Eukaryotic Elongation Factor 1A (eEF1A) Is Methylated at Lys-390 by a METTL21-Like Methyltransferase

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