메뉴 건너뛰기




Volumn 3, Issue 108, 2011, Pages

Neuroblastoma: Differential inhibitor sensitivity of anaplastic lymphoma kinase variants found in neuroblastoma

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CRIZOTINIB; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE INHIBITOR; ANAPLASTIC LYMPHOMA KINASE; MUTANT PROTEIN; PROTEIN KINASE INHIBITOR; PROTEIN TYROSINE KINASE; PYRAZOLE DERIVATIVE; PYRIDINE DERIVATIVE;

EID: 81055126433     PISSN: 19466234     EISSN: 19466242     Source Type: Journal    
DOI: 10.1126/scitranslmed.3002950     Document Type: Article
Times cited : (200)

References (39)
  • 1
    • 0015236227 scopus 로고
    • Special pattern of widespread neuroblastoma with a favourable prognosis
    • G. J. D'Angio, A. E. Evans, C. E. Koop, Special pattern of widespread neuroblastoma with a favourable prognosis. Lancet 1, 1046-1049 (1971).
    • (1971) Lancet , vol.1 , pp. 1046-1049
    • D'Angio, G.J.1    Evans, A.E.2    Koop, C.E.3
  • 6
    • 66949152073 scopus 로고    scopus 로고
    • Anaplastic lymphoma kinase: Signalling in development and disease
    • R. H. Palmer, E. Vernersson, C. Grabbe, B. Hallberg, Anaplastic lymphoma kinase: Signalling in development and disease. Biochem. J. 420, 345-361 (2009).
    • (2009) Biochem. J. , vol.420 , pp. 345-361
    • Palmer, R.H.1    Vernersson, E.2    Grabbe, C.3    Hallberg, B.4
  • 8
    • 58149289668 scopus 로고    scopus 로고
    • High incidence of DNA mutations and gene amplifications of the ALK gene in advanced sporadic neuroblastoma tumours
    • H. Carén, F. Abel, P. Kogner, T. Martinsson, High incidence of DNA mutations and gene amplifications of the ALK gene in advanced sporadic neuroblastoma tumours. Biochem. J. 416, 153-159 (2008).
    • (2008) Biochem. J. , vol.416 , pp. 153-159
    • Carén, H.1    Abel, F.2    Kogner, P.3    Martinsson, T.4
  • 13
    • 79959890277 scopus 로고    scopus 로고
    • Anaplastic thyroid cancers harbor novel oncogenic mutations of the ALK gene
    • A. K. Murugan, M. Xing, Anaplastic thyroid cancers harbor novel oncogenic mutations of the ALK gene. Cancer Res. 71, 4403-4411 (2011).
    • (2011) Cancer Res. , vol.71 , pp. 4403-4411
    • Murugan, A.K.1    Xing, M.2
  • 14
    • 37549059613 scopus 로고    scopus 로고
    • Cytoreductive antitumor activity of PF-2341066, a novel inhibitor of anaplastic lymphoma kinase and c-Met, in experimental models of anaplastic large-cell lymphoma
    • J. G. Christensen, H. Y. Zou, M. E. Arango, Q. Li, J. H. Lee, S. R. McDonnell, S. Yamazaki, G. R. Alton, B. Mroczkowski, G. Los, Cytoreductive antitumor activity of PF-2341066, a novel inhibitor of anaplastic lymphoma kinase and c-Met, in experimental models of anaplastic large-cell lymphoma. Mol. Cancer Ther. 6, 3314-3322 (2007).
    • (2007) Mol. Cancer Ther. , vol.6 , pp. 3314-3322
    • Christensen, J.G.1    Zou, H.Y.2    Arango, M.E.3    Li, Q.4    Lee, J.H.5    McDonnell, S.R.6    Yamazaki, S.7    Alton, G.R.8    Mroczkowski, B.9    Los, G.10
  • 21
    • 22544440004 scopus 로고    scopus 로고
    • Activation and inhibition of anaplastic lymphoma kinase receptor tyrosine kinase by monoclonal antibodies and absence of agonist activity of pleiotrophin
    • C. Moog-Lutz, J. Degoutin, J. Y. Gouzi, Y. Frobert, N. Brunet-de Carvalho, J. Bureau, C. Créminon, M. Vigny, Activation and inhibition of anaplastic lymphoma kinase receptor tyrosine kinase by monoclonal antibodies and absence of agonist activity of pleiotrophin. J. Biol. Chem. 280, 26039-26048 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 26039-26048
    • Moog-Lutz, C.1    Degoutin, J.2    Gouzi, J.Y.3    Frobert, Y.4    Brunet-de Carvalho, N.5    Bureau, J.6    Créminon, C.7    Vigny, M.8
  • 22
    • 0345686458 scopus 로고    scopus 로고
    • Template-directed assembly of receptor signaling complexes
    • A. L. Shrout, D. J. Montefusco, R. M. Weis, Template-directed assembly of receptor signaling complexes. Biochemistry 42, 13379-13385 (2003).
    • (2003) Biochemistry , vol.42 , pp. 13379-13385
    • Shrout, A.L.1    Montefusco, D.J.2    Weis, R.M.3
  • 23
    • 33745002702 scopus 로고    scopus 로고
    • An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor
    • X. Zhang, J. Gureasko, K. Shen, P. A. Cole, J. Kuriyan, An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor. Cell 125, 1137-1149 (2006).
    • (2006) Cell , vol.125 , pp. 1137-1149
    • Zhang, X.1    Gureasko, J.2    Shen, K.3    Cole, P.A.4    Kuriyan, J.5
  • 27
    • 0024450708 scopus 로고
    • Autophosphorylation activates the soluble cytoplasmic domain of the insulin receptor in an intermolecular reaction
    • M. H. Cobb, B. C. Sang, R. Gonzalez, E. Goldsmith, L. Ellis, Autophosphorylation activates the soluble cytoplasmic domain of the insulin receptor in an intermolecular reaction. J. Biol. Chem. 264, 18701-18706 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 18701-18706
    • Cobb, M.H.1    Sang, B.C.2    Gonzalez, R.3    Goldsmith, E.4    Ellis, L.5
  • 28
    • 0035185571 scopus 로고    scopus 로고
    • Structure and autoregulation of the insulin-like growth factor 1 receptor kinase
    • S. Favelyukis, J. H. Till, S. R. Hubbard, W. T. Miller, Structure and autoregulation of the insulin-like growth factor 1 receptor kinase. Nat. Struct. Biol. 8, 1058-1063 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1058-1063
    • Favelyukis, S.1    Till, J.H.2    Hubbard, S.R.3    Miller, W.T.4
  • 29
    • 33344455174 scopus 로고    scopus 로고
    • Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction
    • C. M. Furdui, E. D. Lew, J. Schlessinger, K. S. Anderson, Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction. Mol. Cell 21, 711-717 (2006).
    • (2006) Mol. Cell , vol.21 , pp. 711-717
    • Furdui, C.M.1    Lew, E.D.2    Schlessinger, J.3    Anderson, K.S.4
  • 30
    • 0031024404 scopus 로고    scopus 로고
    • Divalent ion effects and insights into the catalytic mechanism of protein tyrosine kinase Csk
    • M. R. Grace, C. T. Walsh, P. A. Cole, Divalent ion effects and insights into the catalytic mechanism of protein tyrosine kinase Csk. Biochemistry 36, 1874-1881 (1997).
    • (1997) Biochemistry , vol.36 , pp. 1874-1881
    • Grace, M.R.1    Walsh, C.T.2    Cole, P.A.3
  • 31
  • 33
    • 75349110926 scopus 로고    scopus 로고
    • Structural and mechanistic underpinnings of the differential drug sensitivity of EGFR mutations in non-small cell lung cancer
    • M. J. Eck, C. H. Yun, Structural and mechanistic underpinnings of the differential drug sensitivity of EGFR mutations in non-small cell lung cancer. Biochim. Biophys. Acta 1804, 559-566 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 559-566
    • Eck, M.J.1    Yun, C.H.2
  • 35
    • 33847323129 scopus 로고    scopus 로고
    • Epidermal growth factor receptor mutations in lung cancer
    • S. V. Sharma, D. W. Bell, J. Settleman, D. A. Haber, Epidermal growth factor receptor mutations in lung cancer. Nat. Rev. Cancer 7, 169-181 (2007).
    • (2007) Nat. Rev. Cancer , vol.7 , pp. 169-181
    • Sharma, S.V.1    Bell, D.W.2    Settleman, J.3    Haber, D.A.4
  • 36
    • 33748066632 scopus 로고    scopus 로고
    • Kinetic analysis of epidermal growth factor receptor somatic mutant proteins shows increased sensitivity to the epidermal growth factor receptor tyrosine kinase inhibitor, erlotinib
    • K. D. Carey, A. J. Garton, M. S. Romero, J. Kahler, S. Thomson, S. Ross, F. Park, J. D. Haley, N. Gibson, M. X. Sliwkowski, Kinetic analysis of epidermal growth factor receptor somatic mutant proteins shows increased sensitivity to the epidermal growth factor receptor tyrosine kinase inhibitor, erlotinib. Cancer Res. 66, 8163-8171 (2006).
    • (2006) Cancer Res. , vol.66 , pp. 8163-8171
    • Carey, K.D.1    Garton, A.J.2    Romero, M.S.3    Kahler, J.4    Thomson, S.5    Ross, S.6    Park, F.7    Haley, J.D.8    Gibson, N.9    Sliwkowski, M.X.10
  • 39
    • 81055148536 scopus 로고    scopus 로고
    • note
    • Acknowledgments: We thank members of the Lemmon, Mossé, and Maris laboratories for valuable discussions, and Pfizer for their gift of crizotinib. Funding: This work was funded in part by the U.S. Army Peer-Reviewed Medical Research Program (W81XWH-10-1-0212/3 to M.A.L. and Y.P.M.), NIH grant R01-CA140198 (Y.P.M.), the Carly Hillman Fund (Y.P.M.), the Alex's Lemonade Stand Foundation (J.M.M.), and the Abramson Family Cancer Research Institute (J.M.M.). S.C.B. was supported by an NIH Training Grant in Structural Biology (T32-GM008275). A.C.W. was supported by a fellowship from the St. Baldrick's Foundation. Author contributions: S.C.B. designed and performed in vitro studies of ALK-TKD, analyzed and interpreted the data, and drafted the manuscript. A.C.W. designed and performed cellular and in vivo experiments, analyzed and interpreted the data, and drafted the manuscript. E.A.H., J.C., L.T.B., J.S.P., K.C., Y.T., and H.Z. made important contributions to cellular and in vivo experiments and/or data analysis. E.L.C., J.G.C., J.M.M., Y.P.M., and M.A.L. guided study design, implementation, and interpretation; provided conceptual direction; and wrote the manuscript with S.C.B. and A.C.W. Competing interests: J.G.C. is an employee of Pfizer, the developer of crizotinib. J.M.M. and Y.P.M. are authors on a patent related to the discovery of ALK mutations filed by the Children's Hospital of Philadelphia (WO/2009/103061 or PCT/US2009/034288: Methods and Compositions for Identifying, Diagnosing, and Treating Neuroblastoma). The other authors declare that they have no competing interests.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.