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Volumn 305, Issue 5, 2001, Pages 989-1010

Stability engineering of antibody single-chain Fv fragments

Author keywords

Antibody engineering; Protein folding; Protein stability; Recombinant antibodies; scFv fragments

Indexed keywords

RECOMBINANT ANTIBODY;

EID: 0035793208     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.4265     Document Type: Review
Times cited : (511)

References (137)
  • 22
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • (1994) Biophys. J. , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 37
    • 0018721964 scopus 로고
    • The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain
    • (1979) J. Biochem. , vol.86 , pp. 1433-1441
    • Goto, Y.1    Hamaguchi, K.2
  • 43
  • 45
    • 0031574037 scopus 로고    scopus 로고
    • Antibody-ribosome-mRNA (ARM), complexes as efficient selection particles for in vitro display and evolution of antibody combining sites
    • (1997) Nucl. Acids Res. , vol.25 , pp. 5132-5134
    • He, M.Y.1    Taussig, M.J.2
  • 60
  • 71
    • 0029294009 scopus 로고
    • Intracellular antibodies (intrabodies) as research reagents and therapeutic molecules for gene therapy
    • (1995) Immunotechnology , vol.1 , pp. 1-19
    • Marasco, W.A.1
  • 72
    • 0033214755 scopus 로고    scopus 로고
    • In vitro folding and thermodynamic stability of an antibody fragment selected in vivo for high expression levels in Escherichia coli cytoplasm
    • (1999) J. Mol. Biol. , vol.292 , pp. 921-929
    • Martineau, P.1    Betton, J.-M.2
  • 80
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • (1986) Methods Enzymol. , vol.131 , pp. 266-290
    • Pace, C.N.1
  • 87
    • 0027008593 scopus 로고
    • Monovalent and bivalent antibody fragments produced in Escherichia coli: Engineering, folding and antigen-binding
    • (1992) Immunolog. Rev. , vol.130 , pp. 151-188
    • Plückthun, A.1
  • 103
    • 0032516802 scopus 로고    scopus 로고
    • A reversibly unfolding fragment of P22 tailspike protein with native structure: The isolated beta-helix domain
    • (1998) J. Mol. Biol. , vol.281 , pp. 227-234
    • Schuler, B.1    Seckler, R.2
  • 113
    • 0028050350 scopus 로고
    • Rapid evolution of a protein in vitro by DNA shuffling
    • (1994) Nature , vol.370 , pp. 389-391
    • Stemmer, W.P.C.1
  • 132
    • 0032524034 scopus 로고    scopus 로고
    • An intrinsically stable antibody scFv fragment can tolerate the loss of both disulfide bonds and fold correctly
    • (1998) FEBS Letters , vol.237 , pp. 357-361
    • Wörn, A.1    Plückthun, A.2
  • 133
    • 0040964401 scopus 로고    scopus 로고
    • Different equilibrium stability behavior of scFv fragments: Identification, classification and improvement by protein engineering
    • (1999) Biochemistry , vol.38 , pp. 8739-8750
    • Wörn, A.1    Plückthun, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.