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Volumn 424, Issue 2, 2009, Pages 179-189

Mapping the ligand-binding pocket of integrin α5β1 using a gain-of-function approach

Author keywords

Antagonist; Fibronectin; Gain of function; Integrin; RGD motif; Synergy region

Indexed keywords

ARG GLY ASPS; CYCLIC PEPTIDES; EXTRACELLULAR MATRIX PROTEIN; GAIN-OF-FUNCTION; GAIN-OF-FUNCTION ANALYSIS; HOMOLOGY MODELS; HUMAN FIBRONECTIN; IN-VIVO; INTEGRINS; LIGAND BINDING; LOOP RESIDUES; RGD MOTIF; SYNERGY SEQUENCE; THERAPEUTIC POTENTIALS; UPPER SURFACE; ZEBRAFISH;

EID: 70450203639     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20090992     Document Type: Article
Times cited : (22)

References (56)
  • 2
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signalling machines
    • Hynes, R. O. (2002) Integrins: bidirectional, allosteric signalling machines. Cell 110, 673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 3
    • 62149091091 scopus 로고    scopus 로고
    • Signal co-operation between integrins and other receptor systems
    • Streuli, C. H. and Akhtar, N. (2009) Signal co-operation between integrins and other receptor systems. Biochem. J. 418, 491-506
    • (2009) Biochem. J , vol.418 , pp. 491-506
    • Streuli, C.H.1    Akhtar, N.2
  • 4
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher, M. D. and Ruoslahti, E. (1984) Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 309, 30-33
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 5
    • 0027971378 scopus 로고
    • The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function
    • Aota, S., Nomizu, M. and Yamada, K. M. (1994) The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J. Biol. Chem. 269, 24756-24761
    • (1994) J. Biol. Chem , vol.269 , pp. 24756-24761
    • Aota, S.1    Nomizu, M.2    Yamada, K.M.3
  • 6
    • 0030798854 scopus 로고    scopus 로고
    • Defining the topology of integrin α5β1-fibronectin interactions using inhibitory anti-α5 and anti-β1 monoclonal antibodies: Evidence that the synergy sequence of fibronectin is recognized by the amino-terminal repeats of the α5 subunit
    • Mould, A. P., Askari, J. A., Aota, S., Yamada, K. M., Irie, A., Takada, Y., Mardon, H. J. and Humphries, M. J. (1997) Defining the topology of integrin α5β1-fibronectin interactions using inhibitory anti-α5 and anti-β1 monoclonal antibodies: evidence that the synergy sequence of fibronectin is recognized by the amino-terminal repeats of the α5 subunit. J. Biol. Chem. 272, 17283-17292
    • (1997) J. Biol. Chem , vol.272 , pp. 17283-17292
    • Mould, A.P.1    Askari, J.A.2    Aota, S.3    Yamada, K.M.4    Irie, A.5    Takada, Y.6    Mardon, H.J.7    Humphries, M.J.8
  • 7
    • 0034678405 scopus 로고    scopus 로고
    • Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis
    • Redick, S. D., Settles, D. L., Briscoe, G. and Erickson, H. P. (2000) Defining fibronectin's cell adhesion synergy site by site-directed mutagenesis. J. Cell Biol. 149, 521-527
    • (2000) J. Cell Biol , vol.149 , pp. 521-527
    • Redick, S.D.1    Settles, D.L.2    Briscoe, G.3    Erickson, H.P.4
  • 8
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy, D. J., Aukhil, I. and Erickson, H. P. (1996) 2.0 Å crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 84, 155-164
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 9
    • 58549106104 scopus 로고    scopus 로고
    • Caveolin-1 regulates glioblastoma aggressiveness through the control of α5β1 integrin expression and modulates glioblastoma responsiveness to SJ749, an α5β1 integrin antagonist
    • Martin, S., Cosset, E. C., Terrand, J., Maglott, A., Takeda, K. and Dontenwill, M. (2009) Caveolin-1 regulates glioblastoma aggressiveness through the control of α5β1 integrin expression and modulates glioblastoma responsiveness to SJ749, an α5β1 integrin antagonist. Biochim Biophys Acta. 1793, 354-367
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 354-367
    • Martin, S.1    Cosset, E.C.2    Terrand, J.3    Maglott, A.4    Takeda, K.5    Dontenwill, M.6
  • 11
    • 42049107076 scopus 로고    scopus 로고
    • Loss of E-cadherin promotes ovarian cancer metastasis via α5 integrin, which is a therapeutic target
    • Yamada, S. D. and Lengyel, E. (2008) Loss of E-cadherin promotes ovarian cancer metastasis via α5 integrin, which is a therapeutic target. Cancer Res. 68, 2329-2339
    • (2008) Cancer Res , vol.68 , pp. 2329-2339
    • Yamada, S.D.1    Lengyel, E.2
  • 12
    • 0033843942 scopus 로고    scopus 로고
    • Regulation of angiogenesis in vivo by ligation of integrin α5β1 with the central cell-binding domain of fibronectin
    • Kim, S., Bell, K., Mousa, S. A. and Varner, J. A. (2000) Regulation of angiogenesis in vivo by ligation of integrin α5β1 with the central cell-binding domain of fibronectin. Am. J. Pathol. 156, 1345-1362
    • (2000) Am. J. Pathol , vol.156 , pp. 1345-1362
    • Kim, S.1    Bell, K.2    Mousa, S.A.3    Varner, J.A.4
  • 14
    • 33745137492 scopus 로고    scopus 로고
    • Suppression and regression of choroidal neovascularization by systemic administration of an α5β1 integrin antagonist
    • Umeda, N., Kachi, S., Akiyama, H., Zahn, G., Vossmeyer, D., Stragies, R. and Campochiaro, P. A. (2006) Suppression and regression of choroidal neovascularization by systemic administration of an α5β1 integrin antagonist. Mol. Pharmacol. 69, 1820-1828
    • (2006) Mol. Pharmacol , vol.69 , pp. 1820-1828
    • Umeda, N.1    Kachi, S.2    Akiyama, H.3    Zahn, G.4    Vossmeyer, D.5    Stragies, R.6    Campochiaro, P.A.7
  • 15
    • 34548829958 scopus 로고    scopus 로고
    • Modulation of hypoxia induced neovascularization by JSM6427, an integrin α5β1 inhibiting molecule
    • Maier, A. K., Kociok, N., Zahn, G., Vossmeyer, D., Stragies, R., Muether, P. S. and Joussen, A. M. (2007) Modulation of hypoxia induced neovascularization by JSM6427, an integrin α5β1 inhibiting molecule. Curr. Eye Res. 32, 801-812
    • (2007) Curr. Eye Res , vol.32 , pp. 801-812
    • Maier, A.K.1    Kociok, N.2    Zahn, G.3    Vossmeyer, D.4    Stragies, R.5    Muether, P.S.6    Joussen, A.M.7
  • 17
    • 34547687853 scopus 로고    scopus 로고
    • Selective inhibition of lymphangiogenesis by integrin α5 blockade: Functional role of integrins in lymphangiogenesis
    • Dietrich T., Onderka J., Bock F., Kruse F. E., Vossmeyer D., Stragies R., Zahn G., Cursiefen C. (2007) Selective inhibition of lymphangiogenesis by integrin α5 blockade: functional role of integrins in lymphangiogenesis. Am. J. Pathol. 171, 361-372
    • (2007) Am. J. Pathol , vol.171 , pp. 361-372
    • Dietrich, T.1    Onderka, J.2    Bock, F.3    Kruse, F.E.4    Vossmeyer, D.5    Stragies, R.6    Zahn, G.7    Cursiefen, C.8
  • 18
    • 70350731216 scopus 로고    scopus 로고
    • Preclinical evaluation of the novel small molecule integrin α5β1 inhibitor JSM6427 in monkey and rabbit models of choroidal neovascularization
    • in the press
    • Zahn G., Vossmeyer, D., Stragies, R., Wills, M., Wong C. G., Loeffler, K. U., Adamis, A. P. and Knolle, J. (2009) Preclinical evaluation of the novel small molecule integrin α5β1 inhibitor JSM6427 in monkey and rabbit models of choroidal neovascularization. Arch. Ophthalmol., in the press
    • (2009) Arch. Ophthalmol
    • Zahn, G.1    Vossmeyer, D.2    Stragies, R.3    Wills, M.4    Wong, C.G.5    Loeffler, K.U.6    Adamis, A.P.7    Knolle, J.8
  • 20
    • 59449094255 scopus 로고    scopus 로고
    • Volociximab, a chimeric monoclonal antibody that specifically binds α5β1 integrin: A phase I, pharmacokinetic, and biological correlative study
    • Ricart, A. D., Tolcher, A. W., Liu, G., Holen, K., Schwartz, G., Albertini, M., Weiss, G., Yazji, S., Ng, C. and Wilding, G. (2008) Volociximab, a chimeric monoclonal antibody that specifically binds α5β1 integrin: a phase I, pharmacokinetic, and biological correlative study. Clin. Cancer Res. 14, 7924-7929
    • (2008) Clin. Cancer Res , vol.14 , pp. 7924-7929
    • Ricart, A.D.1    Tolcher, A.W.2    Liu, G.3    Holen, K.4    Schwartz, G.5    Albertini, M.6    Weiss, G.7    Yazji, S.8    Ng, C.9    Wilding, G.10
  • 21
    • 0037023363 scopus 로고    scopus 로고
    • Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
    • Xiong, J.-P., Stehle, T., Zhang, R., Joachimiak, A., Frech, M., Goodman, S. and Arnaout, M. A. (2002) Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand. Science 296, 151-155
    • (2002) Science , vol.296 , pp. 151-155
    • Xiong, J.-P.1    Stehle, T.2    Zhang, R.3    Joachimiak, A.4    Frech, M.5    Goodman, S.6    Arnaout, M.A.7
  • 22
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • Xiao, T., Takagi, J., Coller, B. S., Wang, J. H. and Springer, T. A. (2004) Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature 432, 59-67
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    Coller, B.S.3    Wang, J.H.4    Springer, T.A.5
  • 23
    • 50249106884 scopus 로고    scopus 로고
    • Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin αIIbβ3
    • Springer, T. A., Zhu, J. and Xiao, T. (2008) Structural basis for distinctive recognition of fibrinogen γC peptide by the platelet integrin αIIbβ3. J. Cell Biol. 182, 791-800
    • (2008) J. Cell Biol , vol.182 , pp. 791-800
    • Springer, T.A.1    Zhu, J.2    Xiao, T.3
  • 24
    • 34250792823 scopus 로고    scopus 로고
    • Probing integrin selectivity: Rational design of highly active and selective ligands for the α5β1 and αvβ3 integrin receptor
    • Heckmann D., Meyer A., Marinelli, L., Zahn, G., Stragies, R. and Kessler, H. (2007) Probing integrin selectivity: rational design of highly active and selective ligands for the α5β1 and αvβ3 integrin receptor. Angew. Chem. Int. Ed. Engl. 46, 3571-357
    • (2007) Angew. Chem. Int. Ed. Engl , vol.46 , pp. 3571-4357
    • Heckmann, D.1    Meyer, A.2    Marinelli, L.3    Zahn, G.4    Stragies, R.5    Kessler, H.6
  • 25
    • 21244467582 scopus 로고    scopus 로고
    • Ligand binding analysis for human α5β1 integrin: Strategies for designing new α5β1 integrin antagonists
    • Marinelli, L., Meyer, A., Heckmann, D., Lavecchia, A., Novellino, E. and Kessler, H. (2005) Ligand binding analysis for human α5β1 integrin: strategies for designing new α5β1 integrin antagonists. J. Med. Chem. 48, 4204-4207
    • (2005) J. Med. Chem , vol.48 , pp. 4204-4207
    • Marinelli, L.1    Meyer, A.2    Heckmann, D.3    Lavecchia, A.4    Novellino, E.5    Kessler, H.6
  • 26
    • 0027976103 scopus 로고
    • Isolation of a highly specific ligand for the α5β1 integrin from a phage display library
    • Koivunen, E., Wang, B. and Ruoslahti, E. (1994) Isolation of a highly specific ligand for the α5β1 integrin from a phage display library. J. Cell Biol. 124, 373-380
    • (1994) J. Cell Biol , vol.124 , pp. 373-380
    • Koivunen, E.1    Wang, B.2    Ruoslahti, E.3
  • 27
    • 0028899525 scopus 로고
    • Phage libraries displaying cyclic peptides with different ring sizes: Ligand specificities of the RGD-directed integrins
    • Koivunen, E., Wang, B. and Ruoslahti, E. (1995) Phage libraries displaying cyclic peptides with different ring sizes: ligand specificities of the RGD-directed integrins. Biotechnology 13, 265-270
    • (1995) Biotechnology , vol.13 , pp. 265-270
    • Koivunen, E.1    Wang, B.2    Ruoslahti, E.3
  • 28
    • 0032475978 scopus 로고    scopus 로고
    • Identification of amino acid residues that form part of the ligand-binding pocket of integrin α5β1
    • Mould, A. P., Burrows, L. and Humphries, M. J. (1998) Identification of amino acid residues that form part of the ligand-binding pocket of integrin α5β1. J. Biol. Chem. 273, 25664-25672
    • (1998) J. Biol. Chem , vol.273 , pp. 25664-25672
    • Mould, A.P.1    Burrows, L.2    Humphries, M.J.3
  • 30
    • 0034617222 scopus 로고    scopus 로고
    • Molecular basis of ligand recognition by integrin α5β1. II. Specificity of Arg-Gly-Asp binding is determined by Trp157 of the α subunit
    • Humphries, J. D., Askari, J. A., Zhang, X-P., Takada, Y., Humphries, M. J. and Mould, A. P. (2000) Molecular basis of ligand recognition by integrin α5β1. II. Specificity of Arg-Gly-Asp binding is determined by Trp157 of the α subunit. J. Biol. Chem. 275, 20337-20345
    • (2000) J. Biol. Chem , vol.275 , pp. 20337-20345
    • Humphries, J.D.1    Askari, J.A.2    Zhang, X.-P.3    Takada, Y.4    Humphries, M.J.5    Mould, A.P.6
  • 32
    • 0141625303 scopus 로고    scopus 로고
    • Structure of integrin α5β1 in complex with fibronectin
    • Takagi, J., Strokovich, K., Springer, T. A. and Walz, T. (2003) Structure of integrin α5β1 in complex with fibronectin. EMBO J. 22, 4607-4615
    • (2003) EMBO J , vol.22 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 35
    • 0035881279 scopus 로고    scopus 로고
    • Identification and characterization of a novel fibronectin in zebrafish
    • Zhao, Q., Liu, X. and Collodi, P. (2001) Identification and characterization of a novel fibronectin in zebrafish. Exp. Cell Res. 268, 211-219
    • (2001) Exp. Cell Res , vol.268 , pp. 211-219
    • Zhao, Q.1    Liu, X.2    Collodi, P.3
  • 36
    • 0013307787 scopus 로고    scopus 로고
    • Conformational changes in the integrin βA domain provide a mechanism for signal transduction via hybrid domain movement
    • Mould, A. P., Barton, S. J., Askari, J. A., McEwan, P. A., Buckley, P. A., Craig, S. E. and Humphries, M. J. (2003) Conformational changes in the integrin βA domain provide a mechanism for signal transduction via hybrid domain movement. J. Biol. Chem. 278, 17028-17035
    • (2003) J. Biol. Chem , vol.278 , pp. 17028-17035
    • Mould, A.P.1    Barton, S.J.2    Askari, J.A.3    McEwan, P.A.4    Buckley, P.A.5    Craig, S.E.6    Humphries, M.J.7
  • 38
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S. and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 40
    • 20044361821 scopus 로고    scopus 로고
    • Evidence that monoclonal antibodies directed against the integrin β subunit plexin/semaphorin/integrin domain stimulate function by inducing receptor extension
    • Mould, A. P., Travis, M. A., Barton, S. J., Hamilton, J. A., Askari, J. A., Craig, S. E., Macdonald, P. R., Kammerer, R. A., Buckley, P. A. and Humphries, M. J. (2005) Evidence that monoclonal antibodies directed against the integrin β subunit plexin/semaphorin/integrin domain stimulate function by inducing receptor extension. J. Biol. Chem. 280, 4238-4246
    • (2005) J. Biol. Chem , vol.280 , pp. 4238-4246
    • Mould, A.P.1    Travis, M.A.2    Barton, S.J.3    Hamilton, J.A.4    Askari, J.A.5    Craig, S.E.6    Macdonald, P.R.7    Kammerer, R.A.8    Buckley, P.A.9    Humphries, M.J.10
  • 41
    • 33845922350 scopus 로고    scopus 로고
    • N-glycosylation of the β-propeller domain of the integrin α5 subunit is essential for α5α1 heterodimerization, expression on the cell surface, and its biological function
    • Isaji, T., Sato, Y., Zhao, Y., Miyoshi, E., Wada, Y., Taniguchi, N. and Gu, J. (2006) N-glycosylation of the β-propeller domain of the integrin α5 subunit is essential for α5α1 heterodimerization, expression on the cell surface, and its biological function. J. Biol. Chem. 281, 33258-33267
    • (2006) J. Biol. Chem , vol.281 , pp. 33258-33267
    • Isaji, T.1    Sato, Y.2    Zhao, Y.3    Miyoshi, E.4    Wada, Y.5    Taniguchi, N.6    Gu, J.7
  • 42
    • 0028805249 scopus 로고
    • Critical amino acid residues for ligand binding are clustered in a predicted β-turn of the third N-terminal repeat in the integrin α4 and α5 subunits
    • Irie, A., Kamata, T., Puzon-McLaughlin, W. and Takada, Y. (1995) Critical amino acid residues for ligand binding are clustered in a predicted β-turn of the third N-terminal repeat in the integrin α4 and α5 subunits. EMBO J. 15, 5550-5556
    • (1995) EMBO J , vol.15 , pp. 5550-5556
    • Irie, A.1    Kamata, T.2    Puzon-McLaughlin, W.3    Takada, Y.4
  • 43
    • 19344369648 scopus 로고    scopus 로고
    • An integrin-dependent role of pouch endoderm in hyoid cartilage development
    • Crump, J. G., Swartz, M. E. and Kimmel, C. B. (2004) An integrin-dependent role of pouch endoderm in hyoid cartilage development. PLoS Biol. 2, E244
    • (2004) PLoS Biol , vol.2
    • Crump, J.G.1    Swartz, M.E.2    Kimmel, C.B.3
  • 45
    • 40749103428 scopus 로고    scopus 로고
    • Role of the β-subunit arginine/lysine finger in integrin heterodimer formation and function
    • Gupta, V., Alonso, J. L., Sugimori, T., Essafi, M., Xiong, J. P. and Arnaout, M. A. (2008) Role of the β-subunit arginine/lysine finger in integrin heterodimer formation and function. J. Immunol. 180, 1713-1718
    • (2008) J. Immunol , vol.180 , pp. 1713-1718
    • Gupta, V.1    Alonso, J.L.2    Sugimori, T.3    Essafi, M.4    Xiong, J.P.5    Arnaout, M.A.6
  • 46
    • 0035941265 scopus 로고    scopus 로고
    • Amino acid residues in the αIIb subunit that are critical for ligand binding to integrin αIIbα3 are clustered in the β-propeller model
    • Kamata, T., Tieu, K. K., Irie, A., Springer, T. A. and Takada, Y. (2001) Amino acid residues in the αIIb subunit that are critical for ligand binding to integrin αIIbα3 are clustered in the β-propeller model. J. Biol. Chem. 276, 44275-44283
    • (2001) J. Biol. Chem , vol.276 , pp. 44275-44283
    • Kamata, T.1    Tieu, K.K.2    Irie, A.3    Springer, T.A.4    Takada, Y.5
  • 47
    • 0032541043 scopus 로고    scopus 로고
    • Splice variants of the Drosophila PS2 integrins differentially interact with RGD-containing fragments of the extracellular proteins tiggrin, ten-m, and D-laminin 2
    • Graner, M. W., Bunch, T. A., Baumgartner, S., Kerschen, A. and Brower, D. L. (1998) Splice variants of the Drosophila PS2 integrins differentially interact with RGD-containing fragments of the extracellular proteins tiggrin, ten-m, and D-laminin 2. J. Biol. Chem. 273, 18235-18241
    • (1998) J. Biol. Chem , vol.273 , pp. 18235-18241
    • Graner, M.W.1    Bunch, T.A.2    Baumgartner, S.3    Kerschen, A.4    Brower, D.L.5
  • 48
    • 34548483403 scopus 로고    scopus 로고
    • Bunch, T. A, Kendall, T. L., Shakalya, K., Mahadevan, D. and Brower, D. L. (2007) Modulation of ligand binding by alternative splicing of the αPS2 integrin subunit. J. Cell. Biochem. 102, 211-23
    • Bunch, T. A, Kendall, T. L., Shakalya, K., Mahadevan, D. and Brower, D. L. (2007) Modulation of ligand binding by alternative splicing of the αPS2 integrin subunit. J. Cell. Biochem. 102, 211-23
  • 49
    • 34547594178 scopus 로고    scopus 로고
    • Distinct acidic clusters and hydrophobic residues in the alternative splice domains X1 and X2 of α7 integrins define specificity for laminin isoforms
    • von der Mark H., Pöschl E., Lanig H., Sasaki T., Deutzman, R. and von der Mark, K. (2007) Distinct acidic clusters and hydrophobic residues in the alternative splice domains X1 and X2 of α7 integrins define specificity for laminin isoforms. J. Mol. Biol. 371, 1188-1203
    • (2007) J. Mol. Biol , vol.371 , pp. 1188-1203
    • von der Mark, H.1    Pöschl, E.2    Lanig, H.3    Sasaki, T.4    Deutzman, R.5    von der Mark, K.6
  • 50
    • 0033406615 scopus 로고    scopus 로고
    • Fine mapping of inhibitory anti-α5 monoclonal antibody epitopes that differentially affect integrin-ligand binding
    • Burrows, L., Clark, K., Mould, A. P. and Humphries, M. J. (1999) Fine mapping of inhibitory anti-α5 monoclonal antibody epitopes that differentially affect integrin-ligand binding. Biochem. J. 344, 527-533
    • (1999) Biochem. J , vol.344 , pp. 527-533
    • Burrows, L.1    Clark, K.2    Mould, A.P.3    Humphries, M.J.4
  • 52
    • 70450181482 scopus 로고    scopus 로고
    • Rajecki, R. (2009) Investigational integrin antagonist well-tolerated, shows promise for AMD in first human trials. Ophthalmology Times, 1 May, http://ophthalmologytimes.modernmedicine.com
    • Rajecki, R. (2009) Investigational integrin antagonist well-tolerated, shows promise for AMD in first human trials. Ophthalmology Times, 1 May, http://ophthalmologytimes.modernmedicine.com
  • 53
    • 12144273121 scopus 로고    scopus 로고
    • In vivo drug discovery in the zebrafish
    • Zon, L. I. and Peterson, R. T. (2005) In vivo drug discovery in the zebrafish. Nat. Rev. Drug Discov. 4, 35-44
    • (2005) Nat. Rev. Drug Discov , vol.4 , pp. 35-44
    • Zon, L.I.1    Peterson, R.T.2
  • 54
    • 59649120717 scopus 로고    scopus 로고
    • Species differences in small molecule binding to αIIβa3 are the result of sequence differences in 2 loops of the αIIb α propeller
    • Basani, R. B, Zhu, H., Thornton, M. A., Soto, C. S., Degrado, W. F., Kowalska, M. A., Bennett, J. S. and Poncz, M. (2009) Species differences in small molecule binding to αIIβa3 are the result of sequence differences in 2 loops of the αIIb α propeller. Blood 113, 902-910
    • (2009) Blood , vol.113 , pp. 902-910
    • Basani, R.B.1    Zhu, H.2    Thornton, M.A.3    Soto, C.S.4    Degrado, W.F.5    Kowalska, M.A.6    Bennett, J.S.7    Poncz, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.