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3.7: Appendix References

  • Page ID
    1.  Hochhaus, A. & La Rosee, P. Imatinib therapy in chronic myelogenous leukemia: strategies to avoid and overcome resistance. Leukemia 18, 1321-1331 (2004).
    2. Weisberg, E., Manley, P. W., Cowan-Jacob, S. W., Hochhaus, A. & Griffin, J. D. Second generation inhibitors of BCR-ABL for the treatment of imatinib-resistant chronic myeloid leukaemia. Nature Reviews Cancer 7, 345-356 (2007).
    3. Druker, B. J. & Lydon, N. B. Lessons learned from the development of an Abl tyrosine kinase inhibitor for chronic myelogenous leukemia. J. Clin. Invest. 105, 3-7 (2000).
    4. Shah, N. P. et al. Overriding Imatinib Resistance with a Novel ABL Kinase Inhibitor. Science 305, 399-401 (2004).
    5. Tokarski, J. S. et al. The Structure of Dasatinib (BMS-354825) Bound to Activated ABL Kinase Domain Elucidates Its Inhibatory Activity against Imatinib-Resistant ABL Mutants. Cancer Res. 66, 5790-5797 (2006).
    6. 6. Wisniewski, D. et al. Characterization of potent inhibitors of the Bcr-Abl and the c-kit receptor tyrosine kinases. Cancer Res. 62, 4244-4255 (2002).
    7. La Rosee, P., Corbin, A. S., Stoffregen, E. P., Deininger, M. W. & Druker, B. J. Activity of the Bcr-Abl kinase inhibitor PD180970 against clinically relevant BcrAbl isoforms that cause resistance to imatinib mesylate (Gleevec, STI571). Cancer Res. 62, 7149-7153 (2002).
    8. Carter, T. A. et al. Inhibition of drug-resistant mutants of ABL, KIT, and EGF receptor kinases. Proc. Natl. Acad. Sci. U. S. A. 102, 11011-11016 (2005).
    9. Harrington, E. A. et al. VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo. Nature Medicine (New York, NY, United States) 10, 262-267 (2004).
    10. Young, M. A. et al. Structure of the Kinase Domain of an Imatinib-Resistant Abl Mutant in Complex with the Aurora Kinase Inhibitor VX-680. Cancer Res. 66, 1007-1014 (2006).
    11. Brasher, B. B. & Van Etten, R. A. c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the Src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines. J. Biol. Chem. 275, 35631-35637 (2000).
    12. Barker, S. et al. Characterization of pp60c-src Tyrosine Kinase Activities Using a Continuous Assay: Autoactivation of the Enzyme Is an Intermolecular Autophosphorylation Process. Biochemistry 34, 14843-51 (1995).
    13. Seeliger, M. A. et al. High yield bacterial expression of active c-Abl and c-Src tyrosine kinases. Protein Sci. 14, 3135-3139 (2005).