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Volumn 6, Issue 2, 2010, Pages 128-138

Structure-Guided design of antibodies

Author keywords

Affinity maturation; Antibody engineering; Effector function; Protein stability; Structure based design

Indexed keywords

DESIGN; ENGINEERING EDUCATION; MONOCLONAL ANTIBODIES;

EID: 77953660480     PISSN: 15734099     EISSN: None     Source Type: Journal    
DOI: 10.2174/157340910791202469     Document Type: Article
Times cited : (23)

References (100)
  • 1
    • 0035166917 scopus 로고    scopus 로고
    • IMGT, the international ImMunoGeneTics database
    • Lefranc, M.P. IMGT, the international ImMunoGeneTics database. Nucleic Acids Res., 2001, 29, 207-209.
    • (2001) Nucleic Acids Res , vol.29 , pp. 207-209
    • Lefranc, M.P.1
  • 3
    • 60849128549 scopus 로고    scopus 로고
    • Monoclonal antibodies as innovative therapeutics
    • Reichert, J.M. Monoclonal antibodies as innovative therapeutics. Curr. Pharm. Biotechnol., 2008, 9, 423-430.
    • (2008) Curr. Pharm. Biotechnol , vol.9 , pp. 423-430
    • Reichert, J.M.1
  • 5
    • 48549105161 scopus 로고    scopus 로고
    • Molecular engineering and design of therapeutic antibodies
    • Presta, L.G. Molecular engineering and design of therapeutic antibodies. Curr. Opin. Immunol, 2008, 20, 460-470.
    • (2008) Curr. Opin. Immunol , vol.20 , pp. 460-470
    • Presta, L.G.1
  • 8
    • 0000146003 scopus 로고
    • A theoretical model of gamma-globulin catabolism
    • Brambell, F.W.; Hemmings, W.A.; Morris, I.G. A theoretical model of gamma-globulin catabolism. Nature, 1964, 203, 1352-1354.
    • (1964) Nature , vol.203 , pp. 1352-1354
    • Brambell, F.W.1    Hemmings, W.A.2    Morris, I.G.3
  • 9
    • 0030566654 scopus 로고    scopus 로고
    • Complement and Fc-receptors in regulation of the antibody response
    • Heyman, B. Complement and Fc-receptors in regulation of the antibody response. Immunol. Lett., 1996, 54, 195-199.
    • (1996) Immunol. Lett , vol.54 , pp. 195-199
    • Heyman, B.1
  • 10
    • 0030821164 scopus 로고    scopus 로고
    • Structural insights into the evolution of an antibody combining site
    • Wedemayer, G.J.; Patten, P.A.; Wang, L.H.; Schultz, P.G.; Stevens, R.C. Structural insights into the evolution of an antibody combining site. Science, 1997, 276, 1665-1669.
    • (1997) Science , vol.276 , pp. 1665-1669
    • Wedemayer, G.J.1    Patten, P.A.2    Wang, L.H.3    Schultz, P.G.4    Stevens, R.C.5
  • 11
    • 0033405041 scopus 로고    scopus 로고
    • Molecular dynamics and free-energy calculations applied to affinity maturation in antibody 48G7
    • Chong, L.T.; Duan, Y.; Wang, L.; Massova, I.; Kollman, P.A. Molecular dynamics and free-energy calculations applied to affinity maturation in antibody 48G7. Proc. Natl. Acad. Sci. USA, 1999, 96, 14330-14335.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14330-14335
    • Chong, L.T.1    Duan, Y.2    Wang, L.3    Massova, I.4    Kollman, P.A.5
  • 12
    • 4744369286 scopus 로고    scopus 로고
    • Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody
    • Midelfort, K.S.; Hernandez, H.H.; Lippow, S.M.; Tidor, B.; Drennan, C.L.; Wittrup, K.D. Substantial energetic improvement with minimal structural perturbation in a high affinity mutant antibody. J. Mol. Biol., 2004, 343, 685-701.
    • (2004) J. Mol. Biol , vol.343 , pp. 685-701
    • Midelfort, K.S.1    Hernandez, H.H.2    Lippow, S.M.3    Tidor, B.4    Drennan, C.L.5    Wittrup, K.D.6
  • 13
    • 0030580057 scopus 로고    scopus 로고
    • Antibody-antigen interactions: Contact analysis and binding site topography
    • MacCallum, R.M.; Martin, A.C.; Thornton, J.M. Antibody-antigen interactions: contact analysis and binding site topography. J. Mol. Biol., 1996, 262, 732-745.
    • (1996) J. Mol. Biol , vol.262 , pp. 732-745
    • MacCallum, R.M.1    Martin, A.C.2    Thornton, J.M.3
  • 14
    • 0036420965 scopus 로고    scopus 로고
    • Molecular recognition in antibody-antigen complexes
    • Sundberg, E.J.; Mariuzza, R.A. Molecular recognition in antibody-antigen complexes. Adv. Protein Chem., 2002, 61, 119-160.
    • (2002) Adv. Protein Chem , vol.61 , pp. 119-160
    • Sundberg, E.J.1    Mariuzza, R.A.2
  • 15
    • 0038103565 scopus 로고    scopus 로고
    • X-ray snapshots of the maturation of an antibody response to a protein antigen
    • Li, Y.; Li, H.; Yang, F.; Smith-Gill, S.J.; Mariuzza, R.A. X-ray snapshots of the maturation of an antibody response to a protein antigen. Nat. Struct. Biol., 2003, 10, 482-488.
    • (2003) Nat. Struct. Biol , vol.10 , pp. 482-488
    • Li, Y.1    Li, H.2    Yang, F.3    Smith-Gill, S.J.4    Mariuzza, R.A.5
  • 16
    • 0033555271 scopus 로고    scopus 로고
    • On the importance of being aromatic at an antibody-protein antigen interface: Mutagenesis of the extracellular interferon gamma receptor and recognition by the neutralizing antibody A6
    • Hofstädter, K.; Stuart, F.; Jiang, L.; Vrijbloed, J. W.; Robinson, J. A. On the importance of being aromatic at an antibody-protein antigen interface: mutagenesis of the extracellular interferon gamma receptor and recognition by the neutralizing antibody A6. J. Mol. Biol., 1999, 255, 805-815.
    • (1999) J. Mol. Biol , vol.255 , pp. 805-815
    • Hofstädter, K.1    Stuart, F.2    Jiang, L.3    Vrijbloed, J.W.4    Robinson, J.A.5
  • 18
    • 0028052272 scopus 로고
    • Contribution to antibody-antigen interaction of structurally perturbed antigenic residues upon antibody binding
    • Tsumoto, K.; Ueda, Y.; Maenaka, K.; Watanabe, K.; Ogasahara, K.; Yutani, K.; Kumagai, I. Contribution to antibody-antigen interaction of structurally perturbed antigenic residues upon antibody binding. J. Biol. Chem., 1994, 269, 28777-28782.
    • (1994) J. Biol. Chem , vol.269 , pp. 28777-28782
    • Tsumoto, K.1    Ueda, Y.2    Maenaka, K.3    Watanabe, K.4    Ogasahara, K.5    Yutani, K.6    Kumagai, I.7
  • 19
    • 34547460183 scopus 로고    scopus 로고
    • Molecular evolution of affinity and flexibility in the immune system
    • Thorpe, I.F.; Brooks, C.L. Molecular evolution of affinity and flexibility in the immune system. Proc. Natl. Acad. Sci. USA, 2007, 104, 8821-8826.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 8821-8826
    • Thorpe, I.F.1    Brooks, C.L.2
  • 20
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • Lo Conte, L.; Chothia, C.; Janin, J. The atomic structure of protein-protein recognition sites. J. Mol. Biol., 1999, 285, 2177-2198.
    • (1999) J. Mol. Biol , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 21
    • 33745323376 scopus 로고    scopus 로고
    • Trends in antibody sequence changes during the somatic hypermutation process
    • Clark, L.A.; Ganesan, S.; Papp, S.; van Vlijmen, H.W.T. Trends in antibody sequence changes during the somatic hypermutation process. J. Immunol., 2006, 177, 333-340.
    • (2006) J. Immunol , vol.177 , pp. 333-340
    • Clark, L.A.1    Ganesan, S.2    Papp, S.3    van Vlijmen, H.W.T.4
  • 23
    • 50649095790 scopus 로고    scopus 로고
    • Macromolecular modeling with rosetta
    • Das, R.; Baker, D. Macromolecular modeling with rosetta. Annu. Rev. Biochem., 2008, 77, 363-382.
    • (2008) Annu. Rev. Biochem , vol.77 , pp. 363-382
    • Das, R.1    Baker, D.2
  • 25
    • 0032546610 scopus 로고    scopus 로고
    • Construction of a novel redox protein by rational design: Conversion of a disulfide bridge into a mononuclear iron-sulfur center
    • Benson, D.E.; Wisz, M.S.; Liu, W.; Hellinga, H.W. Construction of a novel redox protein by rational design: conversion of a disulfide bridge into a mononuclear iron-sulfur center. Biochemistry, 1998, 37, 7070-7076.
    • (1998) Biochemistry , vol.37 , pp. 7070-7076
    • Benson, D.E.1    Wisz, M.S.2    Liu, W.3    Hellinga, H.W.4
  • 26
    • 2942601118 scopus 로고    scopus 로고
    • Computational and experimental probes of symmetry mismatches in the Arc repressor-DNA complex
    • Spector, S.; Sauer, R.T.; Tidor, B. Computational and experimental probes of symmetry mismatches in the Arc repressor-DNA complex. J. Mol. Biol., 2004, 340, 253-261.
    • (2004) J. Mol. Biol , vol.340 , pp. 253-261
    • Spector, S.1    Sauer, R.T.2    Tidor, B.3
  • 28
    • 77953659618 scopus 로고    scopus 로고
    • Altered antibodies having improved antigen-binding affinity
    • W0/2005/011376
    • Van Vlijmen, H.; Sherman, B.W.H.; Lugovskoy, A.A. Altered antibodies having improved antigen-binding affinity. W0/2005/011376.
    • van Vlijmen, H.1    Sherman, B.W.H.2    Lugovskoy, A.A.3
  • 29
    • 35148855712 scopus 로고    scopus 로고
    • Computational design of antibody-affinity improvement beyond in vivo maturation
    • Lippow, S.M.; Wittrup, K.D.; Tidor, B. Computational design of antibody-affinity improvement beyond in vivo maturation. Nat. Biotechnol., 2007, 25, 1171-1176.
    • (2007) Nat. Biotechnol , vol.25 , pp. 1171-1176
    • Lippow, S.M.1    Wittrup, K.D.2    Tidor, B.3
  • 30
    • 59449096415 scopus 로고    scopus 로고
    • Toward high-resolution homology modeling of antibody Fv regions and application to antibody-antigen docking
    • Sivasubramanian, A.; Sircar, A.; Chaudhury, S.; Gray, J.J. Toward high-resolution homology modeling of antibody Fv regions and application to antibody-antigen docking. Proteins, 2009, 74, 497-514.
    • (2009) Proteins , vol.74 , pp. 497-514
    • Sivasubramanian, A.1    Sircar, A.2    Chaudhury, S.3    Gray, J.J.4
  • 33
    • 67649647815 scopus 로고    scopus 로고
    • Improving the species cross-reactivity of an antibody using computational design
    • Farady, C.J.; Sellers, B.D.; Jacobson, M.P.; Craik, C.S. Improving the species cross-reactivity of an antibody using computational design. Bioorg. Med. Chem. Lett., 2009, 19, 3744-3747.
    • (2009) Bioorg. Med. Chem. Lett , vol.19 , pp. 3744-3747
    • Farady, C.J.1    Sellers, B.D.2    Jacobson, M.P.3    Craik, C.S.4
  • 34
    • 38449104580 scopus 로고    scopus 로고
    • Humanization of antibodies
    • Almagro, J.C.; Fransson, J. Humanization of antibodies. Front. Biosci., 2008, 13, 1619-1633.
    • (2008) Front. Biosci , vol.13 , pp. 1619-1633
    • Almagro, J.C.1    Fransson, J.2
  • 35
    • 0022558297 scopus 로고
    • Replacing the complementarity-determining regions in a human antibody with those from a mouse
    • Jones, P.T.; Dear, P.H.; Foote, J.; Neuberger, M.S.; Winter, G. Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature, 1986, 321, 522-525.
    • (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
  • 36
    • 0023920595 scopus 로고
    • Reshaping human antibodies: Grafting an antilysozyme activity
    • Verhoeyen, M.; Milstein, C.; Winter, G. Reshaping human antibodies: grafting an antilysozyme activity. Science, 1988, 239, 1534-1536.
    • (1988) Science , vol.239 , pp. 1534-1536
    • Verhoeyen, M.1    Milstein, C.2    Winter, G.3
  • 38
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia, C.; Lesk, A.M. Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol., 1987, 196, 901-917.
    • (1987) J. Mol. Biol , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 39
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • Al-Lazikani, B.; Lesk, A.M.; Chothia, C. Standard conformations for the canonical structures of immunoglobulins. J. Mol. Biol., 1997, 273, 927-948.
    • (1997) J. Mol. Biol , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 41
    • 0026438009 scopus 로고
    • Engineering a humanized bispecific F(ab')2 fragment for improved binding to T cells
    • Rodrigues, M.L.; Shalaby, M.R.; Werther, W.; Presta, L.; Carter, P. Engineering a humanized bispecific F(ab')2 fragment for improved binding to T cells. Int. J. Cancer Suppl., 1992, 7, 45-50.
    • (1992) Int. J. Cancer Suppl , vol.7 , pp. 45-50
    • Rodrigues, M.L.1    Shalaby, M.R.2    Werther, W.3    Presta, L.4    Carter, P.5
  • 42
    • 0030856731 scopus 로고    scopus 로고
    • Humanization of an anti-vascular endothelial growth factor monoclonal antibody for the therapy of solid tumors and other disorders
    • Presta, L.G.; Chen, H.; O'Connor, S.J.; Chisholm, V.; Meng, Y. G.; Krummen, L.; Winkler, M.; Ferrara, N. Humanization of an anti-vascular endothelial growth factor monoclonal antibody for the therapy of solid tumors and other disorders. Cancer Res., 1997, 57, 4593-4599.
    • (1997) Cancer Res , vol.57 , pp. 4593-4599
    • Presta, L.G.1    Chen, H.2    O'Connor, S.J.3    Chisholm, V.4    Meng, Y.G.5    Krummen, L.6    Winkler, M.7    Ferrara, N.8
  • 43
    • 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
    • Tan, P.; Mitchell, D.A.; Buss, T.N.; Holmes, M.A.; Anasetti, C.; Foote, J. "Superhumanized" antibodies: reduction of immunogenic potential by complementarity-determining region grafting with human germline sequences: application to an anti-CD28. J. Immunol., 2002, 169, 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
  • 44
    • 17644422139 scopus 로고    scopus 로고
    • Use of human germline genes in a CDR homology-based approach to antibody humanization
    • Hwang, W.Y.K.; Almagro, J.C.; Buss, T.N.; Tan, P.; Foote, J. Use of human germline genes in a CDR homology-based approach to antibody humanization. Methods, 2005, 36, 35-42.
    • (2005) Methods , vol.36 , pp. 35-42
    • Hwang, W.Y.K.1    Almagro, J.C.2    Buss, T.N.3    Tan, P.4    Foote, J.5
  • 45
    • 34249017414 scopus 로고    scopus 로고
    • A molecular immunology approach to antibody humanization and functional optimization
    • Lazar, G.A.; Desjarlais, J.R.; Jacinto, J.; Karki, S.; Hammond, P.W. A molecular immunology approach to antibody humanization and functional optimization. Mol. Immunol., 2007, 44, 1986-1998.
    • (2007) Mol. Immunol , vol.44 , pp. 1986-1998
    • Lazar, G.A.1    Desjarlais, J.R.2    Jacinto, J.3    Karki, S.4    Hammond, P.W.5
  • 47
    • 0025848797 scopus 로고
    • A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties
    • Padlan, E.A. A possible procedure for reducing the immunogenicity of antibody variable domains while preserving their ligand-binding properties. Mol. Immunol., 1991, 25, 489-498.
    • (1991) Mol. Immunol , vol.25 , pp. 489-498
    • Padlan, E.A.1
  • 48
    • 0035824579 scopus 로고    scopus 로고
    • Role of oligosaccharide residues of IgG1-Fc in Fcgamma RIIb binding
    • Mimura, Y. Role of oligosaccharide residues of IgG1-Fc in Fcgamma RIIb binding. J. Biol. Chem., 2001, 276, 45539-45547.
    • (2001) J. Biol. Chem , vol.276 , pp. 45539-45547
    • Mimura, Y.1
  • 49
    • 0034076307 scopus 로고    scopus 로고
    • Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets
    • Clynes, R.A.; Towers, T.L.; Presta, L.G.; Ravetch, J.V. Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets. Nat. Med., 2000, 6, 443-446.
    • (2000) Nat. Med , vol.6 , pp. 443-446
    • Clynes, R.A.1    Towers, T.L.2    Presta, L.G.3    Ravetch, J.V.4
  • 50
    • 35748949531 scopus 로고    scopus 로고
    • Optimizing engagement of the immune system by anti-tumor antibodies: An engineer's perspective
    • Desjarlais, J.R.; Lazar, G.A.; Zhukovsky, E.A.; Chu, S.Y. Optimizing engagement of the immune system by anti-tumor antibodies: an engineer's perspective. Drug Discov. Today, 2007, 12, 898-910.
    • (2007) Drug Discov. Today , vol.12 , pp. 898-910
    • Desjarlais, J.R.1    Lazar, G.A.2    Zhukovsky, E.A.3    Chu, S.Y.4
  • 51
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for Fcgamma RI, Fcgamma RII, Fcgamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fcgamma R
    • Shields, R.L. High resolution mapping of the binding site on human IgG1 for Fcgamma RI, Fcgamma RII, Fcgamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fcgamma R. J. Biol. Chem., 2000, 276, 6591-6604.
    • (2000) J. Biol. Chem , vol.276 , pp. 6591-6604
    • Shields, R.L.1
  • 52
    • 0033044588 scopus 로고    scopus 로고
    • Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity
    • Uma a, P.; Jean-Mairet, J.; Moudry, R.; Amstutz, H.; Bailey, J.E. Engineered glycoforms of an antineuroblastoma IgG1 with optimized antibody-dependent cellular cytotoxic activity. Nat. Biotech., 1999, 17, 176-180.
    • (1999) Nat. Biotech , vol.17 , pp. 176-180
    • Uma a, P.1    Jean-Mairet, J.2    Moudry, R.3    Amstutz, H.4    Bailey, J.E.5
  • 53
    • 0034691322 scopus 로고    scopus 로고
    • The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex
    • Sondermann, P.; Huber, R.; Oosthuizen, V.; Jacob, U. The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature, 2000, 406, 267-273.
    • (2000) Nature , vol.406 , pp. 267-273
    • Sondermann, P.1    Huber, R.2    Oosthuizen, V.3    Jacob, U.4
  • 55
    • 53349120501 scopus 로고    scopus 로고
    • Optimization of antibody binding to FcgammaRIIa enhances macrophage phagocytosis of tumor cells
    • Richards, J.O.; Karki, S.; Lazar, G.A.; Chen, H.; Dang, W.; Desjarlais, J.R. Optimization of antibody binding to FcgammaRIIa enhances macrophage phagocytosis of tumor cells. Mol. Cancer Ther., 2008, 7, 2517-2527.
    • (2008) Mol. Cancer Ther , vol.7 , pp. 2517-2527
    • Richards, J.O.1    Karki, S.2    Lazar, G.A.3    Chen, H.4    Dang, W.5    Desjarlais, J.R.6
  • 56
    • 39149106011 scopus 로고    scopus 로고
    • Structural characterization of a mutated, ADCC-enhanced human Fc fragment
    • Oganesyan, V.; Damschroder, M.M.; Leach, W.; Wu, H.; Dall'Acqua, W.F. Structural characterization of a mutated, ADCC-enhanced human Fc fragment. Mol. Immunol., 2008, 45, 1872-1882.
    • (2008) Mol. Immunol , vol.45 , pp. 1872-1882
    • Oganesyan, V.1    Damschroder, M.M.2    Leach, W.3    Wu, H.4    Dall'acqua, W.F.5
  • 59
    • 0034042660 scopus 로고    scopus 로고
    • Multiple roles for the major histocompatibility complex class I- related receptor FcRn
    • Ghetie, V.; Ward, E.S. Multiple roles for the major histocompatibility complex class I- related receptor FcRn. Annu. Rev. Immunol., 2000, 15, 739-766.
    • (2000) Annu. Rev. Immunol , vol.15 , pp. 739-766
    • Ghetie, V.1    Ward, E.S.2
  • 60
    • 34248655131 scopus 로고    scopus 로고
    • Tunable pharmacokinetics: Modifying the in vivo half-life of antibodies by directed mutagenesis of the Fc fragment
    • Olafsen, T.; Kenanova, V.E.; Wu, A.M. Tunable pharmacokinetics: modifying the in vivo half-life of antibodies by directed mutagenesis of the Fc fragment. Nat. Protoc., 2006, 1, 2048-2060.
    • (2006) Nat. Protoc , vol.1 , pp. 2048-2060
    • Olafsen, T.1    Kenanova, V.E.2    Wu, A.M.3
  • 61
    • 0028808880 scopus 로고
    • Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants
    • Raghavan, M.; Bonagura, V.R.; Morrison, S.L.; Bjorkman, P.J. Analysis of the pH dependence of the neonatal Fc receptor/immunoglobulin G interaction using antibody and receptor variants. Biochemistry, 1995, 34, 14649-14657.
    • (1995) Biochemistry , vol.34 , pp. 14649-14657
    • Raghavan, M.1    Bonagura, V.R.2    Morrison, S.L.3    Bjorkman, P.J.4
  • 62
    • 0031093498 scopus 로고    scopus 로고
    • Delineation of the amino acid residues involved in transcytosis and catabolism of mouse IgG1
    • Medesan, C.; Matesoi, D.; Radu, C.; Ghetie, V.; Ward, E.S. Delineation of the amino acid residues involved in transcytosis and catabolism of mouse IgG1. J. Immunol., 1997, 155, 2211.
    • (1997) J. Immunol , vol.158 , pp. 2211
    • Medesan, C.1    Matesoi, D.2    Radu, C.3    Ghetie, V.4    Ward, E.S.5
  • 63
    • 0028089908 scopus 로고
    • Crystal structure of the complex of rat neonatal Fc receptor with Fc
    • Burmeister, W.P.; Huber, A.H.; Bjorkman, P.J. Crystal structure of the complex of rat neonatal Fc receptor with Fc. Nature, 1994, 372, 379-383.
    • (1994) Nature , vol.372 , pp. 379-383
    • Burmeister, W.P.1    Huber, A.H.2    Bjorkman, P.J.3
  • 64
    • 48549105161 scopus 로고    scopus 로고
    • Molecular engineering and design of therapeutic antibodies
    • Presta, L.G. Molecular engineering and design of therapeutic antibodies. Curr. Opin. Immunol., 2008, 20, 460-470.
    • (2008) Curr. Opin. Immunol , vol.20 , pp. 460-470
    • Presta, L.G.1
  • 65
    • 67649207267 scopus 로고    scopus 로고
    • Engineering human IgG1 affinity to human neonatal Fc receptor: Impact of affinity improvement on pharmacokinetics in primates
    • Yeung, Y.A.; Leabman, M.K.; Marvin, J.S.; Qiu, J.; Adams, C.W.; Lien, S.; Starovasnik, M.A.; Lowman, H.B. Engineering human IgG1 affinity to human neonatal Fc receptor: impact of affinity improvement on pharmacokinetics in primates. J. Immunol., 2009, 152, 7663.
    • (2009) J. Immunol , vol.152 , pp. 7663
    • Yeung, Y.A.1    Leabman, M.K.2    Marvin, J.S.3    Qiu, J.4    Adams, C.W.5    Lien, S.6    Starovasnik, M.A.7    Lowman, H.B.8
  • 67
    • 33747631571 scopus 로고    scopus 로고
    • Properties of human IgG1s engineered for enhanced binding to the neonatal Fc Receptor (FcRn)
    • Dall'Acqua, W.F. Properties of human IgG1s engineered for enhanced binding to the neonatal Fc Receptor (FcRn). J. Biol. Chem., 2006, 251, 23514-23524.
    • (2006) J. Biol. Chem , vol.251 , pp. 23514-23524
    • Dall'acqua, W.F.1
  • 70
    • 50249132634 scopus 로고    scopus 로고
    • Antibody therapeutics, antibody engineering, and the merits of protein stability
    • Demarest, S.J.; Glaser, S.M. Antibody therapeutics, antibody engineering, and the merits of protein stability. Curr. Opin. Drug Discov. Dev., 2008, 11, 675-687.
    • (2008) Curr. Opin. Drug Discov. Dev , vol.11 , pp. 675-687
    • Demarest, S.J.1    Glaser, S.M.2
  • 71
    • 0025162270 scopus 로고
    • A comparison of strategies to stabilize immunoglobulin Fv-fragments
    • Glockshuber, R.; Malia, M.; Pfitzinger, I.; Pluckthun, A. A comparison of strategies to stabilize immunoglobulin Fv-fragments. Biochemistry, 1990, 29, 1362-1367.
    • (1990) Biochemistry , vol.29 , pp. 1362-1367
    • Glockshuber, R.1    Malia, M.2    Pfitzinger, I.3    Pluckthun, A.4
  • 72
    • 0028275293 scopus 로고
    • Design of interchain disulfide bonds in the framework region of the Fv fragment of the monoclonal antibody B3
    • Jung, S.H.; Pastan, I.; Lee, B. Design of interchain disulfide bonds in the framework region of the Fv fragment of the monoclonal antibody B3. Proteins, 1994, 19, 35-47.
    • (1994) Proteins , vol.19 , pp. 35-47
    • Jung, S.H.1    Pastan, I.2    Lee, B.3
  • 73
    • 0028959129 scopus 로고
    • Development of a humanized disulfide-stabilized anti-p185HER2 Fv-beta-lactamase fusion protein for activation of a cephalosporin doxorubicin prodrug
    • Rodrigues, M.L.; Presta, L. G.; Kotts, C.E.; Wirth, C.; Mordenti, J.; Osaka, G.; Wong, W.L.; Nuijens, A.; Blackburn, B.; Carter, P. Development of a humanized disulfide-stabilized anti-p185HER2 Fv-beta-lactamase fusion protein for activation of a cephalosporin doxorubicin prodrug. Cancer Res., 1995, 55, 63-70.
    • (1995) Cancer Res , vol.55 , pp. 63-70
    • Rodrigues, M.L.1    Presta, L.G.2    Kotts, C.E.3    Wirth, C.4    Mordenti, J.5    Osaka, G.6    Wong, W.L.7    Nuijens, A.8    Blackburn, B.9    Carter, P.10
  • 74
    • 0029557830 scopus 로고
    • Thermal stabilization of a single-chain Fv antibody fragment by introduction of a disulphide bond
    • Young, N.M.; MacKenzie, C.R.; Narang, S.A.; Oomen, R.P.; Baenziger, J.E. Thermal stabilization of a single-chain Fv antibody fragment by introduction of a disulphide bond. FEBS Lett., 1995, 577, 135-139.
    • (1995) FEBS Lett , vol.577 , pp. 135-139
    • Young, N.M.1    Mackenzie, C.R.2    Narang, S.A.3    Oomen, R.P.4    Baenziger, J.E.5
  • 75
    • 0032538296 scopus 로고    scopus 로고
    • The nature of antibody heavy chain residue H6 strongly influences the stability of a VH domain lacking the disulfide bridge
    • Langedijk, A.C.; Honegger, A.; Maat, J.; Planta, R.J.; van Schaik, R.C.; Pluckthun, A. The nature of antibody heavy chain residue H6 strongly influences the stability of a VH domain lacking the disulfide bridge. J. Mol. Biol., 1998, 283, 95-110.
    • (1998) J. Mol. Biol , vol.283 , pp. 95-110
    • Langedijk, A.C.1    Honegger, A.2    Maat, J.3    Planta, R.J.4    van Schaik, R.C.5    Pluckthun, A.6
  • 76
    • 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, S.M.; Moldenhauer, G.; Martin, A.C.; Kupriyanova, O.A.; Little, M. 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., 1997, 10, 445-453.
    • (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
  • 77
    • 0035827218 scopus 로고    scopus 로고
    • The influence of the buried glutamine or glutamate residue in position 6 on the structure of immunoglobulin variable domains
    • Honegger, A.; Pluckthun, A. The influence of the buried glutamine or glutamate residue in position 6 on the structure of immunoglobulin variable domains. J. Mol. Biol., 2001, 309, 687-699.
    • (2001) J. Mol. Biol , vol.309 , pp. 687-699
    • Honegger, A.1    Pluckthun, A.2
  • 78
    • 0035827149 scopus 로고    scopus 로고
    • The importance of framework residues H6, H7 and H10 in antibody heavy chains: Experimental evidence for a new structural subclassification of antibody V(H) domains
    • Jung, S.; Spinelli, S.; Schimmele, B.; Honegger, A.; Pugliese, L.; Cambillau, C.; Pluckthun, A. The importance of framework residues H6, H7 and H10 in antibody heavy chains: experimental evidence for a new structural subclassification of antibody V(H) domains. J. Mol. Biol., 2001, 309, 701-716.
    • (2001) J. Mol. Biol , vol.309 , pp. 701-716
    • Jung, S.1    Spinelli, S.2    Schimmele, B.3    Honegger, A.4    Pugliese, L.5    Cambillau, C.6    Pluckthun, A.7
  • 79
    • 0037227517 scopus 로고    scopus 로고
    • Biophysical properties of human antibody variable domains
    • Ewert, S.; Huber, T.; Honegger, A.; Pluckthun, A. Biophysical properties of human antibody variable domains. J. Mol. Biol., 2003, 325, 531-553.
    • (2003) J. Mol. Biol , vol.325 , pp. 531-553
    • Ewert, S.1    Huber, T.2    Honegger, A.3    Pluckthun, A.4
  • 80
    • 0034635335 scopus 로고    scopus 로고
    • Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides
    • Knappik, A.; Ge, L.; Honegger, A.; Pack, P.; Fischer, M.; Wellnhofer, G.; Hoess, A.; Wolle, J.; Pluckthun, A.; Virnekas, B. Fully synthetic human combinatorial antibody libraries (HuCAL) based on modular consensus frameworks and CDRs randomized with trinucleotides. J. Mol. Biol., 2000, 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    Wellnhofer, G.6    Hoess, A.7    Wolle, J.8    Pluckthun, A.9    Virnekas, B.10
  • 81
    • 0037452533 scopus 로고    scopus 로고
    • Structure-based improvement of the biophysical properties of immunoglobulin VH domains with a generalizable approach
    • Ewert, S.; Honegger, A.; Pluckthun, A. Structure-based improvement of the biophysical properties of immunoglobulin VH domains with a generalizable approach. Biochemistry, 2003, 42, 1517-1528.
    • (2003) Biochemistry , vol.42 , pp. 1517-1528
    • Ewert, S.1    Honegger, A.2    Pluckthun, A.3
  • 82
    • 4143110187 scopus 로고    scopus 로고
    • Stability improvement of antibodies for extracellular and intracellular applications: CDR grafting to stable frameworks and structure-based framework engineering
    • Ewert, S.; Honegger, A.; Pluckthun, A. Stability improvement of antibodies for extracellular and intracellular applications: CDR grafting to stable frameworks and structure-based framework engineering. Methods, 2004, 34, 184-199.
    • (2004) Methods , vol.34 , pp. 184-199
    • Ewert, S.1    Honegger, A.2    Pluckthun, A.3
  • 83
    • 60749123075 scopus 로고    scopus 로고
    • The influence of the framework core residues on the biophysical properties of immunoglobulin heavy chain variable domains
    • Honegger, A.; Malebranche, A.D.; Rothlisberger, D.; Pluckthun, A. The influence of the framework core residues on the biophysical properties of immunoglobulin heavy chain variable domains. Protein Eng. Des. Sel., 2009, 22, 121-134.
    • (2009) Protein Eng. Des. Sel , vol.22 , pp. 121-134
    • Honegger, A.1    Malebranche, A.D.2    Rothlisberger, D.3    Pluckthun, A.4
  • 84
    • 33847416982 scopus 로고    scopus 로고
    • A broad range of Fab stabilities within a host of therapeutic IgGs
    • Garber, E.; Demarest, S.J. A broad range of Fab stabilities within a host of therapeutic IgGs. Biochem. Biophys. Res. Commun., 2007, 355, 751-757.
    • (2007) Biochem. Biophys. Res. Commun , vol.355 , pp. 751-757
    • Garber, E.1    Demarest, S.J.2
  • 85
    • 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. 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., 1997, 10, 435-444.
    • (1997) Protein Eng , vol.10 , pp. 435-444
    • Nieba, L.1    Honegger, A.2    Krebber, C.3    Pluckthun, A.4
  • 86
    • 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, P.S.; Vasmatzis, G.; Beers, R.; Lee, B.; Pastan, I. Improved stability and yield of a Fv-toxin fusion protein by computer design and protein engineering of the Fv. J. Mol. Biol., 1998, 281, 917-928.
    • (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
  • 88
    • 0032558362 scopus 로고    scopus 로고
    • Mutual stabilization of VL and VH in single-chain antibody fragments, investigated with mutants engineered for stability
    • Wörn, A.; Plückthun, A. Mutual stabilization of VL and VH in single-chain antibody fragments, investigated with mutants engineered for stability. Biochemistry, 1998, 37, 13120-13127.
    • (1998) Biochemistry , vol.37 , pp. 13120-13127
    • Wörn, A.1    Plückthun, A.2
  • 89
    • 0040964401 scopus 로고    scopus 로고
    • Different equilibrium stability behavior of ScFv fragments: Identification, classification, and improvement by protein engineering
    • Wörn, A.; Plückthun, A. Different equilibrium stability behavior of ScFv fragments: identification, classification, and improvement by protein engineering. Biochemistry, 1999, 38, 8739-8750.
    • (1999) Biochemistry , vol.38 , pp. 8739-8750
    • Wörn, A.1    Plückthun, A.2
  • 90
    • 14844339334 scopus 로고    scopus 로고
    • Domain interactions in the Fab fragment: A comparative evaluation of the single-chain Fv and Fab format engineered with variable domains of different stability
    • Röthlisberger, D.; Honegger, A.; Plückthun, A. Domain interactions in the Fab fragment: a comparative evaluation of the single-chain Fv and Fab format engineered with variable domains of different stability. J. Mol. Biol., 2005, 347, 773-789.
    • (2005) J. Mol. Biol , vol.347 , pp. 773-789
    • Röthlisberger, D.1    Honegger, A.2    Plückthun, A.3
  • 91
    • 41249087476 scopus 로고    scopus 로고
    • Comprehensive analysis of the factors contributing to the stability and solubility of autonomous human VH domains
    • Barthelemy, P.A.; Raab, H.; Appleton, B.A.; Bond, C.J.; Wu, P.; Wiesmann, C.; Sidhu, S.S. Comprehensive analysis of the factors contributing to the stability and solubility of autonomous human VH domains. J. Biol. Chem., 2008, 283, 3639-3654.
    • (2008) J. Biol. Chem , vol.283 , pp. 3639-3654
    • Barthelemy, P.A.1    Raab, H.2    Appleton, B.A.3    Bond, C.J.4    Wu, P.5    Wiesmann, C.6    Sidhu, S.S.7
  • 92
    • 0037133506 scopus 로고    scopus 로고
    • Biophysical properties of camelid V(HH) domains compared to those of human V(H)3 domains
    • Ewert, S.; Cambillau, C.; Conrath, K.; Pluckthun, A. Biophysical properties of camelid V(HH) domains compared to those of human V(H)3 domains. Biochemistry, 2002, 41, 3628-3636.
    • (2002) Biochemistry , vol.41 , pp. 3628-3636
    • Ewert, S.1    Cambillau, C.2    Conrath, K.3    Pluckthun, A.4
  • 98
    • 33744964246 scopus 로고    scopus 로고
    • Single variable domain-IgG fusion. A novel recombinant approach to Fc domain-containing bispecific antibodies
    • Shen, J.; Vil, M.D.; Jimenez, X.; Iacolina, M.; Zhang, H.; Zhu, Z. Single variable domain-IgG fusion. A novel recombinant approach to Fc domain-containing bispecific antibodies. J. Biol. Chem., 2006, 281, 10706-10714.
    • (2006) J. Biol. Chem , vol.281 , pp. 10706-10714
    • Shen, J.1    Vil, M.D.2    Jimenez, X.3    Iacolina, M.4    Zhang, H.5    Zhu, Z.6


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