Histone methyltransferase KMT2A: developmental regulation to oncogenic transformation

CpG islands and the regulation of transcription

Deaton, A. M., & Bird, A. (2011) · Genes & Development · doi:10.1101/gad.2037511 · Cited by 3,187 · see citing works

Cancer chemotherapy and beyond: Current status, drug candidates, associated risks and progress in targeted therapeutics

Anand, U., Dey, A., Chandel, A. K. S., Sanyal, R., Mishra, A., Pandey, D. K., Falco, V. D., Upadhyay, A., Kandimalla, R. J. L., Chaudhary, A., et al. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2022.02.007 · Cited by 1,936 · see citing works

Methylation of lysine 4 on histone H3: intricacy of writing and reading a single epigenetic mark

Ruthenburg, A. J., Allis, C. D., & Wysocka, J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.12.014 · Cited by 1,147 · see citing works

The COMPASS Family of Histone H3K4 Methylases: Mechanisms of Regulation in Development and Disease Pathogenesis

Shilatifard, A. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-051710-134100 · Cited by 1,091 · see citing works

MLL Targets SET Domain Methyltransferase Activity to Hox Gene Promoters

Milne, T. A., Briggs, S. D., Brock, H. W., Martin, M. E., Gibbs, D. Y., Allis, C. D., & Hess, J. L. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00741-4 · Cited by 1,051 · see citing works

Multivalent engagement of chromatin modifications by linked binding modules

Ruthenburg, A. J., Li, H., Patel, D. J., & Allis, C. D. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2298 · Cited by 1,015 · see citing works

Altered Hox expression and segmental identity in Mll-mutant mice

Yu, B., Hess, J. L., Horning, S. E., Brown, G. A. J., & Korsmeyer, S. J. (1995) · Nature · doi:10.1038/378505a0 · Cited by 872 · 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

Menin Associates with a Trithorax Family Histone Methyltransferase Complex and with the Hoxc8 Locus

Hughes, C. M., Rozenblatt–Rosen, O., Milne, T. A., Copeland, T. D., Levine, S. S., Lee, J. C., Hayes, D. N., Shanmugam, K. S., Bhattacharjee, A., Biondi, C., et al. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00081-4 · Cited by 645 · see citing works

Histone H3 lysine 4 methylation is mediated by Set1 and required for cell growth and rDNA silencing in Saccharomyces cerevisiaePreprint

Briggs, S. D., Bryk, M., Strahl, B. D., Cheung, W. L., Davie, J. K., Dent, S., Winston, F., & Allis, C. D. (2001) · Genes & Development · doi:10.1101/gad.940201 · Cited by 596 · see citing works

Hijacked in cancer: the MLL/KMT2 family of methyltransferases

Rao, R., & Dou, Y. (2015) · Nature Reviews. Cancer · doi:10.1038/nrc3929 · Cited by 558 · see citing works

Roles and regulation of histone methylation in animal development

Jambhekar, A., Dhall, A., & Shi, Y. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0151-1 · Cited by 556 · see citing works

Backtracking leukemia to birth: Identification of clonotypic gene fusion sequences in neonatal blood spots

Gale, K. B., Ford, A. M., Repp, R., Borkhardt, A., Keller, C., Eden, O. B., & Greaves, M. F. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.25.13950 · Cited by 549 · see citing works

The menin inhibitor revumenib in KMT2A-rearranged or NPM1-mutant leukaemia

Issa, G. C., Aldoss, I. T., DiPersio, J. F., Cuglievan, B., Stone, R. M., Arellano, M. L., Thirman, M. J., Patel, M. R., Dickens, D. S., Shenoy, S. M., et al. (2023) · Nature · doi:10.1038/s41586-023-05812-3 · Cited by 531 · see citing works

Molecular mechanisms of leukemogenesis mediated by MLL fusion proteins

Ayton, P. M., & Cleary, M. L. (2001) · Oncogene · doi:10.1038/sj.onc.1204639 · Cited by 499 · see citing works

Methylation of histone H3 at lysine 4 is highly conserved and correlates with transcriptionally active nuclei in Tetrahymena

Strahl, B. D., Ohba, R., Cook, R. G., & Allis, C. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14967 · Cited by 491 · see citing works

The DOT1L inhibitor pinometostat reduces H3K79 methylation and has modest clinical activity in adult acute leukemia

Stein, E. M., Garcia-Manero, G., Rizzieri, D. A., Tibes, R., Berdeja, J. G., Savona, M. R., Jongen-Lavrenic, M., Altman, J. K., Thomson, B., Blakemore, S. J., et al. (2018) · Blood · doi:10.1182/blood-2017-12-818948 · Cited by 461 · see citing works

Achieving clinical success with BET inhibitors as anti-cancer agents

Shorstova, T., Foulkes, W. D., & Witcher, M. (2021) · British Journal of Cancer · doi:10.1038/s41416-021-01321-0 · Cited by 358 · see citing works

The Pathogenesis of Mixed-Lineage Leukemia

Muntean, A. G., & Hess, J. L. (2011) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-011811-132434 · Cited by 347 · see citing works

Targeting MLL1 H3K4 Methyltransferase Activity in Mixed-Lineage Leukemia

Cao, F., Townsend, E. C., Karataş, H., Xu, J., Li, L., Lee, S. H. F., Liu, L., Chen, Y., Ouillette, P. D., Zhu, J., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2013.12.001 · Cited by 306 · see citing works

Outcome of Infants Younger Than 1 Year With Acute Lymphoblastic Leukemia Treated With the Interfant-06 Protocol: Results From an International Phase III Randomized Study

Pieters, R., Lorenzo, P. D., Ancliffe, P., Aversa, L. A., Brethon, B., Biondi, A., Campbell, M., Escherich, G., Ferster, A., Gardner, R., et al. (2019) · Journal of Clinical Oncology · doi:10.1200/jco.19.00261 · Cited by 301 · see citing works

MEN1 mutations mediate clinical resistance to menin inhibition

Perner, F., Stein, E. M., Wenge, D. V., Singh, S., Kim, J., Apazidis, A., Rahnamoun, H., Anand, D., Marinaccio, C., Hatton, C., et al. (2023) · Nature · doi:10.1038/s41586-023-05755-9 · Cited by 255 · see citing works

MLL-AF9-Induced Leukemogenesis Requires Co-Expression of the Wild Type Mll Allele

Thiel, A. T., Blessington, P., Zou, T., Feather, D., Wu, X.-J., Yan, J.-Z., Zhang, H., Liu, Z.-G., Ernst, P., Koretzky, G., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.12.034 · Cited by 249 · see citing works

Multiple Interactions Recruit MLL1 and MLL1 Fusion Proteins to the HOXA9 Locus in Leukemogenesis

Milne, T. A., Kim, J., Wang, G. G., Stadler, S. C., Basrur, V., Whitcomb, S. J., Wang, Z., Ruthenburg, A. J., Elenitoba‐Johnson, K. S. J., Roeder, R. G., et al. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.05.011 · Cited by 231 · see citing works

The KMT2A recombinome of acute leukemias in 2023

Meyer, C., Larghero, P., Lopes, B. A., Burmeister, T., Gröger, D., Sutton, R., Venn, N. C., Cazzaniga, G., Abascal, L. C., Анатольевич, Ц. Г., et al. (2023) · Leukemia · doi:10.1038/s41375-023-01877-1 · Cited by 231 · see citing works

Pro Isomerization in MLL1 PHD3-Bromo Cassette Connects H3K4me Readout to CyP33 and HDAC-Mediated Repression

Wang, Z., Song, J., Milne, T. A., Wang, G. G., Li, H., Allis, C. D., & Patel, D. J. (2010) · Cell · doi:10.1016/j.cell.2010.05.016 · Cited by 203 · see citing works

Histone deacetylase inhibition rescues structural and functional brain deficits in a mouse model of Kabuki syndrome

Bjornsson, H. T., Benjamin, J. S., Zhang, L., Weissman, J., Gerber, E. E., Chen, Y.-C., Vaurio, R. G., Potter, M. C., Hansen, K. D., & Dietz, H. C. (2014) · Science Translational Medicine · doi:10.1126/scitranslmed.3009278 · Cited by 194 · see citing works

Structural basis of nucleosome recognition and modification by MLL methyltransferases

Xue, H., Yao, T., Mi, C., Zhu, G., Li, Y., Yuan, G., Chen, Y., Lei, M., & Huang, J. (2019) · Nature · doi:10.1038/s41586-019-1528-1 · Cited by 192 · see citing works

Up-regulation of a HOXA-PBX3 homeobox-gene signature following down-regulation of miR-181 is associated with adverse prognosis in patients with cytogenetically abnormal AML.

Li, Z.-J., Huang, H., Li, Y.-Y., Jiang, X., Chen, P., Arnovitz, S., Radmacher, M., Maharry, K., Elkahloun, A., Yang, X., et al. (2012) · Blood · doi:10.1182/blood-2011-10-386235 · Cited by 182 · see citing works

Function of leukemogenic mixed lineage leukemia 1 (MLL) fusion proteins through distinct partner protein complexes

Biswas, D., Milne, T. A., Basrur, V., Kim, J., Elenitoba‐Johnson, K. S. J., Allis, C. D., & Roeder, R. G. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1111498108 · Cited by 168 · see citing works

Phosphorylation of MLL by ATR is required for execution of mammalian S-phase checkpoint

Liu, H., Takeda, S., Kumar, R., Westergard, T. D., Brown, E. J., Pandita, T. K., Cheng, E. H. Y., & Hsieh, J. J.-D. (2010) · Nature · doi:10.1038/nature09350 · Cited by 156 · see citing works

PBX3 is an important cofactor of HOXA9 in leukemogenesis

Li, Z., Zhang, Z., Li, Y., Arnovitz, S., Chen, P., Huang, H., Jiang, X., Hong, G.-M., Kunjamma, R. B., Ren, H., et al. (2012) · Blood · doi:10.1182/blood-2012-07-442004 · Cited by 154 · see citing works

Neuronal Kmt2a/Mll1 Histone Methyltransferase Is Essential for Prefrontal Synaptic Plasticity and Working Memory

Jakovcevski, M., Ruan, H., Shen, E. Y., Dincer, A., Javidfar, B., Ma, Q., Peter, C., Cheung, I. K., Mitchell, A., Jiang, Y., et al. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.3004-14.2015 · Cited by 138 · see citing works

Impact of high-risk cytogenetics on outcomes for children and young adults receiving CD19-directed CAR T-cell therapy

Leahy, A. B., Devine, K. J., Li, Y., Liu, H., Myers, R. M., DiNofia, A. M., Wray, L., Rheingold, S. R., Callahan, C. A., Baniewicz, D., et al. (2021) · Blood · doi:10.1182/blood.2021012727 · Cited by 116 · see citing works

Mixed lineage leukemia: a structure–function perspective of the MLL1 protein

Cosgrove, M. S., & Patel, A. B. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07609.x · Cited by 113 · see citing works

Predictors of outcomes in adults with acute myeloid leukemia and KMT2A rearrangements

Issa, G. C., Zarka, J. G., Sasaki, K., Qiao, W., Pak, D., Ning, J., Short, N. J., Haddad, F., Tang, Z., Patel, K. P., et al. (2021) · Blood Cancer Journal · doi:10.1038/s41408-021-00557-6 · Cited by 108 · see citing works

Structure-guided development of YEATS domain inhibitors by targeting π-π-π stacking

Li, X., Li, X.-M., Jiang, Y., Liu, Z., Cui, Y., Fung, K. Y., van der Beelen, S. H. E., Tian, G., Wan, L., Shi, X., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0144-y · Cited by 107 · see citing works

Discovery of a Highly Potent, Cell-Permeable Macrocyclic Peptidomimetic (MM-589) Targeting the WD Repeat Domain 5 Protein (WDR5)–Mixed Lineage Leukemia (MLL) Protein–Protein Interaction

Karataş, H., Li, Y., Liu, L., Ji, J., Lee, S. H. F., Chen, Y., Yang, J., Huang, L., Bernard, D., Xu, J., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01796 · Cited by 103 · see citing works

MLL protects CpG clusters from methylation within the Hoxa9 gene, maintaining transcript expression

Erfurth, F. E., Popovic, R., Grembecka, J. E., Cierpicki, T., Theisler, C. M., Xia, Z., Stuart, T., Dı́az, M. O., Bushweller, J. H., & Zeleznik‐Le, N. J. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0800090105 · Cited by 101 · see citing works

Recurrent YAP1 and KMT2A Gene Rearrangements in a Subset of MUC4-negative Sclerosing Epithelioid Fibrosarcoma

Kao, Y., Lee, J., Zhang, L., Sung, Y., Swanson, D. M., Hsieh, T., Liu, Y., Agaram, N. P., Huang, H.-Y., Dickson, B. C., et al. (2019) · The American Journal of Surgical Pathology · doi:10.1097/pas.0000000000001382 · Cited by 94 · see citing works

MLL/WDR5 Complex Regulates Kif2A Localization to Ensure Chromosome Congression and Proper Spindle Assembly during Mitosis

Ali, A., Veeranki, S. N., Chinchole, A., & Tyagi, S. (2017) · Developmental Cell · doi:10.1016/j.devcel.2017.05.023 · Cited by 91 · see citing works

Diverse functions of PHD fingers of the MLL/KMT2 subfamily

Ali, M., Hom, R. A., Blakeslee, W. W., Ikenouye, L., & Kutateladze, T. G. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.11.016 · Cited by 84 · see citing works

Single-cell transcriptomics reveals a distinct developmental state of KMT2A-rearranged infant B-cell acute lymphoblastic leukemia

Khabirova, E., Jardine, L., Coorens, T. H. H., Webb, S., Treger, T. D., Engelbert, J., Porter, T., Prigmore, E., Collord, G., Piapi, A., et al. (2022) · Nature Medicine · doi:10.1038/s41591-022-01720-7 · Cited by 84 · see citing works

A Molecular Switch between Mammalian MLL Complexes Dictates Response to Menin–MLL Inhibition

Soto‐Feliciano, Y. M., Rivera, F. J. S., Perner, F., Barrows, D., Kastenhuber, E. R., Ho, Y.-J., Carroll, T., Xiong, Y., Anand, D., Soshnev, A. A., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0416 · Cited by 84 · see citing works

Update on rational targeted therapy in AML

Shafer, D. A., & Grant, S. (2016) · Blood Reviews · doi:10.1016/j.blre.2016.02.001 · Cited by 79 · see citing works

Cryo-EM structure of the human MLL1 core complex bound to the nucleosome

Park, S. H., Ayoub, A. M., Lee, Y., Xu, J., Kim, H., Zheng, W. H., Zhang, B., Liang, S., An, S., Zhang, Y., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13550-2 · Cited by 68 · see citing works

Loss of MLL PHD Finger 3 Is Necessary for MLL-ENL–Induced Hematopoietic Stem Cell Immortalization

Chen, J., Santillan, D. A., Koonce, M., Wei, W., Luo, R. T., Thirman, M. J., Zeleznik‐Le, N. J., & Dı́az, M. O. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-6514 · Cited by 68 · see citing works

KMT2A: Umbrella Gene for Multiple Diseases

Castiglioni, S., Fede, E. D., Bernardelli, C., Lettieri, A., Parodi, C., Grazioli, P., Colombo, E. A., Ancona, S., Milani, D., Ottaviano, E., et al. (2022) · Genes · doi:10.3390/genes13030514 · Cited by 67 · see citing works

Keratin 23 (K23), a novel acidic keratin, is highly induced by histone deacetylase inhibitors during differentiation of pancreatic cancer cells

Zhang, J., Wang, L., Huang, H., Nelson, M., & Smith, D. I. (2001) · Genes Chromosomes and Cancer · doi:10.1002/1098-2264(2000)9999:9999 · Cited by 66 · see citing works

Updates in KMT2A Gene Rearrangement in Pediatric Acute Lymphoblastic Leukemia

Górecki, M., Kozioł, I., Kopystecka, A., Budzyńska, J., Zawitkowska, J., & Lejman, M. (2023) · Biomedicines · doi:10.3390/biomedicines11030821 · Cited by 62 · see citing works

Discovery of a dual WDR5 and Ikaros PROTAC degrader as an anti-cancer therapeutic

Li, D., Yu, X., Kottur, J., Gong, W., Zhang, Z., Storey, A. J., Tsai, Y., Uryu, H., Shen, Y., Byrum, S. D., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02340-8 · Cited by 61 · see citing works

Small-Molecule Inhibition of the Acyl-Lysine Reader ENL as a Strategy against Acute Myeloid Leukemia

Liu, Y., Li, Q., Alikarami‬, F., Barrett, D. R., Mahdavi, L., Li, H., Tang, S., Khan, T. A., Michino, M., Hill, C., et al. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-21-1307 · Cited by 59 · see citing works

KDM5A mutations identified in autism spectrum disorder using forward genetics

Hayek, L. E., Tuncay, İ. O., Nijem, N., Russell, J. L., Ludwig, S. M., Kaur, K. J., Li, X., Anderton, P. D., Tang, M., Gerard, A., et al. (2020) · eLife · doi:10.7554/elife.56883 · Cited by 59 · see citing works

MLL1 and MLL1 fusion proteins have distinct functions in regulating leukemic transcription program

Xu, J., Li, L., Xiong, J., denDekker, A., Ye, A., Karatas, H., Liu, L., Wang, H., Qin, Z., Wang, S.-M., et al. (2016) · Cell Discovery · doi:10.1038/celldisc.2016.8 · Cited by 56 · see citing works

Mutually suppressive roles of KMT2A and KDM5C in behaviour, neuronal structure, and histone H3K4 methylation

Vallianatos, C. N., Raines, B., Porter, R. S., Bonefas, K. M., Wu, M. C., Garay, P. M., Collette, K. M., Seo, Y. A., Dou, Y., Keegan, C. E., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-1001-6 · Cited by 53 · see citing works

Neuronal Deletion of Kmt2a/Mll1 Histone Methyltransferase in Ventral Striatum is Associated with Defective Spike-Timing-Dependent Striatal Synaptic Plasticity, Altered Response to Dopaminergic Drugs, and Increased Anxiety

Shen, E., Jiang, Y. P., Javidfar, B., Kassim, B. S., Loh, Y. E., Ma, Q., Mitchell, A., Pothula, V., Stewart, A. F., Ernst, P., et al. (2016) · Neuropsychopharmacology · doi:10.1038/npp.2016.144 · Cited by 52 · see citing works

KMT2A rearranged acute lymphoblastic leukaemia: Unravelling the genomic complexity and heterogeneity of this high-risk disease

Forgione, M. O., McClure, B. J., Eadie, L. N., Yeung, D. T. O., & White, D. L. (2019) · Cancer Letters · doi:10.1016/j.canlet.2019.11.005 · Cited by 50 · see citing works

Discovery of Selective Small-Molecule Inhibitors for the ENL YEATS Domain

Ma, X. R., Xu, L., Xu, S., Klein, B. J., Wang, H., Das, S. K., Li, K., Yang, K. S., Sohail, S. Q., Chapman, A., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c00367 · Cited by 49 · see citing works

Menin inhibitor ziftomenib (KO-539) synergizes with drugs targeting chromatin regulation or apoptosis and sensitizes acute myeloid leukemia with MLL rearrangement or NPM1 mutation to venetoclax

Rausch, J., Dzama, M. M., Dolgikh, N., Stiller, H. L., Bohl, S., Lahrmann, C., Kunz, K., Kessler, L. V., Echchannaoui, H., Chen, C.-W. D., et al. (2023) · Haematologica · doi:10.3324/haematol.2022.282160 · Cited by 49 · see citing works

Mechanism for DPY30 and ASH2L intrinsically disordered regions to modulate the MLL/SET1 activity on chromatin

Lee, Y., Ayoub, A. M., Park, S.-H., Liang, S., Xu, J., Mao, F., Zheng, W. H., Zhang, Y., Cho, U., & Dou, Y. (2021) · Nature Communications · doi:10.1038/s41467-021-23268-9 · Cited by 42 · see citing works

KMT2 Family of H3K4 Methyltransferases: Enzymatic Activity-dependent and -independent Functions

Van, H. T., Xie, G., Dong, P., Liu, Z. J., & Ge, K. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168453 · Cited by 41 · see citing works

Pan-sarcoma genomic analysis of KMT2A rearrangements reveals distinct subtypes defined by YAP1–KMT2A–YAP1 and VIM–KMT2A fusions

Massoth, L. R., Hung, Y. P., Nardi, V., Nielsen, G. P., Hasserjian, R. P., Louissaint, A., Fisch, A. S., Deshpande, V., Zukerberg, L. R., Lennerz, J. K., et al. (2020) · Modern Pathology · doi:10.1038/s41379-020-0582-4 · Cited by 40 · see citing works

MLL gene amplification in acute myeloid leukemia and myelodysplastic syndromes is associated with characteristic clinicopathological findings and TP53 gene mutation

Tang, G., Dinardo, C. D., Zhang, L., Ravandi, F., Khoury, J. D., Huh, Y. O., Muzzafar, T., Medeiros, L. J., Wang, S. A., & Bueso-Ramos, C. (2014) · Human Pathology · doi:10.1016/j.humpath.2014.09.008 · Cited by 40 · see citing works

Long noncoding RNAs: emerging regulators of normal and malignant hematopoiesis

Qiu, Y., Xu, M., & Huang, S. (2021) · Blood · doi:10.1182/blood.2021011992 · Cited by 39 · see citing works

Small Molecule Menin Inhibitors: Novel Therapeutic Agents Targeting Acute Myeloid Leukemia with KMT2A Rearrangement or NPM1 Mutation

Thomas, X. (2024) · Oncology and Therapy · doi:10.1007/s40487-024-00262-x · Cited by 38 · see citing works

Multistate structures of the MLL1-WRAD complex bound to H2B-ubiquitinated nucleosome

Rahman, S., Hoffmann, N. A., Worden, E. J., Smith, M. L., Namitz, K. E. W., Knutson, B. A., Cosgrove, M. S., & Wolberger, C. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2205691119 · Cited by 36 · see citing works

A dose escalation study of RO6870810/TEN-10 in patients with acute myeloid leukemia and myelodysplastic syndrome

Roboz, G. J., Desai, P. M., Lee, S., Ritchie, E. K., Winer, E. S., DeMario, M., Brennan, B. J., Nüesch, E., Chesné, E., Brennan, L., et al. (2021) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2021.1881509 · Cited by 36 · see citing works

KMT2A histone methyltransferase contributes to colorectal cancer development by promoting cathepsin Z transcriptional activation

Yang, F., Zhang, D., Hu, T., Zhao, H., Zhao, X., Lou, Z., He, Y., Qin, W., Xia, J., Zhang, X., et al. (2019) · Cancer Medicine · doi:10.1002/cam4.2226 · Cited by 35 · see citing works

KMT2A ( MLL ) fusions in aggressive sarcomas in young adults

Yoshida, A., Arai, Y., Tanzawa, Y., Wakai, S., Hama, N., Kawai, A., & Shibata, T. (2019) · Histopathology · doi:10.1111/his.13926 · Cited by 32 · see citing works

Efficacy of combined CDK9/BET inhibition in preclinical models of MLL-rearranged acute leukemia

McCalmont, H., Li, K. L., Jones, L., Toubia, J., Bray, S. C. E., Casolari, D. A., Mayoh, C., Samaraweera, S. E., Lewis, I. D., Prinjha, R. K., et al. (2020) · Blood Advances · doi:10.1182/bloodadvances.2019000586 · Cited by 30 · see citing works

Non-canonical MLL1 activity regulates centromeric phase separation and genome stability

Liang, S., Yang, Z. F., An, S., Yang, W., Kim, S., Oh, H., Xu, J., Yin, J., Wang, H., Lenz, H., et al. (2023) · Nature Cell Biology · doi:10.1038/s41556-023-01270-1 · Cited by 28 · see citing works

Inhibition of Methyltransferase DOT1L Sensitizes to Sorafenib Treatment AML Cells Irrespective of MLL-Rearrangements: A Novel Therapeutic Strategy for Pediatric AML

Lonetti, A., Indio, V., Laginestra, M. A., Tarantino, G., Chiarini, F., Astolfi, A., Bertuccio, S. N., Martelli, A. M., Locatelli, F., Pession, A., et al. (2020) · Cancers · doi:10.3390/cancers12071972 · Cited by 28 · see citing works

MLL-AF4 cooperates with PAF1 and FACT to drive high-density enhancer interactions in leukemia

Crump, N. T., Smith, A., Godfrey, L., Dopico-Fernandez, A. M., Denny, N., Harman, J. R., Hamley, J. C., Jackson, N., Chahrour, C., Riva, S. G., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-40981-9 · Cited by 27 · see citing works

Disorders of histone methylation: Molecular basis and clinical syndromes

Ojaimi, M. A., Banimortada, B. J., Othman, A. A., Riedhammer, K. M., Almannai, M., & El‐Hattab, A. W. (2022) · Clinical Genetics · doi:10.1111/cge.14181 · Cited by 27 · see citing works

Targeting Chromatin Complexes in Myeloid Malignancies and Beyond: From Basic Mechanisms to Clinical Innovation

Perner, F., & Armstrong, S. A. (2020) · Cells · doi:10.3390/cells9122721 · Cited by 25 · see citing works

Proteasome inhibition targets the KMT2A transcriptional complex in acute lymphoblastic leukemia

Kamens, J. L., Nance, S., Koss, C., Xu, B., Cotton, A., Lam, J. W., Garfinkle, E. A. R., Nallagatla, P., Smith, A. M. R., Mitchell, S., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36370-x · Cited by 23 · see citing works

Minimal residual disease and outcome characteristics in infant KMT2A-germline acute lymphoblastic leukaemia treated on the Interfant-06 protocol

Stutterheim, J., Lorenzo, P. D., van der Sluis, I. M., Alten, J., Ancliffe, P., Attarbaschi, A., Aversa, L. A., Boer, J. M., Biondi, A., Brethon, B., et al. (2021) · European Journal of Cancer · doi:10.1016/j.ejca.2021.10.004 · Cited by 23 · see citing works

Novel germline mutation KMT2A G3131S confers genetic susceptibility to familial myeloproliferative neoplasms

Yin, L., Xie, S., Chen, Y., Li, W., Jiang, X. P., Li, H., Li, J., Wu, Z., Xiao, X., Zhang, G., et al. (2021) · Annals of Hematology · doi:10.1007/s00277-021-04562-4 · Cited by 21 · see citing works

Increasing histone acetylation improves sociability and restores learning and memory in KAT6B-haploinsufficient mice

Bergamasco, M., Vanyai, H. K., Garnham, A. L., Geoghegan, N. D., Vogel, A. P., Eccles, S., Rogers, K. L., Smyth, G. K., Blewitt, M. E., Hannan, A. J., et al. (2024) · Journal of Clinical Investigation · doi:10.1172/jci167672 · Cited by 20 · see citing works

Cytogenetic manifestation of chromosome 11 duplication/amplification in acute myeloid leukemia

Šárová, I., Březinová, J., Zemanová, Z., Izáková, S., Lizcová, L., Malinová, E., Berková, A., Čermák, J., Maaloufová, J., Nováková, L., et al. (2010) · Cancer Genetics and Cytogenetics · doi:10.1016/j.cancergencyto.2010.02.012 · Cited by 20 · see citing works

Allelic complexity of KMT2A partial tandem duplications in acute myeloid leukemia and myelodysplastic syndromes

Tsai, H. K., Gibson, C. J., Murdock, H. M., Davineni, P. K., Harris, M. H., Wang, E. S., Gondek, L. P., Kim, A. S., Nardi, V., & Lindsley, R. C. (2022) · Blood Advances · doi:10.1182/bloodadvances.2022007613 · Cited by 19 · see citing works

KMT2A associates with PHF5A-PHF14-HMG20A-RAI1 subcomplex in pancreatic cancer stem cells and epigenetically regulates their characteristics

Mouti, M. A., Deng, S., Pook, M., Malzahn, J., Rendek, A., Militi, S., Nibhani, R., Soonawalla, Z. F., Oppermann, U. C. T., Hwang, C., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41297-4 · Cited by 16 · see citing works

A Pan-Cancer Study of KMT2 Family as Therapeutic Targets in Cancer

Zhu, J., Liu, Z., Liang, X., Wang, L., Wu, D., Mao, W., & Shen, D. (2022) · Journal of Oncology · doi:10.1155/2022/3982226 · Cited by 16 · see citing works

Wiedemann–Steiner Syndrome: Case Report and Review of Literature

Yu, H., Zhang, G., Yu, S., & Wu, W. (2022) · Children · doi:10.3390/children9101545 · Cited by 16 · see citing works

Dangerous liaisons: cooperation between Pbx3, Meis1 and Hoxa9 in leukemia

Thorne, R., & Milne, T. A. (2015) · Haematologica · doi:10.3324/haematol.2015.129932 · Cited by 15 · see citing works

Prognostic significance ofKMT2A-PTD in patients with acute myeloid leukaemia: a systematic review and meta-analysis

Wu, Y., Ma, M., Wu, X., Deng, J., Liu, X., Zheng, X. Y., & Gong, Y. (2023) · BMJ Open · doi:10.1136/bmjopen-2022-062376 · Cited by 13 · see citing works

A novel deletion mutation in KMT2A identified in a child with ID/DD and blood eosinophilia

Zhang, H., Xiang, B., Chen, H., Chen, X. '., & Cai, T. (2019) · BMC Medical Genetics · doi:10.1186/s12881-019-0776-0 · Cited by 11 · see citing works

Expanding the Spectrum of KDM5C Neurodevelopmental Disorder: A Novel De Novo Stop Variant in a Young Woman and Emerging Genotype–Phenotype Correlations

Lintas, C., Bottillo, I., Sacco, R., Azzarà, A., Cassano, I., Ciccone, M. P., Grammatico, P., & Gurrieri, F. (2022) · Genes · doi:10.3390/genes13122266 · Cited by 8 · see citing works

Double minute chromosomes in acute myeloid leukemia and myelodysplastic syndromes are associated with complex karyotype, monosomal karyotype, TP53 deletion, and TP53 mutations

Wang, N., Yuan, L., Jing, Y., Fan, K.-K., Jin, H., Lv, C., Wang, L., & Yu, L. (2021) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.1080/10428194.2021.1919663 · Cited by 8 · see citing works

KMT2A‐D pathogenicity, prevalence, and variation according to a population database

Larson, J. K., Hunter‐Schlichting, D., Crowgey, E. L., Mills, L. J., Druley, T. E., & Marcotte, E. L. (2022) · Cancer Medicine · doi:10.1002/cam4.5443 · Cited by 7 · see citing works

Sequential deregulation of histone marks, chromatin accessibility and gene expression in response to PROTAC-induced degradation of ASH2L

Barsoum, M., Sayadi-Boroujeni, R., Stenzel, A. T., Bussmann, P., Lüscher‐Firzlaff, J., & Lüscher, B. (2023) · Scientific Reports · doi:10.1038/s41598-023-49284-x · Cited by 5 · see citing works

Biological hierarchy from genotype to phenotype in syndromic and non-syndromic autism spectrum disorder

Qing, Z., Yin, Z., Chen, B., Rao, Z., Yin, D., Li, D., Lu, Y., Shi, M., Li, S., Xu, Y., et al. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1964684