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

Recently Discovered Ezh2 and Ehmt2 (G9A) Inhibitors

Soumyanarayanan, U., & Dymock, B. W. (2016) · Future Medicinal Chemistry · doi:10.4155/fmc-2016-0096 · Cited by 32

Epigenetic regulators controlling osteogenic lineage commitment and bone formation

Dashti, P., Lewallen, E. A., Gordon, J. A. R., Montecino, M. A., Davie, J., Stein, G. S., van Leeuwen, J. P. T. M., van der Eerden, B. C. J., & van Wijnen, A. J. (2024) · Bone · doi:10.1016/j.bone.2024.117043 · Cited by 32

The nucleophilic amino group of lysine is central for histone lysine methyltransferase catalysis

Temimi, A. H. K. A., Amatdjais‐Groenen, H. I. V., Reddy, Y. V., Blaauw, R. H., Guo, H., Qian, P., & Mecinović, J. (2019) · Communications Chemistry · doi:10.1038/s42004-019-0210-8 · Cited by 31

Epigenetic Regulation of Adipogenesis by Histone-Modifying Enzymes

Macchia, P. E., Nettore, I. C., Franchini, F., Santana-Viera, L., & Ungaro, P. (2021) · Epigenomics · doi:10.2217/epi-2020-0304 · Cited by 30

Integrated Analysis of Genetic Abnormalities of the Histone Lysine Methyltransferases in Prostate Cancer

Zhang, Y., Yan, L., Yao, W., Chen, K., Xu, H., & Ye, Z. (2019) · Medical Science Monitor · doi:10.12659/msm.912294 · Cited by 30

Divergent transcription and epigenetic directionality of human promoters

Lacadie, S. A., Ibrahim, M. M., Gokhale, S., & Ohler, U. (2016) · FEBS Journal · doi:10.1111/febs.13747 · Cited by 28

Lysine methylation by the mitochondrial methyltransferase FAM173B optimizes the function of mitochondrial ATP synthase

Małecki, J., Willemen, H. L. D. M., Pinto, R., Ho, A. Y. Y., Moen, A. R., Kjønstad, I. F., Burgering, B. M. T., Zwartkruis, F. J. T., Eijkelkamp, N., & Falnes, P. Ø. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005473 · Cited by 29

The Autism-Related Protein SETD5 Controls Neural Cell Proliferation through Epigenetic Regulation of rDNA Expression

Nakagawa, T., Hattori, S., Nobuta, R., Kimura, R., Nakagawa, M., Matsumoto, M., Nagasawa, Y., Funayama, R., Miyakawa, T., Inada, T., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101030 · Cited by 27

SETD7 regulates chondrocyte differentiation and glycolysis via the Hippo signaling pathway and HIF‑1α

Li, M., Ning, J., Wang, J., Yan, Q., Zhao, K., & Jia, X. (2021) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2021.5043 · Cited by 27

Human seven-β-strand (METTL) methyltransferases - conquering the universe of protein lysine methylation

Falnes, P. Ø., Małecki, J., Herrera, M. C., Bengtsen, M. B., & Davydova, E. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.104661 · Cited by 27

The expanding role of the Ehmt2/G9a complex in neurodevelopment

Deimling, S. J., Olsen, J. B., & Tropepe, V. (2017) · Neurogenesis · doi:10.1080/23262133.2017.1316888 · Cited by 27

Functional analysis of the methyltransferase SMYD in the single-cell model organism Tetrahymena thermophila

Zhao, X., Li, Y., Duan, L., Chen, X., Mao, F., Juma, M., Liu, Y., SONG, W. B., & Gao, S. (2020) · Marine Life Science & Technology · doi:10.1007/s42995-019-00025-y · Cited by 25

Genomic Alterations of Dermatofibrosarcoma Protuberans Revealed by Whole Genome Sequencing

Peng, C., Jian, X., Xie, Y., Li, L., Ouyang, J., Tang, L. Y., Zhang, X., Su, J., Zhao, S., Liu, H., et al. (2021) · British Journal of Dermatology · doi:10.1111/bjd.20976 · Cited by 26

The complexity of epigenetic diseases

Brazel, A. J., & Vernimmen, D. (2015) · The Journal of Pathology · doi:10.1002/path.4647 · Cited by 25

Biochemical perspectives on targeting KMT2 methyltransferases in cancer

Zhai, X., & Brownell, J. E. (2021) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2021.05.002 · Cited by 24

Phylogenetic profiling resolves early emergence of PRC2 and illuminates its functional core

Sharaf, A., Vijayanathan, M., Obornı́k, M., & Mozgová, I. (2022) · Life Science Alliance · doi:10.26508/lsa.202101271 · Cited by 25

Lysine Methyltransferases Signaling: Histones are Just the Tip of the Iceberg

Lukinović, V., Casanova, A. G., Roth, G. S., Chuffart, F., & Reynoird, N. (2020) · Current Protein and Peptide Science · doi:10.2174/1871527319666200102101608 · Cited by 22

Efficient differentiation of murine embryonic stem cells requires the binding of CXXC finger protein 1 to DNA or methylated histone H3-Lys4

Mahadevan, J., & Skalnik, D. G. (2016) · Gene · doi:10.1016/j.gene.2016.08.048 · Cited by 24

Quantitative analysis of global protein lysine methylation by mass spectrometry

Lund, P. J., Lehman, S. M., & Garcia, B. A. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.07.036 · Cited by 23

The methyltransferase SETD3-mediated histidine methylation: Biological functions and potential implications in cancers

Shu, W., & Du, H. (2020) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2020.188465 · Cited by 23

Role of NSD1 as potential therapeutic target in tumor

Yang, C., Wang, K., Liang, Q., Tian, T., & Zhong, Z. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105888 · Cited by 23

Repressive histone methylation: A case study in deterministic versus stochastic gene regulation

Lyons, D. B., & Lomvardas, S. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.05.010 · Cited by 23

Barrier-to-Autointegration Factor 1 (BAF/BANF1) Promotes Association of the SETD1A Histone Methyltransferase with Herpes Simplex Virus Immediate-Early Gene Promoters

Oh, H. S., Traktman, P., & Knipe, D. M. (2015) · mBio · doi:10.1128/mbio.00345-15 · Cited by 22

HIRA-mediated loading of histone variant H3.3 controls androgen-induced transcription by regulation of AR/BRD4 complex assembly at enhancers

Morozov, V. M., Riva, A., Sarwar, S., Kim, W.-J., Li, J., Zhou, L. J., Licht, J. D., Daaka, Y., & Ishov, A. M. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad700 · Cited by 24

Intrinsic protein disorder in histone lysine methylation

Lázár, T., Schád, É., Szabó, B., Horváth, T., Mészáros, A., Tompa, P., & Tantos, Á. (2016) · Biology Direct · doi:10.1186/s13062-016-0129-2 · Cited by 21

KMT1 family methyltransferases regulate heterochromatin–nuclear periphery tethering via histone and non‐histone protein methylation

Rao, R. A., Ketkar, A. A., Kedia, N., Krishnamoorthy, V. K., Lakshmanan, V., Kumar, P., Mohanty, A., Kumar, S. D., Raja, S. O., Gulyani, A., et al. (2019) · EMBO Reports · doi:10.15252/embr.201643260 · Cited by 21

Histone Methyltransferase SETDB1 Promotes Immune Evasion in Colorectal Cancer via FOSB-Mediated Downregulation of MicroRNA-22 through BATF3/PD-L1 Pathway

Tian, J., Wang, W., Zhu, J., Zhuang, Y., Qi, C., Cai, Z., Yan, W., Lu, W., & Shang, A. (2022) · Journal of Immunology Research · doi:10.1155/2022/4012920 · Cited by 20

Recent Advances in Glioma Cancer Treatment: Conventional and Epigenetic Realms

Fath, M. K., Babakhaniyan, K., Anjomrooz, M., Jalalifar, M.-R., Alizadeh, S. D., Pourghasem, Z., Oshagh, P. A., Azargoonjahromi, A., Almasi, F., Manzoor, H. Z., et al. (2022) · Vaccines · doi:10.3390/vaccines10091448 · Cited by 23

Histone Modifications in Acute Kidney Injury

Wang, J., Shen, F., Liu, F., & Zhuang, S. (2022) · Kidney Diseases · doi:10.1159/000527799 · Cited by 23

Comparative genomic analysis of SET domain family reveals the origin, expansion, and putative function of the arthropod-specific SmydA genes as histone modifiers in insects

Jiang, F., Liu, Q. F., Wang, Y., Zhang, J., Wang, H., Song, T., Yang, M., Wang, X., & Kang, L. (2017) · GigaScience · doi:10.1093/gigascience/gix031 · Cited by 20

Multiple levels of epigenetic control for bone biology and pathology

Montecino, M. A., Stein, G., Stein, J. L., Zaidi, K., & Aguilar, R. (2015) · Bone · doi:10.1016/j.bone.2015.03.013 · Cited by 20

Molecular Evolution of the Substrate Specificity of Chloroplastic Aldolases/Rubisco Lysine Methyltransferases in Plants

Ma, S., Martin‐Laffon, J., Mininno, M., Gigarel, O., Brugière, S., Bastien, O., Tardif, M., Ravanel, S., & Alban, C. (2016) · Molecular Plant · doi:10.1016/j.molp.2016.01.003 · Cited by 20

Intestinal Epithelial Cell-Intrinsic Deletion of Setd7 Identifies Role for Developmental Pathways in Immunity to Helminth Infection

Oudhoff, M. J., Antignano, F., Chenery, A., Burrows, K., Redpath, S. A., Braam, M. J. S., Perona‐Wright, G., & Zaph, C. (2016) · PLoS Pathogens · doi:10.1371/journal.ppat.1005876 · Cited by 20

CRISPR single base editing, neuronal disease modelling and functional genomics for genetic variant analysis: pipeline validation using Kleefstra syndrome EHMT1 haploinsufficiency

Fear, V. S., Forbes, C. A., Anderson, D. R., Rauschert, S., Syn, G., Shaw, N. C., Jamieson, S. E., Ward, M., Baynam, G. S., & Lassmann, T. (2022) · Stem Cell Research & Therapy · doi:10.1186/s13287-022-02740-3 · Cited by 19

KMT2C Induced by FABP5P3 Aggravates Keratinocyte Hyperproliferation and Psoriasiform Skin Inflammation by Upregulating the Transcription of PIK3R3

Huang, S., Zhen, Y., Yin, X., Yang, Z., Li, X., Wang, R., Wen, H., Zhong, H., Yan, J., & Sun, Q. (2022) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2022.06.025 · Cited by 19

Closing in on human methylation—the versatile family of seven-β-strand (METTL) methyltransferases

Falnes, P. Ø. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae816 · Cited by 20

Environmental influences on the epigenomes of herpetofauna and fish

Hammond, S. A., Nelson, C. J., & Helbing, C. C. (2015) · Biochemistry and Cell Biology · doi:10.1139/bcb-2015-0111 · Cited by 19

SET domain‐containing protein 5 is required for expression of primordial germ cell specification‐associated genes in murine embryonic stem cells

Yu, S. E., Kim, M. S., Park, S. H., Yoo, B., Kim, K.-H., & Jang, Y. (2017) · Cell Biochemistry and Function · doi:10.1002/cbf.3269 · Cited by 13

Chromatin‐modifying drugs and metabolites in cell fate control

Yao, Z., Chen, Y., Cao, W., & Shyh‐Chang, N. (2020) · Cell Proliferation · doi:10.1111/cpr.12898 · Cited by 18

Transcription factors, chromatin proteins and the diversification of Hemiptera

Vidal, N. M., Grazziotin, A. L., Iyer, L. M., Aravind, L., & Venâncio, T. M. (2015) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2015.07.001 · Cited by 19

γ-Thialysine versus Lysine: An Insight into the Epigenetic Methylation of Histones

Temimi, A. H. K. A., Bruijne, R. V. D. W.-D., Proietti, G., Guo, H., Qian, P., & Mecinović, J. (2019) · Bioconjugate Chemistry · doi:10.1021/acs.bioconjchem.9b00313 · Cited by 18

The epigenetic players and the chromatin marks involved in the articular cartilage during osteoarthritis

Lafont, J. E., Moustaghfir, S., Durand, A.-L., & Mallein‐Gérin, F. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1070241 · Cited by 18

The Interplay between Dysregulated Metabolism and Epigenetics in Cancer

Bassal, M. A. (2023) · Biomolecules · doi:10.3390/biom13060944 · Cited by 19

Epigenetics of Schizophrenia

Gavin, D. P., & Floreani, C. V. (2014) · International review of neurobiology · doi:10.1016/b978-0-12-801311-3.00005-6 · Cited by 17

Identification and Characterizations of Novel, Selective Histone Methyltransferase SET7 Inhibitors by Scaffold Hopping- and 2D-Molecular Fingerprint-Based Similarity Search

Ding, H., Lu, W., Hu, J., Liu, Y., Zhang, C., Lian, F., Zhang, N., Meng, F., Luo, C., & Chen, K. (2018) · Molecules · doi:10.3390/molecules23030567 · Cited by 18

Genetic alteration of histone lysine methyltransferases and their significance in renal cell carcinoma

Yan, L., Zhang, Y., Ding, B., Zhou, H., Yao, W., & Xu, H. (2019) · PeerJ · doi:10.7717/peerj.6396 · Cited by 18

SETD1A Methyltransferase Is Physically and Functionally Linked to the DNA Damage Repair Protein RAD18

Alsulami, M., Munawar, N., Dillon, E., Oliviero, G., Wynne, K. J., Alsolami, M., Moss, C., Gaora, P. Ó., O’Meara, F., Cotter, D., et al. (2019) · Molecular & Cellular Proteomics · doi:10.1074/mcp.ra119.001518 · Cited by 18

Detecting genomic variation underlying phenotypic characteristics of reintroduced Coho salmon (Oncorhynchus kisutch)

Horn, R. L., Kamphaus, C. M., Murdoch, K., & Narum, S. R. (2020) · Conservation Genetics · doi:10.1007/s10592-020-01307-0 · Cited by 18

The Structure, Activity, and Function of the SETD3 Protein Histidine Methyltransferase

Witecka, A., Kwiatkowski, S., Ishikawa, T., & Drożak, J. (2021) · Life · doi:10.3390/life11101040 · Cited by 18

Epigenomic Analysis in a Cell-Based Model Reveals the Roles of H3K9me3 in Breast Cancer Transformation

Li, Q., Lei, P., Zhao, Q., Li, L., Wei, G., & Wu, M. (2017) · Epigenomics · doi:10.2217/epi-2016-0183 · Cited by 18

Histone Methyltransferases Useful in Gastric Cancer Research

Reyes, D. A., Sarriá, V. M. S., Salazar-Viedma, M., & D’Afonseca, V. (2021) · Cancer Informatics · doi:10.1177/11769351211039862 · Cited by 17

The functions and roles of C2H2 zinc finger proteins in hepatocellular carcinoma

Li, Q., Guoqian, T., & Wu, F. (2023) · Frontiers in Physiology · doi:10.3389/fphys.2023.1129889 · Cited by 17

Importance of the main chain of lysine for histone lysine methyltransferase catalysis

Temimi, A. H. K. A., Teeuwen, R. S., Tran, V., Altunc, A. J., Lenstra, D. C., Ren, W.-S., Qian, P., Guo, H., & Mecinović, J. (2019) · Organic & Biomolecular Chemistry · doi:10.1039/c9ob01038f · Cited by 17

Computational analyses on genetic alterations in the NSD genes family and the implications for colorectal cancer development

D’Afonseca, V., González, G., Salazar, M., & Arencibia, A. D. (2020) · ecancermedicalscience · doi:10.3332/ecancer.2020.1001 · Cited by 17

Comparative Gene Analysis Focused on Silica Cell Wall Formation: Identification of Diatom-Specific SET Domain Protein Methyltransferases

Nemoto, M., Iwaki, S., Moriya, H., Monden, Y., Tamura, T., Inagaki, K., Mayama, S., & Obuse, K. (2020) · Marine Biotechnology · doi:10.1007/s10126-020-09976-1 · Cited by 15

Catalytic inhibition of H3K9me2 writers disturbs epigenetic marks during bovine nuclear reprogramming

Sampaio, R. V., Sangalli, J. R., De, T. H. C., Ambrizi, D. R., del Collado, M., Bridi, A., de Ávila, A. C. F. C. M., Macabelli, C. H., Oliveira, L. J., da Silveira, J. C., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-67733-9 · Cited by 17

Protein Lysine Methyltransferase SMYD2: A Promising Small Molecule Target for Cancer Therapy

Zheng, Q., Zhang, W., & Rao, G.-W. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00325 · Cited by 16

NSD2 as a Promising Target in Hematological Disorders

Azagra, A., & Cobaleda, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911075 · Cited by 16

The lysine methyltransferases SET and MYND domain containing 2 (Smyd2) and Enhancer of Zeste 2 (Ezh2) co-regulate osteoblast proliferation and mineralization

Dashti, P., van de Peppel, J., Thaler, R., Paradise, C. R., Stein, G. S., Montecino, M. A., van Leeuwen, J. P. T. M., van der Eerden, B. C. J., Dudakovic, A., & van Wijnen, A. J. (2022) · Gene · doi:10.1016/j.gene.2022.146928 · Cited by 16

Arabidopsis thaliana: a powerful model organism to explore histone modifications and their upstream regulations

Yang, Y. P., Wang, S., Wang, Z., Gao, R., & Lee, J. (2023) · Epigenetics · doi:10.1080/15592294.2023.2211362 · Cited by 17

A de novo missense variant in EZH1 associated with developmental delay exhibits functional deficits in Drosophila melanogaster

Jangam, S. V., Briere, L. C., Jay, K. L., Andrews, J. C., Walker, M., Rodan, L. H., High, F. A., Undiagnosed Diseases Network, Yamamoto, S., Sweetser, D. A., et al. (2023) · Genetics · doi:10.1093/genetics/iyad110 · Cited by 14

The METTL20 Homologue from Agrobacterium tumefaciens Is a Dual Specificity Protein-lysine Methyltransferase That Targets Ribosomal Protein L7/L12 and the β Subunit of Electron Transfer Flavoprotein (ETFβ)

Małecki, J., Dahl, H.-A., Moen, A. R., Davydova, E., & Falnes, P. Ø. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.709261 · Cited by 16

Lead discovery, chemical optimization, and biological evaluation studies of novel histone methyltransferase SET7 small-molecule inhibitors

Hou, Z., Min, W., Zhang, R., Niu, A., Li, Y., Cao, L., Han, J., Luo, C., Yang, P., & Ding, H. (2020) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2020.127061 · Cited by 16

Functional validation of variants of unknown significance using CRISPR gene editing and transcriptomics: A Kleefstra syndrome case study

Fear, V. S., Forbes, C. A., Anderson, D. R., Rauschert, S., Syn, G., Shaw, N. C., Jones, M., Forrest, A. R. R., Baynam, G. S., & Lassmann, T. (2022) · Gene · doi:10.1016/j.gene.2022.146287 · Cited by 16

The SET-domain protein CgSet4 negatively regulates antifungal drug resistance via the ergosterol biosynthesis transcriptional regulator CgUpc2a

Bhakt, P., Raney, M., & Kaur, R. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102485 · Cited by 17

SETDB1 Triple Tudor Domain Ligand, ( R , R )-59, Promotes Methylation of Akt1 in Cells

Uguen, M., Deng, Y., Li, F., Shell, D. J., Norris-Drouin, J. L., Stashko, M. A., Ackloo, S. Z., Arrowsmith, C. H., James, L. I., Liu, P., et al. (2023) · ACS Chemical Biology · doi:10.1021/acschembio.3c00280 · Cited by 15

Hsp70 (HSPA1) Lysine Methylation Status as a Potential Prognostic Factor in Metastatic High-Grade Serous Carcinoma

Jakobsson, M. E., Moen, A. R., Davidson, B., & Falnes, P. Ø. (2015) · PLoS ONE · doi:10.1371/journal.pone.0140168 · Cited by 15

Therapeutic targeting of chromatin alterations in leukemia and solid tumors

Perner, F., Berg, T., Sasca, D., Mersiowsky, S., Gadrey, J. Y., Thomas, J. M., Kühn, M. W. M., & Lübbert, M. (2025) · International Journal of Cancer · doi:10.1002/ijc.35389 · Cited by 16

Identification of Novel Potent NSD2-PWWP1 Ligands Using Structure-Based Design and Computational Approaches

Carlino, L., Astles, P. C., Ackroyd, B., Ahmed, A., Chan, C., Collie, G. W., Dale, I. L., O’Donovan, D. H., Fawcett, C. H., Fruscia, P. D., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00215 · Cited by 16

Lysine Ethylation by Histone Lysine Methyltransferases

Temimi, A. H. K. A., Martin, M., Meng, Q., Lenstra, D. C., Qian, P., Guo, H., Weinhold, E. G., & Mecinović, J. (2019) · ChemBioChem · doi:10.1002/cbic.201900359 · Cited by 14

Sodium Valproate Modulates the Methylation Status of Lysine Residues 4, 9 and 27 in Histone H3 of HeLa Cells

Mello, M. L. S., Rocha, M. A., & Vidal, B. D. C. (2022) · Current Molecular Pharmacology · doi:10.2174/1874467215666220316110405 · Cited by 13

Cytoplasmic localization of SETDB1‑induced Warburg effect via c‑MYC‑LDHA axis enhances migration and invasion in breast carcinoma

Yang, W., Wei, Y., Wang, T., Xu, Y. X., Jin, X., Qian, H., Yang, S., & He, S. (2024) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2024.5364 · Cited by 13

The protein methylation network in yeast: A landmark in completeness for a eukaryotic post-translational modification

Hamey, J. J., & Wilkins, M. R. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2215431120 · Cited by 13

Insights into the Action of Inhibitor Enantiomers against Histone Lysine Demethylase 5A

Horton, J. R., Liu, X., Wu, L., Zhang, K., Shanks, J. R., Zhang, X., Rai, G., Mott, B. T., Jansen, D. J., Kales, S. C., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00261 · Cited by 13

SETD5 modulates homeostasis of hematopoietic stem cells by mediating RNA Polymerase II pausing in cooperation with HCF-1

Li, M., Qiu, C., Bian, Y., Shi, D., Wang, B., Ma, Q., Wang, X., Shi, J., Zhang, L., Ma, Y., et al. (2021) · Leukemia · doi:10.1038/s41375-021-01481-1 · Cited by 15

Lysine methyltransferase 5C increases the proliferation and metastatic abilities of clear cell renal cell carcinoma via aerobic glycolysis

Zeng, B., Wan, R., Chang, K. S., Li, J., Zhang, X., Shi, G., Ye, D., & Xu, F. (2024) · International Journal of Oncology · doi:10.3892/ijo.2024.5633 · Cited by 12

Discovery of a Highly Potent and Selective Inhibitor Targeting Protein Lysine Methyltransferase NSD2

Wei, J., Shi, Q., Li, B., Yang, H. J., Liu, L., Zhou, R., Feng, Z., Yang, Z., Zhan, J., Xiong, X., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00639 · Cited by 12

The function of histone methyltransferase SETDB1 and its roles in liver cancer

Zhang, E., & He, P. (2024) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2024.1500263 · Cited by 11

Poly ADP-ribosylation of SET8 leads to aberrant H4K20 methylation in mammalian nuclear genome

Estève, P., Sen, S., Vishnu, U. S., Ruse, C. I., Chin, H. G., & Pradhan, S. (2022) · Communications Biology · doi:10.1038/s42003-022-04241-8 · Cited by 11

Function of the MYND Domain and C-Terminal Region in Regulating the Subcellular Localization and Catalytic Activity of the SMYD Family Lysine Methyltransferase Set5

Jaiswal, D., Turniansky, R., Moresco, J. J., Ikram, S., Ramaprasad, G., Akinwole, A., Wolf, J. B., Yates, J. R., & Green, E. M. (2019) · Molecular and Cellular Biology · doi:10.1128/mcb.00341-19 · Cited by 13

Euchromatin histone methyltransferase II (EHMT2) regulates the expression of ras-related GTP binding C (RRAGC) protein

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