The histone methyltransferase Dot1/DOT1L as a critical regulator of the cell cycle

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MLL-rearranged Leukemia is Dependent on Aberrant H3K79 Methylation by DOT1L

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Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks

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Dot1p Modulates Silencing in Yeast by Methylation of the Nucleosome Core

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The key to development: interpreting the histone code?

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Potent inhibition of DOT1L as treatment of MLL-fusion leukemia

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The Paf1 Complex Is Required for Histone H3 Methylation by COMPASS and Dot1p: Linking Transcriptional Elongation to Histone Methylation

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lncRNA-dependent mechanisms of androgen-receptor-regulated gene activation programs

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Chromatin-modifying enzymes as modulators of reprogramming

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Cyclin-dependent kinases and cell-cycle transitions: does one fit all?

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Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation

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Methylation of Histone H4 Lysine 20 Controls Recruitment of Crb2 to Sites of DNA Damage

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Histone Methylation

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Lysine methylation within the globular domain of histone H3 by Dot1 is important for telomeric silencing and Sir protein associationPreprint

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Histone H3.3 is enriched in covalent modifications associated with active chromatin

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DOT1L/KMT4 Recruitment and H3K79 Methylation Are Ubiquitously Coupled with Gene Transcription in Mammalian Cells

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The pachytene checkpoint

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Identification of High-Copy Disruptors of Telomeric Silencing in Saccharomyces cerevisiae

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Histone Crosstalk between H2B Monoubiquitination and H3 Methylation Mediated by COMPASS

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Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction

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Ubiquitination of Histone H2B by Rad6 Is Required for Efficient Dot1-mediated Methylation of Histone H3 Lysine 79

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Structure of the Catalytic Domain of Human DOT1L, a Non-SET Domain Nucleosomal Histone Methyltransferase

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The Paf1 Complex Is Essential for Histone Monoubiquitination by the Rad6-Bre1 Complex, Which Signals for Histone Methylation by COMPASS and Dot1p

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Chemical mechanisms of histone lysine and arginine modifications

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The Histone H3K79 Methyltransferase Dot1L Is Essential for Mammalian Development and Heterochromatin Structure

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Histone demethylase JMJD3 contributes to epigenetic control of <i>INK4a/ARF</i> by oncogenic RAS

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Structural and Sequence Motifs of Protein (Histone) Methylation Enzymes

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Lysine-79 of histone H3 is hypomethylated at silenced loci in yeast and mammalian cells: A potential mechanism for position-effect variegation

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Disruptor of Telomeric Silencing-1 Is a Chromatin-specific Histone H3 Methyltransferase

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The H3K36 demethylase Jhdm1b/Kdm2b regulates cell proliferation and senescence through p15Ink4b

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Role of Dot1-Dependent Histone H3 Methylation in G1 and S Phase DNA Damage Checkpoint Functions of Rad9

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The DNA Damage Checkpoint Response Requires Histone H2B Ubiquitination by Rad6-Bre1 and H3 Methylation by Dot1

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Catalytic site remodelling of the DOT1L methyltransferase by selective inhibitors

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DOT1L, the H3K79 methyltransferase, is required for MLL-AF9-mediated leukemogenesis.

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Distinctive Core Histone Post-Translational Modification Patterns in Arabidopsis thaliana

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Disulfide-directed histone ubiquitylation reveals plasticity in hDot1L activation

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Histone H2B Ubiquitylation Controls Processive Methylation but Not Monomethylation by Dot1 and Set1

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Histone H3 phosphorylation – A versatile chromatin modification for different occasions

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Proteasomal ATPases link ubiquitylation of histone H2B to methylation of histone H3.

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Requirement for Dot1l in murine postnatal hematopoiesis and leukemogenesis by MLL translocation

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Interplay of Chromatin Modifiers on a Short Basic Patch of Histone H4 Tail Defines the Boundary of Telomeric Heterochromatin

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Histone methyltransferase Dot1 and Rad9 inhibit single‐stranded DNA accumulation at DSBs and uncapped telomeres

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Linking Cell Cycle to Histone Modifications: SBF and H2B Monoubiquitination Machinery and Cell-Cycle Regulation of H3K79 Dimethylation

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Role for the Silencing Protein Dot1 in Meiotic Checkpoint Control

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Leukemic transformation by the MLL-AF6 fusion oncogene requires the H3K79 methyltransferase Dot1l

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Histone H3 Lysine 79 Methyltransferase Dot1 Is Required for Immortalization by MLL Oncogenes

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Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states

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The RING Finger Protein MSL2 in the MOF Complex Is an E3 Ubiquitin Ligase for H2B K34 and Is Involved in Crosstalk with H3 K4 and K79 Methylation

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Heterochromatin formation involves changes in histone modifications over multiple cell generations

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DOT1L regulates dystrophin expression and is critical for cardiac functionPreprint

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Early mammalian erythropoiesis requires the Dot1L methyltransferase

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Selective Di- or Trimethylation of Histone H3 Lysine 76 by Two DOT1 Homologs Is Important for Cell Cycle Regulation in Trypanosoma brucei

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Histone H2BK123 monoubiquitination is the critical determinant for H3K4 and H3K79 trimethylation by COMPASS and Dot1

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Deficiency of H3K79 Histone Methyltransferase Dot1-like Protein (DOT1L) Inhibits Cell Proliferation

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Characterization of the grappa Gene, the Drosophila Histone H3 Lysine 79 Methyltransferase

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Abrogation of MLL–AF10 and CALM–AF10-mediated transformation through genetic inactivation or pharmacological inhibition of the H3K79 methyltransferase Dot1l

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Deficiency in Mammalian Histone H2B Ubiquitin Ligase Bre1 (Rnf20/Rnf40) Leads to Replication Stress and Chromosomal Instability

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A charge-based interaction between histone H4 and Dot1 is required for H3K79 methylation and telomere silencing: identification of a new trans-histone pathwayPreprint

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Structure of the Conserved Core of the Yeast Dot1p, a Nucleosomal Histone H3 Lysine 79 Methyltransferase

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Histone H2A phosphorylation and H3 methylation are required for a novel Rad9 DSB repair function following checkpoint activation

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Dot1 and Histone H3K79 Methylation in Natural Telomeric and HM Silencing

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Identification of Histone Demethylases in Saccharomyces cerevisiae

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Phosphorylation of the budding yeast 9-1-1 complex is required for Dpb11 function in the full activation of the UV-induced DNA damage checkpoint

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Bat3 facilitates H3K79 dimethylation by DOT1L and promotes DNA damage‐induced 53BP1 foci at G1/G2 cell‐cycle phases

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Docking onto chromatin via the Saccharomyces cerevisiae Rad9 Tudor domain

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Human Histone H3K79 Methyltransferase DOT1L Methyltransferase Binds Actively Transcribing RNA Polymerase II to Regulate Gene Expression

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Changes in H3K79 Methylation During Preimplantation Development in Mice

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Methylation of Histone H3 on Lysine 79 Associates with a Group of Replication Origins and Helps Limit DNA Replication Once per Cell Cycle

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Covalent modifications of histones during mitosis and meiosis

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Identification of histone methylation multiplicities patterns in the brain of senescence-accelerated prone mouse 8

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Protein phosphatases take the mitotic stage

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The Leukemia-Associated Mllt10/Af10-Dot1l Are Tcf4/β-Catenin Coactivators Essential for Intestinal Homeostasis

Mahmoudi, T., Boj, S. F., Hatzis, P., Li, V. S. W., Taouatas, N., Vries, R. G. J., Teunissen, H., Begthel, H., Korving, J., Mohammed, S., et al. (2010) · PLoS Biology · doi:10.1371/journal.pbio.1000539 · Cited by 86 · see citing works

Methylation of histone H3 lysine-79 by Dot1p plays multiple roles in the response to UV damage in Saccharomyces cerevisiae

Bostelman, L. J., Keller, A. M., Albrecht, A. M., Arat, A., & Thompson, J. S. (2007) · DNA repair · doi:10.1016/j.dnarep.2006.12.010 · Cited by 85 · see citing works

ES Cell Cycle Progression and Differentiation Require the Action of the Histone Methyltransferase Dot1L

Barry, E., Krueger, W. H., Jakuba, C. M., Veilleux, E. S., Ambrosi, D. J., Nelson, C. E., & Rasmussen, T. P. (2009) · Stem Cells · doi:10.1002/stem.86 · Cited by 80 · see citing works

Histone Methyltransferase DOT1L Drives Recovery of Gene Expression after a Genotoxic Attack

Oksenych, V., Zhovmer, A. S., Ziani, S., Mari, P., Eberová, J., Nardò, T., Stefanini, M., Giglia‐Mari, G., Egly, J., & Coin, F. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003611 · Cited by 78 · see citing works

Chromatin Assembly Factor 1 Interacts with Histone H3 Methylated at Lysine 79 in the Processes of Epigenetic Silencing and DNA Repair

Zhou, H., Madden, B. J., Muddiman, D. C., & Zhang, Z. (2006) · Biochemistry · doi:10.1021/bi0521083 · Cited by 73 · see citing works

X-Ray Survival Characteristics and Genetic Analysis for Nine Saccharomyces Deletion Mutants That Show Altered Radiation Sensitivity

Game, J. C., Williamson, M. S., & Baccari, C. (2004) · Genetics · doi:10.1534/genetics.104.028613 · Cited by 71 · see citing works

Essential role of DOT1L in maintaining normal adult hematopoiesis

Nguyen, A. T., He, J., Taranova, O., & Zhang, Y. (2011) · Cell Research · doi:10.1038/cr.2011.115 · Cited by 71 · see citing works

Structure and regulation of the mDot1 gene, a mouse histone H3 methyltransferase

Zhang, W., Hayashizaki, Y., & Kone, B. C. (2004) · Biochemical Journal · doi:10.1042/bj20030839 · Cited by 65 · see citing works

Global reduction of the epigenetic H3K79 methylation mark and increased chromosomal instability in CALM-AF10–positive leukemias

Lin, Y.-H., Kakadia, P. M., Chen, Y., Li, Y.-Q., Deshpande, A. J., Buske, C., Zhang, K.-L., Zhang, Y., Xu, G.-L., & Bohlander, S. K. (2009) · Blood · doi:10.1182/blood-2009-03-209395 · Cited by 64 · see citing works

The Dot1 Histone Methyltransferase and the Rad9 Checkpoint Adaptor Contribute to Cohesin-Dependent Double-Strand Break Repair by Sister Chromatid Recombination in Saccharomyces cerevisiae

Conde, F., Refolio, E., Cordón-Preciado, V., Cortés‐Ledesma, F., Aragón, L., Aguilera, A., & San-Segundo, P. A. (2009) · Genetics · doi:10.1534/genetics.109.101899 · Cited by 64 · see citing works

The establishment of gene silencing at single-cell resolution

Nishimura, E. O., Dudoit, S., & Rine, J. (2009) · Nature Genetics · doi:10.1038/ng.402 · Cited by 62 · see citing works

Kinetics of Re-establishing H3K79 Methylation Marks in Global Human Chromatin*

Sweet, S. M. M., Li, M., Thomas, P. M., Durbin, K. R., & Kelleher, N. L. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145094 · Cited by 61 · see citing works

Evidence That the Histone Methyltransferase Dot1 Mediates Global Genomic Repair by Methylating Histone H3 on Lysine 79

Tatum, D. M., & Li, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.241570 · Cited by 61 · see citing works

Dot1-Dependent Histone H3K79 Methylation Promotes Activation of the Mek1 Meiotic Checkpoint Effector Kinase by Regulating the Hop1 Adaptor

Ontoso, D., Acosta, I., van Leeuwen, F., Freire, R., & San-Segundo, P. A. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003262 · Cited by 61 · see citing works

Dynamic Regulation of Histone H3 Methylated at Lysine 79 within a Tissue-specific Chromatin Domain

Im, H., Park, C., Feng, Q. F., Johnson, K. D., Kiekhaefer, C. M., Choi, K., Zhang, Y., & Bresnick, E. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m300890200 · Cited by 60 · see citing works

Progressive methylation of ageing histones by Dot1 functions as a timer

Vos, D. E. D., Frederiks, F., Terweij, M., van Welsem, T., Verzijlbergen, K. F., Iachina, E., de Graaf, E. L., Altelaar, M. A. F., Oudgenoeg, G., Heck, A. J. R., et al. (2011) · EMBO Reports · doi:10.1038/embor.2011.131 · Cited by 59 · see citing works

Characterization of the DOT1L Network: Implications of Diverse Roles for DOT1L

Park, G., Gong, Z., Chen, J., & Kim, J. (2010) · The Protein Journal · doi:10.1007/s10930-010-9242-8 · Cited by 56 · see citing works

The ZFP-1(AF10)/DOT-1 Complex Opposes H2B Ubiquitination to Reduce Pol II Transcription

Cecere, G., Hoersch, S., Jensen, M. B., Dixit, S., & Grishok, A. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.06.002 · Cited by 56 · see citing works

Aqp5 Is a New Transcriptional Target of Dot1a and a Regulator of Aqp2

Wu, H., Chen, L., Zhang, X., Zhou, Q., Li, J.-M., Berger, S., Borok, Z., Zhou, B., Xiao, Z. S., Yin, H., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0053342 · Cited by 55 · see citing works

DOT1A-dependent H3K76 methylation is required for replication regulation in Trypanosoma brucei

Gassen, A., Brechtefeld, D., Schandry, N., Arteaga-Salas, J. M., Israel, L., Imhof, A., & Janzen, C. J. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks801 · Cited by 54 · see citing works

Role of Dot1 in the Response to Alkylating DNA Damage in Saccharomyces cerevisiae: Regulation of DNA Damage Tolerance by the Error-Prone Polymerases Polζ/Rev1

Conde, F., & San-Segundo, P. A. (2008) · Genetics · doi:10.1534/genetics.108.089003 · Cited by 51 · see citing works

The tudor protein survival motor neuron (SMN) is a chromatin-binding protein that interacts with methylated histone H3 lysine 79

Sabra, M., Texier, P., Maalouf, J. E., & Lomonte, P. (2013) · Journal of Cell Science · doi:10.1242/jcs.126003 · Cited by 43 · see citing works

Histone H3K79 methyltransferase Dot1L is directly activated by thyroid hormone receptor during Xenopus metamorphosis

Matsuura, K., Fujimoto, K., Das, B., Fu, L., Lu, C. D., & Shi, Y. (2012) · Cell & Bioscience · doi:10.1186/2045-3701-2-25 · Cited by 43 · see citing works

Regulation of the DNA Damage Response and Gene Expression by the Dot1L Histone Methyltransferase and the 53Bp1 Tumour Suppressor

Fitzgerald, J., Moureau, S., Drogaris, P., O’Connell, E., Abshiru, N. A., Verreault, A., Thibault, P., Grenon, M., & Lowndes, N. F. (2011) · PLoS ONE · doi:10.1371/journal.pone.0014714 · Cited by 41 · see citing works

Regulation of tolerance to DNA alkylating damage by Dot1 and Rad53 in Saccharomyces cerevisiae

Conde, F., Ontoso, D., Acosta, I., Gallego-Sánchez, A., Bueno, A., & San-Segundo, P. A. (2010) · DNA repair · doi:10.1016/j.dnarep.2010.07.003 · Cited by 39 · see citing works

A lysine-rich region in Dot1p is crucial for direct interaction with H2B ubiquitylation and high level methylation of H3K79

Oh, S., Jeong, K., Kim, H., Kwon, C. S., & Lee, D. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.07.100 · Cited by 38 · see citing works

Loss of H3 K79 Trimethylation Leads to Suppression of Rtt107-dependent DNA Damage Sensitivity through the Translesion Synthesis Pathway

Lévesque, N., Leung, G. P., Fok, A. K., Schmidt, T. I., & Kobor, M. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.116855 · Cited by 37 · see citing works

Dot1 binding induces chromatin rearrangements by histone methylation-dependent and -independent mechanisms

Stulemeijer, I. J. E., Pike, B. L., Faber, A. W., Verzijlbergen, K. F., van Welsem, T., Frederiks, F., Lenstra, T. L., Holstege, F. C. P., Gasser, S. M., & van Leeuwen, F. (2011) · Epigenetics & Chromatin · doi:10.1186/1756-8935-4-2 · Cited by 37 · see citing works

Histone Monoubiquitylation Position Determines Specificity and Direction of Enzymatic Cross-talk with Histone Methyltransferases Dot1L and PRC2

Whitcomb, S. J., Fierz, B., McGinty, R. K., Holt, M. T., Ito, T., Muir, T. W., & Allis, C. D. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.361824 · Cited by 35 · see citing works

Dynamics of DOT1L localization and H3K79 methylation during meiotic prophase I in mouse spermatocytes

Ontoso, D., Kauppi, L., Keeney, S., & San-Segundo, P. A. (2013) · Chromosoma · doi:10.1007/s00412-013-0438-5 · Cited by 35 · see citing works

Involvement of DOT1L in the Remodeling of Heterochromatin Configuration During Early Preimplantation Development in Mice1

Ooga, M., Suzuki, M. G., & Aoki, F. (2013) · Biology of Reproduction · doi:10.1095/biolreprod.113.113258 · Cited by 35 · see citing works

The checkpoint Saccharomyces cerevisiae Rad9 protein contains a tandem tudor domain that recognizes DNA

Lancelot, N., Charier, G., Couprie, J., Duband‐Goulet, I., Alpha‐Bazin, B., Quéméneur, É., Ma, É., Marsolier‐Kergoat, M., Ropars, V., Charbonnier, J., et al. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm607 · Cited by 31 · see citing works

Methylation of H3 K4 and K79 is not strictly dependent on H2B K123 ubiquitylation

Foster, E. R., & Downs, J. A. (2009) · The Journal of Cell Biology · doi:10.1083/jcb.200812088 · Cited by 22 · see citing works

Spironolactone Rescues Dot1a-Af9-Mediated Repression of Endothelin-1 and Improves Kidney Injury in Streptozotocin-Induced Diabetic Rats

Zhou, Q., Liu, K., Wu, H., Chen, L., Veeraragoo, P., Yuan, M., Xiao, Z. S., Peng, W., Ao, X., Tang, R., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047360 · Cited by 19 · see citing works

UV sensitive mutations in histone H3 in Saccharomyces cerevisiae that alter specific K79 methylation states genetically act through distinct DNA repair pathways

Evans, M. L., Bostelman, L. J., Albrecht, A. M., Keller, A. M., Strande, N. T., & Thompson, J. S. (2008) · Current Genetics · doi:10.1007/s00294-008-0182-1 · Cited by 18 · see citing works

Nonredundant Requirement for Multiple Histone Modifications for the Early Anaphase Release of the Mitotic Exit Regulator Cdc14 from Nucleolar Chromatin

Hwang, W. W., & Madhani, H. D. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000588 · Cited by 18 · see citing works

Heterologous expression reveals distinct enzymatic activities of two DOT1 histone methyltransferases ofTrypanosoma brucei

Frederiks, F., van Welsem, T., Oudgenoeg, G., Heck, A. J. R., Janzen, C. J., & van Leeuwen, F. (2010) · Journal of Cell Science · doi:10.1242/jcs.073882 · Cited by 16 · see citing works

H3 K79 dimethylation marks developmental activation of the β-globin gene but is reduced upon LCR-mediated high-level transcription

Sawado, T., Halow, J. M., Im, H., Ragoczy, T., Bresnick, E. H., Bender, M. A., & Groudine, M. T. (2008) · Blood · doi:10.1182/blood-2007-12-128983 · Cited by 15 · see citing works

Evolutionary Conservation Levels of Subunits of Histone-Modifying Protein Complexes in Fungi

Nishida, H. (2009) · Comparative and Functional Genomics · doi:10.1155/2009/379317 · Cited by 13 · see citing works

Effect of histone methyltransferase gene mutations on sporulation in S. cerevisiae

Morohashi, N., Mitchell, A. P., & Shimizu, M. (2005) · Nucleic Acids Symposium Series · doi:10.1093/nass/49.1.325 · Cited by 7 · see citing works

The roles of DNA, RNA and histone methylation in ageing and cancer

Michalak, E. M., Burr, M. L., Bannister, A. J., & Dawson, M. A. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0143-1 · Cited by 549 · see citing works

De Novo Nonsense Mutations in KAT6A, a Lysine Acetyl-Transferase Gene, Cause a Syndrome Including Microcephaly and Global Developmental Delay

Arboleda, V. A., Lee, H., Dorrani, N., Zadeh, N., Willis, M. J. H., Macmurdo, C., Manning, M. A., Hanson‐Kahn, A., Hudgins, L., Barthélémy, F., et al. (2015) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2015.01.017 · Cited by 141 · see citing works

Histone H2B monoubiquitination: roles to play in human malignancy

Cole, A. J., Clifton-Bligh, R. J., & Marsh, D. J. (2014) · Endocrine Related Cancer · doi:10.1530/erc-14-0185 · Cited by 129 · see citing works

The emerging roles of DOT1L in leukemia and normal development

McLean, C. M., Karemaker, I. D., & van Leeuwen, F. (2014) · Leukemia · doi:10.1038/leu.2014.169 · Cited by 118 · see citing works

The upstreams and downstreams of H3K79 methylation by DOT1L

Vlaming, H., & van Leeuwen, F. (2016) · Chromosoma · doi:10.1007/s00412-015-0570-5 · Cited by 102 · see citing works

Prognostic and therapeutic value of disruptor of telomeric silencing-1-like (DOT1L) expression in patients with ovarian cancer

Zhang, X., Liu, D., Li, M., Cao, C., Wan, D., Xi, B., Li, W., Tan, J., Wang, J., Wu, Z., et al. (2017) · Journal of Hematology & Oncology · doi:10.1186/s13045-017-0400-8 · Cited by 96 · see citing works

Transcriptomic profiling of gene expression and RNA processing during Leishmania major differentiation

Dillon, L. A. L., Okrah, K., Hughitt, V. K., Suresh, R., Li, Y., Fernandes, M. C., Belew, A. T., Bravo, H. C., Mosser, D. M., & El-Sayed, N. M. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv656 · Cited by 80 · see citing works

Menin “reads” H3K79me2 mark in a nucleosomal context

Lin, J., Wu, Y., Tian, G., Yu, D., Yang, E., Lam, W. H., Liu, Z., Jing, Y., Dang, S., Bao, X., et al. (2023) · Science · doi:10.1126/science.adc9318 · Cited by 71 · see citing works

Direct and Indirect Targeting of HOXA9 Transcription Factor in Acute Myeloid Leukemia

Lambert, M., Alioui, M., Jambon, S., Depauw, S., van Seuningen, I., & David-Cordonnier, M. (2019) · Cancers · doi:10.3390/cancers11060837 · Cited by 58 · see citing works

DOT1L modulates the senescence-associated secretory phenotype through epigenetic regulation of IL1A

Leon, K. E., Buj, R., Lesko, E., Dahl, E. S., Chen, C.-W., Tangudu, N. K., Imamura-Kawasawa, Y., Kossenkov, A. V., Hobbs, R. P., & Aird, K. M. (2021) · Journal of Cell Biology · doi:10.1083/jcb.202008101 · Cited by 70 · see citing works

Chromatin Proteomics Reveals Variable Histone Modifications during the Life Cycle of Trypanosoma cruzi

de Jesus, T. C. L., Nunes, V. S., Lopes, M. D. C., Martil, D. E., Iwai, L. K., Moretti, N. S., Machado, F. C., de Lima-Stein, M. L., Thiemann, O. H., Elias, M. C., et al. (2016) · Journal of Proteome Research · doi:10.1021/acs.jproteome.6b00208 · Cited by 61 · see citing works

DOT1L promotes progenitor proliferation and primes neuronal layer identity in the developing cerebral cortex

Franz, H., Villarreal, A., Heidrich, S., Videm, P., Kilpert, F., Mestres, I., Calegari, F., Backofen, R., Manke, T., & Vogel, T. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky953 · Cited by 54 · see citing works

DOT1L histone methyltransferase regulates the expression of BCAT1 and is involved in sphere formation and cell migration of breast cancer cell lines

Oktyabri, D., Ishimura, A., Tange, S., Terashima, M., & Suzuki, T. (2016) · Biochimie · doi:10.1016/j.biochi.2016.01.005 · Cited by 52 · see citing works

DOT1L Activity Promotes Proliferation and Protects Cortical Neural Stem Cells from Activation of ATF4-DDIT3-Mediated ER Stress In Vitro

Roidl, D., Hellbach, N., Bovio, P. P., Villarreal, A., Heidrich, S., Nestel, S., Grüning, B. A., Bönisch, U., & Vogel, T. (2015) · Stem Cells · doi:10.1002/stem.2187 · Cited by 48 · see citing works

Writers, Readers, and Erasers of Epigenetic Marks

Nicholson, T. B., Veland, N., & Chen, T. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800206-3.00003-3 · Cited by 45 · see citing works

H3K79 methylation directly precedes the histone‐to‐protamine transition in mammalian spermatids and is sensitive to bacterial infections

Dottermusch-Heidel, C., Klaus, E. S., Gonzalez, N. H., Bhushan, S., Meinhardt, A., Bergmann, M. M., Renkawitz‐Pohl, R., Rathke, C., & Steger, K. (2014) · Andrology · doi:10.1111/j.2047-2927.2014.00248.x · Cited by 45 · see citing works

DOT1L-mediated murine neuronal differentiation associates with H3K79me2 accumulation and preserves SOX2-enhancer accessibility

Ferrari, F., Arrigoni, L., Franz, H., Izzo, A., Butenko, L., Trompouki, E., Vogel, T., & Manke, T. (2020) · Nature Communications · doi:10.1038/s41467-020-19001-7 · Cited by 44 · see citing works

Preferential Phosphorylation on Old Histones during Early Mitosis in Human Cells

Lin, S., Yuan, Z., Han, Y., Marchione, D. M., & Garcia, B. A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.726067 · Cited by 41 · see citing works

Targeting Histone Methyltransferase DOT1L by a Novel Psammaplin A Analog Inhibits Growth and Metastasis of Triple-Negative Breast Cancer

Byun, W. S., Kim, W. K., Han, H., Chung, H., Jang, K., Kim, H. S., Kim, S., Kim, D., Bae, E. S., Park, S., et al. (2019) · Molecular Therapy — Oncolytics · doi:10.1016/j.omto.2019.09.005 · Cited by 41 · see citing works

Distinct histone methylation and transcription profiles are established during the development of cellular quiescence in yeast

Young, C., Hillyer, C., Hokamp, K., Fitzpatrick, D. J., Konstantinov, N. K., Welty, J., Ness, S. A., Werner‐Washburne, M., Fleming, A. B., & Osley, M. A. (2017) · BMC Genomics · doi:10.1186/s12864-017-3509-9 · Cited by 41 · see citing works

MLL1 and DOT1L cooperate with meningioma-1 to induce acute myeloid leukemia.

Riedel, S. S., Haladyna, J. N., Bezzant, M., Stevens, B. M., Pollyea, D., Sinha, A., Armstrong, S., Wei, Q., Pollock, R., Daigle, S., et al. (2016) · Journal of Clinical Investigation · doi:10.1172/jci80825 · Cited by 38 · see citing works

The role of H3K79 methylation in transcription and the DNA damage response

Ljungman, M. E., Parks, L., Hulbatte, R. S., & Bedi, K. (2017) · Mutation Research/Reviews in Mutation Research · doi:10.1016/j.mrrev.2017.11.001 · Cited by 36 · see citing works

Hypoxia induces DOT1L in articular cartilage to protect against osteoarthritis

Roover, A. D., Escribano-Núñez, A., Cornelis, F. M. F., Cherifi, C., Casas-Fraile, L., Sermon, A., Cailotto, F., Lories, R. J. U., & Monteagudo, S. (2021) · JCI Insight · doi:10.1172/jci.insight.150451 · Cited by 36 · see citing works

The Role of DNA/Histone Modifying Enzymes and Chromatin Remodeling Complexes in Testicular Germ Cell Tumors

Lobo, J., Henrique, R., & Jerónimo, C. (2018) · Cancers · doi:10.3390/cancers11010006 · Cited by 35 · see citing works

The Kdm/Kmt gene families in the self-fertilizing mangrove rivulus fish, Kryptolebias marmoratus, suggest involvement of histone methylation machinery in development and reproduction

Fellous, A., Earley, R. L., & Silvestre, F. (2018) · Gene · doi:10.1016/j.gene.2018.11.046 · Cited by 34 · see citing works

Cocaine Administration and Its Withdrawal Enhance the Expression of Genes Encoding Histone-Modifying Enzymes and Histone Acetylation in the Rat Prefrontal Cortex

Sadakierska−Chudy, A., Frankowska, M., Jastrzębska, J., Wydra, K., Miszkiel, J., Sanak, M., & Filip, M. (2017) · Neurotoxicity Research · doi:10.1007/s12640-017-9728-7 · Cited by 32 · see citing works

Disruptor of telomeric silencing 1-like promotes ovarian cancer tumor growth by stimulating pro-tumorigenic metabolic pathways and blocking apoptosis

Chava, S., Wajapeyee, N., Edwards, Y. J. K., & Gupta, R. (2021) · Oncogenesis · doi:10.1038/s41389-021-00339-6 · Cited by 31 · see citing works

Selective DOT1L, LSD1, and HDAC Class I Inhibitors Reduce HOXA9 Expression in MLL-AF9 Rearranged Leukemia Cells, But Dysregulate the Expression of Many Histone-Modifying Enzymes

Lillico, R., Lawrence, C. K., & Lakowski, T. M. (2018) · Journal of Proteome Research · doi:10.1021/acs.jproteome.8b00118 · Cited by 30 · see citing works

Germline and Somatic Whole-Exome Sequencing Identifies New Candidate Genes Involved in Familial Predisposition to Serrated Polyposis Syndrome

de Lima, Y. S., Arnau‐Collell, C., Díaz‐Gay, M., Bonjoch, L., Franch‐Expósito, S., Muñoz, J., Moreira, L., Ocaña, T., Cuatrecasas, M., Herrera‐Pariente, C., et al. (2021) · Cancers · doi:10.3390/cancers13040929 · Cited by 27 · see citing works

Chemical biology and pharmacology of histone lysine methylation inhibitors

Barghout, S. H., Machado, R. A. C., & Baršytė-Lovejoy, D. (2022) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2022.194840 · Cited by 27 · see citing works

Discovery of Novel Disruptor of Silencing Telomeric 1-Like (DOT1L) Inhibitors using a Target-Specific Scoring Function for the (S)-Adenosyl- l -methionine (SAM)-Dependent Methyltransferase Family

Wang, Y., Li, L., Zhang, B., Xing, J., Chen, S., Wan, W., Song, Y., Jiang, H., Jiang, H., Luo, C., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01785 · Cited by 26 · see citing works

Dot1 histone methyltransferases share a distributive mechanism but have highly diverged catalytic properties

Stulemeijer, I. J. E., Vos, D. E. D., van Harten, K., Joshi, O., Blomberg, O. S., van Welsem, T., Terweij, M., Vlaming, H., de Graaf, E. L., Altelaar, M. A. F., et al. (2015) · Scientific Reports · doi:10.1038/srep09824 · Cited by 25 · see citing works

Ready, SET, Go: Post-translational regulation of the histone lysine methylation network in budding yeast

Separovich, R. J., & Wilkins, M. R. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100939 · Cited by 25 · see citing works

DOT1L regulates MTDH ‐mediated angiogenesis in triple‐negative breast cancer: intermediacy of NF‐κB‐HIF1α axis

Neeli, P. K., Sahoo, S., Karnewar, S., Singuru, G., Pulipaka, S., Annamaneni, S., & Kotamraju, S. (2022) · FEBS Journal · doi:10.1111/febs.16605 · Cited by 25 · see citing works

The Role of DOT1L in Normal and Malignant Hematopoiesis

Arnold, O., Barbosa, K., Deshpande, A. J., & Zhu, N. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.917125 · Cited by 24 · see citing works

Association of H3K79 monomethylation (an epigenetic signature) with arsenic-induced skin lesions

Bhattacharjee, P., Paul, S., Bhattacharjee, S., Giri, A. K., & Bhattacharjee, P. (2017) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/j.mrfmmm.2017.11.001 · Cited by 24 · see citing works

Identification and Verification of Potential Therapeutic Target Genes in Berberine-Treated Zucker Diabetic Fatty Rats through Bioinformatics Analysis

Wu, Y. S., Chen, Y.-T., Bao, Y., Li, Z.-M., Zhou, X., He, J.-N., Dai, S., & Li, C. (2016) · PLoS ONE · doi:10.1371/journal.pone.0166378 · Cited by 22 · see citing works

Computational de-orphanization of the olive oil biophenol oleacein: Discovery of new metabolic and epigenetic targets

Cuyàs, E., Castillo, D., Llorach-Parés, L., Lozano‐Sánchez, J., Verdura, S., Nonell‐Canals, A., Brunet, J., Bosch‐Barrera, J., Joven, J., Valdés, R., et al. (2019) · Food and Chemical Toxicology · doi:10.1016/j.fct.2019.05.037 · Cited by 22 · see citing works

Primitive Erythropoiesis in the Mouse is Independent of DOT1L Methyltransferase Activity

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DOT1L regulates chromatin reorganization and gene expression during sperm differentiation

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Beyond the tail: the consequence of context in histone post-translational modification and chromatin research

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Restoration of Functional Glycosylation of α-Dystroglycan in FKRP Mutant Mice Is Associated with Muscle Regeneration

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DOT1L bridges transcription and heterochromatin formation at mammalian pericentromeres

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Structural Basis of Nucleosome Recognition and Modulation

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Targeted disruption of the histone lysine 79 methyltransferase Dot1L in nephron progenitors causes congenital renal dysplasia

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The Role of Dot1l in Prenatal and Postnatal Murine Chondrocytes and Trabecular Bone

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Targeting the Histone Methyltransferase Disruptor of Telomeric Silencing 1-Like Restricts Avian Leukosis Virus Subgroup J Replication by Restoring the Innate Immune Response in Chicken Macrophages

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Role of several histone lysine methyltransferases in tumor development

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Clonal and microclonal mutational heterogeneity in high hyperdiploid acute lymphoblastic leukemia

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An epigenetic regulator-related score (EpiScore) predicts survival in patients with diffuse large B cell lymphoma and identifies patients who may benefit from epigenetic therapy

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Design, synthesis and anti leukemia cells proliferation activities of pyrimidylaminoquinoline derivatives as DOT1L inhibitors

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Trimethylation of histone H3K76 by Dot1B enhances cell cycle progression after mitosis in Trypanosoma cruzi

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Synthetic lethality and synergetic effect: the effective strategies for therapy of IDH-mutated cancers

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Synergistic antitumor effect of combined EZH2 and DOT1L inhibition in B-cell lymphoma

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The big picture of chromatin biology by cryo-EM

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DOT-1.1-dependent H3K79 methylation promotes normal meiotic progression and meiotic checkpoint function in C. elegans

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Histone H3 K79 methylation states play distinct roles in UV-induced sister chromatid exchange and cell cycle checkpoint arrest in Saccharomyces cerevisiae

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Structure-guided mutational analysis reveals the functional requirements for product specificity of DOT1 enzymes

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Connecting the DOTs on Cell Identity

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An emerging maestro of immune regulation: how DOT1L orchestrates the harmonies of the immune system

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Differentiation and localization of interneurons in the developing spinal cord depends on DOT1L expression

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Rare de novo gain-of-function missense variants in DOT1L are associated with developmental delay and congenital anomalies

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Nuclear DNA replication and repair in parasites of the genusLeishmania: Exploiting differences to develop innovative therapeutic approaches

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2D-DIGE proteomic analysis of vastus lateralis from COPD patients with low and normal fat free mass index and healthy controls

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Critical roles of protein methyltransferases and demethylases in the regulation of embryonic stem cell fate

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Epigenetics in a Spectrum of Myeloid Diseases and Its Exploitation for Therapy

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The role of histone H3 lysine demethylases in glioblastoma

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Histone H3K79 demethylation by KDM2B facilitates proper DNA replication through PCNA dissociation from chromatin

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Influence of a pre-stimulation with chronic low-dose UVB on stress response mechanisms in human skin fibroblasts

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Copy-number variation and protein expression of DOT1L in pancreatic adenocarcinoma as a potential drug target

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Discovery of the first-in-class DOT1L PROTAC degrader

Yim, H., Sun, R., Xu, Z., Kim, H. S., Kim, M. J., Cao, T., Xie, L., Chen, X., Kanıskan, H. Ü., & Jin, J. J. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117595 · Cited by 12 · see citing works

Insights into novel emerging epigenetic drugs in myeloid malignancies

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The extraordinary thermal stability of EstA from S. islandicus is independent of post translational modifications

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The Role of Histone Methylation and Methyltransferases in Gene Regulation

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Bookmarking by histone methylation ensures chromosomal integrity during mitosis

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A Novel Frameshift Mutation in KAT6A Is Associated with Pancraniosynostosis

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Epigenetic insight into regulatory role of chromatin covalent modifications in lifecycle and virulence of Phytophthora

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Identification of epigenetic histone modifications and analysis of histone lysine methyltransferases in Alexandrium pacificum

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A novel germline variant in the DOT1L gene co-segregating in a Dutch family with a history of melanoma

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Dot1L Promotes Stress-Induced Cardiac Hypertrophy in Mice via Tbx6

Liu, J., Jin, Y., Zuo, S., Mu, C., Wang, B., Huang, D., Liu, Q., Zhang, K., Song, J., Xuan, C., et al. (2025) · Circulation Research · doi:10.1161/circresaha.124.324940 · Cited by 6 · see citing works

DOT1L promotes phenotypic transition of vascular smooth muscle cells following vascular injury in diabetes through activation of the FGFR4/PI3K/AKT/Jag/Notch signaling pathway

Zhang, J., Wu, D., Cheng, C., Yang, Z., Chen, Z., Liu, L., Li, W., Wang, W., Huang, C., & Yang, J. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.112223 · Cited by 6 · see citing works

Targeting ‘histone mark’: Advanced approaches in epigenetic regulation of telomere dynamics in cancer

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H3K79 methylation promotes rapid growth of Alexandrium pacificum under high light intensity via increased photosynthesis

Zhu, Z., Qi, J., Zhang, Q., & Sui, Z. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.164788 · Cited by 5 · see citing works

The Role of DOT1L Methyltransferase Activity in Fetal HematopoiesisPreprint

Malcom, C. A., Piasecka‐Srader, J., Chakravarthi, V. P., Borosha, S., Ratri, A., Alvarez, N. S., Vivian, J. L., Fields, T. A., Rumi, M. A. K., & Fields, P. E. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.09.30.319889 · Cited by 5 · see citing works

Gene Transcription as a Therapeutic Target in Leukemia

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Discovery of Novel Non-nucleoside DOT1LR231Q Inhibitors with Improved Pharmacokinetic Properties and Anti-lung Cancer Efficacy

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Drosophila melanogaster positive transcriptional elongation factors regulate metabolic and sex-biased expression in adults

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Overview of Epigenetic Signatures and Their Regulation by Epigenetic Modification Enzymes

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The H3K79 methylase DOT1, unreported in photosynthetic plants, exists in Alexandrium pacificum and participates in its growth regulation

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Chromatin environment-dependent effects of DOT1L on gene expression in male germ cells

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

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Shared Genetic Features of Psoriasis and Myocardial Infarction: Insights From a Weighted Gene Coexpression Network Analysis

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A medicinal chemistry perspective on disruptor of telomeric silencing 1-like: Its mechanisms and modulators in cancer treatment

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Therapeutic targeting of tricarboxylic acid cycle and oxidative phosphorylation: a critical analysis of metabolic interventions in cancer treatment

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Post-translational modifications in retinoblastoma: mechanisms, immune regulation, and therapeutic opportunities

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Impacts of Histone Lysine Methylation on Chromatin

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DOT1L Methyltransferase Activity Preserves SOX2-Enhancer Accessibility And Prevents Activation of Repressed Genes In Murine Stem CellsPreprint

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NRF1 Transcriptomic Signatures Contribute to the Pathogenesis of the Most Aggressive Brain Cancer - Glioblastoma

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Interaction of the NuA4 Complex and Chromatin Modifications with the DNA Damage Tolerance Pathway

Renaud-Young, M. M. (2015) · Libraries and Cultural Resources (University of Calgary) · doi:10.11575/prism/26597

Linking the Cell Cycle to Histone Modifications: Dot1, G1/S, and Cycling K79me2

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Deficiency of H3K79 Histone Methyltransferase Dot1-like Protein (DOT1L) Inhibits Cell Proliferation

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The many faces of histone H3K79 methylation

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DOT1L and H3K79 Methylation in Transcription and Genomic Stability

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The Relationship Between DOT1L, Histone H3 Methylation, and Genome Stability in Cancer

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