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Volumn 89, Issue 2, 2013, Pages 169-174

Overproduction of a C5a receptor antagonist (C5aRA) in Escherichia coli

Author keywords

Batch fermentation; C5aR antagonist; Escherichia coli; NusA

Indexed keywords

COMPLEMENT COMPONENT C5A RECEPTOR; ELONGATION FACTOR; ESCHERICHIA COLI PROTEIN; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; NUSA PROTEIN, E COLI; THIOREDOXIN; TRANSCRIPTION FACTOR;

EID: 84876249941     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2013.03.004     Document Type: Article
Times cited : (2)

References (20)
  • 2
    • 77955883153 scopus 로고    scopus 로고
    • Complement: A key system for immune surveillance and homeostasis
    • D. Ricklin, G. Hajishengallis, K. Yang, and J.D. Lambris Complement: a key system for immune surveillance and homeostasis Nat. Immunol. 11 2010 785 797
    • (2010) Nat. Immunol. , vol.11 , pp. 785-797
    • Ricklin, D.1    Hajishengallis, G.2    Yang, K.3    Lambris, J.D.4
  • 3
    • 0024041055 scopus 로고
    • Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: Differences between crystal and solution conformations
    • D.G. Nettesheim, R.P. Edalji, K.W. Mollison, J. Greer, and E.R. Zuiderweg Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: differences between crystal and solution conformations Proc. Natl. Acad. Sci. USA 85 1988 5036 5040
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5036-5040
    • Nettesheim, D.G.1    Edalji, R.P.2    Mollison, K.W.3    Greer, J.4    Zuiderweg, E.R.5
  • 5
    • 17644388462 scopus 로고    scopus 로고
    • Role of C5a in inflammatory responses
    • DOI 10.1146/annurev.immunol.23.021704.115835
    • R.F. Guo, and P.A. Ward Role of C5a in inflammatory responses Annu. Rev. Immunol. 23 2005 821 852 (Pubitemid 40563186)
    • (2005) Annual Review of Immunology , vol.23 , pp. 821-852
    • Guo, R.-F.1    Ward, P.A.2
  • 6
    • 0034861323 scopus 로고    scopus 로고
    • Anaphylatoxins and infectious and non-infectious inflammatory diseases
    • DOI 10.1016/S0161-5890(01)00041-4, PII S0161589001000414
    • J. Kohl Anaphylatoxins and infectious and non-infectious inflammatory diseases Mol. Immunol. 38 2001 175 187 (Pubitemid 32786775)
    • (2001) Molecular Immunology , vol.38 , Issue.2-3 , pp. 175-187
    • Kohl, J.1
  • 9
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 10
    • 0029874193 scopus 로고    scopus 로고
    • High cell-density culture of Escherichia coli
    • DOI 10.1016/0167-7799(96)80930-9
    • S.Y. Lee High cell-density culture of Escherichia coli Trends Biotechnol. 14 1996 98 105 (Pubitemid 26079509)
    • (1996) Trends in Biotechnology , vol.14 , Issue.3 , pp. 98-105
    • Lee, S.Y.1
  • 11
    • 82455208943 scopus 로고    scopus 로고
    • High-level production of a kringle domain variant by high-cell-density cultivation of Escherichia coli
    • S.H. Jang, C.H. Lee, Y.S. Kim, and K.J. Jeong High-level production of a kringle domain variant by high-cell-density cultivation of Escherichia coli Appl. Microbiol. Biotechnol. 92 2011 327 336
    • (2011) Appl. Microbiol. Biotechnol. , vol.92 , pp. 327-336
    • Jang, S.H.1    Lee, C.H.2    Kim, Y.S.3    Jeong, K.J.4
  • 12
    • 81755177697 scopus 로고    scopus 로고
    • High-level production of a single chain antibody against anthrax toxin in Escherichia coli by high cell density cultivation
    • K.J. Jeong, and M. Rani High-level production of a single chain antibody against anthrax toxin in Escherichia coli by high cell density cultivation Bioprocess Biosyst. Eng. 34 2011 811 817
    • (2011) Bioprocess Biosyst. Eng. , vol.34 , pp. 811-817
    • Jeong, K.J.1    Rani, M.2
  • 13
    • 0042768090 scopus 로고    scopus 로고
    • Protein disulfide bond formation in prokaryotes
    • DOI 10.1146/annurev.biochem.72.121801.161459
    • H. Kadokura, F. Katzen, and J. Beckwith Protein disulfide bond formation in prokaryotes Annu. Rev. Biochem. 72 2003 111 135 (Pubitemid 36930443)
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 111-135
    • Kadokura, H.1    Katzen, F.2    Beckwith, J.3
  • 14
    • 78651301416 scopus 로고    scopus 로고
    • Recombinant antibodies: Engineering and production in yeast and bacterial hosts
    • K.J. Jeong, S.H. Jang, and N. Velmurugan Recombinant antibodies: engineering and production in yeast and bacterial hosts Biotechnol. J. 6 2011 16 27
    • (2011) Biotechnol. J. , vol.6 , pp. 16-27
    • Jeong, K.J.1    Jang, S.H.2    Velmurugan, N.3
  • 15
    • 33749180935 scopus 로고    scopus 로고
    • Functional expression of Candida antarctica lipase B in the Escherichia coli cytoplasm - A screening system for a frequently used biocatalyst
    • DOI 10.1007/s00253-006-0369-7
    • D. Liu, R.D. Schmid, and M. Rusnak Functional expression of Candida Antarctica lipase B in the Escherichia coli cytoplasm - a screening system for a frequently used biocatalyst Appl. Microbiol. Biotechnol. 72 2006 1024 1032 (Pubitemid 44477381)
    • (2006) Applied Microbiology and Biotechnology , vol.72 , Issue.5 , pp. 1024-1032
    • Liu, D.1    Schmid, R.D.2    Rusnak, M.3
  • 16
    • 33846046407 scopus 로고    scopus 로고
    • Fermentation process for tetrameric human collagen prolyl 4-hydroxylase in Escherichia coli: Improvement by gene optimisation of the PDI/β subunit and repeated addition of the inducer anhydrotetracycline
    • DOI 10.1016/j.jbiotec.2006.10.017, PII S0168165606009011
    • A. Neubauer, J. Soini, M. Bollok, M. Zenker, J. Sandqvist, J. Myllyharju, and P. Neubauer Fermentation process for tetrameric human collagen prolyl 4-hydroxylase in Escherichia coli: improvement by gene optimisation of the PDI/beta subunit and repeated addition of the inducer anhydrotetracycline J. Biotechnol. 128 2007 308 321 (Pubitemid 46074202)
    • (2007) Journal of Biotechnology , vol.128 , Issue.2 , pp. 308-321
    • Neubauer, A.1    Soini, J.2    Bollok, M.3    Zenker, M.4    Sandqvist, J.5    Myllyharju, J.6    Neubauer, P.7
  • 17
    • 52949132991 scopus 로고    scopus 로고
    • Expression of Candida antarctica lipase B in Pichia pastoris and various Escherichia coli systems
    • M.W. Larsen, U.T. Bornscheuer, and K. Hult Expression of Candida antarctica lipase B in Pichia pastoris and various Escherichia coli systems Protein Expr. Purif. 62 2008 90 97
    • (2008) Protein Expr. Purif. , vol.62 , pp. 90-97
    • Larsen, M.W.1    Bornscheuer, U.T.2    Hult, K.3
  • 18
    • 0037518221 scopus 로고    scopus 로고
    • Characterization of factors favoring the expression of soluble protozoan tubulin proteins in Escherichia coli
    • DOI 10.1016/S1046-5928(03)00006-8
    • L.M. MacDonald, A. Armson, R.C. Thompson, and J.A. Reynoldson Characterization of factors favoring the expression of soluble protozoan tubulin proteins in Escherichia coli Protein Expr. Purif. 29 2003 117 122 (Pubitemid 36599801)
    • (2003) Protein Expression and Purification , vol.29 , Issue.1 , pp. 117-122
    • MacDonald, L.M.1    Armson, A.2    Thompson, R.C.A.3    Reynoldson, J.A.4
  • 19
    • 0033486169 scopus 로고    scopus 로고
    • Expression of a recombinant Toxoplasma gondii ROP2 fragment as a fusion protein in bacteria circumvents insolubility and proteolytic degradation
    • A. Jacquet, V. Daminet, M. Haumont, L. Garcia, S. Chaudoir, A. Bollen, and R. Biemans Expression of a recombinant Toxoplasma gondii ROP2 fragment as a fusion protein in bacteria circumvents insolubility and proteolytic degradation Protein Expr. Purif. 17 1999 392 400
    • (1999) Protein Expr. Purif. , vol.17 , pp. 392-400
    • Jacquet, A.1    Daminet, V.2    Haumont, M.3    Garcia, L.4    Chaudoir, S.5    Bollen, A.6    Biemans, R.7
  • 20
    • 29344475982 scopus 로고    scopus 로고
    • Comparison of SUMO fusion technology with traditional gene fusion systems: Enhanced expression and solubility with SUMO
    • DOI 10.1110/ps.051812706
    • J.G. Marblestone, S.C. Edavettal, Y. Lim, P. Lim, X. Zuo, and T.R. Butt Comparison of SUMO fusion technology with traditional gene fusion systems: enhanced expression and solubility with SUMO Protein Sci. 15 2006 182 189 (Pubitemid 43004245)
    • (2006) Protein Science , vol.15 , Issue.1 , pp. 182-189
    • Marblestone, J.G.1    Edavettal, S.C.2    Lim, Y.3    Lim, P.4    Zuo, X.5    Butt, T.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.