메뉴 건너뛰기




Volumn 14, Issue 1-2, 2005, Pages 33-55

Monoclonal and recombinant antibodies, 30 years after...

Author keywords

Engineering; Expression system; Immunotherapy; Phage display; Recombinant antibodies

Indexed keywords

ABCIXIMAB; ADALIMUMAB; ALEMTUZUMAB; ANTICALIN; AVASTATIN; BASILIXIMAB; CETUXIMAB; DACLIZUMAB; EFALIZUMAB; GEMTUZUMAB OZOGAMICIN; IBRITUMOMAB TIUXETAN; INFLIXIMAB; J 591; LUMILIXIMAB; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY IDEC 114; MONOCLONAL ANTIBODY IDEC 151; MONOCLONAL ANTIBODY IDEC C9.1; NATALIZUMAB; OKT 3; OMALIZUMAB; PALIVIZUMAB; RADIOISOTOPE; RECOMBINANT ANTIBODY; RITUXIMAB; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY; TOSITUMOMAB I 131; TRASTUZUMAB; TROMBOVIEW; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 30944449218     PISSN: 10932607     EISSN: None     Source Type: Journal    
DOI: 10.3233/hab-2005-141-206     Document Type: Review
Times cited : (43)

References (216)
  • 1
    • 2442552141 scopus 로고    scopus 로고
    • Monoclonal antibodies market
    • J. Reichert and A. Pavlou, Monoclonal antibodies market, Nature Rev 3 (2004), 383-384.
    • (2004) Nature Rev , vol.3 , pp. 383-384
    • Reichert, J.1    Pavlou, A.2
  • 2
    • 14844285410 scopus 로고    scopus 로고
    • The therapeutic antibodies market to 2008
    • A. Pavlou and M.J. Belsey, The therapeutic antibodies market to 2008, Eur J Pharm Biopharm 59 (2005), 389-396.
    • (2005) Eur J Pharm Biopharm , vol.59 , pp. 389-396
    • Pavlou, A.1    Belsey, M.J.2
  • 3
    • 16644391767 scopus 로고    scopus 로고
    • Antibody-cytokine fusion proteins for the therapy of cancer
    • G. Helguera and M.L. Penichet, Antibody-cytokine fusion proteins for the therapy of cancer, Methods Mol Med 109 (2005), 347-374.
    • (2005) Methods Mol Med , vol.109 , pp. 347-374
    • Helguera, G.1    Penichet, M.L.2
  • 4
    • 8644240039 scopus 로고    scopus 로고
    • Antibody-cytokine fusion proteins: Innovative weapons in the war against cancer
    • J.S. Dela Cruz, T.H. Huang, M.L. Penichet and S.L. Morrison, Antibody-cytokine fusion proteins: innovative weapons in the war against cancer, Clin Exp Med 4(2) (2004), 57-64.
    • (2004) Clin Exp Med , vol.4 , Issue.2 , pp. 57-64
    • Dela Cruz, J.S.1    Huang, T.H.2    Penichet, M.L.3    Morrison, S.L.4
  • 5
    • 15244351004 scopus 로고    scopus 로고
    • Overview of monoclonal antibodies in cancer therapy: Present and promise
    • M. Stern and R. Herrmann, Overview of monoclonal antibodies in cancer therapy: present and promise, Crit Rev Oncol Hematol 54 (2005), 11-29.
    • (2005) Crit Rev Oncol Hematol , vol.54 , pp. 11-29
    • Stern, M.1    Herrmann, R.2
  • 6
    • 16644401173 scopus 로고    scopus 로고
    • The use of antibodies to coagulation factors for anticoagulant therapy
    • M. Jacquemin and J.M. Saint-Remy, The use of antibodies to coagulation factors for anticoagulant therapy, Curr Med Chem 11 (2004), 2291-2296.
    • (2004) Curr Med Chem , vol.11 , pp. 2291-2296
    • Jacquemin, M.1    Saint-Remy, J.M.2
  • 7
    • 0036958769 scopus 로고    scopus 로고
    • Therapeutic potential of monoclonal antibodies in myocardial reperfusion injury
    • A. Nigam and S.L. Kopecky, Therapeutic potential of monoclonal antibodies in myocardial reperfusion injury, Am J Cardiovasc Drugs 2 (2002), 367-376.
    • (2002) Am J Cardiovasc Drugs , vol.2 , pp. 367-376
    • Nigam, A.1    Kopecky, S.L.2
  • 8
    • 4444342539 scopus 로고    scopus 로고
    • Passive antibody therapy for infectious diseases
    • A. Casadevall, E. Dadachova and L.A. Pirofski, Passive antibody therapy for infectious diseases, Nat Rev Microbiol 2(9) (2004), 695-703.
    • (2004) Nat Rev Microbiol , vol.2 , Issue.9 , pp. 695-703
    • Casadevall, A.1    Dadachova, E.2    Pirofski, L.A.3
  • 9
    • 13244269945 scopus 로고    scopus 로고
    • Single-chain fragment variable antibody piezoi-imunosensors
    • Z. Shen, G.A. Stryker, R.L. Mernaugh, L. Yu, H. Yan and X. Zeng, Single-chain fragment variable antibody piezoi-imunosensors, Anal Chem 77 (2005), 797-805.
    • (2005) Anal Chem , vol.77 , pp. 797-805
    • Shen, Z.1    Stryker, G.A.2    Mernaugh, R.L.3    Yu, L.4    Yan, H.5    Zeng, X.6
  • 12
    • 0016756272 scopus 로고
    • Continous cultures of fused cells secreting antibody of predefined specificity
    • G. Kohler and C. Milstein, Continous cultures of fused cells secreting antibody of predefined specificity, Nature 256 (1975), 495-497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 13
    • 0021999401 scopus 로고
    • Human anti-murine immunoglobulin responses in patients receiving monoclonal antibody therapy
    • R.W. Schroff, K.F. Foon, S.M. Beatty, R.K. Oldham and A.C.J. Morgan, Human anti-murine immunoglobulin responses in patients receiving monoclonal antibody therapy, Cancer Res 45 (1985), 879-885.
    • (1985) Cancer Res , vol.45 , pp. 879-885
    • Schroff, R.W.1    Foon, K.F.2    Beatty, S.M.3    Oldham, R.K.4    Morgan, A.C.J.5
  • 14
    • 0021716682 scopus 로고
    • Chimeric human antibody molecules mouse antigen-binding domains with human constant region domains
    • S.L. Morrison, M.J. Johnson, L.A. Herzenberg and V.T. Oi, Chimeric human antibody molecules mouse antigen-binding domains with human constant region domains, Proc Natl Acad Sci USA 81 (1984), 6851-6855.
    • (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
  • 15
    • 0022558297 scopus 로고
    • Replacing the complementary-determining regions in a human antibody with those from a mouse
    • P.T. Jones, P.H. Dear, J. Foote, M. Neuberger and G. Winter, Replacing the complementary-determining regions in a human antibody with those from a mouse, Nature 321 (1986), 522-525.
    • (1986) Nature , vol.321 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3    Neuberger, M.4    Winter, G.5
  • 16
    • 0042838162 scopus 로고    scopus 로고
    • Humanization of predicted T-cell epitopes reduces the immunogenicity of chimeric antibodies: New evidence supporting a simple method
    • L. Roque-Navarro, C. Mateo, J. Lombardero, G. Mustelier, A. Fernandez, K. Sosa, S.L. Morrison and R. Perez, Humanization of predicted T-cell epitopes reduces the immunogenicity of chimeric antibodies: new evidence supporting a simple method, Hybrid Hybridomics 22 (2003), 245-257.
    • (2003) Hybrid Hybridomics , vol.22 , pp. 245-257
    • Roque-Navarro, L.1    Mateo, C.2    Lombardero, J.3    Mustelier, G.4    Fernandez, A.5    Sosa, K.6    Morrison, S.L.7    Perez, R.8
  • 17
    • 0034532441 scopus 로고    scopus 로고
    • Removal of amphipathic epitopes from genetically engineered antibodies: Production of modified immunoglobulins with reduced immunogenicity
    • C. Mateo, J. Lombardero, E. Moreno, G. Bombino, J. Coloma, L. Wims, S.L. Morrison and R. Perez, Removal of amphipathic epitopes from genetically engineered antibodies: production of modified immunoglobulins with reduced immunogenicity, Hybridoma 19 (2000), 463-471.
    • (2000) Hybridoma , vol.19 , pp. 463-471
    • Mateo, C.1    Lombardero, J.2    Moreno, E.3    Bombino, G.4    Coloma, J.5    Wims, L.6    Morrison, S.L.7    Perez, R.8
  • 18
    • 0037434552 scopus 로고    scopus 로고
    • Influence of immunogenicity on the long-term efficacy of infliximab in Crohn's disease
    • F. Baert, M. Noman, S. Vermeire, G. Van Assche, G DH, A. Carbonez and P. Rutgeerts, Influence of immunogenicity on the long-term efficacy of infliximab in Crohn's disease, N Engl J Med 348(7) (2003), 601-608.
    • (2003) N Engl J Med , vol.348 , Issue.7 , pp. 601-608
    • Baert, F.1    Noman, M.2    Vermeire, S.3    Van Assche, G.4    Dh, G.5    Carbonez, A.6    Rutgeerts, P.7
  • 20
    • 0023911111 scopus 로고
    • Reshaping human antibodies for therapy
    • L. Riechmann, H. Clark, H. Waldmann and G. Winter, Reshaping human antibodies for therapy, Nature 332 (1988), 323-327.
    • (1988) Nature , vol.332 , pp. 323-327
    • Riechmann, L.1    Clark, H.2    Waldmann, H.3    Winter, G.4
  • 21
    • 0026559783 scopus 로고
    • Antibody framework residues affecting the conformation of the hypervariable loops
    • J. Foote and G. Winter, Antibody framework residues affecting the conformation of the hypervariable loops, J Mol Biol 224 (1992), 487-499.
    • (1992) J Mol Biol , vol.224 , pp. 487-499
    • Foote, J.1    Winter, G.2
  • 22
    • 0037100379 scopus 로고    scopus 로고
    • Superhumanized antibodies: Reduction of immunogenic potential by complementarity-determining region grafting with human germline sequences: Application to an anti-CD28
    • P. Tan, D.A. Mitchell, T.N. Buss, M.A. Holmes, C. Anasetti and J. Foote, Superhumanized antibodies: reduction of immunogenic potential by complementarity-determining region grafting with human germline sequences: application to an anti-CD28, J Immunol 169 (2002), 1119-1125.
    • (2002) J Immunol , vol.169 , pp. 1119-1125
    • Tan, P.1    Mitchell, D.A.2    Buss, T.N.3    Holmes, M.A.4    Anasetti, C.5    Foote, J.6
  • 24
    • 0025964038 scopus 로고
    • Structure, function and properties of antibody binding sites
    • I.S. Mian, A.R. Bradwell and A.J. Olson, Structure, function and properties of antibody binding sites, J Mol Biol 217 (1991), 133-151.
    • (1991) J Mol Biol , vol.217 , pp. 133-151
    • Mian, I.S.1    Bradwell, A.R.2    Olson, A.J.3
  • 25
    • 0028289241 scopus 로고
    • Anatomy of the antibody molecule
    • E. Padlan, Anatomy of the antibody molecule, Mol Immunol 31 (1994), 169-217.
    • (1994) Mol Immunol , vol.31 , pp. 169-217
    • Padlan, E.1
  • 26
    • 0028798104 scopus 로고
    • Identification of specificity-determining residues in antibodies
    • E. Padlan, C. Abergel and J.P. Tipper, Identification of specificity-determining residues in antibodies, FASEB J 9 (1995), 133-139.
    • (1995) FASEB J , vol.9 , pp. 133-139
    • Padlan, E.1    Abergel, C.2    Tipper, J.P.3
  • 27
    • 3142550714 scopus 로고    scopus 로고
    • SDR grafting of a murine antibody using multiple human germline templates to minimize its immunogenicity
    • N.R. Gonzales, E. Padlan, R. De Pascalis, P. Schuck, J. Schlom and S.V. Kashmiri, SDR grafting of a murine antibody using multiple human germline templates to minimize its immunogenicity, Mol Immunol 41 (2004), 863-872.
    • (2004) Mol Immunol , vol.41 , pp. 863-872
    • Gonzales, N.R.1    Padlan, E.2    De Pascalis, R.3    Schuck, P.4    Schlom, J.5    Kashmiri, S.V.6
  • 29
    • 0025848797 scopus 로고
    • A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties
    • E. Padlan, A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties, Mol Immunol 28 (1991), 489-498.
    • (1991) Mol Immunol , vol.28 , pp. 489-498
    • Padlan, E.1
  • 30
    • 0032952032 scopus 로고    scopus 로고
    • Effect of humanization by variable domain resurfacing on the antiviral activity of a single-chain antibody against respiratory syncitial virus
    • S. Delagrave, J. Catalan, C. Sweet, G. Drabik, A. Henry, A. Rees, T.P. Monath and F. Guirakhoo, Effect of humanization by variable domain resurfacing on the antiviral activity of a single-chain antibody against respiratory syncitial virus, Protein Eng 12 (1999), 357-362.
    • (1999) Protein Eng , vol.12 , pp. 357-362
    • Delagrave, S.1    Catalan, J.2    Sweet, C.3    Drabik, G.4    Henry, A.5    Rees, A.6    Monath, T.P.7    Guirakhoo, F.8
  • 31
    • 0028141993 scopus 로고
    • Guiding the selection of human antibodies from phage display repertoires to a single epitope of an antigen
    • L.S. Jespers, A. Roberts, S.M. Mahler, G. Winter and H.R. Hoogenboom, Guiding the selection of human antibodies from phage display repertoires to a single epitope of an antigen, Biotechnology (N Y) 12(9) (1994), 899-903.
    • (1994) Biotechnology (N Y) , vol.12 , Issue.9 , pp. 899-903
    • Jespers, L.S.1    Roberts, A.2    Mahler, S.M.3    Winter, G.4    Hoogenboom, H.R.5
  • 32
    • 0030993418 scopus 로고    scopus 로고
    • Antibody humanization using monovalent phage display
    • M. Baca, L.G. Presta, S. O'Connor and J.A. Wells, Antibody humanization using monovalent phage display, J Biol Chem 272 (1997), 10678-10684.
    • (1997) J Biol Chem , vol.272 , pp. 10678-10684
    • Baca, M.1    Presta, L.G.2    O'Connor, S.3    Wells, J.A.4
  • 33
    • 0032850677 scopus 로고    scopus 로고
    • Multinational study of the efficacy and safety of humanized anti-HER2 monoclonal antibody in women who have HER2-overexpressing metastatic breast cancer that has progressed after chemotherapy for metastatic disease
    • M.A. Cobleigh, C.L. Vogel, D. Tripathy, N.J. Robert, S. Scholl, L. Fehrenbacher, J.M. Wolter, V. Paton, S. Shak, G. Lieberman et al., Multinational study of the efficacy and safety of humanized anti-HER2 monoclonal antibody in women who have HER2-overexpressing metastatic breast cancer that has progressed after chemotherapy for metastatic disease, J Clin Oncol 17 (1999), 2639-2648.
    • (1999) J Clin Oncol , vol.17 , pp. 2639-2648
    • Cobleigh, M.A.1    Vogel, C.L.2    Tripathy, D.3    Robert, N.J.4    Scholl, S.5    Fehrenbacher, L.6    Wolter, J.M.7    Paton, V.8    Shak, S.9    Lieberman, G.10
  • 34
    • 0035884115 scopus 로고    scopus 로고
    • Serological analysis of human anti-human antibody responses in colon cancer patients treated with repeated doses of humanized monoclonal antibody A33
    • G.L. Ritter, L.S. Cohen, C.J. Williams, E.C. Richards, L.J. Old and S. Welt, Serological analysis of human anti-human antibody responses in colon cancer patients treated with repeated doses of humanized monoclonal antibody A33, Cancer Res 61 (2001), 6851.
    • (2001) Cancer Res , vol.61 , pp. 6851
    • Ritter, G.L.1    Cohen, L.S.2    Williams, C.J.3    Richards, E.C.4    Old, L.J.5    Welt, S.6
  • 35
    • 0033866627 scopus 로고    scopus 로고
    • Antibody humanization: A case of the Empror's new clothes?
    • M. Clark, Antibody humanization: a case of the Empror's new clothes? Immunol (Today) 21 (2000), 397-402.
    • (2000) Immunol (Today) , vol.21 , pp. 397-402
    • Clark, M.1
  • 36
    • 14744294919 scopus 로고
    • Primatization of recombinant antibodies for immunotherapy of human dieases: A macaque/human chimeric antibody against human CD4
    • R. Newman, J. Alberts, D. Anderson, K. Carner, C. Heard, F. Norton, R. Raab, M. Reff, S. Shuey and N. Hanna, Primatization of recombinant antibodies for immunotherapy of human dieases: a macaque/human chimeric antibody against human CD4, Biotechnology (N Y) 10 (1992), 1455-1459.
    • (1992) Biotechnology (N Y) , vol.10 , pp. 1455-1459
    • Newman, R.1    Alberts, J.2    Anderson, D.3    Carner, K.4    Heard, C.5    Norton, F.6    Raab, R.7    Reff, M.8    Shuey, S.9    Hanna, N.10
  • 37
    • 0027729309 scopus 로고
    • Cloning and sequence analysis of kappa and gamma cynomolgus monkey immunoglobulin cDNAs
    • A.P. Lewis, K.A. Barber, H.J. Cooper, M.J. Sims, J. Worden and J.S. Crowe, Cloning and sequence analysis of kappa and gamma cynomolgus monkey immunoglobulin cDNAs, Dev Comp Immunol 17 (1993), 549-560.
    • (1993) Dev Comp Immunol , vol.17 , pp. 549-560
    • Lewis, A.P.1    Barber, K.A.2    Cooper, H.J.3    Sims, M.J.4    Worden, J.5    Crowe, J.S.6
  • 38
    • 0033921144 scopus 로고    scopus 로고
    • Preclinical development of keliximab, a primatized anti-CD4 monoclonal antibody, in human CD4 transgenic mice: Characterization of the model and safety studies
    • P.J. Bugelski, D.J. Herzyk, S. Rehm, A.G. Harmsen, E.V. Gore, D.M. Williams, B.E. Maleeff, A.M. Bagder, A. Truneh, S.R. O'Brien et al., Preclinical development of keliximab, a primatized anti-CD4 monoclonal antibody, in human CD4 transgenic mice: characterization of the model and safety studies, Hum Exp Toxicol 19 (2000), 230-243.
    • (2000) Hum Exp Toxicol , vol.19 , pp. 230-243
    • Bugelski, P.J.1    Herzyk, D.J.2    Rehm, S.3    Harmsen, A.G.4    Gore, E.V.5    Williams, D.M.6    Maleeff, B.E.7    Bagder, A.M.8    Truneh, A.9    O'Brien, S.R.10
  • 39
    • 11344288548 scopus 로고    scopus 로고
    • Technology evaluation: Lumiliximab, Biogen Idee
    • J.M. Reichert, Technology evaluation: lumiliximab, Biogen Idee, Curr Opin Mol Ther 6 (2004), 675-683.
    • (2004) Curr Opin Mol Ther , vol.6 , pp. 675-683
    • Reichert, J.M.1
  • 40
    • 0035852787 scopus 로고    scopus 로고
    • A human myeloma cell line suitable for the generation of human monoclonal antibodies
    • A. Karpas, A. Dremucheva and B.H. Czepulkowski, A human myeloma cell line suitable for the generation of human monoclonal antibodies, Proc Natl Acad Sci USA 98 (2001), 1799-1804.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 1799-1804
    • Karpas, A.1    Dremucheva, A.2    Czepulkowski, B.H.3
  • 42
    • 0031753237 scopus 로고    scopus 로고
    • Enhanced human cell engraftment in mice deficient in RAG2 and the common cytokine receptor g chain
    • J.P. Goldman, M.P. Blundell, L. Lopes, C. Kinnon, J. Di Santo and A.J. Thrasher, Enhanced human cell engraftment in mice deficient in RAG2 and the common cytokine receptor g chain, Brit J Hematol 103 (1998), 335-342.
    • (1998) Brit J Hematol , vol.103 , pp. 335-342
    • Goldman, J.P.1    Blundell, M.P.2    Lopes, L.3    Kinnon, C.4    Di Santo, J.5    Thrasher, A.J.6
  • 44
    • 0035997956 scopus 로고    scopus 로고
    • The trimera mouse: A system for generating human monoclonal antibodies and modeling human diseases
    • E. Llan, R. Eren, I. Lubin, O. Nussbaum, Z. Zauberman and S. Dagan, The trimera mouse: a system for generating human monoclonal antibodies and modeling human diseases, Curr Opin Mol Ther 4 (2002), 102-109.
    • (2002) Curr Opin Mol Ther , vol.4 , pp. 102-109
    • Llan, E.1    Eren, R.2    Lubin, I.3    Nussbaum, O.4    Zauberman, Z.5    Dagan, S.6
  • 46
    • 0036900286 scopus 로고    scopus 로고
    • Antibody discovery: The use of transgenic mice to generate human monoclonal antibodies for therapeutics
    • S.-A. Kellermann and L. Green, Antibody discovery: the use of transgenic mice to generate human monoclonal antibodies for therapeutics, Curr Opin Biotech 13 (2002), 593-597.
    • (2002) Curr Opin Biotech , vol.13 , pp. 593-597
    • Kellermann, S.-A.1    Green, L.2
  • 47
    • 0028883531 scopus 로고
    • Production of fully human antibodies by transgenic mice
    • A. Jakobovits, Production of fully human antibodies by transgenic mice, Curr Opin Biotechnol 6 (1995), 561-566.
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 561-566
    • Jakobovits, A.1
  • 48
    • 0036644329 scopus 로고    scopus 로고
    • Efficient isolation of novel human monoclonal antibodies with neutralizing activity against HIV-1 from transgenic mice expressing human Ig loci
    • Y. He, W.J. Honnen, C.P. Krachmarov, M. Burkhart, S.C. Kayman, J. Corvalan and A. Pinter, Efficient isolation of novel human monoclonal antibodies with neutralizing activity against HIV-1 from transgenic mice expressing human Ig loci, J Immunol 169 (2002), 595-605.
    • (2002) J Immunol , vol.169 , pp. 595-605
    • He, Y.1    Honnen, W.J.2    Krachmarov, C.P.3    Burkhart, M.4    Kayman, S.C.5    Corvalan, J.6    Pinter, A.7
  • 49
    • 4143050397 scopus 로고    scopus 로고
    • Safety, pharmacokinetics, and activity of ABX-EGF, a fully human anti-epidermal growth factor receptor monoclonal antibody in patients with metastatic renal cell cancer
    • E.K. Rowinsky, G.H. Schwartz, J.A. Gollob, J.A. Thompson, N.J. Vogelzang, R. Figlin, R. Bukowski, N. Haas, P. Lockbaum, Y.P. Li et al., Safety, pharmacokinetics, and activity of ABX-EGF, a fully human anti-epidermal growth factor receptor monoclonal antibody in patients with metastatic renal cell cancer, J Clin Oncol 22(15) (2004), 3003-3015.
    • (2004) J Clin Oncol , vol.22 , Issue.15 , pp. 3003-3015
    • Rowinsky, E.K.1    Schwartz, G.H.2    Gollob, J.A.3    Thompson, J.A.4    Vogelzang, N.J.5    Figlin, R.6    Bukowski, R.7    Haas, N.8    Lockbaum, P.9    Li, Y.P.10
  • 51
    • 0027319101 scopus 로고
    • Control of IgG/Fc glycosylation: A comparison of oligosaccharides from chimeric human/mouse and mouse subclass immunoglobulin Gs
    • J. Lund, N. Takahashi, H. Nakagawa, M. Goodall, T. Bentley, S.A. Hindley, R. Tyler and R. Jefferis, Control of IgG/Fc glycosylation: a comparison of oligosaccharides from chimeric human/mouse and mouse subclass immunoglobulin Gs, Mol Immunol 30 (1993), 741-748.
    • (1993) Mol Immunol , vol.30 , pp. 741-748
    • Lund, J.1    Takahashi, N.2    Nakagawa, H.3    Goodall, M.4    Bentley, T.5    Hindley, S.A.6    Tyler, R.7    Jefferis, R.8
  • 52
    • 0021678856 scopus 로고
    • A unique human IgG antibody with anti-a-galactosyl specificity
    • U. Galili, E.A. Rachmilewitz, A. Peleg and I. Flechner, A unique human IgG antibody with anti-a-galactosyl specificity, J Exp Med 160 (1984), 1519-1531.
    • (1984) J Exp Med , vol.160 , pp. 1519-1531
    • Galili, U.1    Rachmilewitz, E.A.2    Peleg, A.3    Flechner, I.4
  • 53
    • 0031033895 scopus 로고    scopus 로고
    • Effect of glycosylation on antibody function: Implications for genetic engineering
    • A. Wright and S.L. Morrison, Effect of glycosylation on antibody function: implications for genetic engineering, Trends Biotechnol 15 (1997), 26-32.
    • (1997) Trends Biotechnol , vol.15 , pp. 26-32
    • Wright, A.1    Morrison, S.L.2
  • 54
    • 0034681121 scopus 로고    scopus 로고
    • Double trans-chromosomic mice: Maintenance of two individual human chromosome fragments containing Ig heavy and kappa loci and expression of fully human antibodies
    • K. Tomizuka, T. Shinohara, H. Yoshida, H. Uejima, H. Ohguma, S. Tanaka, K. Sato, M. Oshimura and I. Ishida, Double trans-chromosomic mice: maintenance of two individual human chromosome fragments containing Ig heavy and kappa loci and expression of fully human antibodies, Proc Natl Acad Sci USA 97 (2000), 722-727.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 722-727
    • Tomizuka, K.1    Shinohara, T.2    Yoshida, H.3    Uejima, H.4    Ohguma, H.5    Tanaka, S.6    Sato, K.7    Oshimura, M.8    Ishida, I.9
  • 57
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • G.P. Smith, Filamentous fusion phage: novel expression vectors that display cloned antigens on the virion surface, Science 228 (1985), 1315-1317.
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 58
    • 0025226085 scopus 로고
    • Phage antibodies: Filamentous phage displaying antibody variable domains
    • J. McCafferty, A.D. Griffiths, G. Winter and D.J. Chiswell, Phage antibodies: filamentous phage displaying antibody variable domains, Nature 348 (1990), 552-554.
    • (1990) Nature , vol.348 , pp. 552-554
    • McCafferty, J.1    Griffiths, A.D.2    Winter, G.3    Chiswell, D.J.4
  • 61
    • 0018567632 scopus 로고
    • Theoretical studies of clonal selection: Minimal antibody repertoire size and reliability of self-non-self discrimination
    • A.S. Perelson and G.F. Oster, Theoretical studies of clonal selection: minimal antibody repertoire size and reliability of self-non-self discrimination, J Theor Biol 81(4) (1979), 645-670.
    • (1979) J Theor Biol , vol.81 , Issue.4 , pp. 645-670
    • Perelson, A.S.1    Oster, G.F.2
  • 63
    • 0027175018 scopus 로고
    • Combinatorial infection and in vivo recombination: A strategy for making large phage antibody repertoires
    • P. Waterhouse, A.D. Griffiths, K.S. Johnson and G. Winter, Combinatorial infection and in vivo recombination: a strategy for making large phage antibody repertoires, Nucleic Acids Res 21 (1993), 2265-2266.
    • (1993) Nucleic Acids Res , vol.21 , pp. 2265-2266
    • Waterhouse, P.1    Griffiths, A.D.2    Johnson, K.S.3    Winter, G.4
  • 64
    • 0028592565 scopus 로고
    • A new phage display system to construct multicombinatorial libraries of very large antibody repertoires
    • F. Geoffroy, R. Sodoyer and L. Aujame, A new phage display system to construct multicombinatorial libraries of very large antibody repertoires, Gene 151 (1994), 109-113.
    • (1994) Gene , vol.151 , pp. 109-113
    • Geoffroy, F.1    Sodoyer, R.2    Aujame, L.3
  • 65
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • A. Knappik, L. Ge, A. Honegger, P. Pack, M. Fischer, G. Wellnhofer, A. Hoess, J. Wolle, A. Pluckthun and B. Virnekas, Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides, J Mol Biol 296 (2000), 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    Wellnhofer, G.6    Hoess, A.7    Wolle, J.8    Pluckthun, A.9    Virnekas, B.10
  • 66
    • 0035558749 scopus 로고    scopus 로고
    • n-CoDeR concept: Unique types of antibodies for diagnostic use and therapy
    • R. Carlsson and E. Soderlind, n-CoDeR concept: unique types of antibodies for diagnostic use and therapy, Expert Rev Mol Diagn 1 (2001), 102-108.
    • (2001) Expert Rev Mol Diagn , vol.1 , pp. 102-108
    • Carlsson, R.1    Soderlind, E.2
  • 67
    • 0032581506 scopus 로고    scopus 로고
    • Phage T4 SOC and HOC display of biologically active, full-length proteins on the viral capsid
    • Z. Ren and L.W. Black, Phage T4 SOC and HOC display of biologically active, full-length proteins on the viral capsid, Gene 215 (1998), 439-444.
    • (1998) Gene , vol.215 , pp. 439-444
    • Ren, Z.1    Black, L.W.2
  • 68
    • 0027055508 scopus 로고
    • Application of a filamentous phage pVIII fusion protein system suitable for efficient production, screening and mutagenesis of F(ab) antibody fragments
    • W.D. Huse, T.J. Stinchcombe, S.M. Glaser, L. Starr, M. MacLean, K.E. Hellstrom, I. Hellstrom and D.E. Yelton, Application of a filamentous phage pVIII fusion protein system suitable for efficient production, screening and mutagenesis of F(ab) antibody fragments, J Immunol 149 (1992), 3914-3920.
    • (1992) J Immunol , vol.149 , pp. 3914-3920
    • Huse, W.D.1    Stinchcombe, T.J.2    Glaser, S.M.3    Starr, L.4    MacLean, M.5    Hellstrom, K.E.6    Hellstrom, I.7    Yelton, D.E.8
  • 69
    • 0036792077 scopus 로고    scopus 로고
    • A method for the generation of combinatorial antibody libraries using pIX phage display
    • C. Gao, S. Mao, G. Kaufmann, P. Wirshing, R.A. Lerner and K.D. Janda, A method for the generation of combinatorial antibody libraries using pIX phage display, Proc Natl Acad Sci USA 99 (2002), 12612-12616.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 12612-12616
    • Gao, C.1    Mao, S.2    Kaufmann, G.3    Wirshing, P.4    Lerner, R.A.5    Janda, K.D.6
  • 71
    • 0034887457 scopus 로고    scopus 로고
    • Engineering M13 for phage display
    • S.S. Sidhu, Engineering M13 for phage display, Biomol Eng 18 (2001), 57-63.
    • (2001) Biomol Eng , vol.18 , pp. 57-63
    • Sidhu, S.S.1
  • 72
    • 0029585566 scopus 로고
    • Co-selection of cognate antibody-antigen pairs by selectively infective phages
    • C. Krebber, S. Spada, D. Desplancq and A. Plückthun, Co-selection of cognate antibody-antigen pairs by selectively infective phages, FEBS Lett 377 (1995), 227-231.
    • (1995) FEBS Lett , vol.377 , pp. 227-231
    • Krebber, C.1    Spada, S.2    Desplancq, D.3    Plückthun, A.4
  • 73
    • 0027933750 scopus 로고
    • Clonal selection and amplification of phage displayed antibodies by linking antigen recognition and phage replication
    • M. Duenas and C.A. Borrebaeck, Clonal selection and amplification of phage displayed antibodies by linking antigen recognition and phage replication, Biotechnology (N Y) 12 (1994), 999-1002.
    • (1994) Biotechnology (N Y) , vol.12 , pp. 999-1002
    • Duenas, M.1    Borrebaeck, C.A.2
  • 74
    • 0028670306 scopus 로고
    • Direct interaction rescue, a novel filamentous phage technique to study protein-protein interactions
    • K. Gramatikoff, O. Georgiev and W. Schaffner, Direct interaction rescue, a novel filamentous phage technique to study protein-protein interactions, Nucleic Acids Res 22 (1994), 5761-5762.
    • (1994) Nucleic Acids Res , vol.22 , pp. 5761-5762
    • Gramatikoff, K.1    Georgiev, O.2    Schaffner, W.3
  • 75
    • 0033499651 scopus 로고    scopus 로고
    • Selectively infective phage (SIP) technology: Scope and limitations
    • S. Jung, K.M. Arndt, K.M. Muller and A. Pluckthun, Selectively infective phage (SIP) technology: scope and limitations, J Immunol Methods 9 (1999), 93-104.
    • (1999) J Immunol Methods , vol.9 , pp. 93-104
    • Jung, S.1    Arndt, K.M.2    Muller, K.M.3    Pluckthun, A.4
  • 76
    • 0031560775 scopus 로고    scopus 로고
    • Selectively-infective phage (SIP): A mechanistic dissection of a novel in vivo selection for protein-ligand interactions
    • C. Krebber, S. Spada, D. Desplancq, A. Krebber, L. Ge and A. Plückthun, Selectively-infective phage (SIP): a mechanistic dissection of a novel in vivo selection for protein-ligand interactions, J Mol Biol 268 (1997), 607-618.
    • (1997) J Mol Biol , vol.268 , pp. 607-618
    • Krebber, C.1    Spada, S.2    Desplancq, D.3    Krebber, A.4    Ge, L.5    Plückthun, A.6
  • 77
    • 0347634533 scopus 로고    scopus 로고
    • Bivalent antibody phage display mimics natural immunoglobulin
    • C.V. Lee, S.S. Sidhu and G. Fuh, Bivalent antibody phage display mimics natural immunoglobulin, J Immunol Methods 284 (2004), 119-132.
    • (2004) J Immunol Methods , vol.284 , pp. 119-132
    • Lee, C.V.1    Sidhu, S.S.2    Fuh, G.3
  • 79
    • 0034213959 scopus 로고    scopus 로고
    • Partial protection to respiratory syncytial virus (RSV) elicited in mice by intranasal immunization using live staphylococci with surface-displayed RSV-peptides
    • F. Cano, H. Plotnicky-Gilquin, T.N. Nguyen, S. Liljeqvist, P. Samuelson, J.Y. Bonnefoy, S. Stahl and A. Robert, Partial protection to respiratory syncytial virus (RSV) elicited in mice by intranasal immunization using live staphylococci with surface-displayed RSV-peptides, Vaccine 18 (2000), 2743-2752.
    • (2000) Vaccine , vol.18 , pp. 2743-2752
    • Cano, F.1    Plotnicky-Gilquin, H.2    Nguyen, T.N.3    Liljeqvist, S.4    Samuelson, P.5    Bonnefoy, J.Y.6    Stahl, S.7    Robert, A.8
  • 80
    • 0034051291 scopus 로고    scopus 로고
    • Autodisplay: Functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter
    • C.T. Latteman, J. Maurer, E. Gerland and T.F. Meyer, Autodisplay: functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter, J Bacteriol 182 (2000), 3726-3733.
    • (2000) J Bacteriol , vol.182 , pp. 3726-3733
    • Latteman, C.T.1    Maurer, J.2    Gerland, E.3    Meyer, T.F.4
  • 81
    • 1842857805 scopus 로고    scopus 로고
    • Flow cytometric screening of yeast surface display libraries
    • M. Feldhaus and R. Siegel, Flow cytometric screening of yeast surface display libraries, Methods Mol Biol 263 (2004), 311-332.
    • (2004) Methods Mol Biol , vol.263 , pp. 311-332
    • Feldhaus, M.1    Siegel, R.2
  • 82
    • 3042647616 scopus 로고    scopus 로고
    • Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries
    • B.R. Harvey, G. Georgiou, A. Hayhurst, K.J. Jeong, B.L. Iverson and G.K. Rogers, Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries, Proc Natl Acad Sci USA 101 (2004), 9193-9198.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9193-9198
    • Harvey, B.R.1    Georgiou, G.2    Hayhurst, A.3    Jeong, K.J.4    Iverson, B.L.5    Rogers, G.K.6
  • 84
    • 12244255090 scopus 로고    scopus 로고
    • Applications of ribosome display to antibody drug discovery
    • M.A. Groves and J.K. Osbourn, Applications of ribosome display to antibody drug discovery, Expert Opin Biol Ther 5 (2005), 125-135.
    • (2005) Expert Opin Biol Ther , vol.5 , pp. 125-135
    • Groves, M.A.1    Osbourn, J.K.2
  • 85
    • 0033733267 scopus 로고    scopus 로고
    • Selecting and evolving functional proteins in vitro by ribosome display
    • J. Hanes, L. Jermutus and A. Pluckthun, Selecting and evolving functional proteins in vitro by ribosome display, Adv Protein Chem 328 (2000), 404-430.
    • (2000) Adv Protein Chem , vol.328 , pp. 404-430
    • Hanes, J.1    Jermutus, L.2    Pluckthun, A.3
  • 86
    • 0033664270 scopus 로고    scopus 로고
    • Picomolar affinity antibodies from a fully synthetic nave library selected and evolved by ribosome display
    • J. Hanes, C. Schaffitzel, A. Knappik and A. Pluckthun, Picomolar affinity antibodies from a fully synthetic nave library selected and evolved by ribosome display, Nat Biotechnol 18 (2000), 1287-1292.
    • (2000) Nat Biotechnol , vol.18 , pp. 1287-1292
    • Hanes, J.1    Schaffitzel, C.2    Knappik, A.3    Pluckthun, A.4
  • 88
    • 0042203776 scopus 로고    scopus 로고
    • Development of an advanced polysome display system dependent on a specific protein-RNA motif interaction
    • S.Y. Sawata and K. Taira, Development of an advanced polysome display system dependent on a specific protein-RNA motif interaction, Nucleic Acids Res (2001), Suppl.:99-100.
    • (2001) Nucleic Acids Res , Issue.SUPPL. , pp. 99-100
    • Sawata, S.Y.1    Taira, K.2
  • 90
    • 0030748513 scopus 로고    scopus 로고
    • Triabodies: Single chain Fv fragments without a linker form trivalent trimers
    • P. Iliades, A.A. Kortt and P.J. Hudson, Triabodies: single chain Fv fragments without a linker form trivalent trimers, FEBS Lett 409 (1997), 437-441.
    • (1997) FEBS Lett , vol.409 , pp. 437-441
    • Iliades, P.1    Kortt, A.A.2    Hudson, P.J.3
  • 92
    • 0027183934 scopus 로고
    • A recombinant immunotoxin containing a disulfide-stabilized fv fragment
    • U. Brinkmann, Y. Reiter, S.H. Jung, B. Lee and I. Pastan, A recombinant immunotoxin containing a disulfide-stabilized fv fragment, Proc Natl Acad Sci USA 90 (1993), 7538-7542.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7538-7542
    • Brinkmann, U.1    Reiter, Y.2    Jung, S.H.3    Lee, B.4    Pastan, I.5
  • 93
    • 0029766875 scopus 로고    scopus 로고
    • Engineering antibody Fv fragments for cancer detection and therapy: Disulfide-stabilized Fv fragments
    • Y. Reiter, U. Brinkmann, B. Lee and I. Pastan, Engineering antibody Fv fragments for cancer detection and therapy: disulfide-stabilized Fv fragments, Nat Biotechnol 14 (1996), 1239-1245.
    • (1996) Nat Biotechnol , vol.14 , pp. 1239-1245
    • Reiter, Y.1    Brinkmann, U.2    Lee, B.3    Pastan, I.4
  • 94
    • 0029946383 scopus 로고    scopus 로고
    • Knobs-into-holes engineering of antibody CH3 domains for heavy chain heterodimerization
    • J.B. Ridgway, L.G. Presta and P. Carter, knobs-into-holes engineering of antibody CH3 domains for heavy chain heterodimerization, Protein Eng 9 (1996), 617-621.
    • (1996) Protein Eng , vol.9 , pp. 617-621
    • Ridgway, J.B.1    Presta, L.G.2    Carter, P.3
  • 95
    • 3843109039 scopus 로고    scopus 로고
    • Bivalent Fv antibody fragments obtained by substituting the constant domains of Fab fragment with heterotetrameric molybdopterin synthase
    • K. Petrov, M. Dion, L. Hoffmann, T. Dintinger, A. Defontaine and C. Tellier, Bivalent Fv antibody fragments obtained by substituting the constant domains of Fab fragment with heterotetrameric molybdopterin synthase, J Mol Biol 341 (2004), 1039-1048.
    • (2004) J Mol Biol , vol.341 , pp. 1039-1048
    • Petrov, K.1    Dion, M.2    Hoffmann, L.3    Dintinger, T.4    Defontaine, A.5    Tellier, C.6
  • 97
    • 0037124466 scopus 로고    scopus 로고
    • PEGylated antibodies and antibody fragments for improved therapy: A review
    • A.P. Chapman, PEGylated antibodies and antibody fragments for improved therapy: a review, Adv Drug Deliv Rev 54 (2002), 531-545.
    • (2002) Adv Drug Deliv Rev , vol.54 , pp. 531-545
    • Chapman, A.P.1
  • 99
    • 0022555989 scopus 로고
    • Bispecific monoclonal antibodies from hybrid hybridomas
    • M.R. Suresh, A.C. Cuello and C. Milstein, Bispecific monoclonal antibodies from hybrid hybridomas, Methods Enzymol 121 (1986), 210-228.
    • (1986) Methods Enzymol , vol.121 , pp. 210-228
    • Suresh, M.R.1    Cuello, A.C.2    Milstein, C.3
  • 100
    • 0030009282 scopus 로고    scopus 로고
    • Leucine Zipper dimerized bivalent and bispecific scFv antibodies from a semi-synthetic antibody phage display library
    • J. de Kruif and T. Logtenberg, Leucine Zipper dimerized bivalent and bispecific scFv antibodies from a semi-synthetic antibody phage display library, J Biol Chem 271 (1996), 7630-7634.
    • (1996) J Biol Chem , vol.271 , pp. 7630-7634
    • De Kruif, J.1    Logtenberg, T.2
  • 101
    • 0029890636 scopus 로고    scopus 로고
    • Minibody: A novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high level targeting of xenografts
    • S. Hu, L. Shively, A. Raubitschek, M. Sherman, L.E. Williams, J.Y. Wong, J.E. Shively and A.M. Wu, Minibody: a novel engineered anti-carcinoembryonic antigen antibody fragment (single-chain Fv-CH3) which exhibits rapid, high level targeting of xenografts, Cancer Res 56 (1996), 3055-3061.
    • (1996) Cancer Res , vol.56 , pp. 3055-3061
    • Hu, S.1    Shively, L.2    Raubitschek, A.3    Sherman, M.4    Williams, L.E.5    Wong, J.Y.6    Shively, J.E.7    Wu, A.M.8
  • 102
    • 12944312223 scopus 로고    scopus 로고
    • A new format of bispecific antibody: Highly efficient heterodimerization, expression and tumor cell lysis
    • Z. Xie, N. Guo, M. Yu, M. Hu and B. Shen, A new format of bispecific antibody: highly efficient heterodimerization, expression and tumor cell lysis, J Immunol Methods 296 (2005), 95-101.
    • (2005) J Immunol Methods , vol.296 , pp. 95-101
    • Xie, Z.1    Guo, N.2    Yu, M.3    Hu, M.4    Shen, B.5
  • 104
    • 0032403273 scopus 로고    scopus 로고
    • Recombinant Fv immunotoxins and Fv fragments as novel agents for cancer therapy and diagnosis
    • Y. Reiter and I. Pastan, Recombinant Fv immunotoxins and Fv fragments as novel agents for cancer therapy and diagnosis, TIBTECH 16 (1998), 513-520.
    • (1998) TIBTECH , vol.16 , pp. 513-520
    • Reiter, Y.1    Pastan, I.2
  • 105
    • 0035181464 scopus 로고    scopus 로고
    • Strategies for enzyme/prodrug cancer therapy
    • G. Xu and H.L. McLeod, Strategies for enzyme/prodrug cancer therapy, Clin Cancer Res 7 (2001), 3314-3324.
    • (2001) Clin Cancer Res , vol.7 , pp. 3314-3324
    • Xu, G.1    McLeod, H.L.2
  • 106
    • 19944427731 scopus 로고    scopus 로고
    • Sustained tumor regression of human colorectal cancer xenografts using a multifunctional mannosylated fusion protein in antibody-directed enzyme prodrug therapy
    • S.K. Sharma, R.B. Pedley, J. Bhatia, G.M. Boxer, E. El-Emir, U. Qureshi, B. Tolner, H. Lowe, N.P. Michael, N. Minton et al., Sustained tumor regression of human colorectal cancer xenografts using a multifunctional mannosylated fusion protein in antibody-directed enzyme prodrug therapy, Clin Cancer Res 11 (2005), 814-825.
    • (2005) Clin Cancer Res , vol.11 , pp. 814-825
    • Sharma, S.K.1    Pedley, R.B.2    Bhatia, J.3    Boxer, G.M.4    El-Emir, E.5    Qureshi, U.6    Tolner, B.7    Lowe, H.8    Michael, N.P.9    Minton, N.10
  • 107
    • 7444263583 scopus 로고    scopus 로고
    • A prostate-specific membrane antigen-targeted monoclonal antibody-chemotherapeutic conjugate designed for the treatment of prostate cancer
    • M.D. Henry, S. Wen, M.D. Silva, S. Chandra, M. Milton and P.J. Worland, A prostate-specific membrane antigen-targeted monoclonal antibody- chemotherapeutic conjugate designed for the treatment of prostate cancer, Cancer Res 64 (2004), 7995-8001.
    • (2004) Cancer Res , vol.64 , pp. 7995-8001
    • Henry, M.D.1    Wen, S.2    Silva, M.D.3    Chandra, S.4    Milton, M.5    Worland, P.J.6
  • 108
    • 14844286972 scopus 로고    scopus 로고
    • Apoptotic killing of B-chronic lymphocytic leukemia tumor cells by allicin generated in situ using a rituximab-alliinase conjugate
    • F.D. Arditti, A. Rabinkov, T. Miron, Y. Reisner, A. Berrebi, M. Wilchek and D. Mirelman, Apoptotic killing of B-chronic lymphocytic leukemia tumor cells by allicin generated in situ using a rituximab-alliinase conjugate, Mol Cancer Ther 4(2) (2005), 325-331.
    • (2005) Mol Cancer Ther , vol.4 , Issue.2 , pp. 325-331
    • Arditti, F.D.1    Rabinkov, A.2    Miron, T.3    Reisner, Y.4    Berrebi, A.5    Wilchek, M.6    Mirelman, D.7
  • 112
    • 0036251627 scopus 로고    scopus 로고
    • Heavy-chain antibodies in camelidae; a case of evolutionary innovation
    • V.K. Nguyen, C. Su, S. Muyldermans and W. van der Loo, Heavy-chain antibodies in camelidae; a case of evolutionary innovation, Immunogenetics 54 (2002), 39-47.
    • (2002) Immunogenetics , vol.54 , pp. 39-47
    • Nguyen, V.K.1    Su, C.2    Muyldermans, S.3    Van Der Loo, W.4
  • 113
    • 0037235949 scopus 로고    scopus 로고
    • Engineered antibodies
    • P.J. Hudson and C. Souriau, Engineered antibodies, Nat Med 9 (2003), 129-134.
    • (2003) Nat Med , vol.9 , pp. 129-134
    • Hudson, P.J.1    Souriau, C.2
  • 116
    • 0034830063 scopus 로고    scopus 로고
    • Isolation of the new antigen receptor from wobbegong sharks, and use as a scaffold for the display of protein loop libraries
    • S.D. Nuttall, U.V. Krishnan, M. Hattarki, R. De Gori, R.A. Irving and P.J. Hudson, Isolation of the new antigen receptor from wobbegong sharks, and use as a scaffold for the display of protein loop libraries, Mol Immunol 38 (2001), 313-326.
    • (2001) Mol Immunol , vol.38 , pp. 313-326
    • Nuttall, S.D.1    Krishnan, U.V.2    Hattarki, M.3    De Gori, R.4    Irving, R.A.5    Hudson, P.J.6
  • 120
    • 0042780350 scopus 로고    scopus 로고
    • Designing repeat proteins: Well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins
    • H.K. Binz, M.T. Stumpp, P. Forrer, H. Amstutz and A. Pluckthun, Designing repeat proteins: well-expressed, soluble and stable proteins from combinatorial libraries of consensus ankyrin repeat proteins, J Mol Biol 332 (2003), 489-503.
    • (2003) J Mol Biol , vol.332 , pp. 489-503
    • Binz, H.K.1    Stumpp, M.T.2    Forrer, P.3    Amstutz, H.4    Pluckthun, A.5
  • 121
    • 21744440783 scopus 로고    scopus 로고
    • Intracellular kinase inhibitors selected from combinatorial libraries of designed ankyrin repeat proteins
    • P. Amstutz, H.K. Binz, P. Parizek, M.T. Stumpp, A. Kohl, G. Grutter, P. Forrer and A. Pluckthun, Intracellular kinase inhibitors selected from combinatorial libraries of designed ankyrin repeat proteins, J Biol Chem 280 (2005), 24715-24722.
    • (2005) J Biol Chem , vol.280 , pp. 24715-24722
    • Amstutz, P.1    Binz, H.K.2    Parizek, P.3    Stumpp, M.T.4    Kohl, A.5    Grutter, G.6    Forrer, P.7    Pluckthun, A.8
  • 122
    • 0037007445 scopus 로고    scopus 로고
    • Tuning ligand affinity, specificity, and folding stability of an engineered lipocalin variant - A so-called anticalin - Using a molecular random approach
    • S. Schlehuber and A. Skerra, Tuning ligand affinity, specificity, and folding stability of an engineered lipocalin variant - a so-called anticalin - using a molecular random approach, Biophys Chem 96 (2002), 213-228.
    • (2002) Biophys Chem , vol.96 , pp. 213-228
    • Schlehuber, S.1    Skerra, A.2
  • 123
    • 12844276589 scopus 로고    scopus 로고
    • Lipocalins in drug discovery: From natural ligand-binding proteins to anticalins
    • S. Schlehuber and A. Skerra, Lipocalins in drug discovery: from natural ligand-binding proteins to anticalins, Drug Discov Today 10(1) (2005), 23-33.
    • (2005) Drug Discov Today , vol.10 , Issue.1 , pp. 23-33
    • Schlehuber, S.1    Skerra, A.2
  • 124
    • 0034780636 scopus 로고    scopus 로고
    • Duocalins: Engineered ligand-binding proteins with dual specificity derived from the lipocalin fold
    • S. Schlehuber and A. Skerra, Duocalins: engineered ligand-binding proteins with dual specificity derived from the lipocalin fold, Biol Chem 382 (2001), 1335-1342.
    • (2001) Biol Chem , vol.382 , pp. 1335-1342
    • Schlehuber, S.1    Skerra, A.2
  • 126
    • 13444249481 scopus 로고    scopus 로고
    • Targeting tumor angiogenesis with adenovirus-delivered anti-Tie2 intrabody
    • M. Popkov, N. Jendreyko, D.B. McGavern, C. Rader and C.F.I. Barbas, Targeting tumor angiogenesis with adenovirus-delivered anti-Tie2 intrabody, Cancer Res 65 (2005), 972-981.
    • (2005) Cancer Res , vol.65 , pp. 972-981
    • Popkov, M.1    Jendreyko, N.2    McGavern, D.B.3    Rader, C.4    Barbas, C.F.I.5
  • 127
    • 22544471858 scopus 로고    scopus 로고
    • Intrabodies as drug discovery tools and therapeutics
    • M. Stocks, Intrabodies as drug discovery tools and therapeutics, Curr Opin Chem Biol (2005).
    • (2005) Curr Opin Chem Biol
    • Stocks, M.1
  • 129
    • 0043123378 scopus 로고    scopus 로고
    • Single domain intracellular antibodies: A minimal fragment for direct in vivo selection of antigen-specific intrabodies
    • T. Tanaka, M.N. Lobato and T.H. Rabbitts, Single domain intracellular antibodies: a minimal fragment for direct in vivo selection of antigen-specific intrabodies, J Mol Biol 331 (2003), 1109-1120.
    • (2003) J Mol Biol , vol.331 , pp. 1109-1120
    • Tanaka, T.1    Lobato, M.N.2    Rabbitts, T.H.3
  • 130
    • 20444391361 scopus 로고    scopus 로고
    • Phenotypic knockout of VEGF-R2 and Tie-2 with an intradiabody reduces tumor growth and angiogenesis in vivo
    • N. Jendreyko, M. Popkov, C. Rader and C.F. Barbas, 3rd: Phenotypic knockout of VEGF-R2 and Tie-2 with an intradiabody reduces tumor growth and angiogenesis in vivo, Proc Natl Acad Sci USA 102(23) (2005), 8293-8298.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.23 , pp. 8293-8298
    • Jendreyko, N.1    Popkov, M.2    Rader, C.3    Barbas III, C.F.4
  • 131
    • 4143103580 scopus 로고    scopus 로고
    • Antigen-independent selection of intracellular stable antibody frameworks
    • A. Auf der Maur, K. Tissot and A. Barberis, Antigen-independent selection of intracellular stable antibody frameworks, Methods 34 (2004), 215-224.
    • (2004) Methods , vol.34 , pp. 215-224
    • Auf Der Maur, A.1    Tissot, K.2    Barberis, A.3
  • 132
    • 4143109060 scopus 로고    scopus 로고
    • The intracellular antibody capture technology: Towards the high-throughput selection of functional intracellular antibodies for target validation
    • M. Visintin, M. Quondam and A. Cattaneo, The intracellular antibody capture technology: towards the high-throughput selection of functional intracellular antibodies for target validation, Methods 34(2) (2004), 200-214.
    • (2004) Methods , vol.34 , Issue.2 , pp. 200-214
    • Visintin, M.1    Quondam, M.2    Cattaneo, A.3
  • 133
    • 4444260465 scopus 로고    scopus 로고
    • Therapeutic antibody gene transfer: An active approach to passive immunity
    • J.M. Bakker, W.K. Bleeker and P.W. Parren, Therapeutic antibody gene transfer: an active approach to passive immunity, Mol Ther 10 (2004), 411-416.
    • (2004) Mol Ther , vol.10 , pp. 411-416
    • Bakker, J.M.1    Bleeker, W.K.2    Parren, P.W.3
  • 134
    • 17044398110 scopus 로고    scopus 로고
    • Making cell-permeable antibodies (Transbody) through fusion transduction domains (PTD) with single chain variable fragment (scFv) antibodies: Potential advantages over antibodies expressed within the intracellular environment (Intrabody)
    • B.C. Heng and T. Cao, Making cell-permeable antibodies (Transbody) through fusion transduction domains (PTD) with single chain variable fragment (scFv) antibodies: Potential advantages over antibodies expressed within the intracellular environment (Intrabody), Med Hypotheses 64 (2005), 1105-1108.
    • (2005) Med Hypotheses , vol.64 , pp. 1105-1108
    • Heng, B.C.1    Cao, T.2
  • 135
    • 1842635138 scopus 로고    scopus 로고
    • The role of idiotype vaccines in the treatment of human B-cell malignancies
    • M. Bendandi, The role of idiotype vaccines in the treatment of human B-cell malignancies, Expert Rev Vaccines 3 (2004), 163-170.
    • (2004) Expert Rev Vaccines , vol.3 , pp. 163-170
    • Bendandi, M.1
  • 138
    • 0027129063 scopus 로고
    • Antigenized antibodies
    • M. Zanetti, Antigenized antibodies, Nature 355 (1992), 476-477.
    • (1992) Nature , vol.355 , pp. 476-477
    • Zanetti, M.1
  • 139
    • 18144368148 scopus 로고    scopus 로고
    • Antigenized antibodies expressing Vbeta8.2 TCR peptides immunize against rat experimental allergic encephalomyelitis
    • C. Musselli, S. Daverio-Zanetti and M. Zanetti, Antigenized antibodies expressing Vbeta8.2 TCR peptides immunize against rat experimental allergic encephalomyelitis, J Immune Based Ther Vaccines 2 (2004), 9.
    • (2004) J Immune Based Ther Vaccines , vol.2 , pp. 9
    • Musselli, C.1    Daverio-Zanetti, S.2    Zanetti, M.3
  • 141
    • 0034330041 scopus 로고    scopus 로고
    • Natural catalytic antibodies (abzymes) in normalcy and pathology
    • G.A. Nevinsky, T.G. Kanyshkova and V.N. Buneva, Natural catalytic antibodies (abzymes) in normalcy and pathology, Biochemistry 65 (2000), 1245-1255.
    • (2000) Biochemistry , vol.65 , pp. 1245-1255
    • Nevinsky, G.A.1    Kanyshkova, T.G.2    Buneva, V.N.3
  • 144
    • 10044297246 scopus 로고    scopus 로고
    • Investigation of active form of catalytic antibody light chain 41S-2-L
    • Y. Mitsuda, K. Tsuruhata, E. Hifumi, M. Takagi and T. Uda, Investigation of active form of catalytic antibody light chain 41S-2-L, Immunol Lett 96 (2005), 63-71.
    • (2005) Immunol Lett , vol.96 , pp. 63-71
    • Mitsuda, Y.1    Tsuruhata, K.2    Hifumi, E.3    Takagi, M.4    Uda, T.5
  • 146
    • 0041664969 scopus 로고    scopus 로고
    • Controlled release of anti-cocaine catalytic antibody from biodegradable polymer microspheres
    • P. Homayoun, T. Mandal, D. Landry and H. Komiskey, Controlled release of anti-cocaine catalytic antibody from biodegradable polymer microspheres, J Pharm Pharmacol 55 (2003), 933-938.
    • (2003) J Pharm Pharmacol , vol.55 , pp. 933-938
    • Homayoun, P.1    Mandal, T.2    Landry, D.3    Komiskey, H.4
  • 147
    • 4544371858 scopus 로고    scopus 로고
    • Catalytic antibodies: Hapten design strategies and screening methods
    • Y. Xu, N. Yamamoto and K.D. Janda, Catalytic antibodies: hapten design strategies and screening methods, Bioorg Med Chem 12 (2004), 5247-5268.
    • (2004) Bioorg Med Chem , vol.12 , pp. 5247-5268
    • Xu, Y.1    Yamamoto, N.2    Janda, K.D.3
  • 149
    • 3543069890 scopus 로고    scopus 로고
    • Procaryotic expression of antibodies and affibodies
    • L.A. Fernandez, Procaryotic expression of antibodies and affibodies, Curr Opin Biotech 15 (2004), 364-373.
    • (2004) Curr Opin Biotech , vol.15 , pp. 364-373
    • Fernandez, L.A.1
  • 150
    • 1442352581 scopus 로고    scopus 로고
    • High-level accumulation of a recombinant antibody fragment in the periplasm of escherichia coli requires a triple-mutant (degP prc spr) host strain
    • C. Chen, B. Snedecor, J.C. Nishihara, J.C. Joly, N. McFarland, D.C. Andersen, J.E. Battersby and K.M. Champion, High-level accumulation of a recombinant antibody fragment in the periplasm of escherichia coli requires a triple-mutant (degP prc spr) host strain, Biotechnol Bioeng 85 (2004), 463-474.
    • (2004) Biotechnol Bioeng , vol.85 , pp. 463-474
    • Chen, C.1    Snedecor, B.2    Nishihara, J.C.3    Joly, J.C.4    McFarland, N.5    Andersen, D.C.6    Battersby, J.E.7    Champion, K.M.8
  • 151
    • 0034756555 scopus 로고    scopus 로고
    • Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones
    • R. Levy, R. Weiss, G. Chen, B.L. Iverson and G. Georgiou, Production of correctly folded Fab antibody fragment in the cytoplasm of Escherichia coli trxB gor mutants via the coexpression of molecular chaperones, Protein Expr Purif 23(2) (2001), 338-347.
    • (2001) Protein Expr Purif , vol.23 , Issue.2 , pp. 338-347
    • Levy, R.1    Weiss, R.2    Chen, G.3    Iverson, B.L.4    Georgiou, G.5
  • 152
    • 0033760702 scopus 로고    scopus 로고
    • Specific secretion of active single-chain Fv antibodies into the supernatants of Escherichia coli cultures by use of the hemolysin system
    • L.A. Fernandez, I. Sola, L. Enjuanes and V. de Lorenzo, Specific secretion of active single-chain Fv antibodies into the supernatants of Escherichia coli cultures by use of the hemolysin system, Appl Environ Microbiol 66 (2000), 5024-5029.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 5024-5029
    • Fernandez, L.A.1    Sola, I.2    Enjuanes, L.3    De Lorenzo, V.4
  • 155
    • 0036307716 scopus 로고    scopus 로고
    • Functional production and characterization of a fibrin-specific single-chain antibody fragment from Bacillus subtilis: Effects of molecular chaperones and a wall-bound protease on antibody fragment production
    • S-C. Wu, J.C. Yeung, Y. Duan, R. Ye, S.J. Szarka, H.R. Habibi and S-J. Wong, Functional production and characterization of a fibrin-specific single-chain antibody fragment from Bacillus subtilis: Effects of molecular chaperones and a wall-bound protease on antibody fragment production, Appl Environ Microbiol 68 (2002), 3261-3269.
    • (2002) Appl Environ Microbiol , vol.68 , pp. 3261-3269
    • Wu, S.-C.1    Yeung, J.C.2    Duan, Y.3    Ye, R.4    Szarka, S.J.5    Habibi, H.R.6    Wong, S.-J.7
  • 157
    • 0027303712 scopus 로고
    • Synthesis and expression of a DNA encoding the Fv domain of an antilysozyme monoclonal antibody, HyHEL10, in Streptomyces lividans
    • Y. Ueda, K. Tsumoto, K. Watanabe and I. Kumagai, Synthesis and expression of a DNA encoding the Fv domain of an antilysozyme monoclonal antibody, HyHEL10, in Streptomyces lividans, Gene 129 (1993), 129-134.
    • (1993) Gene , vol.129 , pp. 129-134
    • Ueda, Y.1    Tsumoto, K.2    Watanabe, K.3    Kumagai, I.4
  • 158
    • 0028408177 scopus 로고
    • Production of the immunoglobulin variable domain REiv via a fusion protein synthetized and secreted by Staphylococcus carnosus
    • J. Pschorr, B. Bieseler and H.J. Fritz, Production of the immunoglobulin variable domain REiv via a fusion protein synthetized and secreted by Staphylococcus carnosus, Biol Chem Happe Seyler 375 (1994), 271-280.
    • (1994) Biol Chem Happe Seyler , vol.375 , pp. 271-280
    • Pschorr, J.1    Bieseler, B.2    Fritz, H.J.3
  • 160
    • 0035166478 scopus 로고    scopus 로고
    • Baculovirus expression cassette vectors for rapid production of complete human IgG from phage display selected antibody fragments
    • M. Liang, S. Dubel, D. Li, I. Queitsch, W. Li and E.K. Bautz, Baculovirus expression cassette vectors for rapid production of complete human IgG from phage display selected antibody fragments, J Immunol Methods 247(1-2) (2001), 119-130.
    • (2001) J Immunol Methods , vol.247 , Issue.1-2 , pp. 119-130
    • Liang, M.1    Dubel, S.2    Li, D.3    Queitsch, I.4    Li, W.5    Bautz, E.K.6
  • 161
    • 1642290177 scopus 로고    scopus 로고
    • Human antibody production using insect-cell expression systems
    • M.C. Guttieri and M. Liang, Human antibody production using insect-cell expression systems, Methods Mol Biol 248 (2004), 269-299.
    • (2004) Methods Mol Biol , vol.248 , pp. 269-299
    • Guttieri, M.C.1    Liang, M.2
  • 162
    • 0038666527 scopus 로고    scopus 로고
    • High-yield production of recombinant antibody fragments in HEK-293 cells using sodium butyrate
    • J. Grunberg, K. Knogler, R. Waibel and I. Novak-Hofer, High-yield production of recombinant antibody fragments in HEK-293 cells using sodium butyrate, Biotechniques 34 (2003), 968-972.
    • (2003) Biotechniques , vol.34 , pp. 968-972
    • Grunberg, J.1    Knogler, K.2    Waibel, R.3    Novak-Hofer, I.4
  • 164
    • 1542650080 scopus 로고    scopus 로고
    • The state of biopharmaceutical manufacturing
    • D.T. Molowa and R. Mazanet, The state of biopharmaceutical manufacturing, Biotechnol Annu Rev 9 (2003), 285-302.
    • (2003) Biotechnol Annu Rev , vol.9 , pp. 285-302
    • Molowa, D.T.1    Mazanet, R.2
  • 165
    • 8344271026 scopus 로고    scopus 로고
    • Production or recombinant protein therapeutics in cultivated mammalian cells
    • F.M. Wurm, Production or recombinant protein therapeutics in cultivated mammalian cells, Nat Biotech 22 (2004), 1393-1398.
    • (2004) Nat Biotech , vol.22 , pp. 1393-1398
    • Wurm, F.M.1
  • 166
    • 0032843939 scopus 로고    scopus 로고
    • Towards molecular farming in the future: Pichia pastoris-based production of single-chain antibody fragments
    • R. Fischer, J. Drossard, N. Emans, U. Commandeur and S. Hellwig, Towards molecular farming in the future: Pichia pastoris-based production of single-chain antibody fragments, Biotechnol Appl Biochem 30 (1999), 117-120.
    • (1999) Biotechnol Appl Biochem , vol.30 , pp. 117-120
    • Fischer, R.1    Drossard, J.2    Emans, N.3    Commandeur, U.4    Hellwig, S.5
  • 168
    • 0034879260 scopus 로고    scopus 로고
    • Factors affecting the production of a single-chain antibody fragment by Aspergillus awamori in a stirred tank reactor
    • A. Sotiriadis, T. Keshavarz and E. Keshavarz-Moore, Factors affecting the production of a single-chain antibody fragment by Aspergillus awamori in a stirred tank reactor, Biotechnol Prog 17 (2001), 618-623.
    • (2001) Biotechnol Prog , vol.17 , pp. 618-623
    • Sotiriadis, A.1    Keshavarz, T.2    Keshavarz-Moore, E.3
  • 170
    • 0037362471 scopus 로고    scopus 로고
    • Molecular farming of recombinant antibodies in plant
    • S. Schillberg, R. Fischer and N. Emans, Molecular farming of recombinant antibodies in plant, Cell Mol Life Sci 60 (2003), 433-445.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 433-445
    • Schillberg, S.1    Fischer, R.2    Emans, N.3
  • 171
    • 0036535775 scopus 로고    scopus 로고
    • Plantibodies: Applications, advantages and bottlenecks
    • E. Stoger, M. Sack, R. Fischer and P. Christou, Plantibodies: applications, advantages and bottlenecks, Curr Opin Biotech 13 (2002), 161-166.
    • (2002) Curr Opin Biotech , vol.13 , pp. 161-166
    • Stoger, E.1    Sack, M.2    Fischer, R.3    Christou, P.4
  • 172
    • 0024959945 scopus 로고
    • Production of antibodies in transgenic plants
    • A. Hiatt, R. Cafferkey and K. Bowdish, Production of antibodies in transgenic plants, Nature 342 (1989), 76-78.
    • (1989) Nature , vol.342 , pp. 76-78
    • Hiatt, A.1    Cafferkey, R.2    Bowdish, K.3
  • 175
    • 0031835622 scopus 로고    scopus 로고
    • Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans
    • J. Ma, B.Y. Hikmat, K. Wycoff, N.D. Vine, D. Charlelegue, L. Yu, M.B. Hein and T. Lehner, Characterization of a recombinant plant monoclonal secretory antibody and preventive immunotherapy in humans, Nat Med 4 (1998), 601-606.
    • (1998) Nat Med , vol.4 , pp. 601-606
    • Ma, J.1    Hikmat, B.Y.2    Wycoff, K.3    Vine, N.D.4    Charlelegue, D.5    Yu, L.6    Hein, M.B.7    Lehner, T.8
  • 176
    • 14744293469 scopus 로고    scopus 로고
    • Antibody processing and engineering in plants, and new strategies for vaccine production
    • J. Ma, P.M. Drake, D. Charlelegue, P. Obregon and A. Prada, Antibody processing and engineering in plants, and new strategies for vaccine production, Vaccine 23 (2005), 1814-1818.
    • (2005) Vaccine , vol.23 , pp. 1814-1818
    • Ma, J.1    Drake, P.M.2    Charlelegue, D.3    Obregon, P.4    Prada, A.5
  • 178
  • 181
    • 0041887181 scopus 로고    scopus 로고
    • Making recombinant proteins in animals - Different systems, different applications
    • M.K. Dick, D. Lacroix, F. Pothier and M.A. Sirard, Making recombinant proteins in animals - different systems, different applications, Trends Biotechnol 21 (2003), 394-399.
    • (2003) Trends Biotechnol , vol.21 , pp. 394-399
    • Dick, M.K.1    Lacroix, D.2    Pothier, F.3    Sirard, M.A.4
  • 182
    • 0035313152 scopus 로고    scopus 로고
    • Therapeutic antibody expression technology
    • H.E. Chadd and S.M. Chamow, Therapeutic antibody expression technology, Curr Opin Biotechnol 12(2) (2001), 188-194.
    • (2001) Curr Opin Biotechnol , vol.12 , Issue.2 , pp. 188-194
    • Chadd, H.E.1    Chamow, S.M.2
  • 183
    • 0033032935 scopus 로고    scopus 로고
    • Cell-free expression of two single-chain monoclonal antibodies against lysozyme: Effect of domain arrangement on the expression
    • H. Merk, W. Stiege, K. Tsumoto, I. Kumagai and V.A. Erdmann, Cell-free expression of two single-chain monoclonal antibodies against lysozyme: effect of domain arrangement on the expression, J Biochem 125 (1999), 328-333.
    • (1999) J Biochem , vol.125 , pp. 328-333
    • Merk, H.1    Stiege, W.2    Tsumoto, K.3    Kumagai, I.4    Erdmann, V.A.5
  • 184
    • 0037070555 scopus 로고    scopus 로고
    • Expression of a Fab fragment of catalytic antibody 6D9 in an Escherichia coli in vitro coupled transcription/translation system
    • X. Jiang, Y. Ookubo, Y. Fuji, H. Nakano and T. Yamane, Expression of a Fab fragment of catalytic antibody 6D9 in an Escherichia coli in vitro coupled transcription/translation system, FEBS Lett 514 (2002), 290-294.
    • (2002) FEBS Lett , vol.514 , pp. 290-294
    • Jiang, X.1    Ookubo, Y.2    Fuji, Y.3    Nakano, H.4    Yamane, T.5
  • 185
    • 0031021109 scopus 로고    scopus 로고
    • Functional antibody production using cell-free translation: Effects of protein disulfide isomerase and chaperones
    • L.A. Ryabova, D. Desplancq, A.S. Spirin and A. Pluckthun, Functional antibody production using cell-free translation: effects of protein disulfide isomerase and chaperones, Nat Biotechnol 15 (1997), 79-84.
    • (1997) Nat Biotechnol , vol.15 , pp. 79-84
    • Ryabova, L.A.1    Desplancq, D.2    Spirin, A.S.3    Pluckthun, A.4
  • 186
    • 3142771251 scopus 로고    scopus 로고
    • Chaperone-assisted folding of a single-chain antibody in a reconstitued translation system
    • B.W. Ying, H. Taguchi, H. Ueda and T. Ueda, Chaperone-assisted folding of a single-chain antibody in a reconstitued translation system, Biochem Biophys Res Commun 320 (2004), 1359-1364.
    • (2004) Biochem Biophys Res Commun , vol.320 , pp. 1359-1364
    • Ying, B.W.1    Taguchi, H.2    Ueda, H.3    Ueda, T.4
  • 188
    • 2242455924 scopus 로고    scopus 로고
    • Engineering the protein N-glycosylation pathway in insect cells for production of biantennary complex N-glycans
    • J. Hollister, E. Grabenhorst, M. Nimtz, H. Conradt and D.L. Jarvis, Engineering the protein N-glycosylation pathway in insect cells for production of biantennary complex N-glycans, Biochem 41 (2002), 15093-15104.
    • (2002) Biochem , vol.41 , pp. 15093-15104
    • Hollister, J.1    Grabenhorst, E.2    Nimtz, M.3    Conradt, H.4    Jarvis, D.L.5
  • 189
    • 0032848329 scopus 로고    scopus 로고
    • Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells
    • E. Grabenhorst, P. Schlenke, S. Pohl, M. Nimtz and H.S. Conradt, Genetic engineering of recombinant glycoproteins and the glycosylation pathway in mammalian host cells, Glycoconj J 16 (1999), 81-97.
    • (1999) Glycoconj J , vol.16 , pp. 81-97
    • Grabenhorst, E.1    Schlenke, P.2    Pohl, S.3    Nimtz, M.4    Conradt, H.S.5
  • 190
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoam IgG1 with optimized antibody-dependant cellular cytotoxic activity
    • P. Umana, J. Jean-Mairet, R. Moudry, H. Amstutz and J.E. Bailey, Engineered glycoforms of an antineuroblastoam IgG1 with optimized antibody-dependant cellular cytotoxic activity, Nat Biotech 17 (1999), 176-180.
    • (1999) Nat Biotech , vol.17 , pp. 176-180
    • Umana, P.1    Jean-Mairet, J.2    Moudry, R.3    Amstutz, H.4    Bailey, J.E.5
  • 191
    • 0034192958 scopus 로고    scopus 로고
    • A new Chinese hamster ovary cell line expressing a2,6-sialyltransferase used as universal host for the production of human-like sialylated recombinant glycoproteins
    • A. Bragonzi, G. Distefano, L.D. Buckberry, G. Acerbis, C. Foglieni, D. Lamotte, G. Campi, A. Marc, M.R. Soria, N. Jenkins et al., A new Chinese hamster ovary cell line expressing a2,6-sialyltransferase used as universal host for the production of human-like sialylated recombinant glycoproteins, Biochem Biophys Acta 1474 (2000), 273-282.
    • (2000) Biochem Biophys Acta , vol.1474 , pp. 273-282
    • Bragonzi, A.1    Distefano, G.2    Buckberry, L.D.3    Acerbis, G.4    Foglieni, C.5    Lamotte, D.6    Campi, G.7    Marc, A.8    Soria, M.R.9    Jenkins, N.10
  • 192
    • 12244295475 scopus 로고    scopus 로고
    • Improvement of glycosylation in insect cells with mammalian glycosyltransferases
    • G-D. Chang, C-J. Chen, C-Y. Lin, H-C. Chen and H. Chen, Improvement of glycosylation in insect cells with mammalian glycosyltransferases, J Biotechnol 102 (2003), 61-71.
    • (2003) J Biotechnol , vol.102 , pp. 61-71
    • Chang, G.-D.1    Chen, C.-J.2    Lin, C.-Y.3    Chen, H.-C.4    Chen, H.5
  • 195
    • 13444262282 scopus 로고    scopus 로고
    • The humanization of N-glycosylation pathways in yeast
    • S. Wildt and Y.U. Gerngross, The humanization of N-glycosylation pathways in yeast, Nat Rev Microbiol 3 (2005), 119-128.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 119-128
    • Wildt, S.1    Gerngross, Y.U.2
  • 196
    • 0242321082 scopus 로고    scopus 로고
    • Genetic engineering of Pichia pastoris to humanize N-glycosylation of proteins
    • R.K. Bretthauer, Genetic engineering of Pichia pastoris to humanize N-glycosylation of proteins, Trends Biotechnol 21 (2003), 459-462.
    • (2003) Trends Biotechnol , vol.21 , pp. 459-462
    • Bretthauer, R.K.1
  • 198
    • 4444231014 scopus 로고    scopus 로고
    • Engineering of an artificial glycosylation pathway blocked in core oligosaccharide assembly in the yeast Pichia pastoris: Production of complexe humanized glycoproteins with terminal galactose
    • P. Bobrowicz, R.C. Davidson, H. Li, T.I. Potgieter, J.H. Nett, S.R. Hamilton, T.A. Stadheim, R.G. Miele, B. Bobrowics, T. Mitchell et al., Engineering of an artificial glycosylation pathway blocked in core oligosaccharide assembly in the yeast Pichia pastoris: production of complexe humanized glycoproteins with terminal galactose, Glycobiology 14 (2004), 757-766.
    • (2004) Glycobiology , vol.14 , pp. 757-766
    • Bobrowicz, P.1    Davidson, R.C.2    Li, H.3    Potgieter, T.I.4    Nett, J.H.5    Hamilton, S.R.6    Stadheim, T.A.7    Miele, R.G.8    Bobrowics, B.9    Mitchell, T.10
  • 199
    • 0035097824 scopus 로고    scopus 로고
    • Identification of peptides that target the endothelial cell-specific lox-1 receptor
    • S.J. White, S.A. Nicklin, T. Sawamura and A.M. Baker, Identification of peptides that target the endothelial cell-specific lox-1 receptor, Hypertension 37 (2001), 449-455.
    • (2001) Hypertension , vol.37 , pp. 449-455
    • White, S.J.1    Nicklin, S.A.2    Sawamura, T.3    Baker, A.M.4
  • 200
    • 0033499631 scopus 로고    scopus 로고
    • Phage display of cDNA repertoires: The pVI display system and its applications for the selection of immunogenic ligands
    • S.E. Hufton, P.T. Moerkerk, E.V. Meulemans, A. de Bruïne, J-W. Arends and H.R. Hoogenboom, Phage display of cDNA repertoires: the pVI display system and its applications for the selection of immunogenic ligands, J Immunol Methods 231 (1999), 39-51.
    • (1999) J Immunol Methods , vol.231 , pp. 39-51
    • Hufton, S.E.1    Moerkerk, P.T.2    Meulemans, E.V.3    De Bruïne, A.4    Arends, J.-W.5    Hoogenboom, H.R.6
  • 202
    • 0034746958 scopus 로고    scopus 로고
    • Rapid identification of a tobacco mosaic virus epitope by using a coat protein gene-fragment-pVIII fusion library
    • A. Holzem, J.M. Nahring and R. Fischer, Rapid identification of a tobacco mosaic virus epitope by using a coat protein gene-fragment-pVIII fusion library, J Gen Virol 82 (2001), 9-15.
    • (2001) J Gen Virol , vol.82 , pp. 9-15
    • Holzem, A.1    Nahring, J.M.2    Fischer, R.3
  • 206
    • 4143137525 scopus 로고    scopus 로고
    • Effect of linker sequences between the antibody variable domains on the formation, stability and biological activity of a bispecific tandem diabody
    • F. Le Gall, U. Reusch, M. Little and S.M. Kipriyanov, Effect of linker sequences between the antibody variable domains on the formation, stability and biological activity of a bispecific tandem diabody, Protein Eng Des Sel 17 (2004), 357-366.
    • (2004) Protein Eng Des Sel , vol.17 , pp. 357-366
    • Le Gall, F.1    Reusch, U.2    Little, M.3    Kipriyanov, S.M.4
  • 207
    • 11144238604 scopus 로고    scopus 로고
    • Bispecific minibodies targeting HER2/neu and CD16 exhibit improved tumor lysis when placed in a divalent tumor antigen binding format
    • L.S. Shahied, Y. Tang, R.K. Alpaugh, R. Somer, D. Greenspon and L.M. Weiner, Bispecific minibodies targeting HER2/neu and CD16 exhibit improved tumor lysis when placed in a divalent tumor antigen binding format, J Biol Chem 279 (2004), 53907-53914.
    • (2004) J Biol Chem , vol.279 , pp. 53907-53914
    • Shahied, L.S.1    Tang, Y.2    Alpaugh, R.K.3    Somer, R.4    Greenspon, D.5    Weiner, L.M.6
  • 208
    • 21244441508 scopus 로고    scopus 로고
    • A fully human recombinant IgG-like bispecific antibody to both the epidermal growth factor receptor and the insulin-like growth factor receptor for enhanced antitumor activity
    • D. Lu, H. Zhang, H. Koo, J. Tonra, P. Balderes, M. Prewett, E. Corcoran, V. Mangalampalli, R. Bassi, D. Anselma et al., A fully human recombinant IgG-like bispecific antibody to both the epidermal growth factor receptor and the insulin-like growth factor receptor for enhanced antitumor activity, J Biol Chem 280 (2005), 19665-19672.
    • (2005) J Biol Chem , vol.280 , pp. 19665-19672
    • Lu, D.1    Zhang, H.2    Koo, H.3    Tonra, J.4    Balderes, P.5    Prewett, M.6    Corcoran, E.7    Mangalampalli, V.8    Bassi, R.9    Anselma, D.10
  • 209
    • 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
    • S.M. Kipriyanov, M. Little, H. Kropshofer, F. Breitling, S. Gotter and S. Dubel, Affinity enhancement of a recombinant antibody: formation of complexes with multiple valency by a single-chain Fv fragment-core streptavidin fusion, Protein Eng 9 (1996), 203-211.
    • (1996) Protein Eng , vol.9 , pp. 203-211
    • Kipriyanov, S.M.1    Little, M.2    Kropshofer, H.3    Breitling, F.4    Gotter, S.5    Dubel, S.6
  • 210
    • 0034830739 scopus 로고    scopus 로고
    • Dimeric and trimeric antibodies: High avidity scFvs for cancer targeting
    • A.A. Kortt, O. Dolezal, B.E. Power and P.J. Hudson, Dimeric and trimeric antibodies: high avidity scFvs for cancer targeting, Biomol Eng 18 (2001), 95-108.
    • (2001) Biomol Eng , vol.18 , pp. 95-108
    • Kortt, A.A.1    Dolezal, O.2    Power, B.E.3    Hudson, P.J.4
  • 213
    • 0036285666 scopus 로고    scopus 로고
    • A phase I study withHodgkin an anti-CD30 ricin A-chain immunotoxin (Ki-4.dgA) in patients with refractory CD30+ Hodgkin's and non Hodgkin's lymphoma
    • R. Schnell, O. Staak, P. Borchmann, G. Schwartz, B. Matthey, H. Hansen, J. Schindler, V. Ghetie, E.S. Vitetta, V. Diehl et al., A phase I study withHodgkin an anti-CD30 ricin A-chain immunotoxin (Ki-4.dgA) in patients with refractory CD30+ Hodgkin's and non Hodgkin's lymphoma, Clin Cancer Res 8 (2002), 1179-1786.
    • (2002) Clin Cancer Res , vol.8 , pp. 1179-1786
    • Schnell, R.1    Staak, O.2    Borchmann, P.3    Schwartz, G.4    Matthey, B.5    Hansen, H.6    Schindler, J.7    Ghetie, V.8    Vitetta, E.S.9    Diehl, V.10
  • 214
    • 17644378667 scopus 로고    scopus 로고
    • Immunogenicity of enginneered antibodies
    • W.Y.K. Hwang and J. Foote, Immunogenicity of enginneered antibodies, Methods 36 (2005), 3-10.
    • (2005) Methods , vol.36 , pp. 3-10
    • Hwang, W.Y.K.1    Foote, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.