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

Phenotypic characterization of SETD3 knockout Drosophila

Tiebe, M., Lutz, M., Levy, D., & Teleman, A. A. (2018) · PLoS ONE · doi:10.1371/journal.pone.0201609 · Cited by 7

Methylation of elongation factor 1A by yeast Efm4 or human eEF1A-KMT2 involves a beta-hairpin recognition motif and crosstalks with phosphorylation

Hamey, J. J., Nguyen, A., Haddad, M., Vázquez-Campos, X., Pfeiffer, P. G., & Wilkins, M. R. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105639 · Cited by 6

Functions of SETD7 during development, homeostasis and cancer

Soshnikova, N. V. (2019) · Stem Cell Investigation · doi:10.21037/sci.2019.06.10 · Cited by 7

Cascading proton transfers are a hallmark of the catalytic mechanism of SAM‐dependent methyltransferases

Zhao, L. N., & Kaldis, P. (2020) · FEBS Letters · doi:10.1002/1873-3468.13799 · Cited by 7

Identification of substrates and sequence requirements for CARNMT1-mediated histidine methylation of C3H zinc fingers

Małecki, J., Weirich, S., Ramírez‐Garrastacho, M., Hagen, L., Al-Egly, J., Anonsen, J. H., Schroer, L., Herrera, M. C., Davydova, E., Slupphaug, G., et al. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.110335 · Cited by 6

The SET7 protein of Leishmania donovani moderates the parasite’s response to a hostile oxidative environment

Pal, J., Sharma, V., Khanna, A., & Saha, S. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.105720 · Cited by 6

GLP and G9a histone methyltransferases as potential therapeutic targets for lymphoid neoplasms

Silva-Carvalho, A. É., Filiú-Braga, L. D. D. C., Bogéa, G. M. R., de Assis, A. J. B., Pittella-Silva, F., & Saldanha‐Araújo, F. (2024) · Cancer Cell International · doi:10.1186/s12935-024-03441-y · Cited by 6

EHMT1/GLP; Biochemical Function and Association with Brain Disorders

Adam, M. A., & Isles, A. R. (2017) · Epigenomes · doi:10.3390/epigenomes1030015 · Cited by 6

Intestinal NSD2 Aggravates Nonalcoholic Steatohepatitis Through Histone Modifications

Zhang, Y., Qiao, Y., Li, Z., Liu, D., Jin, Q., Guo, J., Li, X., Chen, L., Liu, L., & Peng, L. (2024) · Advanced Science · doi:10.1002/advs.202402551 · Cited by 6

Tumor suppressors in follicular lymphoma

Graham, C., & LeBrun, D. P. (2014) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428194.2014.982638 · Cited by 6

Identification and functional characterization of lysine methyltransferases of Entamoeba histolytica

Borbolla‐Vázquez, J., Orozco, E., Medina‐Gómez, C., Martínez‐Higuera, A., Javier‐Reyna, R., Chávez, B., Betanzos, A., & Rodríguez, M. A. (2016) · Molecular Microbiology · doi:10.1111/mmi.13394 · Cited by 6

Structural Analysis of SMYD3 Lysine Methyltransferase for the Development of Competitive and Specific Enzyme Inhibitors

Jarrell, D. K., Hassell, K. N., Alshiraihi, I., Crans, D. C., & Brown, M. A. (2021) · Diseases · doi:10.3390/diseases10010004 · Cited by 6

The methyltransferase SETD3 regulates mRNA alternative splicing through interacting with hnRNPK

Kong, Y., Shu, W., Wang, S., Yin, Z.-H., Duan, H., Li, K., & Du, H. (2024) · Cell Insight · doi:10.1016/j.cellin.2024.100198 · Cited by 5

Set2‐mediated H3K36 methylation states redundantly repress the production of antisense transcripts: role in transcription regulation

Mei, Y.-C., Feng, J., He, F., Li, Y., Liu, Y., Li, F., Chen, Y. Z., & Du, H. (2021) · FEBS Open Bio · doi:10.1002/2211-5463.13226 · Cited by 5

Epigenetics in intellectual disability

Jakub, T. E., Quesnel, K., Keung, C., Bérubé, N. G., & Kramer, J. M. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-823577-5.00030-1 · Cited by 5

Genetic Biodiversity and Posttranslational Modifications of Protease Serine Endopeptidase in Different Strains of Sordaria fimicola

Naureen, U., Khosa, A. N., Mukhtar, M. A., Nabi, F., Ahmed, N., & Saleem, M. (2023) · BioMed Research International · doi:10.1155/2023/2088988 · Cited by 5

The SET29 and SET7 proteins of Leishmania donovani exercise non-redundant convergent as well as collaborative functions in moderating the parasite’s response to oxidative stress

Sharma, V., Pal, J., Dashora, V., Chattopadhyay, S., Kapoor, Y., Singha, B., Arimbasseri, G. A., & Saha, S. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108208 · Cited by 5

Preparation, Biochemical Analysis, and Structure Determination of SET Domain Histone Methyltransferases

Bergamin, E., & Couture, J. F. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.01.004 · Cited by 5

Epigenetics and Cancer

Kelly, A. D., & Issa, J. J. (2016) · Energy balance and cancer · doi:10.1007/978-3-319-41610-6_1 · Cited by 5

Translational Pharmacokinetic-Pharmacodynamic Modeling for an Orally Available Novel Inhibitor of Epigenetic Regulator Enhancer of Zeste Homolog 2

Yamazaki, S., Gukasyan, H. J., Wang, H., Uryu, S. A., & Sharma, S. (2020) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.119.263491 · Cited by 5

The role of histone methylation in renal cell cancer: an update

Hou, Y., Yuan, Y., Li, Y., Wang, L., Hu, J., & Liu, X. (2022) · Molecular Biology Reports · doi:10.1007/s11033-022-08124-3 · Cited by 5

Aberrant histone modifications in pediatric brain tumors

Hamanishi, E. T., Dang, D., & Venneti, S. (2025) · Frontiers in Oncology · doi:10.3389/fonc.2025.1587157 · Cited by 4

Treatability of the KMT2-Associated Neurodevelopmental Disorders Using Antisense Oligonucleotide-Based Treatments

Zardetto, B., van Roon‐Mom, W., Aartsma-Rus, A. M., & Lauffer, M. C. (2024) · Human Mutation · doi:10.1155/2024/9933129 · Cited by 4

In silico analysis of RNA interference components and miRNAs-like RNAs in the seed-borne necrotrophic fungus Alternaria brassicicola

Kwasiborski, A., Bastide, F., Hamon, B., Poupard, P., Simoneau, P., & Guillemette, T. (2021) · Fungal Biology · doi:10.1016/j.funbio.2021.12.004 · Cited by 4

Determination of Histone Methyltransferase Structure by Crystallography

Wilson, J. R. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2481-4_7 · Cited by 4

Cell consequences of loss of function of the epigenetic factor EHMT1

Iglesias-Ortega, L., Megías-Fernández, C., Domínguez-Giménez, P., Jimeno-González, S., & Rivero, S. (2023) · Cellular Signalling · doi:10.1016/j.cellsig.2023.110734 · Cited by 4

Reprogramming host histone modifications by bacterial pathogens

Zelikman, S., Yi, S.-J., & Kim, K. (2026) · Molecules and Cells · doi:10.1016/j.mocell.2026.100321 · Cited by 4

Targeting the Tumor Epigenetic Regulator SETDB1 for Tumor Therapy

Peng, C. Y., Zhou, N., Chen, T., Lei, J., Chen, C., & Zhu, S. (2024) · Current Cancer Drug Targets · doi:10.2174/0115680096311909240721160523 · Cited by 2

Epigenetic Enzymes and Drawbacks of Conventional Therapeutic Regimens

Ganai, S. A. (2019) · Springer eBooks · doi:10.1007/978-981-13-8019-8_2 · Cited by 3

Methyltransferase SET domain family and its relationship with cardiovascular development and diseases

Xing, J., & Jie, W. (2022) · Journal of Zhejiang University (Medical Sciences) · doi:10.3724/zdxbyxb-2021-0192 · Cited by 3

Zebrafish SETD3 mediated ubiquitination of phosphoprotein limits spring viremia of carp virus infection

Zhao, X., Ji, N., Guo, J., Huang, W., Feng, J., Shi, Y., Chen, K., Wang, J., & Zou, J. (2023) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2023.108870 · Cited by 3

Hungry for control: metabolite signaling to chromatin in Plasmodium falciparum

Lappalainen, R., Kumar, M., & Duraisingh, M. T. (2024) · Current Opinion in Microbiology · doi:10.1016/j.mib.2024.102430 · Cited by 3

Doctor of Philosophy (PhD)

Biss, M. (2015) · Cited by 3

Identification of SETD4 as an Onco‐Immunological Biomarker Encompassing the Tumor Microenvironment, Prognoses, and Therapeutic Responses in Various Human Cancers

Zhong, Y., Wang, R., Huang, Z., Hu, Z., Peng, B., Chen, B., & Sun, L. (2025) · Immunity Inflammation and Disease · doi:10.1002/iid3.70126 · Cited by 2

Yet to SET: Plasmodium falciparum Histone Lysine Methyltransferases

Shah, D., & Karmodiya, K. (2025) · ACS Infectious Diseases · doi:10.1021/acsinfecdis.5c00578 · Cited by 2

Elucidating the Molecular Basis of Thermal Stress Response in Juvenile Turbot (Scophthalmus maximus) via an Integrative Transcriptome–Metabolome Approach

Chen, X., Gao, T., Wang, Z., Chen, S., Zhang, N., Zhang, X., & Jia, Y. (2025) · Biology · doi:10.3390/biology14101413 · Cited by 2

Depleting CBR1 increases chemosensitivity by reducing stemness and quiescence traits in non-small cell lung cancer

Li, W., Zhao, J., Lan, W., Ye, X., & Ying, K. (2025) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b2400509 · Cited by 2

TaHST2 silencing shapes basal heat tolerance in allohexaploid wheat

Zhang, R., Liu, G., Zhai, S., Meng, X., Yu, J., Zhang, Y., Wen, S., Luo, X., Han, W., Lou, H., et al. (2026) · Nature Plants · doi:10.1038/s41477-026-02257-0 · Cited by 2

Update of the Methyltransferase Gene Family: Classification, Evolution and Biological Functions

Katsafadou, A. I., Falnes, P. Ø., Bruford, E. A., Braschi, B., Hanson, Q., Hall, M. D., Thompson, D. C., Nebert, D. W., & Vasiliou, V. (2026) · Human Genomics · doi:10.1186/s40246-026-00949-4 · Cited by 3

Metabolic Deregulations Affecting Chromatin Architecture: One-Carbon Metabolism and Krebs Cycle Impact Histone Methylation

Saavedra, F., Boyarchuk, E., Alvarez, F., Almouzni, G., & Loyola, A. (2019) · RNA technologies · doi:10.1007/978-3-030-14792-1_23 · Cited by 2

Histone Modifying Enzymes as Targets for Therapeutic Intervention in Oesophageal Adenocarcinoma

Pickering, O. J., Breininger, S. P., Underwood, T., & Walters, Z. S. (2021) · Cancers · doi:10.3390/cancers13164084 · Cited by 2

Not all Is SET for Methylation: Evolution of Eukaryotic Protein Methyltransferases

Erlendson, A. A., & Freitag, M. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2481-4_1 · Cited by 2

Unmasking the mammalian SET domain-containing protein 4

Wang, Y., & Shen, Z. (2022) · NAR Cancer · doi:10.1093/narcan/zcac021 · Cited by 2

Nuclear Morphofunctional Organization and Epigenetic Characteristics in Somatic Cells of T. infestans (Klug, 1834)

Mello, M. L. S. (2023) · Pathogens · doi:10.3390/pathogens12081030 · Cited by 1

Comparative transcriptome and methylome of polar bears, giant and red pandas reveal diet‐driven adaptive evolution

Chen, L., Ma, J., Xu, W., Shen, F., Yang, Z., Sonne, C., Dietz, R., Li, L., Jie, X., Li, L., et al. (2024) · Evolutionary Applications · doi:10.1111/eva.13731 · Cited by 2

Role of SMYD2 in gastrointestinal cancer progression (Review)

Xia, K., Zhou, Y., Xie, Y., & Cai, Y. (2025) · Oncology Letters · doi:10.3892/ol.2025.15028 · Cited by 2

A System for Enzymatic Lysine Methylation in a Desired Sequence Context

Aileni, V. K., Davydova, E., Moen, A. R., & Falnes, P. Ø. (2017) · ACS Omega · doi:10.1021/acsomega.6b00486 · Cited by 2

Cloning, expression, purification and crystallization ofSchizosaccharomyces pombeSet7, a putative histone methyltransferase

Mevius, D. E. H. F., Shen, Y., Morishita, M., & di Luccio, E. (2016) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x16003794 · Cited by 2

Epigenetics in Intellectual Disability

Bérubé, N. G., & Kramer, J. M. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-417114-5.00018-8 · Cited by 2

Structure‐Based Drug Design

Ferreira, L. L. G., & Andricopulo, A. D. (2021) · Wiley eBooks · doi:10.1002/0471266949.bmc141.pub2 · Cited by 2

Epigenome dysregulation resulting from NSD1 mutation in head and neck squamous cell carcinomaPreprint

Farhangdoost, N., Horth, C., Hu, B., Bareke, E., Chen, X., Li, Y., Coradin, M., Garcia, B. A., Lü, C., & Majewski, J. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.05.30.124057 · Cited by 2

Phylogenetic profiling suggests early origin of the core subunits of Polycomb Repressive Complex 2 (PRC2)Preprint

Sharaf, A., Vijayanathan, M., Oborník, M., & Mozgová, I. (2021) · bioRxiv · doi:10.1101/2021.07.16.452543 · Cited by 3

Setdb2 Regulates Inflammatory Trigger-Induced Trained Immunity of Macrophages Through Two Different Epigenetic MechanismsPreprint

Osborne, T. F., Jaiswal, A., Halász, L., & Williams, D. L. (2025) · Research Square · doi:10.21203/rs.3.rs-6702384/v1 · Cited by 2

Epigenetic Enzymes and Their Mutations in Cancer

Dalmızrak, A., & Dalmızrak, Ö. (2023) · Epigenetics and human health · doi:10.1007/978-3-031-42365-9_2 · Cited by 1

Silencing PsASH2 affects embryo development in the cotton mealybug

Wang, K., Zen, L., Sheng, L., Lü, F., Lin, Q., Li, Y., & Tong, H. (2025) · Insect Molecular Biology · doi:10.1111/imb.13003 · Cited by 1

Alpha-centractin is a novel substrate of SETD3 methyltransferase in vitro

Witecka, A., Emmel, P., Ślusarczyk, K., Kamińska, J. Z., Zaród, M., Ishikawa, T., & Drożak, J. (2025) · PeerJ · doi:10.7717/peerj.20195 · Cited by 1

Comparative Genomics of the Endosymbiont Cardinium Causing Reproductive Manipulation in Encarsia Parasitoid Wasps

Schultz, D. L., Stouthamer, C. M., Kelly, S. E., Mathieson, O. L., Kleiner, M., Hunter, M. S., & Schmitz‐Esser, S. (2025) · MicrobiologyOpen · doi:10.1002/mbo3.70084 · Cited by 1

Kmt2c/Mll3 Haploinsufficiency Causes Autism-like Behavioral Deficits in Mice

Ma, K., Webb, M., Hayder, H., & Qin, L. (2025) · Biomolecules · doi:10.3390/biom15111547 · Cited by 1

A unified therapeutic theory for treating cancer via master regulators of the universal apoptosis network

Joseph, D., Kongoli, F., You, F., & Inufusa, H. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-03066-2 · Cited by 2

Emerging Epigenetic Therapies—Lysine Methyltransferase/PRC Complex Inhibitors

Pande, V., Pocalyko, D. J., & Dhanak, D. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800206-3.00019-7 · Cited by 1

Inhibitors of Jumonji C-Domain Histone Demethylases

Staller, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800206-3.00020-3 · Cited by 1

Implications for Chromatin Biology in Toxicology

Katz, T. A., & Walker, C. L. (2018) · Elsevier eBooks · doi:10.1016/b978-0-12-812433-8.00004-6 · Cited by 1

Oncogene: An epigenetic regulation

Nagaraja, S. S., & Nagarajan, D. (2021) · Elsevier eBooks · doi:10.1016/b978-0-323-85652-2.00017-8 · Cited by 2

Therapeutic Targeting of the Regulators of Cancer Epigenomes

Al-Janabi, I. I. (2023) · Al-Rafidain Journal of Medical Sciences · doi:10.54133/ajms.v5i.128 · Cited by 1

Histone modifications

Morse, R. H. (2024) · Elsevier eBooks · doi:10.1016/b978-0-12-814809-9.00002-0 · Cited by 1

The role of CFP1 in murine embryonic stem cell function and liver regeneration

Mahadevan, J. (2015) · IUScholarWorks (Indiana University) · doi:10.7912/c2/1897 · Cited by 1

Selective Small‐Molecule Inhibitors of Protein Methyltransferases

Kanıskan, H. Ü., & Jin, J. J. (2019) · Methods and principles in medicinal chemistry · doi:10.1002/9783527809257.ch9 · Cited by 1

Characterizing the Roles of Nuclear Proteins DBC1, G9A, and GLP in Adipocyte Function and Metabolic Health

Able, A. (2019) · doi:10.31390/gradschool_dissertations.5076 · Cited by 1

The Function of the ASH1L Histone Methyltransferase in Cancer: A Chemical Biology Approach

Rogawski, D. S. (2016) · Deep Blue (University of Michigan) · Cited by 1

The N-terminal methyltransferase homologs NRMT1 and NRMT2 exhibit novel regulation of activity through heterotrimer formation.

Faughn, J. (2018) · doi:10.18297/etd/3012

Histone methylation in the freeze-tolerant wood frog, Rana sylvatica

Hawkins, L. J. (2016) · Carleton University's Institutional Repository (MacOdrum Library, Carleton University) · doi:10.22215/etd/2016-11675 · Cited by 1

Setdb2 Regulates Inflammatory Trigger Induced Trained Immunity of Macrophages Through Two Different Epigenetic MechanismsPreprint

Jaiswal, A., Halász, L., Williams, D. L., & Osborne, T. F. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.18.644013 · Cited by 1

Mechanisms of transcriptional regulation in the maintenance of β cell function

Maganti, A. V. (2015) · IUScholarWorks (Indiana University) · doi:10.7912/c2b88b

Transcriptional silencing of endogenous retroviruses by the novel lysine methyltransferase co-repressor hnRNP K

Thompson, P. J. (2015) · cIRcle (University of British Columbia) · doi:10.14288/1.0221305

Targeting Histone Lysine Methyltransferases in Cancer

Trojer, P. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782628484-00127

Análise de expressão de genes da família SETD em leucemia linfocítica crônica

Piazera, F. Z. (2015) · RIUnB Institutional Repository (University of Brasília) · doi:10.26512/2015.10.d.20588

KMT1/Suv39 methyltransferase family regulates peripheral heterochromatin tethering via histone and non-histone protein methylationsPreprint

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. (2018) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/240952 · Cited by 1

No Oxygen? No Problem! Epigenetic mechanisms of anoxia tolerance in a champion anaerobe, the red-eared slider turtle (Trachemys scripta elegans)

Wijenayake, S. (2017) · Carleton University's Institutional Repository (MacOdrum Library, Carleton University) · doi:10.22215/etd/2017-12053

Mutational and functional analyses of Kabuki syndrome genes demonstrate critical roles in craniofacial, heart and brain development

Laarhoven, P. M. V. (2015) · doi:10.25677/18mb-r737

Genome-wide occupancy of Polycomb group proteins and chromatin remodeler SPLAYED and their interplay in Arabidopsis

Shu, J. (2019) · Scholarship@Western (Western University)

Lysine Methyltransferases and Their Inhibitors

Stazi, G., Zwergel, C., & Valente, S. (2019) · Topics in medicinal chemistry · doi:10.1007/7355_2019_72

The Cell Nucleus and Its Compartments

Mierke, C. T. (2020) · Biological and medical physics, biomedical engineering · doi:10.1007/978-3-030-58532-7_10

Análise de expressão da metiltransferase SETD4 em leucemia linfoide aguda e sua relação com a leucemogênese

Telles, L. A. M. (2016) · doi:10.26512/2016.08.d.22088

Peer Review #1 of "Genetic alteration of histone lysine methyltransferases and their significance in renal cell carcinoma (v0.2)"

(2019) · PeerJ · doi:10.7287/peerj.6396v0.2/reviews/1

Peer Review #1 of "Genetic alteration of histone lysine methyltransferases and their significance in renal cell carcinoma (v0.1)"

(2019) · PeerJ · doi:10.7287/peerj.6396v0.1/reviews/1

Peer Review #2 of "Genetic alteration of histone lysine methyltransferases and their significance in renal cell carcinoma (v0.2)"

(2019) · PeerJ · doi:10.7287/peerj.6396v0.2/reviews/2

Peer Review #2 of "Genetic alteration of histone lysine methyltransferases and their significance in renal cell carcinoma (v0.1)"

(2019) · PeerJ · doi:10.7287/peerj.6396v0.1/reviews/2

[Research Progress of Role and Mechanism of SETD7 in Tumor Occurrence and Progression].

Cao, L., Wang, M., & Xu, K. (2023) · PubMed Central · doi:10.3779/j.issn.1009-3419.2023.106.02

The role of VRK1 in chromatin remodeling: regulation of histone post-translational modifications and epigenetic enzymes

Monte-Serrano, E. (2023) · Gredos (University of Salamanca) · doi:10.14201/gredos.153146

Efeitos do Valproato de Sódio nos níveis de metilações da histona H3, na interação VPA-histonas e na regulação dos genes p16ink4a e p21waf1/cip1 em células HeLa

Rocha, M. A. (2022) · doi:10.47749/t/unicamp.2022.1255182

A mitochondrial SET domain protein is essential in T. brucei and required for mitochondrial morphology and functionPreprint

Knight, E. W., Ventura, R. A., Mukala, N., & Morris, M. T. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.02.23.581798

Exploration into the MLL4/WRAD Enzyme-Substrate Network: Systematic In Vitro Identification of CFP1 as a Potential Non-Histone Substrate of the MLL4 Lysine Methyltransferase

Boulter, M., Collins, R., & Biggar, K. K. (2025) · Epigenomes · doi:10.3390/epigenomes9040041

Identification of a somatic H3K23me3 methyltransferase SET-19 in C. elegansPreprint

Xu, M., Fan, Z., Yan, C., Chen, X., Huang, X., Zhu, C., Hong, M., Cheng, J., Hou, X., Li, S., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.24.713969

Development of tumour therapies : from target validation of TTLL12 to tests of a small molecule XRP44X in pre-clinical models of cancer

Semenchenko, K. (2014) · theses.fr (ABES) · doi:10.70675/80090366z28f9z4067za036zc31b95911a52

Rôle de l'épigénétique dans la régulation des collagènes dans les chondrocytes articulaires humains : nouveaux aspects pour la compréhension de l'homéostasie du cartilage

Durand, A.-L. (2017) · theses.fr (ABES) · doi:10.70675/c3325ce5zba48z49d0z9cacz5702d147b639

A trans-methylation mechanism between the two major H3K9 methyltransferases SETDB1 and SUV39H1 regulates heterochromatin establishment

Cruz‐Tapias, P. (2018) · theses.fr (ABES) · doi:10.70675/95b1db38zceccz4ac5z89f0z4d27b9f45efb

Effets des métabolites réactifs du benzène et d'une mutation oncogénique sur SetD2, une histone méthyltransférase

Berthelet, J. (2019) · theses.fr (ABES) · doi:10.70675/c500e9a8ze222z4b0czb01ez8ede9a4f765f

Régulation et rôle de la compaction de la chromatine dans des cellules pluripotentes et lors de la différentiation

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