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Volumn 201, Issue 1, 1997, Pages 35-55

Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system

Author keywords

antibody library; monoclonal antibody; phage display; single chain Fv

Indexed keywords

AMPICILLIN; MESSENGER RNA; MONOCLONAL ANTIBODY; RECOMBINANT PROTEIN;

EID: 0031032155     PISSN: 00221759     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-1759(96)00208-6     Document Type: Article
Times cited : (438)

References (81)
  • 2
    • 0028823758 scopus 로고
    • Synthetic human antibodies: Selecting and evolving functional proteins
    • Barbas III, C.F. and Wagner, J. (1995) Synthetic human antibodies: Selecting and evolving functional proteins. Methods Companion Methods Enzymol. 8, 94.
    • (1995) Methods Companion Methods Enzymol. , vol.8 , pp. 94
    • Barbas C.F. III1    Wagner, J.2
  • 3
  • 5
    • 0025098151 scopus 로고
    • Preparation and characterization of polyclonal and monoclonal antibodies against the insecticide DDT
    • Bürgisser, D., Frey, S., Gutte, B. and Klauser, S. (1990) Preparation and characterization of polyclonal and monoclonal antibodies against the insecticide DDT. Biochem. Biophys. Res. Commun. 166, 1228.
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 1228
    • Bürgisser, D.1    Frey, S.2    Gutte, B.3    Klauser, S.4
  • 6
    • 0022336676 scopus 로고
    • Immunoglobulin transcripts and molecular history of a hybridoma that produces antibody to carcinoembryonic antigen
    • Cabilly, S. and Riggs, A.D. (1985) Immunoglobulin transcripts and molecular history of a hybridoma that produces antibody to carcinoembryonic antigen. Gene 40, 157.
    • (1985) Gene , vol.40 , pp. 157
    • Cabilly, S.1    Riggs, A.D.2
  • 7
    • 0023780011 scopus 로고
    • Hybridoma fusion cell lines contain an aberrant kappa transcript
    • Carroll, W.L., Mendel, E. and Levy, S. (1988) Hybridoma fusion cell lines contain an aberrant kappa transcript. Mol. Immunol. 25, 991.
    • (1988) Mol. Immunol. , vol.25 , pp. 991
    • Carroll, W.L.1    Mendel, E.2    Levy, S.3
  • 8
    • 0025835310 scopus 로고
    • Making antibody fragments using phage display libraries
    • Clackson, T., Hoogenboom, H.R., Griffiths, A.D. and Winter, G. (1991) Making antibody fragments using phage display libraries. Nature 352, 624.
    • (1991) Nature , vol.352 , pp. 624
    • Clackson, T.1    Hoogenboom, H.R.2    Griffiths, A.D.3    Winter, G.4
  • 9
    • 0028848508 scopus 로고
    • A phage display vector with improved stability, applicability and ease of manipulation
    • Courtney, B.C., Williams, K.C. and Schlager, J.J. (1995) A phage display vector with improved stability, applicability and ease of manipulation. Gene 165, 139.
    • (1995) Gene , vol.165 , pp. 139
    • Courtney, B.C.1    Williams, K.C.2    Schlager, J.J.3
  • 10
    • 0025254304 scopus 로고
    • Regulated expression of foreign genes fused to lac: Control by glucose levels in growth medium
    • De Bellis, D. and Schwartz, I. (1990) Regulated expression of foreign genes fused to lac: control by glucose levels in growth medium. Nucleic Acids Res. 18, 1311.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1311
    • De Bellis, D.1    Schwartz, I.2
  • 12
    • 0028136310 scopus 로고
    • Multimerization behaviour of single chain Fv variants for the tumor-binding antibody B72.3
    • Desplancq, D., King, D.J., Lawson, A.D.G. and Mountain, A. (1994) Multimerization behaviour of single chain Fv variants for the tumor-binding antibody B72.3. Prot. Eng. 7, 1027.
    • (1994) Prot. Eng. , vol.7 , pp. 1027
    • Desplancq, D.1    King, D.J.2    Lawson, A.D.G.3    Mountain, A.4
  • 13
    • 0023948010 scopus 로고
    • High efficiency transformation of E. coli by high voltage electroporation
    • Dower, J.W., Miller, J.F. and Ragsdale, C.W. (1988) High efficiency transformation of E. coli by high voltage electroporation. Nucleic Acids Res. 16, 6127.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6127
    • Dower, J.W.1    Miller, J.F.2    Ragsdale, C.W.3
  • 14
    • 0028609602 scopus 로고
    • Elimination of endogenous aberrant kappa chain transcripts from sp2/0-derived hybridoma cells by specific ribozyme cleavage: Utility in genetic therapy of HIV-1 infections
    • Duan, L. and Pomerantz, R.J. (1994) Elimination of endogenous aberrant kappa chain transcripts from sp2/0-derived hybridoma cells by specific ribozyme cleavage: utility in genetic therapy of HIV-1 infections. Nucleic Acids Res. 22, 5433.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5433
    • Duan, L.1    Pomerantz, R.J.2
  • 15
    • 0029076741 scopus 로고
    • Phage display used for gene cloning of human recombinant antibody against the erythrocyte surface antigen, rhesus D
    • Dziegiel, M., Nielson, L.K., Anderson, P.S., Blancher, A., Dickmeiss, E. and Engberg, J. (1995) Phage display used for gene cloning of human recombinant antibody against the erythrocyte surface antigen, rhesus D. J. Immunol. Methods 182, 7.
    • (1995) J. Immunol. Methods , vol.182 , pp. 7
    • Dziegiel, M.1    Nielson, L.K.2    Anderson, P.S.3    Blancher, A.4    Dickmeiss, E.5    Engberg, J.6
  • 16
    • 0028324575 scopus 로고
    • Structural and dynamic properties of the Fv fragment and the single-chain Fv fragment of an antibody in solution investigated by heteronuclear three-dimensional NMR spectroscopy
    • Freund, C., Ross, A., Plückthun, A. and Holak, T.A. (1994) Structural and dynamic properties of the Fv fragment and the single-chain Fv fragment of an antibody in solution investigated by heteronuclear three-dimensional NMR spectroscopy. Biochemistry 33, 3296.
    • (1994) Biochemistry , vol.33 , pp. 3296
    • Freund, C.1    Ross, A.2    Plückthun, A.3    Holak, T.A.4
  • 17
    • 0001587390 scopus 로고
    • Expressing antibodies in Escherichia coli
    • C.A.K. Borrebaeck (Ed.), Oxford University Press, Oxford
    • Ge, L., Knappik, A., Pack, P., Freund, C. and Plückthun, A. (1995) Expressing antibodies in Escherichia coli. In: C.A.K. Borrebaeck (Ed.), Antibody Engineering, 2nd edn. Oxford University Press, Oxford, p. 229.
    • (1995) Antibody Engineering, 2nd Edn. , pp. 229
    • Ge, L.1    Knappik, A.2    Pack, P.3    Freund, C.4    Plückthun, A.5
  • 18
    • 0026589089 scopus 로고
    • Original and artificial antibodies
    • Gherardi, E. and Milstein, C. (1992) Original and artificial antibodies. Nature 357, 201.
    • (1992) Nature , vol.357 , pp. 201
    • Gherardi, E.1    Milstein, C.2
  • 19
    • 0025162270 scopus 로고
    • A comparison of strategies to stabilize immunoglobulin Fv-fragments
    • Glockshuber, R., Malia, M., Pfitzinger, I. and Plückthun, A. (1990) A comparison of strategies to stabilize immunoglobulin Fv-fragments. Biochemistry 29, 1362.
    • (1990) Biochemistry , vol.29 , pp. 1362
    • Glockshuber, R.1    Malia, M.2    Pfitzinger, I.3    Plückthun, A.4
  • 20
    • 0026356266 scopus 로고
    • Humanization of monoclonal antibodies
    • Güssow, D. and Seemann, G. (1991) Humanization of monoclonal antibodies. Methods Enzymol. 203, 99.
    • (1991) Methods Enzymol. , vol.203 , pp. 99
    • Güssow, D.1    Seemann, G.2
  • 21
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom, H.R., Griffiths, A.D., Johnson, K.S., Chiswell, D., Hudson, P. and Winter, G. (1991) Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res. 19, 4133.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4133
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.4    Hudson, P.5    Winter, G.6
  • 22
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension
    • Horton, R.M., Hunt, H.D., Ho, S.N., Pullen, J.K. and Pease, L.R. (1989) Engineering hybrid genes without the use of restriction enzymes: Gene splicing by overlap extension. Gene 77, 61.
    • (1989) Gene , vol.77 , pp. 61
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 26
    • 0029615426 scopus 로고
    • pFab60: A new, efficient vector for expression of antibody Fab fragments displayed on phage
    • Johansen, L.K., Albrechtsen, B., Andersen, H.W. and Engberg, J. (1995) pFab60: a new, efficient vector for expression of antibody Fab fragments displayed on phage. Prot. Eng. 8, 1063.
    • (1995) Prot. Eng. , vol.8 , pp. 1063
    • Johansen, L.K.1    Albrechtsen, B.2    Andersen, H.W.3    Engberg, J.4
  • 28
    • 0029796811 scopus 로고    scopus 로고
    • Monovalent single-chain Fv fragments and bivalent miniantibodies bound to vesicular stomatitis virus (VSV) protect against lethal infection
    • Kalinke, U., Krebber, A., Krebber, C., Bucher, E., Plückthun, A., Zinkernagel, R.M. and Hengartner, H. (1996) Monovalent single-chain Fv fragments and bivalent miniantibodies bound to vesicular stomatitis virus (VSV) protect against lethal infection. Eur. J. Immunol. 26, 2801.
    • (1996) Eur. J. Immunol. , vol.26 , pp. 2801
    • Kalinke, U.1    Krebber, A.2    Krebber, C.3    Bucher, E.4    Plückthun, A.5    Zinkernagel, R.M.6    Hengartner, H.7
  • 29
    • 0025910746 scopus 로고
    • Linkage of recognition and replication functions by assembling combinatorial antibody Fab libraries along phage surfaces
    • Kang, A.S., Barbas, C.F., Janda, K.D., Benkovic, S.J. and Lerner, R.A. (1991) Linkage of recognition and replication functions by assembling combinatorial antibody Fab libraries along phage surfaces. Proc. Natl. Acad. Sci. USA 88, 4363.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4363
    • Kang, A.S.1    Barbas, C.F.2    Janda, K.D.3    Benkovic, S.J.4    Lerner, R.A.5
  • 30
    • 0027076380 scopus 로고
    • A general method for chimerization of monoclonal antibodies by inverse polymerase chain reaction which conserves authentic N-terminal sequences
    • Kaluza, B., Betzl, G., Shao, H., Diamantstein, T. and Weidle, U.H. (1992) A general method for chimerization of monoclonal antibodies by inverse polymerase chain reaction which conserves authentic N-terminal sequences. Gene 122, 321.
    • (1992) Gene , vol.122 , pp. 321
    • Kaluza, B.1    Betzl, G.2    Shao, H.3    Diamantstein, T.4    Weidle, U.H.5
  • 31
    • 0018726056 scopus 로고
    • A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines
    • Kearney, J.F., Radbruch, A., Liesegang, B. and Rajewski, K. (1979) A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines. J. Immunol. 123, 1548.
    • (1979) J. Immunol. , vol.123 , pp. 1548
    • Kearney, J.F.1    Radbruch, A.2    Liesegang, B.3    Rajewski, K.4
  • 32
    • 0027398107 scopus 로고
    • Optimization of primers for cloning libraries of mouse immunoglobulin genes using the polymerase chain reaction
    • Kettleborough, C.A., Saldanha, J., Ansell, K.H. and Bendig, M.M. (1993) Optimization of primers for cloning libraries of mouse immunoglobulin genes using the polymerase chain reaction. Eur. J. Immunol. 23, 206.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 206
    • Kettleborough, C.A.1    Saldanha, J.2    Ansell, K.H.3    Bendig, M.M.4
  • 33
    • 0028258055 scopus 로고
    • Isolation of tumor cell-specific single-chain Fv from immunized mice using phage-antibody libraries and the re-construction of whole antibodies from these antibody fragments
    • Kettleborough, C.A., Ansell, K.H., Allen, R.W., Rosell-Vives, E., Güssow, D.H. and Bendig, M.M. (1994) Isolation of tumor cell-specific single-chain Fv from immunized mice using phage-antibody libraries and the re-construction of whole antibodies from these antibody fragments. Eur. J. Immunol. 24, 952.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 952
    • Kettleborough, C.A.1    Ansell, K.H.2    Allen, R.W.3    Rosell-Vives, E.4    Güssow, D.H.5    Bendig, M.M.6
  • 34
    • 0028073310 scopus 로고
    • An improved affinity tag based on the FLAG peptide for the detection and purification of recombinant antibody fragments
    • Knappik, A. and Plückthun, A. (1994) An improved affinity tag based on the FLAG peptide for the detection and purification of recombinant antibody fragments. BioTechniques 17, 754.
    • (1994) BioTechniques , vol.17 , pp. 754
    • Knappik, A.1    Plückthun, A.2
  • 35
    • 0028966985 scopus 로고
    • Engineered turns of a recombinant antibody improve its in vivo folding
    • Knappik, A. and Plückthun, A. (1995) Engineered turns of a recombinant antibody improve its in vivo folding. Prot. Eng. 8, 81.
    • (1995) Prot. Eng. , vol.8 , pp. 81
    • Knappik, A.1    Plückthun, A.2
  • 36
    • 0017135663 scopus 로고
    • Derivation of specific antibody-producing tissue culture and tumor lines by cell fusion
    • Köhler, G. and Milstein, C. (1976) Derivation of specific antibody-producing tissue culture and tumor lines by cell fusion. Eur. J. Immunol. 6, 511.
    • (1976) Eur. J. Immunol. , vol.6 , pp. 511
    • Köhler, G.1    Milstein, C.2
  • 37
    • 0029585566 scopus 로고
    • Co-selection of cognate antibody-antigen pairs by selectively-infective phages
    • Krebber, C., Spada, S., Desplancq, D. and Plückthun, A. (1995) Co-selection of cognate antibody-antigen pairs by selectively-infective phages. FEBS Lett. 377, 227.
    • (1995) FEBS Lett. , vol.377 , pp. 227
    • Krebber, C.1    Spada, S.2    Desplancq, D.3    Plückthun, A.4
  • 38
    • 0030608365 scopus 로고    scopus 로고
    • Inclusion of an upstream transcriptional terminator in phage display vectors abolishes background expression of toxic fusions with coat protein g3p
    • Krebber, A., Burmester, J. and Plückthun, A. (1996a) Inclusion of an upstream transcriptional terminator in phage display vectors abolishes background expression of toxic fusions with coat protein g3p. Gene 178, 71.
    • (1996) Gene , vol.178 , pp. 71
    • Krebber, A.1    Burmester, J.2    Plückthun, A.3
  • 40
    • 0026766271 scopus 로고
    • Rapid isolation of immunoglobulin variable genes from cell lysates of rat hybridomas by polymerase chain reaction
    • Kütemeier, G., Harloff, C. and Mocikat, R. (1992) Rapid isolation of immunoglobulin variable genes from cell lysates of rat hybridomas by polymerase chain reaction. Hybridoma 11, 23.
    • (1992) Hybridoma , vol.11 , pp. 23
    • Kütemeier, G.1    Harloff, C.2    Mocikat, R.3
  • 41
    • 0029986050 scopus 로고    scopus 로고
    • Cloning and characterization of cDNAs coding for heavy and light chains of a monoclonal antibody (MabB23) specific for human plasma apolipoprotein B-100
    • Kwak, J.-W., Choi, B.-K., Lee, D.-I., Kang, Y.-K., Seo, Y.-G., Cho, W.-K. and Han, M.H. (1996) Cloning and characterization of cDNAs coding for heavy and light chains of a monoclonal antibody (MabB23) specific for human plasma apolipoprotein B-100. Gene 169, 237.
    • (1996) Gene , vol.169 , pp. 237
    • Kwak, J.-W.1    Choi, B.-K.2    Lee, D.-I.3    Kang, Y.-K.4    Seo, Y.-G.5    Cho, W.-K.6    Han, M.H.7
  • 42
    • 0028929950 scopus 로고
    • Paratope characterization by structural modelling of two anti-cortisol single-chain variable fragments produced in E. coli
    • Le Calvez, H., Fieschi, J., Green, J.M., Marchesi, N., Chauveau, J. and Baty, D. (1995) Paratope characterization by structural modelling of two anti-cortisol single-chain variable fragments produced in E. coli. Mol. Immunol. 32, 185.
    • (1995) Mol. Immunol. , vol.32 , pp. 185
    • Le Calvez, H.1    Fieschi, J.2    Green, J.M.3    Marchesi, N.4    Chauveau, J.5    Baty, D.6
  • 43
    • 0029561993 scopus 로고
    • Spectroscopic, calorimetric, and kinetic demonstration of conformational adaption in peptide-antibody recognition
    • Leder, L., Berger, C., Bornhauser, S., Wendt, H., Ackermann, F., Jelesarov, I. and Bosshard, H.R. (1995) Spectroscopic, calorimetric, and kinetic demonstration of conformational adaption in peptide-antibody recognition. Biochemistry 34, 16509.
    • (1995) Biochemistry , vol.34 , pp. 16509
    • Leder, L.1    Berger, C.2    Bornhauser, S.3    Wendt, H.4    Ackermann, F.5    Jelesarov, I.6    Bosshard, H.R.7
  • 44
    • 0003044623 scopus 로고
    • Purification of native proteins from the cytoplasm and periplasm of Escherichia coli using IMAC and histidine tails: A comparison of proteins and protocols
    • Lindner, P., Guth, B., Wülfing, C., Krebber, C., Steipe, B., Müller, F. and Plückthun, A. (1992) Purification of native proteins from the cytoplasm and periplasm of Escherichia coli using IMAC and histidine tails: A comparison of proteins and protocols. Methods Companion Methods Enzymol. 4, 41.
    • (1992) Methods Companion Methods Enzymol. , vol.4 , pp. 41
    • Lindner, P.1    Guth, B.2    Wülfing, C.3    Krebber, C.4    Steipe, B.5    Müller, F.6    Plückthun, A.7
  • 46
    • 0026343486 scopus 로고
    • Selecting high-affinity binding proteins by monovalent phage display
    • Lowman, H.B., Bass, S.H., Simpson, N. and Wells, J.A. (1991) Selecting high-affinity binding proteins by monovalent phage display. Biochemistry 30, 10832.
    • (1991) Biochemistry , vol.30 , pp. 10832
    • Lowman, H.B.1    Bass, S.H.2    Simpson, N.3    Wells, J.A.4
  • 49
    • 0025226085 scopus 로고
    • Phage antibodies: Filamentous phage displaying antibody variable domains
    • McCafferty, J., Griffiths, A.D., Winter, G. and Chiswell, D.J. (1990) Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348, 552.
    • (1990) Nature , vol.348 , pp. 552
    • McCafferty, J.1    Griffiths, A.D.2    Winter, G.3    Chiswell, D.J.4
  • 50
    • 0029116810 scopus 로고
    • A murine antibody to Shigella dysenteriae type 1 employs V-genes that contain a rearranged codon for the a light chain
    • Miller, C.E., Huppi, K., Siwarski, D., Karpas, A., Newman, A., Mainhart, C. and Glaudemans, C.P.J. (1995) A murine antibody to Shigella dysenteriae type 1 employs V-genes that contain a rearranged codon for the A light chain. Mol. Immunol. 32, 679.
    • (1995) Mol. Immunol. , vol.32 , pp. 679
    • Miller, C.E.1    Huppi, K.2    Siwarski, D.3    Karpas, A.4    Newman, A.5    Mainhart, C.6    Glaudemans, C.P.J.7
  • 51
    • 0023052239 scopus 로고
    • An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein
    • Munro, S. and Pelham, H.R. (1986) An Hsp70-like protein in the ER: Identity with the 78 kd glucose-regulated protein and immunoglobulin heavy chain binding protein. Cell 46, 291.
    • (1986) Cell , vol.46 , pp. 291
    • Munro, S.1    Pelham, H.R.2
  • 52
  • 54
    • 0022930739 scopus 로고
    • Cloning and complete nucleotide sequence of the Escherichia coli glutamine permease operon (glnHPQ)
    • Nohno, T., Saito, T. and Hong, J.-S. (1986) Cloning and complete nucleotide sequence of the Escherichia coli glutamine permease operon (glnHPQ). Mol. Gen. Genet. 205, 260.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 260
    • Nohno, T.1    Saito, T.2    Hong, J.-S.3
  • 55
    • 0029981792 scopus 로고    scopus 로고
    • Light chain shuffling of a high affinity antibody results in a drift in epitope recognition
    • Ohlin, M., Owman, H., Mach, M. and Borrebaeck, C.A.K. (1996) Light chain shuffling of a high affinity antibody results in a drift in epitope recognition. Mol. Immunol. 33, 47.
    • (1996) Mol. Immunol. , vol.33 , pp. 47
    • Ohlin, M.1    Owman, H.2    Mach, M.3    Borrebaeck, C.A.K.4
  • 56
    • 1542698957 scopus 로고
    • Cloning immunoglobulin variable domains for expression by the polymerase chain reaction
    • Orlandi, R., Güssow, D.H., Jones, P.T. and Winter, G. (1989) Cloning immunoglobulin variable domains for expression by the polymerase chain reaction. Proc. Natl. Acad. Sci. USA 86, 3833.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3833
    • Orlandi, R.1    Güssow, D.H.2    Jones, P.T.3    Winter, G.4
  • 58
    • 0029950981 scopus 로고    scopus 로고
    • Improved cloning of antibody variable regions from hybridomas by an antisense-directed RNAse H digestion of the P3-X63-Ag8.653 derived pseudogene mRNA
    • Ostermeier, C. and Michel, H. (1996) Improved cloning of antibody variable regions from hybridomas by an antisense-directed RNAse H digestion of the P3-X63-Ag8.653 derived pseudogene mRNA. Nucleic Acids Res. 24, 1979.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1979
    • Ostermeier, C.1    Michel, H.2
  • 59
    • 0028872393 scopus 로고
    • Crystals of an antibody Fv fragment against an integral membrane protein diffracting to 1.28 Å resolution
    • Ostermeier, C., Essen L.-O. and Michel, H. (1995) Crystals of an antibody Fv fragment against an integral membrane protein diffracting to 1.28 Å resolution. Proteins 21, 74.
    • (1995) Proteins , vol.21 , pp. 74
    • Ostermeier, C.1    Essen, L.-O.2    Michel, H.3
  • 60
    • 0027442660 scopus 로고
    • Improved bivalent miniantibodies, with identical avidity as whole antibodies, produced by high cell density fermentation of Escherichia coli
    • Pack, P., Kujau, M., Schroeckh, V., Knüpfer, U., Wenderoth, R., Riesenberg, D. and Plückthun, A. (1993) Improved bivalent miniantibodies, with identical avidity as whole antibodies, produced by high cell density fermentation of Escherichia coli. Biotechnology 11, 1271.
    • (1993) Biotechnology , vol.11 , pp. 1271
    • Pack, P.1    Kujau, M.2    Schroeckh, V.3    Knüpfer, U.4    Wenderoth, R.5    Riesenberg, D.6    Plückthun, A.7
  • 61
    • 0028949091 scopus 로고
    • Tetravalent miniantibodies with high avidity assembling in Escherichia coli
    • Pack, P., Müller, K., Zahn, R. and Plückthun, A. (1995) Tetravalent miniantibodies with high avidity assembling in Escherichia coli. J. Mol. Biol. 246, 28.
    • (1995) J. Mol. Biol. , vol.246 , pp. 28
    • Pack, P.1    Müller, K.2    Zahn, R.3    Plückthun, A.4
  • 62
    • 0002205730 scopus 로고
    • Recombinant antibodies
    • C.J. van Oss and M.H.V. van Regenmortel (Eds.), Marcel Dekker, New York
    • Plückthun, A. (1994) Recombinant antibodies. In: C.J. van Oss and M.H.V. van Regenmortel (Eds.), Immunochemistry. Marcel Dekker, New York, p. 201.
    • (1994) Immunochemistry , pp. 201
    • Plückthun, A.1
  • 64
  • 66
    • 0028335616 scopus 로고
    • Stabilization of the Fv fragments in recombinant immunotoxins by disulfide bonds engineered into conserved framework regions
    • Reiter, Y., Brinkmann, U., Kreitmann, R.J., Jung, S-H., Lee, B. and Pastan, I. (1994) Stabilization of the Fv fragments in recombinant immunotoxins by disulfide bonds engineered into conserved framework regions. Biochemistry 33, 5451.
    • (1994) Biochemistry , vol.33 , pp. 5451
    • Reiter, Y.1    Brinkmann, U.2    Kreitmann, R.J.3    Jung, S.-H.4    Lee, B.5    Pastan, I.6
  • 67
    • 0027184954 scopus 로고
    • Phage display and selection of a site-directed randomized single-chain antibody Fv fragment for its affinity improvement
    • Riechmann, L. and Weill, M. (1993) Phage display and selection of a site-directed randomized single-chain antibody Fv fragment for its affinity improvement. Biochemistry 32, 8848.
    • (1993) Biochemistry , vol.32 , pp. 8848
    • Riechmann, L.1    Weill, M.2
  • 68
    • 0002440928 scopus 로고
    • Molecular Cloning
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning. A Laboratory Manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1989) A Laboratory Manual
    • Sambrook, J.1    Fritsch, E.F.2    Maniatis, T.3
  • 69
    • 0023047182 scopus 로고
    • Sequence of the gene for alkaline phosphatase from Escherichia coli JM83
    • Shuttleworth, H., Taylor, J. and Minton, N. (1986) Sequence of the gene for alkaline phosphatase from Escherichia coli JM83. Nucleic Acids Res. 14, 8689.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 8689
    • Shuttleworth, H.1    Taylor, J.2    Minton, N.3
  • 70
    • 0008396004 scopus 로고
    • Proceedings of the First International Workshop on Small-Cell Lung-Cancer Antigens
    • Souhami, R.L., Beverley, P.C.L. and Bobrow, L.G. (1988) Proceedings of the First International Workshop on Small-Cell Lung-Cancer Antigens. Lung Cancer 4, 1.
    • (1988) Lung Cancer , vol.4 , pp. 1
    • Souhami, R.L.1    Beverley, P.C.L.2    Bobrow, L.G.3
  • 71
    • 0025273561 scopus 로고
    • Dissection of functional domains in phage fd adsorption protein
    • Stengele, I., Bross, P., Garcés, X., Giray, J. and Rasched, I. (1990) Dissection of functional domains in phage fd adsorption protein. J. Mol. Biol. 212, 143.
    • (1990) J. Mol. Biol. , vol.212 , pp. 143
    • Stengele, I.1    Bross, P.2    Garcés, X.3    Giray, J.4    Rasched, I.5
  • 72
    • 0023664181 scopus 로고
    • Complete variable region sequence of a nonfunctionally rearranged kappa light chain transcribed in the nonsecretor P3-X63-Ag8.653 myeloma cell line
    • Strohal, R., Kroemer, G., Wick, G. and Kofler, R. (1987) Complete variable region sequence of a nonfunctionally rearranged kappa light chain transcribed in the nonsecretor P3-X63-Ag8.653 myeloma cell line. Nucleic Acids Res. 15, 2771.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 2771
    • Strohal, R.1    Kroemer, G.2    Wick, G.3    Kofler, R.4
  • 73
    • 0028358908 scopus 로고
    • Simple, effective cleanup of DNA ligation reactions prior to electro-transformation
    • Thomas, M.R. (1994) Simple, effective cleanup of DNA ligation reactions prior to electro-transformation. BioTechniques 16, 988.
    • (1994) BioTechniques , vol.16 , pp. 988
    • Thomas, M.R.1
  • 75
    • 0023321780 scopus 로고
    • Somatic point mutations in unrearranged immunoglobuline gene segments encoding the variable region of λ light chains
    • Weiss, S. and Wu, G.E. (1987) Somatic point mutations in unrearranged immunoglobuline gene segments encoding the variable region of λ light chains. EMBO J. 6, 927.
    • (1987) EMBO J. , vol.6 , pp. 927
    • Weiss, S.1    Wu, G.E.2
  • 76
    • 0028988946 scopus 로고
    • The SfiI restriction endonuclease makes a four-strand DNa break at two copies of its recognition sequence
    • Wentzell, L.M., Nobbs, T.J. and Halford, S.E. (1995) The SfiI restriction endonuclease makes a four-strand DNA break at two copies of its recognition sequence. J. Mol. Biol. 248, 581.
    • (1995) J. Mol. Biol. , vol.248 , pp. 581
    • Wentzell, L.M.1    Nobbs, T.J.2    Halford, S.E.3
  • 78
    • 0029007033 scopus 로고
    • An improved phage display antibody cloning system using newly designed PCR primers optimized for Pfu DNA polymerase
    • Yamanaka, H.I., Kirii, Y. and Ohmoto, H. (1995) An improved phage display antibody cloning system using newly designed PCR primers optimized for Pfu DNA polymerase. J. Biochem. 117, 1218.
    • (1995) J. Biochem. , vol.117 , pp. 1218
    • Yamanaka, H.I.1    Kirii, Y.2    Ohmoto, H.3
  • 79
    • 0029564921 scopus 로고
    • CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range
    • Yang, W.-P., Green, K., Pinz-Sweeney, S., Briones, A.T., Burton, D.R. and Barbas III, C.F. (1995) CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range. J. Mol. Biol. 254, 392.
    • (1995) J. Mol. Biol. , vol.254 , pp. 392
    • Yang, W.-P.1    Green, K.2    Pinz-Sweeney, S.3    Briones, A.T.4    Burton, D.R.5    Barbas C.F. III6
  • 80
    • 0027025207 scopus 로고
    • Construction of complex directional complementary DNA libraries in SfiI
    • Zelenetz, A.D. (1992) Construction of complex directional complementary DNA libraries in SfiI. Methods Enzymol. 216, 517.
    • (1992) Methods Enzymol. , vol.216 , pp. 517
    • Zelenetz, A.D.1
  • 81
    • 0028279285 scopus 로고
    • Optimization of primer sequences for mouse scFv repertoire display library construction
    • Zhou, H., Fisher, R.J. and Papas, T.S. (1994) Optimization of primer sequences for mouse scFv repertoire display library construction. Nucleic Acids Res. 22, 888.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 888
    • Zhou, H.1    Fisher, R.J.2    Papas, T.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.