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Volumn 27, Issue 3, 2004, Pages 442-453

Production of recombinant proteins in Escherichia coli

Author keywords

Expression vectors; Molecular chaperones; Secretion

Indexed keywords

DNA; ESCHERICHIA COLI PROTEIN; RECOMBINANT PROTEIN;

EID: 27144466197     PISSN: 14154757     EISSN: 16784685     Source Type: Journal    
DOI: 10.1590/S1415-47572004000300022     Document Type: Review
Times cited : (81)

References (75)
  • 1
    • 0025309315 scopus 로고
    • Outer-membrane PhoE protein of Escherichia coli K-12 as an exposure vetor: Possibilities and limitations
    • Agterberg M, Adriaanse H, van Bruggen A, Karperien M and Tommassen J (1990) Outer-membrane PhoE protein of Escherichia coli K-12 as an exposure vetor: Possibilities and limitations. Gene 88:37-45.
    • (1990) Gene , vol.88 , pp. 37-45
    • Agterberg, M.1    Adriaanse, H.2    van Bruggen, A.3    Karperien, M.4    Tommassen, J.5
  • 2
    • 0033598777 scopus 로고    scopus 로고
    • Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
    • Bessette PH, Åslund F, Beckwith J and Georgiou G (1999) Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm. Proc Natl Acad Sci USA 96:13703-13708.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13703-13708
    • Bessette, P.H.1    Åslund, F.2    Beckwith, J.3    Georgiou, G.4
  • 3
    • 0033153294 scopus 로고    scopus 로고
    • There's a right way and a wrong way: In vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike
    • Betts S and King J (1999) There's a right way and a wrong way: In vivo and in vitro folding, misfolding and subunit assembly of the P22 tailspike. Structure 7:R131-R139.
    • (1999) Structure , vol.7
    • Betts, S.1    King, J.2
  • 4
    • 0028858066 scopus 로고
    • A high-level expression system: Synthesis of human interleukin 1α and its receptor antagonist
    • Birikh KR, Lebedenko EN, Boni IV and Berlin YA (1995) A high-level expression system: Synthesis of human interleukin 1α and its receptor antagonist. Gene 164:341-345.
    • (1995) Gene , vol.164 , pp. 341-345
    • Birikh, K.R.1    Lebedenko, E.N.2    Boni, I.V.3    Berlin, Y.A.4
  • 5
    • 0026327753 scopus 로고
    • A novel strategy for production of a highly expressed recombinant protein in an active form
    • Blackwell JR and Horgan R (1991) A novel strategy for production of a highly expressed recombinant protein in an active form. FEBS Lett 295:10-12.
    • (1991) FEBS Lett , vol.295 , pp. 10-12
    • Blackwell, J.R.1    Horgan, R.2
  • 6
    • 0030051047 scopus 로고    scopus 로고
    • Post-transcriptional regulation of CspA expression in Escherichia coli
    • Brandi A, Pietroni P, Gualerzi CO and Pon CL (1997) Post-transcriptional regulation of CspA expression in Escherichia coli. Mol Microbiol 19:231-240.
    • (1997) Mol Microbiol , vol.19 , pp. 231-240
    • Brandi, A.1    Pietroni, P.2    Gualerzi, C.O.3    Pon, C.L.4
  • 7
    • 0019358924 scopus 로고    scopus 로고
    • Construction and fine mapping of recombinant plasmids containing the rrnB ribosomal RNA operon of E. coli
    • Brosius J, Ullrich A, Raker MA, Gray A, Dull TJ, Gutelt RG and Noller HF (2003) Construction and fine mapping of recombinant plasmids containing the rrnB ribosomal RNA operon of E. coli. Plasmid 6:112-118.
    • (2003) Plasmid , vol.6 , pp. 112-118
    • Brosius, J.1    Ullrich, A.2    Raker, M.A.3    Gray, A.4    Dull, T.J.5    Gutelt, R.G.6    Noller, H.F.7
  • 8
    • 0025348395 scopus 로고
    • Suppression of the negative effect of minor arginine codons on gene expression: Preferential usage of minor codons within the first 25 codons of the Escherichia coli genes
    • Chen G-FT and Inouye M (1990) Suppression of the negative effect of minor arginine codons on gene expression: Preferential usage of minor codons within the first 25 codons of the Escherichia coli genes. Nucleic Acids Res 18:1465-1473.
    • (1990) Nucleic Acids Res , vol.18 , pp. 1465-1473
    • Chen, G.-F.T.1    Inouye, M.2
  • 9
    • 0027960812 scopus 로고
    • Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli
    • Chen G-FT and Inouye M (1994) Role of the AGA/AGG codons, the rarest codons in global gene expression in Escherichia coli. Genes Dev 8:2641-2652.
    • (1994) Genes Dev , vol.8 , pp. 2641-2652
    • Chen, G.-F.T.1    Inouye, M.2
  • 10
    • 0027956532 scopus 로고
    • The influence of adenine-rich motifs in the 3′ portion of the ribosome binding site on human IFN-γ gene expression in Escherichia coli
    • Chen HY, Pomeroy LR, Bjerknes M, Tam J and Jay E (1994) The influence of adenine-rich motifs in the 3' portion of the ribosome binding site on human IFN-γ gene expression in Escherichia coli. J Mol Biol 240:20-27.
    • (1994) J Mol Biol , vol.240 , pp. 20-27
    • Chen, H.Y.1    Pomeroy, L.R.2    Bjerknes, M.3    Tam, J.4    Jay, E.5
  • 11
    • 0022419115 scopus 로고
    • Mutations UP-stream of the ribosome-binding site affect translation efficiency
    • Coleman J, Inouye M and Nakamura K (1985) Mutations UP-stream of the ribosome-binding site affect translation efficiency. J Mol Biol 181:139-143.
    • (1985) J Mol Biol , vol.181 , pp. 139-143
    • Coleman, J.1    Inouye, M.2    Nakamura, K.3
  • 12
    • 0032797898 scopus 로고    scopus 로고
    • Development of an optimised expression system for the screening of antibody libraries displayed on the Escherichia coli surface
    • Daugherty PS, Olsen MJ, Iverson BL, and Georgiou G (1999) Development of an optimised expression system for the screening of antibody libraries displayed on the Escherichia coli surface. Protein Engin 12:613-621.
    • (1999) Protein Engin , vol.12 , pp. 613-621
    • Daugherty, P.S.1    Olsen, M.J.2    Iverson, B.L.3    Georgiou, G.4
  • 13
    • 0020649604 scopus 로고
    • The tac promoter: A functional hybrid derived from the trp and lac promoters
    • De Boer P, Comstock LJ and Vasser M (1983) The tac promoter: A functional hybrid derived from the trp and lac promoters. Proc Natl Acad Sci USA 80:21-25.
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 21-25
    • De Boer, P.1    Comstock, L.J.2    Vasser, M.3
  • 14
    • 0032916816 scopus 로고    scopus 로고
    • Bacterial surface display of an anti-pollutant antibody fragment
    • Dhillon JK, Drew PD and Porter AJR (1999) Bacterial surface display of an anti-pollutant antibody fragment. Lett Appl Microbiol 28:350-354.
    • (1999) Lett Appl Microbiol , vol.28 , pp. 350-354
    • Dhillon, J.K.1    Drew, P.D.2    Porter, A.J.R.3
  • 15
    • 0014273838 scopus 로고
    • Mutants of Escherichia coli with an altered tryptophanyl-transfer ribonucleic acid synthetase
    • Doolittle WF and Yanofsky C (1968) Mutants of Escherichia coli with an altered tryptophanyl-transfer ribonucleic acid synthetase. J Bacteriol 95:1283-1294.
    • (1968) J Bacteriol , vol.95 , pp. 1283-1294
    • Doolittle, W.F.1    Yanofsky, C.2
  • 17
    • 0026602761 scopus 로고
    • A 5′-terminal stemloop structure can stabilize mRNA in Escherichia coli
    • Emory SA, Bouvet P and Belasco JG (1992) A 5'-terminal stemloop structure can stabilize mRNA in Escherichia coli. Genes Dev 6:135-148.
    • (1992) Genes Dev , vol.6 , pp. 135-148
    • Emory, S.A.1    Bouvet, P.2    Belasco, J.G.3
  • 19
    • 14744300636 scopus 로고
    • Specific adhesion and hydrolyis of cellulose by intact Escherichia coli expressing surface anchored cellulase or cellulose binding domains
    • Francisco JA, Stathopoulos C, Warren RAJ, Kilburn DG and Georgiou G (1993) Specific adhesion and hydrolyis of cellulose by intact Escherichia coli expressing surface anchored cellulase or cellulose binding domains. Biotechnol 11:491-495.
    • (1993) Biotechnol , vol.11 , pp. 491-495
    • Francisco, J.A.1    Stathopoulos, C.2    Warren, R.A.J.3    Kilburn, D.G.4    Georgiou, G.5
  • 20
    • 0029983637 scopus 로고    scopus 로고
    • Display of β-lactamase on the Escherichia coli surface: Outer membrane phenotypes conferred by Lpp'-OmpA'-β-lactamase fusions
    • Georgiou G, Stephens DL, Stathopoulos C, Poestshie HL, Mendenhall J and Earhart CF (1996) Display of β-lactamase on the Escherichia coli surface: Outer membrane phenotypes conferred by Lpp'-OmpA'-β-lactamase fusions. Protein Engin 9:239-247.
    • (1996) Protein Engin , vol.9 , pp. 239-247
    • Georgiou, G.1    Stephens, D.L.2    Stathopoulos, C.3    Poestshie, H.L.4    Mendenhall, J.5    Earhart, C.F.6
  • 21
    • 0031012062 scopus 로고    scopus 로고
    • Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines
    • Georgiou G, Staphopoulus C, Daugherty PS, Nayak AR, Iverson BL and Curtiss III R (1997) Display of heterologous proteins on the surface of microorganisms: From the screening of combinatorial libraries to live recombinant vaccines. Nature Biotechnol 15:29-34.
    • (1997) Nature Biotechnol , vol.15 , pp. 29-34
    • Georgiou, G.1    Staphopoulus, C.2    Daugherty, P.S.3    Nayak, A.R.4    Iverson, B.L.5    Curtiss III, R.6
  • 22
    • 0028559525 scopus 로고
    • Folding and aggregation of TEM beta-lactamase: Analogies with the formation of inclusion bodies in Escherichia coli
    • Georgiou G, Valax P, Ostermeier M and Horowitz PM (1994) Folding and aggregation of TEM beta-lactamase: Analogies with the formation of inclusion bodies in Escherichia coli. Protein Sci 3:1953-1960.
    • (1994) Protein Sci , vol.3 , pp. 953-1960
    • Georgiou, G.1    Valax, P.2    Ostermeier, M.3    Horowitz, P.M.4
  • 23
    • 0035881675 scopus 로고    scopus 로고
    • Bacterial flagellin activates basolaterally expressed TLR5 to induce epithelial proinflammatory gene expression
    • Gewirtz AT, Navas TA, Lyons S, Godowski PJ and Madara JL (2001) Bacterial flagellin activates basolaterally expressed TLR5 to induce epithelial proinflammatory gene expression. J Immunol 167:1882-1885.
    • (2001) J Immunol , vol.167 , pp. 1882-1885
    • Gewirtz, A.T.1    Navas, T.A.2    Lyons, S.3    Godowski, P.J.4    Madara, J.L.5
  • 24
    • 0032569733 scopus 로고    scopus 로고
    • Q1 to control expression of genes on high-copy-number plasmids in Escherichia coli
    • Q1 to control expression of genes on high-copy-number plasmids in Escherichia coli. Gene 223:221-231.
    • (1998) Gene , vol.223 , pp. 221-231
    • Glascock, C.B.1    Weickert, M.J.2
  • 25
    • 0023886015 scopus 로고
    • Posttranscriptional regulatory mechanisms in Escherichia coli
    • Gold L (1988) Posttranscriptional regulatory mechanisms in Escherichia coli. Annu Rev Biochem 57:199-233.
    • (1988) Annu Rev Biochem , vol.57 , pp. 199-233
    • Gold, L.1
  • 26
    • 0030033310 scopus 로고    scopus 로고
    • Differential mRNA stability of the cspA gene in the cold-shock response of Escherichia coli
    • Goldenberg D, Azar I and Oppenheim AB (1996) Differential mRNA stability of the cspA gene in the cold-shock response of Escherichia coli. Mol Microbiol 19:241-248.
    • (1996) Mol Microbiol , vol.19 , pp. 241-248
    • Goldenberg, D.1    Azar, I.2    Oppenheim, A.B.3
  • 28
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman S, Wickner S and Maurizi MR (1997) Protein quality control: Triage by chaperones and proteases. Genes Dev 11:815-823.
    • (1997) Genes Dev , vol.11 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 29
    • 0025144939 scopus 로고
    • RNA primary sequence or secondary structure in the translational initiation region controls expression of two variant interferon-β genes in Escherichia coli
    • Gross G, Mielke C, Hollatz I, Blöcker H and Frank R (1990) RNA primary sequence or secondary structure in the translational initiation region controls expression of two variant interferon-β genes in Escherichia coli. J Biol Chem 265:17627-17636.
    • (1990) J Biol Chem , vol.265 , pp. 17627-17636
    • Gross, G.1    Mielke, C.2    Hollatz, I.3    Blöcker, H.4    Frank, R.5
  • 30
    • 0242692671 scopus 로고    scopus 로고
    • Multiple sigma subunits and the partitioning of bacterial transcription space
    • Gruber TM and Gross CA (2003) Multiple sigma subunits and the partitioning of bacterial transcription space. Annu Rev Microbiol 57:441-466.
    • (2003) Annu Rev Microbiol , vol.57 , pp. 441-466
    • Gruber, T.M.1    Gross, C.A.2
  • 31
    • 0025365804 scopus 로고
    • Initiation of mRNA translation in prokaryotes
    • Gualerzi C and Pon CL (1990) Initiation of mRNA translation in prokaryotes. Biochemistry 29:5881-5889.
    • (1990) Biochemistry , vol.29 , pp. 5881-5889
    • Gualerzi, C.1    Pon, C.L.2
  • 32
    • 0028226746 scopus 로고
    • Hypervariable region IV of Salmonella gene fliC encodes a dominant surface epitope and a stabilizing factor for functional flagella
    • He XS, Rivkina M, Stocker BAD and Robinson WS (1994) Hypervariable region IV of Salmonella gene fliC encodes a dominant surface epitope and a stabilizing factor for functional flagella. J Bacteriol 176:2406-2414.
    • (1994) J Bacteriol , vol.176 , pp. 2406-2414
    • He, X.S.1    Rivkina, M.2    Stocker, B.A.D.3    Robinson, W.S.4
  • 33
    • 0037431958 scopus 로고    scopus 로고
    • Disulfide bond isomerization in prokaryotes
    • Hiniker A and Bardwell JCA (2003) Disulfide bond isomerization in prokaryotes. Biochemistry 42:1179-1185.
    • (2003) Biochemistry , vol.42 , pp. 1179-1185
    • Hiniker, A.1    Bardwell, J.C.A.2
  • 34
    • 0028533566 scopus 로고
    • Recent developments in heterologous protein production in Escherichia coli
    • Hockney RC (1994) Recent developments in heterologous protein production in Escherichia coli. Trends Biotechnol 12:456-463.
    • (1994) Trends Biotechnol , vol.12 , pp. 456-463
    • Hockney, R.C.1
  • 35
    • 0026086582 scopus 로고
    • Expression of foreign polypeptides at the Escherichia coli cell surface
    • Hofnung M (1991) Expression of foreign polypeptides at the Escherichia coli cell surface. Methods Cell Biol 34:77-105.
    • (1991) Methods Cell Biol , vol.34 , pp. 77-105
    • Hofnung, M.1
  • 36
    • 0027305038 scopus 로고
    • Chloramphenicol induces the transcription of the major cold shock gene of Escherichia coli, cspA
    • Jiang W, Jones P and Inouye M (1993) Chloramphenicol induces the transcription of the major cold shock gene of Escherichia coli, cspA. J Bacteriol 175:5824-5828.
    • (1993) J Bacteriol , vol.175 , pp. 5824-5828
    • Jiang, W.1    Jones, P.2    Inouye, M.3
  • 37
    • 0023186464 scopus 로고
    • Induction of proteins in response to low temperature in Escherichia coli
    • Jones PG, VanBogelen RA and Neidhardt FC (1987) Induction of proteins in response to low temperature in Escherichia coli. J Bacteriol 169:2092-2095.
    • (1987) J Bacteriol , vol.169 , pp. 2092-2095
    • Jones, P.G.1    VanBogelen, R.A.2    Neidhardt, F.C.3
  • 38
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust RB and Waugh DS (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 8:1668-1674.
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 39
    • 0033961548 scopus 로고    scopus 로고
    • Bacterial cell surface display of an enzyme library for selective screening of improved cellulase variants
    • Kim YS, Jung HC and Pan, JG (2000) Bacterial cell surface display of an enzyme library for selective screening of improved cellulase variants. Appl Environ Microbiol 66:788-793.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 788-793
    • Kim, Y.S.1    Jung, H.C.2    Pan, J.G.3
  • 40
    • 0034051330 scopus 로고    scopus 로고
    • Surface-displayed viral antigens on Salmonella carrier vaccine
    • Lee JS, Shin KS, Pan JG and Kim CJ (2000) Surface-displayed viral antigens on Salmonella carrier vaccine. Nat Biotechnol 18:645-648.
    • (2000) Nat Biotechnol , vol.18 , pp. 645-648
    • Lee, J.S.1    Shin, K.S.2    Pan, J.G.3    Kim, C.J.4
  • 41
    • 0035793043 scopus 로고    scopus 로고
    • RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E
    • Liou GG, Jane WN, Cohen SN, Lin NS and Lin-Chao S (2001) RNA degradosomes exist in vivo in Escherichia coli as multicomponent complexes associated with the cytoplasmic membrane via the N-terminal region of ribonuclease E. Proc Natl Acad Sci USA 98:63-68.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 63-68
    • Liou, G.G.1    Jane, W.N.2    Cohen, S.N.3    Lin, N.S.4    Lin-Chao, S.5
  • 42
    • 0024404941 scopus 로고
    • Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein
    • Liu G, Topping TB and Randall LL (1989) Physiological role during export for the retardation of folding by the leader peptide of maltose-binding protein. Proc Natl Acad Sci USA 86:9213-9217.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 9213-9217
    • Liu, G.1    Topping, T.B.2    Randall, L.L.3
  • 43
    • 0028947997 scopus 로고
    • Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusion to flagellin: A system designed for exploring protein-protein interactions
    • Lu Z, Murray KS, van Celave V, LaVallie ER, Stahl ML and McCoy JM (1995) Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusion to flagellin: A system designed for exploring protein-protein interactions. Bio/Technology 13:366-372.
    • (1995) Bio/Technology , vol.13 , pp. 366-372
    • Lu, Z.1    Murray, K.S.2    van Celave, V.3    LaVallie, E.R.4    Stahl, M.L.5    McCoy, J.M.6
  • 44
    • 0242693166 scopus 로고    scopus 로고
    • How bacteria assemble flagella
    • Macnab RM (2003) How bacteria assemble flagella. Ann Rev Microbiol 57:77-100.
    • (2003) Ann Rev Microbiol , vol.57 , pp. 77-100
    • Macnab, R.M.1
  • 45
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides SC (1996) Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol Rev 60:512-538.
    • (1996) Microbiol Rev , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 46
    • 0002753601 scopus 로고
    • Expression systems for heterologous protein production
    • Marino MH (1989) Expression systems for heterologous protein production. BioPharm 2:18-33.
    • (1989) BioPharm , vol.2 , pp. 18-33
    • Marino, M.H.1
  • 47
    • 0029920536 scopus 로고    scopus 로고
    • Efficient production of the C-terminal domain of secretory leukoprotease inhibitor as a thrombin-cleavable fusion protein in Escherichi coli
    • Masuda K, Kamimura T, Kanesaki M, Ishii K, Imaizumi A, Sugiyama T, Suzuki T and Ohtsuka E (1996) Efficient production of the C-terminal domain of secretory leukoprotease inhibitor as a thrombin-cleavable fusion protein in Escherichi coli. Protein Engin 9:101-106.
    • (1996) Protein Engin , vol.9 , pp. 101-106
    • Masuda, K.1    Kamimura, T.2    Kanesaki, M.3    Ishii, K.4    Imaizumi, A.5    Sugiyama, T.6    Suzuki, T.7    Ohtsuka, E.8
  • 48
    • 0022021846 scopus 로고
    • Translational initiation frequency of atp genes from Escherichia coli: Identification of an intercistronic sequence that enhances translation
    • McCarthy JEG, Schairer HU and Sebald W (1985) Translational initiation frequency of atp genes from Escherichia coli: Identification of an intercistronic sequence that enhances translation. EMBO J 4:519-526.
    • (1985) EMBO J , vol.4 , pp. 519-526
    • McCarthy, J.E.G.1    Schairer, H.U.2    Sebald, W.3
  • 49
    • 0022486239 scopus 로고
    • Enhancement of translation efficiency by the Escherichia coli atpE translational initiation region: Its fusion with two human genes
    • McCarthy JEG, Sebald W, Gross G and Lammers R (1986) Enhancement of translation efficiency by the Escherichia coli atpE translational initiation region: Its fusion with two human genes. Gene 41:201-206.
    • (1986) Gene , vol.41 , pp. 201-206
    • McCarthy, J.E.G.1    Sebald, W.2    Gross, G.3    Lammers, R.4
  • 50
    • 0036784636 scopus 로고    scopus 로고
    • Bacterial flagellin is an effective adjuvant for CD4+ T cells in vivo
    • McSorley SJ, Ehst BD, Yu Y and Gewirtz AT (2002). Bacterial flagellin is an effective adjuvant for CD4+ T cells in vivo. J Immunol 169:3914-3919.
    • (2002) J Immunol , vol.169 , pp. 3914-3919
    • McSorley, S.J.1    Ehst, B.D.2    Yu, Y.3    Gewirtz, A.T.4
  • 51
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas D and Raina S (1997) Protein folding in the bacterial periplasm. J Bacteriol 179:2465-2471.
    • (1997) J Bacteriol , vol.179 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 53
    • 0032883737 scopus 로고    scopus 로고
    • Cold-inducible cloning vectors for low-temperature protein expression in Escherichia coli: Application to the production of a toxic and proteolytically sensitive fusion protein
    • Mujacic M, Cooper KW and Baneyx F (1999) Cold-inducible cloning vectors for low-temperature protein expression in Escherichia coli: Application to the production of a toxic and proteolytically sensitive fusion protein. Gene 238:325-332.
    • (1999) Gene , vol.238 , pp. 325-332
    • Mujacic, M.1    Cooper, K.W.2    Baneyx, F.3
  • 55
    • 0025868732 scopus 로고
    • Expression and immunogenicity of a streptococcal M protein epitope inserted in Salmonella flagellin
    • Newton SMC, Kotb M, Poirer TP, Stocker BAD and Beachey EH (1991) Expression and immunogenicity of a streptococcal M protein epitope inserted in Salmonella flagellin. Infect Immun 59:2158-2165.
    • (1991) Infect Immun , vol.59 , pp. 2158-2165
    • Newton, S.M.C.1    Kotb, M.2    Poirer, T.P.3    Stocker, B.A.D.4    Beachey, E.H.5
  • 56
    • 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
    • Nishihara K, Kanemori M, Kitagawa M, Yanagi H and Yura T (1998) 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 64:1694-1699.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 58
    • 0028070964 scopus 로고
    • Engineering hyper-expression of bacteriophage Mu C protein by removal of secondary structure at the translation initiation region
    • Ramesh V, De A and Nagaraja V (1994) Engineering hyper-expression of bacteriophage Mu C protein by removal of secondary structure at the translation initiation region. Protein Engin 7:1053-1057.
    • (1994) Protein Engin , vol.7 , pp. 1053-1057
    • Ramesh, V.1    De, A.2    Nagaraja, V.3
  • 59
    • 0028230951 scopus 로고
    • Factor independent activation of rrnB P1-an "extended" promoter with an upstream element that dramatically increases promoter strength
    • Rao L, Ross W, Appleman JA, Gaal T, Leirmo S, Schlax PJ, Record MT and Gourse RL (1994) Factor independent activation of rrnB P1-an "extended" promoter with an upstream element that dramatically increases promoter strength. J Mol Biol 235:1421-1435.
    • (1994) J Mol Biol , vol.235 , pp. 1421-1435
    • Rao, L.1    Ross, W.2    Appleman, J.A.3    Gaal, T.4    Leirmo, S.5    Schlax, P.J.6    Record, M.T.7    Gourse, R.L.8
  • 61
    • 0345451829 scopus 로고
    • Interaction of the operator of the tryptophan operon with repressor
    • Rose JK and Yanofsky C (1974) Interaction of the operator of the tryptophan operon with repressor. Proc Natl Acad Sci USA 71:3134-3138.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 3134-3138
    • Rose, J.K.1    Yanofsky, C.2
  • 62
    • 0141727632 scopus 로고    scopus 로고
    • The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway
    • Schierle CF, Berkmen M, Huber D, Kumamoto C, Boyd D and Beckwith J (2003) The DsbA signal sequence directs efficient, cotranslational export of passenger proteins to the Escherichia coli periplasm via the signal recognition particle pathway. J Bacteriol 185:5706-5713.
    • (2003) J Bacteriol , vol.185 , pp. 5706-5713
    • Schierle, C.F.1    Berkmen, M.2    Huber, D.3    Kumamoto, C.4    Boyd, D.5    Beckwith, J.6
  • 63
    • 0016154301 scopus 로고
    • The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites
    • Shine J and Dalgarno L (1974) The 3'-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites. Proc Natl Acad Sci USA 71:1342-1346.
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 1342-1346
    • Shine, J.1    Dalgarno, L.2
  • 64
    • 0029916414 scopus 로고    scopus 로고
    • Characterization of Escherichia coli expressing an Lpp-OmpA (46159)-PhoA fusion protein localized in the outer membrane
    • Staphopoulos C, Georgiou G and Earhart CF (1996) Characterization of Escherichia coli expressing an Lpp-OmpA (46159)-PhoA fusion protein localized in the outer membrane. Appl Microbiol Biotechnol 45:112-119.
    • (1996) Appl Microbiol Biotechnol , vol.45 , pp. 112-119
    • Staphopoulos, C.1    Georgiou, G.2    Earhart, C.F.3
  • 65
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier FW (1991) Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J Mol Biol 219:37-44.
    • (1991) J Mol Biol , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 66
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier FW and Moffat BA (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189:113-130.
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffat, B.A.2
  • 67
    • 0035313153 scopus 로고    scopus 로고
    • Advances in Escherichia coli production of therapeutic proteins
    • Swartz JR (2001) Advances in Escherichia coli production of therapeutic proteins. Curr Opin Biotechnol 12:195-201.
    • (2001) Curr Opin Biotechnol , vol.12 , pp. 195-201
    • Swartz, J.R.1
  • 68
    • 0026660548 scopus 로고
    • Production of mature bovine pancreatic ribonuclease in Escherichia coli
    • Tarragona-Fiol A, Taylorson CJ, Ward JM and Rabin BR (1992) Production of mature bovine pancreatic ribonuclease in Escherichia coli. Gene 118:239-245.
    • (1992) Gene , vol.118 , pp. 239-245
    • Tarragona-Fiol, A.1    Taylorson, C.J.2    Ward, J.M.3    Rabin, B.R.4
  • 69
    • 0029786163 scopus 로고    scopus 로고
    • Protein folding in the cytoplasm of Escherichia coli: Requirements for the DnaK-DnaJ-GrpE and GroEL-GroES molecular chaperone machines
    • Thomas JG and Baneyx F (1996) Protein folding in the cytoplasm of Escherichia coli: Requirements for the DnaK-DnaJ-GrpE and GroEL-GroES molecular chaperone machines. Mol Microbiol 21:1185-1196.
    • (1996) Mol Microbiol , vol.21 , pp. 1185-1196
    • Thomas, J.G.1    Baneyx, F.2
  • 70
    • 0034945481 scopus 로고    scopus 로고
    • Investigation of the 'switch-epitope' concept with random peptide libraries displayed as thioredoxin loop fusions
    • Tripp BC, Lu ZJ, Bourque K, Sookdeo H and McCoy JM (2001) Investigation of the 'switch-epitope' concept with random peptide libraries displayed as thioredoxin loop fusions. Protein Engineering 14:367-377.
    • (2001) Protein Engineering , vol.14 , pp. 367-377
    • Tripp, B.C.1    Lu, Z.J.2    Bourque, K.3    Sookdeo, H.4    McCoy, J.M.5
  • 71
    • 0026544545 scopus 로고
    • The influence of ribosome-binding-site elements on translational efficiency in Bacillus subtilis and Escherichia coli
    • Vellanoweth RI and Rabinowitz JC (1992) The influence of ribosome-binding-site elements on translational efficiency in Bacillus subtilis and Escherichia coli. Mol Microbiol 6:1105-1114.
    • (1992) Mol Microbiol , vol.6 , pp. 1105-1114
    • Vellanoweth, R.I.1    Rabinowitz, J.C.2
  • 72
    • 0344560614 scopus 로고    scopus 로고
    • Display of polyhistidine peptides on the Escherichia coli cell surface by using outer membrane protein C as an anchoring motif
    • Xu Z and Lee SY (1999) Display of polyhistidine peptides on the Escherichia coli cell surface by using outer membrane protein C as an anchoring motif. Appl Environ Microbiol 65:5142-5147.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 5142-5147
    • Xu, Z.1    Lee, S.Y.2
  • 74
    • 0028298127 scopus 로고
    • Mutations and off-pathway aggregation of proteins
    • Wetzel R (1994) Mutations and off-pathway aggregation of proteins. Trends Biotechnol 12:193-198.
    • (1994) Trends Biotechnol , vol.12 , pp. 193-198
    • Wetzel, R.1
  • 75
    • 0022534386 scopus 로고
    • Identification of a positive retro-regulator that stabilizes mRNAs in bacteria
    • Wong HC and Chang S (1986) Identification of a positive retro-regulator that stabilizes mRNAs in bacteria. Proc Natl Acad Sci USA 83:3233-3237.
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 3233-3237
    • Wong, H.C.1    Chang, S.2


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