메뉴 건너뛰기




Volumn 46, Issue 2, 2006, Pages 495-502

Expression, purification, and in vitro refolding of a humanized single-chain Fv antibody against human CTLA4 (CD152)

Author keywords

Bacterial expression; CTLA4; In vitro refolding; Single chain Fv antibody

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 33645420672     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2005.09.002     Document Type: Article
Times cited : (34)

References (27)
  • 2
    • 0032931973 scopus 로고    scopus 로고
    • Costimulatory regulation of T cell function
    • C.A. Chambers, and J.P. Allison Costimulatory regulation of T cell function Curr. Opin. Cell Biol. 11 1999 203 210
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 203-210
    • Chambers, C.A.1    Allison, J.P.2
  • 3
    • 0033770215 scopus 로고    scopus 로고
    • CD28, CTLA-4 and their ligand: Who does what and to whom?
    • D.M. Samson CD28, CTLA-4 and their ligand: who does what and to whom? Immunology 101 2000 169
    • (2000) Immunology , vol.101 , pp. 169
    • Samson, D.M.1
  • 6
    • 0031154577 scopus 로고    scopus 로고
    • CTLA-4-Ig prevents lymphoproliferation and fatal multiorgan tissue destruction in CTLA-4 deficient mice
    • E.A. Tivol, S.D. Boyd, S.M. Keon, F. Borriello, P. Nickerson, T.B. Strom, and A.H. Sharpe CTLA-4-Ig prevents lymphoproliferation and fatal multiorgan tissue destruction in CTLA-4 deficient mice J. Immunol. 158 1997 5091
    • (1997) J. Immunol. , vol.158 , pp. 5091
    • Tivol, E.A.1    Boyd, S.D.2    Keon, S.M.3    Borriello, F.4    Nickerson, P.5    Strom, T.B.6    Sharpe, A.H.7
  • 9
    • 0034830739 scopus 로고    scopus 로고
    • Dimeric and trimeric antibodies: High avidity scFvs for cancer targeting
    • A.A. Kortt, Q. Dolezal, B.E. Power, and P.J. Hudson Dimeric and trimeric antibodies: high avidity scFvs for cancer targeting Biomol. Eng. 18 2001 98 108
    • (2001) Biomol. Eng. , vol.18 , pp. 98-108
    • Kortt, A.A.1    Dolezal, Q.2    Power, B.E.3    Hudson, P.J.4
  • 10
    • 0035251612 scopus 로고    scopus 로고
    • Antibody-cytokine fusion proteins for the therapy of cancer
    • M.L. Penichet, and S.L. Morrison Antibody-cytokine fusion proteins for the therapy of cancer J. Immunol. Methods 248 2001 91 101
    • (2001) J. Immunol. Methods , vol.248 , pp. 91-101
    • Penichet, M.L.1    Morrison, S.L.2
  • 12
    • 0032122306 scopus 로고    scopus 로고
    • Antibody engineering: Comparison of bacterial, yeast, insect and mammalian expression systems
    • R. Verma, E. Boleti, and A.J.T. George Antibody engineering: comparison of bacterial, yeast, insect and mammalian expression systems J. Immunol. Methods 216 1998 165 181
    • (1998) J. Immunol. Methods , vol.216 , pp. 165-181
    • Verma, R.1    Boleti, E.2    George, A.J.T.3
  • 13
    • 0034093483 scopus 로고    scopus 로고
    • Molecular characterization and applications of recombinant scFv antibodies to CD152 co-stimulatory molecule
    • M.P. Pistillo, P.L. Tazzari, J.H. Ellis, and G.B. Ferrara Molecular characterization and applications of recombinant scFv antibodies to CD152 co-stimulatory molecule Tissue Antigens 55 2000 229 238
    • (2000) Tissue Antigens , vol.55 , pp. 229-238
    • Pistillo, M.P.1    Tazzari, P.L.2    Ellis, J.H.3    Ferrara, G.B.4
  • 14
    • 0024296631 scopus 로고
    • A rapid and convenient method for the preparation and storage of competent bacterial cells
    • C.T. Chung, and R.H. Niller A rapid and convenient method for the preparation and storage of competent bacterial cells Nucleic Acids Res. 16 1988 3580
    • (1988) Nucleic Acids Res. , vol.16 , pp. 3580
    • Chung, C.T.1    Niller, R.H.2
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0035109511 scopus 로고    scopus 로고
    • Purification, refolding of hybrid hIFN-Kringle 5 expressed in Escherichia coli
    • H. Lu, H. Zhang, Q. Wang, H. Yuan, W. He, Z. Zhao, and Y. Li Purification, refolding of hybrid hIFN-Kringle 5 expressed in Escherichia coli Curr. Microbiol. 42 2001 211 216
    • (2001) Curr. Microbiol. , vol.42 , pp. 211-216
    • Lu, H.1    Zhang, H.2    Wang, Q.3    Yuan, H.4    He, W.5    Zhao, Z.6    Li, Y.7
  • 19
    • 0028966985 scopus 로고
    • Engineered turns of a recombinant antibody improve its in vivo folding
    • A. Knappik, and A. Pluckthun Engineered turns of a recombinant antibody improve its in vivo folding Protein Eng. 8 1995 81 89
    • (1995) Protein Eng. , vol.8 , pp. 81-89
    • Knappik, A.1    Pluckthun, A.2
  • 20
    • 0022036755 scopus 로고
    • Examination of calf prochymotrypsin accumulation in Escherichia coli: Disulfide linkages are a structural component of prochymotrypsin-containing inclusion bodies
    • J.M. Schoemaker, A.H. Brasnett, and F.A.O. Marstion Examination of calf prochymotrypsin accumulation in Escherichia coli: disulfide linkages are a structural component of prochymotrypsin-containing inclusion bodies EMBOJ 4 1985 775 780
    • (1985) EMBOJ , vol.4 , pp. 775-780
    • Schoemaker, J.M.1    Brasnett, A.H.2    Marstion, F.A.O.3
  • 21
    • 0006454079 scopus 로고
    • Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli
    • J. Buchner, and R. Rudolph Renaturation, purification and characterization of recombinant Fab-fragments produced in Escherichia coli Biotechnology 9 1991 157 162
    • (1991) Biotechnology , vol.9 , pp. 157-162
    • Buchner, J.1    Rudolph, R.2
  • 22
    • 0026792807 scopus 로고
    • A method for increasing the yield of properly folded recombinant fusion proteins: Single chain immunotoxins from renaturation of bacterial inclusion bodies
    • J. Buchner, I. Pastan, and U. Brinkmann A method for increasing 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
  • 23
    • 0027908939 scopus 로고
    • Isolation, renaturation, and formation of disulfide bonds of eucaryotic proteins expressed in E. coli as inclusion bodies
    • B. Fisher, I. Sumner, and P. Goodenough Isolation, renaturation, and formation of disulfide bonds of eucaryotic proteins expressed in E. coli as inclusion bodies Biotechnol. Bioeng. 41 1992 3 13
    • (1992) Biotechnol. Bioeng. , vol.41 , pp. 3-13
    • Fisher, B.1    Sumner, I.2    Goodenough, P.3
  • 25
    • 1842410676 scopus 로고    scopus 로고
    • Oxidative renaturation of lysozyme at high concentrations
    • D.L. Hevehan, and E.D.B. Clark Oxidative renaturation of lysozyme at high concentrations Biotechnol. Bioeng. 54 1997 221 230
    • (1997) Biotechnol. Bioeng. , vol.54 , pp. 221-230
    • Hevehan, D.L.1    Clark, E.D.B.2
  • 26
    • 0023290034 scopus 로고
    • The oxidative folding of proteins by disulfide plus thiol does not correlate with redox potential
    • D.B. Wetlaufer, P.A. Branca, and G. Chen The oxidative folding of proteins by disulfide plus thiol does not correlate with redox potential Protein Eng. 1 1987 141 146
    • (1987) Protein Eng. , vol.1 , pp. 141-146
    • Wetlaufer, D.B.1    Branca, P.A.2    Chen, G.3
  • 27
    • 0029916225 scopus 로고    scopus 로고
    • Control of aggregation in protein refolding: The temperature-leap tactic
    • Y. Xie, and D.B. Wetlaufer Control of aggregation in protein refolding: the temperature-leap tactic Protein Sci. 5 1996 517 523
    • (1996) Protein Sci. , vol.5 , pp. 517-523
    • Xie, Y.1    Wetlaufer, D.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.