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Volumn 9, Issue 1, 1998, Pages 102-108

Strategies for selection of antibodies by phage display

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY;

EID: 0031933840     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0958-1669(98)80092-X     Document Type: Article
Times cited : (222)

References (64)
  • 1
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith GP. Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface. Science. 228:1985;1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 2
    • 0025226085 scopus 로고
    • Phage antibodies: Filamentous phage displaying antibody variable domains
    • McCafferty J, Griffiths AD, Winter G, Chiswell DJ. Phage antibodies: filamentous phage displaying antibody variable domains. Nature. 348:1990;552-554.
    • (1990) Nature , vol.348 , pp. 552-554
    • McCafferty, J.1    Griffiths, A.D.2    Winter, G.3    Chiswell, D.J.4
  • 4
    • 0031081318 scopus 로고    scopus 로고
    • Designing and optimizing library selection strategies for generating high-affinity antibodies
    • Hoogenboom HR. Designing and optimizing library selection strategies for generating high-affinity antibodies. Trends Biotechnol. 15:1997;62-70.
    • (1997) Trends Biotechnol , vol.15 , pp. 62-70
    • Hoogenboom, H.R.1
  • 5
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom HR, Griffiths AD, Johnson KS, Chiswell DJ, Hudson P, Winter G. Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res. 19:1991;4133-4137.
    • (1991) Nucleic Acids Res , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 8
    • 0025838021 scopus 로고
    • Assembly of combinatorial antibody libraries on phage surfaces: The gene III site
    • Barbas CF, Kang AS, Lerner RA, Benkovic SJ. Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc Natl Acad Sci USA. 88:1991;7978-7982.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7978-7982
    • Barbas, C.F.1    Kang, A.S.2    Lerner, R.A.3    Benkovic, S.J.4
  • 9
    • 0025718897 scopus 로고
    • Expression of antibody Fab domains on bacteriophage surfaces
    • Chang CN, Landolfi NF, Queen C. Expression of antibody Fab domains on bacteriophage surfaces. J Immunol. 147:1991;3610-3614.
    • (1991) J Immunol , vol.147 , pp. 3610-3614
    • Chang, C.N.1    Landolfi, N.F.2    Queen, C.3
  • 10
    • 0025910746 scopus 로고
    • Linkage of recognition and replication functions by assembling combinatorial antibody Fab libraries along phage surfaces
    • Kang AS, Barbas CF, Janda KD, Benkovic SJ, Lerner RA. Linkage of recognition and replication functions by assembling combinatorial antibody Fab libraries along phage surfaces. Proc Natl Acad Sci USA. 88:1991;4363-4366.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4363-4366
    • Kang, A.S.1    Barbas, C.F.2    Janda, K.D.3    Benkovic, S.J.4    Lerner, R.A.5
  • 11
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • Vieira J, Messing J. Production of single-stranded plasmid DNA. Methods Enzymol. 153:1987;3-11.
    • (1987) Methods Enzymol , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2
  • 13
    • 0030667838 scopus 로고    scopus 로고
    • Filamentous phage infection-mediated gene expression: Construction and propagation of the gIII deletion mutant helper phage R408d3
    • Rakonjac J, Jovanovic G, Model P. Filamentous phage infection-mediated gene expression: construction and propagation of the gIII deletion mutant helper phage R408d3. Gene. 198:1997;99-103.
    • (1997) Gene , vol.198 , pp. 99-103
    • Rakonjac, J.1    Jovanovic, G.2    Model, P.3
  • 14
    • 0027197493 scopus 로고
    • 'Diabodies': Small bivalent and bispecific antibody fragments
    • Holliger P, Prospero T, Winter G. 'Diabodies': small bivalent and bispecific antibody fragments. Proc Natl Acad Sci USA. 90:1993;6444-6448.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 6444-6448
    • Holliger, P.1    Prospero, T.2    Winter, G.3
  • 16
    • 0030610418 scopus 로고    scopus 로고
    • The 2.0-Å resolution crystal structure of a trimeric antibody fragment with noncognate VH-VL domain pairs shows a rearrangement of VH CDR3
    • Pei XY, Holliger P, Murzin AG, Williams RL. The 2.0-Å resolution crystal structure of a trimeric antibody fragment with noncognate VH-VL domain pairs shows a rearrangement of VH CDR3. Proc Natl Acad Sci USA. 94:1997;9637-9642.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9637-9642
    • Pei, X.Y.1    Holliger, P.2    Murzin, A.G.3    Williams, R.L.4
  • 17
    • 0030748513 scopus 로고    scopus 로고
    • Triabodies: Single chain Fv fragments without a linker form trivalent trimers
    • Iliades P, Kortt AA, Hudson PJ. Triabodies: single chain Fv fragments without a linker form trivalent trimers. FEBS Lett. 409:1997;437-441.
    • (1997) FEBS Lett , vol.409 , pp. 437-441
    • Iliades, P.1    Kortt, A.A.2    Hudson, P.J.3
  • 18
    • 0029932582 scopus 로고    scopus 로고
    • Specific killing of lymphoma cells by cytotoxic T-cells mediated by a bispecific diabody
    • Holliger P, Brissinck J, Williams RL, Thielemans K, Winter G. Specific killing of lymphoma cells by cytotoxic T-cells mediated by a bispecific diabody. Protein Eng. 9:1996;299-305.
    • (1996) Protein Eng , vol.9 , pp. 299-305
    • Holliger, P.1    Brissinck, J.2    Williams, R.L.3    Thielemans, K.4    Winter, G.5
  • 20
    • 0030743802 scopus 로고    scopus 로고
    • Complement recruitment using bispecific diabodies
    • Kontermann RE, Wing MG, Winter G. Complement recruitment using bispecific diabodies. Nat Biotechnol. 15:1997;629-631.
    • (1997) Nat Biotechnol , vol.15 , pp. 629-631
    • Kontermann, R.E.1    Wing, M.G.2    Winter, G.3
  • 21
    • 0030909820 scopus 로고    scopus 로고
    • Remodeling domain interfaces to enhance heterodimer formation
    • Zhu Z, Presta LG, Zapata G, Carter P. Remodeling domain interfaces to enhance heterodimer formation. Protein Sci. 6:1997;781-788.
    • (1997) Protein Sci , vol.6 , pp. 781-788
    • Zhu, Z.1    Presta, L.G.2    Zapata, G.3    Carter, P.4
  • 24
    • 0025838698 scopus 로고
    • A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals
    • Burton DR, Barbas C III, Persson M, Koenig S, Chanock RM, Lerner RA. A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals. Proc Natl Acad Sci USA. 88:1991;10134-10137.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10134-10137
    • Burton, D.R.1    Barbas C. III2    Persson, M.3    Koenig, S.4    Chanock, R.M.5    Lerner, R.A.6
  • 26
    • 0344035202 scopus 로고    scopus 로고
    • Immunoglobulin genes
    • P.J. Delves, Roitt I. 2 London: Academic Press
    • Tomlinson IM. Immunoglobulin genes. Delves PJ, Roitt I. 2 Encyclopedia of Immunology. 1998;Academic Press, London.
    • (1998) Encyclopedia of Immunology
    • Tomlinson, I.M.1
  • 27
    • 0030200088 scopus 로고    scopus 로고
    • Selection and evolution of high-affinity human anti-viral antibodies
    • Barbas C III, Burton DR. Selection and evolution of high-affinity human anti-viral antibodies. Trends Biotechnol. 14:1996;230-234.
    • (1996) Trends Biotechnol , vol.14 , pp. 230-234
    • Barbas C. III1    Burton, D.R.2
  • 28
    • 0030152049 scopus 로고    scopus 로고
    • Characteristics of human antibody repertoires following active immune responses in vivo
    • Ohlin M, Borrebaeck CA. Characteristics of human antibody repertoires following active immune responses in vivo. Mol Immunol. 33:1996;583-592.
    • (1996) Mol Immunol , vol.33 , pp. 583-592
    • Ohlin, M.1    Borrebaeck, C.A.2
  • 30
    • 0031568670 scopus 로고    scopus 로고
    • Human anti-nicotinic acetylcholine receptor recombinant Fab fragments isolated from thymus-derived phage display libraries from myasthenia gravis patients reflect predominant specificities in serum and block the action of pathogenic serum antibodies
    • Graus YF, de Baets MH, Parren PW, Berrih AS, Wokke J, van Breda Vriesman PJ, Burton DR. Human anti-nicotinic acetylcholine receptor recombinant Fab fragments isolated from thymus-derived phage display libraries from myasthenia gravis patients reflect predominant specificities in serum and block the action of pathogenic serum antibodies. J Immunol. 158:1997;1919-1929.
    • (1997) J Immunol , vol.158 , pp. 1919-1929
    • Graus, Y.F.1    De Baets, M.H.2    Parren, P.W.3    Berrih, A.S.4    Wokke, J.5    Van Breda Vriesman, P.J.6    Burton, D.R.7
  • 33
    • 0029950801 scopus 로고    scopus 로고
    • Recombinant rabbit Fab with binding activity to type-1 plasminogen activator inhibitor derived from a phage-display library against human alpha-granules
    • Lang IM, Barbas C III, Schleef RR. Recombinant rabbit Fab with binding activity to type-1 plasminogen activator inhibitor derived from a phage-display library against human alpha-granules. Gene. 172:1996;295-298.
    • (1996) Gene , vol.172 , pp. 295-298
    • Lang, I.M.1    Barbas C. III2    Schleef, R.R.3
  • 34
    • 0028825910 scopus 로고
    • Selection of specific phage-display antibodies using libraries derived from chicken immunoglobulin genes
    • Davies EL, Smith JS, Birkett CR, Manser JM, Anderson DD, Young JR. Selection of specific phage-display antibodies using libraries derived from chicken immunoglobulin genes. J Immunol Methods. 186:1995;125-135.
    • (1995) J Immunol Methods , vol.186 , pp. 125-135
    • Davies, E.L.1    Smith, J.S.2    Birkett, C.R.3    Manser, J.M.4    Anderson, D.D.5    Young, J.R.6
  • 35
    • 0030210311 scopus 로고    scopus 로고
    • Chicken monoclonal antibody isolated by a phage display system
    • Yamanaka HI, Inoue T, Ikeda TO. Chicken monoclonal antibody isolated by a phage display system. J Immunol. 157:1996;1156-1162.
    • (1996) J Immunol , vol.157 , pp. 1156-1162
    • Yamanaka, H.I.1    Inoue, T.2    Ikeda, T.O.3
  • 36
    • 9344223986 scopus 로고    scopus 로고
    • Human antibodies with sub-nanomolar affinities isolated from a large non-immunized phage display library
    • 10 clone) naive scFv phage library is constructed from V-genes of 43 non-immunised human donors and used to rapidly recover nanomolar and sub-nanomolar affinity antibodies to multiple haptens and protein antigens.
    • 10 clone) naive scFv phage library is constructed from V-genes of 43 non-immunised human donors and used to rapidly recover nanomolar and sub-nanomolar affinity antibodies to multiple haptens and protein antigens.
    • (1996) Nat Biotechnol , vol.14 , pp. 309-314
    • Vaughan, T.J.1    Williams, A.J.2    Pritchard, K.3    Osbourn, J.K.4    Pope, A.R.5    Earnshaw, J.C.6    McCafferty, J.7    Hodits, R.A.8    Wilton, J.9    Johnson, K.10
  • 38
    • 0026673067 scopus 로고
    • By-passing immunisation: Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro
    • Hoogenboom HR, Winter G. By-passing immunisation: human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro. J Mol Biol. 227:1992;381-388.
    • (1992) J Mol Biol , vol.227 , pp. 381-388
    • Hoogenboom, H.R.1    Winter, G.2
  • 40
    • 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. 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. 248:1995;97-105.
    • (1995) J Mol Biol , vol.248 , pp. 97-105
    • De Kruif, J.1    Boel, E.2    Logtenberg, T.3
  • 41
    • 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. Rapid selection of cell subpopulation-specific human monoclonal antibodies from a synthetic phage antibody library. Proc Natl Acad Sci USA. 92:1995;3938-3942.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3938-3942
    • De Kruif, J.1    Terstappen, L.2    Boel, E.3    Logtenberg, T.4
  • 43
    • 0029876546 scopus 로고    scopus 로고
    • Characterization of human variable domain antibody fragments against the U1 RNA-associated A protein, selected from a synthetic and patient-derived combinatorial V gene library
    • de Wildt R, Finnern R, Ouwehand WH, Griffiths AD, van Venrooij W, Hoet RM. Characterization of human variable domain antibody fragments against the U1 RNA-associated A protein, selected from a synthetic and patient-derived combinatorial V gene library. Eur J Immunol. 26:1996;629-639.
    • (1996) Eur J Immunol , vol.26 , pp. 629-639
    • De Wildt, R.1    Finnern, R.2    Ouwehand, W.H.3    Griffiths, A.D.4    Van Venrooij, W.5    Hoet, R.M.6
  • 44
    • 0030237274 scopus 로고    scopus 로고
    • Human recombinant antibody fragments specific for a rye-grass pollen allergen: Characterization and potential applications
    • de Lalla C, Tamborini E, Longhi R, Tresoldi E, Manoni M, Siccardi AG, Arosio P, Sidoli A. Human recombinant antibody fragments specific for a rye-grass pollen allergen: characterization and potential applications. Mol Immunol. 33:1996;1049-1058.
    • (1996) Mol Immunol , vol.33 , pp. 1049-1058
    • De Lalla, C.1    Tamborini, E.2    Longhi, R.3    Tresoldi, E.4    Manoni, M.5    Siccardi, A.G.6    Arosio, P.7    Sidoli, A.8
  • 45
    • 0031564066 scopus 로고    scopus 로고
    • Characterization of events during the late stages of HPV 16 infection in vivo using high-affinity synthetic Fabs to E4
    • of special interest. An interesting example of a high affinity (1.0 nM) Fab, isolated directly from a synthetic phage antibody library, being used in basic research; in this case to characterise events in papillomavirus infection.
    • Doorbar J, Foo C, Colman N, Medcalf L, Hartley O, Prospero T, Napthiene S, Stirling J, Winter G, Griffin H. Characterization of events during the late stages of HPV 16 infection in vivo using high-affinity synthetic Fabs to E4. of special interest Virology. 238:1997;40-52 An interesting example of a high affinity (1.0 nM) Fab, isolated directly from a synthetic phage antibody library, being used in basic research; in this case to characterise events in papillomavirus infection.
    • (1997) Virology , vol.238 , pp. 40-52
    • Doorbar, J.1    Foo, C.2    Colman, N.3    Medcalf, L.4    Hartley, O.5    Prospero, T.6    Napthiene, S.7    Stirling, J.8    Winter, G.9    Griffin, H.10
  • 46
    • 0030803049 scopus 로고    scopus 로고
    • Direct demonstration of MuSK involvement in acetycholine receptor clustering through identification of agonist ScFv
    • of outstanding interest. A titilating example of how antibodies with agonist activity can be derived by phage display. Potentially, agonists can yield much information about receptor biology. In this case the antibodies with receptor agonist activity (against MuSK) are selected directly from a large naive library.
    • Xie M-H, Yuan J, Adams C, Gurney A. Direct demonstration of MuSK involvement in acetycholine receptor clustering through identification of agonist ScFv. of outstanding interest Nat Biotechnol. 15:1997;768-771 A titilating example of how antibodies with agonist activity can be derived by phage display. Potentially, agonists can yield much information about receptor biology. In this case the antibodies with receptor agonist activity (against MuSK) are selected directly from a large naive library.
    • (1997) Nat Biotechnol , vol.15 , pp. 768-771
    • Xie M-H1    Yuan, J.2    Adams, C.3    Gurney, A.4
  • 48
    • 0029564921 scopus 로고
    • CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range
    • Yang WP, Green K, Pinz SS, Briones AT, Burton DR, Barbas C III. CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range. J Mol Biol. 254:1995;392-403.
    • (1995) J Mol Biol , vol.254 , pp. 392-403
    • Yang, W.P.1    Green, K.2    Pinz, S.S.3    Briones, A.T.4    Burton, D.R.5    Barbas C. III6
  • 50
    • 0028348564 scopus 로고
    • In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity
    • Barbas CF, Hu D, Dunlop N, Sawyer L, Cababa D, Hendry RM, Nara PL, Burton DR. In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity. Proc Natl Acad Sci USA. 91:1994;3809-3813.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 3809-3813
    • Barbas, C.F.1    Hu, D.2    Dunlop, N.3    Sawyer, L.4    Cababa, D.5    Hendry, R.M.6    Nara, P.L.7    Burton, D.R.8
  • 51
    • 0029961133 scopus 로고    scopus 로고
    • The imprint of somatic hypermutation on the repertoire of human germline V genes
    • of special interest. A comprehensive study of the human antibody response showing that initially diversity is focused at the centre of the binding site, but somatic hypermutation spreads diversity to regions at the periphery of the binding site that are highly conserved in the primary repertoire.
    • Tomlinson IM, Walter G, Jones PT, Dear PH, Sonnhammer EL, Winter G. The imprint of somatic hypermutation on the repertoire of human germline V genes. of special interest J Mol Biol. 256:1996;813-817 A comprehensive study of the human antibody response showing that initially diversity is focused at the centre of the binding site, but somatic hypermutation spreads diversity to regions at the periphery of the binding site that are highly conserved in the primary repertoire.
    • (1996) J Mol Biol , vol.256 , pp. 813-817
    • Tomlinson, I.M.1    Walter, G.2    Jones, P.T.3    Dear, P.H.4    Sonnhammer, E.L.5    Winter, G.6
  • 52
    • 0031586002 scopus 로고    scopus 로고
    • The creation of diversity in the human immunoglobulin V(lambda) repertoire
    • Ignatovich O, Tomlinson IM, Jones PT, Winter G. The creation of diversity in the human immunoglobulin V(lambda) repertoire. J Mol Biol. 268:1997;69-77.
    • (1997) J Mol Biol , vol.268 , pp. 69-77
    • Ignatovich, O.1    Tomlinson, I.M.2    Jones, P.T.3    Winter, G.4
  • 53
    • 0028223378 scopus 로고
    • In vitro selection from protein and peptide libraries
    • Clackson T, Wells JA. In vitro selection from protein and peptide libraries. Trends Biotechnol. 12:1994;173-184.
    • (1994) Trends Biotechnol , vol.12 , pp. 173-184
    • Clackson, T.1    Wells, J.A.2
  • 54
    • 0027082901 scopus 로고
    • Antibody engineering by codon-based mutagenesis in a filamentous phage system
    • Glaser SM, Yelton DE, Huse WD. Antibody engineering by codon-based mutagenesis in a filamentous phage system. J Immunol. 149:1992;3903-3913.
    • (1992) J Immunol , vol.149 , pp. 3903-3913
    • Glaser, S.M.1    Yelton, D.E.2    Huse, W.D.3
  • 55
    • 0028559783 scopus 로고
    • Trinucleotide phosphoramidites: Ideal reagents for the synthesis of mixed oligonucleotides for random mutagenesis
    • Virnekas B, Ge L, Pluckthun A, Schneider KC, Wellnhofer G, Moroney SE. Trinucleotide phosphoramidites: ideal reagents for the synthesis of mixed oligonucleotides for random mutagenesis. Nucleic Acids Res. 22:1994;5600-5607.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5600-5607
    • Virnekas, B.1    Ge, L.2    Pluckthun, A.3    Schneider, K.C.4    Wellnhofer, G.5    Moroney, S.E.6
  • 56
    • 0027761151 scopus 로고
    • Antibody engineering by parsimonious mutagenesis
    • Balint RF, Larrick JW. Antibody engineering by parsimonious mutagenesis. Gene. 137:1993;109-118.
    • (1993) Gene , vol.137 , pp. 109-118
    • Balint, R.F.1    Larrick, J.W.2
  • 57
    • 0029881373 scopus 로고    scopus 로고
    • Identification of functional and structural amino-acid residues by parsimonious mutagenesis
    • Schier R, Balint RF, McCall A, Apell G, Larrick JW, Marks JD. Identification of functional and structural amino-acid residues by parsimonious mutagenesis. Gene. 169:1996;147-155.
    • (1996) Gene , vol.169 , pp. 147-155
    • Schier, R.1    Balint, R.F.2    McCall, A.3    Apell, G.4    Larrick, J.W.5    Marks, J.D.6
  • 58
    • 0026699293 scopus 로고
    • Selection of phage antibodies by binding affinity. Mimicking affinity maturation
    • Hawkins RE, Russell SJ, Winter G. Selection of phage antibodies by binding affinity. Mimicking affinity maturation. J Mol Biol. 226:1992;889-896.
    • (1992) J Mol Biol , vol.226 , pp. 889-896
    • Hawkins, R.E.1    Russell, S.J.2    Winter, G.3
  • 59
    • 0005229135 scopus 로고    scopus 로고
    • Mimicking somatic hypermutation: Affinity maturation of antibodies displayed on bacteriophage using a bacterial mutator strain
    • of special interest. In a process that closely mimics the somatic hypermutation in B-cells, an anti-hapten antibody was affinity matured 100-fold by propagating phage in a mutator strain (E. coli mutD5) between selection.
    • Low NM, Holliger PH, Winter G. Mimicking somatic hypermutation: affinity maturation of antibodies displayed on bacteriophage using a bacterial mutator strain. of special interest J Mol Biol. 260:1996;359-368 In a process that closely mimics the somatic hypermutation in B-cells, an anti-hapten antibody was affinity matured 100-fold by propagating phage in a mutator strain (E. coli mutD5) between selection.
    • (1996) J Mol Biol , vol.260 , pp. 359-368
    • Low, N.M.1    Holliger, P.H.2    Winter, G.3
  • 60
    • 0030485173 scopus 로고    scopus 로고
    • Efficient in vitro affinity maturation of phage antibodies using BIAcore guided selections
    • Schier R, Marks JD. Efficient in vitro affinity maturation of phage antibodies using BIAcore guided selections. Hum Antibodies Hybridomas. 7:1996;97-105.
    • (1996) Hum Antibodies Hybridomas , vol.7 , pp. 97-105
    • Schier, R.1    Marks, J.D.2
  • 63
    • 0031908473 scopus 로고    scopus 로고
    • Pathfinder selection: In situ isolation of novel antibodies
    • of outstanding interest. A technique using a ligand or antibody-peroxidase conjugate to direct the deposition of biotin-tyramine free radicals within a very local area. Phage antibodies binding close by will be biotinylated and can be retrieved on streptavidin magnetic beads
    • Osbourn JK, Derbyshire E, Vaughan T, Field A, Johnson K. Pathfinder selection: in situ isolation of novel antibodies. of outstanding interest Immunotechnology. 1998; A technique using a ligand or antibody-peroxidase conjugate to direct the deposition of biotin-tyramine free radicals within a very local area. Phage antibodies binding close by will be biotinylated and can be retrieved on streptavidin magnetic beads.
    • (1998) Immunotechnology
    • Osbourn, J.K.1    Derbyshire, E.2    Vaughan, T.3    Field, A.4    Johnson, K.5


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