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Volumn 1292, Issue , 2015, Pages 39-51

Assays to characterize molecular chaperone function in vitro

Author keywords

Aggregation suppression; Chaperone assay; Chaperone function; Citrate synthase; Protein aggregation; Protein folding; Protein refolding

Indexed keywords

CHAPERONE; CITRATE SYNTHASE; MITOCHONDRIAL ENZYME;

EID: 84964240132     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-2522-3_3     Document Type: Article
Times cited : (15)

References (22)
  • 1
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: Life on the verge of death
    • Richter K, Haslbeck M, Buchner J (2010) The heat shock response: life on the verge of death. Mol Cell 40:253–266
    • (2010) Mol Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 3
    • 0037007283 scopus 로고    scopus 로고
    • Molecular chaperones- cellular machines for protein folding
    • Walter S, Buchner J (2002) Molecular chaperones- cellular machines for protein folding. Angew Chem Int Ed Engl 41: 1098–1113
    • (2002) Angew Chem Int Ed Engl , vol.41 , pp. 1098-1113
    • Walter, S.1    Buchner, J.2
  • 4
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B, Weissman J, Horwich A (2006) Molecular chaperones and protein quality control. Cell 125:443–451
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 5
    • 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 HH, Buchner J (1991) Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Biotechnology (N Y) 9:825–829
    • (1991) Biotechnology (N Y) , vol.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolph, R.2    Kohler, H.H.3    Buchner, J.4
  • 6
    • 0027065105 scopus 로고
    • Purifi ed chaperonin 60 (GroEL) interacts with the nonnative states of a multitude of Escherichia coli proteins
    • Viitanen PV, Gatenby AA, Lorimer GH (1992) Purifi ed chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins. Protein Sci 1:363–369
    • (1992) Protein Sci , vol.1 , pp. 363-369
    • Viitanen, P.V.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 7
    • 0024578552 scopus 로고
    • GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli
    • Goloubinoff P, Gatenby AA, Lorimer GH (1989) GroE heat-shock proteins promote assembly of foreign prokaryotic ribulose bisphosphate carboxylase oligomers in Escherichia coli. Nature 337:44–47
    • (1989) Nature , vol.337 , pp. 44-47
    • Goloubinoff, P.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 8
    • 0026702578 scopus 로고
    • Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures
    • Mendoza JA, Lorimer GH, Horowitz PM (1992) Chaperonin cpn60 from Escherichia coli protects the mitochondrial enzyme rhodanese against heat inactivation and supports folding at elevated temperatures. J Biol Chem 267:17631–17634
    • (1992) J Biol Chem , vol.267 , pp. 17631-17634
    • Mendoza, J.A.1    Lorimer, G.H.2    Horowitz, P.M.3
  • 9
    • 0031024691 scopus 로고    scopus 로고
    • A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state
    • Lee GJ, Roseman AM, Saibil HR, Vierling E (1997) A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state. EMBO J 16:659–671
    • (1997) EMBO J , vol.16 , pp. 659-671
    • Lee, G.J.1    Roseman, A.M.2    Saibil, H.R.3    Vierling, E.4
  • 11
    • 0032509224 scopus 로고    scopus 로고
    • GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase
    • Grallert H, Rutkat K, Buchner J (1998) GroEL traps dimeric and monomeric unfolding intermediates of citrate synthase. J Biol Chem 273:33305–33310
    • (1998) J Biol Chem , vol.273 , pp. 33305-33310
    • Grallert, H.1    Rutkat, K.2    Buchner, J.3
  • 12
    • 0033575217 scopus 로고    scopus 로고
    • Analysis of GroE-assisted folding under nonpermissive conditions
    • Grallert H, Buchner J (1999) Analysis of GroE-assisted folding under nonpermissive conditions. J Biol Chem 274:20171–20177
    • (1999) J Biol Chem , vol.274 , pp. 20171-20177
    • Grallert, H.1    Buchner, J.2
  • 13
    • 0027925678 scopus 로고
    • What does protein refolding in vitro tell us about protein folding in the cell?
    • Jaenicke R (1993) What does protein refolding in vitro tell us about protein folding in the cell? Philos Trans R Soc Lond B Biol Sci 339:287–294
    • (1993) Philos Trans R Soc Lond B Biol Sci , vol.339 , pp. 287-294
    • Jaenicke, R.1
  • 14
    • 0031943566 scopus 로고    scopus 로고
    • Analysis of chaperone function using citrate synthase as nonnative substrate protein
    • Buchner J, Grallert H, Jakob U (1998) Analysis of chaperone function using citrate synthase as nonnative substrate protein. Methods Enzymol 290:323–338
    • (1998) Methods Enzymol , vol.290 , pp. 323-338
    • Buchner, J.1    Grallert, H.2    Jakob, U.3
  • 16
    • 0028940309 scopus 로고
    • Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo
    • Jakob U, Lilie H, Meyer I, Buchner J (1995) Transient interaction of Hsp90 with early unfolding intermediates of citrate synthase. Implications for heat shock in vivo. J Biol Chem 270:7288–7294
    • (1995) J Biol Chem , vol.270 , pp. 7288-7294
    • Jakob, U.1    Lilie, H.2    Meyer, I.3    Buchner, J.4
  • 17
    • 21244497886 scopus 로고    scopus 로고
    • Disassembling protein aggregates in the yeast cytosol: The cooperation of Hsp26 with Ssa1 and Hsp 104
    • Haslbeck M, Miess A, Stromer T, Walter S, Buchner J (2005) Disassembling protein aggregates in the yeast cytosol: The cooperation of Hsp26 with Ssa1 and Hsp 104. J Biol Chem 280:23861–23868
    • (2005) J Biol Chem , vol.280 , pp. 23861-23868
    • Haslbeck, M.1    Miess, A.2    Stromer, T.3    Walter, S.4    Buchner, J.5
  • 18
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger M, Graber S, Gaestel M, Buchner J (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J 16:221–229
    • (1997) EMBO J , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 19
    • 0037465694 scopus 로고    scopus 로고
    • GroE-dependent expression and purifi cation of pig heart mitochondrial citrate synthase in Escherichia coli
    • Haslbeck M, Schuster I, Grallert H (2003) GroE-dependent expression and purifi cation of pig heart mitochondrial citrate synthase in Escherichia coli. J Chromatogr B Analyt Technol Biomed Life Sci 786:127–136
    • (2003) J Chromatogr B Analyt Technol Biomed Life Sci , vol.786 , pp. 127-136
    • Haslbeck, M.1    Schuster, I.2    Grallert, H.3
  • 20
    • 0014010554 scopus 로고
    • Citrate-condensing enzymeoxaloacetate binary complex. Studies on its physical and chemical properties
    • Srere PA (1966) Citrate-condensing enzymeoxaloacetate binary complex. Studies on its physical and chemical properties. J Biol Chem 241:2157–2165
    • (1966) J Biol Chem , vol.241 , pp. 2157-2165
    • Srere, P.A.1
  • 22
    • 0026058532 scopus 로고
    • Conformational stability of pig citrate synthase and some active-site mutants
    • Zhi W, Srere PA, Evans CT (1991) Conformational stability of pig citrate synthase and some active-site mutants. Biochemistry 30:9281–9286
    • (1991) Biochemistry , vol.30 , pp. 9281-9286
    • Zhi, W.1    Srere, P.A.2    Evans, C.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.