The MLL3/4 H3K4 methyltransferase complex in establishing an active enhancer landscape

Epigenetic Regulations of GABAergic Neurotransmission: Relevance for Neurological Disorders and Epigenetic Therapy

Shrestha, S., & Offer, S. M. (2016) · Medical Epigenetics · doi:10.1159/000444713 · Cited by 8,949 · see citing works

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 5,759 · see citing works

Mutational landscape and significance across 12 major cancer types

Kandoth, C., McLellan, M. D., Vandin, F., Ye, K., Niu, B., Lu, C., Xie, M., Zhang, Q., McMichael, J. F., Wyczalkowski, M. A., et al. (2013) · Nature · doi:10.1038/nature12634 · Cited by 4,419 · see citing works

Comprehensive genomic characterization of squamous cell lung cancers

The Cancer Genome Atlas Research Network (2012) · Nature · doi:10.1038/nature11404 · Cited by 3,994 · see citing works

The Consensus Coding Sequences of Human Breast and Colorectal Cancers

Sjöblom, T., Jones, S., Wood, L. D., Parsons, D. W., Lin, J., Barber, T. D., Mandelker, D. L., Leary, R. J., Ptak, J., Silliman, N., et al. (2006) · Science · doi:10.1126/science.1133427 · Cited by 3,161 · see citing works

The molecular hallmarks of epigenetic control

Allis, C. D., & Jenuwein, T. (2016) · Nature Reviews Genetics · doi:10.1038/nrg.2016.59 · Cited by 2,809 · see citing works

The mutational landscape of lethal castration-resistant prostate cancer

Grasso, C. S., Wu, Y.-M., Robinson, D. R., Cao, X., Dhanasekaran, S. M., Khan, A. P., Quist, M. J., Jing, X., Lonigro, R. J., Brenner, J. C., et al. (2012) · Nature · doi:10.1038/nature11125 · Cited by 2,517 · see citing works

Mediator and cohesin connect gene expression and chromatin architecture

Kagey, M. H., Newman, J. J., Bilodeau, S., Zhan, Y., Orlando, D. A., van Berkum, N. L., Ebmeier, C. C., Goossens, J., Rahl, P. B., Levine, S. S., et al. (2010) · Nature · doi:10.1038/nature09380 · Cited by 1,939 · see citing works

Epigenome editing by a CRISPR-Cas9-based acetyltransferase activates genes from promoters and enhancers

Hilton, I. B., D’Ippolito, A. M., Vockley, C. M., Thakore, P. I., Crawford, G. E., Reddy, T. E., & Gersbach, C. A. (2015) · Nature Biotechnology · doi:10.1038/nbt.3199 · Cited by 1,879 · see citing works

Frequent mutation of histone-modifying genes in non-Hodgkin lymphoma

Morin, R. D., Mendez-Lago, M., Mungall, A. J., Goya, R., Mungall, K. L., Corbett, R. D., Johnson, N. A., Severson, T. M., Chiu, R., Field, M., et al. (2011) · Nature · doi:10.1038/nature10351 · Cited by 1,614 · see citing works

The promoter-specific transcription factor Sp1 binds to upstream sequences in the SV40 early promoter

Dynan, W. S., & Tjian, R. (1983) · Cell · doi:10.1016/0092-8674(83)90210-6 · Cited by 1,445 · see citing works

UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development

Agger, K., Cloos, P. A., Christensen, J. F., Pasini, D., Rose, S., Rappsilber, J., Issaeva, I., Canaani, E., Salcini, A. E., & Helin, K. (2007) · Nature · doi:10.1038/nature06145 · Cited by 1,392 · see citing works

The nuts and bolts of AGC protein kinases

Pearce, L. R., Komander, D., & Alessi, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2822 · Cited by 1,294 · see citing works

Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes

Dalgliesh, G. L., Furge, K., Greenman, C., Chen, L., Bignell, G., Butler, A., Davies, H., Edkins, S., Hardy, C., Latimer, C., et al. (2010) · Nature · doi:10.1038/nature08672 · Cited by 1,173 · see citing works

Long-range enhancer–promoter contacts in gene expression control

Schoenfelder, S., & Fraser, P. (2019) · Nature Reviews Genetics · doi:10.1038/s41576-019-0128-0 · Cited by 1,102 · see citing works

A small-cell lung cancer genome with complex signatures of tobacco exposure

Pleasance, E., Stephens, P. J., O’Meara, S., McBride, D. J., Meynert, A. M., Jones, D., Lin, M., Beare, D. M., Lau, K. W., Greenman, C., et al. (2009) · Nature · doi:10.1038/nature08629 · Cited by 1,067 · see citing works

Whole-genome analysis informs breast cancer response to aromatase inhibition

Ellis, M. J., Ding, L., Shen, D., Luo, J. R., Suman, V. J., Wallis, J. W., Tine, B. A. V., Hoog, J., Goiffon, R., Goldstein, T. C., et al. (2012) · Nature · doi:10.1038/nature11143 · Cited by 1,023 · see citing works

Discovery and prioritization of somatic mutations in diffuse large B-cell lymphoma (DLBCL) by whole-exome sequencing

Lohr, J. G., Stojanov, P., Lawrence, M. S., Auclair, D., Chapuy, B., Sougnez, C. L., Cruz‐Gordillo, P., Knoechel, B., Asmann, Y. W., Slager, S. L., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1121343109 · Cited by 977 · see citing works

Analysis of the coding genome of diffuse large B-cell lymphoma

Pasqualucci, L., Trifonov, V. A., Fabbri, G., Ma, J., Rossi, D., Chiarenza, A., Wells, V. A., Grunn, A., Messina, M., Elliott, O., et al. (2011) · Nature Genetics · doi:10.1038/ng.892 · Cited by 971 · see citing works

Pax-2 controls multiple steps of urogenital development

Torres, M., Gómez‐Pardo, E., Dressler, G. R., & Gruß, P. (1995) · Development · doi:10.1242/dev.121.12.4057 · Cited by 895 · see citing works

Whole-genome sequencing of liver cancers identifies etiological influences on mutation patterns and recurrent mutations in chromatin regulators

Fujimoto, A., Totoki, Y., Abe, T., Boroevich, K. A., Hosoda, F., Hà, N. H., Aoki, M., Hosono, N., Kubo, M., Miya, F., et al. (2012) · Nature Genetics · doi:10.1038/ng.2291 · Cited by 868 · see citing works

Dissecting the genomic complexity underlying medulloblastoma

Jones, D. T. W., Jäger, N., Kool, M., Zichner, T., Hutter, B., Sultan, M., Cho, Y.-J., Pugh, T. J., Hovestadt, V., Stütz, A. M., et al. (2012) · Nature · doi:10.1038/nature11284 · Cited by 839 · see citing works

A histone H3 lysine 27 demethylase regulates animal posterior development

Lan, F., Bayliss, P. E., Rinn, J. L., Whetstine, J. R., Wang, J. K., Chen, S., Iwase, S., Alpatov, R., Issaeva, I., Canaani, E., et al. (2007) · Nature · doi:10.1038/nature06192 · Cited by 782 · see citing works

Demethylation of H3K27 Regulates Polycomb Recruitment and H2A Ubiquitination

Lee, M. G., Villa, R., Trojer, P., Norman, J. A., Yan, K.-P., Reinberg, D., Croce, L. D., & Shiekhattar, R. (2007) · Science · doi:10.1126/science.1149042 · Cited by 772 · see citing works

Regulation of MLL1 H3K4 methyltransferase activity by its core components

Dou, Y., Milne, T. A., Ruthenburg, A. J., Lee, S., Lee, J. W., Verdine, G. L., Allis, C. D., & Roeder, R. G. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1128 · Cited by 764 · see citing works

Medulloblastoma exome sequencing uncovers subtype-specific somatic mutations

Pugh, T. J., Weeraratne, S. D., Archer, T. C., Pomeranz Krummel, D. A., Auclair, D., Bochicchio, J., Carneiro, M. O., Carter, S. L., Cibulskis, K., Erlich, R. L., et al. (2012) · Nature · doi:10.1038/nature11329 · Cited by 750 · see citing works

Frequent mutations of chromatin remodeling genes in transitional cell carcinoma of the bladder

Gui, Y., Guo, G., Huang, Y., Hu, X., Tang, A., Gao, S., Wu, R., Chen, C., Li, X., Zhou, L., et al. (2011) · Nature Genetics · doi:10.1038/ng.907 · Cited by 748 · see citing works

Organization and regulation of gene transcription

Cramer, P. (2019) · Nature · doi:10.1038/s41586-019-1517-4 · Cited by 732 · see citing works

Determinants of enhancer and promoter activities of regulatory elements

Andersson, R., & Sandelin, A. (2020) · Nature Reviews Genetics · doi:10.1038/s41576-019-0173-8 · Cited by 713 · see citing works

Enhancers as non-coding RNA transcription units: recent insights and future perspectives

Li, W., Notani, D., & Rosenfeld, M. G. (2016) · Nature Reviews Genetics · doi:10.1038/nrg.2016.4 · Cited by 710 · see citing works

The Genetic Landscape of the Childhood Cancer Medulloblastoma

Parsons, D. W., Li, M., Zhang, X., Jones, S., Leary, R. J., Lin, J., Boca, S. M., Carter, H. K., Samayoa, J. A., Bettegowda, C., et al. (2010) · Science · doi:10.1126/science.1198056 · Cited by 708 · see citing works

Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases

Hong, S., Cho, Y., Yu, L., Yu, H., Veenstra, T. D., & Ge, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707292104 · Cited by 700 · see citing works

Selective and accurate initiation of transcription at the ad2 major late promotor in a soluble system dependent on purified rna polymerase ii and dna

Weil, P. A., Luse, D. S., Segall, J., & Roeder, R. G. (1979) · Cell · doi:10.1016/0092-8674(79)90065-5 · Cited by 663 · see citing works

Developmental enhancers and chromosome topology

Furlong, E. E. M., & Levine, M. (2018) · Science · doi:10.1126/science.aau0320 · Cited by 641 · see citing works

Exome sequencing of gastric adenocarcinoma identifies recurrent somatic mutations in cell adhesion and chromatin remodeling genes

Zang, Z. J., Cutcutache, I., Poon, S. L., Zhang, S. L., McPherson, J. R., Tao, J., Rajasegaran, V., Heng, H. L., Deng, N., Gan, A., et al. (2012) · Nature Genetics · doi:10.1038/ng.2246 · Cited by 614 · see citing works

Genetics of Follicular Lymphoma Transformation

Pasqualucci, L., Khiabanian, H., Fangazio, M., Vasishtha, M., Messina, M., Holmes, A. B., Ouillette, P. D., Trifonov, V. A., Rossi, D., Tabbò, F., et al. (2014) · Cell Reports · doi:10.1016/j.celrep.2013.12.027 · Cited by 570 · see citing works

Circadian Rhythm Disruption Promotes Lung Tumorigenesis

Papagiannakopoulos, T., Bauer, M. R., Davidson, S. M., Heimann, M., Subbaraj, L., Bhutkar, A., Bartlebaugh, J., Vander Heiden, M. G., & Jacks, T. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.07.001 · Cited by 557 · see citing works

Nephric lineage specification by Pax2 and Pax8Preprint

Bouchard, M., Souabni, A., Mandler, M., Neubüser, A., & Busslinger, M. (2002) · Genes & Development · doi:10.1101/gad.240102 · Cited by 552 · see citing works

Mapping Human Epigenomes

Rivera, C. M., & Ren, B. (2013) · Cell · doi:10.1016/j.cell.2013.09.011 · Cited by 550 · see citing works

PTIP Associates with MLL3- and MLL4-containing Histone H3 Lysine 4 Methyltransferase Complex

Cho, Y., Hong, T., Hong, S., Guo, H. W., Yu, H., Kim, D., Guszczynski, T., Dressler, G. R., Copeland, T. D., Kalkum, M., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701574200 · Cited by 528 · see citing works

Genetic heterogeneity of diffuse large B-cell lymphoma

Zhang, J., Grubor, V. D., Love, C., Banerjee, A., Richards, K. L., Mieczkowski, P. A., Dunphy, C. H., Choi, W., Au, W. Y., Srivastava, G., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205299110 · Cited by 527 · see citing works

Epigenetic balance of gene expression by Polycomb and COMPASS families

Piunti, A., & Shilatifard, A. (2016) · Science · doi:10.1126/science.aad9780 · Cited by 524 · see citing works

H3K4 mono- and di-methyltransferase MLL4 is required for enhancer activation during cell differentiation

Lee, J.-E., Wang, C., Xu, S., Cho, Y.-W., Wang, L., Feng, X., Baldridge, A., Sartorelli, V., Zhuang, L., Peng, W., et al. (2013) · eLife · doi:10.7554/elife.01503 · Cited by 522 · see citing works

Clinical implications of genomic alterations in the tumour and circulation of pancreatic cancer patients

Sausen, M., Phallen, J., Adleff, V., Jones, S., Leary, R. J., Barrett, M. T., Anagnostou, V., Parpart-Li, S., Murphy, D., Kay Li, Q., et al. (2015) · Nature Communications · doi:10.1038/ncomms8686 · Cited by 484 · see citing works

Disruption of KMT2D perturbs germinal center B cell development and promotes lymphomagenesis

Zhang, J., Dominguez-Sola, D., Hussein, S., Lee, J., Holmes, A. B., Bansal, M., Vlasevska, S., Mo, T., Tang, H., Basso, K., et al. (2015) · Nature Medicine · doi:10.1038/nm.3940 · Cited by 463 · see citing works

The MLL3/MLL4 Branches of the COMPASS Family Function as Major Histone H3K4 Monomethylases at Enhancers

Hu, D., Gao, X., Morgan, M. A., Herz, H.-M., Smith, E. R., & Shilatifard, A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01181-13 · Cited by 439 · see citing works

The histone lysine methyltransferase KMT2D sustains a gene expression program that represses B cell lymphoma development

Ortega-Molina, A., Boss, I. W., Canela, A., Pan, H., Jiang, Y., Zhao, C., Jiang, M., Hu, D., Agirre, X., Niesvizky, I., et al. (2015) · Nature Medicine · doi:10.1038/nm.3943 · Cited by 438 · see citing works

PI3K inhibition results in enhanced estrogen receptor function and dependence in hormone receptor–positive breast cancer

Bosch, A., Li, Z., Bergamaschi, A., Ellis, H., Toska, E., Prat, A., Tao, J. J., Spratt, D. E., Viola, N. T., Castel, P., et al. (2015) · Science Translational Medicine · doi:10.1126/scitranslmed.aaa4442 · Cited by 432 · see citing works

Mll3 and Mll4 Facilitate Enhancer RNA Synthesis and Transcription from Promoters Independently of H3K4 Monomethylation

Dorighi, K. M., Swigut, T., Henriques, T., Bhanu, N. V., Scruggs, B. S., Nady, N., Still, C. D., Garcia, B. A., Adelman, K., & Wysocka, J. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.04.018 · Cited by 403 · see citing works

COMPASS, a Histone H3 (Lysine 4) Methyltransferase Required for Telomeric Silencing of Gene Expression

Krogan, N. J., Dover, J., Khorrami, S., Greenblatt, J., Schneider, J., Johnston, M., & Shilatifard, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200023200 · Cited by 403 · see citing works

Enhancer-associated H3K4 monomethylation by Trithorax-related, the <i>Drosophila</i> homolog of mammalian Mll3/Mll4

Herz, H.-M., Mohan, M., Garruss, A. S., Liang, K., Takahashi, Y.-H., Mickey, K., Voets, O., Verrijzer, C. P., & Shilatifard, A. (2012) · Genes &amp; Development · doi:10.1101/gad.201327.112 · Cited by 388 · see citing works

The expanding landscape of ‘oncohistone’ mutations in human cancers

Nacev, B. A., Feng, L., Bagert, J. D., Lemiesz, A. E., Gao, J., Soshnev, A. A., Kundra, R., Schultz, N., Muir, T. W., & Allis, C. D. (2019) · Nature · doi:10.1038/s41586-019-1038-1 · Cited by 384 · see citing works

The role of enhancers in cancer

Sur, I., & Taipale, J. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.62 · Cited by 382 · see citing works

Knockdown of ALR (MLL2) Reveals ALR Target Genes and Leads to Alterations in Cell Adhesion and Growth

Issaeva, I., Zonis, Y. A., Rozovskaia, T., Orlovsky, K., Croce, C. M., Nakamura, T., Mazo, A., Eisenbach, L., & Canaani, E. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01506-06 · Cited by 380 · see citing works

Super-Enhancer-Driven Transcriptional Dependencies in Cancer

Sengupta, S., & George, R. E. (2017) · Trends in cancer · doi:10.1016/j.trecan.2017.03.006 · Cited by 349 · see citing works

The genomic landscape of metastatic breast cancer highlights changes in mutation and signature frequencies

Angus, L., Smid, M., Wilting, S. M., van Riet, J., van Hoeck, A., Nguyen, L., Nik‐Zainal, S., Steenbruggen, T. G., Tjan‐Heijnen, V. C. G., Labots, M., et al. (2019) · Nature Genetics · doi:10.1038/s41588-019-0507-7 · Cited by 311 · see citing works

UTX and UTY Demonstrate Histone Demethylase-Independent Function in Mouse Embryonic Development

Shpargel, K. B., Sengoku, T., Yokoyama, S., & Magnuson, T. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002964 · Cited by 310 · see citing works

MLL3 Is a Haploinsufficient 7q Tumor Suppressor in Acute Myeloid Leukemia

Chen, C., Liu, Y., Rappaport, A., Kitzing, T. M., Schultz, N. D., Zhao, Z., Shroff, A., Dickins, R. A., Vakoc, C. R., Bradner, J. E., et al. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.03.016 · Cited by 308 · see citing works

Histone H3 lysine 4 methyltransferase KMT2D

Froimchuk, E., Jang, Y., & Ge, K. (2017) · Gene · doi:10.1016/j.gene.2017.06.056 · Cited by 300 · see citing works

Genetics of diffuse large B-cell lymphoma

Pasqualucci, L., & Dalla‐Favera, R. (2018) · Blood · doi:10.1182/blood-2017-11-764332 · Cited by 284 · see citing works

COMPASS and SWI/SNF complexes in development and disease

Cenik, B. K., & Shilatifard, A. (2020) · Nature Reviews Genetics · doi:10.1038/s41576-020-0278-0 · Cited by 269 · see citing works

PI3K pathway regulates ER-dependent transcription in breast cancer through the epigenetic regulator KMT2D

Toska, E., Osmanbeyoglu, H. U., Castel, P., Chan, C., Hendrickson, R. C., Elkabets, M., Dickler, M. N., Scaltriti, M., Leslie, C. S., Armstrong, S. A., et al. (2017) · Science · doi:10.1126/science.aah6893 · Cited by 262 · see citing works

The BRCT-Domain Containing Protein PTIP Links PAX2 to a Histone H3, Lysine 4 Methyltransferase Complex

Patel, S. R., Kim, D., Levitan, I., & Dressler, G. R. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.09.004 · Cited by 249 · see citing works

UTX and MLL4 Coordinately Regulate Transcriptional Programs for Cell Proliferation and Invasiveness in Breast Cancer Cells

Kim, J., Sharma, A., Dhar, S. S., Lee, S.-H., Gu, B., Chan, C., Lin, H., & Lee, M. G. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-1896 · Cited by 246 · see citing works

50+ years of eukaryotic transcription: an expanding universe of factors and mechanisms

Roeder, R. G. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0287-x · Cited by 246 · see citing works

Structural basis for activity regulation of MLL family methyltransferases

Li, Y., Han, J., Zhang, Y., Cao, F., Liu, Z., Li, S., Wu, J., Hu, C., Wang, Y., Jin, S., et al. (2016) · Nature · doi:10.1038/nature16952 · Cited by 244 · see citing works

KMT2D Deficiency Impairs Super-Enhancers to Confer a Glycolytic Vulnerability in Lung Cancer

Alam, H., Tang, M., Maitituoheti, M., Dhar, S. S., Kumar, M., Han, C. Y., Ambati, C. R., Amin, S. B., Gu, B., Chen, T.-Y., et al. (2020) · Cancer Cell · doi:10.1016/j.ccell.2020.03.005 · Cited by 243 · see citing works

A UTX-MLL4-p300 Transcriptional Regulatory Network Coordinately Shapes Active Enhancer Landscapes for Eliciting Transcription

Wang, S., Tang, Z., Chen, C.-W. D., Shimada, M., Koche, R. P., Wang, L.-H., Nakadai, T., Chramiec, A. G., Krivtsov, A. V., Armstrong, S. A., et al. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.06.028 · Cited by 242 · see citing works

Enhancer priming by H3K4 methyltransferase MLL4 controls cell fate transition

Wang, C., Lee, J.-E., Lai, B., Macfarlan, T. S., Xu, S., Zhuang, L., Liu, C., Peng, W., & Ge, K. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1606857113 · Cited by 242 · see citing works

Identification of H3K4me1-associated proteins at mammalian enhancers

Local, A., Huang, H., de Albuquerque, C. P., Singh, N., Lee, A. Y., Wang, W., Wang, C., Hsia, J. E., Shiau, A. K., Ge, K., et al. (2017) · Nature Genetics · doi:10.1038/s41588-017-0015-6 · Cited by 234 · see citing works

Lung neuroendocrine tumours: deep sequencing of the four World Health Organization histotypes reveals chromatin‐remodelling genes as major players and a prognostic role for TERT , RB1 , MEN1 and KMT2D

Simbolo, M., Mafficini, A., Sikora, K. O., Fassan, M., Barbi, S., Corbo, V., Mastracci, L., Rusev, B. C., Grillo, F., Vicentini, C., et al. (2016) · The Journal of Pathology · doi:10.1002/path.4853 · Cited by 234 · see citing works

Activation of gene expression by adenovirus and herpesvirus regulatory genes acting in trans and by a cis-acting adenovirus enhancer element

Imperiale, M. J., Feldman, L. T., & Nevins, J. R. (1983) · Cell · doi:10.1016/0092-8674(83)90215-5 · Cited by 233 · see citing works

Regulatory Enhancer–Core-Promoter Communication via Transcription Factors and Cofactors

Zabidi, M. A., & Stark, A. (2016) · Trends in Genetics · doi:10.1016/j.tig.2016.10.003 · Cited by 228 · see citing works

UTX regulates mesoderm differentiation of embryonic stem cells independent of H3K27 demethylase activity

Wang, C., Lee, J., Cho, Y., Xiao, Y., Jin, Q., Liu, C., & Ge, K. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1204166109 · Cited by 219 · see citing works

Histone H3K4 monomethylation catalyzed by Trr and mammalian COMPASS-like proteins at enhancers is dispensable for development and viability

Rickels, R., Herz, H.-M., Sze, C. C., Cao, K., Morgan, M. A., Collings, C. K., Gause, M., Takahashi, Y.-H., Wang, L., Rendleman, E. J., et al. (2017) · Nature Genetics · doi:10.1038/ng.3965 · Cited by 217 · see citing works

Identification of somatic mutations in non-small cell lung carcinomas using whole-exome sequencing

Liu, P., Morrison, C., Wang, L., Xiong, D., Vedell, P. T., Cui, P., Hua, X., Ding, F. H., Lü, Y., James, M. A., et al. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs148 · Cited by 207 · see citing works

Histone H3 lysine 4 monomethylation modulates long-range chromatin interactions at enhancers

Yan, J., Chen, S.-A. A., Local, A., Liu, T., Qiu, Y., Lee, A. Y., Jung, I., Preißl, S., Rivera, C. M., Wang, C., et al. (2018) · Cell Research · doi:10.1038/cr.2018.1 · Cited by 198 · see citing works

DNA-damage-induced differentiation of leukaemic cells as an anti-cancer barrier

Santos, M. A., Faryabi, R. B., Ergen, A. V., Day, A., Malhowski, A. J., Canela, A., Onozawa, M., Lee, J., Callén, E., Gutierrez‐Martinez, P., et al. (2014) · Nature · doi:10.1038/nature13483 · Cited by 195 · see citing works

MLL3/MLL4 are required for CBP/p300 binding on enhancers and super-enhancer formation in brown adipogenesis

Lai, B., Lee, J.-E., Jang, Y., Wang, L., Peng, W., & Ge, K. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx234 · Cited by 191 · see citing works

New Insights into mTOR Signaling: mTORC2 and Beyond

Alessi, D. R., Pearce, L. R., & García‐Martínez, J. M. (2009) · Science Signaling · doi:10.1126/scisignal.267pe27 · Cited by 188 · see citing works

Targeted inactivation of MLL3 histone H3–Lys-4 methyltransferase activity in the mouse reveals vital roles for MLL3 in adipogenesis

Lee, J., Saha, P., Yang, Q.-H., Lee, S., Park, J. Y., Suh, Y., Lee, S., Chan, L., Roeder, R. G., & Lee, J. W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810100105 · Cited by 187 · see citing works

Resetting the epigenetic balance of Polycomb and COMPASS function at enhancers for cancer therapy

Wang, L., Zhao, Z., Ozark, P. A., Fantini, D., Marshall, S. A., Rendleman, E. J., Cozzolino, K., Louis, N., He, X., Morgan, M. A., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0034-6 · Cited by 184 · see citing works

Cytogenetic, Molecular Genetic, and Clinical Characteristics of Acute Myeloid Leukemia With a Complex Karyotype

Mrózek, K. (2008) · Seminars in Oncology · doi:10.1053/j.seminoncol.2008.04.007 · Cited by 182 · see citing works

Visualizing transcription factor dynamics in living cells

Liu, Z. J., & Tjian, R. (2018) · The Journal of Cell Biology · doi:10.1083/jcb.201710038 · Cited by 182 · see citing works

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 175 · see citing works

COMPASS Ascending: Emerging clues regarding the roles of MLL3/KMT2C and MLL2/KMT2D proteins in cancer

Fagan, R. J., & Dingwall, A. K. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.05.024 · Cited by 174 · see citing works

SET1 and p300 Act Synergistically, through Coupled Histone Modifications, in Transcriptional Activation by p53

Tang, Z., Chen, W., Shimada, M., Nguyen, U. T. T., Kim, J., Sun, X., Sengoku, T., McGinty, R. K., Fernandez, J., Muir, T. W., et al. (2013) · Cell · doi:10.1016/j.cell.2013.06.027 · Cited by 165 · see citing works

Enhancer Logic and Mechanics in Development and Disease

Rickels, R. A., & Shilatifard, A. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.04.003 · Cited by 165 · see citing works

FOXA1 Directs H3K4 Monomethylation at Enhancers via Recruitment of the Methyltransferase MLL3

Jozwik, K. M., Chernukhin, I. V., Sérandour, A. A., Nagarajan, S., & Carroll, J. S. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.11.028 · Cited by 164 · see citing works

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 · see citing works

Novel Somatic and Germline Mutations in Cancer Candidate Genes in Glioblastoma, Melanoma, and Pancreatic Carcinoma

Balakrishnan, A., Bleeker, F. E., Lamba, S., Rodolfo, M., Daniotti, M., Scarpa, A., van Tilborg, A. A., Leenstra, S., Zanon, C., & Bardelli, A. (2007) · Cancer Research · doi:10.1158/0008-5472.can-07-0065 · Cited by 161 · see citing works

PTIP Promotes Chromatin Changes Critical for Immunoglobulin Class Switch Recombination

Daniel, J. A., Santos, M. A., Wang, Z., Zang, C., Schwab, K. R., Janković, M., Filsuf, D., Chen, H. T., Gazumyan, A., Yamane, A., et al. (2010) · Science · doi:10.1126/science.1187942 · Cited by 160 · see citing works

HOXA9 Reprograms the Enhancer Landscape to Promote Leukemogenesis

Sun, Y., Zhou, B., Mao, F., Xu, J., Miao, H., Zou, Z., Phuc Khoa, L. T., Jang, Y., Cai, S., Witkin, M., et al. (2018) · Cancer Cell · doi:10.1016/j.ccell.2018.08.018 · Cited by 152 · see citing works

MLL4 Is Required to Maintain Broad H3K4me3 Peaks and Super-Enhancers at Tumor Suppressor Genes

Dhar, S. S., Zhao, D., Lin, T., Gu, B., Pal, K., Wu, S. J., Alam, H., Lv, J., Yun, K., Gopalakrishnan, V., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.04.028 · Cited by 145 · see citing works

Chromatin modifying gene mutations in follicular lymphoma

Green, M. R. (2017) · Blood · doi:10.1182/blood-2017-08-737361 · Cited by 141 · see citing works

WRAD: enabler of the SET1-family of H3K4 methyltransferases

Ernst, P., & Vakoc, C. R. (2012) · Briefings in Functional Genomics · doi:10.1093/bfgp/els017 · Cited by 140 · see citing works

UTX/KDM6A Loss Enhances the Malignant Phenotype of Multiple Myeloma and Sensitizes Cells to EZH2 inhibition

Ezponda, T., Dupéré-Richer, D., Will, C., Small, E. C., Varghese, N., Patel, T., Nabet, B., Popovic, R., Oyer, J. A., Bulic, M., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.09.078 · Cited by 139 · see citing works

KMT2C mediates the estrogen dependence of breast cancer through regulation of ERα enhancer function

Gala, K. P., Li, Q., Sinha, A., Razavi, P., Dorso, M. A., Sánchez-Vega, F., Chung, Y. R., Hendrickson, R. C., Hsieh, J. J.-D., Berger, M. F., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0273-5 · Cited by 133 · see citing works

KMT2D maintains neoplastic cell proliferation and global histone H3 lysine 4 monomethylation

Guo, C., Chen, L. H., Huang, Y., Chang, C., Wang, P., Pirozzi, C. J., Qin, X., Bao, X., Greer, P. K., McLendon, R. E., et al. (2013) · Oncotarget · doi:10.18632/oncotarget.1555 · Cited by 132 · see citing works

Drosophila UTX Is a Histone H3 Lys27 Demethylase That Colocalizes with the Elongating Form of RNA Polymerase II

Smith, E. R., Lee, M. G., Winter, B., Droz, N. M., Eissenberg, J. C., Shiekhattar, R., & Shilatifard, A. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01504-07 · Cited by 129 · see citing works

Small Cell Lung Cancer Exhibits Frequent Inactivating Mutations in the Histone Methyltransferase KMT2D/MLL2 : CALGB 151111 (Alliance)

Augert, A., Zhang, Q., Bates, B. M., Cui, M., Wang, X., Wildey, G. M., Dowlati, A., & MacPherson, D. P. (2016) · Journal of Thoracic Oncology · doi:10.1016/j.jtho.2016.12.011 · Cited by 115 · see citing works

Next-generation sequencing reveals frequent consistent genomic alterations in small cell undifferentiated lung cancer

Ross, J. S., Wang, K., Elkadi, O., Tarasen, A. J., Foulke, L., Sheehan, C. E., Otto, G. A., Palmer, G. A., Yelensky, R., Lipson, D., et al. (2014) · Journal of Clinical Pathology · doi:10.1136/jclinpath-2014-202447 · Cited by 104 · see citing works

A New Family of Nuclear Receptor Coregulators That Integrate Nuclear Receptor Signaling through CREB-Binding Protein

Mahajan, M., & Samuels, H. H. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.14.5048-5063.2000 · Cited by 103 · see citing works

Utx Is Required for Proper Induction of Ectoderm and Mesoderm during Differentiation of Embryonic Stem Cells

Morales, C., Laugesen, A., & Helin, K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060020 · Cited by 98 · see citing works

Clinical correlation of extensive-stage small-cell lung cancer genomics

Dowlati, A., Lipka, M. B., McColl, K. S., Dabir, S., Behtaj, M., Kresak, A. M., Miron, A., Yang, M., Sharma, N., Fu, P., et al. (2016) · Annals of Oncology · doi:10.1093/annonc/mdw005 · Cited by 88 · see citing works

The Hippo effector Yorkie activates transcription by interacting with a histone methyltransferase complex through Ncoa6

Qing, Y., Yin, F., Wang, W., Zheng, Y., Guo, P., Schozer, F., Deng, H., & Pan, D. (2014) · eLife · doi:10.7554/elife.02564 · Cited by 72 · see citing works

Frequent Alteration of MLL3 Frameshift Mutations in Microsatellite Deficient Colorectal Cancer

Watanabe, Y., Castoro, R. J., Kim, H. S., North, B., Oikawa, R., Hiraishi, T., Ahmed, S., Chung, W., Cho, M.-Y., Toyota, M., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0023320 · Cited by 71 · see citing works

Role of PTIP in Class Switch Recombination and Long-Range Chromatin Interactions at the Immunoglobulin Heavy Chain Locus

Schwab, K. R., Patel, S. R., & Dressler, G. R. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.00990-10 · Cited by 70 · see citing works

KMT2D/MLL2 inactivation is associated with recurrence in adult-type granulosa cell tumors of the ovary

Hillman, R. T., Celestino, J., Terranova, C. J., Beird, H. C., Gumbs, C. E., Little, L., Nguyen, T., Thornton, R., Tippen, S. P., Zhang, J., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-04950-x · Cited by 70 · see citing works

Histone H3K27 Trimethylation Inhibits H3 Binding and Function of SET1-Like H3K4 Methyltransferase Complexes

Kim, D., Tang, Z., Shimada, M., Fierz, B., Houck-Loomis, B. R., Bar‐Dagan, M., Lee, S., Lee, S., Muir, T. W., Roeder, R. G., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00601-13 · Cited by 68 · see citing works

PI3K Inhibition Activates SGK1 via a Feedback Loop to Promote Chromatin-Based Regulation of ER-Dependent Gene Expression

Toska, E., Castel, P., Chhangawala, S., Arruabarrena-Aristorena, A., Chan, C., Hristidis, V. C., Cocco, E., Sallaku, M., Xu, G., Park, J., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.111 · Cited by 68 · see citing works

Nuclear receptor coactivator/coregulator NCoA6(NRC) is a pleiotropic coregulator involved in transcription, cell survival, growth and development

Mahajan, M., & Samuels, H. H. (2008) · Nuclear Receptor Signaling · doi:10.1621/nrs.06002 · Cited by 63 · see citing works

Proteomic profiling identifies key coactivators utilized by mutant ERα proteins as potential new therapeutic targets

Gates, L. A., Gu, G., Chen, Y., Rohira, A. D., Lei, J. T., Hamilton, R. A., Yu, Y., Lonard, D. M., Wang, J., Wang, S., et al. (2018) · Oncogene · doi:10.1038/s41388-018-0284-2 · Cited by 62 · see citing works

Expression Levels of KMT2C and SLC20A1 Identified by Information-theoretical Analysis Are Powerful Prognostic Biomarkers in Estrogen Receptor-positive Breast Cancer

Sato, K., & Akimoto, K. (2016) · Clinical Breast Cancer · doi:10.1016/j.clbc.2016.11.005 · Cited by 55 · see citing works

Far upstream sequences are required for efficient transcription from the adenovirus-2 E1A transcription unit

Sassone‐Corsi, P., Hen, R., Borrelli, E., Leff, T., & Chambon, P. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.24.8735 · Cited by 41 · see citing works

Mutation of epigenetic regulators TET2 and MLL3 in patients with HTLV-I-induced acute adult T-cell leukemia

Yeh, C., Bai, X. T., Moles, R., Ratner, L., Waldmann, T. A., Watanabe, T., & Nicot, C. (2016) · Molecular Cancer · doi:10.1186/s12943-016-0500-z · Cited by 39 · see citing works

Exome sequencing identifies frequent mutation of MLL2 in non–small cell lung carcinoma from Chinese patients

Yin, S., Yang, J., Lin, B., Deng, W., Zhang, Y., Yi, X., Shi, Y., Tao, Y., Cai, J., Wu, C., et al. (2014) · Scientific Reports · doi:10.1038/srep06036 · Cited by 38 · see citing works

A PTIP–PA1 subcomplex promotes transcription for IgH class switching independently from the associated MLL3/MLL4 methyltransferase complexPreprint

Starnes, L. M., Su, D., Pikkupeura, L. M., Weinert, B. T., Santos, M. A., Mund, A., Soria, R., Cho, Y., Pozdnyakova, I., Højfeldt, M. K., et al. (2016) · Genes & Development · doi:10.1101/gad.268797.115 · Cited by 36 · see citing works

Restoration of KMT2C/MLL3 in human colorectal cancer cells reinforces genome-wide H3K4me1 profiles and influences cell growth and gene expression

Larsson, C., Cordeddu, L., Siggens, L., Pandzic, T., Kundu, S., He, L., Ali, M. A., Pristovšek, N., Hartman, K., Ekwall, K., et al. (2020) · Clinical Epigenetics · doi:10.1186/s13148-020-00863-z · Cited by 35 · see citing works

Mutant p53 regulates enhancer-associated H3K4 monomethylation through interactions with the methyltransferase MLL4

Rahnamoun, H., Hong, J., Sun, Z., Lee, J. H., Lu, H., & Lauberth, S. M. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003387 · Cited by 34 · see citing works

A small UTX stabilization domain of Trr is conserved within mammalian MLL3-4/COMPASS and is sufficient to rescue loss of viability in null animalsPreprint

Rickels, R. A., Wang, L., Iwanaszko, M., Ozark, P. A., Morgan, M. A., Piunti, A., Khalatyan, N., Soliman, S. H. A., Rendleman, E. J., Savas, J. N., et al. (2020) · Genes & Development · doi:10.1101/gad.339762.120 · Cited by 33 · see citing works

Enhancer Talk

Snetkova, V., & Skok, J. A. (2018) · Epigenomics · doi:10.2217/epi-2017-0157 · Cited by 32 · see citing works

Histone methyltransferases regulate the transcriptional expression of ERα and the proliferation of tamoxifen-resistant breast cancer cells

Kim, S.-S., Lee, M. H., & Lee, M. (2020) · Breast Cancer Research and Treatment · doi:10.1007/s10549-019-05517-0 · Cited by 29 · see citing works

Role of UTX in Retinoic Acid Receptor-Mediated Gene Regulation in Leukemia

Rocha-Viegas, L., Villa, R., Gutiérrez, A., Iriondo, O., Shiekhattar, R., & Croce, L. D. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00839-14 · Cited by 28 · see citing works

Genetic mutational status of genes regulating epigenetics: Role of the histone methyltransferase KMT2D in triple negative breast tumors

Morcillo-García, S., Noblejas‐López, M. D. M., Nieto‐Jiménez, C., Pérez‐Peña, J., Nuncia‐Cantarero, M., Győrffy, B., Amir, E., Pandiella, A., Galán‐Moya, E. M., & Ocaña, A. (2019) · PLoS ONE · doi:10.1371/journal.pone.0209134 · Cited by 26 · see citing works

Structural basis of histone H2A lysine 119 deubiquitination by Polycomb repressive deubiquitinase BAP1/ASXL1

Thomas, J. F., Valencia‐Sánchez, M. I., Tamburri, S., Gloor, S. L., Rustichelli, S., Godínez-López, V., Ioannes, P. D., Lee, R., Abini-Agbomson, S., Gretarsson, K. H., et al. (2023) · Science Advances · doi:10.1126/sciadv.adg9832 · Cited by 53 · see citing works

ASXL1/2 mutations and myeloid malignancies

Medina, E. A., Delma, C. R., & Yang, F. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01336-x · Cited by 54 · see citing works

Glucocorticoid receptor signaling: intricacies and therapeutic opportunities

Clarisse, D., Moortel, L. V., Leene, C. V., Gevaert, K., & Bosscher, K. D. (2024) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.01.012 · Cited by 49 · see citing works

Alterations of Chromatin Regulators in the Pathogenesis of Urinary Bladder Urothelial Carcinoma

Hoffmann, M. J., & Schulz, W. A. (2021) · Cancers · doi:10.3390/cancers13236040 · Cited by 37 · see citing works

Dynamic regulation of BDNF gene expression by estradiol and lncRNA HOTAIR

Deb, P., Chini, A., Guha, P., Rishi, A., Bhan, A., Brady, B., Perrotti, L. I., & Mandal, S. S. (2023) · Gene · doi:10.1016/j.gene.2023.148055 · Cited by 34 · see citing works

KMT2C and KMT2D aberrations in breast cancer

Tinsley, E. A., Bredin, P., Toomey, S., Hennessy, B. T., & Furney, S. J. (2024) · Trends in cancer · doi:10.1016/j.trecan.2024.02.003 · Cited by 33 · see citing works

Deciphering the interplay of histone post-translational modifications in cancer: Co-targeting histone modulators for precision therapy

Kawaf, R. R., Ramadan, W. S. H., & El‐Awady, R. (2024) · Life Sciences · doi:10.1016/j.lfs.2024.122639 · Cited by 27 · see citing works

Polysaccharides from Platycodonis Radix ameliorated respiratory syncytial virus-induced epithelial cell apoptosis and inflammation through activation of miR-181a-mediated Hippo and SIRT1 pathways

Li, J., Liu, M., Lv, J.-N., Chen, R., Ding, K., & He, J. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2021.108510 · Cited by 23 · see citing works

LncRNA MIR31HG fosters stemness malignant features of non-small cell lung cancer via H3K4me1- and H3K27Ace-mediated GLI2 expression

Chen, W., Wang, F., Yu, X., Qi, J., Dong, H., Cui, B., Zhang, Q., Wu, Y., An, J., Ni, N., et al. (2023) · Oncogene · doi:10.1038/s41388-023-02883-4 · Cited by 22 · see citing works

Identification of putative enhancer-like elements predicts regulatory networks active in planarian adult stem cells

Neiro, J., Sridhar, D., Dattani, A., & Aboobaker, A. A. (2022) · eLife · doi:10.7554/elife.79675 · Cited by 20 · see citing works

Bivalent chromatin: a developmental balancing act tipped in cancer

Glancy, E., Choy, N., & Eckersley-Maslin, M. A. (2024) · Biochemical Society Transactions · doi:10.1042/bst20230426 · Cited by 23 · see citing works

FXR-regulated COX6A2 triggers mitochondrial apoptosis of pancreatic β-cell in type 2 diabetes

Shao, L., Kong, X., Lv, S., Shu, X., Ma, X., Ai, X., Yan, D., & Ying, Y. (2024) · Cell Death and Disease · doi:10.1038/s41419-024-07302-4 · Cited by 16 · see citing works

Molecular insights of KMT2D and clinical aspects of Kabuki syndrome type 1

Golden, C. S., Williams, S., & Serrano, M. D. L. Á. (2023) · Birth Defects Research · doi:10.1002/bdr2.2183 · Cited by 14 · see citing works

Clustered PHD domains in KMT2/MLL proteins are attracted by H3K4me3 and H3 acetylation-rich active promoters and enhancers

Stroynowska-Czerwinska, A. M., Klimczak, M., Pastor, M., Kazrani, A. A., Misztal, K., & Bochtler, M. (2023) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04651-1 · Cited by 14 · see citing works

ASXLs binding to the PHD2/3 fingers of MLL4 provides a mechanism for the recruitment of BAP1 to active enhancers

Zhang, Y., Xie, G., Lee, J., Zandian, M., Sudarshan, D., Estavoyer, B., Benz, C., Viita, T., Asgaritarghi, G., Lachance, C., et al. (2024) · Nature Communications · doi:10.1038/s41467-024-49391-x · Cited by 13 · see citing works

A Virus-Packageable CRISPR System Identifies Host Dependency Factors Co-Opted by Multiple HIV-1 Strains

Montoya, V. R., Ready, T. M., Felton, A., Fine, S. R., OhAinle, M., & Emerman, M. (2023) · mBio · doi:10.1128/mbio.00009-23 · Cited by 13 · see citing works

Kabuki syndrome stem cell models reveal locus specificity of histone methyltransferase 2D (KMT2D/MLL4)

Jefri, M., Zhang, X., Stumpf, P. S., Zhang, L., Peng, H., Hettige, N. C., Théroux, J., Aouabed, Z., Wilson, K., Deshmukh, S., et al. (2022) · Human Molecular Genetics · doi:10.1093/hmg/ddac121 · Cited by 11 · see citing works

HNF4A guides the MLL4 complex to establish and maintain H3K4me1 at gene regulatory elements

Thakur, A., Park, K., Cullum, R., Fuglerud, B. M., Khoshnoodi, M., Drissler, S., Stephan, T. L., Lotto, J., Kim, D., Gonzalez, F. J., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-05835-0 · Cited by 10 · see citing works

Histone lysine methylation modifiers controlled by protein stability

Park, S., Cho, J. H., Kim, J., & Kim, J. (2024) · Experimental & Molecular Medicine · doi:10.1038/s12276-024-01329-5 · Cited by 9 · see citing works

Histone lysine methyltransferases MLL3 and MLL4 direct gene expression to produce platelets efficiently

Gao, G., Moreira, J. D., Das, P., Lin, K., Ge, K., Chen, T., Lu, Y., & Santos, M. A. (2025) · Nature Communications · doi:10.1038/s41467-025-61247-6 · Cited by 8 · see citing works

Histone methyltransferase KMT2D contributes to the protection of myocardial ischemic injury

Liu, S.-B., Meng, X., Li, Y., Wang, J., Guo, H., Wang, C., & Zhu, B. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.946484 · Cited by 7 · see citing works

The MLL3/GRHL2 complex regulates malignant transformation and anti-tumor immunity in squamous cancer

Nam, C., Huang, G., Zheng, Y., Zhao, H., Pan, Y., Hu, B., Wenger, T. A., Van, H. T., Xu, L., Li, E., et al. (2025) · The Journal of Experimental Medicine · doi:10.1084/jem.20240758 · Cited by 6 · see citing works

Trajectories from single-cells to PAX5-driven leukemia reveal PAX5-MYC interplay in vivo

Auer, F., Morcos, M. N. F., Sipola, M., Akhtar, I., Moisio, S., Vogt, J., Haag, R., Lahnalampi, M., Tuononen, T. J., Hänel, A., et al. (2025) · Leukemia · doi:10.1038/s41375-025-02626-2 · Cited by 6 · see citing works

Somatic KMT2D loss-of-function mutations in lung squamous cell carcinoma: a single-center cohort study

Fang, Z., Wu, X., Li, X., Wang, C., Zhao, Y., Zhang, Q., Jablonska, P. A., Rosa, A. L., Dempke, W. C. M., Furqan, M., et al. (2024) · Journal of Thoracic Disease · doi:10.21037/jtd-24-134 · Cited by 5 · see citing works

KMT2D: A key emerging epigenetic regulator in head and neck diseases and tumors

Wang, K., Zhan, F., Yang, X., Jiao, M., Wang, P., Zhang, H., Shang, W., Deng, J., & Wang, L. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123523 · Cited by 4 · see citing works

Single-Cell Transcriptome Analysis Defines Expression of Kabuki Syndrome-Associated KMT2D Targets and Interacting Partners

Enkhmandakh, B., Robson, P., Joshi, P., Vijaykumar, A., Shin, D., Mina, M., & Bayarsaihan, D. (2022) · Stem Cells International · doi:10.1155/2022/4969441 · Cited by 4 · see citing works

Intestinal-Type Adenocarcinoma in Head and Neck: Dissecting Oncogenic Gene Alterations Through Whole Transcriptome and Exome Analysis

Bell, D., Bell, A., Weber, R. S., & Hanna, E. Y. (2023) · Modern Pathology · doi:10.1016/j.modpat.2023.100372 · Cited by 3 · see citing works

A Recent Update on the Epigenetic Repertoire and Chromatin Modifying Therapy in Diabetes Mellitus: A Comprehensive Review

Wang, X., Zhao, D., Beeraka, N. M., Spandana, T., Sri, C. D., Nishanth, V. V., Uthaiah, C. A., Leihang, Z., Sugur, K., Liu, J., et al. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220802090446 · Cited by 3 · see citing works

The COMPASS complex maintains the metastatic capacity imparted by a subpopulation of cells in UPS

Ban, G. I., Puviindran, V., Yu, X., Nadesan, P., Tang, Y. J., Ou, J., Guardino, N. J., Nakagawa, M., Browne, M. R., Wallace, A., et al. (2024) · iScience · doi:10.1016/j.isci.2024.110187 · Cited by 2 · see citing works

Antagonism and selective modulation of the human glucocorticoid receptor both reduce recruitment of p300/CBP and the Mediator complexPreprint

Moortel, L. V., Verhee, A., Houtman, R., Melchers, D., Delhaye, L., Thommis, J., Gevaert, K., Eyckerman, S., & Bosscher, K. D. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.15.540854 · Cited by 2 · see citing works

Identification of biomarkers and enrichment analysis in pancreatic adenocarcinoma through transcriptome analysis

Shariff, E. A., Khan, A. U., Hasan, Z., Azharuddin, A., Tabassum, R., & Al-Enazi, K. M. (2025) · International Journal of Hepatobiliary and Pancreatic Diseases · doi:10.5348/100106z04es2025ra · Cited by 1 · see citing works

The MLL4: Roles in cell differentiation, adipogenesis and cancer

Zhang, Y., Lv, K., Ma, X., Wang, L., & Xu, Y. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117371 · Cited by 1 · see citing works

Targeting lysine methyltransferase 2C deficiency: New frontiers in breast cancer therapy and prognosis

Tong, S., Wang, Q., Chen, Y., Bo, Z., Zhang, Y., & Liu, Y. (2026) · Clinical and Translational Medicine · doi:10.1002/ctm2.70617 · Cited by 1 · see citing works

SMARCA4 activation engages FOSL1 to drive enhancer reprogramming and tumorigenic phenotypes in SMARCA4-deficient LUAD cells

Yang, H.-J., Kim, E.-J., Kim, S., Song, S.-H., & Kim, T. (2026) · Cell Death Discovery · doi:10.1038/s41420-026-03100-3 · Cited by 1 · see citing works

BCORL1 S878G, GNB1 G116S, SH2B3 A536T, and KMT2D S3708R tetramutation co-contribute to a pediatric acute myeloid leukemia: Case report and literature review

Wang, L., Chen, S., Shen, Y., & Si, P. (2022) · Frontiers in Pediatrics · doi:10.3389/fped.2022.993952 · Cited by 1 · see citing works

Using Sister Chromatid Exchange Assay to Detect Homologous Recombination Deficiency in Epigenetically Deregulated Urothelial Carcinoma Cells

Rampias, T. N., & Klinakis, A. (2023) · Methods in molecular biology · doi:10.1007/978-1-0716-3291-8_7 · Cited by 1 · see citing works

Research progress of histone methylation modification in early embryonic development and related diseases

Bai, D., ZiHui, Y. A. N., ShanYao, L. I. U., WenQiang, L. I. U., & ShaoRong, G. A. O. (2023) · Scientia Sinica Vitae · doi:10.1360/ssv-2023-0134 · Cited by 1 · see citing works

Epigenetic modulation of cell fate during pancreas development.

Bele, S. D., Wokasch, A. S., & GANNON, M. A. (2023) · PubMed · Cited by 1 · see citing works

The role of chromatin-related epigenetic modulations in CAKUT

König, L., & Schmidts, M. (2025) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2024.11.006 · Cited by 1 · see citing works

A Virus-Packageable CRISPR System Identifies Host Dependency Factors Across Multiple HIV-1 StrainsPreprint

Montoya, V. R., Ready, T. M., Felton, A., Fine, S. R., OhAinle, M., & Emerman, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.11.03.515041 · Cited by 1 · see citing works

Structural and Biochemical Analysis of Histone H3.1 Recognition Mechanisms by TonsukuPreprint

Couture, J., Davarinejad, H., Muñoz, M. A., Joshi, M., Sarvan, S., Ross, A., Brunzelle, J. S., & Alarcon, E. I. (2023) · SSRN Electronic Journal · doi:10.2139/ssrn.4500927

The tumor-maintaining function of UTX/KDM6A in DNA replication and the PARP1-dependent repair pathwayPreprint

Yeh, L.-W., Chen, J.-W., Yeh, J.-Y., Kao, M.-H., Hong, H.-C., Wu, S., Cheung, W., Liu, T.-Y., Aberin, M. A. E., Paas-Oliveros, E., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.05.31.596824

The tumor-maintaining function of UTX/KDM6A in DNA replication and the PARP1-dependent repair pathwayPreprint

Wang, S., Yeh, L.-W., Chen, J.-W., Yeh, J.-Y., Kao, M.-H., Hong, H.-C., Wu, S., Cheung, W., Liu, T.-Y., Aberin, M. A. E., et al. (2024) · Research Square · doi:10.21203/rs.3.rs-4620473/v1

KMT2C and KMT2D regulate skeletal development through stage-specific epigenetic control of chondrogenesis

Quickstad, G., Bikas, D. V., Bond, M. L., Vardabasso, S., Wyper, A. N., Park, Y.-K., Ge, K., Loeser, R. F., Magnuson, T., & Shpargel, K. B. (2026) · Bone Research · doi:10.1038/s41413-026-00584-8

Spatiotemporal dynamics of histone H3K27 demethylase during development

Tsai, Y., Chung, Y.-C., Yang, C., Lee, C.-H., Liu, C.-W., Huang, S.-M., & Wang, L.-H. (2025) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2025.104360

The Histone‐Lysine N‐Methyltransferase (KMT2) Family in Health and Disease

Wang, Q., Bo, Z., Zhang, Y., Chen, Y., Wang, Z., Tong, S., Xu, A., Zhang, G., & Liu, Y. (2026) · MedComm · doi:10.1002/mco2.70728

Epigenetic regulatory role of KMT2C and its interaction with miRNAs: New perspectives in cancer biology

Oktar, P. A., Babadag, S., Güneş, M. Y., Aydoğdu, G. Ö., & Ezer, Ü. (2026) · Gene Reports · doi:10.1016/j.genrep.2026.102513

SLA2 is Associated With Immune evasion and Exhaustion of CD8 + T Cells in Gastric Cancer

Zhang, Y., Li, X., & XIANG, R. (2026) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.71164

Decoding LncRNA-mediated epigenetic rewiring of protein lysine methyltransferases in cancer: A comprehensive review of mechanisms and therapeutic implications

Ibrahim, S., Ghazaly, H. E., Khella, M. S., & AbdelHamid, S. G. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.152625

Prdm15 deficiency perturbs hematopoietic stem and progenitor cell homeostasis

Dong, Q., Xiao, W., Huang, J., Sun, Z., Liang, M., Wang, M.-J., Wang, Q., Zong, X., Li, A., Wang, Y., et al. (2026) · Journal of genetics and genomics/Journal of Genetics and Genomics · doi:10.1016/j.jgg.2026.07.009

Kmt2c and Kmt2d histone methyltransferase deficiencies compromise macrophage function

Al, B., Jung, Y., Alvarez, Y., Scarpa, A., Hamid, A., Jang, Y., Ge, K., Domenico, E. D., Beyer, M. D., Weighardt, H., et al. (2026) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiag110

Long non-coding RNA-gm33782 exacerbates acute kidney injury by upregulating the PA1-MLL3/MLL4 complex and promoting histone H3 lysine 4 monomethylation-dependent forkhead box O3 enhancer activation

Tan, R., Jia, J., Bai, Q., Li, T., Wang, H., Xian-ying, L., Shu, J., Mao, N., Kantawong, F., & Wang, L. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.154449

Multifaceted role of genetic and epigenetic architecture of glucose homeostasis and diabetes

Khokhar, M. (2026) · npj Metabolic Health and Disease · doi:10.1038/s44324-026-00135-z

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 · see citing works

The MLL3/MLL4 Branches of the COMPASS Family Function as Major Histone H3K4 Monomethylases at Enhancers

Hu, D., Gao, X., Morgan, M. A., Herz, H.-M., Smith, E. R., & Shilatifard, A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01181-13 · Cited by 439 · see citing works

Enhancer epigenomic regulation in differentiation, development and cancer

Ge, K. (2018) · The FASEB Journal · doi:10.1096/fasebj.2018.32.1_supplement.524.5

Multiple Roles for the MLL/COMPASS Family in the Epigenetic Regulation of Gene Expression and in Cancer

Meeks, J. J., & Shilatifard, A. (2017) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-050216-034333 · Cited by 44 · see citing works

Enhancer regulation by H3K4me1 methyltransferases MLL3/MLL4

Ge, K. (2022) · The FASEB Journal · doi:10.1096/fasebj.2022.36.s1.l7540