메뉴 건너뛰기




Volumn 1804, Issue 3, 2010, Pages 454-462

Inhibitors of the Abl kinase directed at either the ATP- or myristate-binding site

Author keywords

Abl; Abl structure; Imatinib resistance; Kinase inhibitors; Myristate binders

Indexed keywords

ABELSON KINASE; ADENOSINE TRIPHOSPHATE; AMM 710; AMM 714; AP 24534; BCR ABL PROTEIN; DASATINIB; IMATINIB; MYRISTIC ACID; NILOTINIB; TADIGNA; UNCLASSIFIED DRUG;

EID: 75349104148     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.12.009     Document Type: Article
Times cited : (64)

References (47)
  • 1
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases - the major drug targets of the twenty-first century?
    • Cohen P. Protein kinases - the major drug targets of the twenty-first century?. Nat. Rev. Drug Discov. 1 (2002) 309-315
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 309-315
    • Cohen, P.1
  • 2
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang J., Yang P.L., and Gray N.S. Targeting cancer with small molecule kinase inhibitors. Nat. Rev. Cancer 9 (2009) 28-39
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 3
    • 75349097371 scopus 로고    scopus 로고
    • Protein tyrosine kinases as target for cancer and other indications
    • Fabbro D., and McCormick F. (Eds), Humana Press, Totowa NJ
    • Pearson M., Garcia-Echeverria C., and Fabbro D. Protein tyrosine kinases as target for cancer and other indications. In: Fabbro D., and McCormick F. (Eds). Protein Tyrosine Kinases: From Inhibitors to Useful Drugs (2006), Humana Press, Totowa NJ 1-31
    • (2006) Protein Tyrosine Kinases: From Inhibitors to Useful Drugs , pp. 1-31
    • Pearson, M.1    Garcia-Echeverria, C.2    Fabbro, D.3
  • 7
    • 2642558897 scopus 로고    scopus 로고
    • Characterization of a conserved structural determinant controlling protein kinase sensitivity to selective inhibitors
    • Blencke S., Zech B., Engkvist O., Greff Z., O{double acute}rfi L., Horváth L., Kéri G., Ullrich A., and Daub H. Characterization of a conserved structural determinant controlling protein kinase sensitivity to selective inhibitors. Chem. Biol. 11 (2004) 691-701
    • (2004) Chem. Biol. , vol.11 , pp. 691-701
    • Blencke, S.1    Zech, B.2    Engkvist, O.3    Greff, Z.4    Orfi, L.5    Horváth, L.6    Kéri, G.7    Ullrich, A.8    Daub, H.9
  • 8
    • 0025117392 scopus 로고
    • Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome
    • Daley G.Q., Van Etten R.A., and Baltimore D. Induction of chronic myelogenous leukemia in mice by the P210bcr/abl gene of the Philadelphia chromosome. Science 247 (1990) 824-830
    • (1990) Science , vol.247 , pp. 824-830
    • Daley, G.Q.1    Van Etten, R.A.2    Baltimore, D.3
  • 11
    • 3142676436 scopus 로고    scopus 로고
    • Overriding imatinib resistance with a novel ABL kinase inhibitor
    • Shah N.P., Tran C., Lee F.Y., Chen P., Norris D., and Sawyers C.L. Overriding imatinib resistance with a novel ABL kinase inhibitor. Science 305 (2004) 399-401
    • (2004) Science , vol.305 , pp. 399-401
    • Shah, N.P.1    Tran, C.2    Lee, F.Y.3    Chen, P.4    Norris, D.5    Sawyers, C.L.6
  • 12
    • 0035800507 scopus 로고    scopus 로고
    • Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification
    • Gorre M.E., Mohammed M., Ellwood K., Hsu N., Paquette R., Rao P.N., and Sawyers C.L. Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification. Science 293 (2001) 876-880
    • (2001) Science , vol.293 , pp. 876-880
    • Gorre, M.E.1    Mohammed, M.2    Ellwood, K.3    Hsu, N.4    Paquette, R.5    Rao, P.N.6    Sawyers, C.L.7
  • 16
    • 49649108911 scopus 로고    scopus 로고
    • Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib
    • Vajpai N., Strauss A., Fendrich G., Cowan-Jacob S.W., Manley P.W., Grzesiek S., and Jahnke W. Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib. J. Biol. Chem. 283 (2008) 18292-18302
    • (2008) J. Biol. Chem. , vol.283 , pp. 18292-18302
    • Vajpai, N.1    Strauss, A.2    Fendrich, G.3    Cowan-Jacob, S.W.4    Manley, P.W.5    Grzesiek, S.6    Jahnke, W.7
  • 22
    • 29144464371 scopus 로고    scopus 로고
    • Advances in the structural biology, design and clinical development of Bcr-Abl kinase inhibitors for the treatment of chronic myeloid leukaemia
    • Manley P.W., Cowan-Jacob S.W., and Mestan J. Advances in the structural biology, design and clinical development of Bcr-Abl kinase inhibitors for the treatment of chronic myeloid leukaemia. Biochim. Biophys. Acta 1754 (2005) 3-13
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 3-13
    • Manley, P.W.1    Cowan-Jacob, S.W.2    Mestan, J.3
  • 24
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
    • Nagar B., Bornmann W.G., Pellicena P., Schindler T., Veach D.R., Miller W.T., Clarkson B., and Kuriyan J. Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571). Cancer Res. 62 (2002) 4236-4243
    • (2002) Cancer Res. , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3    Schindler, T.4    Veach, D.R.5    Miller, W.T.6    Clarkson, B.7    Kuriyan, J.8
  • 25
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W., Harrison S.C., and Eck M.J. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385 (1997) 595-562
    • (1997) Nature , vol.385 , pp. 595-562
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 26
    • 0037459341 scopus 로고    scopus 로고
    • Variation on a Src-like theme
    • Harrison S.C. Variation on a Src-like theme. Cell 112 (2003) 737-740
    • (2003) Cell , vol.112 , pp. 737-740
    • Harrison, S.C.1
  • 27
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: the fats of the matter
    • Resh M.D. Myristylation and palmitylation of Src family members: the fats of the matter. Cell 76 (1994) 411-413
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 30
    • 0037459344 scopus 로고    scopus 로고
    • Mechanisms of autoinhibition and STI-571/imatinib resistance revealed by mutagenesis of BCR-ABL
    • Azam M., Latek R., and Daley G.Q. Mechanisms of autoinhibition and STI-571/imatinib resistance revealed by mutagenesis of BCR-ABL. Cell 112 (2003) 831-840
    • (2003) Cell , vol.112 , pp. 831-840
    • Azam, M.1    Latek, R.2    Daley, G.Q.3
  • 32
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales T.E., and Engen J.R. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25 (2006) 158-170
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 33
    • 47249138657 scopus 로고    scopus 로고
    • Current status of therapy for chronic myeloid leukemia: a review of drug development
    • Padmanabhan S., Ravella S., Curiel T., and Giles F. Current status of therapy for chronic myeloid leukemia: a review of drug development. Future Oncol. 4 (2008) 359-377
    • (2008) Future Oncol. , vol.4 , pp. 359-377
    • Padmanabhan, S.1    Ravella, S.2    Curiel, T.3    Giles, F.4
  • 34
    • 58749091073 scopus 로고    scopus 로고
    • Chaperone over-expression in Escherichia coli: apparent increased yields of soluble recombinant protein kinases are due mainly to soluble aggregates
    • Haacke A., Fendrich G., Ramage P., and Geiser M. Chaperone over-expression in Escherichia coli: apparent increased yields of soluble recombinant protein kinases are due mainly to soluble aggregates. Protein Expr. Purif. 64 (2009) 185-193
    • (2009) Protein Expr. Purif. , vol.64 , pp. 185-193
    • Haacke, A.1    Fendrich, G.2    Ramage, P.3    Geiser, M.4
  • 39
    • 0017706693 scopus 로고
    • A simple generalized equation for the analysis of multiple inhibitions of Michaelis-Menten kinetic systems
    • Chou T.-C., and Talalay P. A simple generalized equation for the analysis of multiple inhibitions of Michaelis-Menten kinetic systems. J. Biol. Chem. 252 (1977) 6438-6442
    • (1977) J. Biol. Chem. , vol.252 , pp. 6438-6442
    • Chou, T.-C.1    Talalay, P.2
  • 40
    • 0002658306 scopus 로고
    • The median-effect principle and the combination index for quantitation of synergism and antagonism
    • Chou T.-C., and Rideout D.C. (Eds), Academic Press, San Diego, Calif.
    • Chou T.-C. The median-effect principle and the combination index for quantitation of synergism and antagonism. In: Chou T.-C., and Rideout D.C. (Eds). Synergism and Antagonism in Chemotherapy (1991), Academic Press, San Diego, Calif. 61-102
    • (1991) Synergism and Antagonism in Chemotherapy , pp. 61-102
    • Chou, T.-C.1
  • 41
    • 63749101636 scopus 로고    scopus 로고
    • Structural biology contributions to tyrosine kinase drug discovery
    • Cowan-Jacob S.W., Moebitz H., and Fabbro D. Structural biology contributions to tyrosine kinase drug discovery. Curr. Opin. Cell Biol. 21 (2009) 280-28
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 280-28
    • Cowan-Jacob, S.W.1    Moebitz, H.2    Fabbro, D.3
  • 42
    • 33845197964 scopus 로고    scopus 로고
    • Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism
    • Kornev A.P., Haste N.M., Taylor S.S., and Eyck L.F. Surface comparison of active and inactive protein kinases identifies a conserved activation mechanism. Proc. Natl. Acad. Sci. USA 103 (2006) 17783-17788
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 17783-17788
    • Kornev, A.P.1    Haste, N.M.2    Taylor, S.S.3    Eyck, L.F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.