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Volumn 26, Issue , 1997, Pages 27-45

Structural and mechanistic determinants of affinity and specificity of ligands discovered or engineered by phage display

Author keywords

Mechanism; Peptide receptor structures; Selectivity

Indexed keywords

ANTIBODY; ATRIAL NATRIURETIC FACTOR; ERYTHROPOIETIN RECEPTOR; HLA DR1 ANTIGEN; HUMAN GROWTH HORMONE; LIGAND; PEPTIDE; PROTEIN A; RECEPTOR; STREPTAVIDIN; ZINC FINGER PROTEIN;

EID: 0030966598     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.26.1.27     Document Type: Review
Times cited : (58)

References (98)
  • 1
    • 0028533869 scopus 로고
    • Proximity versus allostery: The role of regulated protein dimerization in biology
    • Austin DJ, Crabtree RG, Schreiber SL. 1994. Proximity versus allostery: the role of regulated protein dimerization in biology. Chem. Biol. 1:125-29
    • (1994) Chem. Biol. , vol.1 , pp. 125-129
    • Austin, D.J.1    Crabtree, R.G.2    Schreiber, S.L.3
  • 2
    • 0027449373 scopus 로고
    • Identification of a hexapeptide that mimics a conformation-dependent binding site of acetylcholine receptor by use of a phage-epitope library
    • Balass M, Heldman Y, Cabilly S, Givol D, Katchalski-Katzir E, et al. 1993. Identification of a hexapeptide that mimics a conformation-dependent binding site of acetylcholine receptor by use of a phage-epitope library. Proc. Natl. Acad. Sci. USA 90:10638-42
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10638-10642
    • Balass, M.1    Heldman, Y.2    Cabilly, S.3    Givol, D.4    Katchalski-Katzir, E.5
  • 4
    • 0030013607 scopus 로고    scopus 로고
    • Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins
    • Belshaw PJ, Ho SN, Crabtree GR, Schreiber SL. 1996. Controlling protein association and subcellular localization with a synthetic ligand that induces heterodimerization of proteins. Proc. Natl. Acad. Sci. USA 93:4604-7
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4604-4607
    • Belshaw, P.J.1    Ho, S.N.2    Crabtree, G.R.3    Schreiber, S.L.4
  • 6
    • 0029677974 scopus 로고    scopus 로고
    • How pathogens exploit interactions mediated by SH3 domains
    • Bliska J. 1996. How pathogens exploit interactions mediated by SH3 domains. Chem. Biol. 3:7-11
    • (1996) Chem. Biol. , vol.3 , pp. 7-11
    • Bliska, J.1
  • 7
    • 0028939035 scopus 로고
    • Comprehensive epitope analysis of monoclonal anti-proenkephalin antibodies using phage display libraries and synthetic peptides: Revelation of antibody fine specificities caused by somatic mutations in the variable genes
    • Böttger V, Böttger A, Lane EB, Spruce BA. 1995. Comprehensive epitope analysis of monoclonal anti-proenkephalin antibodies using phage display libraries and synthetic peptides: revelation of antibody fine specificities caused by somatic mutations in the variable genes. J. Mol. Biol. 247:932-46
    • (1995) J. Mol. Biol. , vol.247 , pp. 932-946
    • Böttger, V.1    Böttger, A.2    Lane, E.B.3    Spruce, B.A.4
  • 12
    • 0001937093 scopus 로고
    • Human antibodies to viral pathogens from phage display libraries
    • ed. RM Chanock, Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press
    • Burton DR. 1995. Human antibodies to viral pathogens from phage display libraries. Vaccines 95: Mol. Approaches Control Infect. Dis. Annu. Meet., 12th, ed. RM Chanock, pp. 1-11. Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press
    • (1995) Vaccines 95: Mol. Approaches Control Infect. Dis. Annu. Meet., 12th , pp. 1-11
    • Burton, D.R.1
  • 13
    • 0029021085 scopus 로고
    • Anti-melanoma antibodies from melanoma patients immunized with genetically modified autologous tumor cells: Selection of specific antibodies from single-chain Fv fusion phage libraries
    • Cai X, Garen A. 1995. Anti-melanoma antibodies from melanoma patients immunized with genetically modified autologous tumor cells: selection of specific antibodies from single-chain Fv fusion phage libraries. Proc. Natl. Acad. Sci. USA 92:6537-41
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6537-6541
    • Cai, X.1    Garen, A.2
  • 14
    • 0028223378 scopus 로고
    • In vitro selection from protein and peptide libraries
    • Clackson T, Wells JA. 1994. In vitro selection from protein and peptide libraries. Trends Biotechnol. 12:173-84
    • (1994) Trends Biotechnol. , vol.12 , pp. 173-184
    • Clackson, T.1    Wells, J.A.2
  • 15
    • 0028911488 scopus 로고
    • Identification of biologically active peptides using random libraries displayed on phage
    • Cortese R, Monaci P, Nicosia A, Luzzago A, Felici F, et al. 1995. Identification of biologically active peptides using random libraries displayed on phage. Curr. Opin. Biotechnol. 6:73-80
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 73-80
    • Cortese, R.1    Monaci, P.2    Nicosia, A.3    Luzzago, A.4    Felici, F.5
  • 16
    • 0029445419 scopus 로고
    • Principles and applications of recombinant antibody phage display technology to plant biology
    • Crosby WL, Schorr P. 1995. Principles and applications of recombinant antibody phage display technology to plant biology. Methods Cell Biol. 50:85-99
    • (1995) Methods Cell Biol. , vol.50 , pp. 85-99
    • Crosby, W.L.1    Schorr, P.2
  • 17
    • 0029120476 scopus 로고
    • Phage peptide libraries for the selection of highly specific ligands
    • Daniels DA, Dion A, Lane DP. 1995. Phage peptide libraries for the selection of highly specific ligands. Exp. Opin. Ther. Pat. 5:901-12
    • (1995) Exp. Opin. Ther. Pat. , vol.5 , pp. 901-912
    • Daniels, D.A.1    Dion, A.2    Lane, D.P.3
  • 18
    • 0027997708 scopus 로고
    • The characterization of p53 binding phage isolated from phage peptide display libraries
    • Daniels DA, Lane DP. 1994. The characterization of p53 binding phage isolated from phage peptide display libraries. J. Mol. Biol. 243:639-52
    • (1994) J. Mol. Biol. , vol.243 , pp. 639-652
    • Daniels, D.A.1    Lane, D.P.2
  • 19
    • 0028926814 scopus 로고
    • Selection and application of human single chain Fv antibody fragments from a semi-synthetic phage antibody display library with designed CDR3 regions
    • de Kruif J, Boel E, Logtenberg T. 1995. Selection and application of human single chain Fv antibody fragments from a semi-synthetic phage antibody display library with designed CDR3 regions. J. Mol. Biol. 248:97-105
    • (1995) J. Mol. Biol. , vol.248 , pp. 97-105
    • De Kruif, J.1    Boel, E.2    Logtenberg, T.3
  • 20
    • 0029008062 scopus 로고
    • Rapid selection of cell subpopulation-specific human monoclonal antibodies from a synthetic phage antibody library
    • de Kruif J, Terstappen L, Boel E, Logtenberg T. 1995. Rapid selection of cell subpopulation-specific human monoclonal antibodies from a synthetic phage antibody library. Proc. Natl. Acad. Sci. USA 92:3938-42
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3938-3942
    • De Kruif, J.1    Terstappen, L.2    Boel, E.3    Logtenberg, T.4
  • 21
    • 0029060370 scopus 로고
    • Basis for selection of improved carbohydrate-binding single-chain antibodies from synthetic gene libraries
    • Deng SJ, MacKenzie CR, Hirama T, Brousseau R, Lowary TL, et al. 1995. Basis for selection of improved carbohydrate-binding single-chain antibodies from synthetic gene libraries. Proc. Natl. Acad. Sci. USA 92:4992-96
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 4992-4996
    • Deng, S.J.1    MacKenzie, C.R.2    Hirama, T.3    Brousseau, R.4    Lowary, T.L.5
  • 22
    • 0028841350 scopus 로고
    • Potent and selective Kunitz domain inhibitors of plasma kallikrein designed by phage display
    • Dennis MS, Herzka A, Lazarus RA. 1995. Potent and selective Kunitz domain inhibitors of plasma kallikrein designed by phage display. J. Biol. Chem. 270:25411-17
    • (1995) J. Biol. Chem. , vol.270 , pp. 25411-25417
    • Dennis, M.S.1    Herzka, A.2    Lazarus, R.A.3
  • 23
    • 0028138396 scopus 로고
    • Structural mimicry and enhanced immunogenicity of peptide epitopes displayed on filamentous bacteriophage. The V3 loop of HIV-1 gp120
    • Di Marzo Veronese F, Willis AE, Boyer-Thompson C, Appela E, Perham RN. 1994. Structural mimicry and enhanced immunogenicity of peptide epitopes displayed on filamentous bacteriophage. The V3 loop of HIV-1 gp120. J. Mol. Biol. 243:167-72
    • (1994) J. Mol. Biol. , vol.243 , pp. 167-172
    • Di Marzo Veronese, F.1    Willis, A.E.2    Boyer-Thompson, C.3    Appela, E.4    Perham, R.N.5
  • 25
    • 0028831142 scopus 로고
    • Neutralizing recombinant antibodies to a conformational V2- and CD4-binding site-sensitive epitope of HIV-1 gp120 isolated by using an epitope-masking procedure
    • Ditzel HJ, Binley JM, Moore JP, Sodroski J, Sullivan N, et al. 1995. Neutralizing recombinant antibodies to a conformational V2- and CD4-binding site-sensitive epitope of HIV-1 gp120 isolated by using an epitope-masking procedure. J. Immunol. 154:893-906
    • (1995) J. Immunol. , vol.154 , pp. 893-906
    • Ditzel, H.J.1    Binley, J.M.2    Moore, J.P.3    Sodroski, J.4    Sullivan, N.5
  • 26
    • 8244243807 scopus 로고
    • Antibody repertoire to self and the virus in HIV-1 infection probed by phage display libraries
    • ed. RM Chanock, Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press
    • Ditzel HJ, Burton DR. 1995. Antibody repertoire to self and the virus in HIV-1 infection probed by phage display libraries. Vaccines 95: Mol. Approaches Control Infect. Dis. Annu. Meet., 12th, ed. RM Chanock, pp. 19-26. Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press
    • (1995) Vaccines 95: Mol. Approaches Control Infect. Dis. Annu. Meet., 12th , pp. 19-26
    • Ditzel, H.J.1    Burton, D.R.2
  • 27
    • 14744290518 scopus 로고
    • Bacteriophage surface display of an immunoglobulin-binding domain of Staphylococcus aureus protein A
    • Djojonegoro BM, Benedik MJ, Wilson RC. 1994. Bacteriophage surface display of an immunoglobulin-binding domain of Staphylococcus aureus protein A. BioTechnology 12:169-72
    • (1994) BioTechnology , vol.12 , pp. 169-172
    • Djojonegoro, B.M.1    Benedik, M.J.2    Wilson, R.C.3
  • 28
    • 0028835093 scopus 로고
    • Peptide phage libraries can be an efficient tool for identifying antibody ligands for polyclonal antisera
    • Dybwad A, Bogen B, Natvig JB, Foerre OE, Sioud M. 1995. Peptide phage libraries can be an efficient tool for identifying antibody ligands for polyclonal antisera. Clin. Exp. Immunol. 102:438-42
    • (1995) Clin. Exp. Immunol. , vol.102 , pp. 438-442
    • Dybwad, A.1    Bogen, B.2    Natvig, J.B.3    Foerre, O.E.4    Sioud, M.5
  • 29
    • 0029076741 scopus 로고
    • Phage display used for gene cloning of human recombinant antibody against the erythrocyte surface antigen, rhesus D
    • Dziegiel M, Nielsen LK, Andersen PS, Blancher A, Dickmeiss E, et al. 1995. Phage display used for gene cloning of human recombinant antibody against the erythrocyte surface antigen, rhesus D. J. Immunol. Methods 182:7-19
    • (1995) J. Immunol. Methods , vol.182 , pp. 7-19
    • Dziegiel, M.1    Nielsen, L.K.2    Andersen, P.S.3    Blancher, A.4    Dickmeiss, E.5
  • 30
    • 0029084673 scopus 로고
    • Macrocyclic peptidomimetics - Forcing peptides into bioactive conformations
    • Fairlie DP, Abbenante G, March DR. 1995. Macrocyclic peptidomimetics - forcing peptides into bioactive conformations. Curr. Med. Chem. 2:654-86
    • (1995) Curr. Med. Chem. , vol.2 , pp. 654-686
    • Fairlie, D.P.1    Abbenante, G.2    March, D.R.3
  • 31
    • 0027962645 scopus 로고
    • Two binding orientations for peptides to the Src SH3 domain: Development of a general model for SH3-ligand interactions
    • Feng S, Chen JK, Yu H, Simon JA, Schreiber SL. 1994. Two binding orientations for peptides to the Src SH3 domain: development of a general model for SH3-ligand interactions. Science 266:1241-47
    • (1994) Science , vol.266 , pp. 1241-1247
    • Feng, S.1    Chen, J.K.2    Yu, H.3    Simon, J.A.4    Schreiber, S.L.5
  • 32
    • 0028216366 scopus 로고
    • A general strategy to identify mimotopes of pathological antigens using only random peptide libraries and human sera
    • Folgori A, Tafi R, Meola A, Felici F, Galfré G, et al. 1994. A general strategy to identify mimotopes of pathological antigens using only random peptide libraries and human sera. EMBO J. 13:2236-43
    • (1994) EMBO J. , vol.13 , pp. 2236-2243
    • Folgori, A.1    Tafi, R.2    Meola, A.3    Felici, F.4    Galfré, G.5
  • 33
    • 0027994772 scopus 로고
    • Scanning whole cells with phage-display libraries: Identification of peptide ligands that modulate cell functions
    • Fong S, Doyle LV, Devlin JJ, Doyle MV. 1994. Scanning whole cells with phage-display libraries: identification of peptide ligands that modulate cell functions. Drug Dev. Res. 33:64-70
    • (1994) Drug Dev. Res. , vol.33 , pp. 64-70
    • Fong, S.1    Doyle, L.V.2    Devlin, J.J.3    Doyle, M.V.4
  • 34
    • 0028808005 scopus 로고
    • Screening of cyclic peptide phage libraries identifies ligands that bind streptavidin with high affinity
    • Giebel LB, Cass R, Milligan DL, Young D, Arze R, et al. 1995. Screening of cyclic peptide phage libraries identifies ligands that bind streptavidin with high affinity. Biochemistry 34:15430-35
    • (1995) Biochemistry , vol.34 , pp. 15430-15435
    • Giebel, L.B.1    Cass, R.2    Milligan, D.L.3    Young, D.4    Arze, R.5
  • 35
    • 0028277928 scopus 로고
    • High-affinity urokinase receptor antagonists identified with bacteriophage peptide display
    • Goodson RJ, Doyle MV, Kaufman SE, Rosenberg S. 1994. High-affinity urokinase receptor antagonists identified with bacteriophage peptide display. Proc. Natl. Acad. Sci. USA 91:7129-33
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 7129-7133
    • Goodson, R.J.1    Doyle, M.V.2    Kaufman, S.E.3    Rosenberg, S.4
  • 36
    • 0028886129 scopus 로고
    • A1, HPA-1a) form of platelet glycoprotein IIIa from a V gene phage display library
    • A1, HPA-1a) form of platelet glycoprotein IIIa from a V gene phage display library. Blood 86:4430-36
    • (1995) Blood , vol.86 , pp. 4430-4436
    • Griffin, H.M.1    Ouwehand, W.H.2
  • 37
    • 0027473684 scopus 로고
    • Human antiself antibodies with high specificity from phage display libraries
    • Griffiths AD, Malmqvist M, Marks JD, Bye JM, Embleton MJ, et al. 1993. Human antiself antibodies with high specificity from phage display libraries. EMBO J. 12:725-34
    • (1993) EMBO J. , vol.12 , pp. 725-734
    • Griffiths, A.D.1    Malmqvist, M.2    Marks, J.D.3    Bye, J.M.4    Embleton, M.J.5
  • 38
    • 0027185153 scopus 로고
    • Promiscuous and allele specific anchors in HLA-DR binding peptides
    • Hammer J, Valsasnin P, Tolba K, Bolin D, Higelin J, et al. 1993. Promiscuous and allele specific anchors in HLA-DR binding peptides. Cell 74:197-203
    • (1993) Cell , vol.74 , pp. 197-203
    • Hammer, J.1    Valsasnin, P.2    Tolba, K.3    Bolin, D.4    Higelin, J.5
  • 40
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin CH. 1995. Dimerization of cell surface receptors in signal transduction. Cell 80:213-23
    • (1995) Cell , vol.80 , pp. 213-223
    • Heldin, C.H.1
  • 41
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signalling in cell adhesion
    • Hynes RO. 1992. Integrins: versatility, modulation, and signalling in cell adhesion. Cell 69:11-25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 42
    • 0029170325 scopus 로고
    • Cloning of ligand-binding domains of bacterial receptors by phage display
    • Jacobsson K, Frykberg L. 1995. Cloning of ligand-binding domains of bacterial receptors by phage display. BioTechniques 18:878-85
    • (1995) BioTechniques , vol.18 , pp. 878-885
    • Jacobsson, K.1    Frykberg, L.2
  • 43
    • 0028227930 scopus 로고
    • In vitro selection of zinc fingers with altered DNA-binding specificity
    • Jamieson AC, Kim S-H, Wells JA. 1994. In vitro selection of zinc fingers with altered DNA-binding specificity. Biochemistry 33:5689-95
    • (1994) Biochemistry , vol.33 , pp. 5689-5695
    • Jamieson, A.C.1    Kim, S.-H.2    Wells, J.A.3
  • 44
    • 0030069683 scopus 로고    scopus 로고
    • Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides
    • Jardetzky TS, Brown JH, Gorga JC, Stern LJ, Urban RG, et al. 1996. Crystallographic analysis of endogenous peptides associated with HLA-DR1 suggests a common, polyproline II-like conformation for bound peptides. Proc. Natl. Acad. Sci. USA 93:734-38
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 734-738
    • Jardetzky, T.S.1    Brown, J.H.2    Gorga, J.C.3    Stern, L.J.4    Urban, R.G.5
  • 46
    • 0028841829 scopus 로고
    • Binding to protein targets of peptidic leads discovered by phage display: Crystal structures of streptavidin-bound linear and cyclic peptide ligands containing the HPQ sequence
    • Katz BA. 1995. Binding to protein targets of peptidic leads discovered by phage display: crystal structures of streptavidin-bound linear and cyclic peptide ligands containing the HPQ sequence. Biochemistry 34:15421-29
    • (1995) Biochemistry , vol.34 , pp. 15421-15429
    • Katz, B.A.1
  • 47
    • 0029990033 scopus 로고    scopus 로고
    • Preparation of a protein dimerizing ligand by topochemistry and structure-based design
    • Katz BA. 1996. Preparation of a protein dimerizing ligand by topochemistry and structure-based design. J. Am. Chem. Soc. 118:2355-56
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 2355-2356
    • Katz, B.A.1
  • 49
    • 0029152204 scopus 로고
    • Structure-based design of high affinity streptavidin binding cyclic peptides containing thioether cross-links
    • Katz BA, Johnson CR, Cass RT. 1995. Structure-based design of high affinity streptavidin binding cyclic peptides containing thioether cross-links. J. Am. Chem. Soc. 117:8541-47
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8541-8547
    • Katz, B.A.1    Johnson, C.R.2    Cass, R.T.3
  • 50
    • 0029830635 scopus 로고    scopus 로고
    • Structure-based design tools: Structural and thermodynamic comparison with biotin of a small molecule that binds to streptavidin with micromolar affinity
    • Katz BA, Liu B, Cass RT. 1996. Structure-based design tools: structural and thermodynamic comparison with biotin of a small molecule that binds to streptavidin with micromolar affinity. J. Am. Chem. Soc. 118:7914-7920
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 7914-7920
    • Katz, B.A.1    Liu, B.2    Cass, R.T.3
  • 51
    • 0029360353 scopus 로고
    • Topochemistry for preparing ligands that dimerize receptors
    • Katz BA, Stroud RM, Collins N, Liu B, Arze R. 1995. Topochemistry for preparing ligands that dimerize receptors. Chem. Biol. 2:591-600
    • (1995) Chem. Biol. , vol.2 , pp. 591-600
    • Katz, B.A.1    Stroud, R.M.2    Collins, N.3    Liu, B.4    Arze, R.5
  • 52
    • 0027298297 scopus 로고
    • Identification of HIV vaccine candidate peptides by screening random phage epitope libraries
    • Keller PM, Arnold BA, Shaw AR, Tolman RL, Van Middlesworth F, et al. 1993. Identification of HIV vaccine candidate peptides by screening random phage epitope libraries. Virology 193:709-16
    • (1993) Virology , vol.193 , pp. 709-716
    • Keller, P.M.1    Arnold, B.A.2    Shaw, A.R.3    Tolman, R.L.4    Van Middlesworth, F.5
  • 54
    • 0028899525 scopus 로고
    • Phage libraries displaying cyclic peptides with different ring sizes: Ligand specificities of the RGD-directed integrins
    • Koivunen E, Wang B, Ruoslahti E. 1995. Phage libraries displaying cyclic peptides with different ring sizes: ligand specificities of the RGD-directed integrins. BioTechnology 13:265-70
    • (1995) BioTechnology , vol.13 , pp. 265-270
    • Koivunen, E.1    Wang, B.2    Ruoslahti, E.3
  • 55
    • 0029033034 scopus 로고
    • Alternate protein frameworks for molecular recognition
    • Ku J, Schultz PG. 1995. Alternate protein frameworks for molecular recognition. Proc. Natl. Acad. Sci. USA 92:6552-56
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6552-6556
    • Ku, J.1    Schultz, P.G.2
  • 56
    • 0029041192 scopus 로고
    • Selection of peptide ligands for the antimucin core antibody C595 using phage display technology: Definition of candidate epitopes for a cancer vaccine
    • Laing P, Tighe P, Kwiatkowski E, Milligan J, Price M, et al. 1995. Selection of peptide ligands for the antimucin core antibody C595 using phage display technology: definition of candidate epitopes for a cancer vaccine. Clin. Mol. Pathol. 48:M136-41
    • (1995) Clin. Mol. Pathol. , vol.48
    • Laing, P.1    Tighe, P.2    Kwiatkowski, E.3    Milligan, J.4    Price, M.5
  • 58
    • 0029040809 scopus 로고
    • Random mutagenesis of staphylococcal nuclease and phage display selection
    • Light J, Lerner RA. 1995. Random mutagenesis of staphylococcal nuclease and phage display selection. Bioorg. Med. Chem. 3:955-67
    • (1995) Bioorg. Med. Chem. , vol.3 , pp. 955-967
    • Light, J.1    Lerner, R.A.2
  • 59
    • 0029798402 scopus 로고    scopus 로고
    • Functional mimicry of a protein hormone by a peptide agonist: The EPO receptor complex at 2.8 Å
    • Livnah O, Stura EA, Johnson DL, Middleton SA, Mulcahy LS, et al. 1996. Functional mimicry of a protein hormone by a peptide agonist: the EPO receptor complex at 2.8 Å. Science 273:464-71
    • (1996) Science , vol.273 , pp. 464-471
    • Livnah, O.1    Stura, E.A.2    Johnson, D.L.3    Middleton, S.A.4    Mulcahy, L.S.5
  • 60
    • 0030976150 scopus 로고    scopus 로고
    • Bacteriophage display and discovery of peptide leads
    • Lowman HB. 1997. Bacteriophage display and discovery of peptide leads. Annu. Rev. Biophys. Biomol. Struct. 26:XXX-XX
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26
    • Lowman, H.B.1
  • 61
    • 0029894775 scopus 로고    scopus 로고
    • Iterative optimization of high-affinity protease inhibitors using phage display. 2. Pasma kallikrein and thrombin
    • Markland W, Ley AC, Ladner RC. 1996. Iterative optimization of high-affinity protease inhibitors using phage display. 2. Pasma kallikrein and thrombin. Biochemistry 35:8058-67
    • (1996) Biochemistry , vol.35 , pp. 8058-8067
    • Markland, W.1    Ley, A.C.2    Ladner, R.C.3
  • 62
    • 0029953760 scopus 로고    scopus 로고
    • Iterative optimization of high-affinity protease inhibitors using phage display. 1. Pasmin
    • Markland W, Ley AC, Lee SW, Ladner RC. 1996. Iterative optimization of high-affinity protease inhibitors using phage display. 1. Pasmin. Biochemistry 35:8045-88057
    • (1996) Biochemistry , vol.35 , pp. 8045-88057
    • Markland, W.1    Ley, A.C.2    Lee, S.W.3    Ladner, R.C.4
  • 63
    • 0029994999 scopus 로고    scopus 로고
    • Coupling protein design and in vitro selection strategies. Improving specificity and affinity of a designed β-protein IL-6 antagonist
    • Martin F, Toniatti C, Salvati AL, Ciliberto G, Cortese R, et al. 1996. Coupling protein design and in vitro selection strategies. Improving specificity and affinity of a designed β-protein IL-6 antagonist. J. Mol. Biol. 255:86-97
    • (1996) J. Mol. Biol. , vol.255 , pp. 86-97
    • Martin, F.1    Toniatti, C.2    Salvati, A.L.3    Ciliberto, G.4    Cortese, R.5
  • 64
    • 0028592703 scopus 로고
    • An in vitro polysome display system for identifying ligands from very large peptide libraries
    • Mattheakis LC, Bhatt RR, Dower WJ. 1994. An in vitro polysome display system for identifying ligands from very large peptide libraries. Proc. Natl. Acad. Sci. USA 91:9022-26
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9022-9026
    • Mattheakis, L.C.1    Bhatt, R.R.2    Dower, W.J.3
  • 65
    • 0029120867 scopus 로고
    • Tendamistat as a scaffold for conformationally constrained phage peptide libraries
    • McConnell SJ, Hoess RH. 1995. Tendamistat as a scaffold for conformationally constrained phage peptide libraries. J. Mol. Biol. 250:460-70
    • (1995) J. Mol. Biol. , vol.250 , pp. 460-470
    • McConnell, S.J.1    Hoess, R.H.2
  • 66
    • 0028917153 scopus 로고
    • Derivation of vaccines from mimotopes. Immunologic properties of human hepatitis B virus surface antigen mimotopes displayed on filamentous phage
    • Meola A, Delmastro P, Monaci P, Luzzago A, Nicosia A, et al. 1995. Derivation of vaccines from mimotopes. Immunologic properties of human hepatitis B virus surface antigen mimotopes displayed on filamentous phage. J. Immunol. 154:3161-72
    • (1995) J. Immunol. , vol.154 , pp. 3161-3172
    • Meola, A.1    Delmastro, P.2    Monaci, P.3    Luzzago, A.4    Nicosia, A.5
  • 67
    • 0029102175 scopus 로고
    • Phage display: Protein engineering by directed evolution. Curr
    • O'Neil K, Hoess RH. 1995. Phage display: protein engineering by directed evolution. Curr. Opin. Struct. Biol. 5:443-49
    • (1995) Opin. Struct. Biol. , vol.5 , pp. 443-449
    • O'Neil, K.1    Hoess, R.H.2
  • 68
    • 0029058337 scopus 로고
    • Protection against HIV-1 infection in hu-PBL-SCID mice by passive immunization with a neutralizing monoclonal antibody against the gp120 CD4-binding site
    • Parren PW, Ditzel HJ, Gulizia RJ, Binley JM, Barbas III CF, et al. 1995. Protection against HIV-1 infection in hu-PBL-SCID mice by passive immunization with a neutralizing monoclonal antibody against the gp120 CD4-binding site. AIDS 9:F1-6
    • (1995) AIDS , vol.9
    • Parren, P.W.1    Ditzel, H.J.2    Gulizia, R.J.3    Binley, J.M.4    Barbas III, C.F.5
  • 69
    • 0029120428 scopus 로고
    • A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins
    • Pasqualini R, Koivunen E, Ruoslahti E. 1995. A peptide isolated from phage display libraries is a structural and functional mimic of an RGD-binding site on integrins. J. Cell Biol. 130:1189-96
    • (1995) J. Cell Biol. , vol.130 , pp. 1189-1196
    • Pasqualini, R.1    Koivunen, E.2    Ruoslahti, E.3
  • 70
    • 0029932458 scopus 로고    scopus 로고
    • Organ targeting in vivo using phage display peptide libraries
    • Pasqualini R, Ruoslahti E. 1996. Organ targeting in vivo using phage display peptide libraries. Nature 380:364-66
    • (1996) Nature , vol.380 , pp. 364-366
    • Pasqualini, R.1    Ruoslahti, E.2
  • 71
    • 0025773296 scopus 로고
    • Zinc finger-DNA recognition: Crystal structure of a Zif268-DNA complex at 2.1 Å
    • Pavletich N, Pabo CO. 1991. Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 Å. Science 252:809-17
    • (1991) Science , vol.252 , pp. 809-817
    • Pavletich, N.1    Pabo, C.O.2
  • 73
    • 0029960032 scopus 로고    scopus 로고
    • Antibody engineering of recombinant Fv immunotoxins for improved targeting of cancer: Disulfide-stabilized Fv immunotoxins
    • Reiter Y, Pastan I. 1996. Antibody engineering of recombinant Fv immunotoxins for improved targeting of cancer: disulfide-stabilized Fv immunotoxins. Clin. Cancer Res. 2:245-52
    • (1996) Clin. Cancer Res. , vol.2 , pp. 245-252
    • Reiter, Y.1    Pastan, I.2
  • 74
    • 0028333754 scopus 로고
    • Synthetic peptide ligands of the antigen-binding receptor induce programmed cell death in a human B-cell lymphoma
    • Renschler MF, Bhatt RR, Dower WJ, Levy R. 1994. Synthetic peptide ligands of the antigen-binding receptor induce programmed cell death in a human B-cell lymphoma. Proc. Natl. Acad. Sci. USA 91:3623-27
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3623-3627
    • Renschler, M.F.1    Bhatt, R.R.2    Dower, W.J.3    Levy, R.4
  • 75
    • 0028811162 scopus 로고
    • Phage display selection of ligand residues important for Src homology domain binding specificity
    • Rickles RJ, Botfield MC, Zhou X-M, Henry PA, Brugge JS, et al. 1995. Phage display selection of ligand residues important for Src homology domain binding specificity. Proc. Natl. Acad. Sci. USA 92:10909-13
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10909-10913
    • Rickles, R.J.1    Botfield, M.C.2    Zhou, X.-M.3    Henry, P.A.4    Brugge, J.S.5
  • 76
    • 0029978501 scopus 로고    scopus 로고
    • p53 as a target for cancer vaccines: Recombinant canarypox virus vectors expressing p53 protect mice against lethal tumor cell challenge
    • Roth J, Dittmer D, Rea D, Tartaglia J, Paoletti E, et al. 1996. p53 as a target for cancer vaccines: recombinant canarypox virus vectors expressing p53 protect mice against lethal tumor cell challenge. Proc. Natl. Acad. Sci. USA 93:4781-86
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4781-4786
    • Roth, J.1    Dittmer, D.2    Rea, D.3    Tartaglia, J.4    Paoletti, E.5
  • 77
    • 0029005234 scopus 로고
    • CNTF variants with increased biological potency and receptor selectivity define a functional site of receptor interaction
    • Saggio I, Gloaguen I, Poiana G, Laufer R. 1995. CNTF variants with increased biological potency and receptor selectivity define a functional site of receptor interaction. EMBO J. 14:3045-54
    • (1995) EMBO J. , vol.14 , pp. 3045-3054
    • Saggio, I.1    Gloaguen, I.2    Poiana, G.3    Laufer, R.4
  • 78
    • 0029989324 scopus 로고    scopus 로고
    • Isolation of high-affinity monomeric human anti-c-erbb2 single chain Fv using affinity-driven selection
    • Schier R, Bye J, Apell G, McCall A, Adams GP, et al. 1996. Isolation of high-affinity monomeric human anti-c-erbb2 single chain Fv using affinity-driven selection. J. Mol. Biol. 255:28-43
    • (1996) J. Mol. Biol. , vol.255 , pp. 28-43
    • Schier, R.1    Bye, J.2    Apell, G.3    McCall, A.4    Adams, G.P.5
  • 81
    • 0028845856 scopus 로고
    • Contribution of antibody heavy chain CDR1 to digoxin binding analyzed by random mutagenesis of phage-displayed Fab 26-10
    • Short MK, Jeffrey PD, Kwong R-F, Margolies MN. 1995. Contribution of antibody heavy chain CDR1 to digoxin binding analyzed by random mutagenesis of phage-displayed Fab 26-10. J. Biol. Chem. 270:28541-50
    • (1995) J. Biol. Chem. , vol.270 , pp. 28541-28550
    • Short, M.K.1    Jeffrey, P.D.2    Kwong, R.-F.3    Margolies, M.N.4
  • 82
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith GP. 1985. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science 228:1315-17
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 83
    • 0028918852 scopus 로고
    • Rapid identification of highly active and selective substrates for stromelysin and matrilysin using bacteriophage peptide display libraries
    • Smith MM, Shi L, Navre M. 1995. Rapid identification of highly active and selective substrates for stromelysin and matrilysin using bacteriophage peptide display libraries. J. Biol. Chem. 270:6440-49
    • (1995) J. Biol. Chem. , vol.270 , pp. 6440-6449
    • Smith, M.M.1    Shi, L.2    Navre, M.3
  • 84
    • 0028915250 scopus 로고
    • Characterization of epitopes on human p53 using phage-displayed peptide libraries: Insights into antibody-peptide interactions
    • Stephen CW, Helminen P, Lane DP. 1995. Characterization of epitopes on human p53 using phage-displayed peptide libraries: insights into antibody-peptide interactions. J. Mol. Biol. 248:58-78
    • (1995) J. Mol. Biol. , vol.248 , pp. 58-78
    • Stephen, C.W.1    Helminen, P.2    Lane, D.P.3
  • 85
    • 0028907327 scopus 로고
    • Display of peptides and proteins on the surface of bacteriophage λ
    • Sternberg N, Hoess RH. 1995. Display of peptides and proteins on the surface of bacteriophage λ. Proc. Natl. Acad. Sci. USA 92:1609-13
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1609-1613
    • Sternberg, N.1    Hoess, R.H.2
  • 86
    • 0028217202 scopus 로고
    • The crystal structure of affinity-matured human growth hormone at 2 A resolution
    • Ultsch MH, Somers W, Kossiakoff AA, de Vos AM. 1994. The crystal structure of affinity-matured human growth hormone at 2 A resolution. J. Mol. Biol. 236:286-99
    • (1994) J. Mol. Biol. , vol.236 , pp. 286-299
    • Ultsch, M.H.1    Somers, W.2    Kossiakoff, A.A.3    De Vos, A.M.4
  • 87
    • 0029986456 scopus 로고    scopus 로고
    • Selective screening of a large phage display library of plasminogen activator inhibitor 1 mutants to localize interaction sites with either thrombin or the variable region 1 of tissue-type plasminogen activator
    • Van Meijer M, Roelofs Y, Neels J, Horrevoets AJG, Van Zonneveld A-J, et al. 1996. Selective screening of a large phage display library of plasminogen activator inhibitor 1 mutants to localize interaction sites with either thrombin or the variable region 1 of tissue-type plasminogen activator. J. Biol. Chem. 271:7423-28
    • (1996) J. Biol. Chem. , vol.271 , pp. 7423-7428
    • Van Meijer, M.1    Roelofs, Y.2    Neels, J.3    Horrevoets, A.J.G.4    Van Zonneveld, A.-J.5
  • 88
    • 0029020237 scopus 로고
    • Isolation of a high affinity inhibitor of urokinase-type plasminogen activator by phage display of ecotin
    • Wang C-I, Yang Q, Craik CS. 1995. Isolation of a high affinity inhibitor of urokinase-type plasminogen activator by phage display of ecotin. J. Biol. Chem. 270:12250-56
    • (1995) J. Biol. Chem. , vol.270 , pp. 12250-12256
    • Wang, C.-I.1    Yang, Q.2    Craik, C.S.3
  • 89
    • 0028332086 scopus 로고
    • Activation and inhibition of erythropoeitin receptor function: Role of receptor dimerization
    • Watowich SS, Hilton DJ, Lodish HF. 1994. Activation and inhibition of erythropoeitin receptor function: role of receptor dimerization. Mol. Cell. Biol. 14:3535-49
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3535-3549
    • Watowich, S.S.1    Hilton, D.J.2    Lodish, H.F.3
  • 90
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • Wells JA. 1996. Binding in the growth hormone receptor complex. Proc. Natl. Acad. Sci. USA. 93:1-6
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1-6
    • Wells, J.A.1
  • 91
    • 0029008514 scopus 로고
    • Glutathione transferases with novel active sites isolated by phage display from a library of random mutants
    • Widersten M, Mannervik B. 1995. Glutathione transferases with novel active sites isolated by phage display from a library of random mutants. J. Mol. Biol. 250:115-22
    • (1995) J. Mol. Biol. , vol.250 , pp. 115-122
    • Widersten, M.1    Mannervik, B.2
  • 93
    • 0028001658 scopus 로고
    • Bacteriophage display: Peptide libraries and drug discovery
    • Winter J. 1994. Bacteriophage display: peptide libraries and drug discovery. Drug Dev. Res. 33:71-89
    • (1994) Drug Dev. Res. , vol.33 , pp. 71-89
    • Winter, J.1
  • 94
    • 0028861262 scopus 로고
    • Binding epitope of somatostatin defined by phage-displayed peptide libraries
    • Wright RM, Gram H, Vattay A, Byrne S, Lake P, et al. 1995. Binding epitope of somatostatin defined by phage-displayed peptide libraries. Bio-Technology 13:165-69
    • (1995) Bio-Technology , vol.13 , pp. 165-169
    • Wright, R.M.1    Gram, H.2    Vattay, A.3    Byrne, S.4    Lake, P.5
  • 95
    • 9444236174 scopus 로고    scopus 로고
    • Small peptides as potent mimetics of the protein hormone erythropoietin
    • Wrighton NC, Farrell FX, Chang R, Kashyap AK, Barbone FP, et al. 1996. Small peptides as potent mimetics of the protein hormone erythropoietin. Science 273:458-63
    • (1996) Science , vol.273 , pp. 458-463
    • Wrighton, N.C.1    Farrell, F.X.2    Chang, R.3    Kashyap, A.K.4    Barbone, F.P.5
  • 96
    • 0028888530 scopus 로고
    • Building zinc fingers by selection: Toward a therapeutic application
    • Wu H, Yang WP, Barbas III CF. 1995. Building zinc fingers by selection: toward a therapeutic application. Proc. Natl. Acad. Sci. USA 92:344-48
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 344-348
    • Wu, H.1    Yang, W.P.2    Barbas III, C.F.3
  • 97
    • 0029128117 scopus 로고
    • Affinity maturation of the BR96 anti-carcinoma antibody by codon-based mutagenesis
    • Yelton DE, Rosok MJ, Cruz G, Cosand WL, Bajorath J, et al. 1995. Affinity maturation of the BR96 anti-carcinoma antibody by codon-based mutagenesis. J. Immunol. 155:1994-2004
    • (1995) J. Immunol. , vol.155 , pp. 1994-2004
    • Yelton, D.E.1    Rosok, M.J.2    Cruz, G.3    Cosand, W.L.4    Bajorath, J.5
  • 98
    • 0028231880 scopus 로고
    • Structure of a single-chain antibody variable domain (Fv) fragment complexes with a carbohydrate antigen at 1.7 Å resolution
    • Zdanov A, Li Y, Bundle DR, Deng S-J, MacKenzie R, et al. 1994. Structure of a single-chain antibody variable domain (Fv) fragment complexes with a carbohydrate antigen at 1.7 Å resolution. Proc. Natl. Acad. Sci. USA 91:6423-27
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 6423-6427
    • Zdanov, A.1    Li, Y.2    Bundle, D.R.3    Deng, S.-J.4    MacKenzie, R.5


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