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Volumn 2, Issue 2000, 2000, Pages 339-376

Antibody engineering

Author keywords

Antigen; Combinatorial libraries; Library screening; Phage display; scFv

Indexed keywords

ANTIBODY; PEPTIDE LIBRARY; RECOMBINANT PROTEIN;

EID: 0034575023     PISSN: 15239829     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.bioeng.2.1.339     Document Type: Article
Times cited : (203)

References (235)
  • 2
    • 0032200738 scopus 로고    scopus 로고
    • Antibodies come back from the brink
    • Holliger P, Hoogenboom H. 1998. Antibodies come back from the brink. Nat. Biotechnol. 16:1015-16
    • (1998) Nat. Biotechnol. , vol.16 , pp. 1015-1016
    • Holliger, P.1    Hoogenboom, H.2
  • 3
    • 0003536924 scopus 로고    scopus 로고
    • New York: Freeman. 664 pp.
    • Kuby J. 1997. Immunology. New York: Freeman. 664 pp.
    • (1997) Immunology
    • Kuby, J.1
  • 4
    • 0033565413 scopus 로고    scopus 로고
    • Expression, purification and biochemical characterization of recombinant murine secretory component: A novel tool in mucosal immunology
    • Crottet P, Cottet S, Corthesy B. 1999. Expression, purification and biochemical characterization of recombinant murine secretory component: a novel tool in mucosal immunology. Biochem. J. 341:299-306
    • (1999) Biochem. J. , vol.341 , pp. 299-306
    • Crottet, P.1    Cottet, S.2    Corthesy, B.3
  • 5
    • 0029035201 scopus 로고
    • Generation and assembly of secretory antibodies in plants
    • Ma JK, Hiatt A, Hein M, Vine ND, Wang F, et al. 1995. Generation and assembly of secretory antibodies in plants. Science 268:716-19
    • (1995) Science , vol.268 , pp. 716-719
    • Ma, J.K.1    Hiatt, A.2    Hein, M.3    Vine, N.D.4    Wang, F.5
  • 6
    • 0030580057 scopus 로고    scopus 로고
    • Antibody-antigen interactions: Contact analysis and binding site topography
    • MacCallum RM, Martin AC, Thornton JM. 1996. Antibody-antigen interactions: contact analysis and binding site topography. J. Mol. Biol. 262:732-45
    • (1996) J. Mol. Biol. , vol.262 , pp. 732-745
    • Maccallum, R.M.1    Martin, A.C.2    Thornton, J.M.3
  • 7
    • 0031868554 scopus 로고    scopus 로고
    • Anatomy of an antibody molecule: Structure, kinetics, thermodynamics and mutational studies of the anti-lysozyme antibody D1.3
    • Braden BC, Goldman ER, Mariuzza RA, Poljak RJ. 1998. Anatomy of an antibody molecule: structure, kinetics, thermodynamics and mutational studies of the anti-lysozyme antibody D1.3. Immunol. Rev. 163:45-57
    • (1998) Immunol. Rev. , vol.163 , pp. 45-57
    • Braden, B.C.1    Goldman, E.R.2    Mariuzza, R.A.3    Poljak, R.J.4
  • 8
    • 0028014642 scopus 로고
    • Bound water molecules and conformational stabilization help mediate an antigen-antibody association
    • Bhat TN, Bentley GA, Boulot G, Greene MI, Tello D, et al. 1994. Bound water molecules and conformational stabilization help mediate an antigen-antibody association. Proc. Natl. Acad. Sci. USA 91:1089-93
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1089-1093
    • Bhat, T.N.1    Bentley, G.A.2    Boulot, G.3    Greene, M.I.4    Tello, D.5
  • 9
    • 0028580678 scopus 로고
    • Dissecting the energetics of an antibody-antigen interface by alanine shaving and molecular grafting
    • Jin L, Wells JA. 1994. Dissecting the energetics of an antibody-antigen interface by alanine shaving and molecular grafting. Protein Sci. 3:2351-57
    • (1994) Protein Sci. , vol.3 , pp. 2351-2357
    • Jin, L.1    Wells, J.A.2
  • 10
    • 0028916599 scopus 로고
    • A hot spot of binding energy in a hormone-receptor interface
    • Clackson T, Wells JA. 1995. A hot spot of binding energy in a hormone-receptor interface. Science 267:383-86
    • (1995) Science , vol.267 , pp. 383-386
    • Clackson, T.1    Wells, J.A.2
  • 11
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler G, Milstein C. 1975. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256:495-98
    • (1975) Nature , vol.256 , pp. 495-498
    • Kohler, G.1    Milstein, C.2
  • 12
    • 0025978976 scopus 로고
    • Man-made antibodies
    • Winter G, Milstein C. 1991. Man-made antibodies. Nature 349:293-99
    • (1991) Nature , vol.349 , pp. 293-299
    • Winter, G.1    Milstein, C.2
  • 13
    • 0024845655 scopus 로고
    • Expression of functional antibody Fv and Fab fragments in Escherichia coli
    • Pluckthun A, Skerra A. 1989. Expression of functional antibody Fv and Fab fragments in Escherichia coli. Methods Enzymol. 178:497-515
    • (1989) Methods Enzymol. , vol.178 , pp. 497-515
    • Pluckthun, A.1    Skerra, A.2
  • 14
    • 0028609356 scopus 로고
    • Cloning, expression, and characterization of the Fv fragments of the anti-carbohydrate mAbs B1 and B5 as single chain immunotoxins
    • Benhar I, Pastan I. 1994. Cloning, expression, and characterization of the Fv fragments of the anti-carbohydrate mAbs B1 and B5 as single chain immunotoxins. Protein Eng. 7:1509-15
    • (1994) Protein Eng. , vol.7 , pp. 1509-1515
    • Benhar, I.1    Pastan, I.2
  • 15
    • 0028124719 scopus 로고
    • The use of the RACE method to clone hybridoma cDNA when V region primers fail
    • Ruberti F, Cattaneo A, Bradbury A. 1994. The use of the RACE method to clone hybridoma cDNA when V region primers fail. J. Immunol. Methods 173:33-39
    • (1994) J. Immunol. Methods , vol.173 , pp. 33-39
    • Ruberti, F.1    Cattaneo, A.2    Bradbury, A.3
  • 16
    • 0024346547 scopus 로고
    • Rapid cloning of rearranged immunoglobulin genes from human hybridoma cells using mixed primers and the polymerase chain reaction
    • Larrick JW, Danielsson L, Brenner CA, Abrahamson M, Fry KE, et al. 1989. Rapid cloning of rearranged immunoglobulin genes from human hybridoma cells using mixed primers and the polymerase chain reaction. Biochem. Biophys. Res. Commun. 160:1250-56
    • (1989) Biochem. Biophys. Res. Commun. , vol.160 , pp. 1250-1256
    • Larrick, J.W.1    Danielsson, L.2    Brenner, C.A.3    Abrahamson, M.4    Fry, K.E.5
  • 18
    • 1542698957 scopus 로고
    • Cloning immunoglobulin variable domains for expression by the polymerase chain reaction
    • Orlandi R, Gussow DH, Jones PT, Winter G. 1989. Cloning immunoglobulin variable domains for expression by the polymerase chain reaction. Proc. Natl. Acad. Sci. USA 86:3833-37
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 3833-3837
    • Orlandi, R.1    Gussow, D.H.2    Jones, P.T.3    Winter, G.4
  • 19
    • 0031933472 scopus 로고    scopus 로고
    • A definitive set of oligonucleotide primers for amplifying human V regions
    • Sblattero D, Bradbury A. 1998. A definitive set of oligonucleotide primers for amplifying human V regions. Immunotechnology 3:271-78
    • (1998) Immunotechnology , vol.3 , pp. 271-278
    • Sblattero, D.1    Bradbury, A.2
  • 20
    • 0031032155 scopus 로고    scopus 로고
    • Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system
    • Krebber A, Bornhauser S, Burmester J, Honegger A, Willuda J, et al. 1997. Reliable cloning of functional antibody variable domains from hybridomas and spleen cell repertoires employing a reengineered phage display system. J. Immunol. Methods 201:35-55
    • (1997) J. Immunol. Methods , vol.201 , pp. 35-55
    • Krebber, A.1    Bornhauser, S.2    Burmester, J.3    Honegger, A.4    Willuda, J.5
  • 21
    • 0022336676 scopus 로고
    • Immunoglobulin transcripts and molecular history of a hybridoma that produces antibody to carcinoembryonic antigen
    • Cabilly S, Cabilly AD. 1985. Immunoglobulin transcripts and molecular history of a hybridoma that produces antibody to carcinoembryonic antigen. Gene 40:157-61
    • (1985) Gene , vol.40 , pp. 157-161
    • Cabilly, S.1    Cabilly, A.D.2
  • 22
    • 0023780011 scopus 로고
    • Hybridoma fusion cell lines contain an aberrant kappa transcript
    • Carroll WF, Mendel E, Levy S. 1988. Hybridoma fusion cell lines contain an aberrant kappa transcript. Mol. Immunol. 25:991-95
    • (1988) Mol. Immunol. , vol.25 , pp. 991-995
    • Carroll, W.F.1    Mendel, E.2    Levy, S.3
  • 23
    • 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 HFV-1 infections
    • Duan L, Pomerantz RJ. 1994. Elimination of endogenous aberrant kappa chain transcripts from sp2/0-derived hybridoma cells by specific ribozyme cleavage: utility in genetic therapy of HFV-1 infections. Nucleic Acids Res. 22:5433-38
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5433-5438
    • Duan, L.1    Pomerantz, R.J.2
  • 24
    • 0033103560 scopus 로고    scopus 로고
    • Vernier zone residue 4 of mouse sub-group II kappa light chains is a critical determinant for antigen recognition
    • de Haard H, Kazemier B, van der Bent A, Oudshoorn P, Boender P, et al. 1999. Vernier zone residue 4 of mouse sub-group II kappa light chains is a critical determinant for antigen recognition. Immunotechnology 4:203-15
    • (1999) Immunotechnology , vol.4 , pp. 203-215
    • De Haard, H.1    Kazemier, B.2    Van Der Bent, A.3    Oudshoorn, P.4    Boender, P.5
  • 26
    • 0029764444 scopus 로고    scopus 로고
    • Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme
    • Desmyter A, Transue TR, Ghahroudi MA, Thi MH, Poortmans F, et al. 1996. Crystal structure of a camel single-domain VH antibody fragment in complex with lysozyme. Nat. Struct. Biol. 3:803-11
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 803-811
    • Desmyter, A.1    Transue, T.R.2    Ghahroudi, M.A.3    Thi, M.H.4    Poortmans, F.5
  • 27
    • 0033561250 scopus 로고    scopus 로고
    • A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops.
    • Decanniere K, Desmyter A, Lauwereys M, Ghahroudi MA, Muyldermans S, et al. 1999. A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops. Structure 7:361-70
    • (1999) Structure , vol.7 , pp. 361-370
    • Decanniere, K.1    Desmyter, A.2    Lauwereys, M.3    Ghahroudi, M.A.4    Muyldermans, S.5
  • 28
    • 0027953603 scopus 로고
    • Camelising' human antibody fragments: NMR studies on VH domains
    • Davies J, Riechmann L. 1994. 'Camelising' human antibody fragments: NMR studies on VH domains. FEBS Lett. 339: 285-90
    • (1994) FEBS Lett. , vol.339 , pp. 285-290
    • Davies, J.1    Riechmann, L.2
  • 29
    • 0029746203 scopus 로고    scopus 로고
    • Single antibody domains as small recognition units: Design and in vitro antigen selection of camelized, human VH domains with improved protein stability
    • Davies J, Riechmann L. 1996. Single antibody domains as small recognition units: design and in vitro antigen selection of camelized, human VH domains with improved protein stability. Protein Eng. 9: 531-37
    • (1996) Protein Eng. , vol.9 , pp. 531-537
    • Davies, J.1    Riechmann, L.2
  • 30
    • 0029070931 scopus 로고
    • Solution properties of Escherichia coli-expressed VH domain of anti-neuraminidase antibody NC41
    • Kortt AA, Guthrie RE, Hinds MG, Power BE, Ivancic N, et al. 1995. Solution properties of Escherichia coli-expressed VH domain of anti-neuraminidase antibody NC41. J. Protein Chem. 14:167-78
    • (1995) J. Protein Chem. , vol.14 , pp. 167-178
    • Kortt, A.A.1    Guthrie, R.E.2    Hinds, M.G.3    Power, B.E.4    Ivancic, N.5
  • 31
    • 0032763794 scopus 로고    scopus 로고
    • An antibody single-domain phage display library of a native heavy chain variable region: Isolation of functional single-domain VH molecules with a unique interface
    • Reiter Y, Schuck P, Boyd LF, Plaksin D. 1999. An antibody single-domain phage display library of a native heavy chain variable region: isolation of functional single-domain VH molecules with a unique interface. J. Mol. Biol. 290:685-98
    • (1999) J. Mol. Biol. , vol.290 , pp. 685-698
    • Reiter, Y.1    Schuck, P.2    Boyd, L.F.3    Plaksin, D.4
  • 32
    • 0004198722 scopus 로고
    • Protein engineering of antibody binding sites: Recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli
    • Huston JS, Levinson D, Mudgett-Hunter M, Tai MS, Novotny J, et al. 1988. Protein engineering of antibody binding sites: recovery of specific activity in an anti-digoxin single-chain Fv analogue produced in Escherichia coli. Proc. Natl. Acad. Sci. USA 85:5879-83
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5879-5883
    • Huston, J.S.1    Levinson, D.2    Mudgett-Hunter, M.3    Tai, M.S.4    Novotny, J.5
  • 33
    • 0028246088 scopus 로고
    • Effect of the order of antibody variable regions on the expression of the single chain HyHe110 Fv fragment in E. coli and the thermodynamic analysis of its antigen-binding properties
    • Tsumoto K, Nakaoki Y, Ueda Y, Ogasahara K, Yutani K, et al. 1994. Effect of the order of antibody variable regions on the expression of the single chain HyHe110 Fv fragment in E. coli and the thermodynamic analysis of its antigen-binding properties. Biochem. Biophys. Res. Commun. 201:546-51
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 546-551
    • Tsumoto, K.1    Nakaoki, Y.2    Ueda, Y.3    Ogasahara, K.4    Yutani, K.5
  • 34
    • 0033032935 scopus 로고    scopus 로고
    • Cell-free expression of two single chain monoclonal antibodies against lysozyme: Effect of domain arrangement on the expression
    • Merk H, Stiege W, Tsumoto K, Kumagai I, Erdmann VA. 1999. Cell-free expression of two single chain monoclonal antibodies against lysozyme: effect of domain arrangement on the expression. J. Biochem. 125:328-33
    • (1999) J. Biochem. , vol.125 , pp. 328-333
    • Merk, H.1    Stiege, W.2    Tsumoto, K.3    Kumagai, I.4    Erdmann, V.A.5
  • 35
    • 0025952336 scopus 로고
    • An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli
    • Takkinan K, Laukkanen M-L, Sizmann D, Alfthan K, Immonen T, et al. 1991. An active single-chain antibody containing a cellulase linker domain is secreted by Escherichia coli. Protein Eng. 4:837-41
    • (1991) Protein Eng. , vol.4 , pp. 837-841
    • Takkinan, K.1    Laukkanen, M.-L.2    Sizmann, D.3    Alfthan, K.4    Immonen, T.5
  • 36
    • 0025788111 scopus 로고
    • Conformational stability, folding, and ligand-binding affinity of single-chain Fv immunoglobulin fragments expressed in Escherichia coli
    • Pantoliano M, Bird RE, Johnson S, Asel ED, Dodd SW, et al. 1991. Conformational stability, folding, and ligand-binding affinity of single-chain Fv immunoglobulin fragments expressed in Escherichia coli. Biochemistry 30:10117-25
    • (1991) Biochemistry , vol.30 , pp. 10117-10125
    • Pantoliano, M.1    Bird, R.E.2    Johnson, S.3    Asel, E.D.4    Dodd, S.W.5
  • 37
    • 0029955258 scopus 로고    scopus 로고
    • Selection for linkers for a catalytic single-chain antibody using phage display technology
    • Tang Y, Jiang N, Parakh C, Hilvert D. 1996. Selection for linkers for a catalytic single-chain antibody using phage display technology. J. Biol. Chem. 271:15682-86
    • (1996) J. Biol. Chem. , vol.271 , pp. 15682-15686
    • Tang, Y.1    Jiang, N.2    Parakh, C.3    Hilvert, D.4
  • 38
    • 0031584314 scopus 로고    scopus 로고
    • Importance of the linker in expression of single-chain fv antibody fragments: Optimisation of peptide sequence using phage display technology
    • Turner DJ, Ritter MA, George AJ. 1997. Importance of the linker in expression of single-chain Fv antibody fragments: optimisation of peptide sequence using phage display technology. J. Immunol. Methods 205:43-54
    • (1997) J. Immunol. Methods , vol.205 , pp. 43-54
    • Turner, D.J.1    Ritter, M.A.2    George, A.J.3
  • 39
    • 0032568591 scopus 로고    scopus 로고
    • Optimizing the stability of single chain proteins by linker length and compositional mutagenesis
    • Robinson C, Sauer R. 1998. Optimizing the stability of single chain proteins by linker length and compositional mutagenesis. Proc. Natl. Acad. Sci. USA 95:5929-34
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5929-5934
    • Robinson, C.1    Sauer, R.2
  • 40
    • 0031813249 scopus 로고    scopus 로고
    • Non-repetitive single-chain fv linkers selected by selectively infective phage (SIP) technology
    • Hennecke F, Krebber C, Pluckthun A. 1998. Non-repetitive single-chain Fv linkers selected by selectively infective phage (SIP) technology. Protein Eng. 11:405-10
    • (1998) Protein Eng. , vol.11 , pp. 405-410
    • Hennecke, F.1    Krebber, C.2    Pluckthun, A.3
  • 41
    • 0026502047 scopus 로고
    • High level Escherichia coli expression and production of a bivalent humanized antibody fragment
    • Carter P, Kelley RF, Rodrigues ML, Snedecor B, Covarrubias M, et al. 1992. High level Escherichia coli expression and production of a bivalent humanized antibody fragment. Bio-Technology 10:163-67
    • (1992) Bio-technology , vol.10 , pp. 163-167
    • Carter, P.1    Kelley, R.F.2    Rodrigues, M.L.3    Snedecor, B.4    Covarrubias, M.5
  • 42
    • 0028348843 scopus 로고
    • A general vector, pASK84, for cloning, bacterial production, and single-step purification of antibody Fab fragments
    • Skerra A. 1994. A general vector, pASK84, for cloning, bacterial production, and single-step purification of antibody Fab fragments. Gene 141:79-84
    • (1994) Gene , vol.141 , pp. 79-84
    • Skerra, A.1
  • 43
    • 0030561202 scopus 로고    scopus 로고
    • Biophysical methods for the determination of antibody-antigen affinities
    • Neri D, Montigiani S, Kirkham PM. 1996. Biophysical methods for the determination of antibody-antigen affinities. Trends Biotechnol. 14:465-70
    • (1996) Trends Biotechnol. , vol.14 , pp. 465-470
    • Neri, D.1    Montigiani, S.2    Kirkham, P.M.3
  • 45
    • 0021964141 scopus 로고
    • Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay
    • Friguet B, Chaffotte AF, Djavadi-Ohaniance L, Goldberg ME. 1985. Measurements of the true affinity constant in solution of antigen-antibody complexes by enzyme-linked immunosorbent assay. J. Immunol. Methods 77:305-19
    • (1985) J. Immunol. Methods , vol.77 , pp. 305-319
    • Friguet, B.1    Chaffotte, A.F.2    Djavadi-Ohaniance, L.3    Goldberg, M.E.4
  • 46
    • 0029804729 scopus 로고    scopus 로고
    • Antibody characterization by isothermal titration calorimetry
    • Livingstone JR. 1996. Antibody characterization by isothermal titration calorimetry. Nature 384:491-92
    • (1996) Nature , vol.384 , pp. 491-492
    • Livingstone, J.R.1
  • 47
    • 0030994634 scopus 로고    scopus 로고
    • Yeast surface display for screening combinatorial polypeptide libraries
    • Boder ET, Wittrup KD. 1997. Yeast surface display for screening combinatorial polypeptide libraries. Nat. Biotechnol. 15: 553-57
    • (1997) Nat. Biotechnol. , vol.15 , pp. 553-557
    • Boder, E.T.1    Wittrup, K.D.2
  • 52
    • 0030039913 scopus 로고    scopus 로고
    • Competition BIAcore for measuring true affinities: Large differences from values determined from binding kinetics
    • Nieba L, Krebber A, Pluckthun A. 1996. Competition BIAcore for measuring true affinities: large differences from values determined from binding kinetics. Anal. Biochem. 234:155-65
    • (1996) Anal. Biochem. , vol.234 , pp. 155-165
    • Nieba, L.1    Krebber, A.2    Pluckthun, A.3
  • 54
    • 0030583234 scopus 로고    scopus 로고
    • Determination of active single chain antibody concentrations in crude periplasmic fractions
    • Kazemier B, de Haard H, Boender P, van Gemen B, Hoogenboom H. 1996. Determination of active single chain antibody concentrations in crude periplasmic fractions. J. Immunol. Methods 194:201-9
    • (1996) J. Immunol. Methods , vol.194 , pp. 201-209
    • Kazemier, B.1    De Haard, H.2    Boender, P.3    Van Gemen, B.4    Hoogenboom, H.5
  • 55
    • 0039711781 scopus 로고    scopus 로고
    • note
    • Deleted in proof
  • 59
    • 0024833055 scopus 로고
    • Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda
    • Huse WD, Sastry L, Iverson SA, Kang AS, Alting-Mees M, et al. 1989. Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda. Science 246:1275-81
    • (1989) Science , vol.246 , pp. 1275-1281
    • Huse, W.D.1    Sastry, L.2    Iverson, S.A.3    Kang, A.S.4    Alting-Mees, M.5
  • 60
    • 0033584995 scopus 로고    scopus 로고
    • Humanization of a murine monoclonal antibody by simultaneous optimization of framework and CDR residues
    • Wu H, Nie Y, Huse WD, Watkins JD. 1999. Humanization of a murine monoclonal antibody by simultaneous optimization of framework and CDR residues. J. Mol. Biol. 294:151-62
    • (1999) J. Mol. Biol. , vol.294 , pp. 151-162
    • Wu, H.1    Nie, Y.2    Huse, W.D.3    Watkins, J.D.4
  • 61
    • 0026699293 scopus 로고
    • Selection of phage antibodies by binding affinity. Mimicking affinity maturation
    • Hawkins RE, Russell SJ, Winter G. 1992. Selection of phage antibodies by binding affinity. Mimicking affinity maturation. J. Mol. Biol. 226:889-96
    • (1992) J. Mol. Biol. , vol.226 , pp. 889-896
    • Hawkins, R.E.1    Russell, S.J.2    Winter, G.3
  • 62
    • 0027933750 scopus 로고
    • Clonal selection and amplification of phage displayed antibodies by linking antigen recognition and phage replication
    • Duenas M, Borrebaeck CA. 1994. Clonal selection and amplification of phage displayed antibodies by linking antigen recognition and phage replication. Bio-Technology 12:999-1002
    • (1994) Bio-technology , vol.12 , pp. 999-1002
    • Duenas, M.1    Borrebaeck, C.A.2
  • 63
  • 65
    • 0032901290 scopus 로고    scopus 로고
    • Phage display technology - Finding a needle in a vast molecular haystack
    • Rodi DJ, Makowski L. 1999. Phage display technology - finding a needle in a vast molecular haystack. Curr. Opin. Biotechnol. 10:87-93
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 87-93
    • Rodi, D.J.1    Makowski, L.2
  • 66
    • 0031933840 scopus 로고    scopus 로고
    • Strategies for selection of antibodies by phage display
    • Griffiths AD, Duncan AR. 1998. Strategies for selection of antibodies by phage display. Curr. Opin. Biotechnol. 9:102-8
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 102-108
    • Griffiths, A.D.1    Duncan, A.R.2
  • 67
    • 14744287360 scopus 로고
    • Targeting recombinant antibodies to the surface of Escherichia coli: Fusion to a peptidoglycan associated lipoprotein
    • Fuchs P, Breitling F, Dubel S, Seehaus T, Little M. 1991. Targeting recombinant antibodies to the surface of Escherichia coli: fusion to a peptidoglycan associated lipoprotein. Bio-Technology 9:1369-72
    • (1991) Bio-technology , vol.9 , pp. 1369-1372
    • Fuchs, P.1    Breitling, F.2    Dubel, S.3    Seehaus, T.4    Little, M.5
  • 68
    • 0027425230 scopus 로고
    • Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface
    • Francisco JA, Campbell R, Iverson BL, Georgiou G. 1993. Production and fluorescence-activated cell sorting of Escherichia coli expressing a functional antibody fragment on the external surface. Proc. Natl. Acad. Sci. USA 90:10444-48
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10444-10448
    • Francisco, J.A.1    Campbell, R.2    Iverson, B.L.3    Georgiou, G.4
  • 69
  • 70
    • 0031012062 scopus 로고    scopus 로고
    • Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines
    • Georgiou G, Stathopoulos C, Daugherty PS, Nayak AR, Iverson BL, et al. 1997. Display of heterologous proteins on the surface of microorganisms: from the screening of combinatorial libraries to live recombinant vaccines. Nat. Biotechnol. 15: 29-34
    • (1997) Nat. Biotechnol. , vol.15 , pp. 29-34
    • Georgiou, G.1    Stathopoulos, C.2    Daugherty, P.S.3    Nayak, A.R.4    Iverson, B.L.5
  • 71
    • 0034049316 scopus 로고    scopus 로고
    • Quantitative analysis of the effect of the mutation frequency on the affinity maturation of antibodies
    • In press
    • Daugherty P, Chen G, Iverson B, Georgiou G. 2000. Quantitative analysis of the effect of the mutation frequency on the affinity maturation of antibodies. Proc. Natl. Acad. Sci. USA. In press
    • (2000) Proc. Natl. Acad. Sci. USA
    • Daugherty, P.1    Chen, G.2    Iverson, B.3    Georgiou, G.4
  • 72
    • 0039119658 scopus 로고    scopus 로고
    • note
    • Deleted in proof
  • 74
    • 0032895913 scopus 로고    scopus 로고
    • In vitro scanning saturation mutagenesis of all the specificity determining residues in an antibody binding site
    • Chen G, Dubrawsky I, Mendez P, Georgiou G, Iverson BL. 1999. In vitro scanning saturation mutagenesis of all the specificity determining residues in an antibody binding site. Protein Eng. 12:349-56
    • (1999) Protein Eng. , vol.12 , pp. 349-356
    • Chen, G.1    Dubrawsky, I.2    Mendez, P.3    Georgiou, G.4    Iverson, B.L.5
  • 75
    • 0039711778 scopus 로고    scopus 로고
    • note
    • Deleted in proof
  • 76
    • 0033152942 scopus 로고    scopus 로고
    • Totally in vitro protein selection using mRNA-protein fusions and ribosome display
    • Roberts RW. 1999. Totally in vitro protein selection using mRNA-protein fusions and ribosome display. Curr. Opin. Chem. Biol. 3:268-73
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 268-273
    • Roberts, R.W.1
  • 77
    • 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
  • 79
    • 0033029174 scopus 로고    scopus 로고
    • In vitro selection methods for screening of peptide and protein libraries
    • Hanes J, Pluckthun A. 1999. In vitro selection methods for screening of peptide and protein libraries. Curr. Top. Microbiol. Immunol. 243:107-22
    • (1999) Curr. Top. Microbiol. Immunol. , vol.243 , pp. 107-122
    • Hanes, J.1    Pluckthun, A.2
  • 80
    • 0031574037 scopus 로고    scopus 로고
    • Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites
    • He M, Taussig MJ. 1997. Antibody-ribosome-mRNA (ARM) complexes as efficient selection particles for in vitro display and evolution of antibody combining sites. Nucleic Acids Res. 25:5132-34
    • (1997) Nucleic Acids Res. , vol.25 , pp. 5132-5134
    • He, M.1    Taussig, M.J.2
  • 81
    • 0030817279 scopus 로고    scopus 로고
    • RNA-peptide fusions for the in vitro selection of peptides and proteins
    • Roberts R, Szostak JW. 1997. RNA-peptide fusions for the in vitro selection of peptides and proteins. Proc. Natl. Acad. Sci. USA 94:12297-302
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12297-12302
    • Roberts, R.1    Szostak, J.W.2
  • 82
  • 84
    • 0030200088 scopus 로고    scopus 로고
    • Selection and evolution of high-affinity human anti-viral antibodies
    • Barbas CF III, Burton DR. 1996. Selection and evolution of high-affinity human anti-viral antibodies. Trends Biotechnol. 14:230-34
    • (1996) Trends Biotechnol. , vol.14 , pp. 230-234
    • Barbas C.F. III1    Burton, D.R.2
  • 85
    • 0026057989 scopus 로고
    • Generation of diverse high-affinity human monoclonal antibodies by repertoire cloning
    • Persson MA, Caothien RH, Burton DR. 1991. Generation of diverse high-affinity human monoclonal antibodies by repertoire cloning. Proc. Natl. Acad. Sci. USA 88:2432-36
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2432-2436
    • Persson, M.A.1    Caothien, R.H.2    Burton, D.R.3
  • 86
    • 0030596493 scopus 로고    scopus 로고
    • Directing antigen specificity towards botulinum neurotoxin with combinatorial phage display libraries
    • Emanuel P, O'Brien T, Burans J, DasGupta BR, Valdes JJ, et al. 1996. Directing antigen specificity towards botulinum neurotoxin with combinatorial phage display libraries. J. Immunol. Methods 193:189-97
    • (1996) J. Immunol. Methods , vol.193 , pp. 189-197
    • Emanuel, P.1    O'Brien, T.2    Burans, J.3    Dasgupta, B.R.4    Valdes, J.J.5
  • 87
    • 0030803394 scopus 로고    scopus 로고
    • Comparison of fusion phage libraries displaying Vh of single chain Fv antibody fragments derived from the antibody repertoire of a vaccinated melanoma patient as a source of melanoma-specific targeting molecules
    • Cai XH, Garen A. 1997. Comparison of fusion phage libraries displaying Vh of single chain Fv antibody fragments derived from the antibody repertoire of a vaccinated melanoma patient as a source of melanoma-specific targeting molecules. Proc. Natl. Acad. Sci. USA 94:9261-66
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9261-9266
    • Cai, X.H.1    Garen, A.2
  • 88
    • 0031931487 scopus 로고    scopus 로고
    • Isolation of a high-affinity stable single-chain Fv specific for mesothelin from DNA-immunized mice by phage display and construction of a recombinant immunotoxin with anti-tumor activity
    • Chowdhury PS, Viner JL, Beers R, Pastan I. 1998. Isolation of a high-affinity stable single-chain Fv specific for mesothelin from DNA-immunized mice by phage display and construction of a recombinant immunotoxin with anti-tumor activity. Proc. Natl. Acad. Sci. USA 95:669-74
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 669-674
    • Chowdhury, P.S.1    Viner, J.L.2    Beers, R.3    Pastan, I.4
  • 89
    • 0033536071 scopus 로고    scopus 로고
    • Phage-display library selection of high-affinity human single-chain antibodies to tumor-associated carbohydrate antigens sialyl Lewisx and Lewisx
    • Mao S, Gao C, Lo CH, Wirsching P, Wong CH, et al. 1999. Phage-display library selection of high-affinity human single-chain antibodies to tumor-associated carbohydrate antigens sialyl Lewisx and Lewisx. Proc. Natl. Acad. Sci. USA 96:6953-58
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6953-6958
    • Mao, S.1    Gao, C.2    Lo, C.H.3    Wirsching, P.4    Wong, Ch.5
  • 90
    • 9344223986 scopus 로고    scopus 로고
    • Human antibodies with sub-nanomolar affinities isolated from a large non-immunized phage display library
    • Vaughan TJ, Williams AJ, Pritchard K, Osbourn JK, Pope AR, et al. 1996. Human antibodies with sub-nanomolar affinities isolated from a large non-immunized phage display library. Nat. Biotechnol. 14: 309-14
    • (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
  • 92
    • 0027473684 scopus 로고
    • Human anti-self antibodies with high specificity from phage display libraries
    • Griffiths AD, Malmqvist M, Marks JD, Bye JM, Embleton MJ, et al. 1993. Human anti-self 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
  • 93
    • 0030803049 scopus 로고    scopus 로고
    • Direct demonstration of MuSK involvement in acetylcholine receptor clustering through identification of agonist scfv
    • Xie M-H, Yuan J, Adams C, Gurney A. 1997. Direct demonstration of MuSK involvement in acetylcholine receptor clustering through identification of agonist scFv. Nat. Biotechnol. 15:768-71
    • (1997) Nat. Biotechnol. , vol.15 , pp. 768-771
    • Xie, M.-H.1    Yuan, J.2    Adams, C.3    Gurney, A.4
  • 94
    • 0032560552 scopus 로고    scopus 로고
    • Synthetic human antibodies and a strategy for protein engineering
    • Winter G. 1998. Synthetic human antibodies and a strategy for protein engineering. FEBS Lett. 430:92-94
    • (1998) FEBS Lett. , vol.430 , pp. 92-94
    • Winter, G.1
  • 95
    • 0026673067 scopus 로고
    • Bypassing immunisation. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro
    • Hoogenboom HR, Winter G. 1992. Bypassing immunisation. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro. J. Mol. Biol. 227:381-88
    • (1992) J. Mol. Biol. , vol.227 , pp. 381-388
    • Hoogenboom, H.R.1    Winter, G.2
  • 96
    • 0028006072 scopus 로고
    • Antibody fragments from a 'single pot' phage display library as immunochemical reagents
    • Nissim A, Hoogenboom HR, Tomlinson IM, Flynn G, Midgley C, et al. 1994. Antibody fragments from a 'single pot' phage display library as immunochemical reagents. EMBO J. 13:692-98
    • (1994) EMBO J. , vol.13 , pp. 692-698
    • Nissim, A.1    Hoogenboom, H.R.2    Tomlinson, I.M.3    Flynn, G.4    Midgley, C.5
  • 97
    • 0028291823 scopus 로고
    • Isolation of high affinity human antibodies directly from large synthetic repertoires
    • Griffiths AD, Williams SC, Hartley O, Tomlinson IM, Waterhouse P, et al. 1994. Isolation of high affinity human antibodies directly from large synthetic repertoires. EMBO J. 13:3245-60
    • (1994) EMBO J. , vol.13 , pp. 3245-3260
    • Griffiths, A.D.1    Williams, S.C.2    Hartley, O.3    Tomlinson, I.M.4    Waterhouse, P.5
  • 98
    • 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
  • 99
    • 0026563253 scopus 로고
    • Semisynthetic combinatorial antibody libraries: A chemical solution to the diversity problem
    • Barbas CF, Bain JD, Hoekstra DM, Lerner RA. 1992. Semisynthetic combinatorial antibody libraries: a chemical solution to the diversity problem. Proc. Natl. Acad. Sci. USA 89:4457-61
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4457-4461
    • Barbas, C.F.1    Bain, J.D.2    Hoekstra, D.M.3    Lerner, R.A.4
  • 100
    • 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 RM, Finnern R, Ouwehand WH, Griffiths AD, van Venrooij WJ, et al. 1996. 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. 26:629-39
    • (1996) Eur. J. Immunol. , vol.26 , pp. 629-639
    • De Wildt, R.M.1    Finnern, R.2    Ouwehand, W.H.3    Griffiths, A.D.4    Van Venrooij, W.J.5
  • 101
    • 0033058420 scopus 로고    scopus 로고
    • A recombinant, fully human monoclonal antibody with antitumor activity constructed from phage-displayed antibody fragments
    • Huls GA, Heijnen IA, Cuomo ME, Koningsberger JC, Wiegman L, et al. 1999. A recombinant, fully human monoclonal antibody with antitumor activity constructed from phage-displayed antibody fragments. Nat. Biotechnol. 17:276-81
    • (1999) Nat. Biotechnol. , vol.17 , pp. 276-281
    • Huls, G.A.1    Heijnen, I.A.2    Cuomo, M.E.3    Koningsberger, J.C.4    Wiegman, L.5
  • 102
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs with randomized trinucleotides
    • Knappik A, Ge L, Honegger A, Pack P, Fischer M, et al. 2000. Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs with randomized trinucleotides. J. Mol. Biol. 296:57-86
    • (2000) J. Mol. Biol. , vol.296 , pp. 57-86
    • Knappik, A.1    Ge, L.2    Honegger, A.3    Pack, P.4    Fischer, M.5
  • 103
    • 0029653368 scopus 로고
    • Kinetic and affinity limits on antibodies produced during immune responses
    • Foote J, Eisen HN. 1995. Kinetic and affinity limits on antibodies produced during immune responses. Proc. Natl. Acad. Sci. USA 92:1254-56
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1254-1256
    • Foote, J.1    Eisen, H.N.2
  • 104
    • 0030575802 scopus 로고    scopus 로고
    • Isolation of picomolar affinity anti-c-erbb-2 single-chain Fv by molecular evolution of the complementarity determining regions in the center of the antibody binding site
    • Schier R, McCall A, Adams GP, Marshall KW, Merritt H, et al. 1996. Isolation of picomolar affinity anti-c-erbB-2 single-chain Fv by molecular evolution of the complementarity determining regions in the center of the antibody binding site. J. Mol. Biol. 263:551-67
    • (1996) J. Mol. Biol. , vol.263 , pp. 551-567
    • Schier, R.1    McCall, A.2    Adams, G.P.3    Marshall, K.W.4    Merritt, H.5
  • 105
    • 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-Sweeney S, Briones AT, Burton DR, et al. 1995. CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range. J. Mol. Biol. 254:392-403
    • (1995) J. Mol. Biol. , vol.254 , pp. 392-403
    • Yang, W.P.1    Green, K.2    Pinz-Sweeney, S.3    Briones, A.T.4    Burton, D.R.5
  • 106
    • 0033527584 scopus 로고    scopus 로고
    • Selection and analysis of an optimized anti-VEGF antibody: Crystal structure of an affinity-matured Fab in complex with antigen
    • Chen Y, Wiesmann C, Fuh G, Li B, Christinger HW, et al. 1999. Selection and analysis of an optimized anti-VEGF antibody: crystal structure of an affinity-matured Fab in complex with antigen. J. Mol. Biol. 293:865-81
    • (1999) J. Mol. Biol. , vol.293 , pp. 865-881
    • Chen, Y.1    Wiesmann, C.2    Fuh, G.3    Li, B.4    Christinger, H.W.5
  • 107
    • 0040897758 scopus 로고    scopus 로고
    • note
    • Deleted in proof
  • 109
    • 0030864556 scopus 로고    scopus 로고
    • 3D structural information as a guide to protein engineering using genetic selection
    • Kast P, Hilvert D. 1997. 3D structural information as a guide to protein engineering using genetic selection. Curr. Opin. Struct. Biol. 7:470-79
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 470-479
    • Kast, P.1    Hilvert, D.2
  • 110
    • 0032483392 scopus 로고    scopus 로고
    • Improved stability and yield of a Fv-toxin fusion protein by computer design and protein engineering of the Fv
    • Chowdhury PS, Vasmatzis G, Beers R, Lee B, Pastan I. 1998. Improved stability and yield of a Fv-toxin fusion protein by computer design and protein engineering of the Fv. J. Mol. Biol. 281:917-28
    • (1998) J. Mol. Biol. , vol.281 , pp. 917-928
    • Chowdhury, P.S.1    Vasmatzis, G.2    Beers, R.3    Lee, B.4    Pastan, I.5
  • 111
    • 0023161406 scopus 로고
    • Mutation drift and repertoire shift in the maturation of the immune response
    • Berek C, Milstein C. 1987. Mutation drift and repertoire shift in the maturation of the immune response. Immunol. Rev. 96:23-41
    • (1987) Immunol. Rev. , vol.96 , pp. 23-41
    • Berek, C.1    Milstein, C.2
  • 112
    • 0033593356 scopus 로고    scopus 로고
    • Analysis of heavy and light chain pairings indicates that receptor editing shapes the human antibody repertoire
    • de Wildt RM, Hoet RMA, van Venrooij WJ, Tomlinson IM, Winter G. 1999. Analysis of heavy and light chain pairings indicates that receptor editing shapes the human antibody repertoire. J. Mol. Biol. 285:895-901
    • (1999) J. Mol. Biol. , vol.285 , pp. 895-901
    • De Wildt, R.M.1    Hoet, R.M.A.2    Van Venrooij, W.J.3    Tomlinson, I.M.4    Winter, G.5
  • 113
    • 0026336406 scopus 로고
    • Antibody redesign by chain shuffling from random combinatorial immunoglobulin libraries
    • Kang AS, Jones TM, Burton DR. 1991. Antibody redesign by chain shuffling from random combinatorial immunoglobulin libraries. Proc. Natl. Acad. Sci. USA 88:11120-23
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11120-11123
    • Kang, A.S.1    Jones, T.M.2    Burton, D.R.3
  • 115
    • 14744300211 scopus 로고
    • Bypassing immunization: Building high affinity human antibodies by chain shuffling
    • Marks JD, Griffiths AD, Malmqvist M, Clackson TP, Bye JM, et al. 1992. Bypassing immunization: building high affinity human antibodies by chain shuffling. Bio-Technology 10:779-83
    • (1992) Bio-Technology , vol.10 , pp. 779-783
    • Marks, J.D.1    Griffiths, A.D.2    Malmqvist, M.3    Clackson, T.P.4    Bye, J.M.5
  • 116
    • 0028141993 scopus 로고
    • Guiding the selection of human antibodies from phage display repertoires to a single epitope of an antigen
    • Jespers LS, Roberts A, Mahler SM, Winter G, Hoogenboom HR. 1994. Guiding the selection of human antibodies from phage display repertoires to a single epitope of an antigen. Bio-Technology 12: 899-903
    • (1994) Bio-Technology , vol.12 , pp. 899-903
    • Jespers, L.S.1    Roberts, A.2    Mahler, S.M.3    Winter, G.4    Hoogenboom, H.R.5
  • 117
    • 0029927859 scopus 로고    scopus 로고
    • Affinity maturation of a high-affinity human monoclonal antibody against the third hypervariable loop of human immunodeficiency virus: Use of phage display to improve affinity and broaden strain reactivity
    • Thompson J, Pope T, Tung JS, Chan C, Hollis G, et al. 1996. Affinity maturation of a high-affinity human monoclonal antibody against the third hypervariable loop of human immunodeficiency virus: use of phage display to improve affinity and broaden strain reactivity. J. Mol. Biol. 256:77-88
    • (1996) J. Mol. Biol. , vol.256 , pp. 77-88
    • Thompson, J.1    Pope, T.2    Tung, J.S.3    Chan, C.4    Hollis, G.5
  • 118
    • 0344631762 scopus 로고    scopus 로고
    • Expanding the conformational diversity by random insertions into CDRH2 results in improved anti-estradiol antibodies
    • Lamminmaki U, Pauperio S, Westerlund-Karlsson A, Karvinen J, Virtanen PL, et al. 1999. Expanding the conformational diversity by random insertions into CDRH2 results in improved anti-estradiol antibodies. J. Mol. Biol. 291:589-602
    • (1999) J. Mol. Biol. , vol.291 , pp. 589-602
    • Lamminmaki, U.1    Pauperio, S.2    Westerlund-Karlsson, A.3    Karvinen, J.4    Virtanen, P.L.5
  • 119
    • 85045502002 scopus 로고
    • Randomization of genes by PCR mutagenesis
    • Cadwell RC, Joyce GF. 1992. Randomization of genes by PCR mutagenesis. PCR Methods Appl. 2:28-33
    • (1992) PCR Methods Appl. , vol.2 , pp. 28-33
    • Cadwell, R.C.1    Joyce, G.F.2
  • 121
    • 0028816556 scopus 로고
    • Direct random mutagenesis of gene sized DNA fragments using polymerase chain reaction
    • Fromant M, Blanquet S, Plateau P. 1995. Direct random mutagenesis of gene sized DNA fragments using polymerase chain reaction. Anal. Biochem. 224:347-53
    • (1995) Anal. Biochem. , vol.224 , pp. 347-353
    • Fromant, M.1    Blanquet, S.2    Plateau, P.3
  • 122
    • 0029999325 scopus 로고    scopus 로고
    • Hypermutagenic PCR involving all four transitions and a sizeable proportion of transversions
    • Vartanian J-P, Henry M, Wain-Hobson S. 1996. Hypermutagenic PCR involving all four transitions and a sizeable proportion of transversions. Nucleic Acids Res. 24:2627-31
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2627-2631
    • Vartanian, J.-P.1    Henry, M.2    Wain-Hobson, S.3
  • 123
    • 0033555718 scopus 로고    scopus 로고
    • The effect of high frequency random mutagenesis on in vitro protein evolution: A study on TEM-1 beta-lactamase
    • Zaccolo M, Gherardi E. 1999. The effect of high frequency random mutagenesis on in vitro protein evolution: a study on TEM-1 beta-lactamase. J. Mol. Biol. 285:775-83
    • (1999) J. Mol. Biol. , vol.285 , pp. 775-783
    • Zaccolo, M.1    Gherardi, E.2
  • 124
    • 0026535931 scopus 로고
    • In vitro selection and affinity maturation of antibodies from a naive combinatorial immunoglobulin library
    • Gram H, Marconi LA, Barbas CF, Collet TA, Lerner RA, et al. 1992. In vitro selection and affinity maturation of antibodies from a naive combinatorial immunoglobulin library. Proc. Natl. Acad. Sci. USA 89:3576-80
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3576-3580
    • Gram, H.1    Marconi, L.A.2    Barbas, C.F.3    Collet, T.A.4    Lerner, R.A.5
  • 125
    • 0039711779 scopus 로고    scopus 로고
    • note
    • Deleted in proof
  • 127
    • 0005229135 scopus 로고    scopus 로고
    • Mimicking somatic hypermutation: Affinity maturation of antibodies displayed on bacteriophage using a bacterial mutator strain
    • Low NM, Holliger PH, Winter G. 1996. Mimicking somatic hypermutation: affinity maturation of antibodies displayed on bacteriophage using a bacterial mutator strain. J. Mol. Biol. 260:359-68
    • (1996) J. Mol. Biol. , vol.260 , pp. 359-368
    • Low, N.M.1    Holliger, P.H.2    Winter, G.3
  • 128
    • 0029931209 scopus 로고    scopus 로고
    • Affinity maturation of recombinant antibodies using E. coli mutator cells
    • Irving RA, Kortt AA, Hudson PJ. 1996. Affinity maturation of recombinant antibodies using E. coli mutator cells. Immunotechnology 2:127-43
    • (1996) Immunotechnology , vol.2 , pp. 127-143
    • Irving, R.A.1    Kortt, A.A.2    Hudson, P.J.3
  • 129
    • 0025082684 scopus 로고
    • Additivity of mutational effects in proteins
    • Wells JA. 1990. Additivity of mutational effects in proteins. Biochemistry 29:8509-17
    • (1990) Biochemistry , vol.29 , pp. 8509-8517
    • Wells, J.A.1
  • 130
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • Stemmer WPC. 1994. Rapid evolution of a protein in vitro by DNA shuffling. Nature 370:389-91
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 131
    • 0031909113 scopus 로고    scopus 로고
    • Molecular evolution by staggered extension process (StEP) in vitro recombination
    • Zhao H, Giver L, Shao Z, Affholter JA, Arnold F. 1998. Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat. Biotechnol. 16: 258-61
    • (1998) Nat. Biotechnol. , vol.16 , pp. 258-261
    • Zhao, H.1    Giver, L.2    Shao, Z.3    Affholter, J.A.4    Arnold, F.5
  • 132
    • 0032007562 scopus 로고    scopus 로고
    • Artificial evolution by DNA shuffling
    • Harayama S. 1998. Artificial evolution by DNA shuffling. Trends Biotechnol. 16: 76-82
    • (1998) Trends Biotechnol. , vol.16 , pp. 76-82
    • Harayama, S.1
  • 133
    • 0030048583 scopus 로고    scopus 로고
    • Construction and evolution of antibody-phage libraries by DNA shuffling
    • Crameri A, Cwirla S, Stemmer WPC. 1996. Construction and evolution of antibody-phage libraries by DNA shuffling. Nat. Med. 2:100-2
    • (1996) Nat. Med. , vol.2 , pp. 100-102
    • Crameri, A.1    Cwirla, S.2    Stemmer, W.P.C.3
  • 134
    • 0033584889 scopus 로고    scopus 로고
    • Selection for improved protein stability by phage display
    • Jung S, Honegger A, Pluckthun A. 1999. Selection for improved protein stability by phage display. J. Mol. Biol. 294:163-80
    • (1999) J. Mol. Biol. , vol.294 , pp. 163-180
    • Jung, S.1    Honegger, A.2    Pluckthun, A.3
  • 135
    • 0344813702 scopus 로고    scopus 로고
    • Antibody scFv fragments without disulfide bonds made by molecular evolution
    • Proba K, Worn A, Honegger A, Pluckthun A. 1998. Antibody scFv fragments without disulfide bonds made by molecular evolution. J. Mol. Biol. 275:245-53
    • (1998) J. Mol. Biol. , vol.275 , pp. 245-253
    • Proba, K.1    Worn, A.2    Honegger, A.3    Pluckthun, A.4
  • 136
    • 0031785720 scopus 로고    scopus 로고
    • Use of rituximab, the new FDA-approved antibody
    • Leget GA, Czuczman MS. 1998. Use of Rituximab, the new FDA-approved antibody. Curr. Opin. Oncol. 10:548-51
    • (1998) Curr. Opin. Oncol. , vol.10 , pp. 548-551
    • Leget, G.A.1    Czuczman, M.S.2
  • 137
    • 0032895235 scopus 로고    scopus 로고
    • Trastuzumab, a recombinant DNA-derived humanized monoclonal antibody, a novel agent for the treatment of metastatic breast cancer
    • Goldenberg MM. 1999. Trastuzumab, a recombinant DNA-derived humanized monoclonal antibody, a novel agent for the treatment of metastatic breast cancer. Clin.Ther. 21:309-18
    • (1999) Clin.Ther. , vol.21 , pp. 309-318
    • Goldenberg, M.M.1
  • 139
    • 0021713342 scopus 로고
    • Production of functional chimaeric mouse/human antibody
    • Boulianne GL, Hozumi N, Shulman MJ. 1984. Production of functional chimaeric mouse/human antibody. Nature 312:643-46
    • (1984) Nature , vol.312 , pp. 643-646
    • Boulianne, G.L.1    Hozumi, N.2    Shulman, M.J.3
  • 140
    • 0021716682 scopus 로고
    • Chimeric antibody molecules: Mouse antigen binding domains with human constant region domains
    • Morrison SL, Johnson MJ, Herzenberg LA, Oi VT. 1984. Chimeric antibody molecules: mouse antigen binding domains with human constant region domains. Proc. Natl. Acad. Sci. USA 81: 6851-55
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 6851-6855
    • Morrison, S.L.1    Johnson, M.J.2    Herzenberg, L.A.3    Oi, V.T.4
  • 141
    • 0029587683 scopus 로고
    • The immunogenicity of the 7E3 murine monoclonal Fab antibody fragment variable region is dramatically reduced in humans by substitution of human for murine constant regions
    • Knight DM, Wagner C, Jordan R, McAleer MF, DeRita R, et al. 1995. The immunogenicity of the 7E3 murine monoclonal Fab antibody fragment variable region is dramatically reduced in humans by substitution of human for murine constant regions. Mol. Immunol. 32:1271-81
    • (1995) Mol. Immunol. , vol.32 , pp. 1271-1281
    • Knight, D.M.1    Wagner, C.2    Jordan, R.3    McAleer, M.F.4    Derita, R.5
  • 142
    • 0027008595 scopus 로고
    • Engineering antibodies for therapy
    • Adair JR. 1992. Engineering antibodies for therapy. Immunol. Rev. 130:5-39
    • (1992) Immunol. Rev. , vol.130 , pp. 5-39
    • Adair, J.R.1
  • 144
    • 0022558297 scopus 로고
    • Replacing the complementarity determining regions in a human antibody with those from a mouse
    • Jones PT, Dear PH, Foote J, Neuberger MS, Winter G. 1986. Replacing the complementarity determining regions in a human antibody with those from a mouse. Nature 321:522-25
    • (1986) Nature , vol.321 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3    Neuberger, M.S.4    Winter, G.5
  • 145
    • 0031253786 scopus 로고    scopus 로고
    • VL:VH domain rotations in engineered antibodies: Crystal structures of the Fab fragments from two murine anti-tumor antibodies and their engineered human constructs
    • Banfield MJ, King DJ, Mountain A, Brady RL. 1997. VL:VH domain rotations in engineered antibodies: crystal structures of the Fab fragments from two murine anti-tumor antibodies and their engineered human constructs. Proteins: Struct. Funct. Genet. 29:161-71
    • (1997) Proteins: Struct. Funct. Genet. , vol.29 , pp. 161-171
    • Banfield, M.J.1    King, D.J.2    Mountain, A.3    Brady, R.L.4
  • 146
    • 0026559783 scopus 로고
    • Antibody framework residues affecting the conformation of the hypervariable loops
    • Foote J, Winter G. 1992. Antibody framework residues affecting the conformation of the hypervariable loops. J. Mol. Biol. 224:487-99
    • (1992) J. Mol. Biol. , vol.224 , pp. 487-499
    • Foote, J.1    Winter, G.2
  • 147
    • 0030910482 scopus 로고    scopus 로고
    • Humanization of a mouse monoclonal antibody that blocks the epidermal growth factor receptor: Recovery of antagonistic activity
    • Mateo C, Moreno E, Amour K, Lombardero J, Harris W, et al. 1997. Humanization of a mouse monoclonal antibody that blocks the epidermal growth factor receptor: recovery of antagonistic activity. Immunotechnology 3:71-81
    • (1997) Immunotechnology , vol.3 , pp. 71-81
    • Mateo, C.1    Moreno, E.2    Amour, K.3    Lombardero, J.4    Harris, W.5
  • 148
    • 0025848797 scopus 로고
    • A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties
    • Padlan EA. 1991. A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties. Mol. Immunol. 28:489-98
    • (1991) Mol. Immunol. , vol.28 , pp. 489-498
    • Padlan, E.A.1
  • 149
    • 0032952032 scopus 로고    scopus 로고
    • Effects of humanization by variable domain resurfacing on the antiviral activity of a single-chain antibody against respiratory syncytial virus
    • Delagrave S, Catalan J, Sweet C, Drabik G, Henry A, et al. 1999. Effects of humanization by variable domain resurfacing on the antiviral activity of a single-chain antibody against respiratory syncytial virus. Protein Eng. 12:357-62
    • (1999) Protein Eng. , vol.12 , pp. 357-362
    • Delagrave, S.1    Catalan, J.2    Sweet, C.3    Drabik, G.4    Henry, A.5
  • 151
    • 0032555214 scopus 로고    scopus 로고
    • A phage display approach for rapid antibody humanization: Designed combinatorial V gene libraries
    • Rader C, Cheresh DA, Barbas CF, 3rd. 1998. A phage display approach for rapid antibody humanization: designed combinatorial V gene libraries. Proc. Natl. Acad. Sci. USA 95:8910-15
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 8910-8915
    • Rader, C.1    Cheresh, D.A.2    Barbas C.F. III3
  • 152
    • 0342437532 scopus 로고    scopus 로고
    • Production of human antibody repertoires in transgenic mice
    • Bruggemann M, Taussig MJ. 1997. Production of human antibody repertoires in transgenic mice. Curr. Opin. Biotechnol. 8:455-58
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 455-458
    • Bruggemann, M.1    Taussig, M.J.2
  • 153
    • 8944243547 scopus 로고    scopus 로고
    • High-avidity human IgG kappa monoclonal antibodies from a novel strain of minilocus transgenic mice
    • Fishwild DM, O'Donnell SL, Bengoechea T, Hudson DV, Harding F, et al. 1996. High-avidity human IgG kappa monoclonal antibodies from a novel strain of minilocus transgenic mice. Nat. Biotechnol. 14:845-51
    • (1996) Nat. Biotechnol. , vol.14 , pp. 845-851
    • Fishwild, D.M.1    O'Donnell, S.L.2    Bengoechea, T.3    Hudson, D.V.4    Harding, F.5
  • 154
    • 0031039315 scopus 로고    scopus 로고
    • Functional transplant of megabase human immunoglobulin loci recapitulates human antibody response in mice
    • Mendez M, Green L, Corvalan J, Jia X-C, Maynard-Currie C, et al. 1997. Functional transplant of megabase human immunoglobulin loci recapitulates human antibody response in mice. Nat. Genet. 15:146-56
    • (1997) Nat. Genet. , vol.15 , pp. 146-156
    • Mendez, M.1    Green, L.2    Corvalan, J.3    Jia, X.-C.4    Maynard-Currie, C.5
  • 155
    • 0033559606 scopus 로고    scopus 로고
    • Eradication of established tumors by a fully human monoclonal antibody to the epidermal growth factor receptor without concomitant chemotherapy
    • Yang XD, Jia XC, Corvalan JR, Wang P, Davis CG, et al. 1999. Eradication of established tumors by a fully human monoclonal antibody to the epidermal growth factor receptor without concomitant chemotherapy. Cancer Res. 59:1236-43
    • (1999) Cancer Res. , vol.59 , pp. 1236-1243
    • Yang, X.D.1    Jia, X.C.2    Corvalan, J.R.3    Wang, P.4    Davis, C.G.5
  • 156
    • 0032822643 scopus 로고    scopus 로고
    • Fully human anti-interleukin-8 monoclonal antibodies: Potential therapeutics for the treatment of inflammatory disease states
    • Yang XD, Corvalan JR, Wang P, Roy CM, Davis CG. 1999. Fully human anti-interleukin-8 monoclonal antibodies: potential therapeutics for the treatment of inflammatory disease states. J. Leukocyte Biol. 66:401-10
    • (1999) J. Leukocyte Biol. , vol.66 , pp. 401-410
    • Yang, X.D.1    Corvalan, J.R.2    Wang, P.3    Roy, C.M.4    Davis, C.G.5
  • 157
    • 0030748513 scopus 로고    scopus 로고
    • Triabodies: Single chain Fv fragments without a linker form trivalent trimers
    • Iliades P, Kortt AA, Hudson PJ. 1997. Triabodies: single chain Fv fragments without a linker form trivalent trimers. FEBS Lett. 409:437-41
    • (1997) FEBS Lett. , vol.409 , pp. 437-441
    • Iliades, P.1    Kortt, A.A.2    Hudson, P.J.3
  • 158
    • 0030953197 scopus 로고    scopus 로고
    • Single-chain Fv fragments of anti-neuraminidase antibody NC10 containing five-and ten-residue linkers form dimers and with zero-residue linker a trimer
    • Kortt AA, Lah M, Oddie GW, Gruen CL, Burns JE, et al. 1997. Single-chain Fv fragments of anti-neuraminidase antibody NC10 containing five-and ten-residue linkers form dimers and with zero-residue linker a trimer. Protein Eng. 10: 423-33
    • (1997) Protein Eng. , vol.10 , pp. 423-433
    • Kortt, A.A.1    Lah, M.2    Oddie, G.W.3    Gruen, C.L.4    Burns, J.E.5
  • 159
    • 0032801102 scopus 로고    scopus 로고
    • Di-, tri-and tetrameric single chain Fv antibody fragments against human CD19: Effect of valency on cell binding
    • Le Gall F, Kipriyanov SM, Moldenhauer G, Little M. 1999. Di-, tri-and tetrameric single chain Fv antibody fragments against human CD19: effect of valency on cell binding. FEBS Lett. 453: 164-68
    • (1999) FEBS Lett. , vol.453 , pp. 164-168
    • Le Gall, F.1    Kipriyanov, S.M.2    Moldenhauer, G.3    Little, M.4
  • 160
    • 0030738617 scopus 로고    scopus 로고
    • New protein engineering approaches to multivalent and bispecific antibody fragments
    • Pluckthun A, Pack P. 1997. New protein engineering approaches to multivalent and bispecific antibody fragments. Immunotechnology 3:83-105
    • (1997) Immunotechnology , vol.3 , pp. 83-105
    • Pluckthun, A.1    Pack, P.2
  • 162
    • 0032478777 scopus 로고    scopus 로고
    • Orientation of antigen binding sites in dimeric and trimeric single chain fv antibody fragments
    • Lawrence LJ, Kortt AA, Iliades P, Tulloch PA, Hudson PJ. 1998. Orientation of antigen binding sites in dimeric and trimeric single chain Fv antibody fragments. FEBS Lett. 425:479-84
    • (1998) FEBS Lett. , vol.425 , pp. 479-484
    • Lawrence, L.J.1    Kortt, A.A.2    Iliades, P.3    Tulloch, P.A.4    Hudson, P.J.5
  • 163
    • 0030610418 scopus 로고    scopus 로고
    • The 2.0 Å resolution crystal structure of a trimeric antibody fragment with non-cognate Vh/Vl domain pairs shows a rearrangement of Vh CDR3
    • Pei XY, Holliger P, Murzin A, Williams RL. 1997. The 2.0 Å resolution crystal structure of a trimeric antibody fragment with non-cognate Vh/Vl domain pairs shows a rearrangement of Vh CDR3. Proc. Natl. Acad. Sci. USA 94:9637-42
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9637-9642
    • Pei, X.Y.1    Holliger, P.2    Murzin, A.3    Williams, R.L.4
  • 164
    • 0032144281 scopus 로고    scopus 로고
    • Model and simulation of multi-valent binding to fixed ligands
    • Muller KM, Arndt KM, Pluckthun A. 1998. Model and simulation of multi-valent binding to fixed ligands. Anal. Biochem. 261:149-58
    • (1998) Anal. Biochem. , vol.261 , pp. 149-158
    • Muller, K.M.1    Arndt, K.M.2    Pluckthun, A.3
  • 165
    • 0029918942 scopus 로고    scopus 로고
    • Tumor localization of anti-CEA single-chain Fvs: Improved tumor targeting by non-covalent dimers
    • Wu AM, Chen W, Raubitschek A, Williams LE, Neumaier M, et al. 1996. Tumor localization of anti-CEA single-chain Fvs: improved tumor targeting by non-covalent dimers. Immunotechnology 2:21-36
    • (1996) Immunotechnology , vol.2 , pp. 21-36
    • Wu, A.M.1    Chen, W.2    Raubitschek, A.3    Williams, L.E.4    Neumaier, M.5
  • 166
    • 0031942906 scopus 로고    scopus 로고
    • Prolonged in vivo tumour retention of a human diabody targeting the extracellular domain of human HER2/neu
    • Adams GP, Schier R, McCall AM, Crawford RS, Wolf EJ, et al. 1998. Prolonged in vivo tumour retention of a human diabody targeting the extracellular domain of human HER2/neu. Br. J. Cancer 77: 1405-12
    • (1998) Br. J. Cancer , vol.77 , pp. 1405-1412
    • Adams, G.P.1    Schier, R.2    McCall, A.M.3    Crawford, R.S.4    Wolf, E.J.5
  • 167
    • 0029877588 scopus 로고    scopus 로고
    • Affinity enhancement of a recombinant antibody: Formation of complexes with multiple valency by a single-chain fv fragment-core streptavidin fusion
    • Kipriyanov SM, Little M, Kropshofer H, Breitling F, Gotter S, et al. 1996. Affinity enhancement of a recombinant antibody: formation of complexes with multiple valency by a single-chain Fv fragment-core streptavidin fusion. Protein Eng. 9:203-11
    • (1996) Protein Eng. , vol.9 , pp. 203-211
    • Kipriyanov, S.M.1    Little, M.2    Kropshofer, H.3    Breitling, F.4    Gotter, S.5
  • 168
    • 0032822839 scopus 로고    scopus 로고
    • Recombinant antibody constructs in cancer therapy
    • Hudson PJ. 1999. Recombinant antibody constructs in cancer therapy. Curr. Opin. Immunol. 11:548-57
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 548-557
    • Hudson, P.J.1
  • 170
  • 171
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin Fv fragment in Escherichia coli
    • Skerra A, Pluckthun A. 1988. Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science 240: 1038-41
    • (1988) Science , vol.240 , pp. 1038-1041
    • Skerra, A.1    Pluckthun, A.2
  • 172
    • 0023922661 scopus 로고
    • Escherichia coli expression of an active chimeric antibody fragment
    • Better M, Chang CP, Robinson RR, Horwitz A. 1988. Escherichia coli expression of an active chimeric antibody fragment. Science 240:1041-43
    • (1988) Science , vol.240 , pp. 1041-1043
    • Better, M.1    Chang, C.P.2    Robinson, R.R.3    Horwitz, A.4
  • 173
    • 0027312336 scopus 로고
    • Bacterial expression of immunoglobulin fragments
    • Skerra A. 1993. Bacterial expression of immunoglobulin fragments. Curr. Opin. Immunol. 5:256-62
    • (1993) Curr. Opin. Immunol. , vol.5 , pp. 256-262
    • Skerra, A.1
  • 174
    • 0027973672 scopus 로고
    • Bacterial aspects associated with the expression of a single-chain antibody fragment in Escherichia coli
    • Somerville JE Jr, Goshorn SC, Fell HP, Darveau RP. 1994. Bacterial aspects associated with the expression of a single-chain antibody fragment in Escherichia coli. Appl. Microbiol. Biotechnol. 42:595-603
    • (1994) Appl. Microbiol. Biotechnol. , vol.42 , pp. 595-603
    • Somerville J.E., Jr.1    Goshorn, S.C.2    Fell, H.P.3    Darveau, R.P.4
  • 175
    • 0030731211 scopus 로고    scopus 로고
    • Regulation and expression of human fabs under the control of the Escherichia coli arabinose promoter, pBAD
    • Clark MA, Hammond FR, Papaioannou A, Hawkins NJ, Ward RL. 1997. Regulation and expression of human Fabs under the control of the Escherichia coli arabinose promoter, pBAD. Immunotechnology 3:217-26
    • (1997) Immunotechnology , vol.3 , pp. 217-226
    • Clark, M.A.1    Hammond, F.R.2    Papaioannou, A.3    Hawkins, N.J.4    Ward, R.L.5
  • 176
    • 0026350603 scopus 로고
    • Secretion and in vivo folding of the Fab fragment of the antibody McPc603 in Escherichia coli: Influence of disulphides and cis-prolines
    • Skerra A, Pluckthun A. 1991. Secretion and in vivo folding of the Fab fragment of the antibody McPC603 in Escherichia coli: influence of disulphides and cis-prolines. Protein Eng. 4:971-79
    • (1991) Protein Eng. , vol.4 , pp. 971-979
    • Skerra, A.1    Pluckthun, A.2
  • 177
    • 2642652226 scopus 로고    scopus 로고
    • Selection for a periplasmic factor improving phage display and functional periplasmic expression
    • Bothmann H, Pluckthun A. 1998. Selection for a periplasmic factor improving phage display and functional periplasmic expression. Nat. Biotechnol. 16:376-80
    • (1998) Nat. Biotechnol. , vol.16 , pp. 376-380
    • Bothmann, H.1    Pluckthun, A.2
  • 178
    • 0030041230 scopus 로고    scopus 로고
    • Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab' fragment expressed in Escherichia coli
    • Humphreys DP, Weir N, Lawson A, Mountain A, Lund PA. 1996. Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab' fragment expressed in Escherichia coli. FEBS Lett. 380:194-97
    • (1996) FEBS Lett. , vol.380 , pp. 194-197
    • Humphreys, D.P.1    Weir, N.2    Lawson, A.3    Mountain, A.4    Lund, P.A.5
  • 179
    • 0033117352 scopus 로고    scopus 로고
    • Escherichia coli skp chaperone coexpression improves solubility and phage display of single-chain antibody fragments
    • Hayhurst A, Harris WJ. 1999. Escherichia coli skp chaperone coexpression improves solubility and phage display of single-chain antibody fragments. Protein Exp. Purif. 15:336-43
    • (1999) Protein Exp. Purif. , vol.15 , pp. 336-343
    • Hayhurst, A.1    Harris, W.J.2
  • 180
    • 0029017297 scopus 로고
    • A point mutation in a murine immunoglobulin V-region strongly influences the antibody yield in Escherichia coli
    • Duenas M, Ayala M, Vazquez J, Ohlin M, Soderlind E, et al. 1995. A point mutation in a murine immunoglobulin V-region strongly influences the antibody yield in Escherichia coli. Gene 158:61-66
    • (1995) Gene , vol.158 , pp. 61-66
    • Duenas, M.1    Ayala, M.2    Vazquez, J.3    Ohlin, M.4    Soderlind, E.5
  • 181
    • 0030912095 scopus 로고    scopus 로고
    • Identification of framework residues in a secreted recombinant antibody fragment that controls production level and localization in Escherichia coli
    • Forsberg G, Forsgren M, Jaki M, Norin M, Sterky C, et al. 1997. Identification of framework residues in a secreted recombinant antibody fragment that controls production level and localization in Escherichia coli. J. Biol. Chem. 272:12430-36
    • (1997) J. Biol. Chem. , vol.272 , pp. 12430-12436
    • Forsberg, G.1    Forsgren, M.2    Jaki, M.3    Norin, M.4    Sterky, C.5
  • 182
    • 0030965970 scopus 로고    scopus 로고
    • Disrupting the hydrophobic patches at the antibody variable/constant domain interface: Improved in vivo folding and physical characterization of an engineered scFv fragment
    • Nieba L, Honegger A, Krebber C, Pluckthun A. 1997. Disrupting the hydrophobic patches at the antibody variable/constant domain interface: improved in vivo folding and physical characterization of an engineered scFv fragment. Protein Eng. 10:435-44
    • (1997) Protein Eng. , vol.10 , pp. 435-444
    • Nieba, L.1    Honegger, A.2    Krebber, C.3    Pluckthun, A.4
  • 183
    • 0030916353 scopus 로고    scopus 로고
    • Two amino acid mutations in an anti-human CD3 single chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity
    • Kipriyanov SM, Moldenhauer G, Martin AC, Kupriyanova OA, Little M. 1997. Two amino acid mutations in an anti-human CD3 single chain Fv antibody fragment that affect the yield on bacterial secretion but not the affinity. Protein Eng. 10:445-53
    • (1997) Protein Eng. , vol.10 , pp. 445-453
    • Kipriyanov, S.M.1    Moldenhauer, G.2    Martin, A.C.3    Kupriyanova, O.A.4    Little, M.5
  • 184
    • 1842295679 scopus 로고    scopus 로고
    • Improving in vivo folding and stability of a single-chain Fv antibody fragment by loop grafting
    • Jung S, Pluckthun A. 1997. Improving in vivo folding and stability of a single-chain Fv antibody fragment by loop grafting. Protein Eng. 10:959-66
    • (1997) Protein Eng. , vol.10 , pp. 959-966
    • Jung, S.1    Pluckthun, A.2
  • 185
    • 0040964401 scopus 로고    scopus 로고
    • Different equilibrium stability behavior of ScFv fragments: Identification, classification, and improvement by protein engineering
    • Worn A, Pluckthun A. 1999. Different equilibrium stability behavior of ScFv fragments: identification, classification, and improvement by protein engineering. Biochemistry 38:8739-50
    • (1999) Biochemistry , vol.38 , pp. 8739-8750
    • Worn, A.1    Pluckthun, A.2
  • 186
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • Buchner J, Rudolph R. 1991. Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli. Bio-Technology 9:157-62
    • (1991) Bio-Technology , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 187
    • 0029980026 scopus 로고    scopus 로고
    • Effect of additives on the renaturation of reduced lysozyme in the presence of 4 M urea
    • Maeda Y, Yamada H, Ueda T, Imoto T. 1996. Effect of additives on the renaturation of reduced lysozyme in the presence of 4 M urea. Protein Eng. 9:461-65
    • (1996) Protein Eng. , vol.9 , pp. 461-465
    • Maeda, Y.1    Yamada, H.2    Ueda, T.3    Imoto, T.4
  • 188
    • 0026792807 scopus 로고
    • A method for increasing the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies
    • Buchner J, Pastan I, Brinkmann U. 1992. A method for increasing the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal. Biochem. 205:263-70
    • (1992) Anal. Biochem. , vol.205 , pp. 263-270
    • Buchner, J.1    Pastan, I.2    Brinkmann, U.3
  • 189
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R, Lilie H. 1996. In vitro folding of inclusion body proteins. FASEB J. 10:49-56
    • (1996) FASEB J. , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 191
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli
    • Lilie H, Schwarz E, Rudolph R. 1998. Advances in refolding of proteins produced in E. coli. Curr. Opin. Biotechnol. 9:497-501
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 192
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • Derman AI, Prinz WA, Belin D, Beckwith J. 1993. Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262:1744-47
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 193
    • 0029068068 scopus 로고
    • Functional antibody single-chain fragments from the cytoplasm of Escherichia coli: Influence of thioredoxin reductase (TrxB)
    • Proba K, Ge L, Pluckthun A. 1995. Functional antibody single-chain fragments from the cytoplasm of Escherichia coli: influence of thioredoxin reductase (TrxB). Gene 159:203-7
    • (1995) Gene , vol.159 , pp. 203-207
    • Proba, K.1    Ge, L.2    Pluckthun, A.3
  • 194
    • 0028785535 scopus 로고
    • Functional expression of a single-chain anti-progesterone antibody fragment in the cytoplasm of a mutant Escherichia coli
    • He M, Hamon M, Liu H, Kang A, Taussig MJ. 1995. Functional expression of a single-chain anti-progesterone antibody fragment in the cytoplasm of a mutant Escherichia coli. Nucleic Acids Res. 23: 4009-10
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4009-4010
    • He, M.1    Hamon, M.2    Liu, H.3    Kang, A.4    Taussig, M.J.5
  • 195
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the escherichia coli cytoplasm
    • Bessette PH, Aslund F, Beckwith J, Georgiou G. 1999. Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc. Natl. Acad. Sci. USA 96:13703-8
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Aslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 196
    • 0032771488 scopus 로고    scopus 로고
    • The selection of intracellular antibodies
    • Cattaneo A, Biocca S. 1999. The selection of intracellular antibodies. Trends Biotechnol. 17:115-21
    • (1999) Trends Biotechnol. , vol.17 , pp. 115-121
    • Cattaneo, A.1    Biocca, S.2
  • 197
    • 0032524034 scopus 로고    scopus 로고
    • An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly
    • Worn A, Pluckthun A. 1998. An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly. FEBS Lett. 427:357-61
    • (1998) FEBS Lett. , vol.427 , pp. 357-361
    • Worn, A.1    Pluckthun, A.2
  • 198
    • 0031575401 scopus 로고    scopus 로고
    • A natural antibody missing a cysteine in VH: Consequences for thermodynamic stability and folding
    • Proba K, Honegger A, Pluckthun A. 1997. A natural antibody missing a cysteine in VH: consequences for thermodynamic stability and folding. J. Mol. Biol. 265:161-72
    • (1997) J. Mol. Biol. , vol.265 , pp. 161-172
    • Proba, K.1    Honegger, A.2    Pluckthun, A.3
  • 199
    • 0032479180 scopus 로고    scopus 로고
    • Expression of an antibody fragment at high levels in the bacterial cytoplasm
    • Martineau P, Jones P, Winter G. 1998. Expression of an antibody fragment at high levels in the bacterial cytoplasm. J. Mol. Biol. 280:117-27
    • (1998) J. Mol. Biol. , vol.280 , pp. 117-127
    • Martineau, P.1    Jones, P.2    Winter, G.3
  • 201
    • 0033520343 scopus 로고    scopus 로고
    • Intrabody construction and expression: I. The critical role of VL domain stability
    • Ohage E, Steipe B. 1999. Intrabody construction and expression: I. The critical role of VL domain stability. J. Mol. Biol. 291:1119-28
    • (1999) J. Mol. Biol. , vol.291 , pp. 1119-1128
    • Ohage, E.1    Steipe, B.2
  • 202
    • 0033520452 scopus 로고    scopus 로고
    • Intrabody construction and expression: II. A synthetic catalytic Fv fragment
    • Ohage EC, Wirtz P, Barnikow J, Steipe B. 1999. Intrabody construction and expression: II. A synthetic catalytic Fv fragment. J. Mol. Biol. 291:1129-34
    • (1999) J. Mol. Biol. , vol.291 , pp. 1129-1134
    • Ohage, E.C.1    Wirtz, P.2    Barnikow, J.3    Steipe, B.4
  • 203
    • 0029797560 scopus 로고    scopus 로고
    • Oral immunization with an anti-idiotypic antibody to the exoglycolipid antigen protects against experimental Chlamydia trachomatis infection
    • Whittum-Hudson JA, An LL, Saltzman WM, Prendergast RA, MacDonald AB. 1996. Oral immunization with an anti-idiotypic antibody to the exoglycolipid antigen protects against experimental Chlamydia trachomatis infection. Nat. Med. 2:1116-21
    • (1996) Nat. Med. , vol.2 , pp. 1116-1121
    • Whittum-Hudson, J.A.1    An, L.L.2    Saltzman, W.M.3    Prendergast, R.A.4    MacDonald, A.B.5
  • 204
    • 0033168269 scopus 로고    scopus 로고
    • Exploiting antibody-based technologies to manage environmental pollution
    • Harris B. 1999. Exploiting antibody-based technologies to manage environmental pollution. Trends Biotechnol. 17: 290-96
    • (1999) Trends Biotechnol. , vol.17 , pp. 290-296
    • Harris, B.1
  • 205
    • 0032910690 scopus 로고    scopus 로고
    • A recombinant single-chain antibody fragment that neutralizes toxin II from the venom of the scorpion Androctonus australis hector
    • Mousli M, Devaux C, Rochat H, Goyffon M, Billiad P. 1999. A recombinant single-chain antibody fragment that neutralizes toxin II from the venom of the scorpion Androctonus australis hector. FEBS Lett. 442:183-88
    • (1999) FEBS Lett. , vol.442 , pp. 183-188
    • Mousli, M.1    Devaux, C.2    Rochat, H.3    Goyffon, M.4    Billiad, P.5
  • 206
    • 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 III, Hu D, Dunlop N, Sawyer L, Cababa D, et al. 1994. 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 91:3809-13
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3809-3813
    • Barbas C.F. III1    Hu, D.2    Dunlop, N.3    Sawyer, L.4    Cababa, D.5
  • 207
    • 0031449456 scopus 로고    scopus 로고
    • Passive immunization with a human monoclonal antibody protects hu-PBL-SCID mice against challenge by primary isolates of HIV-1
    • Gauduin MC, Parren PW, Weir R, Barbas CF, Burton DR, et al. 1997. Passive immunization with a human monoclonal antibody protects hu-PBL-SCID mice against challenge by primary isolates of HIV-1. Nat. Med. 3:1389-93
    • (1997) Nat. Med. , vol.3 , pp. 1389-1393
    • Gauduin, M.C.1    Parren, P.W.2    Weir, R.3    Barbas, C.F.4    Burton, D.R.5
  • 208
    • 0029294009 scopus 로고
    • Intracellular antibodies (intrabodies) as research reagents and therapeutic molecules for gene therapy
    • Marasco W. 1995. Intracellular antibodies (intrabodies) as research reagents and therapeutic molecules for gene therapy. Immunotechnology 1:1-19
    • (1995) Immunotechnology , vol.1 , pp. 1-19
    • Marasco, W.1
  • 209
    • 0033617248 scopus 로고    scopus 로고
    • Targeted gene delivery to mammalian cells by filamentous bacteriophage
    • Poul MA, Marks JD. 1999. Targeted gene delivery to mammalian cells by filamentous bacteriophage. J. Mol. Biol. 288: 203-11
    • (1999) J. Mol. Biol. , vol.288 , pp. 203-211
    • Poul, M.A.1    Marks, J.D.2
  • 210
    • 0027275371 scopus 로고
    • Design, intracellular exression, and activity of a human anti-human immunodeficiency virus type I gp120 single-chain antibody
    • Marasco W, Haseltine WA, Chen S. 1993. Design, intracellular exression, and activity of a human anti-human immunodeficiency virus type I gp120 single-chain antibody. Proc. Natl. Acad. Sci. USA 90:7889-93
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7889-7893
    • Marasco, W.1    Haseltine, W.A.2    Chen, S.3
  • 211
    • 0028955535 scopus 로고
    • Phenotypic knockout of the high-affinity human interleukin 2 receptor by intracellular single-chain antibodies against the alpha subunit of the receptor
    • Richardson JH, Sodroski JG, Waldmann TA, Marasco WA. 1995. Phenotypic knockout of the high-affinity human interleukin 2 receptor by intracellular single-chain antibodies against the alpha subunit of the receptor. Proc. Natl. Acad. Sci. USA 92:3137-41
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3137-3141
    • Richardson, J.H.1    Sodroski, J.G.2    Waldmann, T.A.3    Marasco, W.A.4
  • 212
    • 0028148050 scopus 로고
    • Intracellular expression of single chain antibodies reverts ErbB-2 transformation
    • Beerli RR, Weis W, Hynes NE. 1994. Intracellular expression of single chain antibodies reverts ErbB-2 transformation. J. Biol. Chem. 289:23931-36
    • (1994) J. Biol. Chem. , vol.289 , pp. 23931-23936
    • Beerli, R.R.1    Weis, W.2    Hynes, N.E.3
  • 213
    • 9544250404 scopus 로고    scopus 로고
    • Clinical evidence of efficient tumor targeting based on single-chain Fv antibody selected from a combinatorial library
    • Begent RHJ. 1996. Clinical evidence of efficient tumor targeting based on single-chain Fv antibody selected from a combinatorial library. Nat. Med. 2:979-84
    • (1996) Nat. Med. , vol.2 , pp. 979-984
    • Begent, R.H.J.1
  • 214
    • 0025912062 scopus 로고
    • Monoclonal antibodies in diagnosis and therapy
    • Waldmann TA. 1991. Monoclonal antibodies in diagnosis and therapy. Science 252:1657-62
    • (1991) Science , vol.252 , pp. 1657-1662
    • Waldmann, T.A.1
  • 215
    • 0029118828 scopus 로고
    • Radiometal labeling of recombinant proteins by a genetically engineered minimal chelation site: Technetium-99m coordination by single-chain Fv antibody fusion proteins through a C-terminal cysteinyl peptide
    • George AJ, Jamar F, Tai MS, Heelan BT, Adams GP, et al. 1995. Radiometal labeling of recombinant proteins by a genetically engineered minimal chelation site: technetium-99m coordination by single-chain Fv antibody fusion proteins through a C-terminal cysteinyl peptide. Proc. Natl. Acad. Sci. USA 92:8358-62
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 8358-8362
    • George, A.J.1    Jamar, F.2    Tai, M.S.3    Heelan, B.T.4    Adams, G.P.5
  • 217
    • 0032884409 scopus 로고    scopus 로고
    • Stable one-step technetium-99m labeling of histagged recombinant proteins with a novel Tc(I)-carbonyl complex
    • Waibel R, Alberto R, Willuda J, Finnern R, Schibli R, et al. 1999. Stable one-step technetium-99m labeling of histagged recombinant proteins with a novel Tc(I)-carbonyl complex. Nat. Biotechnol. 17:897-901
    • (1999) Nat. Biotechnol. , vol.17 , pp. 897-901
    • Waibel, R.1    Alberto, R.2    Willuda, J.3    Finnern, R.4    Schibli, R.5
  • 219
    • 0033118889 scopus 로고    scopus 로고
    • Inhibitory effects of combinations of HER-2/neu antibody and chemotherapeutic agents used for treatment of human breast cancers
    • Pegram M, Hsu S, Lewis G, Pietras R, Beryt M, et al. 1999. Inhibitory effects of combinations of HER-2/neu antibody and chemotherapeutic agents used for treatment of human breast cancers. Oncogene 18:2241-51
    • (1999) Oncogene , vol.18 , pp. 2241-2251
    • Pegram, M.1    Hsu, S.2    Lewis, G.3    Pietras, R.4    Beryt, M.5
  • 221
    • 0001160175 scopus 로고    scopus 로고
    • In vitro and in vivo targeting of immunoliposomal doxorubicin to human B-cell lymphoma
    • Lopes de Menezes DE, Pilarski LM, Allen TM. 1998. In vitro and in vivo targeting of immunoliposomal doxorubicin to human B-cell lymphoma. Cancer Res. 58:3320-30
    • (1998) Cancer Res. , vol.58 , pp. 3320-3330
    • Lopes De Menezes, D.E.1    Pilarski, L.M.2    Allen, T.M.3
  • 222
    • 0032872567 scopus 로고    scopus 로고
    • Monoclonal antibody drug conjugates in the treatment of cancer
    • Trail PA, Bianchi AB. 1999. Monoclonal antibody drug conjugates in the treatment of cancer. Curr. Opin. Immunol. 11:584-88
    • (1999) Curr. Opin. Immunol. , vol.11 , pp. 584-588
    • Trail, P.A.1    Bianchi, A.B.2
  • 223
    • 0033567023 scopus 로고    scopus 로고
    • Pharmacokinetics and antitumor activity of a bivalent disulfide-stabilized Fv immunotoxin with improved antigen binding to erbB2
    • Bera TK, Viner J, Brinkmann E, Pastan I. 1999. Pharmacokinetics and antitumor activity of a bivalent disulfide-stabilized Fv immunotoxin with improved antigen binding to erbB2. Cancer Res. 59:4018-22
    • (1999) Cancer Res. , vol.59 , pp. 4018-4022
    • Bera, T.K.1    Viner, J.2    Brinkmann, E.3    Pastan, I.4
  • 224
    • 0031838498 scopus 로고    scopus 로고
    • Clinical trials with pseudomonas exotoxin immunotoxins
    • Pai LH, Pastan I. 1998. Clinical trials with Pseudomonas exotoxin immunotoxins. Curr. Top. Microbiol. Immunol. 234: 83-96
    • (1998) Curr. Top. Microbiol. Immunol. , vol.234 , pp. 83-96
    • Pai, L.H.1    Pastan, I.2
  • 225
    • 0032904481 scopus 로고    scopus 로고
    • Recombinant immunotoxins directed against the c-erb-2/HER2/neu oncogene product: In vitro cytotoxicity, pharmacokinatics, and in vivo efficacy studies in xenograft models
    • Rosenblum MG, Shawver LK, Marks JW, Bringk J, Cheung L, et al. 1999. Recombinant immunotoxins directed against the c-erb-2/HER2/neu oncogene product: in vitro cytotoxicity, pharmacokinatics, and in vivo efficacy studies in xenograft models. Clin. Cancer Res. 5:865-74
    • (1999) Clin. Cancer Res. , vol.5 , pp. 865-874
    • Rosenblum, M.G.1    Shawver, L.K.2    Marks, J.W.3    Bringk, J.4    Cheung, L.5
  • 227
    • 0029096112 scopus 로고
    • Engineering high affinity humanized anti-p185(HER2)/anti-CD3 bispecific F(ab′)2 for efficient lysis of p185(HER2) overexpressing tumor cells
    • Zhu Z, Lewis GD, Carter P. 1995. Engineering high affinity humanized anti-p185(HER2)/anti-CD3 bispecific F(ab′)2 for efficient lysis of p185(HER2) overexpressing tumor cells. Int. J. Cancer 62: 319-24
    • (1995) Int. J. Cancer , vol.62 , pp. 319-324
    • Zhu, Z.1    Lewis, G.D.2    Carter, P.3
  • 228
    • 0030858083 scopus 로고    scopus 로고
    • Bispecific antibody-dependent cellular cytotoxicity of HER2/neu-overexpressing tumor cells by Fc-gamma receptor type I-expressing cells
    • Keler T, Graziano RF, Mandai A, Wallace PK, Fisher J, et al. 1997. Bispecific antibody-dependent cellular cytotoxicity of HER2/neu-overexpressing tumor cells by Fc-gamma receptor type I-expressing cells. Cancer Res. 57:4008-14
    • (1997) Cancer Res. , vol.57 , pp. 4008-4014
    • Keler, T.1    Graziano, R.F.2    Mandai, A.3    Wallace, P.K.4    Fisher, J.5
  • 229
    • 0032513528 scopus 로고    scopus 로고
    • Construction and characterization of a bispecific diabody for retargeting T cells to human carcinomas
    • Helfrich W, Kroesen BJ, Roovers RC, Westers L, Molema G, et al. 1998. Construction and characterization of a bispecific diabody for retargeting T cells to human carcinomas. Int. J. Cancer 76:232-39
    • (1998) Int. J. Cancer , vol.76 , pp. 232-239
    • Helfrich, W.1    Kroesen, B.J.2    Roovers, R.C.3    Westers, L.4    Molema, G.5
  • 230
    • 0031409362 scopus 로고    scopus 로고
    • Epidermal growth factor receptor inhibition by a monoclonal antibody as anticancer therapy
    • Mendelsohn J. 1997. Epidermal growth factor receptor inhibition by a monoclonal antibody as anticancer therapy. Clin. Cancer Res. 3:2703-7
    • (1997) Clin. Cancer Res. , vol.3 , pp. 2703-2707
    • Mendelsohn, J.1
  • 231
    • 0033302303 scopus 로고    scopus 로고
    • Transport of molecules, particles, and cells in solid tumors
    • Jain RK. 1999. Transport of molecules, particles, and cells in solid tumors. Annu. Rev. Biomed. Eng. 1:241-63
    • (1999) Annu. Rev. Biomed. Eng. , vol.1 , pp. 241-263
    • Jain, R.K.1
  • 232
    • 0026327378 scopus 로고
    • Construction, binding properties, metabolism, and tumor-targeting of a single-chain Fv derived from the pancarcinoma monoclonal antibody CC49
    • Milenic DE, Yokota T, Filpula DR, Finkelman MAJ, Dodd SW, et al. 1991. Construction, binding properties, metabolism, and tumor-targeting of a single-chain Fv derived from the pancarcinoma monoclonal antibody CC49. Cancer Res. 51:6363-71
    • (1991) Cancer Res. , vol.51 , pp. 6363-6371
    • Milenic, D.E.1    Yokota, T.2    Filpula, D.R.3    Finkelman, M.A.J.4    Dodd, S.W.5
  • 233
    • 0032006660 scopus 로고    scopus 로고
    • Increased affinity leads to improved selective tumor delivery of single-chain Fv antibodies
    • Adams GP, Schier R, Marshall K, Wolf EJ, McCall AM, et al. 1998. Increased affinity leads to improved selective tumor delivery of single-chain Fv antibodies. Cancer Res. 58:485-90
    • (1998) Cancer Res. , vol.58 , pp. 485-490
    • Adams, G.P.1    Schier, R.2    Marshall, K.3    Wolf, E.J.4    McCall, A.M.5
  • 234
    • 0028885668 scopus 로고
    • Biodistribution of monoclonal antibodies: Scale-up from mouse to human using a physiologically based pharmacokinetic model
    • Baxter LT, Zhu H, Mackensen DG, Butler WF, Jain RK. 1995. Biodistribution of monoclonal antibodies: scale-up from mouse to human using a physiologically based pharmacokinetic model. Cancer Res. 55:4611-22
    • (1995) Cancer Res. , vol.55 , pp. 4611-4622
    • Baxter, L.T.1    Zhu, H.2    Mackensen, D.G.3    Butler, W.F.4    Jain, R.K.5
  • 235
    • 0033555628 scopus 로고    scopus 로고
    • Increased binding affinity and valence of recombinant antibody fragments lead to improved targeting of tumoral angiogenesis
    • Viti F, Tarli L, Giovannoni L, Zardi L, Neri D. 1999. Increased binding affinity and valence of recombinant antibody fragments lead to improved targeting of tumoral angiogenesis. Cancer Res. 59:347-52
    • (1999) Cancer Res. , vol.59 , pp. 347-352
    • Viti, F.1    Tarli, L.2    Giovannoni, L.3    Zardi, L.4    Neri, D.5


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