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Volumn 127, Issue 2, 2007, Pages 244-257

Inclusion body anatomy and functioning of chaperone-mediated in vivo inclusion body disassembly during high-level recombinant protein production in Escherichia coli

Author keywords

Chaperones; Disaggregation; Inclusion bodies; Recombinant protein production

Indexed keywords

AGGLOMERATION; CELLS; CONFORMATIONS; ENZYMES; GENETIC ENGINEERING; PHYSIOLOGY; PROTEINS;

EID: 33846222898     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2006.07.004     Document Type: Article
Times cited : (63)

References (55)
  • 1
    • 0026784986 scopus 로고
    • Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli
    • Allen S.P., Polazzi J.O., Gierse J.K., and Easton A.M. Two novel heat shock genes encoding proteins produced in response to heterologous protein expression in Escherichia coli. J. Bacteriol. 174 (1992) 6938-6947
    • (1992) J. Bacteriol. , vol.174 , pp. 6938-6947
    • Allen, S.P.1    Polazzi, J.O.2    Gierse, J.K.3    Easton, A.M.4
  • 2
    • 78649638046 scopus 로고    scopus 로고
    • Improving heterologous protein folding via molecular chaperone, foldase co-expression
    • Vaillancourt P.E. (Ed), Humana Press, Totowa, NJ
    • Baneyx F., and Palumbo J.L. Improving heterologous protein folding via molecular chaperone, foldase co-expression. In: Vaillancourt P.E. (Ed). E. coli Gene Expression Protocols (2002), Humana Press, Totowa, NJ 171-197
    • (2002) E. coli Gene Expression Protocols , pp. 171-197
    • Baneyx, F.1    Palumbo, J.L.2
  • 3
    • 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
  • 4
    • 0026568947 scopus 로고
    • DnaK-mediated alterations in human growth hormone protein inclusion bodies
    • Blum P., Velligan M., Lin N., and Matin A. DnaK-mediated alterations in human growth hormone protein inclusion bodies. BioTechnology 10 (1992) 301-304
    • (1992) BioTechnology , vol.10 , pp. 301-304
    • Blum, P.1    Velligan, M.2    Lin, N.3    Matin, A.4
  • 5
    • 0035951410 scopus 로고    scopus 로고
    • Protein aggregation as bacterial inclusion bodies is reversible
    • Carrió M.M., and Villaverde A. Protein aggregation as bacterial inclusion bodies is reversible. FEBS Lett. 489 (2001) 29-33
    • (2001) FEBS Lett. , vol.489 , pp. 29-33
    • Carrió, M.M.1    Villaverde, A.2
  • 6
    • 0037468523 scopus 로고    scopus 로고
    • Role of molecular chaperones in inclusion body formation
    • Carrió M.M., and Villaverde A. Role of molecular chaperones in inclusion body formation. FEBS Lett. 537 (2003) 215-221
    • (2003) FEBS Lett. , vol.537 , pp. 215-221
    • Carrió, M.M.1    Villaverde, A.2
  • 7
    • 18244398660 scopus 로고    scopus 로고
    • Localization of chaperones DnaK and GroEL in bacterial inclusion bodies
    • Carrió M.M., and Villaverde A. Localization of chaperones DnaK and GroEL in bacterial inclusion bodies. J. Bacteriol. 187 (2005) 3599-3601
    • (2005) J. Bacteriol. , vol.187 , pp. 3599-3601
    • Carrió, M.M.1    Villaverde, A.2
  • 8
    • 0032754814 scopus 로고    scopus 로고
    • Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble forms
    • Carrió M.M., Corchero J.L., and Villaverde A. Proteolytic digestion of bacterial inclusion body proteins during dynamic transition between soluble and insoluble forms. Biochim. Biophys. Acta 1434 (1999) 170-176
    • (1999) Biochim. Biophys. Acta , vol.1434 , pp. 170-176
    • Carrió, M.M.1    Corchero, J.L.2    Villaverde, A.3
  • 10
    • 0034816874 scopus 로고    scopus 로고
    • In situ proteolytic digestion of inclusion body polypeptides occurs as a cascade process
    • Cubarsí R., Carrió M.M., and Villaverde A. In situ proteolytic digestion of inclusion body polypeptides occurs as a cascade process. Biochem. Biophys. Res. Commun. 282 (2001) 436-441
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 436-441
    • Cubarsí, R.1    Carrió, M.M.2    Villaverde, A.3
  • 11
    • 0034647887 scopus 로고    scopus 로고
    • Size-dependent disaggregation of stable proteins aggregates by the DnaK chaperone machinery
    • Diamant S., Ben-Zvi A.P., Bukau B., and Goloubinoff P. Size-dependent disaggregation of stable proteins aggregates by the DnaK chaperone machinery. J. Biol. Chem. 275 (2000) 21107-21113
    • (2000) J. Biol. Chem. , vol.275 , pp. 21107-21113
    • Diamant, S.1    Ben-Zvi, A.P.2    Bukau, B.3    Goloubinoff, P.4
  • 12
    • 3542997762 scopus 로고    scopus 로고
    • Optimized procedures for purification and solubilization of basic fibroblast growth factor inclusion bodies
    • Estapé D., and Rinas U. Optimized procedures for purification and solubilization of basic fibroblast growth factor inclusion bodies. Biotechnol. Tech. 10 (1996) 481-484
    • (1996) Biotechnol. Tech. , vol.10 , pp. 481-484
    • Estapé, D.1    Rinas, U.2
  • 13
    • 0033607790 scopus 로고    scopus 로고
    • Folding kinetics of the all-beta-sheet protein human basic fibroblast growth factor, a structural homolog of interleukin-1β
    • Estapé D., and Rinas U. Folding kinetics of the all-beta-sheet protein human basic fibroblast growth factor, a structural homolog of interleukin-1β. J. Biol. Chem. 274 (1999) 34083-34088
    • (1999) J. Biol. Chem. , vol.274 , pp. 34083-34088
    • Estapé, D.1    Rinas, U.2
  • 14
    • 0032532007 scopus 로고    scopus 로고
    • Susceptibility towards intramolecular disulphide-bond formation affects conformational stability and folding of human basic fibroblast growth factor
    • Estapé D., van den Heuvel J., and Rinas U. Susceptibility towards intramolecular disulphide-bond formation affects conformational stability and folding of human basic fibroblast growth factor. Biochem. J. 335 (1998) 343-349
    • (1998) Biochem. J. , vol.335 , pp. 343-349
    • Estapé, D.1    van den Heuvel, J.2    Rinas, U.3
  • 15
    • 0029989229 scopus 로고    scopus 로고
    • Expression of correctly folded proteins in Escherichia coli
    • Georgiou G., and Valax P. Expression of correctly folded proteins in Escherichia coli. Curr. Opin. Biotechnol. 7 (1996) 190-197
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 190-197
    • Georgiou, G.1    Valax, P.2
  • 16
    • 0024578552 scopus 로고
    • GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
    • Goloubinoff P., Gatenby A.A., and Lorimer G.H. GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 337 (1989) 44-47
    • (1989) Nature , vol.337 , pp. 44-47
    • Goloubinoff, P.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 17
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P., Mogk A., Ben-Zvi A.P., Tomoyasu T., and Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 13732-13737
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Ben-Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 18
    • 0025352546 scopus 로고
    • Protein composition of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli
    • Hart R.A., Rinas U., and Bailey J.E. Protein composition of Vitreoscilla hemoglobin inclusion bodies produced in Escherichia coli. J. Biol. Chem. 265 (1990) 12728-12733
    • (1990) J. Biol. Chem. , vol.265 , pp. 12728-12733
    • Hart, R.A.1    Rinas, U.2    Bailey, J.E.3
  • 19
    • 0034518308 scopus 로고    scopus 로고
    • Kinetics of heat-shock response and inclusion body formation during temperature-induced production of basic fibroblast growth factor in high-cell density cultures of recombinant Escherichia coli
    • Hoffmann F., and Rinas U. Kinetics of heat-shock response and inclusion body formation during temperature-induced production of basic fibroblast growth factor in high-cell density cultures of recombinant Escherichia coli. Biotechnol. Prog. 16 (2000) 1000-1007
    • (2000) Biotechnol. Prog. , vol.16 , pp. 1000-1007
    • Hoffmann, F.1    Rinas, U.2
  • 20
    • 0035180274 scopus 로고    scopus 로고
    • Plasmid amplification in Escherichia coli after temperature upshift is impaired by induction of recombinant protein synthesis
    • Hoffmann F., and Rinas U. Plasmid amplification in Escherichia coli after temperature upshift is impaired by induction of recombinant protein synthesis. Biotechnol. Lett. 23 (2001) 1819-1825
    • (2001) Biotechnol. Lett. , vol.23 , pp. 1819-1825
    • Hoffmann, F.1    Rinas, U.2
  • 21
    • 3142726475 scopus 로고    scopus 로고
    • Roles of heat-shock chaperones in the production of recombinant proteins in Escherichia coli
    • Hoffmann F., and Rinas U. Roles of heat-shock chaperones in the production of recombinant proteins in Escherichia coli. Adv. Biochem. Eng. Biotechnol. 89 (2004) 143-161
    • (2004) Adv. Biochem. Eng. Biotechnol. , vol.89 , pp. 143-161
    • Hoffmann, F.1    Rinas, U.2
  • 22
    • 0035809039 scopus 로고    scopus 로고
    • Kinetic model of in vivo folding and inclusion body formation in recombinant Escherichia coli
    • Hoffmann F., Posten C., and Rinas U. Kinetic model of in vivo folding and inclusion body formation in recombinant Escherichia coli. Biotechnol. Bioeng. 72 (2001) 315-322
    • (2001) Biotechnol. Bioeng. , vol.72 , pp. 315-322
    • Hoffmann, F.1    Posten, C.2    Rinas, U.3
  • 23
    • 0037027382 scopus 로고    scopus 로고
    • Metabolic adaptation of Escherichia coli during temperature-induced recombinant protein synthesis. 1. Synthesis kinetics of catabolic enzymes
    • Hoffmann F., Weber J., and Rinas U. Metabolic adaptation of Escherichia coli during temperature-induced recombinant protein synthesis. 1. Synthesis kinetics of catabolic enzymes. Biotechnol. Bioeng. 80 (2002) 313-319
    • (2002) Biotechnol. Bioeng. , vol.80 , pp. 313-319
    • Hoffmann, F.1    Weber, J.2    Rinas, U.3
  • 25
    • 0028064780 scopus 로고
    • Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES
    • Kandror O., Busconi L., Sherman M., and Goldberg A.L. Rapid degradation of an abnormal protein in Escherichia coli involves the chaperones GroEL and GroES. J. Biol. Chem. 269 (1994) 23575-23582
    • (1994) J. Biol. Chem. , vol.269 , pp. 23575-23582
    • Kandror, O.1    Busconi, L.2    Sherman, M.3    Goldberg, A.L.4
  • 26
    • 0033621330 scopus 로고    scopus 로고
    • Rapid degradation of an abnormal protein in Escherichia coli proceeds through repeated cycles of association with GroEL
    • Kandror O., Sherman M., and Goldberg A. Rapid degradation of an abnormal protein in Escherichia coli proceeds through repeated cycles of association with GroEL. J. Biol. Chem. 274 (1999) 37743-37749
    • (1999) J. Biol. Chem. , vol.274 , pp. 37743-37749
    • Kandror, O.1    Sherman, M.2    Goldberg, A.3
  • 27
    • 0025927672 scopus 로고
    • Properties of recombinant protein-containing inclusion bodies in Escherichia coli
    • Seetharam R., and Sharma S.K. (Eds), Marcel Dekker Inc.,, New York
    • Kane J.F., and Hartley D.L. Properties of recombinant protein-containing inclusion bodies in Escherichia coli. In: Seetharam R., and Sharma S.K. (Eds). Purification and Analysis of Recombinant Proteins (1991), Marcel Dekker Inc.,, New York 121-145
    • (1991) Purification and Analysis of Recombinant Proteins , pp. 121-145
    • Kane, J.F.1    Hartley, D.L.2
  • 28
    • 0035856592 scopus 로고    scopus 로고
    • The effect of co-overproduction of DnaK/DnaJ/GrpE and ClpB proteins on the removal of heat-aggregated proteins from Escherichia coli ΔclpB mutant cells-new insight into the role of Hsp70 in a functional cooperation with Hsp100
    • Ke{ogonek}dzierska S., and Matuszewska E. The effect of co-overproduction of DnaK/DnaJ/GrpE and ClpB proteins on the removal of heat-aggregated proteins from Escherichia coli ΔclpB mutant cells-new insight into the role of Hsp70 in a functional cooperation with Hsp100. FEMS Microbiol. Lett. 204 (2001) 355-360
    • (2001) FEMS Microbiol. Lett. , vol.204 , pp. 355-360
    • Kedzierska, S.1    Matuszewska, E.2
  • 29
    • 0033063634 scopus 로고    scopus 로고
    • The role of DnaK/DnaJ and GroEL/GroEL systems in the removal of endogenous proteins aggregated by heat-shock from Escherichia coli cells
    • Ke{ogonek}dzierska S., Staniszewska M., We{ogonek}grzyn A., and Taylor A. The role of DnaK/DnaJ and GroEL/GroEL systems in the removal of endogenous proteins aggregated by heat-shock from Escherichia coli cells. FEBS Lett. 446 (1999) 331-337
    • (1999) FEBS Lett. , vol.446 , pp. 331-337
    • Kedzierska, S.1    Staniszewska, M.2    Wegrzyn, A.3    Taylor, A.4
  • 30
    • 0035074376 scopus 로고    scopus 로고
    • DnaK/DnaJ chaperone system reactivates endogenous E. coli thermostable FBP aldolase in vivo and in vitro, the effect is enhanced by GroE heat shock proteins
    • Ke{ogonek}dzierska S., Jezierski G., and Taylor A. DnaK/DnaJ chaperone system reactivates endogenous E. coli thermostable FBP aldolase in vivo and in vitro, the effect is enhanced by GroE heat shock proteins. Cell Stress Chaperones 6 (2001) 29-37
    • (2001) Cell Stress Chaperones , vol.6 , pp. 29-37
    • Kedzierska, S.1    Jezierski, G.2    Taylor, A.3
  • 31
    • 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 9 (1991) 825-829
    • (1991) Biotechnology , vol.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolph, R.2    Kohler, H.H.3    Buchner, J.4
  • 32
    • 0029239706 scopus 로고
    • Simple fed-batch technique for high-cell density cultivation of Escherichia coli
    • Korz D.J., Rinas U., Hellmuth K., Sanders E.A., and Deckwer W.-D. Simple fed-batch technique for high-cell density cultivation of Escherichia coli. J. Biotechnol. 39 (1995) 59-65
    • (1995) J. Biotechnol. , vol.39 , pp. 59-65
    • Korz, D.J.1    Rinas, U.2    Hellmuth, K.3    Sanders, E.A.4    Deckwer, W.-D.5
  • 33
    • 0029852402 scopus 로고    scopus 로고
    • Degradation by protease Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock, HtrA protease action in vivo and in vitro
    • Laskowska E., Kuczynska-Wisnik D., Skorko-Glonek J., and Taylor A. Degradation by protease Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock, HtrA protease action in vivo and in vitro. Mol. Microbiol. 22 (1996) 555-571
    • (1996) Mol. Microbiol. , vol.22 , pp. 555-571
    • Laskowska, E.1    Kuczynska-Wisnik, D.2    Skorko-Glonek, J.3    Taylor, A.4
  • 34
    • 23244441404 scopus 로고    scopus 로고
    • Processes for production of active α-glucosidase by in vivo reactivation from inclusion bodies. Evaluation of processes using in vivo reactivation from inclusion bodies
    • LeThanh H., and Hoffmann F. Processes for production of active α-glucosidase by in vivo reactivation from inclusion bodies. Evaluation of processes using in vivo reactivation from inclusion bodies. Biotechnol. Prog. 21 (2005) 1053-1061
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1053-1061
    • LeThanh, H.1    Hoffmann, F.2
  • 36
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB
    • Mogk A., Tomoyasu T., Goloubinoff P., Rüdiger S., Röder D., Langen H., and Bukau B. Identification of thermolabile Escherichia coli proteins: Prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18 (1999) 6934-6949
    • (1999) EMBO J. , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rüdiger, S.4    Röder, D.5    Langen, H.6    Bukau, B.7
  • 37
    • 0142125283 scopus 로고    scopus 로고
    • Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation
    • Mogk A., Deuerling E., Vorderwülbecke S., Vierling E., and Bukau B. Small heat shock proteins, ClpB and the DnaK system form a functional triade in reversing protein aggregation. Mol. Microbiol. 50 (2003) 585-595
    • (2003) Mol. Microbiol. , vol.50 , pp. 585-595
    • Mogk, A.1    Deuerling, E.2    Vorderwülbecke, S.3    Vierling, E.4    Bukau, B.5
  • 38
    • 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. 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
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 1694-1699
    • Nishihara, K.1    Kanemori, M.2    Kitagawa, M.3    Yanagi, H.4    Yura, T.5
  • 39
    • 1842760472 scopus 로고    scopus 로고
    • The impact of dnaKJ overexpression on recombinant protein solubility results from antagonistic effects on the control of protein quality
    • Petersson L., Carrió M.M., Vera A., and Villaverde A. The impact of dnaKJ overexpression on recombinant protein solubility results from antagonistic effects on the control of protein quality. Biotechnol. Lett. 26 (2004) 595-601
    • (2004) Biotechnol. Lett. , vol.26 , pp. 595-601
    • Petersson, L.1    Carrió, M.M.2    Vera, A.3    Villaverde, A.4
  • 40
    • 0026660841 scopus 로고
    • Protein compositional analysis of inclusion bodies produced in recombinant Escherichia coli
    • Rinas U., and Bailey J.E. Protein compositional analysis of inclusion bodies produced in recombinant Escherichia coli. Appl. Microbiol. Biotechnol. 37 (1992) 609-614
    • (1992) Appl. Microbiol. Biotechnol. , vol.37 , pp. 609-614
    • Rinas, U.1    Bailey, J.E.2
  • 41
    • 0027408105 scopus 로고
    • Overexpression of bacterial hemoglobin causes incorporation of pre-β-lactamase into cytoplasmic inclusion bodies
    • Rinas U., and Bailey J.E. Overexpression of bacterial hemoglobin causes incorporation of pre-β-lactamase into cytoplasmic inclusion bodies. Appl. Environ. Microbiol. 59 (1993) 561-566
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 561-566
    • Rinas, U.1    Bailey, J.E.2
  • 42
    • 0033597834 scopus 로고    scopus 로고
    • On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES
    • Sakikawa C., Taguchi H., Makino Y., and Yoshida M. On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES. J. Biol. Chem. 274 (1999) 21251-21256
    • (1999) J. Biol. Chem. , vol.274 , pp. 21251-21256
    • Sakikawa, C.1    Taguchi, H.2    Makino, Y.3    Yoshida, M.4
  • 43
    • 23044456332 scopus 로고    scopus 로고
    • Characterization of the aggregates formed during recombinant protein expression in bacteria
    • Schrödel A., and de Marco A. Characterization of the aggregates formed during recombinant protein expression in bacteria. BUC Biochem. 6 (2005) 10
    • (2005) BUC Biochem. , vol.6 , pp. 10
    • Schrödel, A.1    de Marco, A.2
  • 44
    • 0030569008 scopus 로고    scopus 로고
    • Two-step chromatographic procedure for purification of basic fibroblast growth factor from recombinant Escherichia coli and characterization of the equilibrium parameters of adsorption
    • Seeger A., and Rinas U. Two-step chromatographic procedure for purification of basic fibroblast growth factor from recombinant Escherichia coli and characterization of the equilibrium parameters of adsorption. J. Chromatogr. A 746 (1996) 17-24
    • (1996) J. Chromatogr. A , vol.746 , pp. 17-24
    • Seeger, A.1    Rinas, U.2
  • 45
    • 0028970554 scopus 로고
    • Comparison of temperature- and isopropyl-β-d-thiogalacto-pyranosid-induced synthesis of basic fibroblast growth factor in high-cell density cultures of recombinant Escherichia coli
    • Seeger A., Schneppe B., McCarthy J.E.G., Deckwer W.-D., and Rinas U. Comparison of temperature- and isopropyl-β-d-thiogalacto-pyranosid-induced synthesis of basic fibroblast growth factor in high-cell density cultures of recombinant Escherichia coli. Enzyme Microb. Technol. 17 (1995) 947-953
    • (1995) Enzyme Microb. Technol. , vol.17 , pp. 947-953
    • Seeger, A.1    Schneppe, B.2    McCarthy, J.E.G.3    Deckwer, W.-D.4    Rinas, U.5
  • 47
    • 0031705810 scopus 로고    scopus 로고
    • Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG in vivo
    • Thomas J.G., and Baneyx F. Roles of the Escherichia coli small heat shock proteins IbpA and IbpB in thermal stress management: comparison with ClpA, ClpB, and HtpG in vivo. J. Bacteriol. 180 (1998) 5165-5172
    • (1998) J. Bacteriol. , vol.180 , pp. 5165-5172
    • Thomas, J.G.1    Baneyx, F.2
  • 48
    • 0033933125 scopus 로고    scopus 로고
    • ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells
    • Thomas J.G., and Baneyx F. ClpB and HtpG facilitate de novo protein folding in stressed Escherichia coli cells. Mol. Microbiol. 36 (2000) 1360-1370
    • (2000) Mol. Microbiol. , vol.36 , pp. 1360-1370
    • Thomas, J.G.1    Baneyx, F.2
  • 49
    • 0035029482 scopus 로고    scopus 로고
    • Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol
    • Tomoyasu T., Mogk A., Langen H., Goloubinoff P., and Bukau B. Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol. Mol. Microbiol. 40 (2001) 397-413
    • (2001) Mol. Microbiol. , vol.40 , pp. 397-413
    • Tomoyasu, T.1    Mogk, A.2    Langen, H.3    Goloubinoff, P.4    Bukau, B.5
  • 50
    • 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
  • 51
    • 24044505987 scopus 로고    scopus 로고
    • Lon and ClpP proteases participate in the physiological disintegration of bacterial inclusion bodies
    • Vera A., Aris A., Carrio M., Gonzalez-Montalban N., and Villaverde A. Lon and ClpP proteases participate in the physiological disintegration of bacterial inclusion bodies. J. Biotechnol. 119 (2005) 163-171
    • (2005) J. Biotechnol. , vol.119 , pp. 163-171
    • Vera, A.1    Aris, A.2    Carrio, M.3    Gonzalez-Montalban, N.4    Villaverde, A.5
  • 52
  • 53
    • 2942596463 scopus 로고    scopus 로고
    • Unscrambling an egg: protein disaggregation by AAA+ proteins
    • Weibezahn J., Bukau B., and Mogk A. Unscrambling an egg: protein disaggregation by AAA+ proteins. Microb. Cell Fact. 3 (2004) 1
    • (2004) Microb. Cell Fact. , vol.3 , pp. 1
    • Weibezahn, J.1    Bukau, B.2    Mogk, A.3
  • 54
    • 26844539619 scopus 로고    scopus 로고
    • Novel insights into the mechanism of chaperone-assisted protein disaggregation
    • Weibezahn J., Schlieker C., Tessarz P., Mogk A., and Bukau B. Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biol. Chem. 386 (2005) 739-744
    • (2005) Biol. Chem. , vol.386 , pp. 739-744
    • Weibezahn, J.1    Schlieker, C.2    Tessarz, P.3    Mogk, A.4    Bukau, B.5
  • 55
    • 0033214052 scopus 로고    scopus 로고
    • ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation
    • Zolkiewski M. ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. J. Biol. Chem. 274 (1999) 28083-28086
    • (1999) J. Biol. Chem. , vol.274 , pp. 28083-28086
    • Zolkiewski, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.