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Volumn 16, Issue 7, 1998, Pages 677-681

An efficient route to human bispecific IgG

Author keywords

Antibody engineering; Applied immunology; Phage display

Indexed keywords

IMMUNOGLOBULIN G; IMMUNOGLOBULIN LIGHT CHAIN;

EID: 0031876578     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/nbt0798-677     Document Type: Article
Times cited : (397)

References (41)
  • 2
    • 0028786757 scopus 로고
    • Toward the production of bispecific antibody fragments for clinical applications
    • Carter, P., Ridgway J., and Zhu, Z. 1995. Toward the production of bispecific antibody fragments for clinical applications. J. Hematother. 4:463-470.
    • (1995) J. Hematother. , vol.4 , pp. 463-470
    • Carter, P.1    Ridgway, J.2    Zhu, Z.3
  • 3
    • 0030738617 scopus 로고    scopus 로고
    • New protein engineering approaches to multivalent and bispecific antibody fragments
    • Plückthun, A. and Pack, P. 1997. New protein engineering approaches to multivalent and bispecific antibody fragments. Immunotechnology 3:83-105.
    • (1997) Immunotechnology , vol.3 , pp. 83-105
    • Plückthun, A.1    Pack, P.2
  • 4
    • 0020518331 scopus 로고
    • Hybrid hybriodomas and their use in immunohistochemistry
    • Milstein, C. and Cuello, A.C. 1983. Hybrid hybriodomas and their use in immunohistochemistry. Nature 305:537-540.
    • (1983) Nature , vol.305 , pp. 537-540
    • Milstein, C.1    Cuello, A.C.2
  • 5
    • 0022555989 scopus 로고
    • Bispecific monoclonal antibodies from hybrid hydridomas
    • Suresh, M.R., Cuello, A.C., and Milstein, C. 1986. Bispecific monoclonal antibodies from hybrid hydridomas. Methods Enzymol. 121:210-228.
    • (1986) Methods Enzymol. , vol.121 , pp. 210-228
    • Suresh, M.R.1    Cuello, A.C.2    Milstein, C.3
  • 7
    • 0031552589 scopus 로고    scopus 로고
    • Stable heterodimers from remodeling the domain interface of a homodimer using a phage display library
    • Atwell, S., Ridgway, J.B.B., Wells, J.A., and Carter, P. 1997. Stable heterodimers from remodeling the domain interface of a homodimer using a phage display library. J. Mol. Biol. 270:26-35.
    • (1997) J. Mol. Biol. , vol.270 , pp. 26-35
    • Atwell, S.1    Ridgway, J.B.B.2    Wells, J.A.3    Carter, P.4
  • 9
    • 0021145557 scopus 로고
    • Disulfide bond engineered into T4 lysozyme: Stabilization of the protein toward thermal inactivation
    • Perry, L.J. and Wetzel, R. 1984. Disulfide bond engineered into T4 lysozyme: stabilization of the protein toward thermal inactivation. Science 276:555-557.
    • (1984) Science , vol.276 , pp. 555-557
    • Perry, L.J.1    Wetzel, R.2
  • 10
    • 0022998684 scopus 로고
    • In vivo formation and stability of engineered disulfide bonds in subtilisin
    • Wells, J.A. and Powers, D.P. 1986. In vivo formation and stability of engineered disulfide bonds in subtilisin. J. Biol. Chem. 261:6564-6570.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6564-6570
    • Wells, J.A.1    Powers, D.P.2
  • 11
    • 0028006072 scopus 로고
    • Antibody fragments from a "single pot" phage display library as immunochemical reagents
    • Nissim, A., Hoogenboom, H.R., Tomlinson, I.M., Flynn, G., Midgley, C., Lane, D., and Winter, G. 1994. Antibody fragments from a "single pot" phage display library as immunochemical reagents. EMBO J. 13:692-698.
    • (1994) EMBO J. , vol.13 , pp. 692-698
    • Nissim, A.1    Hoogenboom, H.R.2    Tomlinson, I.M.3    Flynn, G.4    Midgley, C.5    Lane, D.6    Winter, G.7
  • 18
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein a from Staphylococcus aureus at 2.9- and 2.8 Å resolution
    • Deisenhofer, J. 1981. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9-and 2.8 Å resolution. Biochemistry 20:2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 20
    • 0025602626 scopus 로고
    • Protein-protein recognition and the association of immunoglobulin constant domains
    • Miller, S. 1990. Protein-protein recognition and the association of immunoglobulin constant domains. J. Mol. Biol. 216:965-973.
    • (1990) J. Mol. Biol. , vol.216 , pp. 965-973
    • Miller, S.1
  • 21
    • 0027258331 scopus 로고
    • Bispecific receptor globulins, novel tools for the study of cellular interactions. Preparation and characterization of an E-selectin/P-selectin bispecific receptor globulin
    • Dietsch, M.T., Smith, V.F., Cosand, W.L., Damle, N.K., Ledbetter, J.A., Linsley, P.S., and Aruffo, A. 1993. Bispecific receptor globulins, novel tools for the study of cellular interactions. Preparation and characterization of an E-selectin/P-selectin bispecific receptor globulin. J. Immunol. Methods 162:123-132.
    • (1993) J. Immunol. Methods , vol.162 , pp. 123-132
    • Dietsch, M.T.1    Smith, V.F.2    Cosand, W.L.3    Damle, N.K.4    Ledbetter, J.A.5    Linsley, P.S.6    Aruffo, A.7
  • 22
    • 0024204319 scopus 로고
    • Remission induction in non-Hodgkin lymphoma with reshaped human monoclonal antibody CAMPATH-1H
    • Hale, G., Dyer, M.J.S., Clark, M.R., Phillips, J.M., Marcus, R., Riechmann, L. et al. 1988. Remission induction in non-Hodgkin lymphoma with reshaped human monoclonal antibody CAMPATH-1H. Lancet 2:1394-1399.
    • (1988) Lancet , vol.2 , pp. 1394-1399
    • Hale, G.1    Dyer, M.J.S.2    Clark, M.R.3    Phillips, J.M.4    Marcus, R.5    Riechmann, L.6
  • 23
    • 0028231359 scopus 로고
    • A phase 1B trial of humanized monoclonal antibody M195 (anti-CD33) in myeloid leukemia: Specific targeting without immunogenicity
    • Caron, P.C., Juric, J.G., Scott, A.M., Finn, R.D., Divgi, R.D., Graham, M.C. et al. 1994. A phase 1B trial of humanized monoclonal antibody M195 (anti-CD33) in myeloid leukemia: specific targeting without immunogenicity. Blood 83:1760-1768.
    • (1994) Blood , vol.83 , pp. 1760-1768
    • Caron, P.C.1    Juric, J.G.2    Scott, A.M.3    Finn, R.D.4    Divgi, R.D.5    Graham, M.C.6
  • 24
    • 0028786364 scopus 로고
    • Evaluation of a complementarity-determining region-grafted (humanized) anticarcinoembryonic antigen monoclonal antibody in preclinical and clinical studies
    • Sharkey, R.M., Malik, J., Shevitz, J., Behr, T., Dunn, R., Swayne, L.C. et al. 1995. Evaluation of a complementarity-determining region-grafted (humanized) anticarcinoembryonic antigen monoclonal antibody in preclinical and clinical studies. Cancer Res. 55:5935s-5945s.
    • (1995) Cancer Res. , vol.55
    • Sharkey, R.M.1    Malik, J.2    Shevitz, J.3    Behr, T.4    Dunn, R.5    Swayne, L.C.6
  • 27
    • 0031014538 scopus 로고    scopus 로고
    • A phase I trial of humanized anti-interleukin 2 receptor antibody in renal transplantation
    • Vincenti, F., Lantz, M., Birnbaum, J., Garovoy, M., Mould, D., Hakimi, J. et al. 1997. A phase I trial of humanized anti-interleukin 2 receptor antibody in renal transplantation. Transplantation 63:33-38.
    • (1997) Transplantation , vol.63 , pp. 33-38
    • Vincenti, F.1    Lantz, M.2    Birnbaum, J.3    Garovoy, M.4    Mould, D.5    Hakimi, J.6
  • 28
    • 0029564921 scopus 로고
    • CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range
    • Yang, W.-P., Green, K., Pinz-Sweeney, S., Briones, A.T., Burton, D.R, and Barbas, C.F. 1995. CDR walking mutagenesis for the affinity maturation of a potent human anti-HIV-1 antibody into the picomolar range. J. Mol. Biol. 254:392-403.
    • (1995) J. Mol. Biol. , vol.254 , pp. 392-403
    • Yang, W.-P.1    Green, K.2    Pinz-Sweeney, S.3    Briones, A.T.4    Burton, D.R.5    Barbas, C.F.6
  • 29
    • 0030575802 scopus 로고    scopus 로고
    • Isolation of picomolar affinity anti-c-erbB-2 single-chain Fv by molecular evolution of the complementarity determining regions in the center of the antibody binding site
    • Schier, R., McCall, A., Adam, G.P., Marshall, K.W., Merritt, H., Yim M. et al. 1996. Isolation of picomolar affinity anti-c-erbB-2 single-chain Fv by molecular evolution of the complementarity determining regions in the center of the antibody binding site. J. Mol. Biol. 263:551-567.
    • (1996) J. Mol. Biol. , vol.263 , pp. 551-567
    • Schier, R.1    McCall, A.2    Adam, G.P.3    Marshall, K.W.4    Merritt, H.5    Yim, M.6
  • 30
    • 0028338333 scopus 로고
    • In vitro assembly of repertoires of antibody chains on the surface of phage by renaturation
    • Figini, M., Marks, J.D., Winter, G. and Griffiths, A.D. 1994. In vitro assembly of repertoires of antibody chains on the surface of phage by renaturation. J. Mol. Biol. 239:68-78.
    • (1994) J. Mol. Biol. , vol.239 , pp. 68-78
    • Figini, M.1    Marks, J.D.2    Winter, G.3    Griffiths, A.D.4
  • 32
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D., and Zakour, R.A. 1987. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 34
    • 0001789834 scopus 로고
    • Transient production of proteins using an adenovirus transformed cell line
    • Gorman, C.M., Gies, D.R., and McCray, G. 1990. Transient production of proteins using an adenovirus transformed cell line. DNA and Protein Engineering Techniques 2:3-10.
    • (1990) DNA and Protein Engineering Techniques , vol.2 , pp. 3-10
    • Gorman, C.M.1    Gies, D.R.2    McCray, G.3
  • 38
    • 0021712450 scopus 로고
    • Aligning amino acid sequences: Comparison of commonly used methods
    • Feng, D.F. and Doolittle, R.F. 1985. Aligning amino acid sequences: comparison of commonly used methods. J. Mol. Evol. 21:112-123.
    • (1985) J. Mol. Evol. , vol.21 , pp. 112-123
    • Feng, D.F.1    Doolittle, R.F.2
  • 39
    • 0023084055 scopus 로고
    • Progressive alignment as a prerequisite to correct phylogenetic trees
    • Feng, D. F. and Doolittle, R. F. 1987. Progressive alignment as a prerequisite to correct phylogenetic trees. J. Mol. Evol. 25:351-360.
    • (1987) J. Mol. Evol. , vol.25 , pp. 351-360
    • Feng, D.F.1    Doolittle, R.F.2
  • 40
    • 0025025261 scopus 로고
    • Progressive alignment and phylogenetic tree construction of protein sequences
    • Feng, D.F. and Doolittle, R.F. 1990. Progressive alignment and phylogenetic tree construction of protein sequences. Methods Enzymol. 183:375-387.
    • (1990) Methods Enzymol. , vol.183 , pp. 375-387
    • Feng, D.F.1    Doolittle, R.F.2
  • 41
    • 0030803049 scopus 로고    scopus 로고
    • Direct demonstration of MuSK involvement in acetylcholine receptor clustering through identification of agonist ScFv
    • Xie, M.H., Yuan, J., Adams, C., and Gurney, A. 1997. Direct demonstration of MuSK involvement in acetylcholine receptor clustering through identification of agonist ScFv. Nature Biotechnology 15:768-771.
    • (1997) Nature Biotechnology , vol.15 , pp. 768-771
    • Xie, M.H.1    Yuan, J.2    Adams, C.3    Gurney, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.