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Volumn 23, Issue 4, 2013, Pages 489-501

Molecular mechanism of SSR128129E, an extracellularly acting, small-molecule, allosteric inhibitor of fgf receptor signaling

(25)  Herbert, Corentin a   Schieborr, Ulrich b   Saxena, Krishna b   Juraszek, Jarek c   De Smet, Frederik d,e   Alcouffe, Chantal a   Bianciotto, Marc a   Saladino, Giorgio c   Sibrac, David a   Kudlinzki, Denis b   Sreeramulu, Sridhar b   Brown, Alan f   Rigon, Patrice a   Herault, Jean Pascal a   Lassalle, Gilbert a   Blundell, Tom L f   Rousseau, Frederic e   Gils, Ann e   Schymkowitz, Joost e   Tompa, Peter g,h   more..

a SANOFI   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ANTINEOPLASTIC AGENT; EPIDERMAL GROWTH FACTOR RECEPTOR KINASE INHIBITOR; FIBROBLAST GROWTH FACTOR RECEPTOR; SSR 128129E; UNCLASSIFIED DRUG;

EID: 84876401041     PISSN: 15356108     EISSN: 18783686     Source Type: Journal    
DOI: 10.1016/j.ccr.2013.02.018     Document Type: Article
Times cited : (107)

References (33)
  • 1
    • 61649100307 scopus 로고    scopus 로고
    • The FGF family: biology, pathophysiology and therapy
    • Beenken A., Mohammadi M. The FGF family: biology, pathophysiology and therapy. Nat. Rev. Drug Discov. 2009, 8:235-253.
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 235-253
    • Beenken, A.1    Mohammadi, M.2
  • 3
    • 67649494492 scopus 로고    scopus 로고
    • Optimized molecular dynamics force fields applied to the helix-coil transition of polypeptides
    • Best R.B., Hummer G. Optimized molecular dynamics force fields applied to the helix-coil transition of polypeptides. J. Phys. Chem. B 2009, 113:9004-9015.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 9004-9015
    • Best, R.B.1    Hummer, G.2
  • 4
    • 84876355112 scopus 로고    scopus 로고
    • Inhibition of tumor angiogenesis and growth by a small-molecule multi-FGF receptor blocker with allosteric properties
    • this issue
    • Bono F., De Smet F., Herbert C., DeBock K., Georgiadou M., Fons P., Tjwa M., Alcouffe C., Ny A., Bianciotto M., et al. Inhibition of tumor angiogenesis and growth by a small-molecule multi-FGF receptor blocker with allosteric properties. Cancer Cell 2013, 23:477-488. this issue.
    • (2013) Cancer Cell , vol.23 , pp. 477-488
    • Bono, F.1    De Smet, F.2    Herbert, C.3    DeBock, K.4    Georgiadou, M.5    Fons, P.6    Tjwa, M.7    Alcouffe, C.8    Ny, A.9    Bianciotto, M.10
  • 5
    • 34247239896 scopus 로고    scopus 로고
    • NMR screening applied to the fragment-based generation of inhibitors of creatine kinase exploiting a new interaction proximate to the ATP binding site
    • Bretonnet A.S., Jochum A., Walker O., Krimm I., Goekjian P., Marcillat O., Lancelin J.M. NMR screening applied to the fragment-based generation of inhibitors of creatine kinase exploiting a new interaction proximate to the ATP binding site. J. Med. Chem. 2007, 50:1865-1875.
    • (2007) J. Med. Chem. , vol.50 , pp. 1865-1875
    • Bretonnet, A.S.1    Jochum, A.2    Walker, O.3    Krimm, I.4    Goekjian, P.5    Marcillat, O.6    Lancelin, J.M.7
  • 6
    • 0036490942 scopus 로고    scopus 로고
    • Allosteric binding sites on cell-surface receptors: novel targets for drug discovery
    • Christopoulos A. Allosteric binding sites on cell-surface receptors: novel targets for drug discovery. Nat. Rev. Drug Discov. 2002, 1:198-210.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 198-210
    • Christopoulos, A.1
  • 7
    • 58149193205 scopus 로고    scopus 로고
    • Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders
    • Conn P.J., Christopoulos A., Lindsley C.W. Allosteric modulators of GPCRs: a novel approach for the treatment of CNS disorders. Nat. Rev. Drug Discov. 2009, 8:41-54.
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 41-54
    • Conn, P.J.1    Christopoulos, A.2    Lindsley, C.W.3
  • 9
    • 34250792344 scopus 로고    scopus 로고
    • Structure induction of the T-cell receptor zeta-chain upon lipid binding investigated by NMR spectroscopy
    • Duchardt E., Sigalov A.B., Aivazian D., Stern L.J., Schwalbe H. Structure induction of the T-cell receptor zeta-chain upon lipid binding investigated by NMR spectroscopy. ChemBioChem 2007, 8:820-827.
    • (2007) ChemBioChem , vol.8 , pp. 820-827
    • Duchardt, E.1    Sigalov, A.B.2    Aivazian, D.3    Stern, L.J.4    Schwalbe, H.5
  • 13
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins
    • Hilser V.J., Thompson E.B. Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proc. Natl. Acad. Sci. USA 2007, 104:8311-8315.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 16
    • 58149299971 scopus 로고    scopus 로고
    • Metadynamics: a method to simulate rare events and reconstruct the free energy in biophysics, chemistry and material science
    • Laio A., Gervasio F.L. Metadynamics: a method to simulate rare events and reconstruct the free energy in biophysics, chemistry and material science. Rep. Prog. Phys. 2008, 71:126601.
    • (2008) Rep. Prog. Phys. , vol.71 , pp. 126601
    • Laio, A.1    Gervasio, F.L.2
  • 17
    • 84856694630 scopus 로고    scopus 로고
    • The different flexibility of c-Src and c-Abl kinases regulates the accessibility of a druggable inactive conformation
    • Lovera S., Sutto L., Boubeva R., Scapozza L., Dölker N., Gervasio F.L. The different flexibility of c-Src and c-Abl kinases regulates the accessibility of a druggable inactive conformation. J. Am. Chem. Soc. 2012, 134:2496-2499.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 2496-2499
    • Lovera, S.1    Sutto, L.2    Boubeva, R.3    Scapozza, L.4    Dölker, N.5    Gervasio, F.L.6
  • 19
    • 77955327536 scopus 로고    scopus 로고
    • Intrinsically disordered proteins are potential drug targets
    • Metallo S.J. Intrinsically disordered proteins are potential drug targets. Curr. Opin. Chem. Biol. 2010, 14:481-488.
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 481-488
    • Metallo, S.J.1
  • 20
    • 0001851781 scopus 로고    scopus 로고
    • Application of maximum likelihood methods for macromolecular refinement
    • Daresbury Laboratory, Warrington, United Kingdom
    • Murshudov G.N., Dodson E.J., Vagin A.A. Application of maximum likelihood methods for macromolecular refinement. CCP4 Study Weekend Proceedings: Macromolecular Refinement 1996, 93-104. Daresbury Laboratory, Warrington, United Kingdom.
    • (1996) CCP4 Study Weekend Proceedings: Macromolecular Refinement , pp. 93-104
    • Murshudov, G.N.1    Dodson, E.J.2    Vagin, A.A.3
  • 22
    • 79955642720 scopus 로고    scopus 로고
    • The client protein p53 adopts a molten globule-like state in the presence of Hsp90
    • Park S.J., Borin B.N., Martinez-Yamout M.A., Dyson H.J. The client protein p53 adopts a molten globule-like state in the presence of Hsp90. Nat. Struct. Mol. Biol. 2011, 18:537-541.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 537-541
    • Park, S.J.1    Borin, B.N.2    Martinez-Yamout, M.A.3    Dyson, H.J.4
  • 23
    • 0034718796 scopus 로고    scopus 로고
    • Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin
    • Pellegrini L., Burke D.F., von Delft F., Mulloy B., Blundell T.L. Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin. Nature 2000, 407:1029-1034.
    • (2000) Nature , vol.407 , pp. 1029-1034
    • Pellegrini, L.1    Burke, D.F.2    von Delft, F.3    Mulloy, B.4    Blundell, T.L.5
  • 24
    • 34249071886 scopus 로고    scopus 로고
    • A bias-exchange approach to protein folding
    • Piana S., Laio A. A bias-exchange approach to protein folding. J. Phys. Chem. B 2007, 111:4553-4559.
    • (2007) J. Phys. Chem. B , vol.111 , pp. 4553-4559
    • Piana, S.1    Laio, A.2
  • 25
    • 0033520472 scopus 로고    scopus 로고
    • Structural basis for FGF receptor dimerization and activation
    • Plotnikov A.N., Schlessinger J., Hubbard S.R., Mohammadi M. Structural basis for FGF receptor dimerization and activation. Cell 1999, 98:641-650.
    • (1999) Cell , vol.98 , pp. 641-650
    • Plotnikov, A.N.1    Schlessinger, J.2    Hubbard, S.R.3    Mohammadi, M.4
  • 26
    • 4544291665 scopus 로고    scopus 로고
    • Ligand dependent and independent internalization and nuclear translocation of fibroblast growth factor (FGF) receptor 1
    • Reilly J.F., Mizukoshi E., Maher P.A. Ligand dependent and independent internalization and nuclear translocation of fibroblast growth factor (FGF) receptor 1. DNA Cell Biol. 2004, 23:538-548.
    • (2004) DNA Cell Biol. , vol.23 , pp. 538-548
    • Reilly, J.F.1    Mizukoshi, E.2    Maher, P.A.3
  • 27
    • 84859568958 scopus 로고    scopus 로고
    • Assessing the performance of metadynamics and path variables in predicting the binding free energies of p38 inhibitors
    • Saladino G., Gauthier L., Bianciotto M., Gervasio F.L. Assessing the performance of metadynamics and path variables in predicting the binding free energies of p38 inhibitors. J. Chem. Theory Comput. 2012, 8:1165-1170.
    • (2012) J. Chem. Theory Comput. , vol.8 , pp. 1165-1170
    • Saladino, G.1    Gauthier, L.2    Bianciotto, M.3    Gervasio, F.L.4
  • 29
    • 1242307780 scopus 로고    scopus 로고
    • Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif
    • Sigalov A., Aivazian D., Stern L. Homooligomerization of the cytoplasmic domain of the T cell receptor zeta chain and of other proteins containing the immunoreceptor tyrosine-based activation motif. Biochemistry 2004, 43:2049-2061.
    • (2004) Biochemistry , vol.43 , pp. 2049-2061
    • Sigalov, A.1    Aivazian, D.2    Stern, L.3
  • 30
    • 79958044914 scopus 로고    scopus 로고
    • Unstructural biology coming of age
    • Tompa P. Unstructural biology coming of age. Curr. Opin. Struct. Biol. 2011, 21:419-425.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 419-425
    • Tompa, P.1
  • 31
    • 37749053887 scopus 로고    scopus 로고
    • Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions
    • Tompa P., Fuxreiter M. Fuzzy complexes: polymorphism and structural disorder in protein-protein interactions. Trends Biochem. Sci. 2008, 33:2-8.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 2-8
    • Tompa, P.1    Fuxreiter, M.2
  • 32
    • 70450191983 scopus 로고    scopus 로고
    • Dynamic activation of an allosteric regulatory protein
    • Tzeng S.R., Kalodimos C.G. Dynamic activation of an allosteric regulatory protein. Nature 2009, 462:368-372.
    • (2009) Nature , vol.462 , pp. 368-372
    • Tzeng, S.R.1    Kalodimos, C.G.2
  • 33
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • Zhang J., Yang P.L., Gray N.S. Targeting cancer with small molecule kinase inhibitors. Nat. Rev. Cancer 2009, 9:28-39.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.