메뉴 건너뛰기




Volumn 268, Issue 1, 1997, Pages 107-117

Stabilization of a recombinant Fv fragment by base-loop interconnection and V(H)-V(L) permutation

Author keywords

Anti Tac; Antibody engineering; Cancer therapy; dsFv; scFv

Indexed keywords

IMMUNOGLOBULIN FRAGMENT; IMMUNOTOXIN; INTERLEUKIN 2 RECEPTOR ANTIBODY; PSEUDOMONAS EXOTOXIN; RECOMBINANT PROTEIN;

EID: 0031586001     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0850     Document Type: Article
Times cited : (29)

References (33)
  • 3
    • 0028790796 scopus 로고
    • Recombinant immunotoxins: From basic research to cancer therapy
    • Brinkmann U., Pastan I. Recombinant immunotoxins: from basic research to cancer therapy. Methods. 8:1995;143-156.
    • (1995) Methods , vol.8 , pp. 143-156
    • Brinkmann, U.1    Pastan, I.2
  • 4
    • 0026005994 scopus 로고
    • B3(Fv)-PE38KDEL, a single-chain immunotoxin that causes complete regression of a human carcinoma in mice
    • Brinkmann U., Pai L. H., FitzGerald D. J., Willingham M., Pastan I. B3(Fv)-PE38KDEL, a single-chain immunotoxin that causes complete regression of a human carcinoma in mice. Proc. Natl Acad. Sci. USA. 88:1991;8616-8620.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 8616-8620
    • Brinkmann, U.1    Pai, L.H.2    Fitzgerald, D.J.3    Willingham, M.4    Pastan, I.5
  • 6
    • 0026792807 scopus 로고
    • A method to increase the yield of properly folded recombinant fusion proteins: Single-chain immunotoxins from renaturation of bacterial inclusion bodies
    • Buchner J., Pastan I., Brinkmann U. A method to increase the yield of properly folded recombinant fusion proteins: single-chain immunotoxins from renaturation of bacterial inclusion bodies. Anal. Biochem. 205:1992;263-270.
    • (1992) Anal. Biochem. , vol.205 , pp. 263-270
    • Buchner, J.1    Pastan, I.2    Brinkmann, U.3
  • 7
    • 0000449348 scopus 로고
    • Ribbon models of macromolecules
    • Carson M. Ribbon models of macromolecules. J. Mol. Graph. 5:1987;103-106.
    • (1987) J. Mol. Graph , vol.5 , pp. 103-106
    • Carson, M.1
  • 8
    • 0024349836 scopus 로고
    • A recombinant immunotoxin consisting of two antibody variable domains fused to Pseudomonas exotoxin
    • Chaudhary V. K., Queen C., Junghans R. P., Waldmann T. A., FitzGerald D. J., Pastan I. A recombinant immunotoxin consisting of two antibody variable domains fused to Pseudomonas exotoxin. Nature. 339:1989;394-397.
    • (1989) Nature , vol.339 , pp. 394-397
    • Chaudhary, V.K.1    Queen, C.2    Junghans, R.P.3    Waldmann, T.A.4    Fitzgerald, D.J.5    Pastan, I.6
  • 9
    • 0028324575 scopus 로고
    • Structural and dynamic properties of the Fv fragment and the single-chain Fv fragment of an antibody in solution investigated by heteronuclear three-dimensional NMR spectroscopy
    • Freund C., Ross A., Pluckthun A., Holak T. A. Structural and dynamic properties of the Fv fragment and the single-chain Fv fragment of an antibody in solution investigated by heteronuclear three-dimensional NMR spectroscopy. Biochemistry. 33:1994;3296-3303.
    • (1994) Biochemistry , vol.33 , pp. 3296-3303
    • Freund, C.1    Ross, A.2    Pluckthun, A.3    Holak, T.A.4
  • 10
    • 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. 29:1990;1362-1367.
    • (1990) Biochemistry , vol.29 , pp. 1362-1367
    • Glockshuber, R.1    Malia, M.2    Pfitzinger, I.3    Pluckthun, A.4
  • 11
    • 85059706238 scopus 로고
    • Circularly permuted proteins
    • Goldenberg D. P. Circularly permuted proteins. Protein Eng. 2:1989;493-495.
    • (1989) Protein Eng. , vol.2 , pp. 493-495
    • Goldenberg, D.P.1
  • 12
    • 0021095334 scopus 로고
    • Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor
    • Goldenberg D. P., Creighton T. E. Circular and circularly permuted forms of bovine pancreatic trypsin inhibitor. J. Mol. Biol. 165:1983;407-413.
    • (1983) J. Mol. Biol. , vol.165 , pp. 407-413
    • Goldenberg, D.P.1    Creighton, T.E.2
  • 14
    • 0023657391 scopus 로고
    • Functional domains of Pseudomonas exotoxin identified by deletion analysis of the gene expressed in E. coli
    • Hwang J., FitzGerald D. J., Adhya S., Pastan I. Functional domains of Pseudomonas exotoxin identified by deletion analysis of the gene expressed in E. coli. Cell. 48:1987;129-136.
    • (1987) Cell , vol.48 , pp. 129-136
    • Hwang, J.1    Fitzgerald, D.J.2    Adhya, S.3    Pastan, I.4
  • 16
    • 0028057249 scopus 로고
    • Recombinant immunotoxins containing anti-Tac(Fv) and derivatives of Pseudomonas exotoxin produce complete regression in mice of an interleukin-2 receptor-expressing human carcinoma
    • Kreitman R. J., Bailon P., Chaudhary V. K., FitzGerald D. J., Pastan I. Recombinant immunotoxins containing anti-Tac(Fv) and derivatives of Pseudomonas exotoxin produce complete regression in mice of an interleukin-2 receptor-expressing human carcinoma. Blood. 83:1994;426-434.
    • (1994) Blood , vol.83 , pp. 426-434
    • Kreitman, R.J.1    Bailon, P.2    Chaudhary, V.K.3    Fitzgerald, D.J.4    Pastan, I.5
  • 17
    • 0024490818 scopus 로고
    • Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo
    • Luger K., Hommel U., Herold M., Hofsteenge J., Kirschner K. Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo. Science. 243:1989;206-210.
    • (1989) Science , vol.243 , pp. 206-210
    • Luger, K.1    Hommel, U.2    Herold, M.3    Hofsteenge, J.4    Kirschner, K.5
  • 19
    • 0028285899 scopus 로고
    • Improved binding and anti tumor activity of a recombinant anti-erbB2 immunotoxin by disulfide-stabilization of the Fv fragment
    • Reiter Y., Brinkmann U., Jung S.-H., Lee B., Kasprzyk P. G., King C. R., Pastan I. Improved binding and anti tumor activity of a recombinant anti-erbB2 immunotoxin by disulfide-stabilization of the Fv fragment. J. Biol. Chem. 269:1994a;18327-18331.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18327-18331
    • Reiter, Y.1    Brinkmann, U.2    Jung, S.-H.3    Lee, B.4    Kasprzyk, P.G.5    King, C.R.6    Pastan, I.7
  • 20
    • 0028216376 scopus 로고
    • Engineering disulfide bonds into conserved framework regions of Fv fragments: Recombinant immunotoxins containing disulfide-stabilized Fv with improved biochemical characteristics
    • Reiter Y., Brinkmann U., Jung S.-H., Lee B., Pastan I. Engineering disulfide bonds into conserved framework regions of Fv fragments: recombinant immunotoxins containing disulfide-stabilized Fv with improved biochemical characteristics. Protein Eng. 7:1994b;697-704.
    • (1994) Protein Eng. , vol.7 , pp. 697-704
    • Reiter, Y.1    Brinkmann, U.2    Jung, S.-H.3    Lee, B.4    Pastan, I.5
  • 21
    • 0028287925 scopus 로고
    • Cytotoxic and antitumor activity of a recombinant immunotoxin composed of disulfide-stabilized anti-Tac Fv fragment and truncated Pseudomonas exotoxin
    • Reiter Y., Kreitman R. J., Brinkmann U., Pastan I. Cytotoxic and antitumor activity of a recombinant immunotoxin composed of disulfide-stabilized anti-Tac Fv fragment and truncated Pseudomonas exotoxin. Int. J. Cancer. 58:1994c;142-149.
    • (1994) Int. J. Cancer , vol.58 , pp. 142-149
    • Reiter, Y.1    Kreitman, R.J.2    Brinkmann, U.3    Pastan, I.4
  • 22
    • 0029766875 scopus 로고    scopus 로고
    • Engineering antibody Fv fragments for cancer detection and therapy: Disulfide-stabilized Fv fragments
    • Reiter Y., Brinkmann U., Lee B., Pastan I. Engineering antibody Fv fragments for cancer detection and therapy: disulfide-stabilized Fv fragments. Nature/Biotechnology. 14:1996;1239-1245.
    • (1996) Nature/Biotechnology , vol.14 , pp. 1239-1245
    • Reiter, Y.1    Brinkmann, U.2    Lee, B.3    Pastan, I.4
  • 23
    • 0026587998 scopus 로고
    • Structural evidence for induced fit as a mechanism for antibody-antigen recognition
    • Rini J. M., Schulze-Gahmen U., Wilson I. A. Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Science. 255:1992;959-965.
    • (1992) Science , vol.255 , pp. 959-965
    • Rini, J.M.1    Schulze-Gahmen, U.2    Wilson, I.A.3
  • 24
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R., Lilie H. In vitro folding of inclusion body proteins. FASEB J. 10:1996;49-56.
    • (1996) FASEB J. , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 26
    • 0024292736 scopus 로고
    • Assembly of a functional immunoglobulin Fv fragment in Escherichia coli
    • Skerra A., Pluckthun A. Assembly of a functional immunoglobulin Fv fragment in Escherichia coli. Science. 240:1988;1038-1041.
    • (1988) Science , vol.240 , pp. 1038-1041
    • Skerra, A.1    Pluckthun, A.2
  • 27
    • 0028470793 scopus 로고
    • Antigen-induced conformational changes in antibodies: A problem for structural prediction and design
    • Stanfield R. L., Wilson I. A. Antigen-induced conformational changes in antibodies: a problem for structural prediction and design. Trends Biotech. 12:1994;275-279.
    • (1994) Trends Biotech , vol.12 , pp. 275-279
    • Stanfield, R.L.1    Wilson, I.A.2
  • 28
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F. W., Moffatt B. A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:1986;113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 29
    • 0019421207 scopus 로고
    • A monoclonal antibody (anti-Tac) reactive with activated and functionally mature human T cells. I. Production of anti-Tac monoclonal antibody and distribution of Tac (+) cells
    • Uchiyama T., Broder S., Waldmann T. A. A monoclonal antibody (anti-Tac) reactive with activated and functionally mature human T cells. I. Production of anti-Tac monoclonal antibody and distribution of Tac (+) cells. J. Immunol. 4:1981;1393-1397.
    • (1981) J. Immunol. , vol.4 , pp. 1393-1397
    • Uchiyama, T.1    Broder, S.2    Waldmann, T.A.3
  • 30
    • 0342699417 scopus 로고
    • TCR recognition of the MHC-peptide dimer: Structural properties of a ternary complex
    • Vasmatzis G., Cornette J., Sezerman U., DeLisi C. TCR recognition of the MHC-peptide dimer: structural properties of a ternary complex. J. Mol. Biol. 261:1995;72-89.
    • (1995) J. Mol. Biol. , vol.261 , pp. 72-89
    • Vasmatzis, G.1    Cornette, J.2    Sezerman, U.3    Delisi, C.4
  • 31
    • 0028951128 scopus 로고
    • Preparation and characterization of a disulfide-stabilized Fv fragment of the anti-Tac antibody: Comparison with its single-chain analog
    • Webber K. O., Reiter Y., Brinkmann U., Kreitman R. J., Pastan I. Preparation and characterization of a disulfide-stabilized Fv fragment of the anti-Tac antibody: comparison with its single-chain analog. Mol. Immunol. 4:1995;249-258.
    • (1995) Mol. Immunol. , vol.4 , pp. 249-258
    • Webber, K.O.1    Reiter, Y.2    Brinkmann, U.3    Kreitman, R.J.4    Pastan, I.5
  • 32
    • 0027143219 scopus 로고
    • Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains
    • Yang Y. R., Schachman H. K. Aspartate transcarbamoylase containing circularly permuted catalytic polypeptide chains. Proc. Natl Acad. Sci. USA. 90:1993;11980-11984.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 11980-11984
    • Yang, Y.R.1    Schachman, H.K.2
  • 33
    • 0026684815 scopus 로고
    • Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms
    • Yokota T., Milenic D. E., Whitlow M., Schlom J. Rapid tumor penetration of a single-chain Fv and comparison with other immunoglobulin forms. Cancer Res. 52:1992;3402-3408.
    • (1992) Cancer Res. , vol.52 , pp. 3402-3408
    • Yokota, T.1    Milenic, D.E.2    Whitlow, M.3    Schlom, J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.