DOT1L and H3K79 Methylation in Transcription and Genomic Stability
Open accessAbstract
The organization of eukaryotic genomes into chromatin provides challenges for the cell to accomplish basic cellular functions, such as transcription, DNA replication and repair of DNA damage. Accordingly, a range of proteins modify and/or read chromatin states to regulate access to chromosomal DNA. Yeast Dot1 and the mammalian homologue DOT1L are methyltransferases that can add up to three methyl groups to histone H3 lysine 79 (H3K79). H3K79 methylation is implicated in several processes, including transcription elongation by RNA polymerase II, the DNA damage response and cell cycle checkpoint activation. DOT1L is also an important drug target for treatment of mixed lineage leukemia (MLL)-rearranged leukemia where aberrant transcriptional activation is promoted by DOT1L mislocalisation. This review summarizes what is currently known about the role of Dot1/DOT1L and H3K79 methylation in transcription and genomic stability.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
It is difficult to formally prove a direct causative role of any histone modification in mammalian cells.
“Although it is undeniable that histone modifications robustly modulate key cellular processes and there is compelling evidence for the role of histone methylation in DNA processes, as outlined above, it is difficult to formally prove a direct causative role of any histone modification in mammalian cells (see REF. 35 for discussion).”
From The roles of DNA, RNA and histone methylation in ageing and cancer (2019) · cites this paper as [35]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Crystal structure of the nucleosome core particle at 2.8 Å resolution
Luger, K., Mäder, A. W., Richmond, R. K., Sargent, D. F., & Richmond, T. J. (1997) · Nature · doi:10.1038/38444 · Cited by 9,466 · see citing works
The Role of Chromatin during Transcription
Li, B., Carey, M., & Workman, J. L. (2007) · Cell · doi:10.1016/j.cell.2007.01.015 · Cited by 3,503 · see citing works
Elective induction versus spontaneous labor after sonographic diagnosis of fetal macrosomia.
Combs, C. A., Singh, N. B., & Khoury, J. C. (1993) · PubMed · Cited by 2,462 · see citing works
Combinatorial patterns of histone acetylations and methylations in the human genome
Wang, Z., Zang, C., Rosenfeld, J. A., Schones, D. E., Barski, A., Cuddapah, S., Cui, K., Roh, T.-Y., Peng, W., Zhang, M. Q., et al. (2008) · Nature Genetics · doi:10.1038/ng.154 · Cited by 2,331 · see citing works
The diverse functions of histone lysine methylation
Martin, C., & Zhang, Y. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1761 · Cited by 2,066 · see citing works
Twenty-Five Years of the Nucleosome, Fundamental Particle of the Eukaryote Chromosome
Kornberg, R. D., & Lorch, Y. (1999) · Cell · doi:10.1016/s0092-8674(00)81958-3 · Cited by 1,833 · see citing works
Genome Regulation by Polycomb and Trithorax Proteins
Schuettengruber, B., Chourrout, D. M., Vervoort, M., Leblanc, B., & Cavalli, G. (2007) · Cell · doi:10.1016/j.cell.2007.02.009 · Cited by 1,433 · see citing works
Connecting microRNA Genes to the Core Transcriptional Regulatory Circuitry of Embryonic Stem Cells
Marson, A., Levine, S. S., Cole, M. F., Frampton, G. M., Brambrink, T., Johnstone, S. E., Guenther, M. G., Johnston, W. K., Wernig, M., Newman, J. J., et al. (2008) · Cell · doi:10.1016/j.cell.2008.07.020 · Cited by 1,361 · see citing works
MLL translocations, histone modifications and leukaemia stem-cell development
Krivtsov, A., & Armstrong, S. (2007) · Nature Reviews. Cancer · doi:10.1038/nrc2253 · Cited by 1,294 · see citing works
JmjC-domain-containing proteins and histone demethylation
Klose, R. J., Kallin, E. M., & Zhang, Y. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1945 · Cited by 1,290 · see citing works
Double-strand break repair: 53BP1 comes into focus
Panier, S., & Boulton, S. J. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3719 · Cited by 1,090 · see citing works
Ubiquitination of histone H2B regulates H3 methylation and gene silencing in yeast
Sun, Z., & Allis, C. D. (2002) · Nature · doi:10.1038/nature00883 · Cited by 1,076 · see citing works
Botuyan, M. V., Lee, J., Ward, I. M., Kim, J., Thompson, J. R., Chen, J., & Mer, G. (2006) · Cell · doi:10.1016/j.cell.2006.10.043 · Cited by 973 · see citing works
Histone methylation in transcriptional control
Kouzarides, T. (2002) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(02)00287-3 · Cited by 908 · see citing works
Regulation of histone methylation by demethylimination and demethylation
Klose, R. J., & Zhang, Y. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2143 · Cited by 889 · see citing works
Methylated lysine 79 of histone H3 targets 53BP1 to DNA double-strand breaks
Huyen, Y., Zgheib, O., DiTullio Jr, R. A., Gorgoulis, V. G., Zacharatos, P., Petty, T. J., Sheston, E. A., Mellert, H. S., Stavridi, E. S., & Halazonetis, T. D. (2004) · Nature · doi:10.1038/nature03114 · Cited by 884 · see citing works
Many paths to methyltransfer: a chronicle of convergence
Schubert, H. L., Blumenthal, R. M., & Cheng, X. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00090-2 · Cited by 876 · see citing works
Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain
Feng, Q. F., Wang, H., Ng, H., Erdjument‐Bromage, H., Tempst, P., Struhl, K., & Zhang, Y. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00901-6 · Cited by 866 · see citing works
Dot1p Modulates Silencing in Yeast by Methylation of the Nucleosome Core
van Leeuwen, F., Gafken, P. R., & Gottschling, D. E. (2002) · Cell · doi:10.1016/s0092-8674(02)00759-6 · Cited by 853 · see citing works
hDOT1L Links Histone Methylation to Leukemogenesis
Okada, Y., Feng, Q. F., Lin, Y.-H., Jiang, Q., Li, Y., Coffield, V. M., Su, L., Xu, G., & Zhang, Y. (2005) · Cell · doi:10.1016/j.cell.2005.02.020 · Cited by 819 · see citing works
Schübeler, D., MacAlpine, D. M., Scalzo, D., Wirbelauer, C., Kooperberg, C. L., van Leeuwen, F., Gottschling, D. E., O’Neill, L. P., Turner, B. M., Delrow, J. J., et al. (2004) · Genes & Development · doi:10.1101/gad.1198204 · Cited by 795 · see citing works
Phosphorylation and functions of the RNA polymerase II CTDPreprint
Phatnani, H. P., & Greenleaf, A. L. (2006) · Genes & Development · doi:10.1101/gad.1477006 · Cited by 752 · see citing works
Krogan, N. J., Dover, J., Wood, A., Schneider, J., Heidt, J. W., Boateng, M. A., Dean, K., Ryan, O. W., Golshani, A., Johnston, M., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00091-1 · Cited by 706 · see citing works
Erasing the methyl mark: histone demethylases at the center of cellular differentiation and diseasePreprint
Cloos, P. A., Christensen, J., Agger, K., & Helin, K. (2008) · Genes & Development · doi:10.1101/gad.1652908 · Cited by 664 · see citing works
The diverse functions of Dot1 and H3K79 methylationPreprint
Nguyen, A. T., & Zhang, Y. (2011) · Genes & Development · doi:10.1101/gad.2057811 · Cited by 602 · see citing works
Jonkers, I., Kwak, H., & Lis, J. T. (2014) · eLife · doi:10.7554/elife.02407 · Cited by 581 · see citing works
Lin, C., Smith, E. R., Takahashi, H., Lai, K. C., Martin‐Brown, S., Florens, L. A., Washburn, M. P., Conaway, J. W., Conaway, R. C., & Shilatifard, A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.026 · Cited by 574 · see citing works
Chemically ubiquitylated histone H2B stimulates hDot1L-mediated intranucleosomal methylation
McGinty, R. K., Kim, J., Chatterjee, C., Roeder, R. G., & Muir, T. W. (2008) · Nature · doi:10.1038/nature06906 · Cited by 563 · see citing works
Ng, H. H., Feng, Q., Wang, H., Erdjument‐Bromage, H., Tempst, P., Zhang, Y., & Struhl, K. (2002) · Genes & Development · doi:10.1101/gad.1001502 · Cited by 536 · see citing works
Histone H3.3 is enriched in covalent modifications associated with active chromatin
McKittrick, E., Gafken, P. R., Ahmad, K., & Henikoff, S. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0308092100 · Cited by 520 · see citing works
Trans-histone regulatory pathway in chromatin
Briggs, S. D., Xiao, T., Sun, Z., Caldwell, J., Shabanowitz, J., Hunt, D. F., Allis, C. D., & Strahl, B. D. (2002) · Nature · doi:10.1038/nature00970 · Cited by 516 · 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
Steger, D. J., Lefterova, M. I., Ying, L., Stonestrom, A. J., Schupp, M., Zhuo, D. X., Vakoc, A. L., Kim, J., Chen, J., Lazar, M. A., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02076-07 · Cited by 499 · see citing works
The MLL recombinome of acute leukemias in 2013
Meyer, C., Hofmann, J., Burmeister, T., Gröger, D., Park, T. S., Emerenciano, M., Pombo‐de‐Oliveira, M. S., Renneville, A., Villarèse, P., Macintyre, E. A., et al. (2013) · Leukemia · doi:10.1038/leu.2013.135 · Cited by 491 · see citing works
Identification of High-Copy Disruptors of Telomeric Silencing in Saccharomyces cerevisiae
Singer, M. S., Kahana, A., Wolf, A. J., Meisinger, L. L., Peterson, S. E., Goggin, C., Mahowald, M., & Gottschling, D. E. (1998) · Genetics · doi:10.1093/genetics/150.2.613 · Cited by 463 · see citing works
PHF8 mediates histone H4 lysine 20 demethylation events involved in cell cycle progression.
Liu, W., Tanasa, B., Tyurina, O. V., Zhou, T. Y., Gassmann, R., Liu, W. T., Ohgi, K. A., Benner, C., Garcia-Bassets, I., Aggarwal, A. K., et al. (2010) · Nature · doi:10.1038/nature09272 · Cited by 441 · see citing works
Ng, H., Xu, R.-M., Zhang, Y., & Struhl, K. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200433200 · Cited by 432 · see citing works
Min, J., Feng, Q. F., Li, Z., Zhang, Y., & Xu, R.-M. (2003) · Cell · doi:10.1016/s0092-8674(03)00114-4 · Cited by 431 · see citing works
A role for the MLL fusion partner ENL in transcriptional elongation and chromatin modification
Mueller, D., Bach, C., Zeisig, D. T., García-Cuéllar, M.-P., Monroe, S., Sreekumar, A., Zhou, R., Nesvizhskii, A. I., Chinnaiyan, A. M., Hess, J. L., et al. (2007) · Blood · doi:10.1182/blood-2007-05-090514 · Cited by 396 · see citing works
SET domain proteins modulate chromatin domains in eu- and heterochromatin
Jenuwein, T., Laible, G., Dorn, R., & Reuter, G. (1998) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050127 · Cited by 395 · see citing works
Jones, B. T., Su, H., Bhat, A., Lei, H., Bajko, J., Hevi, S., Baltus, G. A., Kadam, S., Zhai, H., Valdez, R., et al. (2008) · PLoS Genetics · doi:10.1371/journal.pgen.1000190 · Cited by 384 · see citing works
Yokoyama, A., Lin, M., Naresh, A., Kitabayashi, I., & Cleary, M. L. (2010) · Cancer Cell · doi:10.1016/j.ccr.2009.12.040 · Cited by 374 · see citing works
Nucleotide excision repair in yeast
Prakash, S., & Prakash, L. (2000) · Mutation research. Fundamental and molecular mechanisms of mutagenesis · doi:10.1016/s0027-5107(00)00037-3 · Cited by 371 · see citing works
Hake, S. B., Garcia, B. A., Duncan, E. M., Kauer, M., Dellaire, G., Shabanowitz, J., Bazett‐Jones, D. P., Allis, C. D., & Hunt, D. F. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509266200 · Cited by 333 · see citing works
Fast signals and slow marks: the dynamics of histone modifications
Barth, T. K., & Imhof, A. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.05.006 · Cited by 333 · see citing works
Corden, J. L. (1990) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(90)90236-5 · Cited by 332 · see citing works
Ng, H., Ciccone, D. N., Morshead, K. B., Oettinger, M. A., & Struhl, K. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0437846100 · Cited by 315 · see citing works
Linking H3K79 trimethylation to Wnt signaling through a novel Dot1-containing complex (DotCom)Preprint
Mohan, M., Herz, H., Takahashi, Y.-H., Lin, C., Lai, K. C., Zhang, Y., Washburn, M. P., Florens, L. A., & Shilatifard, A. (2010) · Genes & Development · doi:10.1101/gad.1898410 · Cited by 312 · see citing works
Bitoun, E., Oliver, P. L., & Davies, K. E. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl444 · Cited by 311 · see citing works
Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development
Qi, H. H., Sarkissian, M., Hu, G., Wang, Z., Bhattacharjee, A., Gordon, D. B., Gonzales, M., Lan, F., Ongusaha, P. P., Huarte, M., et al. (2010) · Nature · doi:10.1038/nature09261 · Cited by 303 · see citing works
Disruptor of Telomeric Silencing-1 Is a Chromatin-specific Histone H3 Methyltransferase
Lacoste, N., Utley, R. T., Hunter, J. M., Poirier, G. G., & Côté, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200366200 · Cited by 298 · see citing works
Wysocki, R., Javaheri, A., Allard, S., Sha, F., Côté, J., & Kron, S. J. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.19.8430-8443.2005 · Cited by 288 · see citing works
Giannattasio, M., Lazzaro, F., Plevani, P., & Muzi-Falconi, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414453200 · Cited by 287 · see citing works
Catalytic site remodelling of the DOT1L methyltransferase by selective inhibitors
Yu, W., Chory, E. J., Wernimont, A. K., Tempel, W., Scopton, A. P., Alexander Joel Federation, Marineau, J., Qi, J., Baršytė-Lovejoy, D., Yi, J., et al. (2012) · Nature Communications · doi:10.1038/ncomms2304 · Cited by 283 · see citing works
Veloso, A., Kirkconnell, K. S., Magnuson, B., Biewen, B., Paulsen, M. T., Wilson, T. E., & Ljungman, M. (2014) · Genome Research · doi:10.1101/gr.171405.113 · Cited by 281 · see citing works
Histone modifications defining active genes persist after transcriptional and mitotic inactivation
Kouskouti, A., & Talianidis, I. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600516 · Cited by 263 · see citing works
Histone H2B Ubiquitylation Controls Processive Methylation but Not Monomethylation by Dot1 and Set1
Shahbazian, M. D., Zhang, K., & Grunstein, M. R. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.010 · Cited by 248 · see citing works
The effect of H3K79 dimethylation and H4K20 trimethylation on nucleosome and chromatin structure
Lu, X., Simon, M. D., Chodaparambil, J. V., Hansen, J. C., Shokat, K. M., & Luger, K. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1489 · Cited by 232 · see citing works
The pol II CTD: new twists in the tail
Zaborowska, J., Egloff, S., & Murphy, S. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3285 · Cited by 227 · see citing works
Self-citationEpigenetics: molecular mechanisms and implications for disease
Handel, A. E., Ebers, G. C., & Ramagopalan, S. V. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.11.003 · Cited by 221 · see citing works
Cho, M.-H., Park, J.-H., Choi, H.-J., Park, M.-K., Won, H.-Y., Park, Y.-J., Lee, C. H., Oh, S.-H., Song, Y.-S., Kim, H. S., et al. (2015) · Nature Communications · doi:10.1038/ncomms8821 · Cited by 211 · see citing works
Chen, C., Koche, R., Sinha, A., Deshpande, A., Zhu, N., Eng, R., Doench, J. G., Xu, H.-M., Chu, S. H., Qi, J., et al. (2015) · Nature Medicine · doi:10.1038/nm.3832 · Cited by 211 · see citing works
Misguided Transcriptional Elongation Causes Mixed Lineage Leukemia
Mueller, D., García-Cuéllar, M.-P., Bach, C., Buhl, S., Maethner, E., & Slany, R. K. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000249 · Cited by 203 · see citing works
Altaf, M., Utley, R. T., Lacoste, N., Tan, S., Briggs, S. D., & Côté, J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.12.002 · Cited by 192 · see citing works
Structure and function of the nucleosome-binding PWWP domain
Su, Q., & Min, J. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.09.001 · Cited by 191 · see citing works
Lazzaro, F., Sapountzi, V., Granata, M., Pellicioli, A., Vaze, M. B., Haber, J. E., Plevani, P., Lydall, D. A., & Muzi-Falconi, M. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.81 · Cited by 190 · see citing works
Milne, T. A., Martin, M. E., Brock, H. W., Slany, R. K., & Hess, J. L. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-1041 · Cited by 181 · see citing works
Schulze-Hentrich, J. M., Jackson, J., Nakanishi, S., Gardner, J. M., Hentrich, T., Haug, J., Johnston, M., Jaspersen, S. L., Kobor, M. S., & Shilatifard, A. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.07.017 · Cited by 180 · see citing works
Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states
Frederiks, F., Tzouros, M., Oudgenoeg, G., van Welsem, T., Fornerod, M. W. J., Krijgsveld, J., & van Leeuwen, F. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1432 · Cited by 172 · see citing works
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
Alpatov, R., Lesch, B. J., Nakamoto-Kinoshita, M., Blanco, M. A., Chen, S., Stützer, A., Armache, K., Simon, M. D., Xu, C., Ali, M., et al. (2014) · Cell · doi:10.1016/j.cell.2014.03.040 · Cited by 163 · see citing works
Suzuki, H., Takatsuka, S., Akashi, H., Yamamoto, E., Nojima, M., Maruyama, R., Kai, M., Yamano, H., Sasaki, Y., Tokino, T., et al. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-1076 · Cited by 158 · see citing works
Histone modifying enzymes and cancer: Going beyond histones
Zhang, K., & Dent, S. (2005) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20615 · Cited by 152 · see citing works
Characterization of the grappa Gene, the Drosophila Histone H3 Lysine 79 Methyltransferase
Shanower, G., Müller, M., Blanton, J. L., Honti, V., Gyurkovics, H., & Schedl, P. D. (2004) · Genetics · doi:10.1534/genetics.104.033191 · Cited by 135 · see citing works
Tomson, B. N., & Arndt, K. M. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.08.011 · Cited by 134 · see citing works
Chatting histone modifications in mammals
Izzo, A., & Schneider, R. (2010) · Briefings in Functional Genomics · doi:10.1093/bfgp/elq024 · Cited by 130 · see citing works
Reciprocal intronic and exonic histone modification regions in humans
Huff, J. T., Plocik, A. M., Guthrie, C., & Yamamoto, K. R. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1924 · Cited by 128 · see citing works
Fingerman, I. M., Li, H.-C., & Briggs, S. D. (2007) · Genes & Development · doi:10.1101/gad.1560607 · Cited by 126 · see citing works
Toh, G. W. ‐., O'Shaughnessy, A. M., Jimeno, S., Dobbie, I. M., Grenon, M., Maffini, S., O’Rorke, A., & Lowndes, N. F. (2006) · DNA repair · doi:10.1016/j.dnarep.2006.03.005 · Cited by 123 · 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
Dot1 and Histone H3K79 Methylation in Natural Telomeric and HM Silencing
Takahashi, Y.-H., Schulze-Hentrich, J. M., Jackson, J., Hentrich, T., Seidel, C. W., Jaspersen, S. L., Kobor, M. S., & Shilatifard, A. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.006 · Cited by 116 · see citing works
Leach, B. I., Kuntimaddi, A., Schmidt, C., Cierpicki, T., Johnson, S. A., & Bushweller, J. H. (2012) · Structure · doi:10.1016/j.str.2012.11.011 · Cited by 114 · see citing works
Wakeman, T. P., Wang, Q., Feng, J., & Wang, X. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.50 · Cited by 113 · see citing works
Docking onto chromatin via the Saccharomyces cerevisiae Rad9 Tudor domain
Grenon, M., Costelloe, T., Jimeno, S., O'Shaughnessy, A. M., Fitzgerald, J., Zgheib, O., Degerth, L., & Lowndes, N. F. (2007) · Yeast · doi:10.1002/yea.1441 · Cited by 110 · see citing works
Kim, S.-K., Jung, I., Lee, H., Kang, K., Kim, M., Jeong, K., Kwon, C. S., Han, Y., Kim, Y. S., Kim, D., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.384057 · Cited by 108 · see citing works
Changes in H3K79 Methylation During Preimplantation Development in Mice
Ooga, M., Inoue, A., Kageyama, S., Akiyama, T., Nagata, M., & Aoki, F. (2007) · Biology of Reproduction · doi:10.1095/biolreprod.107.063453 · Cited by 100 · see citing works
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
Basavapathruni, A., Olhava, E. J., Daigle, S. R., Therkelsen, C. A., Jin, L., Boriack‐Sjodin, P. A., Allain, C. J., Klaus, C. R., Raimondi, A., Scott, M. P., et al. (2014) · Biopharmaceutics & Drug Disposition · doi:10.1002/bdd.1889 · Cited by 79 · 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
DOT1L Inhibition Sensitizes MLL-Rearranged AML to Chemotherapy
Liu, W., Deng, L., Song, Y., & Redell, M. S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0098270 · Cited by 75 · see citing works
Jung, I., Kim, S.-K., Kim, M., Han, Y., Kim, Y. S., Kim, D., & Lee, D. (2012) · Genome Research · doi:10.1101/gr.120634.111 · Cited by 70 · see citing works
Mixed lineage rearranged leukaemia
Stein, E. M., & Tallman, M. S. (2015) · Current Opinion in Hematology · doi:10.1097/moh.0000000000000123 · Cited by 69 · see citing works
A Common Telomeric Gene Silencing Assay Is Affected by Nucleotide Metabolism
Rossmann, M. P., Luo, W., Tsaponina, O., Chabes, A., & Stillman, B. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.03.007 · Cited by 67 · see citing works
Game, J. C., Williamson, M. S., Spicakova, T., & Brown, J. M. (2006) · Genetics · doi:10.1534/genetics.106.057794 · Cited by 67 · see citing works
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
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
Silent information regulator 3: the Goldilocks of the silencing complexPreprint
Norris, A., & Boeke, J. D. (2010) · Genes & Development · doi:10.1101/gad.1865510 · Cited by 62 · see citing works
Chernikova, S. B., Dorth, J. A., Razorenova, O. V., Game, J. C., & Brown, J. M. (2010) · Radiation Research · doi:10.1667/rr2184.1 · Cited by 59 · see citing works
DNA-histone interactions in nucleosomes
Holde, K. E. V., Allen, J., Tatchell, K., Weischet, W. O., & Lohr, D. (1980) · Biophysical Journal · doi:10.1016/s0006-3495(80)84956-3 · Cited by 53 · see citing works
Conde, F., & San-Segundo, P. A. (2008) · Genetics · doi:10.1534/genetics.108.089003 · Cited by 51 · see citing works
Epigenetic mechanisms in human disease.
Feinberg, A. P., Oshimura, M., & Barrett, J. C. (2002) · PubMed · Cited by 47 · see citing works
Xiao, Y., Tang, Z., Fu, X., Yin, J., Liang, Y., Li, C., Li, H., Tian, Q., Roeder, R. G., & Wang, G. (2015) · The EMBO Journal · doi:10.15252/embj.201591279 · Cited by 44 · see citing works
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
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
Ho, L., Sinha, A., Verzi, M. P., Bernt, K. M., Armstrong, S. A., & Shivdasani, R. A. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01463-12 · Cited by 38 · see citing works
Structural Plasticity of Methyllysine Recognition by the Tandem Tudor Domain of 53BP1
Tong, Q., Cui, G., Botuyan, M. V., Rothbart, S. B., Hayashi, R., Musselman, C. A., Singh, N., Appella, E., Strahl, B. D., Mer, G., et al. (2015) · Structure · doi:10.1016/j.str.2014.11.013 · Cited by 38 · see citing works
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
Flagged first, then by citations
3 of the 110 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
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
Targeting Transcription Factors for Cancer Treatment
Lambert, M., Jambon, S., Depauw, S., & David‐Cordonnier, M. (2018) · Molecules · doi:10.3390/molecules23061479 · Cited by 351 · see citing works
Emerging role of PI3K/AKT in tumor-related epigenetic regulation
Yang, Q., Jiang, W., & Hou, P. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.04.001 · Cited by 206 · see citing works
Structural Basis of Dot1L Stimulation by Histone H2B Lysine 120 Ubiquitination
Valencia‐Sánchez, M. I., Ioannes, P. D., Wang, M., Vasilyev, N., Chen, R., Nudler, E., Armache, J., & Armache, K. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.03.029 · Cited by 150 · see citing works
Sundaram, M. K., Hussain, A., Haque, S., Raina, R., & Afroze, N. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29147 · Cited by 142 · see citing works
Structural Basis for Recognition of Ubiquitylated Nucleosome by Dot1L Methyltransferase
Spangler, C. J., Baird, M. R., Hsu, A. L., Barbour, E. H., Koyama, Y., Borgnia, M. J., & McGinty, R. K. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.058 · Cited by 134 · see citing works
Histone Modifications and their Role in Colorectal Cancer (Review)
Qin, J., Wen, B., Liang, Y., Yu, W., & Li, H. (2019) · Pathology & Oncology Research · doi:10.1007/s12253-019-00663-8 · Cited by 121 · see citing works
The Molecular Basis and Therapeutic Aspects of Cisplatin Resistance in Oral Squamous Cell Carcinoma
Cheng, Y., Li, S., Gao, L., Zhi, K., & Ren, W. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.761379 · Cited by 118 · see citing works
Regulation of the Dot1 histone H3K79 methyltransferase by histone H4K16 acetylation
Valencia‐Sánchez, M. I., Ioannes, P. D., Wang, M., Truong, D. M., Lee, R., Armache, J., Boeke, J. D., & Armache, K. (2021) · Science · doi:10.1126/science.abc6663 · Cited by 106 · see citing works
Moritz, L., & Hammoud, S. S. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.895502 · Cited by 92 · see citing works
CRISPR-Cas9 screens identify regulators of antibody–drug conjugate toxicity
Tsui, C. K., Barfield, R. M., Fischer, C. R., Morgens, D. W., Li, A., Smith, B. A. H., Gray, M. A., Bertozzi, C. R., Rabuka, D., & Bassik, M. C. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0342-2 · Cited by 85 · see citing works
BRCA1/BARD1 site-specific ubiquitylation of nucleosomal H2A is directed by BARD1
Witus, S. R., Burrell, A. L., Farrell, D. P., Kang, J., Wang, M., Hansen, J. M., Pravat, A., Tuttle, L. M., Stewart, M. D., Brzović, P. S., et al. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-00556-4 · Cited by 84 · see citing works
Broad domains of histone H3 lysine 4 trimethylation in transcriptional regulation and disease
Park, S., Kim, G. W., Kwon, S. H., & Lee, J. (2020) · FEBS Journal · doi:10.1111/febs.15219 · Cited by 83 · see citing works
Targeting epigenetic regulators for inflammation: Mechanisms and intervention therapy
Zhang, S., Meng, Y., Zhou, L., Qiu, L., Wang, H., Su, D., Zhang, B., Chan, K. M., & Han, J. (2022) · MedComm · doi:10.1002/mco2.173 · Cited by 82 · see citing works
H3K36 trimethylation-mediated biological functions in cancer
Chu, X., Fan, T. T., Tian, H., Zheng, Y., Zhou, Z., Li, S., Li, C., & He, J. (2021) · Clinical Epigenetics · doi:10.1186/s13148-021-01187-2 · Cited by 79 · see citing works
The Chromatin Response to Double-Strand DNA Breaks and Their Repair
Aleksandrov, R., Hristova, R. H., Stoynov, S., & Gospodinov, A. G. (2020) · Cells · doi:10.3390/cells9081853 · Cited by 75 · see citing works
Role of Epigenomics in Bone and Cartilage Disease
van Meurs, J. B. J., Boer, C. G., López-Delgado, L., & Riancho, J. A. (2019) · Journal of Bone and Mineral Research · doi:10.1002/jbmr.3662 · Cited by 74 · 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
An Insight into Reprogramming Barriers to iPSC Generation
Haridhasapavalan, K. K., Raina, K., Dey, C., Adhikari, P., & Thummer, R. P. (2019) · Stem Cell Reviews and Reports · doi:10.1007/s12015-019-09931-1 · Cited by 67 · 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
Antecedent chromatin organization determines cGAS recruitment to ruptured micronuclei
MacDonald, K. M., Nicholson-Puthenveedu, S., Tageldein, M. M., Khasnis, S., Arrowsmith, C. H., & Harding, S. M. (2023) · Nature Communications · doi:10.1038/s41467-023-36195-8 · Cited by 65 · 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
Sahu, A., Köse, K., Kraehenbuehl, L., Byers, C., Holland, A., Tembo, T., Santella, A., Alfonso, A., Li, M., Cordova, M. A., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-32738-7 · Cited by 62 · see citing works
Lung Cancer Therapy Targeting Histone Methylation: Opportunities and Challenges
Chen, Y., Liu, X., Li, Y., Quan, C., Zheng, L., & Huang, K. (2018) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2018.06.001 · Cited by 61 · see citing works
DOT1L complex regulates transcriptional initiation in human erythroleukemic cells
Wu, A., Zhi, J., Tian, T., Cihan, A., Cevher, M. A., Liu, Z., David, Y., Muir, T. W., Roeder, R. G., & Yu, M. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2106148118 · Cited by 59 · see citing works
Álvarez‐Álvarez, M. M., Biayna, J., & Supek, F. (2022) · Nature Communications · doi:10.1038/s41467-022-32285-1 · Cited by 58 · see citing works
Histone post-translational modification and the DNA damage response
Song, H., Shen, R., Liu, X., Yang, X., Xie, K., Guo, Z., & Wang, D. (2022) · Genes & Diseases · doi:10.1016/j.gendis.2022.04.002 · Cited by 54 · see citing works
Wang, S., Sheng, H., Zheng, F., & Zhang, F. (2021) · Phytomedicine · doi:10.1016/j.phymed.2021.153499 · Cited by 53 · see citing works
SETD2: from chromatin modifier to multipronged regulator of the genome and beyond
Molenaar, T. M., & van Leeuwen, F. (2022) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-022-04352-9 · Cited by 51 · see citing works
Genistein Modulates Signaling Pathways and Targets Several Epigenetic Markers in HeLa Cells
Sundaram, M. K., Pramodh, S., Somvanshi, P., Bhardwaj, T., Mandal, R. K., Hussain, A., & Haque, S. (2019) · Genes · doi:10.3390/genes10120955 · Cited by 51 · see citing works
Histone methyltransferase DOT1L controls state-specific identity during B cell differentiation
Aslam, M. A., Alemdehy, M. F., Kwesi‐Maliepaard, E. M., Cagánová, M., Pardieck, I. N., van den Brand, T., Muhaimin, F. I., van Welsem, T., de Rink, I., Song, J., et al. (2021) · EMBO Reports · doi:10.15252/embr.202051184 · Cited by 43 · see citing works
Kwesi‐Maliepaard, E. M., Aslam, M. A., Alemdehy, M. F., van den Brand, T., McLean, C. M., Vlaming, H., van Welsem, T., Korthout, T., Lancini, C., Hendriks, S., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1920372117 · Cited by 43 · see citing works
Histone variant-specific post-translational modifications
Joseph, F. M., & Young, N. L. (2022) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2022.02.012 · Cited by 43 · see citing works
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
Histone methyltransferase DOT1L is essential for self-renewal of germline stem cellsPreprint
Lin, H., Cheng, K., KUBOTA, H. Y., Lan, Y., Riedel, S. S., Kakiuchi, K., Sasaki, K., Bernt, K. M., Bartolomei, M. S., Luo, M., et al. (2022) · Genes & Development · doi:10.1101/gad.349550.122 · Cited by 43 · see citing works
Vlaming, H., McLean, C. M., Korthout, T., Alemdehy, M. F., Hendriks, S., Lancini, C., Palit, S. A. L., Klarenbeek, S., Kwesi‐Maliepaard, E. M., Molenaar, T. M., et al. (2019) · The EMBO Journal · doi:10.15252/embj.2019101564 · Cited by 39 · see citing works
Szczepanek, J., & Tretyn, A. (2023) · Biomolecules · doi:10.3390/biom13111590 · Cited by 43 · see citing works
Liu, L., Zou, J., Guan, Y. A., Zhang, Y., Zhang, W., Zhou, X., Xiong, C., Tolbert, E. M., Zhao, T. C., Bayliss, G. P., et al. (2019) · The FASEB Journal · doi:10.1096/fj.201801861r · Cited by 40 · see citing works
New Potent DOT1L Inhibitors for in Vivo Evaluation in Mouse
Stauffer, F., Weiss, A., Scheufler, C., Möbitz, H., Ragot, C., Beyer, K. S., Calkins, K., Guthy, D. A., Kiffe, M., Eerdenbrugh, B. V., et al. (2019) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00452 · Cited by 40 · see citing works
The histone methyltransferase DOT1L is a new epigenetic regulator of pulmonary fibrosis
Yang, D., Xu, P., Su, H., Zhong, W., Xu, J., Su, Z., & Liu, X. (2022) · Cell Death and Disease · doi:10.1038/s41419-021-04365-5 · Cited by 39 · see citing works
Histone Modifications and the Maintenance of Telomere Integrity
Jezek, M., & Green, E. M. (2019) · Cells · doi:10.3390/cells8020199 · Cited by 39 · see citing works
Role of Histone Methylation in Maintenance of Genome Integrity
Mushtaq, A., Mir, U. S., Hunt, C. R., Pandita, S., Tantray, W. W., Bhat, A., PANDITA, R. K., Altaf, M., & Pandita, T. K. (2021) · Genes · doi:10.3390/genes12071000 · Cited by 42 · see citing works
Willemsen, L., Prange, K. H. M., Neele, A. E., van Roomen, C. P. A. A., Gijbels, M. J., Griffith, G. R., den Toom, M., Beckers, L., Siebeler, R., Spann, N. J., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111703 · Cited by 35 · see citing works
Liao, Q., Yang, J., Ge, S., Chai, P., Fan, J., & Jia, R. (2022) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2022.11.009 · Cited by 34 · see citing works
Sadhu, R. K., Luciano, M., Xi, W., Martinez-Torres, C., Schröder, M., Blum, C., Tarantola, M., Villa, S., Penič, S., Iglič, A., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2306818121 · Cited by 31 · see citing works
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
The role of DOT1L in the proliferation and prognosis of gastric cancer
Song, Z., Wei, Z., Wang, Q., Zhang, X., Tao, X., Wu, N., Liu, X., & Qian, J. (2020) · Bioscience Reports · doi:10.1042/bsr20193515 · Cited by 30 · see citing works
RetractedComprehensive map of ribosomal 2′-O-methylation and C/D box snoRNAs in Drosophila melanogaster
Sklias, A., Cruciani, S., Marchand, V., Spagnuolo, M., Lavergne, G., Bourguignon‐Igel, V., Brambilla, A., Dreos, R., Marygold, S. J., Novoa, E. M., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae139 · Cited by 29 · see citing works
Dysregulated Transcriptional Control in Prostate Cancer
Baumgart, S. J., Nevedomskaya, E., & Haendler, B. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20122883 · Cited by 30 · see citing works
Park, P. H., Yamamoto, T. M., Li, H., Alcivar, A. L., Xia, B., Wang, Y., Bernhardy, A. J., Turner, K. M., Kossenkov, A. V., Watson, Z. L., et al. (2019) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-17-0256 · Cited by 29 · see citing works
How Protein Methylation Regulates Steroid Receptor Function
Malbeteau, L., Pham, T. H., Eve, L., Stallcup, M. R., Poulard, C., & Romancer, M. L. (2021) · Endocrine Reviews · doi:10.1210/endrev/bnab014 · Cited by 29 · see citing works
Gut bacterial L-lysine alters metabolism and histone methylation to drive dendritic cell tolerance
Tang, Q., Fan, G., Peng, X., Sun, X., Kong, X., Zhang, L., Zhang, C., Liu, Y., Yang, J., Yu, K., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.115125 · Cited by 27 · see citing works
Rahe, D. P., & Hobert, O. (2019) · G3 Genes Genomes Genetics · doi:10.1534/g3.119.400328 · Cited by 28 · see citing works
Gibbons, G. S., Chakraborty, A., Grigsby, S. M., Umeano, A. C., Liao, C., Moukha‐Chafiq, O., Pathak, V., Mathew, B., Lee, Y., Dou, Y., et al. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.112023 · Cited by 28 · 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
Characterizing crosstalk in epigenetic signaling to understand disease physiology
Lempiäinen, J. K., & Garcia, B. A. (2023) · Biochemical Journal · doi:10.1042/bcj20220550 · Cited by 26 · see citing works
Wang, X., Wang, H., Xu, B., Jiang, D., Huang, S. H., Yu, H., Wu, Z., & Wu, Q. (2019) · Europe PMC (PubMed Central) · Cited by 26 · see citing works
Gsell, C., Richly, H., Coin, F., & Naegeli, H. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz1229 · Cited by 26 · see citing works
Lysosomes signal through the epigenome to regulate longevity across generations
Zhang, Q., Dang, W., & Wang, M. C. (2025) · Science · doi:10.1126/science.adn8754 · Cited by 24 · see citing works
Nullifying epigenetic writer DOT1L attenuates neointimal hyperplasia
Huang, Y., Urabe, G., Zhang, M., Li, J., Özer, H. G., Wang, B., Kent, K. C., & Guo, L. (2020) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2020.06.002 · Cited by 23 · see citing works
Non-canonical H3K79me2-dependent pathways promote the survival of MLL-rearranged leukemia
Richter, W. F., Shah, R. N., & Ruthenburg, A. (2020) · bioRxiv · doi:10.7554/elife.64960 · Cited by 16 · see citing works
Spangler, C. J., Yadav, S. P., Li, D., Geil, C. N., Smith, C. B., Wang, G. G., Lee, T.-H., & McGinty, R. K. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110369 · Cited by 22 · 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
Chromatin Structure and Dynamics: Focus on Neuronal Differentiation and Pathological Implication
Nothof, S., Magdinier, F., & Van‐Gils, J. (2022) · Genes · doi:10.3390/genes13040639 · Cited by 23 · see citing works
PARP1-DOT1L transcription axis drives acquired resistance to PARP inhibitor in ovarian cancer
Liu, C., Li, J., Xu, F., Chen, L., Ni, M., Wu, J., Zhao, H., Wu, Y., Li, J., Wu, X., et al. (2024) · Molecular Cancer · doi:10.1186/s12943-024-02025-8 · Cited by 22 · see citing works
Dai, S., Horton, J. R., Wilkinson, A. W., Gozani, O., Zhang, X., & Cheng, X. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012319 · Cited by 21 · see citing works
Zhao, C., Zhang, Y., & Zheng, H. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.717540 · Cited by 21 · see citing works
Weinzapfel, E. N., Fedder-Semmes, K. N., Sun, Z., & Keogh, M. (2024) · Biochemical Journal · doi:10.1042/bcj20230342 · Cited by 23 · see citing works
Werner, M., Trauner, M., Schauer, T., Ummethum, H., Márquez-Gómez, E., Lalonde, M., Lee, C. S. K., Tsirkas, I., Sajid, A., Murriello, A. C., et al. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf109 · Cited by 19 · see citing works
Han, H., Chen, G., Zhang, Y., Liu, C., Wang, Y., Zhao, D., Huang, J., & Gong, Z. (2025) · Oncogene · doi:10.1038/s41388-025-03550-6 · Cited by 20 · see citing works
Mao, Y., Sun, Y., Wu, Z., Zheng, J., Zhang, J., Zeng, J., Lee, C., & Kim, J. K. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-04431-y · Cited by 20 · see citing works
Activating the Anaphase Promoting Complex to Enhance Genomic Stability and Prolong Lifespan
Harkness, T. A. A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19071888 · Cited by 19 · see citing works
DOT1L-mediated RAP80 methylation promotes BRCA1 recruitment to elicit DNA repair
Tang, H., Lu, Y.-F., Zeng, R., Liu, C., Shu, Y., Wu, Y., Su, J., Di, L., Qian, J., Zhang, J., et al. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2320804121 · Cited by 19 · see citing works
Basu, S., Nandy, A., & Biswas, D. (2020) · Biochimica et Biophysica Acta. Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2020.194563 · Cited by 20 · see citing works
Szulik, M. W., Davis, K., Bakhtina, A. A., Azarcon, P., Bia, R. D., Horiuchi, E., & Franklin, S. (2020) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00382.2020 · Cited by 19 · see citing works
Jeusset, L. M., & McManus, K. J. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.12.007 · Cited by 18 · see citing works
BMP4 drives primed to naïve transition through PGC-like state
Yu, S.-Y., Zhou, C.-H., He, J.-P., Yao, Z., Huang, X.-N., Rong, B.-W., Zhu, H., Wang, S.-J., Chen, S.-Y., Wang, X., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30325-4 · Cited by 20 · see citing works
DOT1L bridges transcription and heterochromatin formation at mammalian pericentromeres
Malla, A. B., Yu, H., Farris, D., Kadimi, S., Lam, T. T., Cox, A. L., Smith, Z. D., & Lesch, B. J. (2023) · EMBO Reports · doi:10.15252/embr.202256492 · Cited by 18 · see citing works
Structural Basis of Nucleosome Recognition and Modulation
Sundaram, R., & Vasudevan, D. (2020) · BioEssays · doi:10.1002/bies.201900234 · Cited by 18 · see citing works
Dot1l interacts with Zc3h10 to activate Ucp1 and other thermogenic genes
Yi, D., Nguyen, H. P., Dinh, J., Viscarra, J. A., Xie, Y., Lin, F., Zhu, M., Dempersmier, J. M., Wang, Y., & Sul, H. S. (2020) · eLife · doi:10.7554/elife.59990 · Cited by 18 · see citing works
AAontology: An Ontology of Amino Acid Scales for Interpretable Machine Learning
Breimann, S., Kamp, F., Steiner, H., & Frishman, D. (2024) · Journal of Molecular Biology · doi:10.1016/j.jmb.2024.168717 · Cited by 15 · see citing works
Epigenetic Regulation of Nucleotide Excision Repair
Li, W., Jones, K., Burke, T. J., Hossain, M. A., & Lariscy, L. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.847051 · Cited by 17 · see citing works
Nunes, V. S., Moretti, N. S., da Silva, M. S., Elias, M. C., Janzen, C. J., & Schenkman, S. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118694 · Cited by 16 · see citing works
Yang, Y., Wu, C.-Y., Wang, X., Deng, J., Cao, W.-J., Tang, Y.-Z., Wan, C.-C., Chen, Z.-T., Zhan, W.-Y., Shan, H., et al. (2022) · Molecular Therapy · doi:10.1016/j.ymthe.2022.09.019 · Cited by 15 · see citing works
An emerging maestro of immune regulation: how DOT1L orchestrates the harmonies of the immune system
Kealy, L. C., Runting, J., Thiele, D., & Scheer, S. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1385319 · Cited by 15 · see citing works
A machine learning-based framework for modeling transcription elongation
Feng, P., Xiao, A., Fang, M., Wan, F., Li, S., Peng, L., Zhao, D. Y., & Zeng, J. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2007450118 · Cited by 15 · see citing works
DOT1L Regulates Thermogenic Adipocyte Differentiation and Function via Modulating H3K79 Methylation
Shuai, L., Li, B., Jiang, H., Duan, Y.-N., Yang, L., Li, J., & Li, J. (2020) · Diabetes · doi:10.2337/db20-1110 · Cited by 15 · see citing works
Chemical Control System of Epigenetics
Vaijayanthi, T., Pandian, G. N., & Sugiyama, H. (2018) · The Chemical Record · doi:10.1002/tcr.201800067 · Cited by 15 · see citing works
de Cristoforis, A. G., Ferrari, F., Clotman, F., & Vogel, T. (2020) · Molecular Brain · doi:10.1186/s13041-020-00623-3 · Cited by 15 · see citing works
Bozdemir, N., Kablan, T., Biyikli, E., Cinar, O., & Uysal, F. (2025) · Histochemistry and Cell Biology · doi:10.1007/s00418-025-02398-x · Cited by 14 · see citing works
Roles of Chromatin Remodelling and Molecular Heterogeneity in Therapy Resistance in Glioblastoma
Chen, H., Nikolić, A., Singhal, D., & Gallo, M. (2022) · Cancers · doi:10.3390/cancers14194942 · Cited by 15 · see citing works
Barsoum, M., Stenzel, A. T., Bochyńska, A., Kuo, C., Tsompanidis, A., Sayadi-Boroujeni, R., Bussmann, P., Lüscher‐Firzlaff, J., Costa, I. G., & Lüscher, B. (2022) · Scientific Reports · doi:10.1038/s41598-022-25881-0 · Cited by 15 · see citing works
Nil, Z., Deshwar, A. R., Huang, Y., Barish, S., Zhang, X., Choufani, S., Stabej, P. L. Q., Hayes, I., Yap, P., Haldeman‐Englert, C. R., et al. (2023) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2023.09.009 · Cited by 14 · see citing works
CRISPR/Cas9 system is a suitable gene targeting editing tool to filamentous fungus Monascus pilosus
Gong, Y., Li, S., Liu, Q., Chen, F., & Shao, Y. (2024) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-023-12865-x · Cited by 14 · see citing works
Sutter, P. A., Karki, S., Crawley, I., Singh, V., Bernt, K. M., Rowe, D. W., Crocker, S. J., Bayarsaihan, D., & Guzzo, R. M. (2020) · Bone · doi:10.1016/j.bone.2020.115677 · Cited by 15 · see citing works
Epigenetic Regulation of Methylation in Determining the Fate of Dental Mesenchymal Stem Cells
Zhang, H., Fu, H. E., Fang, H., Deng, Q., Huang, H., Hou, D., Wang, M., Yao, Q., Si, Q., Chen, R., et al. (2022) · Stem Cells International · doi:10.1155/2022/5015856 · Cited by 13 · see citing works
Malla, A. B., Rainsford, S. R., Smith, Z. D., & Lesch, B. J. (2023) · Development · doi:10.1242/dev.201497 · Cited by 14 · see citing works
Trans-tail regulation-mediated suppression of cryptic transcription
Choi, J., Ryoo, Z. Y., Cho, D., Lee, H., & Ryu, H. (2021) · Experimental & Molecular Medicine · doi:10.1038/s12276-021-00711-x · Cited by 13 · see citing works
Sherill-Rofe, D., Raban, O., Findlay, S., Rahat, D., Unterman, I., Samiei, A., Yasmeen, A., Kaiser, Z., Kuasne, H., Park, M., et al. (2022) · NAR Cancer · doi:10.1093/narcan/zcac013 · Cited by 12 · see citing works
- Authors
- Wood, K., Tellier, M., & Murphy, S.
- Affiliations
- University of Manchester (GB)
- University of Oxford (GB)
- Corresponding author
- Tellier, Michael
- Murphy, Shona
- Venue
- Biomolecules
- Publisher
- MDPI AG
- Published
- 2018-02-27
- Volume
- 8
- Issue
- 1
- Pages
- 11
- ISSN
- 2218-273X (ISSN-L)
- PMC
- PMC5871980
- OpenAlex
- W2791712220
- Cited by
- 209
- References
- 110
- Citations by year
- 2026: 18 · 2025: 23 · 2024: 23 · 2023: 18 · 2022: 34 · 2021: 33 · 2020: 27 · 2019: 28 · 2018: 5
- FWCI
- 2.33
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Biomolecules (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Wellcome Trust (WT106134AIA)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cancer-related gene regulation
- Keywords
- DOT1L, H3K79 methylation, histone methyltransferase, chromatin organization, transcription elongation, RNA polymerase II, DNA damage response, cell cycle checkpoints, genome stability, MLL-rearranged leukemia, histone modifications
- MeSH terms
- Animals, Histones, Humans, Histone-Lysine N-Methyltransferase, Yeasts, Histone Code, Genomic Instability, Transcription Elongation, Genetic
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review