메뉴 건너뛰기




Volumn 477, Issue , 2015, Pages 56-61

Improved Fab presentation on phage surface with the use of molecular chaperone coplasmid system

Author keywords

Antibody phage display; Coplasmid; Fab presentation; Molecular chaperone

Indexed keywords

CHAPERONE; IMMUNOGLOBULIN D; IMMUNOGLOBULIN F(AB) FRAGMENT; IMMUNOGLOBULIN G; IMMUNOGLOBULIN KAPPA CHAIN; PEPTIDE LIBRARY; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY;

EID: 84963984836     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2015.02.026     Document Type: Article
Times cited : (7)

References (24)
  • 1
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: Methodologies for displaying antibody (Fab) heavy and light chains
    • H.R. Hoogenboom, A.D. Griffiths, K.S. Johnson, D.J. Chiswell, P. Hudson, and G. Winter Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains Nucleic Acids Res. 19 1991 4133 4137
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 2
    • 0025838021 scopus 로고
    • Assembly of combinatorial antibody libraries on phage surfaces: The gene III site
    • C.F. Barbas, A.S. Kang, R.A. Lerner, and S.J. Benkovic Assembly of combinatorial antibody libraries on phage surfaces: the gene III site Proc. Natl. Acad. Sci. U.S.A. 88 1991 7978 7982
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 7978-7982
    • Barbas, C.F.1    Kang, A.S.2    Lerner, R.A.3    Benkovic, S.J.4
  • 3
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • D. Missiakas, and S. Raina Protein folding in the bacterial periplasm J. Bacteriol. 179 1997 2465
    • (1997) J. Bacteriol. , vol.179 , pp. 2465
    • Missiakas, D.1    Raina, S.2
  • 4
    • 33745931632 scopus 로고    scopus 로고
    • A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli
    • M. Schlapschy, S. Grimm, and A. Skerra A system for concomitant overexpression of four periplasmic folding catalysts to improve secretory protein production in Escherichia coli Protein Eng. Des. Sel. 19 2006 385 390
    • (2006) Protein Eng. Des. Sel. , vol.19 , pp. 385-390
    • Schlapschy, M.1    Grimm, S.2    Skerra, A.3
  • 5
    • 0028215226 scopus 로고
    • Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity
    • V.E. Shevchik, G. Condemine, and J. Robert-Baudouy Characterization of DsbC, a periplasmic protein of Erwinia chrysanthemi and Escherichia coli with disulfide isomerase activity EMBO J. 13 1994 2007
    • (1994) EMBO J. , vol.13 , pp. 2007
    • Shevchik, V.E.1    Condemine, G.2    Robert-Baudouy, J.3
  • 6
    • 79952473873 scopus 로고    scopus 로고
    • Periplasmic chaperones used to enhance functional secretion of proteins in E. Coli
    • M. Schlapschy, and A. Skerra Periplasmic chaperones used to enhance functional secretion of proteins in E. coli Methods Mol. Biol. 705 2011 211 224
    • (2011) Methods Mol. Biol. , vol.705 , pp. 211-224
    • Schlapschy, M.1    Skerra, A.2
  • 8
    • 0036224573 scopus 로고    scopus 로고
    • Oxidative protein folding in bacteria
    • J.F. Collet, and J.C. Bardwell Oxidative protein folding in bacteria Mol. Microbiol. 44 2002 1 8
    • (2002) Mol. Microbiol. , vol.44 , pp. 1-8
    • Collet, J.F.1    Bardwell, J.C.2
  • 9
    • 8844270875 scopus 로고    scopus 로고
    • Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm
    • H. Nakamoto, and J.C.A. Bardwell Catalysis of disulfide bond formation and isomerization in the Escherichia coli periplasm Biochim. Biophys. Acta 1694 2004 111 119
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 111-119
    • Nakamoto, H.1    Bardwell, J.C.A.2
  • 11
    • 8844237557 scopus 로고    scopus 로고
    • Quality control in the bacterial periplasm
    • A.R. Duguay, and T.J. Silhavy Quality control in the bacterial periplasm Biochim. Biophys. Acta 1694 2004 121 134
    • (2004) Biochim. Biophys. Acta , vol.1694 , pp. 121-134
    • Duguay, A.R.1    Silhavy, T.J.2
  • 12
    • 2942622465 scopus 로고    scopus 로고
    • Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins
    • E. Bitto, and D.B. McKay Binding of phage-display-selected peptides to the periplasmic chaperone protein SurA mimics binding of unfolded outer membrane proteins FEBS Lett. 568 2004 94 98
    • (2004) FEBS Lett. , vol.568 , pp. 94-98
    • Bitto, E.1    McKay, D.B.2
  • 13
    • 21244447713 scopus 로고    scopus 로고
    • The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition
    • G. Hennecke, J. Nolte, R. Volkmer-Engert, J. Schneider-Mergener, and S. Behrens The periplasmic chaperone SurA exploits two features characteristic of integral outer membrane proteins for selective substrate recognition J. Biol. Chem. 280 2005 23540 23548
    • (2005) J. Biol. Chem. , vol.280 , pp. 23540-23548
    • Hennecke, G.1    Nolte, J.2    Volkmer-Engert, R.3    Schneider-Mergener, J.4    Behrens, S.5
  • 14
    • 34948827356 scopus 로고    scopus 로고
    • Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli
    • J.G. Sklar, T. Wu, D. Kahne, and T.J. Silhavy Defining the roles of the periplasmic chaperones SurA, Skp, and DegP in Escherichia coli Genes Dev. 21 2007 2473 2484
    • (2007) Genes Dev. , vol.21 , pp. 2473-2484
    • Sklar, J.G.1    Wu, T.2    Kahne, D.3    Silhavy, T.J.4
  • 16
    • 25144489575 scopus 로고    scopus 로고
    • Semi-extended solution structure of human myeloma immunoglobulin D determined by constrained X-ray scattering
    • Z. Sun, A. Almogren, P.B. Furtado, B. Chowdhury, M.A. Kerr, and S.J. Perkins Semi-extended solution structure of human myeloma immunoglobulin D determined by constrained X-ray scattering J. Mol. Biol. 353 2005 155 173
    • (2005) J. Mol. Biol. , vol.353 , pp. 155-173
    • Sun, Z.1    Almogren, A.2    Furtado, P.B.3    Chowdhury, B.4    Kerr, M.A.5    Perkins, S.J.6
  • 17
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • A. Sali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 18
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J.D. Thompson, D.G. Higgins, and T.J. Gibson CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucleic Acids Res. 22 1994 4673 4680
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 20
    • 14844339334 scopus 로고    scopus 로고
    • Domain interactions in the Fab fragment: A comparative evaluation of the single-chain Fv and Fab format engineered with variable domains of different stability
    • D. Röthlisberger, A. Honegger, and A. Plückthun Domain interactions in the Fab fragment: a comparative evaluation of the single-chain Fv and Fab format engineered with variable domains of different stability J. Mol. Biol. 347 2005 773 789
    • (2005) J. Mol. Biol. , vol.347 , pp. 773-789
    • Röthlisberger, D.1    Honegger, A.2    Plückthun, A.3
  • 23
    • 0034887457 scopus 로고    scopus 로고
    • Engineering M13 for phage display
    • S.S. Sidhu Engineering M13 for phage display Biomol. Eng. 18 2001 57 63
    • (2001) Biomol. Eng. , vol.18 , pp. 57-63
    • Sidhu, S.S.1
  • 24
    • 0039423955 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis, trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines
    • H. Bothmann, and A. Plückthun The periplasmic Escherichia coli peptidylprolyl cis, trans-isomerase FkpA. I. Increased functional expression of antibody fragments with and without cis-prolines J. Biol. Chem. 275 2000 17100 17105
    • (2000) J. Biol. Chem. , vol.275 , pp. 17100-17105
    • Bothmann, H.1    Plückthun, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.