메뉴 건너뛰기




Volumn 270, Issue 1, 1997, Pages 26-35

Stable heterodimers from remodeling the domain interface of a homodimer using a phage display library

Author keywords

Antibody C(H)3 domains; Bispecific antibody; Domain interface engineering; Heterodimer; Phage display

Indexed keywords

ADHESIN; ANTIBODY; DIMER; GUANIDINE; HYBRID PROTEIN; MUTANT PROTEIN; THREONINE; TRYPTOPHAN;

EID: 0031552589     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1116     Document Type: Article
Times cited : (219)

References (45)
  • 3
    • 0025678186 scopus 로고
    • Hormone phage: An enrichment method for variant proteins with altered binding properties
    • Bass S., Greene R., Wells J. A. Hormone phage: an enrichment method for variant proteins with altered binding properties. Proteins: Struct. Funct. Genet. 8:1990;309-314.
    • (1990) Proteins: Struct. Funct. Genet. , vol.8 , pp. 309-314
    • Bass, S.1    Greene, R.2    Wells, J.A.3
  • 4
    • 0022447254 scopus 로고
    • A model of synthetase/transfer RNA interaction as deduced by protein engineering
    • Bedouelle H., Winter G. A model of synthetase/transfer RNA interaction as deduced by protein engineering. Nature. 320:1986;371-373.
    • (1986) Nature , vol.320 , pp. 371-373
    • Bedouelle, H.1    Winter, G.2
  • 6
    • 0021990138 scopus 로고
    • Protection from genital herpes simplex virus type 2 infection by vaccination with cloned type 1 glycoprotein D
    • Berman P. W., Gregory T., Crase D., Lasky L. A. Protection from genital herpes simplex virus type 2 infection by vaccination with cloned type 1 glycoprotein D. Science. 227:1985;1490-1492.
    • (1985) Science , vol.227 , pp. 1490-1492
    • Berman, P.W.1    Gregory, T.2    Crase, D.3    Lasky, L.A.4
  • 7
    • 0027958903 scopus 로고
    • Electrospray ionization mass spectrometry of recombinantly engineered antibody fragments
    • Bourell J. H., Clauser K. P., Kelley R., Carter P., Stults J. T. Electrospray ionization mass spectrometry of recombinantly engineered antibody fragments. Anal. Chem. 66:1994;2088-2095.
    • (1994) Anal. Chem. , vol.66 , pp. 2088-2095
    • Bourell, J.H.1    Clauser, K.P.2    Kelley, R.3    Carter, P.4    Stults, J.T.5
  • 9
    • 0011154916 scopus 로고
    • Mutagenesis facilitated by the removal or introduction of unique restriction sites
    • Oxford: IRL
    • Carter P. Mutagenesis facilitated by the removal or introduction of unique restriction sites. Mutagenesis: A Practical Approach. 1991;IRL, Oxford.
    • (1991) Mutagenesis: A Practical Approach
    • Carter, P.1
  • 13
    • 0028786757 scopus 로고
    • Toward the production of bispecific antibody fragments for clinical applications
    • Carter P., Ridgway J., Zhu Z. Toward the production of bispecific antibody fragments for clinical applications. J. Hematother. 4:1995;463-470.
    • (1995) J. Hematother. , vol.4 , pp. 463-470
    • Carter, P.1    Ridgway, J.2    Zhu, Z.3
  • 15
    • 0022446237 scopus 로고
    • Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli
    • Chang C. N., Kuang W.-J., Chen E. Y. Nucleotide sequence of the alkaline phosphatase gene of Escherichia coli. Gene. 44:1986;121-125.
    • (1986) Gene , vol.44 , pp. 121-125
    • Chang, C.N.1    Kuang, W.-J.2    Chen, E.Y.3
  • 16
    • 0004140795 scopus 로고
    • Proteins: Structure and Molecular Properties
    • New York: Freeman
    • Creighton T. E. Proteins: Structure and Molecular Properties. 2nd edit. 1993;Freeman, New York.
    • (1993) 2nd edit.
    • Creighton, T.E.1
  • 17
    • 0019522383 scopus 로고
    • Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A fromStaphylococcus aureus at 2.9- and 2.8 Å resolution
    • Deisenhofer J. Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A fromStaphylococcus aureus at 2.9- and 2.8 Å resolution. Biochemistry. 20:1981;2361-2370.
    • (1981) Biochemistry , vol.20 , pp. 2361-2370
    • Deisenhofer, J.1
  • 18
    • 0026535482 scopus 로고
    • Engineering surface charge. 2. A method for purifying heterodimers of Escherichia coli gluathione reductase
    • Deonarain M. P., Scrutton N. S., Perham R. N. Engineering surface charge. 2. A method for purifying heterodimers of Escherichia coli gluathione reductase. Biochemistry. 31:1992;1498-1504.
    • (1992) Biochemistry , vol.31 , pp. 1498-1504
    • Deonarain, M.P.1    Scrutton, N.S.2    Perham, R.N.3
  • 21
    • 0029903942 scopus 로고    scopus 로고
    • Heterodimer formation and activity in the human enzyme galactose-1-phosphate uridylyltransferase
    • Elsevier J. P., Wells L., Quimby B. B., Fridovich-Keil J. L. Heterodimer formation and activity in the human enzyme galactose-1-phosphate uridylyltransferase. Proc. Natl Acad. Sci. USA. 93:1996;7166-7171.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 7166-7171
    • Elsevier, J.P.1    Wells, L.2    Quimby, B.B.3    Fridovich-Keil, J.L.4
  • 22
    • 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., Griffiths A. D. In vitro assembly of repertoires of antibody chains on the surface of phage by renaturation. J. Mol. Biol. 239:1994;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
  • 26
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel T. A., Roberts J. D., Zakour R. A. Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 154:1987;367-382.
    • (1987) Methods Enzymol. , vol.154 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 27
    • 0021191322 scopus 로고
    • DNA sequence analysis of the type-common glycoprotein-D genes of herpes simplex virus types 1 and 2
    • Lasky L. A., Dowbenko D. J. DNA sequence analysis of the type-common glycoprotein-D genes of herpes simplex virus types 1 and 2. DNA. 3:1984;23-29.
    • (1984) DNA , vol.3 , pp. 23-29
    • Lasky, L.A.1    Dowbenko, D.J.2
  • 29
    • 0026343486 scopus 로고
    • Selecting high-affinity binding proteins by monovalent phage display
    • Lowman H. B., Bass S. H., Simpson N., Wells J. A. Selecting high-affinity binding proteins by monovalent phage display. Biochemistry. 30:1991;10832-10838.
    • (1991) Biochemistry , vol.30 , pp. 10832-10838
    • Lowman, H.B.1    Bass, S.H.2    Simpson, N.3    Wells, J.A.4
  • 30
    • 0023868449 scopus 로고
    • An RNA secondary structure workbench
    • Martinez H. M. An RNA secondary structure workbench. Nucl. Acids Res. 16:1988;1789-1798.
    • (1988) Nucl. Acids Res. , vol.16 , pp. 1789-1798
    • Martinez, H.M.1
  • 31
    • 0029966228 scopus 로고    scopus 로고
    • Engineering human immunodeficiency virus 1 protease heterodimers as macromolecular inhibitors of viral maturation
    • McPhee F., Good A. C., Kuntz I. D., Craik C. S. Engineering human immunodeficiency virus 1 protease heterodimers as macromolecular inhibitors of viral maturation. Proc. Natl Acad. Sci. USA. 93:1996;11477-11481.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 11477-11481
    • McPhee, F.1    Good, A.C.2    Kuntz, I.D.3    Craik, C.S.4
  • 32
    • 0025602626 scopus 로고
    • Protein-protein recognition and the association of immunoglobulin constant domains
    • Miller S. Protein-protein recognition and the association of immunoglobulin constant domains. J. Mol. Biol. 216:1990;965-973.
    • (1990) J. Mol. Biol. , vol.216 , pp. 965-973
    • Miller, S.1
  • 33
    • 0024210147 scopus 로고
    • Antibody-selectable filamentous fd phage vectors: Affinity purification of target genes
    • Parmley S. F., Smith G. P. Antibody-selectable filamentous fd phage vectors: affinity purification of target genes. Gene. 73:1988;305-318.
    • (1988) Gene , vol.73 , pp. 305-318
    • Parmley, S.F.1    Smith, G.P.2
  • 34
    • 0020544827 scopus 로고
    • Nucleotide sequence of the gene for heat-stable enterotoxin II of Escherichia coli
    • Picken R. N., Mazaitis A. J., Maas W. K., Rey M., Heyneker H. Nucleotide sequence of the gene for heat-stable enterotoxin II of Escherichia coli. Infect. Immun. 42:1983;269-275.
    • (1983) Infect. Immun. , vol.42 , pp. 269-275
    • Picken, R.N.1    Mazaitis, A.J.2    Maas, W.K.3    Rey, M.4    Heyneker, H.5
  • 36
    • 0342416705 scopus 로고
    • Regeneration of active enzyme by formation of hybrids from inactive derivatives: Implication for active sites shared between polypeptide chains of aspartate transcarbamoylase
    • Robey E. A., Schachman H. K. Regeneration of active enzyme by formation of hybrids from inactive derivatives: implication for active sites shared between polypeptide chains of aspartate transcarbamoylase. Proc. Natl Acad. Sci. USA. 82:1985;361-365.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 361-365
    • Robey, E.A.1    Schachman, H.K.2
  • 40
    • 0026604793 scopus 로고
    • Development of humanized bispecific antibodies reactive with cytotoxic lymphocytes and tumor cells overexpressing theHER2 protooncogene
    • Shalaby M. R., Shepard H. M., Presta L., Rodrigues M. L., Beverley P. C. L., Feldmann M., Carter P. Development of humanized bispecific antibodies reactive with cytotoxic lymphocytes and tumor cells overexpressing theHER2 protooncogene. J. Exp. Med. 175:1992;217-225.
    • (1992) J. Exp. Med. , vol.175 , pp. 217-225
    • Shalaby, M.R.1    Shepard, H.M.2    Presta, L.3    Rodrigues, M.L.4    Beverley, P.C.L.5    Feldmann, M.6    Carter, P.7
  • 41
    • 0021818675 scopus 로고
    • Filamentous fusion phage: Novel expression vectors that display cloned antigens on the virion surface
    • Smith G. P. 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
  • 42
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • Vieira J., Messing J. Production of single-stranded plasmid DNA. Methods Enzymol. 153:1987;3-11.
    • (1987) Methods Enzymol. , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2
  • 43
    • 0023668284 scopus 로고
    • Effects of engineering complementarity charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase
    • Ward W. H. J., Jones D. H., Fersht A. R. Effects of engineering complementarity charged residues into the hydrophobic subunit interface of tyrosyl-tRNA synthetase. Biochemistry. 26:1987;4131-4138.
    • (1987) Biochemistry , vol.26 , pp. 4131-4138
    • Ward, W.H.J.1    Jones, D.H.2    Fersht, A.R.3
  • 44
    • 0008697435 scopus 로고
    • Shared active sites in oligomeric enzymes: Model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis
    • Wente S., Schachman H. K. Shared active sites in oligomeric enzymes: model studies with defective mutants of aspartate transcarbamoylase produced by site-directed mutagenesis. Proc. Natl Acad. Sci. USA. 84:1987;31-35.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 31-35
    • Wente, S.1    Schachman, H.K.2
  • 45
    • 0030909820 scopus 로고    scopus 로고
    • Remodeling domain interfaces to enhance heterodimer formation
    • Zhu Z., Presta L. G., Zapata G., Carter P. Remodeling domain interfaces to enhance heterodimer formation. Protein Sci. 6:1997;781-788.
    • (1997) Protein Sci. , vol.6 , pp. 781-788
    • Zhu, Z.1    Presta, L.G.2    Zapata, G.3    Carter, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.