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

Translating the Histone Code

Jenuwein, T., & Allis, C. D. (2001) · Science · doi:10.1126/science.1063127 · Cited by 9,756

The language of covalent histone modifications

Strahl, B. D., & Allis, C. D. (2000) · Nature · doi:10.1038/47412 · Cited by 8,679

Lanthanum Chloride Inhibits LPS Mediated Expressions of Pro-Inflammatory Cytokines and Adhesion Molecules in HUVECs: Involvement of NF-κB-Jmjd3 Signaling

Chen, X., Xiu, M., Xing, J., Yu, S., Min, D., & Guo, F. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479439 · Cited by 5,760

Selective recognition of methylated lysine 9 on histone H3 by the HP1 chromo domain

Bannister, A. J., Zegerman, P., Partridge, J. F., Miska, E. A., Thomas, J. O., Allshire, R. C., & Kouzarides, T. (2001) · Nature · doi:10.1038/35065138 · Cited by 2,903

Methylation of histone H3 lysine 9 creates a binding site for HP1 proteins

Lachner, M., O'Carroll, D., Rea, S., Mechtler, K., & Jenuwein, T. (2001) · Nature · doi:10.1038/35065132 · Cited by 2,868

Regulation of chromatin structure by site-specific histone H3 methyltransferases

Rea, S., Eisenhaber, F., O'Carroll, D., Strahl, B. D., Sun, Z.-W., Schmid, M., Opravil, S., Mechtler, K., Ponting, C. P., Allis, C. D., et al. (2000) · Nature · doi:10.1038/35020506 · Cited by 2,845

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

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

Role of Histone H3 Lysine 9 Methylation in Epigenetic Control of Heterochromatin Assembly

Nakayama, J.-I., Rice, J. C., Strahl, B. D., Allis, C. D., & Grewal, S. I. S. (2001) · Science · doi:10.1126/science.1060118 · Cited by 1,739

Regulation of Transcription by a Protein Methyltransferase

Chen, D., Ma, H., Hong, H., Koh, S. S., Huang, S., Schurter, B. T., Aswad, D. W., & Stallcup, M. R. (1999) · Science · doi:10.1126/science.284.5423.2174 · Cited by 1,214

A histone H3 methyltransferase controls DNA methylation in Neurospora crassa

Tamaru, H., & Selker, E. U. (2001) · Nature · doi:10.1038/35104508 · Cited by 1,054

Histone H3 lysine 4 methylation is mediated by Set1 and promotes maintenance of active chromatin states in fission yeast

Noma, K.-I., & Grewal, S. I. S. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.182436399 · Cited by 131

ERG-associated protein with SET domain (ESET)-Oct4 interaction regulates pluripotency and represses the trophectoderm lineage

Yeap, L.-S., Hayashi, K., & Surani, M. A. (2009) · Epigenetics & Chromatin · doi:10.1186/1756-8935-2-12 · Cited by 126

In vivo gene regulation using tetracycline-regulatable systems

Stieger, K., Belbellaa, B., Guiner, C. L., Moullier, P., & Rolling, F. (2009) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2008.12.016 · Cited by 130

The TRIM Family Protein KAP1 Inhibits HIV-1 Integration

Allouch, A., Primio, C. D., Alpi, E., Lušić, M., Arosio, D., Giacca, M., & Cereseto, A. (2011) · Cell Host & Microbe · doi:10.1016/j.chom.2011.05.004 · Cited by 137

Mechanism of histone lysine methyl transfer revealed by the structure of SET7/9—AdoMet

Kwon, T., Chang, J. H., Kwak, E., Lee, C. W., Joachimiak, A., Kim, Y. C., Lee, J. W., & Cho, Y. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg025 · Cited by 127

TDP-43: an emerging new player in neurodegenerative diseases

Wang, I., Wu, L., & Shen, C. (2008) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2008.09.001 · Cited by 123

Age-Associated Decrease of the Histone Methyltransferase SUV39H1 in HSC Perturbs Heterochromatin and B Lymphoid Differentiation

Djeghloul, D., Kuranda, K., Kuzniak, I., Barbieri, D., Naguibneva, I., Choisy, C., Bories, J.-C., Dosquet, C., Pla, M., Vanneaux, V., et al. (2016) · Stem Cell Reports · doi:10.1016/j.stemcr.2016.05.007 · Cited by 128

Stage-specific H3K9me3 occupancy ensures retrotransposon silencing in human pre-implantation embryos

Xu, R., Li, S., Wu, Q., Li, C., Jiang, M., Guo, L., Chen, M., Yang, L., Dong, X., Wang, H., et al. (2022) · Cell stem cell · doi:10.1016/j.stem.2022.06.001 · Cited by 121

CircPTK2/PABPC1/SETDB1 axis promotes EMT-mediated tumor metastasis and gemcitabine resistance in bladder cancer

Meng, X., Xiao, W., Sun, J., Li, W., Yuan, H., Yu, T., Zhang, X., & Dong, W. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.216023 · Cited by 126

Chromatin remodeling finds its place in the DNA double-strand break response

Pandita, T. K., & Richardson, C. A. (2009) · Nucleic Acids Research · doi:10.1093/nar/gkn1071 · Cited by 128

KAP1 Promotes Proliferation and Metastatic Progression of Breast Cancer Cells

Addison, J., Koontz, C., Fugett, J. H., Creighton, C. J., Chen, D., Farrugia, M. K., Padon, R. R., Voronkova, M. A., McLaughlin, S. L., Livengood, R. H., et al. (2014) · Cancer Research · doi:10.1158/0008-5472.can-14-1561 · Cited by 123

Dual-specificity histone demethylase KIAA1718 (KDM7A) regulates neural differentiation through FGF4

Huang, C., Xiang, Y., Wang, Y., Li, X., Xu, L., Zhu, Z., Zhang, T., Zhu, Q., Zhang, K., Jing, N., et al. (2010) · Cell Research · doi:10.1038/cr.2010.5 · Cited by 123

DNA Methylation Readers and Cancer: Mechanistic and Therapeutic Applications

Mahmood, N., & Rabbani, S. A. (2019) · Frontiers in Oncology · doi:10.3389/fonc.2019.00489 · Cited by 129

Interplay between DNA methylation, histone modification and chromatin remodeling in stem cells and during development

Ikegami, K., Ohgane, J., Tanaka, S., Yagi, S., & Shiota, K. (2009) · The International Journal of Developmental Biology · doi:10.1387/ijdb.082741ki · Cited by 122

Epigenetic modifications of the immune system in health and disease

Obata, Y., Furusawa, Y., & Hase, K. (2015) · Immunology and Cell Biology · doi:10.1038/icb.2014.114 · Cited by 125

An ERG (ets-related gene)-associated histone methyltransferase interacts with histone deacetylases 1/2 and transcription co-repressors mSin3A/B

Yang, L., Mei, Q., Zielinska‐Kwiatkowska, A., Matsui, Y., Blackburn, M. L., Benedetti, D. J., Krumm, A., Taborsky, G. J., & Chansky, H. A. (2003) · Biochemical Journal · doi:10.1042/bj20020854 · Cited by 124

The SCAN domain family of zinc finger transcription factors

Edelstein, L. C., & Collins, T. (2005) · Gene · doi:10.1016/j.gene.2005.06.022 · Cited by 123

Setdb1 Histone Methyltransferase Regulates Mood-Related Behaviors and Expression of the NMDA Receptor Subunit NR2B

Jiang, Y., Jakovcevski, M., Bharadwaj, R., Connor, C., Schroeder, F. A., Lin, C. L., Straubhaar, J., Martin, G., & Akbarian, S. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.1314-10.2010 · Cited by 118

The Roles of the Methyl-CpG Binding Proteins in Cancer

Parry, L., & Clarke, A. R. (2011) · Genes & Cancer · doi:10.1177/1947601911418499 · Cited by 122

KRAB-zinc finger protein gene expansion in response to active retrotransposons in the murine lineage

Wolf, G., Iaco, A. D., Sun, M., Bruno, M., Tinkham, M., Hoang, D., Mitra, A., Ralls, S., Trono, D., & Macfarlan, T. S. (2020) · eLife · doi:10.7554/elife.56337 · Cited by 118

KRAB-type zinc-finger protein Apak specifically regulates p53-dependent apoptosis

Tian, C., Xing, G., Xie, P., Lu, K., Nie, J., Wang, J., Li, L., Gao, M., Zhang, L., & He, F. (2009) · Nature Cell Biology · doi:10.1038/ncb1864 · Cited by 120

Histone lysine methyltransferase SUV39H1 is a potent target for epigenetic therapy of hepatocellular carcinoma

Chiba, T., Saito, T., Yuki, K., Zen, Y., Koide, S., Kanogawa, N., Motoyama, T., Ogasawara, S., Suzuki, E., Ooka, Y., et al. (2014) · International Journal of Cancer · doi:10.1002/ijc.28985 · Cited by 119

ATM protein kinase: the linchpin of cellular defenses to stress

Bhatti, S., Kozlov, S., Farooqi, A. A., Naqi, A., Lavin, M., & Khanna, K. K. (2011) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-011-0683-9 · Cited by 116

Doxorubicin Down-regulates Krüppel-associated Box Domain-associated Protein 1 Sumoylation That Relieves Its Transcription Repression on p21WAF1/CIP1 in Breast Cancer MCF-7 Cells

Lee, Y.-K., Thomas, S. N., Yang, A. J., & Ann, D. K. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m606306200 · Cited by 117

H3K14ac is linked to methylation of H3K9 by the triple Tudor domain of SETDB1

Jurkowska, R. Z., Su, Q., Kungulovski, G., Tempel, W., Liu, Y., Bashtrykov, P., Stiefelmaier, J., Jurkowski, T. P., Kudithipudi, S., Weirich, S., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-02259-9 · Cited by 115

Silencing of endogenous retroviruses by heterochromatin

Groh, S., & Schotta, G. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2454-8 · Cited by 114

Differential Localization and Independent Acquisition of the H3K9me2 and H3K9me3 Chromatin Modifications in the Caenorhabditis elegans Adult Germ Line

Bessler, J. B., Andersen, E. C., & Villeneuve, A. M. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1000830 · Cited by 115

Multifunctional zinc finger proteins in development and disease

Ladomery, M., & Dellaire, G. (2002) · Annals of Human Genetics · doi:10.1046/j.1469-1809.2002.00121.x · Cited by 115

The Histone Methyltransferase SETDB1 Controls T Helper Cell Lineage Integrity by Repressing Endogenous Retroviruses

Adoue, V., Binet, B., Malbec, A., Fourquet, J., Romagnoli, P., van Meerwijk, J. P. M., Amigorena, S., & Joffre, O. P. (2019) · Immunity · doi:10.1016/j.immuni.2019.01.003 · Cited by 119

Spotting the enemy within: Targeted silencing of foreign DNA in mammalian genomes by the Krüppel-associated box zinc finger protein family

Wolf, G., Greenberg, D., & Macfarlan, T. S. (2015) · Mobile DNA · doi:10.1186/s13100-015-0050-8 · Cited by 111

Replication Stress and Chromatin Context Link ATM Activation to a Role in DNA Replication

Olcina, M. M., Foskolou, I. P., Anbalagan, S., Senra, J. M., Pires, I. M., Jiang, Y., Ryan, A. J., & Hammond, E. M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.019 · Cited by 115

Transposable element regulation and expression in cancer

Grundy, E. E., Diab, N., & Chiappinelli, K. B. (2021) · FEBS Journal · doi:10.1111/febs.15722 · Cited by 125

A cohesin/HUSH- and LINC-dependent pathway controls ribosomal DNA double-strand break repairPreprint

Marnef, A., Finoux, A.-L., Arnould, C., Guillou, E., Daburon, V., Rocher, V., Mangeat, T., Mangeot, P. E., Ricci, E. P., & Legube, G. (2019) · Genes & Development · doi:10.1101/gad.324012.119 · Cited by 125

A KRAB/KAP1-miRNA Cascade Regulates Erythropoiesis Through Stage-Specific Control of Mitophagy

Barde, I., Rauwel, B., Marin-Florez, R. M., Corsinotti, A., Laurenti, E., Verp, S., Offner, S., Marquis, J., Kapopoulou, A., Vanicek, J., et al. (2013) · Science · doi:10.1126/science.1232398 · Cited by 111

The interactome of KRAB zinc finger proteins reveals the evolutionary history of their functional diversification

Helleboid, P., Heusel, M., Duc, J., Piot, C., Thorball, C. W., Coluccio, A., Pontis, J., Imbeault, M., Turelli, P., Aebersold, R. H., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2018101220 · Cited by 113

SETDB1-Mediated Silencing of Retroelements

Fukuda, K., & Shinkai, Y. (2020) · Viruses · doi:10.3390/v12060596 · Cited by 114

Self-interaction of heterochromatin protein 1 is required for direct binding to histone methyltransferase, SUV39H1

Yamamoto, K., & Sonoda, M. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)03021-8 · Cited by 115

Histone methylation is required for oogenesis inDrosophila

Clough, E., Moon, W., Wang, S., Smith, K. M., & Hazelrigg, T. I. (2006) · Development · doi:10.1242/dev.02698 · Cited by 108

Functional Analysis of KAP1 Genomic Recruitment

Iyengar, S., Ivanov, A. V., Jin, V. X., Rauscher, F. J., & Farnham, P. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01331-10 · Cited by 113

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

NXP-2 association with SUMO-2 depends on lysines required for transcriptional repression

Rosendorff, A., Sakakibara, S., Lu, S. S., Kieff, E. D., Xuan, Y., Bacco, A. D., Shi, Y. G., Shi, Y., & Gill, G. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601066103 · Cited by 107

Tripartite Motif Containing 28 (Trim28) Can Regulate Cell Proliferation by Bridging HDAC1/E2F Interactions

Chen, L., Chen, D., Kurtyka, C. A., Rawal, B., Fulp, W. J., Haura, E. B., & Cress, W. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.380865 · Cited by 111

Phosphoproteomic analysis reveals that PP4 dephosphorylates KAP‐1 impacting the DNA damage response

Lee, D.-H., Goodarzi, A. A., Adelmant, G., Pan, Y., Jeggo, P. A., Marto, J. A., & Chowdhury, D. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.86 · Cited by 108

CBX3 regulates efficient RNA processing genome-widePreprint

Smallwood, A., Hon, G. C., Jin, F., Henry, R. E., Espinosa, J. M., & Ren, B. (2012) · Genome Research · doi:10.1101/gr.124818.111 · Cited by 106

Meisetz and the birth of the KRAB motif

Birtle, Z., & Ponting, C. P. (2006) · Bioinformatics · doi:10.1093/bioinformatics/btl498 · Cited by 107

Role of histone methylation and demethylation in adipogenesis and obesity

Okamura, M., Inagaki, T., Tanaka, T., & Sakai, J. (2010) · Organogenesis · doi:10.4161/org.6.1.11121 · Cited by 104

SETDB1 Links the Meiotic DNA Damage Response to Sex Chromosome Silencing in Mice

Hirota, T., Blakeley, P., Sangrithi, M. N., Mahadevaiah, S. K., Encheva, V., Snijders, A. P., Elinati, E., Ojarikre, O. A., de Rooij, D. G., Niakan, K. K., et al. (2018) · Developmental Cell · doi:10.1016/j.devcel.2018.10.004 · Cited by 104

Protein Phosphatase 2A Activity Affects Histone H3 Phosphorylation and Transcription in Drosophila melanogaster

Nowak, S. J., Pai, C.-Y., & Corces, V. G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.17.6129-6138.2003 · Cited by 104

TRIM28 prevents autoinflammatory T cell development in vivo

Chikuma, S., Suita, N., Okazaki, I., Shibayama, S., & Honjo, T. (2012) · Nature Immunology · doi:10.1038/ni.2293 · Cited by 105

Repression of IP-10 by Interactions between Histone Deacetylation and Hypermethylation in Idiopathic Pulmonary Fibrosis

Coward, W. R., Watts, K., Feghali‐Bostwick, C. A., Jenkins, G. R., & Pang, L. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01527-09 · Cited by 105

A Feed-Forward Circuit Controlling Inducible NF-κB Target Gene Activation by Promoter Histone Demethylation

van Essen, D., Zhu, Y., & Saccani, S. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.08.010 · Cited by 107

Association of the transcriptional corepressor TIF1beta with heterochromatin protein 1 (HP1): an essential role for progression through differentiation.Preprint

Cammas, F., Herzog, M., Lerouge, T., Chambon, P., & Losson, R. (2004) · Genes & Development · doi:10.1101/gad.302904 · Cited by 118

Targeting DNA repair in cancer: current state and novel approaches

Klinakis, A., Karagiannis, D., & Rampias, T. N. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03299-8 · Cited by 108

Histone Modifications in Cancer Biology and Prognosis

Kurdistani, S. K. (2010) · Springer eBooks · doi:10.1007/978-3-7643-8989-5_5 · Cited by 106

Loss of transcriptional control over endogenous retroelements during reprogramming to pluripotencyPreprint

Friedli, M., Turelli, P., Kapopoulou, A., Rauwel, B., Castro-Díaz, N., Rowe, H. M., Ecco, G., Unzu, C., Planet, E., Lombardo, A., et al. (2014) · Genome Research · doi:10.1101/gr.172809.114 · Cited by 105

KAPtain in charge of multiple missions: Emerging roles of KAP1

Cheng, C.-T. (2014) · World Journal of Biological Chemistry · doi:10.4331/wjbc.v5.i3.308 · Cited by 113

hnRNP K Coordinates Transcriptional Silencing by SETDB1 in Embryonic Stem Cells

Thompson, P. J., Dulberg, V., Moon, K., Foster, L. J., Chen, C. C. L., Karimi, M. M., & Lorincz, M. C. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1004933 · Cited by 101

Histone Methylation Regulation in Neurodegenerative Disorders

Basavarajappa, B. S., & Subbanna, S. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22094654 · Cited by 103

Analysis of specific lysine histone H3 and H4 acetylation and methylation status in clones of cells with a gene silenced by nickel exposure

Yan, Y., Kluz, T., Zhang, P., Chen, H., & Costa, M. (2003) · Toxicology and Applied Pharmacology · doi:10.1016/s0041-008x(03)00169-8 · Cited by 100

Kruppel-Associated Box Domain-Associated Protein-1 as a Latency Regulator for Kaposi's Sarcoma-Associated Herpesvirus and Its Modulation by the Viral Protein Kinase

Chang, P., Fitzgerald, L. D., Geelen, A. V., Izumiya, Y., Ellison, T. J., Wang, D.-H., Ann, D. K., Luciw, P. A., & Kung, H.-J. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4570 · Cited by 100

Mutations in the ZNF41 Gene Are Associated with Cognitive Deficits: Identification of a New Candidate for X-Linked Mental Retardation

Shoichet, S. A., Hoffmann, K., Menzel, C., Trautmann, U., Moser, B. A., Hoeltzenbein, M., Échenne, B., Partington, M. W., van Bokhoven, H., Moraine, C., et al. (2003) · The American Journal of Human Genetics · doi:10.1086/380309 · Cited by 100

Epigenetics, chromatin and genome organization: recent advances from the ENCODE project

Siggens, L., & Ekwall, K. (2014) · Journal of Internal Medicine · doi:10.1111/joim.12231 · Cited by 105

A map of human PRDM9 binding provides evidence for novel behaviors of PRDM9 and other zinc-finger proteins in meiosis

Altemose, N., Noor, N., Bitoun, E., Tumian, A., Imbeault, M., Chapman, J. R., Aricescu, A. R., & Myers, S. (2017) · eLife · doi:10.7554/elife.28383 · Cited by 101

Control of viral infections by epigenetic-targeted therapy

Nehme, Z., Pasquereau, S., & Herbein, G. (2019) · Clinical Epigenetics · doi:10.1186/s13148-019-0654-9 · Cited by 103

Distinct chromatin signatures of DNA hypomethylation in aging and cancer

Pérez, R. F., Tejedor, J. R., Bayón, G. F., Fernández, A. F., & Fraga, M. F. (2018) · Aging Cell · doi:10.1111/acel.12744 · Cited by 106

Histone Methyltransferase SETDB1: A Common Denominator of Tumorigenesis with Therapeutic Potential

Strepkos, D., Markouli, M., Κλώνου, Α., Papavassiliou, A. G., & Piperi, C. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-2906 · Cited by 102

Heterochromatin Protein 1 Is Extensively Decorated with Histone Code-like Post-translational Modifications

LeRoy, G., Weston, J. T., Zee, B. M., Young, N. L., Plazas-Mayorca, M. D., & Garcia, B. A. (2009) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m900160-mcp200 · Cited by 97

Role of Histone Lysine Methyltransferases SUV39H1 and SETDB1 in Gliomagenesis: Modulation of Cell Proliferation, Migration, and Colony Formation

Spyropoulou, A., Gargalionis, A. N., Dalagiorgou, G., Adamopoulos, C., Papavassiliou, K. A., Lea, R. W., Piperi, C., & Papavassiliou, A. G. (2013) · NeuroMolecular Medicine · doi:10.1007/s12017-013-8254-x · Cited by 95

The Nuclear Oncogene SET Controls DNA Repair by KAP1 and HP1 Retention to Chromatin

Kalousi, A., Hoffbeck, A.-S., Selemenakis, P., Pinder, J. B., Savage, K. I., Khanna, K. K., Brino, L., Dellaire, G., Gorgoulis, V. G., & Soutoglou, E. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.03.005 · Cited by 100

Histone methyltransferase protein SETD2 interacts with p53 and selectively regulates its downstream genes

Xie, P., Tian, C., An, L., Nie, J., Lu, K., Xing, G., Zhang, L., & He, F.-C. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.05.012 · Cited by 96

Interplay between chromatin state, regulator binding, and regulatory motifs in six human cell typesPreprint

Ernst, J., & Kellis, M. (2013) · Genome Research · doi:10.1101/gr.144840.112 · Cited by 99

Chromatin-enriched lncRNAs can act as cell-type specific activators of proximal gene transcription

Werner, M. S., Sullivan, M. A., Shah, R. N., Nadadur, R. D., Grzybowski, A. T., Galat, V., Moskowitz, I. P. G., & Ruthenburg, A. J. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3424 · Cited by 96

Sumoylation in Physiology, Pathology and Therapy

Şahin, U., de Thé, H., & Lallemand-Breitenbach, V. (2022) · Cells · doi:10.3390/cells11050814 · Cited by 98

SUMO‐modified Sp3 represses transcription by provoking local heterochromatic gene silencing

Stielow, B., Sapetschnig, A., Wink, C., Krüger, I., & Suske, G. (2008) · EMBO Reports · doi:10.1038/embor.2008.127 · Cited by 94

Mechanisms of astrocytogenesis in the mammalian brain

Namihira, M., & Nakashima, K. (2013) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2013.06.002 · Cited by 93

PHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis

Zhu, Z., Wang, Y., Li, X., Wang, Y., Xu, L., Wang, X., Sun, T., Dong, X., Chen, L., Mao, H., et al. (2010) · Cell Research · doi:10.1038/cr.2010.75 · Cited by 97

KMT1E Mediated H3K9 Methylation Is Required for the Maintenance of Embryonic Stem Cells by Repressing Trophectoderm Differentiation

Lohmann, F., Loureiro, J., Su, H., Fang, Q., Lei, H., Lewis, T., Yang, Y., Labow, M., Li, E., Chen, T., et al. (2009) · Stem Cells · doi:10.1002/stem.278 · Cited by 93

Hetero-oligomerization Among the TIF Family of RBCC/TRIM Domain-containing Nuclear Cofactors: A Potential Mechanism for Regulating the Switch Between Coactivation and Corepression

Peng, H., Feldman, I., & Rauscher, F. J. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00477-1 · Cited by 91

H1 linker histones silence repetitive elements by promoting both histone H3K9 methylation and chromatin compaction

Healton, S. E., Pinto, H. B., Mishra, L. N., Hamilton, G. A., Wheat, J. C., Świst-Rosowska, K. M., Shukeir, N., Dou, Y., Steidl, U. G., Jenuwein, T., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1920725117 · Cited by 92

Acetylation- and Methylation-Related Epigenetic Proteins in the Context of Their Targets

Javaid, N., & Choi, S. (2017) · Genes · doi:10.3390/genes8080196 · Cited by 97

Regulation of E2F1 Function by the Nuclear Corepressor KAP1

Wang, C., Rauscher, F. J., Cress, W. D., & Chen, J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704757200 · Cited by 93

Structure and Function of Histone H3 Lysine 9 Methyltransferases and Demethylases

Krishnan, S., Horowitz, S. A., & Trievel, R. C. (2011) · ChemBioChem · doi:10.1002/cbic.201000545 · Cited by 92

Rapid embryonic cell cycles defer the establishment of heterochromatin by Eggless/SetDB1 in DrosophilaPreprint

Seller, C. A., Cho, C.-Y., & O’Farrell, P. H. (2019) · Genes & Development · doi:10.1101/gad.321646.118 · Cited by 90

Genetic and epigenetic defects in mental retardation

Kramer, J. M., & van Bokhoven, H. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2008.08.009 · Cited by 91

Maternal Setdb1 Is Required for Meiotic Progression and Preimplantation Development in Mouse

Kim, J., Zhao, H., Dan, J., Kim, S., Hardikar, S., Hollowell, D., Lin, K., Lu, Y., Takata, Y., Shen, J., et al. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1005970 · Cited by 87

SETDB1/NSD-dependent H3K9me3/H3K36me3 dual heterochromatin maintains gene expression profiles by bookmarking poised enhancers

Barral, A., Pozo, G., Ducrot, L., Papadopoulos, G. L., Sauzet, S., Oldfield, A., Cavalli, G., & Déjardin, J. (2022) · Molecular Cell · doi:10.1016/j.molcel.2021.12.037 · Cited by 87

Transcription Factor Effector Domains

Frietze, S. E., & Farnham, P. (2011) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-90-481-9069-0_12 · Cited by 93

Recruitment and Biological Consequences of Histone Modification of H3K27me3 and H3K9me3

Kim, J. H., & Kim, H. (2012) · ILAR Journal · doi:10.1093/ilar.53.3-4.232 · Cited by 94

Primate-restricted KRAB zinc finger proteins and target retrotransposons control gene expression in human neurons

Turelli, P., Playfoot, C. J., Grun, D., Raclot, C., Pontis, J., Coudray, A., Thorball, C. W., Duc, J., Pankevich, E. V., Deplancke, B., et al. (2020) · Science Advances · doi:10.1126/sciadv.aba3200 · Cited by 85

dSETDB1 and SU(VAR)3–9 Sequentially Function during Germline-Stem Cell Differentiation in Drosophila melanogaster

Yoon, J., Lee, K.-S., Park, J., Yu, K., Paik, S., & Kang, Y.-K. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002234 · Cited by 75

ZNF674: A New Krüppel-Associated Box–Containing Zinc-Finger Gene Involved in Nonsyndromic X-Linked Mental Retardation

Lugtenberg, D., Yntema, H. G., Banning, M. J. G., Oudakker, A. R., Firth, H. V., Willatt, L. R., Raynaud, M., Kleefstra, T., Fryns, J., Ropers, H., et al. (2006) · The American Journal of Human Genetics · doi:10.1086/500306 · 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

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

Emerging roles of H3K9me3, SETDB1 and SETDB2 in therapy-induced cellular reprogramming

Torrano, J., Emran, A. A., Hammerlindl, H., & Schaider, H. (2019) · Clinical Epigenetics · doi:10.1186/s13148-019-0644-y · Cited by 87

ATF7IP regulates SETDB1 nuclear localization and increases its ubiquitination

Tsusaka, T., Shimura, C., & Shinkai, Y. (2019) · EMBO Reports · doi:10.15252/embr.201948297 · Cited by 83

KRAB-ZFP Transcriptional Regulators Acting as Oncogenes and Tumor Suppressors: An Overview

Sobocińska, J., Molenda, S., Machnik, M., & Oleksiewicz, U. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22042212 · Cited by 87

Long noncoding RNA XIST: Mechanisms for X chromosome inactivation, roles in sex-biased diseases, and therapeutic opportunities

Li, J., Ming, Z., Yang, L., Wang, T., Liu, G., & Ma, Q. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2022.04.007 · Cited by 89

SETDB1, HP1 and SUV39 promote repositioning of 53BP1 to extend resection during homologous recombination in G2 cells

Alagöz, M., Katsuki, Y., Ogiwara, H., Ogi, T., Shibata, A., Kakarougkas, A., & Jeggo, P. A. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv722 · Cited by 93

DZNep, inhibitor of S-adenosylhomocysteine hydrolase, down-regulates expression of SETDB1 H3K9me3 HMTase in human lung cancer cells

Lee, J.-K., & Kim, K. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.07.128 · Cited by 84

The Gpr1/Zdbf2 locus provides new paradigms for transient and dynamic genomic imprinting in mammalsPreprint

Duffié, R., Ajjan, S., Greenberg, M., Zamudio, N., Escamilla-Del-Arenal, M., Iranzo, J., Okamoto, I., Barbaux, S., Fauque, P., & Bourc’his, D. (2014) · Genes & Development · doi:10.1101/gad.232058.113 · Cited by 89

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

The KAP1 Corepressor Functions To Coordinate the Assembly of De Novo HP1-Demarcated Microenvironments of Heterochromatin Required for KRAB Zinc Finger Protein-Mediated Transcriptional Repression

Sripathy, S. P., Stevens, J., & Schultz, D. C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00487-06 · Cited by 323

ZNF274 recruits the histone methyltransferase SETDB1 to the 39 ends of ZNF genes. PLoS ONE 5: e15082. doi: 10.1371/journal.pone.0015082

Frietze, S., Blahnik, K. R., Jin, V. X., & Farnham, P. (2010)

Genome-Wide Analysis of KAP1 Binding Suggests Autoregulation of KRAB-ZNFs

O'Geen, H., Squazzo, S. L., Iyengar, S., Blahnik, K., Rinn, J. L., Chang, H. Y., Green, R., & Farnham, P. J. (2007) · PLoS Genetics · doi:10.1371/journal.pgen.0030089 · Cited by 178

PJ: Genome-wide analysis of KAP1 binding suggests autoregulation of KRAB-ZNFs. PLoS Genet 2007

Squazzo, S. L., Iyengar, S., Blahnik, K., Rinn, J. L., Chang, H. Y., & Farnham, P. (2013)