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Volumn 169, Issue 2, 1996, Pages 147-155

Identification of functional and structural amino-acid residues by parsimonious mutagenesis

Author keywords

Affinity maturation; c erbB 2; Phage display; Random mutagenesis; Single chain Fv

Indexed keywords

AMINO ACID; NUCLEOTIDE;

EID: 0029881373     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/0378-1119(95)00821-7     Document Type: Article
Times cited : (56)

References (38)
  • 2
    • 0027761151 scopus 로고
    • Antibody engineering by parsimonious mutagenesis
    • Balint, R.F. and Larrick, J.W.: Antibody engineering by parsimonious mutagenesis. Gene 137 (1993) 109-118.
    • (1993) Gene , vol.137 , pp. 109-118
    • Balint, R.F.1    Larrick, J.W.2
  • 3
    • 0028348564 scopus 로고
    • In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity
    • Barbas III, C.F., Hu, D., Dunlop, N., Sawyer, L., Cabara, D., Hendry, R.M., Nara, P.L. and Burton, D.R.: In vitro evolution of a neutralizing human antibody to human immunodeficiency virus type 1 to enhance affinity and broaden strain cross-reactivity. Proc. Natl. Acad. Sci. USA 91 (1994) 3809-3813.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 3809-3813
    • Barbas C.F. III1    Hu, D.2    Dunlop, N.3    Sawyer, L.4    Cabara, D.5    Hendry, R.M.6    Nara, P.L.7    Burton, D.R.8
  • 4
    • 0025944567 scopus 로고
    • A surface expression vector for antibody screening
    • Breitling, S.D., Seehaus, T., Klewinghaus, I. and Little, M.: A surface expression vector for antibody screening. Gene 104 (1991) 147-153.
    • (1991) Gene , vol.104 , pp. 147-153
    • Breitling, S.D.1    Seehaus, T.2    Klewinghaus, I.3    Little, M.4
  • 6
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia, C. and Lesk, A.M.: Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol. 196 (1987) 901-917.
    • (1987) J. Mol. Biol. , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 9
    • 0025254304 scopus 로고
    • Regulated expression of foreign genes fused to lac: Control by glucose levels in growth medium
    • De Bellis, D. and Schwartz, I.: Regulated expression of foreign genes fused to lac: control by glucose levels in growth medium. Nucleic Acids Res. 18 (1990) 1311.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 1311
    • De Bellis, D.1    Schwartz, I.2
  • 10
    • 0027366187 scopus 로고
    • Searching sequence space to engineer proteins: Exponential ensemble mutagenesis
    • Delagrave, S. and Youvan, D.C.: Searching sequence space to engineer proteins: exponential ensemble mutagenesis. Bio/Technology 11 (1993) 1548-1552.
    • (1993) Bio/technology , vol.11 , pp. 1548-1552
    • Delagrave, S.1    Youvan, D.C.2
  • 11
    • 0029653368 scopus 로고
    • Kinetic and affinity limits on antibodies produced during immune responses
    • Foote, J. and Eisen, H.N.: Kinetic and affinity limits on antibodies produced during immune responses. Proc. Natl. Acad. Sci. USA 92 (1995) 1254-1256.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 1254-1256
    • Foote, J.1    Eisen, H.N.2
  • 13
    • 0027473684 scopus 로고
    • Human anti-self antibodies with high specificity from phage display libraries
    • Griffiths, A.D. and Malmqvist, M.: Human anti-self antibodies with high specificity from phage display libraries. EMBO J. 12 (1993) 725-734.
    • (1993) EMBO J. , vol.12 , pp. 725-734
    • Griffiths, A.D.1    Malmqvist, M.2
  • 15
    • 3242793191 scopus 로고
    • Direct clone characterization from plaques and colonies by the polymerase chain reaction
    • Gussow, D. and Clackson, T.: Direct clone characterization from plaques and colonies by the polymerase chain reaction. Nucleic Acids Res. 17 (1989) 4000.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 4000
    • Gussow, D.1    Clackson, T.2
  • 16
    • 0027768856 scopus 로고
    • The contribution of contact and non-contact residues of antibody in the affinity of binding to antigen. The interaction of mutant D1.3 antibodies with lysozyme
    • Hawkins, R.E., Russell, S.J., Baier, M. and Winter, G.: The contribution of contact and non-contact residues of antibody in the affinity of binding to antigen. The interaction of mutant D1.3 antibodies with lysozyme. J. Mol. Biol. 234 (1993) 958-964.
    • (1993) J. Mol. Biol. , vol.234 , pp. 958-964
    • Hawkins, R.E.1    Russell, S.J.2    Baier, M.3    Winter, G.4
  • 17
    • 0026699293 scopus 로고
    • Selection of phage antibodies by binding affinity: Mimicking affinity maturation
    • Hawkins, R.E., Russell, S.J. and Winter, G.: Selection of phage antibodies by binding affinity: mimicking affinity maturation. J. Mol. Biol. 226 (1992) 889-896.
    • (1992) J. Mol. Biol. , vol.226 , pp. 889-896
    • Hawkins, R.E.1    Russell, S.J.2    Winter, G.3
  • 18
    • 0023781763 scopus 로고
    • Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent
    • Hochuli, E., Bannwarth, W., Dobeli, H., Gentz, R. and Stuber, D.: Genetic approach to facilitate purification of recombinant proteins with a novel metal chelate adsorbent. Bio/Technology 6 (1988) 1321-1325.
    • (1988) Bio/technology , vol.6 , pp. 1321-1325
    • Hochuli, E.1    Bannwarth, W.2    Dobeli, H.3    Gentz, R.4    Stuber, D.5
  • 19
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom, H.R., Griffiths, A.D., Johnson, K.S., Chiswell, D.J., Hudson, P. and Winter, G.: Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res. 19 (1991) 4133-4137.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 20
    • 0026673067 scopus 로고
    • Bypassing immunisation: Human antibodies from synthetic repertoires of germ line VH-gene segments rearranged in vitro
    • Hoogenboom, H.R. and Winter, G.: Bypassing immunisation: human antibodies from synthetic repertoires of germ line VH-gene segments rearranged in vitro. J. Mol. Biol. 227 (1992) 381-388.
    • (1992) J. Mol. Biol. , vol.227 , pp. 381-388
    • Hoogenboom, H.R.1    Winter, G.2
  • 21
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran modified gold surface for BIAcore in surface plasmon resonance
    • Johnsson, B., Lofas, S. and Lindqvist, G.: Immobilization of proteins to a carboxymethyldextran modified gold surface for BIAcore in surface plasmon resonance. Anal. Biochem. 198 (1991) 268-277.
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Lofas, S.2    Lindqvist, G.3
  • 24
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system
    • Karlsson, R., Michaelsson, A. and Mattsson, L.: Kinetic analysis of monoclonal antibody-antigen interactions with a new biosensor based analytical system. J. Immunol. Methods 145 (1991) 229-240.
    • (1991) J. Immunol. Methods , vol.145 , pp. 229-240
    • Karlsson, R.1    Michaelsson, A.2    Mattsson, L.3
  • 25
    • 0027228495 scopus 로고
    • Thermodynamic analysis of an antibody functional epitope
    • Kelley, R.F. and O'Connell, M.P.: Thermodynamic analysis of an antibody functional epitope. Biochemistry 32 (1993) 6828-6835.
    • (1993) Biochemistry , vol.32 , pp. 6828-6835
    • Kelley, R.F.1    O'Connell, M.P.2
  • 26
    • 0027136111 scopus 로고
    • Affinity maturation of human growth hormone by monovalent phage display
    • Lowman, H.B. and Wells, J.A.: Affinity maturation of human growth hormone by monovalent phage display. J. Mol. Biol. 234 (1993) 564-578.
    • (1993) J. Mol. Biol. , vol.234 , pp. 564-578
    • Lowman, H.B.1    Wells, J.A.2
  • 30
    • 0019119230 scopus 로고
    • Crystallographic refinement and atomic models of the intact immunoglobulin molecule KOL and its antigen binding fragment at 3.0 Å and 1.9 Å resolution
    • Marquart, M., Deisenhofer, J., Huber, R. and Palm, W.: Crystallographic refinement and atomic models of the intact immunoglobulin molecule KOL and its antigen binding fragment at 3.0 Å and 1.9 Å resolution. J. Mol. Biol. 141 (1980) 369-391.
    • (1980) J. Mol. Biol. , vol.141 , pp. 369-391
    • Marquart, M.1    Deisenhofer, J.2    Huber, R.3    Palm, W.4
  • 31
    • 0025226085 scopus 로고
    • Phage antibodies: Filamentous phage displaying antibody variable domains
    • McCafferty, J., Griffiths, A.D., Winter, G. and Chiswell, D.J.: 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
  • 32
    • 0024362070 scopus 로고
    • On the attribution of binding energy in antigen-antibody complexes McPC 603, D1.3, and HyHEL-5
    • Novotny, J., Bruccoleri, R.E. and Saul, F.A.: On the attribution of binding energy in antigen-antibody complexes McPC 603, D1.3, and HyHEL-5. Biochemistry 28 (1989) 4735-4749.
    • (1989) Biochemistry , vol.28 , pp. 4735-4749
    • Novotny, J.1    Bruccoleri, R.E.2    Saul, F.A.3
  • 34
    • 0029294084 scopus 로고
    • In vitro and in vivo characterization of a human anti-c-erbB-2 single-chain Fv isolated from a filamentous phage antibody library
    • Schier, R., Marks, J.D., Wolf, E.J., Appell, G., Huston, J.S., Weiner, L.M. and Adams, G.P.: In vitro and in vivo characterization of a human anti-c-erbB-2 single-chain Fv isolated from a filamentous phage antibody library. Immunotechnology 1 (1995) 73-81.
    • (1995) Immunotechnology , vol.1 , pp. 73-81
    • Schier, R.1    Marks, J.D.2    Wolf, E.J.3    Appell, G.4    Huston, J.S.5    Weiner, L.M.6    Adams, G.P.7
  • 35
    • 0029989324 scopus 로고    scopus 로고
    • Isolation of high affinity monmeric human anti-c-erbB-2 single chain Fv using affinity driven selection
    • Schier, R., Bye, J., Apell, G., McCall, A., Adams, G.P., Weiner, L.M. and Marks, J.D.: Isolation of high affinity monmeric human anti-c-erbB-2 single chain Fv using affinity driven selection. J. Mol. Biol. 255 (1996) 28-43.
    • (1996) J. Mol. Biol. , vol.255 , pp. 28-43
    • Schier, R.1    Bye, J.2    Apell, G.3    McCall, A.4    Adams, G.P.5    Weiner, L.M.6    Marks, J.D.7
  • 37
    • 0026781840 scopus 로고
    • Refined crystal structure of the influenza virus neuraminidase-NC41 Fab complex
    • R.G., W.
    • Tulip, W.R., Varghese, J.N., Laver, W.G., R.G., W. and Colman, P.M.: Refined crystal structure of the influenza virus neuraminidase-NC41 Fab complex. J. Mol Biol. 227 (1992) 122-148.
    • (1992) J. Mol Biol. , vol.227 , pp. 122-148
    • Tulip, W.R.1    Varghese, J.N.2    Laver, W.G.3    Colman, P.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.