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Volumn 64, Issue 5, 2004, Pages 625-635

Secretory and extracellular production of recombinant proteins using Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI PROTEIN; RECOMBINANT PROTEIN;

EID: 3042660198     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-004-1559-9     Document Type: Short Survey
Times cited : (521)

References (76)
  • 1
    • 0035812882 scopus 로고    scopus 로고
    • Export of Thermits thermophilus alkaline phosphatase via the twin-arginine translocation pathway in Escherichia coli
    • Angelini S, Moreno R, Gouffi K, Santini C, Yamagishi A, Berenguer J, Wu L (2001) Export of Thermits thermophilus alkaline phosphatase via the twin-arginine translocation pathway in Escherichia coli. FEBS Lett 506:103-107
    • (2001) FEBS Lett , vol.506 , pp. 103-107
    • Angelini, S.1    Moreno, R.2    Gouffi, K.3    Santini, C.4    Yamagishi, A.5    Berenguer, J.6    Wu, L.7
  • 2
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • Arie J, Sassoon N, Betton J (2001) Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol Microbiol 39:199-210
    • (2001) Mol Microbiol , vol.39 , pp. 199-210
    • Arie, J.1    Sassoon, N.2    Betton, J.3
  • 3
    • 0037414423 scopus 로고    scopus 로고
    • Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli
    • Barrett CML, Ray N, Thomas JD, Robinson C, Bolhuis A (2003) Quantitative export of a reporter protein, GFP, by the twin-arginine translocation pathway in Escherichia coli. Biochem Biophys Res Comm 304:279-284
    • (2003) Biochem Biophys Res Comm , vol.304 , pp. 279-284
    • Barrett, C.M.L.1    Ray, N.2    Thomas, J.D.3    Robinson, C.4    Bolhuis, A.5
  • 4
    • 2642652226 scopus 로고    scopus 로고
    • Selection for a periplasmic factor improving phage display and periplasmic expression
    • Bothmann H, Pluckthun A (1998) Selection for a periplasmic factor improving phage display and periplasmic expression. Nat Biotechnol 16:376-380
    • (1998) Nat Biotechnol , vol.16 , pp. 376-380
    • Bothmann, H.1    Pluckthun, A.2
  • 5
    • 0039423955 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA
    • Bothmann H, Pluckthun A (2000) The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. J Biol Chem 275:17100-17105
    • (2000) J Biol Chem , vol.275 , pp. 17100-17105
    • Bothmann, H.1    Pluckthun, A.2
  • 6
    • 0035014528 scopus 로고    scopus 로고
    • Isolation of high-affinity ligand-binding proteins by periplasmic expression with cytometric screening (PECS)
    • Chen G, Hayhurst A, Thomas JG, Garvey BR, Iverson BL, Georgiou G (2001) Isolation of high-affinity ligand-binding proteins by periplasmic expression with cytometric screening (PECS). Nat Biotechnol 19:537-542
    • (2001) Nat Biotechnol , vol.19 , pp. 537-542
    • Chen, G.1    Hayhurst, A.2    Thomas, J.G.3    Garvey, B.R.4    Iverson, B.L.5    Georgiou, G.6
  • 7
    • 0033935592 scopus 로고    scopus 로고
    • Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using the Bacillus sp. Endoxylanase signal sequence
    • Choi JH, Jeong KJ, Kim SC, Lee SY (2000) Efficient secretory production of alkaline phosphatase by high cell density culture of recombinant Escherichia coli using the Bacillus sp. Endoxylanase signal sequence. Appl Microbiol Biotechnol 53:640-645
    • (2000) Appl Microbiol Biotechnol , vol.53 , pp. 640-645
    • Choi, J.H.1    Jeong, K.J.2    Kim, S.C.3    Lee, S.Y.4
  • 8
    • 0028371166 scopus 로고
    • An expression system for secretion and purification of a genetically engineered thermostable chimera of protein A and alkaline phosphatase
    • Chowdhury PS, Kushwaha A, Abrol S, Chaudhary VK (1994) An expression system for secretion and purification of a genetically engineered thermostable chimera of protein A and alkaline phosphatase. Protein Expr Purif 5:89-95
    • (1994) Protein Expr Purif , vol.5 , pp. 89-95
    • Chowdhury, P.S.1    Kushwaha, A.2    Abrol, S.3    Chaudhary, V.K.4
  • 9
    • 0344404180 scopus 로고    scopus 로고
    • Overproduction of human granulocyte-colony stimulating factor fused to the PeIB signal peptide in Escherichia coli
    • Chung BH, Sohn M, Oh S, Park U, Poo H, Kim BS, Yu MJ, Lee SK (1998) Overproduction of human granulocyte-colony stimulating factor fused to the PeIB signal peptide in Escherichia coli. J Perm Bioeng 85:443-446
    • (1998) J Perm Bioeng , vol.85 , pp. 443-446
    • Chung, B.H.1    Sohn, M.2    Oh, S.3    Park, U.4    Poo, H.5    Kim, B.S.6    Yu, M.J.7    Lee, S.K.8
  • 10
    • 0029447952 scopus 로고
    • Expression of soluble human interleukin-2 receptor α-chain in Escherichia coli
    • Dracheva S, Palermo RE, Powers GD, Waugh DS (1995) Expression of soluble human interleukin-2 receptor α-chain in Escherichia coli. Protein Expr Purif 6:737-747
    • (1995) Protein Expr Purif , vol.6 , pp. 737-747
    • Dracheva, S.1    Palermo, R.E.2    Powers, G.D.3    Waugh, D.S.4
  • 11
    • 0033760702 scopus 로고    scopus 로고
    • Specific secretion of active single-chain Fv antibodies into the supernatants of Escherichia coli cultures by use of the hemolysin system
    • Fernandez LA, Sola I, Enjuanes L, De Lorenzo V (2000) Specific secretion of active single-chain Fv antibodies into the supernatants of Escherichia coli cultures by use of the hemolysin system. Appl Environ Microbiol 66:5024-5029
    • (2000) Appl Environ Microbiol , vol.66 , pp. 5024-5029
    • Fernandez, L.A.1    Sola, I.2    Enjuanes, L.3    De Lorenzo, V.4
  • 12
    • 0344950388 scopus 로고    scopus 로고
    • Secretory expression in Escherichia coli and single-step purification of a heat-stable alkaline protease
    • Fu Z, Hamid SBA, Razak CAN, Basri M, Salleh AB, Rahman RNZA (2003) Secretory expression in Escherichia coli and single-step purification of a heat-stable alkaline protease. Protein Expr Purif 28:63-68
    • (2003) Protein Expr Purif , vol.28 , pp. 63-68
    • Fu, Z.1    Hamid, S.B.A.2    Razak, C.A.N.3    Basri, M.4    Salleh, A.B.5    Rahman, R.N.Z.A.6
  • 14
    • 0033954498 scopus 로고    scopus 로고
    • Signal sequence and alanine-rich region of streptococcal protein antigen A of Streptococcus sobrinus can direct localization of alkaline phosphatase to the periplasm of Escherichia coli
    • Holt RG, Raju L (2000) Signal sequence and alanine-rich region of streptococcal protein antigen A of Streptococcus sobrinus can direct localization of alkaline phosphatase to the periplasm of Escherichia coli. FEMS Microbiol Lett 184:17-21
    • (2000) FEMS Microbiol Lett , vol.184 , pp. 17-21
    • Holt, R.G.1    Raju, L.2
  • 15
    • 0032747757 scopus 로고    scopus 로고
    • Extracellular secretion of levansucrase from Zymomonas mobilis in Escherichia coli
    • Jang KH, Seo KB, Song KB, Kim CH, Rhee SK (1999) Extracellular secretion of levansucrase from Zymomonas mobilis in Escherichia coli. Bioproc Eng 21:453-458
    • (1999) Bioproc Eng , vol.21 , pp. 453-458
    • Jang, K.H.1    Seo, K.B.2    Song, K.B.3    Kim, C.H.4    Rhee, S.K.5
  • 16
    • 0032524530 scopus 로고    scopus 로고
    • Molecular cloning and characterization of an endoxylanase gene of Bacillus sp. in Escherichia coli
    • Jeong KJ, Lee PC, Park IY, Kim MS, Kim SC (1998) Molecular cloning and characterization of an endoxylanase gene of Bacillus sp. in Escherichia coli. Enzyme Microb Technol 22 (7):599-605
    • (1998) Enzyme Microb Technol , vol.22 , Issue.7 , pp. 599-605
    • Jeong, K.J.1    Lee, P.C.2    Park, I.Y.3    Kim, M.S.4    Kim, S.C.5
  • 17
    • 0034135428 scopus 로고    scopus 로고
    • Secretory production of human leptin in Escherichia coli
    • Jeong KJ, Lee SY (2000) Secretory production of human leptin in Escherichia coli. Biotechnol Bioeng 67:398-407
    • (2000) Biotechnol Bioeng , vol.67 , pp. 398-407
    • Jeong, K.J.1    Lee, S.Y.2
  • 18
    • 0034761654 scopus 로고    scopus 로고
    • Secretory production of human granulocyte colony-stimulating factor in Escherichia coli
    • Jeong KJ, Lee SY (2001) Secretory production of human granulocyte colony-stimulating factor in Escherichia coli. Protein Expr Purif 23(2):311-8
    • (2001) Protein Expr Purif , vol.23 , Issue.2 , pp. 311-318
    • Jeong, K.J.1    Lee, S.Y.2
  • 19
    • 0036793640 scopus 로고    scopus 로고
    • Excretory production of human β-endorphin into culture medium by using outer membrane protein F as a fusion partner in recombinant Escherichia coli
    • Jeong KJ, Lee SY (2002) Excretory production of human β-endorphin into culture medium by using outer membrane protein F as a fusion partner in recombinant Escherichia coli. Appl Environ Microbiol 68:4979-4985
    • (2002) Appl Environ Microbiol , vol.68 , pp. 4979-4985
    • Jeong, K.J.1    Lee, S.Y.2
  • 20
    • 0031280495 scopus 로고    scopus 로고
    • Construction and characterization of versatile cloning vectors for efficient delivery of native foreign proteins to the periplasm of Escherichia coli
    • Jobling MG, Palmer LM, Erbe JL, Holmes RK (1997) Construction and characterization of versatile cloning vectors for efficient delivery of native foreign proteins to the periplasm of Escherichia coli. Plasmid 38(3):158-73
    • (1997) Plasmid , vol.38 , Issue.3 , pp. 158-173
    • Jobling, M.G.1    Palmer, L.M.2    Erbe, J.L.3    Holmes, R.K.4
  • 21
    • 0034731481 scopus 로고    scopus 로고
    • Targeting of active human cytochrome P4501A1 (CYP1A1) to the periplasmic space of Escherichia coli
    • Kaderbhai MA, Ugochukwu CC, Lamb DC, Kelly S (2000) Targeting of active human cytochrome P4501A1 (CYP1A1) to the periplasmic space of Escherichia coli. Biochem Biophys Res Comm 279:803-807
    • (2000) Biochem Biophys Res Comm , vol.279 , pp. 803-807
    • Kaderbhai, M.A.1    Ugochukwu, C.C.2    Lamb, D.C.3    Kelly, S.4
  • 23
    • 0037899477 scopus 로고    scopus 로고
    • Optimization of the extracellular production of a bacterial phytase with Escherichia coli by using different fedbatch fermentation strategies
    • Kleist S, Miksch G, Hitzmann B, Arndt M, Friehs K, Flaschel E (2003) Optimization of the extracellular production of a bacterial phytase with Escherichia coli by using different fedbatch fermentation strategies. Appl Microbiol Biotechnol 61:456-462
    • (2003) Appl Microbiol Biotechnol , vol.61 , pp. 456-462
    • Kleist, S.1    Miksch, G.2    Hitzmann, B.3    Arndt, M.4    Friehs, K.5    Flaschel, E.6
  • 24
    • 0031973556 scopus 로고    scopus 로고
    • Expression and secretion of functional miniantibodies McPC603scFvDhlx in cell-wall-less L-form strains of Proteus mirabilis and Escherichia coli: A comparison of the synthesis capacities of L-form strains with an E. coli producer strain
    • Kujau MJ, Hoischen C, Riesenberg D, Gumpert J (1998) Expression and secretion of functional miniantibodies McPC603scFvDhlx in cell-wall-less L-form strains of Proteus mirabilis and Escherichia coli: A comparison of the synthesis capacities of L-form strains with an E. coli producer strain. Appl Microbiol Biotechnol 49:51-58
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 51-58
    • Kujau, M.J.1    Hoischen, C.2    Riesenberg, D.3    Gumpert, J.4
  • 25
    • 0035957961 scopus 로고    scopus 로고
    • Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli
    • Kurokawa Y, Yanagi H, Yura T (2001) Overproduction of bacterial protein disulfide isomerase (DsbC) and its modulator (DsbD) markedly enhances periplasmic production of human nerve growth factor in Escherichia coli. J Biol Chem 276:14393-14399
    • (2001) J Biol Chem , vol.276 , pp. 14393-14399
    • Kurokawa, Y.1    Yanagi, H.2    Yura, T.3
  • 26
    • 0031148990 scopus 로고    scopus 로고
    • Enhancement of extracellular production of a Cellulomonas fimi exoglucanase in Escherichia coli by the reduction of promoter strength
    • Lam T, Wong RSC, Wong WR (1997) Enhancement of extracellular production of a Cellulomonas fimi exoglucanase in Escherichia coli by the reduction of promoter strength. Enzyme Microb Technol 20:482-488
    • (1997) Enzyme Microb Technol , vol.20 , pp. 482-488
    • Lam, T.1    Wong, R.S.C.2    Wong, W.R.3
  • 27
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar SW, Kolter R (1996) SurA assists the folding of Escherichia coli outer membrane proteins. J Bacteriol 178:1770-1773
    • (1996) J Bacteriol , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 28
    • 0030000710 scopus 로고    scopus 로고
    • Increased efficiency of alkaline phosphatase production levels in Escherichia coli using a degenerate PelB signal sequence
    • Le Calvez H, Green JM, Baty D (1996) Increased efficiency of alkaline phosphatase production levels in Escherichia coli using a degenerate PelB signal sequence. Gene 170:51-55
    • (1996) Gene , vol.170 , pp. 51-55
    • Le Calvez, H.1    Green, J.M.2    Baty, D.3
  • 29
    • 0035916409 scopus 로고    scopus 로고
    • Secretory production of Arthrobacter levan fructotransferase from recombinant Escherichia coli
    • Lee J, Saraswat V, Koh I, Song KB, Park YH, Rhee SK (2001) Secretory production of Arthrobacter levan fructotransferase from recombinant Escherichia coli. FEMS Microbiol Lett 195 (2): 127-132
    • (2001) FEMS Microbiol Lett , vol.195 , Issue.2 , pp. 127-132
    • Lee, J.1    Saraswat, V.2    Koh, I.3    Song, K.B.4    Park, Y.H.5    Rhee, S.K.6
  • 30
    • 0031884604 scopus 로고    scopus 로고
    • High level secetion of recombinant staphylokinase into periplasm of Escherichia coli
    • Lee SJ, Kim IC, Kim DM, Bae KH, Byun SM (1998) High level secetion of recombinant staphylokinase into periplasm of Escherichia coli. Biotechnol Lett 20:113-116
    • (1998) Biotechnol Lett , vol.20 , pp. 113-116
    • Lee, S.J.1    Kim, I.C.2    Kim, D.M.3    Bae, K.H.4    Byun, S.M.5
  • 31
    • 0029874193 scopus 로고    scopus 로고
    • High cell density cultivation of Escherichia coli
    • Lee SY (1996) High cell density cultivation of Escherichia coli. Trends Biotechnol 14:98-105
    • (1996) Trends Biotechnol , vol.14 , pp. 98-105
    • Lee, S.Y.1
  • 32
    • 0036412057 scopus 로고    scopus 로고
    • Cloning and hemolysin-mediated secretory expression of a codon-optimized synthetic human interleukin-6 gene in Escherichia coli
    • Li Y, Chen CX, von Specht B, Hahn HP (2002) Cloning and hemolysin-mediated secretory expression of a codon-optimized synthetic human interleukin-6 gene in Escherichia coli. Gene 25:437-447
    • (2002) Gene , vol.25 , pp. 437-447
    • Li, Y.1    Chen, C.X.2    Von Specht, B.3    Hahn, H.P.4
  • 33
    • 0035919127 scopus 로고    scopus 로고
    • DegP-coexpression minimizes inclusion-body formation upon overproduction of recombinant penicillin acylase in Escherichia coli
    • Lin W, Huang S, Chou CP (2001a) DegP-coexpression minimizes inclusion-body formation upon overproduction of recombinant penicillin acylase in Escherichia coli. Biotechnol Bioeng 73:484-492
    • (2001) Biotechnol Bioeng , vol.73 , pp. 484-492
    • Lin, W.1    Huang, S.2    Chou, C.P.3
  • 34
    • 0034794414 scopus 로고    scopus 로고
    • High-level extracellular production of penicillin acylase by genetic engineering of Escherichia coli
    • Lin W, Huang S, Chou CP (2001b) High-level extracellular production of penicillin acylase by genetic engineering of Escherichia coli. J Chem Technol Biotechnol 76:1030-1037
    • (2001) J Chem Technol Biotechnol , vol.76 , pp. 1030-1037
    • Lin, W.1    Huang, S.2    Chou, C.P.3
  • 35
    • 0035996719 scopus 로고    scopus 로고
    • Using secretion to solve a solubility problem: High-yield expression in Escherichia coli and purification of the bacterial glycoamidase PNGase F
    • Loo T, Patchett ML, Norris GE, Lott JS (2002) Using secretion to solve a solubility problem: high-yield expression in Escherichia coli and purification of the bacterial glycoamidase PNGase F. Protein Expr Purif 24:90-98
    • (2002) Protein Expr Purif , vol.24 , pp. 90-98
    • Loo, T.1    Patchett, M.L.2    Norris, G.E.3    Lott, J.S.4
  • 37
    • 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
  • 38
    • 0036883453 scopus 로고    scopus 로고
    • Efficient secretory overexpression of Bacillus subtilis pectate lyase in Escherichia coli and single-step purification
    • Matsumoto T, Katsura D, Kondo A, Fukuda H (2002) Efficient secretory overexpression of Bacillus subtilis pectate lyase in Escherichia coli and single-step purification. Biochem Eng J 12 (3):175-179
    • (2002) Biochem Eng J , vol.12 , Issue.3 , pp. 175-179
    • Matsumoto, T.1    Katsura, D.2    Kondo, A.3    Fukuda, H.4
  • 40
    • 0031024552 scopus 로고    scopus 로고
    • Extracellular production of a hybrid β-glucanase from Bacillus by Escherichia coli under different cultivation conditions in snaking cultures and bioreactors
    • Miksch G, Neitzel R, Fiedler E, Friehs K, Flaschel E (1997) Extracellular production of a hybrid β-glucanase from Bacillus by Escherichia coli under different cultivation conditions in snaking cultures and bioreactors. Appl Microbiol Biotechnol 47:120-126
    • (1997) Appl Microbiol Biotechnol , vol.47 , pp. 120-126
    • Miksch, G.1    Neitzel, R.2    Fiedler, E.3    Friehs, K.4    Flaschel, E.5
  • 41
    • 0036383441 scopus 로고    scopus 로고
    • Overexpression of the phytase from Escherichia coli and its extracellular production in bioreactors
    • Miksch G, Kleist S, Friehs K, Flaschel E (2002) Overexpression of the phytase from Escherichia coli and its extracellular production in bioreactors. Appl Microbiol Biotechnol 56:685-694
    • (2002) Appl Microbiol Biotechnol , vol.56 , pp. 685-694
    • Miksch, G.1    Kleist, S.2    Friehs, K.3    Flaschel, E.4
  • 42
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas D, Betton JM, Raina S (1996) New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH. Mol Microbiol 21:871-884.
    • (1996) Mol Microbiol , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 43
    • 0022427799 scopus 로고
    • Secretion into the culture medium of a foreign gene product from Escherichia coli: Use of the ompF gene for secretion of human β-endorphin
    • Nagahari K, Kanaya S, Munakata D, Aoyagi Y, Mizushima S (1985) Secretion into the culture medium of a foreign gene product from Escherichia coli: use of the ompF gene for secretion of human β-endorphin. EMBO J 16:3589-3592
    • (1985) EMBO J , vol.16 , pp. 3589-3592
    • Nagahari, K.1    Kanaya, S.2    Munakata, D.3    Aoyagi, Y.4    Mizushima, S.5
  • 44
    • 0345491422 scopus 로고    scopus 로고
    • Secretory production of recombinant protein by a high cell density culture of a protease negative mutant Escherichia coli
    • Park SJ, Georgiou G, Lee SY (1999) Secretory production of recombinant protein by a high cell density culture of a protease negative mutant Escherichia coli. Biotechnol Prog 15:164-167
    • (1999) Biotechnol Prog , vol.15 , pp. 164-167
    • Park, S.J.1    Georgiou, G.2    Lee, S.Y.3
  • 45
    • 0030590390 scopus 로고    scopus 로고
    • Production of the beta-subunit of human chorionic gonadotropin in Escherichia coli and its export mediated by the heat-labile enterotoxin chain-B signal sequence
    • Pillai D, Dixit A, Krishnan T, Garg LC (1996) Production of the beta-subunit of human chorionic gonadotropin in Escherichia coli and its export mediated by the heat-labile enterotoxin chain-B signal sequence. Gene 173(2):271-274
    • (1996) Gene , vol.173 , Issue.2 , pp. 271-274
    • Pillai, D.1    Dixit, A.2    Krishnan, T.3    Garg, L.C.4
  • 46
    • 0031841932 scopus 로고    scopus 로고
    • Efficient of signal peptide changes on the extracellular processing of streptokinase form Escherichia coli requirement for secondary structure at the cleavage junction
    • Pratap J, Dikshit KL (1998) Efficient of signal peptide changes on the extracellular processing of streptokinase form Escherichia coli requirement for secondary structure at the cleavage junction. Mol Gen Genet 258:326-333
    • (1998) Mol Gen Genet , vol.258 , pp. 326-333
    • Pratap, J.1    Dikshit, K.L.2
  • 47
    • 0031572185 scopus 로고    scopus 로고
    • A general strategy for the expression of recombinant human cytochrome P450 s in Escherichia coli using bacterial signal peptides: Expression of CYP3A4, CYP2A6, and CYP2E1
    • Pritchard MP, Ossetian R, Li DN, Henderson CJ, Burchell B, Wolf CR, Friedberg T (1997) A general strategy for the expression of recombinant human cytochrome P450 s in Escherichia coli using bacterial signal peptides: Expression of CYP3A4, CYP2A6, and CYP2E1. Arch Biochem Biophys 345:342-354
    • (1997) Arch Biochem Biophys , vol.345 , pp. 342-354
    • Pritchard, M.P.1    Ossetian, R.2    Li, D.N.3    Henderson, C.J.4    Burchell, B.5    Wolf, C.R.6    Friedberg, T.7
  • 48
    • 0027450561 scopus 로고
    • The complete general secretory pathway in gram-negative bacteria
    • Pugsley AP (1993) The complete general secretory pathway in gram-negative bacteria. Microbiol Rev 57:50-108
    • (1993) Microbiol Rev , vol.57 , pp. 50-108
    • Pugsley, A.P.1
  • 49
    • 0035143586 scopus 로고    scopus 로고
    • Disulfide bonds formation in secretion component PulK provides a possible explanation for the role of DsbA in pullulanase secretion
    • Pugsley AP, Bayan N, Sauvonnet N (2001) Disulfide bonds formation in secretion component PulK provides a possible explanation for the role of DsbA in pullulanase secretion. J Bacteriol 183:1312-1319
    • (2001) J Bacteriol , vol.183 , pp. 1312-1319
    • Pugsley, A.P.1    Bayan, N.2    Sauvonnet, N.3
  • 50
    • 0031736826 scopus 로고    scopus 로고
    • Expression of active human tissue-type plasminogen activator in Escherichia coli
    • Qui J, Swartz JR, Georgiou G (1998) Expression of active human tissue-type plasminogen activator in Escherichia coli. Appl Environ Microbiol 64:4891-4896
    • (1998) Appl Environ Microbiol , vol.64 , pp. 4891-4896
    • Qui, J.1    Swartz, J.R.2    Georgiou, G.3
  • 51
    • 0030971043 scopus 로고    scopus 로고
    • Overproduction of fungal ribotoxin α-sarcin in Escherichia coli: Generation of an active immunotoxin
    • Rathore D, Nayak SK, Batra JK (1997) Overproduction of fungal ribotoxin α-sarcin inEscherichia coli: generation of an active immunotoxin. Gene 190:31-35
    • (1997) Gene , vol.190 , pp. 31-35
    • Rathore, D.1    Nayak, S.K.2    Batra, J.K.3
  • 52
    • 0031766998 scopus 로고    scopus 로고
    • Procaryotic expression of single-chain variable-fragment (scFv) antibodies: Secretion in L-form cells of Proteus mirabilis leads to active product and overcomes the limitations of periplasmic expression in Escherichia coli
    • Rippmann JF, Klein M, Hoischen C, Brocks B, Rettig WJ, Gumpert J, Pfizenmaier K, Mattes R, Moosmayer D (1998) Procaryotic expression of single-chain variable-fragment (scFv) antibodies: secretion in L-form cells of Proteus mirabilis leads to active product and overcomes the limitations of periplasmic expression in Escherichia coli. Appl Environ Microbiol 64(12):4862-4869.
    • (1998) Appl Environ Microbiol , vol.64 , Issue.12 , pp. 4862-4869
    • Rippmann, J.F.1    Klein, M.2    Hoischen, C.3    Brocks, B.4    Rettig, W.J.5    Gumpert, J.6    Pfizenmaier, K.7    Mattes, R.8    Moosmayer, D.9
  • 53
    • 0029346949 scopus 로고
    • Production of soluble and active recombinant murine interleukin-2 in Escherichia coli: High level expression, Kil-induced release, and purification
    • Robbens J, Raeymaekers A, Steidler L, Fiers W, Remaut E (1995) Production of soluble and active recombinant murine interleukin-2 in Escherichia coli: high level expression, Kil-induced release, and purification. Protein Expr Purif 6(4):481-486
    • (1995) Protein Expr Purif , vol.6 , Issue.4 , pp. 481-486
    • Robbens, J.1    Raeymaekers, A.2    Steidler, L.3    Fiers, W.4    Remaut, E.5
  • 54
    • 0031895304 scopus 로고    scopus 로고
    • High-level expression of the thermoalkanophilic lipase from Bacillus thermocatenulatus in Escherichia coli
    • Rua ML, Atomi H, Schmidt-Dannert C, Schmid RD (1998) High-level expression of the thermoalkanophilic lipase from Bacillus thermocatenulatus in Escherichia coli. Appl Microbiol Biotechnol 49:405-410
    • (1998) Appl Microbiol Biotechnol , vol.49 , pp. 405-410
    • Rua, M.L.1    Atomi, H.2    Schmidt-Dannert, C.3    Schmid, R.D.4
  • 55
    • 0035896573 scopus 로고    scopus 로고
    • Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock
    • Santini C, Bernadac A, Zhang M, Chanal A, Ize B, Blanco C, Wu L (2001) Translocation of jellyfish green fluorescent protein via the Tat system of Escherichia coli and change of its periplasmic localization in response to osmotic up-shock. J Biol Chem 276:8159-8164
    • (2001) J Biol Chem , vol.276 , pp. 8159-8164
    • Santini, C.1    Bernadac, A.2    Zhang, M.3    Chanal, A.4    Ize, B.5    Blanco, C.6    Wu, L.7
  • 56
    • 0037294121 scopus 로고    scopus 로고
    • Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli
    • Shokri A, Saden AM and Larsson G (2003) Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli. Appl Microbial Biotechnol 60:654-664
    • (2003) Appl Microbial Biotechnol , vol.60 , pp. 654-664
    • Shokri, A.1    Saden, A.M.2    Larsson, G.3
  • 58
    • 0030916974 scopus 로고    scopus 로고
    • Localization and characterization of inclusion bodies in recombinant Escherichia coli cells overproducing penicillin G acylase
    • Sriubolmas N, Panbangred W, Sriurairatana S, Meevootisom V (1997) Localization and characterization of inclusion bodies in recombinant Escherichia coli cells overproducing penicillin G acylase. Appl Microbiol Biotechnol 47:373-378
    • (1997) Appl Microbiol Biotechnol , vol.47 , pp. 373-378
    • Sriubolmas, N.1    Panbangred, W.2    Sriurairatana, S.3    Meevootisom, V.4
  • 59
    • 0037199161 scopus 로고    scopus 로고
    • A strategy for in vivo screening of subtilisin E reaction specificity in E. coli periplasm
    • Sroga GE, Dordick J (2002) A strategy for in vivo screening of subtilisin E reaction specificity in E. coli periplasm. Biotechnol Bioeng 78:761-769
    • (2002) Biotechnol Bioeng , vol.78 , pp. 761-769
    • Sroga, G.E.1    Dordick, J.2
  • 60
    • 0036412087 scopus 로고    scopus 로고
    • Efficient expression and secretion of recombinant hirudin III in E. coli using the L-asparaginase II signal sequence
    • Tan S, Wu W, Liu J, Kong Y, Pu Y, Yuan R (2002) Efficient expression and secretion of recombinant hirudin III in E. coli using the L-asparaginase II signal sequence. Protein Expr Purif 25:430-436
    • (2002) Protein Expr Purif , vol.25 , pp. 430-436
    • Tan, S.1    Wu, W.2    Liu, J.3    Kong, Y.4    Pu, Y.5    Yuan, R.6
  • 61
    • 0036308536 scopus 로고    scopus 로고
    • Secretory production of recombinant human C-reactive protein in Escherichia coli, capable of binding with phosphorylcholine, and its characterization
    • Tanaka T, Horio T, Matuo Y (2002) Secretory production of recombinant human C-reactive protein in Escherichia coli, capable of binding with phosphorylcholine, and its characterization. Biochem Biophys Res Commun, 295(1):163-6
    • (2002) Biochem Biophys Res Commun , vol.295 , Issue.1 , pp. 163-166
    • Tanaka, T.1    Horio, T.2    Matuo, Y.3
  • 62
    • 0035181362 scopus 로고    scopus 로고
    • Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli
    • Thomas JD, Daniel RA, Errington J, Robinson C (2001) Export of active green fluorescent protein to the periplasm by the twin-arginine translocase (Tat) pathway in Escherichia coli. Mol Microbiol 39:47-53
    • (2001) Mol Microbiol , vol.39 , pp. 47-53
    • Thomas, J.D.1    Daniel, R.A.2    Errington, J.3    Robinson, C.4
  • 63
    • 0036310642 scopus 로고    scopus 로고
    • High-level production of TagI restriction endonuclease by three different expression systems in Escherichia coli cells using the T7 phage promoter
    • Toksoy E, Onsan ZI, Kirdar B (2002) High-level production of TagI restriction endonuclease by three different expression systems in Escherichia coli cells using the T7 phage promoter. Appl Microbiol Biotechnol 59:239-245
    • (2002) Appl Microbiol Biotechnol , vol.59 , pp. 239-245
    • Toksoy, E.1    Onsan, Z.I.2    Kirdar, B.3
  • 64
    • 0034065261 scopus 로고    scopus 로고
    • Extracelllular expression, purification, and characterization of a winter flounder antifreeze polypeptide form Escherichia coli
    • Tong L, Lin Q, Wong WKR, Ali A, Lim D, Sung WL, Hew CL, Yang DSC (2000) Extracelllular expression, purification, and characterization of a winter flounder antifreeze polypeptide form Escherichia coli. Protein Expr Purif 18:175-181
    • (2000) Protein Expr Purif , vol.18 , pp. 175-181
    • Tong, L.1    Lin, Q.2    Wong, W.K.R.3    Ali, A.4    Lim, D.5    Sung, W.L.6    Hew, C.L.7    Yang, D.S.C.8
  • 66
    • 0029557883 scopus 로고
    • Optimization of bacteriocin-release-protein-induced protein release by Escherichia coli: Extracellular production of the periplasmic molecular chaperone FaeE
    • Van der Wal FJ, ten Hagen-Jounman CM, Oudega B, Luirink J (1995) Optimization of bacteriocin-release-protein-induced protein release by Escherichia coli: extracellular production of the periplasmic molecular chaperone FaeE. Appl Microbiol Biotechnol 44:459-465
    • (1995) Appl Microbiol Biotechnol , vol.44 , pp. 459-465
    • Van Der Wal, F.J.1    Ten Hagen-Jounman, C.M.2    Oudega, B.3    Luirink, J.4
  • 67
    • 0031890506 scopus 로고    scopus 로고
    • Optimization of bacterocin release protein (BRP)-mediated protein release by Escherichia coli: Random mutagenesis of the pCloDF13-Derived BRP gene to uncouple lethality and quasi-lysis from protein release
    • Van der Wal FJ, Koningstein G, ten Hagen CM, Oudega B, Luirink J (1998) Optimization of bacterocin release protein (BRP)-mediated protein release by Escherichia coli: random mutagenesis of the pCloDF13-Derived BRP gene to uncouple lethality and quasi-lysis from protein release. Appl Environ Microbiol 64:392-398
    • (1998) Appl Environ Microbiol , vol.64 , pp. 392-398
    • Van Der Wal, F.J.1    Koningstein, G.2    Ten Hagen, C.M.3    Oudega, B.4    Luirink, J.5
  • 68
    • 0032190602 scopus 로고    scopus 로고
    • To1AIII co-expression facilitates the recovery of periplasmic recombinant proteins into the growth medium of Escherichia coli
    • Wan EW, Baneyx F (1998) To1AIII co-expression facilitates the recovery of periplasmic recombinant proteins into the growth medium of Escherichia coli. Protein Expr Purif 14:13-22
    • (1998) Protein Expr Purif , vol.14 , pp. 13-22
    • Wan, E.W.1    Baneyx, F.2
  • 69
    • 0034736407 scopus 로고    scopus 로고
    • Increased production of human proinsulin in the periplasmic space of Escherichia coli by fusion to DsbA
    • Winter J, Neubauer P, Glockshuber R, Rudolph R (2000) Increased production of human proinsulin in the periplasmic space of Escherichia coli by fusion to DsbA. J Biotechnol 84(2):175-185
    • (2000) J Biotechnol , vol.84 , Issue.2 , pp. 175-185
    • Winter, J.1    Neubauer, P.2    Glockshuber, R.3    Rudolph, R.4
  • 70
    • 0037855913 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of diuretic hormone Manduca diuresin from Manduca sexta in Escherichia coli
    • Wong WR, Ali AB, Ma MC (2003) Cloning, expression, and characterization of diuretic hormone Manduca diuresin from Manduca sexta in Escherichia coli. Protein Expr Purif 29:51-57
    • (2003) Protein Expr Purif , vol.29 , pp. 51-57
    • Wong, W.R.1    Ali, A.B.2    Ma, M.C.3
  • 71
    • 0030897393 scopus 로고    scopus 로고
    • Efficient production of heat-labile endotoxin mutant proteins by overexpression of dabA in adegP-deficient Escherichia constrain
    • Wulfing C, Rappuoli R (1997) Efficient production of heat-labile endotoxin mutant proteins by overexpression of dabA in adegP-deficient Escherichia constrain. Arch Microbiol 167:280-283
    • (1997) Arch Microbiol , vol.167 , pp. 280-283
    • Wulfing, C.1    Rappuoli, R.2
  • 72
    • 0036447586 scopus 로고    scopus 로고
    • High-level expression and secretion of recombinant mouse endostatin by Escherichia coli
    • Xu R, Du P, Fan JJ, Zhang Q, Li TP, Gan RB (2002) High-level expression and secretion of recombinant mouse endostatin by Escherichia coli. Protein Expr Purif 24:453-459
    • (2002) Protein Expr Purif , vol.24 , pp. 453-459
    • Xu, R.1    Du, P.2    Fan, J.J.3    Zhang, Q.4    Li, T.P.5    Gan, R.B.6
  • 73
    • 0031904157 scopus 로고    scopus 로고
    • One hundred Seventy-fold increase in excretion of an FV frangmant tumor necrosis factor alpha fusion protein (SFV/TNF-α) from Escherichia coli caused by the synergistic effects of glycine and triton X-100
    • Yang J, Moyana T, Mackenzie S, Xia Q and Xiang J (1998) One hundred Seventy-fold increase in excretion of an FV frangmant tumor necrosis factor alpha fusion protein (SFV/TNF-α) from Escherichia coli caused by the synergistic effects of glycine and triton X-100. Appl Environ Microbiol 64:2669-2874
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2669-2874
    • Yang, J.1    Moyana, T.2    Mackenzie, S.3    Xia, Q.4    Xiang, J.5
  • 74
    • 0035660851 scopus 로고    scopus 로고
    • High level secretory production of human G-CSF by fed-batch culture of recombinant Escherichia coli
    • Yim SC, Jeong KJ, Chang HN, Lee SY (2001) High level secretory production of human G-CSF by fed-batch culture of recombinant Escherichia coli. Bioproc Biosystems Eng 24:249-254
    • (2001) Bioproc Biosystems Eng , vol.24 , pp. 249-254
    • Yim, S.C.1    Jeong, K.J.2    Chang, H.N.3    Lee, S.Y.4
  • 76
    • 0033009713 scopus 로고    scopus 로고
    • Enhancement of expression and apparent secretion of Erwinia chrysanthemi endoglucanase (encoded by celZ) in Escherichia coli B
    • Zhou S, Yomano LP, Saleh AZ, Davis FC, Aldrich HC, Ingram LO (1999) Enhancement of expression and apparent secretion of Erwinia chrysanthemi endoglucanase (encoded by celZ) in Escherichia coli B. Appl Environ Microbiol 65:2439-2445
    • (1999) Appl Environ Microbiol , vol.65 , pp. 2439-2445
    • Zhou, S.1    Yomano, L.P.2    Saleh, A.Z.3    Davis, F.C.4    Aldrich, H.C.5    Ingram, L.O.6


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