메뉴 건너뛰기




Volumn 81, Issue 2, 2012, Pages 157-165

Reliable protein production in a Pseudomonas fluorescens expression system

Author keywords

Protein; Pseudomonas fluorescens; Recombinant

Indexed keywords

PSEUDOMONAS FLUORESCENS;

EID: 80355145782     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2011.09.010     Document Type: Review
Times cited : (45)

References (72)
  • 1
    • 70349765751 scopus 로고    scopus 로고
    • 25 years of recombinant proteins from reactor-grown cells - Where do we go from here?
    • D.L. Hacker, M. De Jesus, and F.M. Wurm 25 years of recombinant proteins from reactor-grown cells - where do we go from here? Biotechnol. Adv. 27 2009 1023 1027
    • (2009) Biotechnol. Adv. , vol.27 , pp. 1023-1027
    • Hacker, D.L.1    De Jesus, M.2    Wurm, F.M.3
  • 2
    • 78650406036 scopus 로고    scopus 로고
    • Process economic benefits of expression technology based on Pseudomonas fluorescens
    • J.A.C. Lim, A. Patkar, G. McDonagh, A. Sinclair, and P. Lucy Process economic benefits of expression technology based on Pseudomonas fluorescens BioProcess Int. 8 2010 62
    • (2010) BioProcess Int. , vol.8 , pp. 62
    • Lim, J.A.C.1    Patkar, A.2    McDonagh, G.3    Sinclair, A.4    Lucy, P.5
  • 3
    • 0037298656 scopus 로고    scopus 로고
    • Safety evaluation of an α-amylase enzyme preparation derived from the archaeal order Thermococcales as expressed in Pseudomonas fluorescens biovar I
    • DOI 10.1016/S0273-2300(03)00002-3
    • T.D. Landry, L. Chew, J.W. Davis, N. Frawley, H.H. Foley, S.J. Stelman, J. Thomas, J. Wolt, and D.S. Hanselman Safety evaluation of an alpha-amylase enzyme preparation derived from the archaeal order Thermococcales as expressed in Pseudomonas fluorescens biovar I Regul. Toxicol. Pharmacol. 37 2003 149 168 (Pubitemid 36349344)
    • (2003) Regulatory Toxicology and Pharmacology , vol.37 , Issue.1 , pp. 149-168
    • Landry, T.D.1    Chew, L.2    Davis, J.W.3    Frawley, N.4    Foley, H.H.5    Stelman, S.J.6    Thomas, J.7    Wolt, J.8    Hanselman, D.S.9
  • 6
    • 33846523370 scopus 로고    scopus 로고
    • The genomic sequence of Pseudomonas fluorescens Pf-5: Insights into biological control
    • DOI 10.1094/PHYTO-97-2-0233
    • J.E. Loper, D.Y. Kobayashi, and I.T. Paulsen The genomic sequence of Pseudomonas fluorescens Pf-5: insights into biological control Phytopathology 97 2007 233 238 (Pubitemid 46167893)
    • (2007) Phytopathology , vol.97 , Issue.2 , pp. 233-238
    • Loper, J.E.1    Kobayashi, D.Y.2    Paulsen, I.T.3
  • 8
    • 0024544412 scopus 로고
    • Complete nucleotide sequence and gene organization of the broad-host-range plasmid RSF1010
    • DOI 10.1016/0378-1119(89)90273-4
    • P. Scholz, V. Haring, B. Wittmann-Liebold, K. Ashman, M. Bagdasarian, and E. Scherzinger Complete nucleotide sequence and gene organization of the broad-host-range plasmid RSF1010 Gene 75 1989 271 288 (Pubitemid 19100128)
    • (1989) Gene , vol.75 , Issue.2 , pp. 271-288
    • Scholz, P.1    Haring, V.2    Wittmann-Liebold, B.3    Ashman, K.4    Bagdasarian, M.5    Scherzinger, E.6
  • 9
    • 0025270236 scopus 로고
    • Cloning vectors, derived from a naturally occurring plasmid of Pseudomonas savastanoi, specifically tailored for genetic manipulations in Pseudomonas
    • DOI 10.1016/0378-1119(90)90507-N
    • C. Nieto, E. Fernandez-Tresguerres, N. Sanchez, M. Vicente, and R. Diaz Cloning vectors, derived from a naturally occurring plasmid of Pseudomonas savastanoi, specifically tailored for genetic manipulations in Pseudomonas Gene 87 1990 145 149 (Pubitemid 20139867)
    • (1990) Gene , vol.87 , Issue.1 , pp. 145-149
    • Nieto, C.1    Fernandez-Tresguerres, E.2    Sanchez, N.3    Vicente, M.4    Diaz, R.5
  • 10
    • 0030852013 scopus 로고    scopus 로고
    • High-efficiency transposon mutagenesis by electroporation of a Pseudomonas fluorescens strain
    • DOI 10.1016/S0378-1097(97)00275-9, PII S0378109797002759
    • F. Artiguenave, R. Vilagines, and C. Danglot High-efficiency transposon mutagenesis by electroporation of a Pseudomonas fluorescens strain FEMS Microbiol. Lett. 153 1997 363 369 (Pubitemid 27359733)
    • (1997) FEMS Microbiology Letters , vol.153 , Issue.2 , pp. 363-369
    • Artiguenave, F.1    Vilagines, R.2    Danglot, C.3
  • 11
    • 0028471858 scopus 로고
    • Efficient transformation of pseudomonas strains with pNI vectors by electroporation
    • N. Itoh, T. Kouzai, and Y. Koide Efficient transformation of pseudomonas strains with pNI vectors by electroporation Biosci. Biotechnol. Biochem. 58 1994 1306 1308
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 1306-1308
    • Itoh, N.1    Kouzai, T.2    Koide, Y.3
  • 12
    • 0037312815 scopus 로고    scopus 로고
    • Modulation of pPS10 host range by plasmid-encoded RepA initiator protein
    • DOI 10.1128/JB.185.4.1367-1375.2003
    • B. Maestro, J.M. Sanz, R. Diaz-Orejas, and E. Fernandez-Tresguerres Modulation of pPS10 Host Range by Plasmid-Encoded RepA Initiator Protein J. Bacteriol. 185 2003 1367 1375 (Pubitemid 36176869)
    • (2003) Journal of Bacteriology , vol.185 , Issue.4 , pp. 1367-1375
    • Maestro, B.1    Sanz, J.M.2    Diaz-Orejas, R.3    Fernandez-Tresguerres, E.4
  • 13
    • 16344374397 scopus 로고    scopus 로고
    • Auxotrophic markers pyrF and proC can replace antibiotic markers on protein production plasmids in high-cell-density Pseudomonas fluorescens fermentation
    • DOI 10.1021/bp049696g
    • J.C. Schneider, A.F. Jenings, D.M. Mun, P.M. McGovern, and L.C. Chew Auxotrophic markers pyrF and proC can replace antibiotic markers on protein production plasmids in high-cell-density Pseudomonas fluorescens fermentation Biotechnol. Prog. 21 2005 343 348 (Pubitemid 40466404)
    • (2005) Biotechnology Progress , vol.21 , Issue.2 , pp. 343-348
    • Schneider, J.C.1    Jenings, A.F.2    Mun, D.M.3    McGovern, P.M.4    Chew, L.C.5
  • 14
    • 0023392267 scopus 로고
    • A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains
    • E. Alani, L. Cao, and N. Kleckner A method for gene disruption that allows repeated use of URA3 selection in the construction of multiply disrupted yeast strains Genetics 116 1987 541 545
    • (1987) Genetics , vol.116 , pp. 541-545
    • Alani, E.1    Cao, L.2    Kleckner, N.3
  • 15
    • 13544273854 scopus 로고    scopus 로고
    • Adaptation of the yeast URA3 selection system to gram-negative bacteria and generation of a ΔbetCDE Pseudomonas putida strain
    • DOI 10.1128/AEM.71.2.883-892.2005
    • T.C. Galvao V. de Lorenzo, Adaptation of the yeast URA3 selection system to gram-negative bacteria and generation of a ΔbetCDE Pseudomonas putida strain Appl. Environ. Microbiol. 71 2005 883 892 (Pubitemid 40223576)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.2 , pp. 883-892
    • Galvao, T.C.1    De Lorenzo, V.2
  • 16
    • 84907124004 scopus 로고
    • Selection of ura5 and ura3 mutants from the two varieties of Cryptococcus neoformans on 5-fluoroorotic acid medium
    • K.J. Kwon-Chung, A. Varma, J.C. Edman, and J.E. Bennett Selection of ura5 and ura3 mutants from the two varieties of Cryptococcus neoformans on 5-fluoroorotic acid medium J. Med. Vet. Mycol. 30 1992 61 69
    • (1992) J. Med. Vet. Mycol. , vol.30 , pp. 61-69
    • Kwon-Chung, K.J.1    Varma, A.2    Edman, J.C.3    Bennett, J.E.4
  • 18
    • 0026080658 scopus 로고
    • Direct selection of stabilised yeast URA3 transformants with 5-fluorouracil
    • M.A. Romanos, K.M. Beesley, and J.J. Clare Direct selection of stabilised yeast URA3 transformants with 5-fluorouracil Nucleic Acids Res. 19 1991 187
    • (1991) Nucleic Acids Res. , vol.19 , pp. 187
    • Romanos, M.A.1    Beesley, K.M.2    Clare, J.J.3
  • 19
    • 0031690616 scopus 로고    scopus 로고
    • Rare homologous gene targeting in Histoplasma capsulatum: Disruption of the URA5(Hc) gene by allelic replacement
    • J.P. Woods, D.M. Retallack, E.L. Heinecke, and W.E. Goldman Rare homologous gene targeting in Histoplasma capsulatum: disruption of the URA5Hc gene by allelic replacement J. Bacteriol. 180 1998 5135 5143 (Pubitemid 28470941)
    • (1998) Journal of Bacteriology , vol.180 , Issue.19 , pp. 5135-5143
    • Woods, J.P.1    Retallack, D.M.2    Heinecke, E.L.3    Goldman, W.E.4
  • 20
    • 0021042016 scopus 로고
    • Activity of the hybrid trp-lac (tac) promoter of Escherichia coli in Pseudomonas putida. Construction of broad-host-range, controlled-expression vectors
    • M.M. Bagdasarian, E. Amann, R. Lurz, B. Ruckert, and M. Bagdasarian Activity of the hybrid trp-lac (tac) promoter of Escherichia coli in Pseudomonas putida. Construction of broad-host-range, controlled-expression vectors Gene 26 1983 273 282 (Pubitemid 14190480)
    • (1983) Gene , vol.26 , Issue.2-3 , pp. 273-282
    • Bagdasarian, M.M.1    Amann, E.2    Lurz, R.3
  • 21
    • 0025992669 scopus 로고
    • Specificity of antitermination mechanisms: Suppression of the terminator cluster T1-T2 of Escherichia coli ribosomal RNA operon, rrnB, by phage λ antiterminators
    • B. Ghosh, E. Grzadzielska, P. Bhattacharya, E. Peralta, J. DeVito, and A. Das Specificity of antitermination mechanisms. Suppression of the terminator cluster T1-T2 of Escherichia coli ribosomal RNA operon, rrnB, by phage lambda antiterminators J. Mol. Biol. 222 1991 59 66 (Pubitemid 121003988)
    • (1991) Journal of Molecular Biology , vol.222 , Issue.1 , pp. 59-66
    • Ghosh, B.1    Grzadzielska, E.2    Bhattacharya, P.3    Peralta, E.4    DeVito, J.5    Das, A.6
  • 22
    • 0022251239 scopus 로고
    • Expression of plasmid encoded Escherichia coli 5S ribosomal ribonucleic acid in Pseudomonas putida
    • DOI 10.1016/0014-5793(85)80390-2
    • R.K. Hartmann, P.P. Henze, N. Ulbrich, and V.A. Erdmann Expression of plasmid encoded Escherichia coli 5S ribosomal ribonucleic acid in Pseudomonas putida FEBS Lett. 188 1985 295 301 (Pubitemid 16249747)
    • (1985) FEBS Letters , vol.188 , Issue.2 , pp. 295-301
    • Hartmann, R.K.1    Henze, P.P.2    Ulbrich, N.3    Erdmann, V.A.4
  • 23
    • 0019793144 scopus 로고
    • The DNA sequence change resulting from the I(Q1) mutation which greatly increases promoter strength
    • M.P. Calos, and J.H. Miller The DNA sequence change resulting from the IQ1 mutation, which greatly increases promoter strength Mol. Gen. Genet. 183 1981 559 560 (Pubitemid 12216647)
    • (1981) Molecular and General Genetics , vol.183 , Issue.3 , pp. 559-560
    • Calos, M.P.1    Miller, J.H.2
  • 26
    • 30644474329 scopus 로고    scopus 로고
    • Identification of anthranilate and benzoate metabolic operons of Pseudomonas fluorescens and functional characterization of their promoter regions
    • D.M. Retallack, T.C. Thomas, Y. Shao, K.L. Haney, S.M. Resnick, V.D. Lee, and C.H. Squires Identification of anthranilate and benzoate metabolic operons of Pseudomonas fluorescens and functional characterization of their promoter regions Microb. Cell Fact. 5 2006 1
    • (2006) Microb. Cell Fact. , vol.5 , pp. 1
    • Retallack, D.M.1    Thomas, T.C.2    Shao, Y.3    Haney, K.L.4    Resnick, S.M.5    Lee, V.D.6    Squires, C.H.7
  • 29
    • 34548142278 scopus 로고    scopus 로고
    • Transport of heterologous proteins to the periplasmic space of Pseudomonas fluorescens using a variety of native signal sequences
    • DOI 10.1007/s10529-007-9415-5
    • D.M. Retallack, J.C. Schneider, J. Mitchell, L. Chew, and H. Liu Transport of heterologous proteins to the periplasmic space of Pseudomonas fluorescens using a variety of native signal sequences Biotechnol. Lett. 29 2007 1483 1491 (Pubitemid 47301355)
    • (2007) Biotechnology Letters , vol.29 , Issue.10 , pp. 1483-1491
    • Retallack, D.M.1    Schneider, J.C.2    Mitchell, J.3    Chew, L.4    Liu, H.5
  • 31
    • 0027216214 scopus 로고
    • Turbo cloning: A fast, efficient method for cloning PCR products and other blunt-ended DNA fragments into plasmids
    • A.C. Boyd Turbo cloning: a fast, efficient method for cloning PCR products and other blunt-ended DNA fragments into plasmids Nucleic Acids Res. 21 1993 817 821 (Pubitemid 23152987)
    • (1993) Nucleic Acids Research , vol.21 , Issue.4 , pp. 817-821
    • Boyd, A.C.1
  • 32
    • 0034788268 scopus 로고    scopus 로고
    • LoxP-directed cloning: Use of Cre recombinase as a universal restriction enzyme
    • 910, 912, 914, 916, 918
    • F. Buchholz, and M. Bishop LoxP-directed cloning: use of Cre recombinase as a universal restriction enzyme Biotechniques 31 2001 906 908 910, 912, 914, 916, 918
    • (2001) Biotechniques , vol.31 , pp. 906-908
    • Buchholz, F.1    Bishop, M.2
  • 33
    • 0034981674 scopus 로고    scopus 로고
    • Development of a FLP/frt system for generating helper-dependent adenoviral vectors
    • DOI 10.1006/mthe.2001.0323
    • P. Ng, C. Beauchamp, C. Evelegh, R. Parks, and F.L. Graham Development of a FLP/frt system for generating helper-dependent adenoviral vectors Mol. Ther. 3 2001 809 815 (Pubitemid 32519562)
    • (2001) Molecular Therapy , vol.3 , Issue.5 , pp. 809-815
    • Ng, P.1    Beauchamp, C.2    Evelegh, C.3    Parks, R.4    Graham, F.L.5
  • 34
    • 79953080436 scopus 로고    scopus 로고
    • Modified gateway system for double shRNA expression and Cre/lox based gene expression
    • N. Radulovich, L. Leung, and M.S. Tsao Modified gateway system for double shRNA expression and Cre/lox based gene expression BMC Biotechnol. 11 1998 24
    • (1998) BMC Biotechnol. , vol.11 , pp. 24
    • Radulovich, N.1    Leung, L.2    Tsao, M.S.3
  • 35
    • 0344333424 scopus 로고    scopus 로고
    • DNA cassette exchange in ES cells mediated by FLF recombinase: An efficient strategy for repeated modification of tagged loci by marker-free constructs
    • DOI 10.1021/bi980288t
    • J. Seibler, D. Schubeler, S. Fiering, M. Groudine, and J. Bode DNA cassette exchange in ES cells mediated by Flp recombinase: an efficient strategy for repeated modification of tagged loci by marker-free constructs Biochemistry 37 1998 6229 6234 (Pubitemid 28213639)
    • (1998) Biochemistry , vol.37 , Issue.18 , pp. 6229-6234
    • Seibler, J.1    Schubeler, D.2    Fiering, S.3    Groudine, M.4    Bode, J.5
  • 36
    • 35448952987 scopus 로고    scopus 로고
    • Construction and evaluation of multisite recombinatorial (Gateway) cloning vectors for Gram-positive bacteria
    • T. Perehinec, S. Qazi, S. Gaddipati, V. Salisbury, C. Rees, and P. Hill Construction and evaluation of multisite recombinatorial (Gateway) cloning vectors for Gram-positive bacteria BMC Mol. Biol. 8 2007 80
    • (2007) BMC Mol. Biol. , vol.8 , pp. 80
    • Perehinec, T.1    Qazi, S.2    Gaddipati, S.3    Salisbury, V.4    Rees, C.5    Hill, P.6
  • 37
    • 79955556740 scopus 로고    scopus 로고
    • Recombinant expression and functional analysis of proteases from Streptococcus pneumoniae, Bacillus anthracis, and Yersinia pestis
    • K. Kwon, J. Hasseman, S. Latham, C. Grose, Y. Do, R. Fleischmann, R. Pieper, and S. Peterson Recombinant expression and functional analysis of proteases from Streptococcus pneumoniae, Bacillus anthracis, and Yersinia pestis BMC Biochemistry 12 2011 17
    • (2011) BMC Biochemistry , vol.12 , pp. 17
    • Kwon, K.1    Hasseman, J.2    Latham, S.3    Grose, C.4    Do, Y.5    Fleischmann, R.6    Pieper, R.7    Peterson, S.8
  • 38
    • 0022399694 scopus 로고
    • Universal restriction endonucleases: Designing novel cleavage specificities by combining adapter oligodeoxynucleotide and enzyme moieties
    • W. Szybalski Universal restriction endonucleases: designing novel cleavage specificities by combining adapter oligodeoxynucleotide and enzyme moieties Gene 40 1985 169 173 (Pubitemid 16107671)
    • (1985) Gene , vol.40 , Issue.2-3 , pp. 169-173
    • Szybalski, W.1
  • 40
    • 0025855940 scopus 로고
    • Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: Protease III degrades high-molecular-weight substrates in vivo
    • F. Baneyx, and G. Georgiou Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: protease III degrades high-molecular-weight substrates in vivo J. Bacteriol. 173 1991 2696 2703
    • (1991) J. Bacteriol. , vol.173 , pp. 2696-2703
    • Baneyx, F.1    Georgiou, G.2
  • 41
    • 0345491422 scopus 로고    scopus 로고
    • Secretory production of recombinant protein by a high cell density culture of a protease negative mutant Escherichia coli strain
    • DOI 10.1021/bp9900108
    • S.J. Park, G. Georgiou, and S.Y. Lee Secretory production of recombinant protein by a high cell density culture of a protease negative mutant Escherichia coli strain Biotechnol. Prog. 15 1999 164 167 (Pubitemid 29174931)
    • (1999) Biotechnology Progress , vol.15 , Issue.2 , pp. 164-167
    • Park, S.J.1    Georgiou, G.2    Lee, S.Y.3
  • 44
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • DOI 10.1016/S0958-1669(99)00003-8
    • F. Baneyx Recombinant protein expression in Escherichia coli Curr. Opin. Biotechnol. 10 1999 411 421 (Pubitemid 29457264)
    • (1999) Current Opinion in Biotechnology , vol.10 , Issue.5 , pp. 411-421
    • Baneyx, F.1
  • 45
    • 79551517798 scopus 로고    scopus 로고
    • Enhancing functional expression of Heterologous Burkholderia lipase in Escherichia coli
    • N. Narayanan, M. Khan, and C.P. Chou Enhancing functional expression of Heterologous Burkholderia lipase in Escherichia coli Mol. Biotechnol. 47 2011 130 143
    • (2011) Mol. Biotechnol. , vol.47 , pp. 130-143
    • Narayanan, N.1    Khan, M.2    Chou, C.P.3
  • 46
    • 0346935999 scopus 로고    scopus 로고
    • DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli
    • DOI 10.1016/S1046-5928(03)00233-X
    • Y. Chen, J. Song, S.F. Sui, and D.N. Wang DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli Protein. Expr. Purif. 32 2003 221 231 (Pubitemid 38039013)
    • (2003) Protein Expression and Purification , vol.32 , Issue.2 , pp. 221-231
    • Chen, Y.1    Song, J.2    Sui, S.-F.3    Wang, D.-N.4
  • 47
    • 0031860811 scopus 로고    scopus 로고
    • Chaperone coexpression plasmids: Differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli
    • K. Nishihara, M. Kanemori, M. Kitagawa, H. Yanagi, and T. Yura Chaperone coexpression plasmids: differential and synergistic roles of DnaK-DnaJ-GrpE and GroEL-GroES in assisting folding of an allergen of Japanese cedar pollen, Cryj2, in Escherichia coli Appl. Environ. Microbiol. 64 1998 1694 1699 (Pubitemid 28234771)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.5 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 48
    • 0026726710 scopus 로고
    • Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli
    • S.C. Lee, and P.O. Olins Effect of overproduction of heat shock chaperones GroESL and DnaK on human procollagenase production in Escherichia coli J. Biol. Chem. 267 1992 2849 2852
    • (1992) J. Biol. Chem. , vol.267 , pp. 2849-2852
    • Lee, S.C.1    Olins, P.O.2
  • 49
    • 0036417347 scopus 로고    scopus 로고
    • Overexpression of dsbc and dsbg markedly improves soluble and functional expression of single-chain fv antibodies in escherichia coli
    • DOI 10.1016/S1046-5928(02)00502-8, PII S1046592802005028
    • Z. Zhang, Z.H. Li, F. Wang, M. Fang, C.C. Yin, Z.Y. Zhou, Q. Lin, and H.L. Huang Overexpression of DsbC and DsbG markedly improves soluble and functional expression of single-chain Fv antibodies in Escherichia coli Protein Expr. Purif. 26 2002 218 228 (Pubitemid 35326539)
    • (2002) Protein Expression and Purification , vol.26 , Issue.2 , pp. 218-228
    • Zhang, Z.1    Li, Z.-H.2    Wang, F.3    Fang, M.4    Yin, C.-C.5    Zhou, Z.-Y.6    Lin, Q.7    Huang, H.-L.8
  • 51
    • 3042545320 scopus 로고    scopus 로고
    • High-throughput screening for soluble recombinant expressed kinases in Escherichia coli and insect cells
    • DOI 10.1016/j.pep.2004.03.003, PII S1046592804001007
    • S.P. Chambers, D.A. Austen, J.R. Fulghum, and W.M. Kim High-throughput screening for soluble recombinant expressed kinases in Escherichia coli and insect cells Protein Expr. Purif. 36 2004 40 47 (Pubitemid 38836762)
    • (2004) Protein Expression and Purification , vol.36 , Issue.1 , pp. 40-47
    • Chambers, S.P.1    Austen, D.A.2    Fulghum, J.R.3    Kim, W.M.4
  • 52
    • 34447631361 scopus 로고    scopus 로고
    • Homologous high-throughput expression and purification of highly conserved E. coli proteins
    • A. Ergin, K. Bussow, J. Sieper, A. Thiel, R. Duchmann, and T. Adam Homologous high-throughput expression and purification of highly conserved E. coli proteins Microb. Cell Fact. 6 2007 18
    • (2007) Microb. Cell Fact. , vol.6 , pp. 18
    • Ergin, A.1    Bussow, K.2    Sieper, J.3    Thiel, A.4    Duchmann, R.5    Adam, T.6
  • 56
    • 17444366186 scopus 로고    scopus 로고
    • Clostridium difficile toxins: Mechanism of action and role in disease
    • DOI 10.1128/CMR.18.2.247-263.2005
    • D.E. Voth, and J.D. Ballard Clostridium difficile toxins: mechanism of action and role in disease Clin. Microbiol. Rev. 18 2005 247 263 (Pubitemid 40548293)
    • (2005) Clinical Microbiology Reviews , vol.18 , Issue.2 , pp. 247-263
    • Voth, D.E.1    Ballard, J.D.2
  • 59
    • 0035145510 scopus 로고    scopus 로고
    • Safety and immunogenicity of increasing doses of a Clostridium difficile toxoid vaccine administered to healthy adults
    • DOI 10.1128/IAI.69.2.988-995.2001
    • K.L. Kotloff, S.S. Wasserman, G.A. Losonsky, W. Thomas Jr., R. Nichols, R. Edelman, M. Bridwell, and T.P. Monath Safety and immunogenicity of increasing doses of a Clostridium difficile toxoid vaccine administered to healthy adults Infect. Immun. 69 2001 988 995 (Pubitemid 32109565)
    • (2001) Infection and Immunity , vol.69 , Issue.2 , pp. 988-995
    • Kotloff, K.L.1    Wasserman, S.S.2    Losonsky, G.A.3    Thomas Jr., W.4    Nichols, R.5    Edelman, R.6    Bridwell, M.7    Monath, T.P.8
  • 60
    • 2942722679 scopus 로고    scopus 로고
    • Antibodies and genetically engineered related molecules: Production and purification
    • DOI 10.1021/bp030070k
    • A.C.A. Roque, C.R. Lowe, and M.Â. Taipa Antibodies and genetically engineered related molecules: production and purification Biotechnol. Prog. 20 2004 639 654 (Pubitemid 38784002)
    • (2004) Biotechnology Progress , vol.20 , Issue.3 , pp. 639-654
    • Roque, A.C.A.1    Lowe, C.R.2    Taipa, M.A.3
  • 64
    • 3042644563 scopus 로고    scopus 로고
    • High-level expression of human cytochrome P450 1A2 by co-expression with human molecular chaperone HDJ-1(Hsp40)
    • DOI 10.1016/j.pep.2004.03.005, PII S1046592804001032
    • T. Ahn, S. Yang, and C.-H. Yun High-level expression of human cytochrome P450 1A2 by co-expression with human molecular chaperone HDJ-1(Hsp40) Protein Expr. Purif. 36 2004 48 52 (Pubitemid 38836763)
    • (2004) Protein Expression and Purification , vol.36 , Issue.1 , pp. 48-52
    • Ahn, T.1    Yang, S.2    Yun, C.-H.3
  • 65
    • 0030041230 scopus 로고    scopus 로고
    • Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab' fragment expressed in Escherichia coli
    • DOI 10.1016/0014-5793(96)00028-2
    • D.P. Humphreys, N. Weir, A. Lawson, A. Mountain, and P.A. Lund Co-expression of human protein disulphide isomerase (PDI) can increase the yield of an antibody Fab' fragment expressed in Escherichia coli FEBS Lett. 380 1996 194 197 (Pubitemid 26058757)
    • (1996) FEBS Letters , vol.380 , Issue.1-2 , pp. 194-197
    • Humphreys, D.P.1    Weir, N.2    Lawson, A.3    Mountain, A.4    Lund, P.A.5
  • 66
    • 0033230290 scopus 로고    scopus 로고
    • Facilitating the formation of disulfide bonds in the Escherichia coli periplasm via coexpression of yeast protein disulfide isomerase
    • X. Zhan, M. Schwaller, H.F. Gilbert, and G. Georgiou Facilitating the formation of disulfide bonds in the Escherichia coli periplasm via coexpression of yeast protein disulfide isomerase Biotechnol. Prog. 15 1999 1033 1038
    • (1999) Biotechnol. Prog. , vol.15 , pp. 1033-1038
    • Zhan, X.1    Schwaller, M.2    Gilbert, H.F.3    Georgiou, G.4
  • 67
    • 79955638409 scopus 로고    scopus 로고
    • Soluble periplasmic production of human granulocyte colony-stimulating factor (G-CSF) in Pseudomonas fluorescens
    • H. Jin, G.T. Cantin, S. Maki, L.C. Chew, S.M. Resnick, J. Ngai, and D.M. Retallack Soluble periplasmic production of human granulocyte colony-stimulating factor (G-CSF) in Pseudomonas fluorescens Protein Expr. Purif. 78 2011 69 77
    • (2011) Protein Expr. Purif. , vol.78 , pp. 69-77
    • Jin, H.1    Cantin, G.T.2    Maki, S.3    Chew, L.C.4    Resnick, S.M.5    Ngai, J.6    Retallack, D.M.7
  • 68
    • 42649095679 scopus 로고    scopus 로고
    • Human granulocyte colony stimulating factor (hG-CSF): Cloning, overexpression, purification and characterization
    • A.L. Vanz, G. Renard, M.S. Palma, J.M. Chies, S.L. Dalmora, L.A. Basso, and D.S. Santos Human granulocyte colony stimulating factor (hG-CSF): cloning, overexpression, purification and characterization Microb. Cell Fact. 7 2008 13
    • (2008) Microb. Cell Fact. , vol.7 , pp. 13
    • Vanz, A.L.1    Renard, G.2    Palma, M.S.3    Chies, J.M.4    Dalmora, S.L.5    Basso, L.A.6    Santos, D.S.7
  • 69
    • 33947581656 scopus 로고    scopus 로고
    • Inactivation and purification of cowpea mosaic virus-like particles displaying peptide antigens from Bacillus anthracis
    • DOI 10.1016/j.jviromet.2006.12.008, PII S0166093406004435
    • J.P. Phelps, N. Dang, and L. Rasochova Inactivation and purification of cowpea mosaic virus-like particles displaying peptide antigens from Bacillus anthracis J. Virol. Methods 141 2007 146 153 (Pubitemid 46476811)
    • (2007) Journal of Virological Methods , vol.141 , Issue.2 , pp. 146-153
    • Phelps, J.P.1    Dang, N.2    Rasochova, L.3
  • 70
    • 0028919805 scopus 로고
    • In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in Escherichia coli and in vitro-transcribed viral cDNA
    • X. Zhao, J.M. Fox, N.H. Olson, T.S. Baker, and M.J. Young In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in Escherichia coli and in vitro-transcribed viral cDNA Virology 207 1995 486 494
    • (1995) Virology , vol.207 , pp. 486-494
    • Zhao, X.1    Fox, J.M.2    Olson, N.H.3    Baker, T.S.4    Young, M.J.5
  • 71
    • 77953082285 scopus 로고    scopus 로고
    • Soluble expression and purification of the anthrax protective antigen in e coli and identification of a novel dominant-negative mutant N435C
    • G. Wu, C. Feng, Y. Hong, A. Guo, S. Cao, J. Dong, L. Lin, and Z. Liu Soluble expression and purification of the anthrax protective antigen in E coli and identification of a novel dominant-negative mutant N435C Appl. Microbiol. Biotechnol. 87 2010 609 616
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 609-616
    • Wu, G.1    Feng, C.2    Hong, Y.3    Guo, A.4    Cao, S.5    Dong, J.6    Lin, L.7    Liu, Z.8
  • 72
    • 0022520944 scopus 로고
    • Growth of Clostridium difficile and production of toxins A and B in complex and defined media
    • S.C. Haslam, J.M. Ketley, T.J. Mitchell, J. Stephen, D.W. Burdon, and D.C. Candy Growth of Clostridium difficile and production of toxins A and B in complex and defined media J. Med. Microbiol. 21 1986 293 297 (Pubitemid 16053517)
    • (1986) Journal of Medical Microbiology , vol.21 , Issue.4 , pp. 293-297
    • Haslam, S.C.1    Ketley, J.M.2    Mitchell, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.