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Volumn 580, Issue 27, 2006, Pages 6471-6476

Effect of temperature on protein quality in bacterial inclusion bodies

Author keywords

Escherichia coli; Inclusion bodies; Protein aggregation; Protein folding; Recombinant protein expression

Indexed keywords

AMYLOID PRECURSOR PROTEIN; GREEN FLUORESCENT PROTEIN; RECOMBINANT PROTEIN;

EID: 33750991319     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2006.10.071     Document Type: Article
Times cited : (140)

References (29)
  • 1
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F., and Mujacic M. Recombinant protein folding and misfolding in Escherichia coli. Nat. Biotechnol. 22 (2004) 1399-1408
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 2
    • 0042193601 scopus 로고    scopus 로고
    • Protein aggregation in recombinant bacteria: biological role of inclusion bodies
    • Villaverde A., and Carrio M.M. Protein aggregation in recombinant bacteria: biological role of inclusion bodies. Biotechnol. Lett. 25 (2003) 1385-1395
    • (2003) Biotechnol. Lett. , vol.25 , pp. 1385-1395
    • Villaverde, A.1    Carrio, M.M.2
  • 5
    • 20444363444 scopus 로고    scopus 로고
    • Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy
    • Ami D., Natalello A., Gatti-Lafranconi P., Lotti M., and Doglia S.M. Kinetics of inclusion body formation studied in intact cells by FT-IR spectroscopy. FEBS Lett. 579 (2005) 3433-3436
    • (2005) FEBS Lett. , vol.579 , pp. 3433-3436
    • Ami, D.1    Natalello, A.2    Gatti-Lafranconi, P.3    Lotti, M.4    Doglia, S.M.5
  • 6
    • 33646106328 scopus 로고    scopus 로고
    • Protein quality in bacterial inclusion bodies
    • Ventura S., and Villaverde A. Protein quality in bacterial inclusion bodies. Trends Biotechnol. 24 (2006) 179-185
    • (2006) Trends Biotechnol. , vol.24 , pp. 179-185
    • Ventura, S.1    Villaverde, A.2
  • 7
    • 0025921901 scopus 로고
    • High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D
    • Tokatlidis K., Dhurjati P., Millet J., Beguin P., and Aubert J.P. High activity of inclusion bodies formed in Escherichia coli overproducing Clostridium thermocellum endoglucanase D. FEBS Lett. 282 (1991) 205-208
    • (1991) FEBS Lett. , vol.282 , pp. 205-208
    • Tokatlidis, K.1    Dhurjati, P.2    Millet, J.3    Beguin, P.4    Aubert, J.P.5
  • 8
    • 33745991934 scopus 로고    scopus 로고
    • Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates
    • de Groot N.S., and Ventura S. Protein activity in bacterial inclusion bodies correlates with predicted aggregation rates. J. Biotechnol. 125 (2006) 110-113
    • (2006) J. Biotechnol. , vol.125 , pp. 110-113
    • de Groot, N.S.1    Ventura, S.2
  • 9
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
    • Sorensen H.P., and Mortensen K.K. Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microbial Cell Factories 4 (2005) 1
    • (2005) Microbial Cell Factories , vol.4 , pp. 1
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 10
    • 0029968943 scopus 로고    scopus 로고
    • Recombinant protein expression at low temperatures under the transcriptional control of the major Escherichia coli cold shock promoter cspA
    • Vasina J.A., and Baneyx F. Recombinant protein expression at low temperatures under the transcriptional control of the major Escherichia coli cold shock promoter cspA. Appl. Environ. Microbiol. 62 (1996) 1444-1447
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1444-1447
    • Vasina, J.A.1    Baneyx, F.2
  • 11
    • 33748691613 scopus 로고    scopus 로고
    • The evaluation of the factors that cause aggregation during recombinant expression in E. coli is simplified by the employment of an aggregation-sensitive reporter
    • Schultz T., Martinez L., and de Marco A. The evaluation of the factors that cause aggregation during recombinant expression in E. coli is simplified by the employment of an aggregation-sensitive reporter. Microbial Cell Factories 5 (2006) 28
    • (2006) Microbial Cell Factories , vol.5 , pp. 28
    • Schultz, T.1    Martinez, L.2    de Marco, A.3
  • 12
    • 33751013053 scopus 로고    scopus 로고
    • The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures
    • Vera A., Gonzalez-Montalban N., Aris A., and Villaverde A. The conformational quality of insoluble recombinant proteins is enhanced at low growth temperatures. Biotechnol. Bioeng. (2006)
    • (2006) Biotechnol. Bioeng.
    • Vera, A.1    Gonzalez-Montalban, N.2    Aris, A.3    Villaverde, A.4
  • 13
    • 0348147593 scopus 로고    scopus 로고
    • Temperature effect on inclusion body formation and stress response in the periplasm of Escherichia coli
    • Hunke S., and Betton J.M. Temperature effect on inclusion body formation and stress response in the periplasm of Escherichia coli. Mol. Microbiol. 50 (2003) 1579-1589
    • (2003) Mol. Microbiol. , vol.50 , pp. 1579-1589
    • Hunke, S.1    Betton, J.M.2
  • 14
    • 0034616258 scopus 로고    scopus 로고
    • Fine architecture of bacterial inclusion bodies
    • Carrio M.M., Cubarsi R., and Villaverde A. Fine architecture of bacterial inclusion bodies. FEBS Lett. 471 (2000) 7-11
    • (2000) FEBS Lett. , vol.471 , pp. 7-11
    • Carrio, M.M.1    Cubarsi, R.2    Villaverde, A.3
  • 15
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 16
    • 33644940173 scopus 로고    scopus 로고
    • Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities
    • de Groot N.S., Aviles F.X., Vendrell J., and Ventura S. Mutagenesis of the central hydrophobic cluster in Abeta42 Alzheimer's peptide. Side-chain properties correlate with aggregation propensities. FEBS J. 273 (2006) 658-668
    • (2006) FEBS J. , vol.273 , pp. 658-668
    • de Groot, N.S.1    Aviles, F.X.2    Vendrell, J.3    Ventura, S.4
  • 17
    • 14744271625 scopus 로고
    • Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation
    • Kiefhaber T., Rudolph R., Kohler H.H., and Buchner J. Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Biotechnology (N Y) 9 (1991) 825-829
    • (1991) Biotechnology (N Y) , vol.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolph, R.2    Kohler, H.H.3    Buchner, J.4
  • 18
    • 0030834850 scopus 로고    scopus 로고
    • Temperature, stability, and the hydrophobic interaction
    • Schellman J.A. Temperature, stability, and the hydrophobic interaction. Biophys. J. 73 (1997) 2960-2964
    • (1997) Biophys. J. , vol.73 , pp. 2960-2964
    • Schellman, J.A.1
  • 19
    • 33644858238 scopus 로고    scopus 로고
    • Annealing prion protein amyloid fibrils at high temperature results in extension of a proteinase K-resistant core
    • Bocharova O.V., Makarava N., Breydo L., Anderson M., Salnikov V.V., and Baskakov I.V. Annealing prion protein amyloid fibrils at high temperature results in extension of a proteinase K-resistant core. J. Biol. Chem. 281 (2006) 2373-2379
    • (2006) J. Biol. Chem. , vol.281 , pp. 2373-2379
    • Bocharova, O.V.1    Makarava, N.2    Breydo, L.3    Anderson, M.4    Salnikov, V.V.5    Baskakov, I.V.6
  • 20
    • 33751020615 scopus 로고    scopus 로고
    • Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli
    • Rinas U., Hoffmann F., Betiku E., Estape D., and Marten S. Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli. J. Biotechnol. (2006)
    • (2006) J. Biotechnol.
    • Rinas, U.1    Hoffmann, F.2    Betiku, E.3    Estape, D.4    Marten, S.5
  • 21
    • 0034105491 scopus 로고    scopus 로고
    • Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli
    • Patra A.K., Mukhopadhyay R., Mukhija R., Krishnan A., Garg L.C., and Panda A.K. Optimization of inclusion body solubilization and renaturation of recombinant human growth hormone from Escherichia coli. Protein Expr. Purif. 18 (2000) 182-192
    • (2000) Protein Expr. Purif. , vol.18 , pp. 182-192
    • Patra, A.K.1    Mukhopadhyay, R.2    Mukhija, R.3    Krishnan, A.4    Garg, L.C.5    Panda, A.K.6
  • 23
    • 0028057034 scopus 로고
    • Secondary structure characterization of beta-lactamase inclusion bodies
    • Przybycien T.M., Dunn J.P., Valax P., and Georgiou G. Secondary structure characterization of beta-lactamase inclusion bodies. Protein Eng. 7 (1994) 131-136
    • (1994) Protein Eng. , vol.7 , pp. 131-136
    • Przybycien, T.M.1    Dunn, J.P.2    Valax, P.3    Georgiou, G.4
  • 24
    • 0344395589 scopus 로고    scopus 로고
    • FT-IR study of heterologous protein expression in recombinant Escherichia coli strains
    • Ami D., Bonecchi L., Cali S., Orsini G., Tonon G., and Doglia S.M. FT-IR study of heterologous protein expression in recombinant Escherichia coli strains. Biochim. Biophys. Acta 1624 (2003) 6-10
    • (2003) Biochim. Biophys. Acta , vol.1624 , pp. 6-10
    • Ami, D.1    Bonecchi, L.2    Cali, S.3    Orsini, G.4    Tonon, G.5    Doglia, S.M.6
  • 26
    • 26844498710 scopus 로고    scopus 로고
    • Sequence determinants of protein aggregation: tools to increase protein solubility
    • Ventura S. Sequence determinants of protein aggregation: tools to increase protein solubility. Microbial Cell Factories 4 (2005) 11
    • (2005) Microbial Cell Factories , vol.4 , pp. 11
    • Ventura, S.1
  • 27
    • 33646589053 scopus 로고    scopus 로고
    • Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy
    • Ami D., Natalello A., Taylor G., Tonon G., and Maria Doglia S. Structural analysis of protein inclusion bodies by Fourier transform infrared microspectroscopy. Biochim. Biophys. Acta 1764 (2006) 793-799
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 793-799
    • Ami, D.1    Natalello, A.2    Taylor, G.3    Tonon, G.4    Maria Doglia, S.5
  • 28
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • Singh S.M., and Panda A.K. Solubilization and refolding of bacterial inclusion body proteins. J. Biosci. Bioeng. 99 (2005) 303-310
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 29
    • 23044456332 scopus 로고    scopus 로고
    • Characterization of the aggregates formed during recombinant protein expression in bacteria
    • Schrodel A., and de Marco A. Characterization of the aggregates formed during recombinant protein expression in bacteria. BMC Biochem. 6 (2005) 10
    • (2005) BMC Biochem. , vol.6 , pp. 10
    • Schrodel, A.1    de Marco, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.