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Volumn 47, Issue 17, 2004, Pages 4166-4177

Human integrin αvβ5: Homology modeling and ligand binding

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA5 INTEGRIN; ALPHAVBETA5 INTEGRIN; ARGINYLGLYCYLASPARTIC ACID; BETA5 INTEGRIN; CARBOXYLIC ACID; CILENGITIDE; INTEGRIN RECEPTOR; LIGAND; LYSINE; SOLVENT; TYROSINE; UNCLASSIFIED DRUG; INTEGRIN; VITRONECTIN RECEPTOR;

EID: 3843120058     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm030635j     Document Type: Article
Times cited : (52)

References (85)
  • 1
    • 0032829104 scopus 로고    scopus 로고
    • Tumor angiogenesis - New drugs on the block
    • (a) Brower, V. Tumor angiogenesis - new drugs on the block. Nat. Biotechnol. 1999, 17, 963-968.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 963-968
    • Brower, V.1
  • 2
    • 0034648765 scopus 로고    scopus 로고
    • Angiogenesis in cancer and other disease
    • (b) Carmeliet, P.; Jain, R. K. Angiogenesis in Cancer and other Disease. Nature 2000, 407, 249-257.
    • (2000) Nature , vol.407 , pp. 249-257
    • Carmeliet, P.1    Jain, R.K.2
  • 3
    • 0038376002 scopus 로고    scopus 로고
    • Molecular regulation of vessel maturation
    • (c) Jain, R. K. Molecular regulation of vessel maturation. Nat. Med. 2003, 9, 685-693.
    • (2003) Nat. Med. , vol.9 , pp. 685-693
    • Jain, R.K.1
  • 4
    • 0042344925 scopus 로고    scopus 로고
    • A boost for tumor starvation
    • (d) Marx, J. A Boost for Tumor Starvation. Science 2003, 301, 452-453.
    • (2003) Science , vol.301 , pp. 452-453
    • Marx, J.1
  • 5
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • (a) Hynes, R. O. Integrins: Versatility, Modulation, and Signaling in Cell Adhesion. Cell 1992, 69, 11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 7
    • 0036039315 scopus 로고    scopus 로고
    • Suppression of tumor angiogenesis through the inhibition of integrin function and signaling in endothelial cells: Which side to target?
    • (c) Ruegg, C.; Dormond, O.; Foletti, A. Suppression of tumor angiogenesis through the inhibition of integrin function and signaling in endothelial cells: which side to target? Endothelium 2002, 9, 151-160.
    • (2002) Endothelium , vol.9 , pp. 151-160
    • Ruegg, C.1    Dormond, O.2    Foletti, A.3
  • 8
    • 0036792466 scopus 로고    scopus 로고
    • Inhibition of endothelial cell survival and angiogenesis by protein kinase A
    • (d) Kim, S.; Bakre, M.; Yin, H.; Varner, J. A. Inhibition of endothelial cell survival and angiogenesis by protein kinase A. J. Clin. Invest. 2002, 110, 933-941.
    • (2002) J. Clin. Invest. , vol.110 , pp. 933-941
    • Kim, S.1    Bakre, M.2    Yin, H.3    Varner, J.A.4
  • 9
    • 0036734093 scopus 로고    scopus 로고
    • A reevaluation of integrins as regulators of angiogenesis
    • (e) Hynes, R. O. A reevaluation of integrins as regulators of angiogenesis. Nature Medicine 2002, 8, 918-921.
    • (2002) Nature Medicine , vol.8 , pp. 918-921
    • Hynes, R.O.1
  • 10
    • 0036679895 scopus 로고    scopus 로고
    • Anti-integrin as novel drug-discovery targets: Potential therapeutic and diagnostic implications
    • (f) Mousa, S. A. Anti-integrin as novel drug-discovery targets: potential therapeutic and diagnostic implications. Curr. Opin. Chem. Biol. 2002, 6, 534-541
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 534-541
    • Mousa, S.A.1
  • 11
    • 0028362876 scopus 로고
    • Requirement of vascular integrin αvβ3 for angiogenesis
    • (a) Brooks, P. C.; Clark, R. A.; Cheresh, D. A. Requirement of Vascular integrin αvβ3 for angiogenesis. Science 1994, 264, 569-571.
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.2    Cheresh, D.A.3
  • 12
    • 0033943076 scopus 로고    scopus 로고
    • Role of alpha v integrins during angiogenesis
    • (b) Eliceiri, B. P.; Cheresh, D. A. Role of alpha v integrins during angiogenesis. Cancer J. 2000, 13, 245-249.
    • (2000) Cancer J. , vol.13 , pp. 245-249
    • Eliceiri, B.P.1    Cheresh, D.A.2
  • 14
    • 0036682030 scopus 로고    scopus 로고
    • Cilengitide targeting of avb3 integrin receptor synergizes with radioimmunotherapy to increase efficacy and apoptosis in breast cancer xenografts
    • Burke, P. A.; DeNardo, S. J.; Miers, L. A.; Lamborn, K. R.; Matzku, S.; DeNardo, G. L. Cilengitide Targeting of avb3 Integrin Receptor Synergizes with Radioimmunotherapy to Increase Efficacy and Apoptosis in Breast Cancer Xenografts. Cancer Res. 2002, 62, 4263-4272.
    • (2002) Cancer Res. , vol.62 , pp. 4263-4272
    • Burke, P.A.1    DeNardo, S.J.2    Miers, L.A.3    Lamborn, K.R.4    Matzku, S.5    DeNardo, G.L.6
  • 15
    • 0025340173 scopus 로고
    • Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin
    • (a) Smith, J. W.; Vesta, D. J.; Irwin, S. V.; Burke, T. A.; Cheresh, D. A. Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin. J. Biol. Chem. 1990, 265, 11008-11013.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11008-11013
    • Smith, J.W.1    Vesta, D.J.2    Irwin, S.V.3    Burke, T.A.4    Cheresh, D.A.5
  • 18
    • 0032514841 scopus 로고    scopus 로고
    • Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all alpha v integrins
    • (a) Bader, B. L.; Rayburn, H.; Crowley, D.; Hynes, R. O. Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all alpha v integrins. Cell 1998, 95, 507-519.
    • (1998) Cell , vol.95 , pp. 507-519
    • Bader, B.L.1    Rayburn, H.2    Crowley, D.3    Hynes, R.O.4
  • 22
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • (b) Hynes, R. O. Integrins: bidirectional, allosteric signaling machines. Cell 2002, 110, 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 23
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • (a) Ruoslahti, E.; Pierschbacher, M. D. New perspectives in cell adhesion: RGD and integrins. Science 1987, 238, 491-497.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 24
    • 0025814801 scopus 로고
    • Arginyl-Glycyl-Aspartic acid (RGD) a cell adhesion motif
    • (b) D'Souza, S. E.; Ginsberg, M. H.; Plow, E. F. Arginyl-Glycyl-Aspartic acid (RGD) a cell adhesion motif. Trends Biochem. Sci. 1991, 16, 246-250.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 246-250
    • D'Souza, S.E.1    Ginsberg, M.H.2    Plow, E.F.3
  • 25
    • 0025880146 scopus 로고
    • Arg-Gly-Asp constrained within cyclic penta-peptides. Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1
    • (a) Aumailley, M.; Gurrath, M.; Müller, G.; Calvete, J.; Timpl, R.; Kessler, H. Arg-Gly-Asp constrained within cyclic penta-peptides. Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragment P1. FEBS Lett. 1991, 291, 50-54.
    • (1991) FEBS Lett. , vol.291 , pp. 50-54
    • Aumailley, M.1    Gurrath, M.2    Müller, G.3    Calvete, J.4    Timpl, R.5    Kessler, H.6
  • 26
    • 33748242298 scopus 로고
    • Dynamic forcing, a method for evaluating activity and selectivity profiles of RGD (Arg-Gly-Asp) peptides
    • (b) Müller, G.; Gurrath, M.; Kessler, H.; Timpl, R. Dynamic Forcing, a Method for Evaluating Activity and Selectivity Profiles of RGD (Arg-Gly-Asp) Peptides. Angew. Chem., Int. Ed. Engl. 1992, 31, 326-328.
    • (1992) Angew. Chem., Int. Ed. Engl. , vol.31 , pp. 326-328
    • Müller, G.1    Gurrath, M.2    Kessler, H.3    Timpl, R.4
  • 27
    • 0027102818 scopus 로고
    • Conformation/activity studies of rationally designed potent anti-adhesive RGD peptides
    • (c) Gurrath, M.; Müller, G.; Kessler, H.; Aumailley, M.; Timpl, R. Conformation/activity studies of rationally designed potent anti-adhesive RGD peptides, Eur. J. Biochem. 1992, 210, 911-921.
    • (1992) Eur. J. Biochem. , vol.210 , pp. 911-921
    • Gurrath, M.1    Müller, G.2    Kessler, H.3    Aumailley, M.4    Timpl, R.5
  • 29
    • 0027997413 scopus 로고
    • Selective recognition of cyclic RGD peptides of NMR defined conformation by αIIbβ3, αvβ3 and α5β1 integrins
    • (e) Pfaff, M.; Tangemann, K.; Müller, B.; Gurrath, M.; Müller, G.; Kessler, H.; Timpl, R.; Engel, J. Selective recognition of cyclic RGD peptides of NMR defined conformation by αIIbβ3, αvβ3 and α5β1 integrins. J. Biol. Chem. 1994, 269, 20233-20238.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20233-20238
    • Pfaff, M.1    Tangemann, K.2    Müller, B.3    Gurrath, M.4    Müller, G.5    Kessler, H.6    Timpl, R.7    Engel, J.8
  • 30
    • 0028711918 scopus 로고
    • Pharmacophore refinement of gpIIb/IIa antagonists based on comparitive studies of antiadhesive cyclic and acyclic RGD peptides
    • (f) Müller, G.; Gurrath, M.; Kessler, H. Pharmacophore refinement of gpIIb/IIa antagonists based on comparitive studies of antiadhesive cyclic and acyclic RGD peptides. J. Comput.-Aided Mol. Des. 1994, 8, 709-730.
    • (1994) J. Comput.-Aided Mol. Des. , vol.8 , pp. 709-730
    • Müller, G.1    Gurrath, M.2    Kessler, H.3
  • 31
    • 0030768536 scopus 로고    scopus 로고
    • Stereoisomeric peptide libraries and peptidomimetics for designing selective inhibitors of the αvβ3 integrin for a new cancer therapy
    • (g) Haubner, R.; Finsinger, D.; Kessler, H. Stereoisomeric Peptide Libraries and Peptidomimetics for Designing Selective Inhibitors of the αvβ3 Integrin for a New Cancer Therapy. Angew. Chem., Int. Ed. 1997, 36, 1374-1389.
    • (1997) Angew. Chem., Int. Ed. , vol.36 , pp. 1374-1389
    • Haubner, R.1    Finsinger, D.2    Kessler, H.3
  • 37
    • 0001943567 scopus 로고    scopus 로고
    • Recent advances in avb3 integrin inhibitors
    • (e) Hölzemann, G. Recent advances in avb3 integrin inhibitors. Drugs 2001, 4, 72-81.
    • (2001) Drugs , vol.4 , pp. 72-81
    • Hölzemann, G.1
  • 38
    • 0035821594 scopus 로고    scopus 로고
    • Solid-phase synthesis of a nonpeptidic RGD mimetic library: New selective αvβ3 integrin antagonists
    • (f) Sulyok, G. A. G.; Gibson, C.; Goodman, S. L.; Hölzemann, G.; Wiesner, M.; Kessler, H. Solid-Phase Synthesis of a Nonpeptidic RGD Mimetic Library: New Selective αvβ3 Integrin Antagonists. J. Med. Chem. 2001, 44, 1938-1950.
    • (2001) J. Med. Chem. , vol.44 , pp. 1938-1950
    • Sulyok, G.A.G.1    Gibson, C.2    Goodman, S.L.3    Hölzemann, G.4    Wiesner, M.5    Kessler, H.6
  • 39
    • 0037186502 scopus 로고    scopus 로고
    • Nanomolar small molecule inhibitors for αvβ6, αvβ5, and αvβ3 integrins
    • (g) Goodman, S. L.; Hölzemann, G.; Sulyok, G. A. G.; Kessler, H. Nanomolar Small Molecule Inhibitors for αvβ6, αvβ5, and αvβ3 Integrins. J. Med. Chem. 2002, 45, 1045-1051.
    • (2002) J. Med. Chem. , vol.45 , pp. 1045-1051
    • Goodman, S.L.1    Hölzemann, G.2    Sulyok, G.A.G.3    Kessler, H.4
  • 41
    • 0030856555 scopus 로고    scopus 로고
    • Changing ligand specificities of αvβ1 and αvβ3 integrins by swapping a short diverse sequence of a β subunit
    • Takagi, J.; Tetsuji, K.; Meredith, J.; Puzon-McLaughlin, W.; Takada, Y.; Changing ligand specificities of αvβ1 and αvβ3 integrins by swapping a short diverse sequence of a β subunit. J. Biol. Chem. 1997, 32, 19794-19800.
    • (1997) J. Biol. Chem. , vol.32 , pp. 19794-19800
    • Takagi, J.1    Tetsuji, K.2    Meredith, J.3    Puzon-McLaughlin, W.4    Takada, Y.5
  • 42
    • 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. L.; Arnaout, M. A. Crystal Structure of the Extracellular Segment of Integrin αvβ3 in Complex with an Arg-Gly-Asp Ligand. Science 2002, 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.L.6    Arnaout, M.A.7
  • 44
    • 0037009042 scopus 로고    scopus 로고
    • Integrin activation takes shape
    • (a) Liddington, R. C.; and Ginsberg, M. H. Integrin activation takes shape. J. Cell Biol. 2002, 158, 833-839.
    • (2002) J. Cell Biol. , vol.158 , pp. 833-839
    • Liddington, R.C.1    Ginsberg, M.H.2
  • 45
    • 0036697001 scopus 로고    scopus 로고
    • Integrin activation and structural rearrangement
    • (b) Takagi, J.; and Springer, T. A. Integrin activation and structural rearrangement. Immunol. Rev. 2002, 186, 141-163.
    • (2002) Immunol. Rev. , vol.186 , pp. 141-163
    • Takagi, J.1    Springer, T.A.2
  • 46
    • 0036696097 scopus 로고    scopus 로고
    • Integrin structure: New twists and turns in dynamic cell adhesion
    • (c) Arnaout, M. A. Integrin structure: new twists and turns in dynamic cell adhesion. Immunol. Rev. 2002 186, 125-140.
    • (2002) Immunol. Rev. , vol.186 , pp. 125-140
    • Arnaout, M.A.1
  • 47
  • 48
    • 0036918741 scopus 로고    scopus 로고
    • Predicted and experimental structures of integrins and β-propellers
    • (a) Springer, T. A. Predicted and experimental structures of integrins and β-propellers. Curr. Opin. Struct. Biol. 2002, 12, 802-813.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 802-813
    • Springer, T.A.1
  • 49
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin αIIbβ3 "inside- out" activation as regulated by its cytoplasmic face
    • (b) Vinogradova, O.; Velyvis, A.; Velyviene, A.; Hu, B.; Haas, T. A.; Plow, E. F.; Qin, J. A structural mechanism of integrin αIIbβ3 "inside-out" activation as regulated by its cytoplasmic face. Cell 2002, 110, 587-597.
    • (2002) Cell , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.A.5    Plow, E.F.6    Qin, J.7
  • 50
    • 0036087390 scopus 로고    scopus 로고
    • Transmembrane signal transduction of the αIIbβ3 integrin
    • (c) Gottschalk, K.-E.; Adams, P. D.; Brunger, A. T.; Kessler, H. Transmembrane signal transduction of the αIIbβ3 integrin. Protein Sci. 2002, 11, 1800-1812.
    • (2002) Protein Sci. , vol.11 , pp. 1800-1812
    • Gottschalk, K.-E.1    Adams, P.D.2    Brunger, A.T.3    Kessler, H.4
  • 51
    • 0037195164 scopus 로고    scopus 로고
    • Three-dimensional model of the human platelet integrin αIIbβ3 based on electron cryomicroscopy and X-ray crystallography
    • (d) Adair, B. D.; Yeager, M. Three-dimensional model of the human platelet integrin αIIbβ3 based on electron cryomicroscopy and X-ray crystallography. PNAS, 2002, 99, 14059-14064.
    • (2002) PNAS , vol.99 , pp. 14059-14064
    • Adair, B.D.1    Yeager, M.2
  • 52
    • 0141625303 scopus 로고    scopus 로고
    • Structure of integrin α5β1 in complex with fibronectin
    • (e) Takagi, J.; Strokovich, K.; Springer, T. A.; Walz, T. Structure of integrin α5β1 in complex with fibronectin. EMBO J. 2003, 22, 4607-4615.
    • (2003) EMBO J. , vol.22 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 53
    • 1642573163 scopus 로고    scopus 로고
    • Evidence for hetero-association of transmembrane helices of integrins
    • (f) Gottschalk, K.-E.; Kessler, H. Evidence for Hetero-Association of Transmembrane helices of Integrins. FEBS Lett. 2004, 557, 253-258.
    • (2004) FEBS Lett. , vol.557 , pp. 253-258
    • Gottschalk, K.-E.1    Kessler, H.2
  • 54
    • 0036903735 scopus 로고    scopus 로고
    • A three-state mechanism of integrin activation signal transduction for integrin αvβ3
    • (a) Gottschalk, K.-E.; Günther, R.; Kessler, H. A Three-State Mechanism of Integrin Activation and Signal Transduction for Integrin αvβ3. ChemBioChem 2002, 3, 470-473.
    • (2002) ChemBioChem , vol.3 , pp. 470-473
    • Gottschalk, K.-E.1    Günther, R.2    Kessler, H.3
  • 55
    • 0037131442 scopus 로고    scopus 로고
    • The structures of integrins and integrin-ligand complexes: Implications for drug design and signal transduction
    • (b) Gottschalk, K.-E.; Kessler, H. The Structures of Integrins and Integrin-Ligand Complexes: Implications for Drug Design and Signal Transduction. Angew. Chem., Int. Ed. 2002, 41, 3767-3774.
    • (2002) Angew. Chem., Int. Ed. , vol.41 , pp. 3767-3774
    • Gottschalk, K.-E.1    Kessler, H.2
  • 56
    • 0141958105 scopus 로고    scopus 로고
    • Docking studies on αvβ3 integrin ligands: Pharmacophore refinement and implication for drug design
    • (c) Marinelli, L.; Lavecchia, A.; Gottschalk, K. E.; Novellino, E.; Kessler, H. Docking studies on αvβ3 Integrin Ligands: Pharmacophore Refinement and Implication for Drug Design. J. Med. Chem. 2003, 46, 4393-4404.
    • (2003) J. Med. Chem. , vol.46 , pp. 4393-4404
    • Marinelli, L.1    Lavecchia, A.2    Gottschalk, K.E.3    Novellino, E.4    Kessler, H.5
  • 57
    • 0036219943 scopus 로고    scopus 로고
    • A 3D structure model of integrin α4β1 complex: Construction of a homology model of β1 and ligand binding analysis
    • (a) You, T. J.; Maxwell, D. S.; Kogan, T. P.; Chen, Q.; Li, J.; Kassir, J.; Holland, G. W.; Dixon, R. A. F. A 3D Structure Model of Integrin α4β1 Complex: Construction of a Homology Model of β1 and Ligand Binding Analysis. Biophys J. 2002, 82, 447-457.
    • (2002) Biophys J. , vol.82 , pp. 447-457
    • You, T.J.1    Maxwell, D.S.2    Kogan, T.P.3    Chen, Q.4    Li, J.5    Kassir, J.6    Holland, G.W.7    Dixon, R.A.F.8
  • 59
  • 61
    • 0027496638 scopus 로고
    • Mutation of putative divalent cation sites in the a4 subunit of the integrin VLA-4: Distinct effects on adhesion to CS1/fibronectin, VCAM-1, and invasin
    • (a) Masumoto, A.; Hemler, M. E. Mutation of putative divalent cation sites in the a4 subunit of the integrin VLA-4: Distinct effects on adhesion to CS1/fibronectin, VCAM-1, and invasin. J Cell Biol 1993, 123, 245-53.
    • (1993) J Cell Biol. , vol.123 , pp. 245-253
    • Masumoto, A.1    Hemler, M.E.2
  • 62
    • 0028951764 scopus 로고
    • Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit association
    • (b) Wilcox, D. A.; Paddock, C. M.; Lyman, S.; Gill, J. C.; Newman, P. J. Glanzmann thrombasthenia resulting from a single amino acid substitution between the second and third calcium-binding domains of GPIIb. Role of the GPIIb amino terminus in integrin subunit association. J. Clin. Invest. 1995, 95, 1553-60.
    • (1995) J. Clin. Invest. , vol.95 , pp. 1553-1560
    • Wilcox, D.A.1    Paddock, C.M.2    Lyman, S.3    Gill, J.C.4    Newman, P.J.5
  • 63
    • 0037443402 scopus 로고    scopus 로고
    • Two novel mutations in the {alpha}IIb calcium-binding domains identify hydrophobic regions essential for {alpha}IIb-{beta}3 biogenesis
    • (c) Mitchell, W. B.; Li, J.; Singh, F.; Michelson, A. D.; Bussel, J.; Coller, B. S.; French, D. L. Two novel mutations in the {alpha}IIb calcium-binding domains identify hydrophobic regions essential for {alpha}IIb-{beta}3 biogenesis. Blood 2003, 101, 2268-76.
    • (2003) Blood , vol.101 , pp. 2268-2276
    • Mitchell, W.B.1    Li, J.2    Singh, F.3    Michelson, A.D.4    Bussel, J.5    Coller, B.S.6    French, D.L.7
  • 64
    • 0037006979 scopus 로고    scopus 로고
    • The role of the specificity-determining loop of integrin β subunit I-like domain in autonomous expression, association with the α subunit, and ligand binding
    • Takagi, J.; DeBottis, D. P.; Erickson, H. P.; Springer, T. A. The role of the specificity-determining loop of integrin β subunit I-like domain in autonomous expression, association with the α subunit, and ligand binding. Biochemistry 2002, 41, 4339-4347.
    • (2002) Biochemistry , vol.41 , pp. 4339-4347
    • Takagi, J.1    DeBottis, D.P.2    Erickson, H.P.3    Springer, T.A.4
  • 65
    • 0034283972 scopus 로고    scopus 로고
    • Identification and in vivo efficacy of small-molecule antagonist of integrin αvβ3 (the vitronectin receptor)
    • Miller, W. H.; Keenan, R. M.; Willette, R. N.; Lark, M. W. Identification and in vivo efficacy of small-molecule antagonist of integrin αvβ3 (the vitronectin receptor). Ther. Focus. 2000, 5, 397-408.
    • (2000) Ther. Focus , vol.5 , pp. 397-408
    • Miller, W.H.1    Keenan, R.M.2    Willette, R.N.3    Lark, M.W.4
  • 67
    • 0036221518 scopus 로고    scopus 로고
    • Identification of critical residues for ligand binding in the integrin beta3 I-domain by site-directed mutagenesis
    • Yamanouchi, J.; Hato, T.; Tamura, T.; Fujita, S. Identification of critical residues for ligand binding in the integrin beta3 I-domain by site-directed mutagenesis. Thromb. Haemost. 2002, 87, 756-762.
    • (2002) Thromb. Haemost. , vol.87 , pp. 756-762
    • Yamanouchi, J.1    Hato, T.2    Tamura, T.3    Fujita, S.4
  • 68
    • 0037008102 scopus 로고    scopus 로고
    • Identification of the principal binding site for RGD-containing ligands in the αvβ3 integrin: A photoaffinity cross-linking study
    • Yahalom, D.; Wittelsberger, A.; Mierke, D. F.; Rosenblatt, M.; Alexander, J. M.; Chorev, M. Identification of the Principal Binding Site for RGD-Containing Ligands in the αvβ3 Integrin: A Photoaffinity Cross-Linking Study. Biochemistry 2002, 41, 8321-8331.
    • (2002) Biochemistry , vol.41 , pp. 8321-8331
    • Yahalom, D.1    Wittelsberger, A.2    Mierke, D.F.3    Rosenblatt, M.4    Alexander, J.M.5    Chorev, M.6
  • 70
    • 0029994263 scopus 로고    scopus 로고
    • Application of the message-address concept to the docking of naltrexone and selective naltrexone-derived opioid antagonists into opioid receptors models
    • (a) Metzger, T. G.; Paterlini, M. G., Portoghese, P. S.; Ferguson, D. M. Application of the message-address concept to the docking of naltrexone and selective naltrexone-derived opioid antagonists into opioid receptors models. Neurochem. Res. 1996, 21, 1287-1294.
    • (1996) Neurochem. Res. , vol.21 , pp. 1287-1294
    • Metzger, T.G.1    Paterlini, M.G.2    Portoghese, P.S.3    Ferguson, D.M.4
  • 71
    • 0032723795 scopus 로고    scopus 로고
    • Dopamine D4/D2 receptor selectivity is determined by a divergent aromatic microdomain contained within the second, third, and seventh membrane-spanning segments
    • (b) Simpson, M. M.; Ballesteros, J. A.; Chiappa, V.; Chen, J.; Suehiro, M.; Hartman, D. S.; Godel, T.; Snyder, L. A.; Sakmar, T. P.; Javitch, J. A. Dopamine D4/D2 receptor selectivity is determined by a divergent aromatic microdomain contained within the second, third, and seventh membrane-spanning segments. Mol. Pharmacol. 1999, 56,1116-1126.
    • (1999) Mol. Pharmacol. , vol.56 , pp. 1116-1126
    • Simpson, M.M.1    Ballesteros, J.A.2    Chiappa, V.3    Chen, J.4    Suehiro, M.5    Hartman, D.S.6    Godel, T.7    Snyder, L.A.8    Sakmar, T.P.9    Javitch, J.A.10
  • 73
    • 0027968068 scopus 로고
    • Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D.; Higgins, D. G.; Gibson, T. J. Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 1994, 22, 4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 75
    • 0036284090 scopus 로고    scopus 로고
    • VEGA: A versatile program to convert, handle, and visualize molecular structure on windows-based PCs
    • Pedretti, A.; Villa, L.; Vistoli, G. VEGA: a Versatile Program to Convert, Handle, and Visualize Molecular Structure on Windows-based PCs. J. Mol. Graph. 2002, 21, 47-49.
    • (2002) J. Mol. Graph. , vol.21 , pp. 47-49
    • Pedretti, A.1    Villa, L.2    Vistoli, G.3
  • 76
    • 0344884028 scopus 로고    scopus 로고
    • San Diego, CA
    • Accelrys, 2001, San Diego, CA.
    • (2001) Accelrys
  • 77
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A.; MacArthur, M. W.; Moss, D. S.; Thornton, J. M. PROCHECK: a Program to Check the Stereochemical Quality of Protein Structures. J. Appl. Crystallogr. 1993, 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
  • 78
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris, G. M.; Goodsell, D. S.; Halliday, R. S.; Huey, R.; Hart, W. E.; Belew, R. K.; Olson, A. J. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 1998, 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 80
    • 3343012886 scopus 로고
    • A Broyden-Fletcher-Goldfarb-Shanno optimization procedure for molecular geometries
    • Head, J.; Zerner, M. C. A Broyden-Fletcher-Goldfarb-Shanno Optimization Procedure for Molecular Geometries. Chem. Phys. Lett. 1985, 122, 264-274.
    • (1985) Chem. Phys. Lett. , vol.122 , pp. 264-274
    • Head, J.1    Zerner, M.C.2
  • 81
    • 0023325062 scopus 로고
    • Strategic approaches to drug design. 1. An integrated software framework for molecular modelling
    • Vinter, J. G.; Davis, A.; Saunders: M. R. Strategic Approaches to Drug Design. 1. An Integrated Software Framework for Molecular Modelling. J. Comput.-Aided Mol. Des. 1987, 1, 31-55.
    • (1987) J. Comput.-Aided Mol. Des. , vol.1 , pp. 31-55
    • Vinter, J.G.1    Davis, A.2    Saunders, M.R.3
  • 82
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity - A rapid access to atomic charges
    • Gasteiger, J.; Marsili, M. Iterative partial equalization of orbital electronegativity - a rapid access to atomic charges. Tetrahedron 1980, 36, 3219-3228.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 84
    • 0033280227 scopus 로고    scopus 로고
    • Improved AMBER torsional parameters for the N-N rotational barrier in diacylhydrazines
    • (a) Chakravorty, S.; Reynolds, C. H. Improved AMBER torsional parameters for the N-N rotational barrier in diacylhydrazines. J. Mol. Graph. Model. 1999, 17, 315-324.
    • (1999) J. Mol. Graph. Model. , vol.17 , pp. 315-324
    • Chakravorty, S.1    Reynolds, C.H.2
  • 85
    • 84962436408 scopus 로고    scopus 로고
    • Hydrazino peptides as foldamers: An extension of the β-peptide concept
    • (b) Günther, R.; Hofmann, H. J. Hydrazino peptides as foldamers: an extension of the β-peptide concept. J. Am. Chem. Soc. 2001, 123, 247-255.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 247-255
    • Günther, R.1    Hofmann, H.J.2


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