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Catalytic site remodelling of the DOT1L methyltransferase by selective inhibitors
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Cites
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Arrowsmith, C. H., Bountra, C., Fish, P. V., Lee, K., & Schapira, M. (2012) · Nature Reviews Drug Discovery · doi:10.1038/nrd3674 · Cited by 1,327
Self-citationMLL translocations, histone modifications and leukaemia stem-cell development
Krivtsov, A. V., & Armstrong, S. A. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2253 · Cited by 1,249
Covalent histone modifications — miswritten, misinterpreted and mis-erased in human cancers
Chi, P., Allis, C. D., & Wang, G. G. (2010) · Nature Reviews Cancer · doi:10.1038/nrc2876 · Cited by 1,099
Selective Killing of Mixed Lineage Leukemia Cells by a Potent Small-Molecule DOT1L Inhibitor
Daigle, S. R., Olhava, E. J., Therkelsen, C. A., Majer, C. R., Sneeringer, C. J., Song, J., Johnston, L. D., Scott, M. P., Smith, J. J., Xiao, Y., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.06.009 · Cited by 923
MLL-Rearranged Leukemia Is Dependent on Aberrant H3K79 Methylation by DOT1L
Bernt, K. M., Zhu, N., Sinha, A. U., Vempati, S., Faber, J., Krivtsov, A. V., Feng, Z., Punt, N., Daigle, A., Bullinger, L., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.06.010 · Cited by 870
Methylation of H3-Lysine 79 Is Mediated by a New Family of HMTases without a SET Domain
Feng, Q., Wang, H., Ng, H. H., Erdjument-Bromage, H., Tempst, P., Struhl, K., & Zhang, Y. (2002) · Current Biology · doi:10.1016/s0960-9822(02)00901-6 · Cited by 865
Hydrogen exchange mass spectrometry for the analysis of protein dynamics
Wales, T. E., & Engen, J. R. (2006) · Mass Spectrometry Reviews · doi:10.1002/mas.20064 · Cited by 862
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Onder, T. T., Kara, N., Cherry, A., Sinha, A. U., Zhu, N., Bernt, K. M., Cahan, P., Mancarci, B. O., Unternaehrer, J., Gupta, P. B., et al. (2012) · Nature · doi:10.1038/nature10953 · Cited by 634
The diverse functions of Dot1 and H3K79 methylation
Nguyen, A. T., & Zhang, Y. (2011) · Genes & Development · doi:10.1101/gad.2057811 · Cited by 597
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
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Steger, D. J., Lefterova, M. I., Ying, L., Stonestrom, A. J., Schupp, M., Zhuo, D., Vakoc, A. L., Kim, J.-E., Chen, J., Lazar, M. A., et al. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.02076-07 · Cited by 497
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Grembecka, J., He, S., Shi, A., Purohit, T., Muntean, A. G., Sorenson, R. J., Showalter, H. D., Murai, M. J., Belcher, A. M., Hartley, T., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.773 · Cited by 462
Protein methyltransferases as a target class for drug discovery
Copeland, R. A., Solomon, M. E., & Richon, V. M. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2974 · Cited by 460
Min, J., Feng, Q., Li, Z., Zhang, Y., & Xu, R.-M. (2003) · Cell · doi:10.1016/s0092-8674(03)00114-4 · Cited by 428
Frye, S. V. (2010) · Nature Chemical Biology · doi:10.1038/nchembio.296 · Cited by 375
Modeling the Initiation and Progression of Human Acute Leukemia in Mice
Barabé, F., Kennedy, J. A., Hope, K. J., & Dick, J. E. (2007) · Science · doi:10.1126/science.1139851 · Cited by 349
Self-citationThe Pathogenesis of Mixed-Lineage Leukemia
Muntean, A. G., & Hess, J. L. (2012) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-011811-132434 · Cited by 344
Linking H3K79 trimethylation to Wnt signaling through a novel Dot1-containing complex (DotCom)
Mohan, M., Herz, H.-M., Takahashi, Y.-H., Lin, C., Lai, K. C., Zhang, Y., Washburn, M. P., Florens, L., & Shilatifard, A. (2010) · Genes & Development · doi:10.1101/gad.1898410 · Cited by 313
DOT1L, the H3K79 methyltransferase, is required for MLL-AF9–mediated leukemogenesis
Nguyen, A. T., Taranova, O., He, J., & Zhang, Y. (2011) · Blood · doi:10.1182/blood-2011-02-334359 · Cited by 275
Conformational Adaptation in Drug–Target Interactions and Residence Time
Copeland, R. A. (2011) · Future Medicinal Chemistry · doi:10.4155/fmc.11.112 · Cited by 196
Chemogenetic Analysis of Human Protein Methyltransferases
Richon, V. M., Johnston, D., Sneeringer, C. J., Jin, L., Majer, C. R., Elliston, K., Jerva, L. F., Scott, M. P., & Copeland, R. A. (2011) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2011.01135.x · Cited by 188
Functional insights from structures of coactivator‐associated arginine methyltransferase 1 domains
Troffer‐Charlier, N., Cura, V., Hassenboehler, P., Moras, D., & Cavarelli, J. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601855 · Cited by 161
Yao, Y., Chen, P., Diao, J., Cheng, G., Deng, L., Anglin, J. L., Prasad, B. V. V., & Song, Y. (2011) · Journal of the American Chemical Society · doi:10.1021/ja206312b · Cited by 160
Basavapathruni, A., Jin, L., Daigle, S. R., Majer, C. R., Therkelsen, C. A., Wigle, T. J., Kuntz, K. W., Chesworth, R., Pollock, R. M., Scott, M. P., et al. (2012) · Chemical Biology & Drug Design · doi:10.1111/cbdd.12050 · Cited by 147
Warner, J. K., Wang, J. C. Y., Takenaka, K., Doulatov, S. R., McKenzie, J. L., Harrington, L. A., & Dick, J. E. (2005) · Leukemia · doi:10.1038/sj.leu.2403917 · Cited by 118
Self-citationStructural Chemistry of Human SET Domain Protein Methyltransferases
Schapira, M. (2011) · Current Chemical Genomics · doi:10.2174/1875397301005010085 · Cited by 110
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Campágna‐Slater, V., Mok, M. W., Nguyen, K. T., Fehér, M., Najmanovich, R., & Schapira, M. (2011) · Journal of Chemical Information and Modeling · doi:10.1021/ci100479z · Cited by 82
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Metadata
- Authors
- Yu, W., Chory, E. J., Wernimont, A. K., Tempel, W., Scopton, A., Federation, A., Marineau, J. J., Qi, J., Barsyte-Lovejoy, D., Yi, J., Marcellus, R., Iacob, R. E., Engen, J. R., Griffin, C., Aman, A., Wienholds, E., Li, F., Pineda, J., Estiu, G., Shatseva, T., Hajian, T., Al-awar, R., Dick, J. E., Vedadi, M., Brown, P. J., Arrowsmith, C. H., Bradner, J. E., & Schapira, M.
- Venue
- Nature Communications
- Published
- 2012-12-18
- Volume
- 3
- Issue
- 1
- Pages
- 1288-1288
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2005829971
- Cited by
- 281
- References
- 28
- FWCI
- 9.64
- Type
- journal article
- Language
- en
- Open access
- bronze
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