SEARCH

SEARCH BY CITATION

References

  • 1
    Bannister A.J., Kouzarides T. (2011) Regulation of chromatin by histone modifications. Cell Res;21:381395.
  • 2
    Copeland R.A., Solomon M.E., Richon V.M. (2009) Protein methyltransferases as a target class for drug discovery. Nat Rev Drug Discov;8:724732 [10.1038/nrd2974].
  • 3
    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) Chemogenetic analysis of human protein methyltransferases. Chem Biol Drug Des;78:199210.
  • 4
    Copeland R.A. (2011) Protein methyltransferase inhibitors as personalized cancer therapeutics. Drug Discov Today Ther Strateg; http://dx.doi.org/10.1016/j.ddstr.2011.08.001 .
  • 5
    Krivtsov A.V., Armstrong S.A. (2007) MLL translocations, histone modifications and leukaemia stem-cell development. Nat Rev Cancer;7:823833.
  • 6
    Okada Y., Feng Q., Lin Y., Jiang Q., Li Y., Coffield V.M., Su L., Xu G., Zhang Y. (2005) hDOT1L links histone methylation to leukemogenesis. Cell [Research Support, Non-U.S. Gov’t Research Support, U.S. Gov’t, P.H.S.];121:167178.
  • 7
    Milne T.A., Briggs S.D., Brock H.W., Martin M.E., Gibbs D., Allis C.D., Hess J.L. (2002) MLL targets SET domain methyltransferase activity to hox gene promoters. Mol Cell;10:11071117.
  • 8
    Krivtsov A.V., Feng Z., Lemieux M.E., Faber J., Vempati S., Sinha A.U., Xia X., Jesneck J., Bracken A.P., Silverman L.B., Kutok J.L., Kung A.L., Armstrong S.A. (2008) H3K79 methylation profiles define murine and human MLL-AF4 leukemias. Cancer Cell;14:355368.
  • 9
    Daigle S.R., Olhava E.J., Therkelsen C.A., Majer C.R., Sneeringer C.J., Song J., Johnston L.D. (2011) Selective killing of mixed lineage leukemia cells by a potent small-molecule DOT1L inhibitor. Cancer Cell;20:5365.
  • 10
    Bernt K.M., Zhu N., Sinha A.U., Vempati S., Faber J., Krivtsov A.V., Feng Z., Punt N., Daigle A., Bullinger L., Pollock R.M., Richon V.M., Kung A.L., Armstrong S.A. (2011) MLL-rearranged leukemia is dependent on aberrant H3K79 methylation by DOT1L. Cancer Cell;20:6678.
  • 11
    Copeland R.A. (2000) Enzymes: A Practical Introduction to Structure, Mechanism and Data Analysis, 2nd edn. New York: Wiley.
  • 12
    Copeland R.A. (2005) Evaluation of enzyme inhibitors in drug discovery. A Guide for Medicinal Chemists and Pharmacologists. New York: Wiley.
  • 13
    Heras B., Martin J.L. (2005) Post-crystallization treatments for improving diffraction quality of protein crystals. Acta Crystallogr D Biol Crystallogr;61(Pt 9):11731180.
  • 14
    Lusty C.J. (1999) A gentle vapor-diffusion technique for cross-linking of protein crystals for cryocrystallography. J Appl Crystallogr;32:106112.
  • 15
    Otwinowski Z., Minor W. (1997) Processing of X-ray diffraction data collected in oscillation mode. In: Carter C.W. Jr, editor. Methods in Enzymology. San Diego: Academic Press; p. 307326.
  • 16
    McCoy A.J., Grosse-Kunstleve R.W., Adams P.D., Winn M.D., Storoni L.C., Read R.J. (2007) Phaser crystallographic software. J Appl Crystallogr;40:658674.
  • 17
    Vagin A.A., Steiner R.A., Lebedev A.A., Potterton L., McNicholas S., Long F., Murshudov G.N. (2004) REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use. Acta Crystallogr D Biol Crystallogr;60(Pt 12 Pt 1):21842195.
  • 18
    Emsley P., Cowtan K. (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr;60(Pt 12 Pt 1):21262132.
  • 19
    Yao Y., Chen P., Diao J., Cheng G., Deng L., Anglin J.L., Prasad B.V., Song Y. (2011) Selective inhibitors of histone methyltransferase DOT1L: design, synthesis, and crystallographic studies. J Am Chem Soc [Research Support, Non-U.S. Gov’t];133:1674616749.
  • 20
    Copeland R.A., Gontarek R., Luo L. (2009) Enzyme Inhibitors: Biostructure-based and mechanism-based design. In: Maden U., Krogsgaard-Larsen P., Stromgaard K., editors. Textbook of Drug Design and Discovery, 4th edn. New York: CRC Press; p. 173188.
  • 21
    Min J., Feng Q., Li Z., Zhang Y., Xu R.M. (2003) Structure of the catalytic domain of human DOT1L, a non-SET domain nucleosomal histone methyltransferase. Cell;112:711723.
  • 22
    Frederiks F., Tzouros M., Oudgenoeg G., van Welsem T., Fornerod M., Krijgsveld J., van Leeuwen F. (2008) Nonprocessive methylation by Dot1 leads to functional redundancy of histone H3K79 methylation states. Nat Struct Mol Biol;15:550557.
  • 23
    Fersht A.R., editor (1999) Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding. New York: Freeman.
  • 24
    Copeland R.A. (2011) Conformational adaptation in drug-target interactions and residence time. Future Med Chem;3:14911501.
  • 25
    Copeland R.A., Pompliano D.L., Meek T.D. (2006) Drug-target residence time and its implications for lead optimization. Nat Rev Drug Discov;5:730739.
  • 26
    Marcinkeviciene J., Kopcho L.M., Yang T., Copeland R.A., Glass B.M., Combs A.P., Falahatpisheh N., Thompson L. (2002) Novel inhibition of porcine pepsin by a substituted piperidine. Preference for one of the enzyme conformers. J Biol Chem;277:2867728682.
  • 27
    Ross M.E., Mahfouz R., Onciu M., Liu H.C., Zhou X., Song G. Shurtleff S.A. (2004) Gene expression profiling of pediatric acute myelogenous leukemia. Blood;104:36793687.