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Volumn 92, Issue 3, 1998, Pages 351-366

The Hsp70 and Hsp60 chaperone machines

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE;

EID: 0032489016     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80928-9     Document Type: Review
Times cited : (2474)

References (112)
  • 1
    • 0027316898 scopus 로고
    • To fold or not to fold
    • Agard, D.A. (1993). To fold or not to fold... Science 260, 1903-1904.
    • (1993) Science , vol.260 , pp. 1903-1904
    • Agard, D.A.1
  • 2
    • 0028003639 scopus 로고
    • ATP induces non-identity of two rings in chaperonin GroEL
    • Bochkareva, E.S., and Girshovich, A.S. (1994). ATP induces non-identity of two rings in chaperonin GroEL. J. Biol. Chem. 269, 23869-23871.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23869-23871
    • Bochkareva, E.S.1    Girshovich, A.S.2
  • 4
    • 0028999582 scopus 로고    scopus 로고
    • Hold 'em and fold 'em: Chaperones and signal transduction
    • Bohen, S.P., Kralli, A., and Yamamoto, K.R. (1996) Hold 'em and fold 'em: Chaperones and signal transduction. Science 268, 1303-1304.
    • (1996) Science , vol.268 , pp. 1303-1304
    • Bohen, S.P.1    Kralli, A.2    Yamamoto, K.R.3
  • 5
    • 0029664944 scopus 로고    scopus 로고
    • The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγs
    • Boisvert, D.C., Wang, J., Otwinowski, Z., Horwich, A.L., and Sigler, P.B. (1996). The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATPγS. Nature Struct. Biol. 3, 170-177.
    • (1996) Nature Struct. Biol. , vol.3 , pp. 170-177
    • Boisvert, D.C.1    Wang, J.2    Otwinowski, Z.3    Horwich, A.L.4    Sigler, P.B.5
  • 6
    • 0027273399 scopus 로고
    • A polypeptide bound by the chaperonin groEL is localized within a central cavity
    • Braig, K., Simon, M., Furuya, F., Hainfeld, J.F., and Horwich, A.L. (1993). A polypeptide bound by the chaperonin groEL is localized within a central cavity. Proc. Natl. Acad. Sci. USA 90, 3978-3982.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3978-3982
    • Braig, K.1    Simon, M.2    Furuya, F.3    Hainfeld, J.F.4    Horwich, A.L.5
  • 8
    • 0029037015 scopus 로고
    • Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication
    • Buchberger, A., Theyssen, H., Schröder, H., McCarty, J.S., Virgallita, G., Milkereit, P., Reinstein, J., and Bukau, B. (1995). Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J. Biol. Chem. 270, 16903-16910.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16903-16910
    • Buchberger, A.1    Theyssen, H.2    Schröder, H.3    McCarty, J.S.4    Virgallita, G.5    Milkereit, P.6    Reinstein, J.7    Bukau, B.8
  • 9
    • 0030598919 scopus 로고    scopus 로고
    • Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding
    • Buchberger, A., Schröder, H., Hesterkamp, T., Schönfeld, H.-J., and Bukau, B. (1996). Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J. Mol. Biol. 261, 328-333.
    • (1996) J. Mol. Biol. , vol.261 , pp. 328-333
    • Buchberger, A.1    Schröder, H.2    Hesterkamp, T.3    Schönfeld, H.-J.4    Bukau, B.5
  • 10
    • 0030966765 scopus 로고    scopus 로고
    • A structural model for GroEL-polypeptide recognition
    • Buckle, A.M., Zahn, R., and Fersht, A.R. (1997). A structural model for GroEL-polypeptide recognition. Proc. Natl. Acad. Sci. USA 94, 3571-3575.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3571-3575
    • Buckle, A.M.1    Zahn, R.2    Fersht, A.R.3
  • 11
    • 0029016593 scopus 로고
    • The origins and consequences of asymmetry in the chaperonin reaction cycle
    • Burston, S.G., Ranson, N.A., and Clarke, A.R. (1995). The origins and consequences of asymmetry in the chaperonin reaction cycle. J. Mol. Biol. 249, 138-152.
    • (1995) J. Mol. Biol. , vol.249 , pp. 138-152
    • Burston, S.G.1    Ranson, N.A.2    Clarke, A.R.3
  • 12
    • 0029823985 scopus 로고    scopus 로고
    • Release of both native and non-native proteins from a cis-only GroEL ternary complex
    • Burston, S.G., Weissman, J.S., Farr, G.W., Fenton, W.A., and Horwich, A.L. (1996). Release of both native and non-native proteins from a cis-only GroEL ternary complex. Nature 383, 96-99.
    • (1996) Nature , vol.383 , pp. 96-99
    • Burston, S.G.1    Weissman, J.S.2    Farr, G.W.3    Fenton, W.A.4    Horwich, A.L.5
  • 13
    • 0028027055 scopus 로고
    • Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy
    • Chen, S., Roseman, A.M., Hunter, A.S., Wood, S.P., Burston, S.G., Ranson, N.A., Clarke, A.R., and Saibil, H.R. (1994). Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature 371, 261-264.
    • (1994) Nature , vol.371 , pp. 261-264
    • Chen, S.1    Roseman, A.M.2    Hunter, A.S.3    Wood, S.P.4    Burston, S.G.5    Ranson, N.A.6    Clarke, A.R.7    Saibil, H.R.8
  • 14
    • 0031577340 scopus 로고    scopus 로고
    • Role of the mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70
    • Dekker, P.J.T., and Pfanner, N. (1997). Role of the mitochondrial GrpE and phosphate in the ATPase cycle of matrix Hsp70. J. Mol. Biol. 270, 321-327.
    • (1997) J. Mol. Biol. , vol.270 , pp. 321-327
    • Dekker, P.J.T.1    Pfanner, N.2
  • 15
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill, K.A., and Chan, H.S. (1997). From Levinthal to pathways to funnels. Nature Struct. Biol. 4, 10-19.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 16
    • 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., Gräber, S., Gaestel, M., and 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    Gräber, S.2    Gaestel, M.3    Buchner, J.4
  • 17
    • 0004167360 scopus 로고    scopus 로고
    • San Diego, CA: Academic Press
    • Ellis, R.J., ed. (1996). The Chaperonins (San Diego, CA: Academic Press).
    • (1996) The Chaperonins
    • Ellis, R.J.1
  • 18
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • Fenton, W.A., and Horwich, A.L. (1997). GroEL-mediated protein folding. Protein Sci. 6, 743-760.
    • (1997) Protein Sci. , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 19
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton, W.A., Kashi, Y., Furtak, K., and Horwich, A.L. (1994). Residues in chaperonin GroEL required for polypeptide binding and release. Nature 371, 614-619.
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 20
    • 0025100372 scopus 로고
    • Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein
    • Flaherty, K.M., Deluca-Flaherty, C., and McKay, D.B. (1990). Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein. Nature 346, 623-628.
    • (1990) Nature , vol.346 , pp. 623-628
    • Flaherty, K.M.1    Deluca-Flaherty, C.2    McKay, D.B.3
  • 21
    • 0028240468 scopus 로고
    • Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. Ii. Structure of the active site with ADP or ATP bound to wild type or mutant ATPase fragment
    • Flaherty, K.M., Wilbanks, S.M., DeLuca-Flaherty, C., and McKay, D.B. (1994). Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type or mutant ATPase fragment. J. Biol. Chem. 269, 12899-12907.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12899-12907
    • Flaherty, K.M.1    Wilbanks, S.M.2    DeLuca-Flaherty, C.3    McKay, D.B.4
  • 22
    • 0024393778 scopus 로고
    • Peptide binding and release by proteins implicated as catalysts of protein assembly
    • Flynn, G.C., Chappell, T.G., and Rothman, J.E. (1989). Peptide binding and release by proteins implicated as catalysts of protein assembly. Science 245, 385-390.
    • (1989) Science , vol.245 , pp. 385-390
    • Flynn, G.C.1    Chappell, T.G.2    Rothman, J.E.3
  • 23
    • 0026059137 scopus 로고
    • Peptide-binding specificity of the molecular chaperone BiP
    • Flynn, G.C., Pohl, J., Flocco, M.T., and Rothman, J.E. (1991). Peptide-binding specificity of the molecular chaperone BiP. Nature 353, 726-730.
    • (1991) Nature , vol.353 , pp. 726-730
    • Flynn, G.C.1    Pohl, J.2    Flocco, M.T.3    Rothman, J.E.4
  • 24
    • 0029887140 scopus 로고    scopus 로고
    • The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding
    • Freeman, B.C., and Morimoto, R.I. (1996). The human cytosolic molecular chaperones hsp90, hsp70 (hsc70) and hdj-1 have distinct roles in recognition of a non-native protein and protein refolding. EMBO J. 15, 2969-2979.
    • (1996) EMBO J. , vol.15 , pp. 2969-2979
    • Freeman, B.C.1    Morimoto, R.I.2
  • 25
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman, J., and Höhfeld, J. (1997). Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci. 22, 87-92.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Höhfeld, J.2
  • 27
    • 0026776331 scopus 로고
    • A cytoplasmic chaperonin that catalyzes β-actin folding
    • Gao, Y., Thomas, J.O., Chow, R.L., Lee, G.H., and Cowan, N.J. (1992). A cytoplasmic chaperonin that catalyzes β-actin folding. Cell 69, 1043-1050.
    • (1992) Cell , vol.69 , pp. 1043-1050
    • Gao, Y.1    Thomas, J.O.2    Chow, R.L.3    Lee, G.H.4    Cowan, N.J.5
  • 28
    • 0027513927 scopus 로고
    • Nucleotide binding properties of bovine brain uncoating ATPase
    • Gao, B., Yumiko, E., Greene, L., and Eisenberg, E. (1993). Nucleotide binding properties of bovine brain uncoating ATPase. J. Biol. Chem. 268, 8507-8513.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8507-8513
    • Gao, B.1    Yumiko, E.2    Greene, L.3    Eisenberg, E.4
  • 29
    • 0028231720 scopus 로고
    • Characterization of nucleotide-free uncoating ATPase and its binding to ATP, ADP and ATP analogues
    • Gao, B., Greene, L., and Eisenberg, E. (1994). Characterization of nucleotide-free uncoating ATPase and its binding to ATP, ADP and ATP analogues. Biochemistry 33, 2048-2054.
    • (1994) Biochemistry , vol.33 , pp. 2048-2054
    • Gao, B.1    Greene, L.2    Eisenberg, E.3
  • 30
    • 0029861712 scopus 로고    scopus 로고
    • β-lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange
    • Gervasoni, P., Staudenmann, W., James, P., Gehrig, P., and Plüthun, A. (1996). β-Lactamase binds to GroEL in a conformation highly protected against hydrogen/deuterium exchange. Proc. Natl. Acad. Sci. USA 93, 12189-12194.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12189-12194
    • Gervasoni, P.1    Staudenmann, W.2    James, P.3    Gehrig, P.4    Plüthun, A.5
  • 31
    • 0031030036 scopus 로고    scopus 로고
    • Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
    • Goldberg, M.S., Zhang, J., Matthews, C.R., Fox, R.O., and Horwich, A.L. (1997). Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proc. Natl. Acad. Sci. USA 94, 1080-1085.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1080-1085
    • Goldberg, M.S.1    Zhang, J.2    Matthews, C.R.3    Fox, R.O.4    Horwich, A.L.5
  • 32
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MgATP
    • Goloubinoff, P., Christeller, J.T., Gatnby, A.A., and Lorimer, G.H. (1989). Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and MgATP. Nature 342, 884-889.
    • (1989) Nature , vol.342 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatnby, A.A.3    Lorimer, G.H.4
  • 33
    • 0028004372 scopus 로고
    • Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins
    • Gordon, C.L., Sather, S.K., Casjens, S., and King, J. (1994). Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins. J. Biol. Chem. 269, 27941-27951.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27941-27951
    • Gordon, C.L.1    Sather, S.K.2    Casjens, S.3    King, J.4
  • 34
    • 0025995773 scopus 로고
    • Cooperativity in ATP hydrolysis by GroEL is increased by GroES
    • Gray, T.E., and Fersht, A.R. (1991). Cooperativity in ATP hydrolysis by GroEL is increased by GroES. FEBS Lett. 292, 254-258.
    • (1991) FEBS Lett. , vol.292 , pp. 254-258
    • Gray, T.E.1    Fersht, A.R.2
  • 35
    • 0030451744 scopus 로고    scopus 로고
    • Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling
    • Groß, M., Robinson, C.V., Mayhew, M., Hartl, F.U., and Radford, S.E. (1996). Significant hydrogen exchange protection in GroEL-bound DHFR is maintained during iterative rounds of substrate cycling. Protein Sci. 5, 2506-2513.
    • (1996) Protein Sci. , vol.5 , pp. 2506-2513
    • Groß, M.1    Robinson, C.V.2    Mayhew, M.3    Hartl, F.U.4    Radford, S.E.5
  • 36
    • 0028584378 scopus 로고
    • ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain
    • Ha, J.-H., and McKay, D.B. (1994). ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain. Biochemistry 33, 14625-14635.
    • (1994) Biochemistry , vol.33 , pp. 14625-14635
    • Ha, J.-H.1    McKay, D.B.2
  • 37
    • 0029161689 scopus 로고
    • Kinetics of nucleotide-induced changes in the tryptophane fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the ATP-induced conformational change follows initial ATP binding
    • Ha, J.-H., and McKay, D.B. (1995). Kinetics of nucleotide-induced changes in the tryptophane fluorescence of the molecular chaperone Hsc70 and its subfragments suggest the ATP-induced conformational change follows initial ATP binding. Biochemistry 34, 11635-11644.
    • (1995) Biochemistry , vol.34 , pp. 11635-11644
    • Ha, J.-H.1    McKay, D.B.2
  • 39
    • 0030936995 scopus 로고    scopus 로고
    • Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK
    • Harrison, C.J., Hayer-Hartl, M., Di Liberto, M., Hartl, F.-U., and Kuriyan, J. (1997). Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK. Science 276, 431-435.
    • (1997) Science , vol.276 , pp. 431-435
    • Harrison, C.J.1    Hayer-Hartl, M.2    Di Liberto, M.3    Hartl, F.-U.4    Kuriyan, J.5
  • 40
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • Hartl, F.U. (1996). Molecular chaperones in cellular protein folding. Nature 381, 571-580.
    • (1996) Nature , vol.381 , pp. 571-580
    • Hartl, F.U.1
  • 41
    • 0029157195 scopus 로고
    • Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding
    • Hayer-Hartl, M., Martin, J., and Hartl, F.-U. (1995). Asymmetrical interaction of GroEL and GroES in the ATPase cycle of assisted protein folding. Science 269, 836-841.
    • (1995) Science , vol.269 , pp. 836-841
    • Hayer-Hartl, M.1    Martin, J.2    Hartl, F.-U.3
  • 43
    • 0344039806 scopus 로고    scopus 로고
    • GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1
    • Höhfeld, J., and Jentsch, S. (1997). GrpE-like regulation of the Hsc70 chaperone by the anti-apoptotic protein BAG-1. EMBO J. 16, 6209-6216.
    • (1997) EMBO J. , vol.16 , pp. 6209-6216
    • Höhfeld, J.1    Jentsch, S.2
  • 44
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES co-chaperonin at 2.8 Å resolution
    • Hunt, J.F., Weaver, A.J., Landry, S.J., Gierasch, L., and Deisenhofer, J. (1996). The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature 379, 37-45.
    • (1996) Nature , vol.379 , pp. 37-45
    • Hunt, J.F.1    Weaver, A.J.2    Landry, S.J.3    Gierasch, L.4    Deisenhofer, J.5
  • 45
    • 0030792944 scopus 로고    scopus 로고
    • Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage
    • Hunt, J.F., van der Vies, S.M., Henry, L., and Deisenhofer, J. (1997). Structural adaptations in the specialized bacteriophage T4 co-chaperonin Gp31 expand the size of the Anfinsen cage. Cell 90, 361-371.
    • (1997) Cell , vol.90 , pp. 361-371
    • Hunt, J.F.1    Van Der Vies, S.M.2    Henry, L.3    Deisenhofer, J.4
  • 46
    • 0027419011 scopus 로고
    • Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: Implications for the mechanism of assisted protein folding
    • Jackson, G.S., Staniforth, R.A., Halsall, D.J., Atkinson, T., Holbrook, J.J., Clarke, A.R., and Burston, S.G. (1993). Binding and hydrolysis of nucleotides in the chaperonin catalytic cycle: implications for the mechanism of assisted protein folding. Biochemistry 32, 2554-2563.
    • (1993) Biochemistry , vol.32 , pp. 2554-2563
    • Jackson, G.S.1    Staniforth, R.A.2    Halsall, D.J.3    Atkinson, T.4    Holbrook, J.J.5    Clarke, A.R.6    Burston, S.G.7
  • 47
    • 0028914392 scopus 로고
    • Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins
    • Jordan, R., and McMacken, R. (1995). Modulation of the ATPase activity of the molecular chaperone DnaK by peptides and the DnaJ and GrpE heat shock proteins. J. Biol. Chem. 270, 4563-4569.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4563-4569
    • Jordan, R.1    McMacken, R.2
  • 48
    • 15844372190 scopus 로고    scopus 로고
    • A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein
    • Karzai, A.W., and McMacken, R. (1996). A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein. J. Biol. Chem. 271, 11236-11246.
    • (1996) J. Biol. Chem. , vol.271 , pp. 11236-11246
    • Karzai, A.W.1    McMacken, R.2
  • 49
    • 0029926871 scopus 로고    scopus 로고
    • Effect of GroEL on there-folding kinetics of α-lactalbumin
    • Katsumata, K., Okazaki, A., and Kuwajima, K. (1996). Effect of GroEL on there-folding kinetics of α-lactalbumin. J. Mol. Biol. 258, 827-838.
    • (1996) J. Mol. Biol. , vol.258 , pp. 827-838
    • Katsumata, K.1    Okazaki, A.2    Kuwajima, K.3
  • 50
    • 0030668929 scopus 로고    scopus 로고
    • Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin
    • Klumpp, M., Baumeister, W., and Essen, L.-O. (1997). Structure of the substrate binding domain of the thermosome, an archaeal group II chaperonin. Cell 91, 263-270.
    • (1997) Cell , vol.91 , pp. 263-270
    • Klumpp, M.1    Baumeister, W.2    Essen, L.-O.3
  • 52
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer, T., Lu, C., Echols, H., Flanagan, J., Hayer, M.K., and Hartl, F.U. (1992a). Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356, 683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 53
    • 0027092285 scopus 로고
    • Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity
    • Langer, T., Pfeifer, G., Martin, J., Baumeister, W., and Hartl, F.-U. (1992b). Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 11, 4757-4765.
    • (1992) EMBO J. , vol.11 , pp. 4757-4765
    • Langer, T.1    Pfeifer, G.2    Martin, J.3    Baumeister, W.4    Hartl, F.-U.5
  • 55
    • 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, G.J., Roseman, A.M., Saibil, H.R., and 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
  • 56
    • 0031457264 scopus 로고    scopus 로고
    • PDZ-like domains mediate binding specificity in the Clp/ Hsp100 family of chaperones and protease regulatory subunits
    • Levchenko, I., Smith, C.K., Walsh, N.P., Sauer, R.T., and Baker, T.A. (1997) PDZ-like domains mediate binding specificity in the Clp/ Hsp100 family of chaperones and protease regulatory subunits. Cell 91, 939-947.
    • (1997) Cell , vol.91 , pp. 939-947
    • Levchenko, I.1    Smith, C.K.2    Walsh, N.P.3    Sauer, R.T.4    Baker, T.A.5
  • 57
    • 0029126927 scopus 로고
    • Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulator
    • Levy, E.J., McCarty, J., Bukau, B., and Chirico, W.J. (1995). Conserved ATPase and luciferase refolding activities between bacteria and yeast Hsp70 chaperones and modulator. FEBS Lett. 368, 435-440.
    • (1995) FEBS Lett. , vol.368 , pp. 435-440
    • Levy, E.J.1    McCarty, J.2    Bukau, B.3    Chirico, W.J.4
  • 58
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek, K., Marszalek, J., Ang, D., Georgopoulos, C., and Zylicz, M. (1991). Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc. Natl. Acad. Sci. USA 88, 2874-2878.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 59
    • 0029052538 scopus 로고
    • The DnaJ chaperone catalytically activates the dnak chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator
    • Liberek, K., Wall, D., and Georgopoulos, C. (1995). The DnaJ chaperone catalytically activates the DnaK chaperone to preferentially bind the sigma 32 heat shock transcriptional regulator. Proc. Natl. Acad. Sci. USA 92, 6224-6228
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6224-6228
    • Liberek, K.1    Wall, D.2    Georgopoulos, C.3
  • 60
    • 0028838951 scopus 로고
    • The hydrophobic nature of GroEL-substrate binding
    • Lin, S., Schwarz, F.P., and Eisenstein, E. (1995). The hydrophobic nature of GroEL-substrate binding. J. Biol. Chem. 270, 1011-1014.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1011-1014
    • Lin, S.1    Schwarz, F.P.2    Eisenstein, E.3
  • 61
    • 0030766287 scopus 로고    scopus 로고
    • Folding with a two-stroke motor
    • Lorimer, G.H. (1997). Folding with a two-stroke motor. Nature (New and Views) 388, 720-723.
    • (1997) Nature (New and Views) , vol.388 , pp. 720-723
    • Lorimer, G.H.1
  • 62
    • 0030024540 scopus 로고    scopus 로고
    • Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
    • Mande, S.C., Mehra, V., Bloom, B.R., and Hol, W.G.J. (1996). Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae. Science 271, 203-207.
    • (1996) Science , vol.271 , pp. 203-207
    • Mande, S.C.1    Mehra, V.2    Bloom, B.R.3    Hol, W.G.J.4
  • 63
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate
    • Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich A. L., and Hartl, F.-U. (1991). Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate. Nature 352, 36-42.
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hartl, F.-U.6
  • 65
    • 0029013908 scopus 로고
    • The role of ATP in the functional cycle of the DnaK chaperone system
    • McCarty, J.S., Buchberger, A., Reinstein, J., and Bukau, B. (1995). The role of ATP in the functional cycle of the DnaK chaperone system. J. Mol. Biol. 249, 126-137.
    • (1995) J. Mol. Biol. , vol.249 , pp. 126-137
    • McCarty, J.S.1    Buchberger, A.2    Reinstein, J.3    Bukau, B.4
  • 66
    • 0025820393 scopus 로고
    • Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese
    • Mendoza, J.A., Rogers, E., Lorimer, G.H., and Horowitz, P.M. (1991). Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J. Biol. Chem. 266, 13044-13049.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13044-13049
    • Mendoza, J.A.1    Rogers, E.2    Lorimer, G.H.3    Horowitz, P.M.4
  • 67
    • 0026489533 scopus 로고
    • Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese
    • Mendoza, J.A., Butler, M.C., and Horowitz, P.M. (1992). Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese. J. Biol. Chem. 267, 24648-24654.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24648-24654
    • Mendoza, J.A.1    Butler, M.C.2    Horowitz, P.M.3
  • 68
    • 0031556950 scopus 로고    scopus 로고
    • Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae
    • Miao, B., Davis, J.E., and Craig, E.A. (1997). Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae. J. Mol. Biol. 265, 541-552.
    • (1997) J. Mol. Biol. , vol.265 , pp. 541-552
    • Miao, B.1    Davis, J.E.2    Craig, E.A.3
  • 70
    • 0029090130 scopus 로고
    • Kinetic analysis of interactions between GroEL and reduced α-lactalbumin. Effect of groes and nucleotides
    • Murai, N., Taguchi, H., and Yoshida, M. (1995). Kinetic analysis of interactions between GroEL and reduced α-lactalbumin. Effect of GroES and nucleotides. J. Biol. Chem. 270, 19957-19963.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19957-19963
    • Murai, N.1    Taguchi, H.2    Yoshida, M.3
  • 71
    • 0030018744 scopus 로고    scopus 로고
    • Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis
    • O'Brien, M.C., Flaherty, K.M., and McKay, D.B. (1996). Lysine 71 of the chaperone protein Hsc70 is essential for ATP hydrolysis. J. Biol. Chem. 271, 15874-15878.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15874-15878
    • O'Brien, M.C.1    Flaherty, K.M.2    McKay, D.B.3
  • 72
    • 0030945296 scopus 로고    scopus 로고
    • GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism
    • Packschies, L., Theyssen, H., Buchberger, A., Bukau, B., Goody, R.S., and Reinstein, J. (1997). GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry 36, 3417-3422.
    • (1997) Biochemistry , vol.36 , pp. 3417-3422
    • Packschies, L.1    Theyssen, H.2    Buchberger, A.3    Bukau, B.4    Goody, R.S.5    Reinstein, J.6
  • 74
    • 0030581175 scopus 로고    scopus 로고
    • NMR structure of the J-domain and the Gly/ Phe-rich region of the Escherichia coli DnaJ chaperone
    • Pellecchia, M., Szyperski, T., Wall, D., Georgopoulos, C., and Wüthrich, K. (1996). NMR structure of the J-domain and the Gly/ Phe-rich region of the Escherichia coli DnaJ chaperone. J. Mol. Biol. 260, 236-250.
    • (1996) J. Mol. Biol. , vol.260 , pp. 236-250
    • Pellecchia, M.1    Szyperski, T.2    Wall, D.3    Georgopoulos, C.4    Wüthrich, K.5
  • 76
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C., Roe, S.M., O'Brien, R., Ladbury, J.E., Piper, P.W., and Pearl, L.H. (1997). Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell 90, 65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 77
    • 0030581148 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain
    • Qian, Y.Q., Patel, D., Hartl, F.U., and McColl, D.J. (1996). Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain. J. Mol. Biol. 260, 224-235.
    • (1996) J. Mol. Biol. , vol.260 , pp. 224-235
    • Qian, Y.Q.1    Patel, D.2    Hartl, F.U.3    McColl, D.J.4
  • 78
    • 0029087065 scopus 로고
    • Chaperonins can catalyze the reversal of early aggregation steps when a protein misfolds
    • Ranson, N.A., Dunster, N.J., Burston, S.G., and Clarke, A.R. (1995). Chaperonins can catalyze the reversal of early aggregation steps when a protein misfolds. J. Mol. Biol. 250, 581-586.
    • (1995) J. Mol. Biol. , vol.250 , pp. 581-586
    • Ranson, N.A.1    Dunster, N.J.2    Burston, S.G.3    Clarke, A.R.4
  • 79
    • 0031557387 scopus 로고    scopus 로고
    • Binding, encapsulation and ejection: Substrate dynamics during a chaperonin-assisted folding reaction
    • Ranson, N.A., Burston, S.G., and Clarke, A.R. (1997). Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction. J. Mol. Biol. 266, 656-664.
    • (1997) J. Mol. Biol. , vol.266 , pp. 656-664
    • Ranson, N.A.1    Burston, S.G.2    Clarke, A.R.3
  • 80
    • 0029863755 scopus 로고    scopus 로고
    • GroEL binds to and unfolds rhodanese posttranslationally
    • Reid, B.G., and Flynn, G.C. (1996). GroEL binds to and unfolds rhodanese posttranslationally. J. Biol. Chem. 271, 7212-7217.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7212-7217
    • Reid, B.G.1    Flynn, G.C.2
  • 82
    • 0030592538 scopus 로고    scopus 로고
    • The chaperonin ATPase cycle: Mechanism of allosteric switching and movements of substrate-binding domains in GroEL
    • Roseman, A.M., Chen, S., White, H., Braig, K., and Saibil, H.R. (1996). The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell 87, 241-251.
    • (1996) Cell , vol.87 , pp. 241-251
    • Roseman, A.M.1    Chen, S.2    White, H.3    Braig, K.4    Saibil, H.R.5
  • 83
    • 0041026092 scopus 로고    scopus 로고
    • Interaction of Hsp70 chaperones with substrates
    • Rüdiger, S., Buchberger, A., and Bukau, B. (1997a). Interaction of Hsp70 chaperones with substrates. Nature Struct. Biol. 4, 342-349.
    • (1997) Nature Struct. Biol. , vol.4 , pp. 342-349
    • Rüdiger, S.1    Buchberger, A.2    Bukau, B.3
  • 84
    • 0030976048 scopus 로고    scopus 로고
    • Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
    • Rüdiger, S., Germeroth, L., Schneider-Mergener, J., and Bukau, B. (1997b). Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 16, 1501-1507.
    • (1997) EMBO J. , vol.16 , pp. 1501-1507
    • Rüdiger, S.1    Germeroth, L.2    Schneider-Mergener, J.3    Bukau, B.4
  • 85
    • 0030804446 scopus 로고    scopus 로고
    • Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL
    • Rye, H.S., Burston, S.G., Fenton, W.A., Beechem, J.M., Xu, Z., Sigler, P.B., and Horwich, A.L. (1997). Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 388, 792-798.
    • (1997) Nature , vol.388 , pp. 792-798
    • Rye, H.S.1    Burston, S.G.2    Fenton, W.A.3    Beechem, J.M.4    Xu, Z.5    Sigler, P.B.6    Horwich, A.L.7
  • 86
  • 87
    • 0028268243 scopus 로고
    • Kinetics of molecular chaperone action
    • Schmid, D., Baici, A., Gehring, H., and Christen, P. (1994). Kinetics of molecular chaperone action. Science 263, 971-973.
    • (1994) Science , vol.263 , pp. 971-973
    • Schmid, D.1    Baici, A.2    Gehring, H.3    Christen, P.4
  • 88
    • 0027427986 scopus 로고
    • DnaK, DnaJ, and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage
    • Schröder, H., Langer, T., Hartl, F.-U., and Bukau, B. (1993). DnaK, DnaJ, and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J. 12, 4137-4144.
    • (1993) EMBO J. , vol.12 , pp. 4137-4144
    • Schröder, H.1    Langer, T.2    Hartl, F.-U.3    Bukau, B.4
  • 89
    • 0029157314 scopus 로고
    • Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding
    • Smith, K.E., and Fisher, M.T. (1995). Interactions between the GroE chaperonins and rhodanese. Multiple intermediates and release and rebinding. J. Biol. Chem. 270, 21517-21523.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21517-21523
    • Smith, K.E.1    Fisher, M.T.2
  • 90
    • 0029126624 scopus 로고
    • The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:Glycoprotein glucosyltransferase
    • Sousa, M., and Parodi, A.J. (1995). The molecular basis for the recognition of misfolded glycoproteins by the UDP-Glc:glycoprotein glucosyltransferase. EMBO J. 14, 4196-4203.
    • (1995) EMBO J. , vol.14 , pp. 4196-4203
    • Sousa, M.1    Parodi, A.J.2
  • 91
    • 0030994081 scopus 로고    scopus 로고
    • How GroES regulates binding of non-native protein to GroEL
    • Sparrer, H., and Buchner, J. (1997). How GroES regulates binding of non-native protein to GroEL. J. Biol. Chem. 272, 14080-14086.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14080-14086
    • Sparrer, H.1    Buchner, J.2
  • 92
    • 0028151509 scopus 로고
    • The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ and GrpE
    • Szabo, A., Langer, T., Schröder, H., Flanagan, J., Bukau, B., and Hartl, F.U. (1994). The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system-DnaK, DnaJ and GrpE. Proc. Natl. Acad. Sci. USA 91, 10345-10349.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10345-10349
    • Szabo, A.1    Langer, T.2    Schröder, H.3    Flanagan, J.4    Bukau, B.5    Hartl, F.U.6
  • 93
    • 0030030946 scopus 로고    scopus 로고
    • A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates
    • Szabo, A., Korzun, R., Hartl, F.U., and Flanagan, J. (1996). A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. EMBO J. 15, 408-417.
    • (1996) EMBO J. , vol.15 , pp. 408-417
    • Szabo, A.1    Korzun, R.2    Hartl, F.U.3    Flanagan, J.4
  • 94
    • 0027987996 scopus 로고
    • NMR structure determination of the Escherichia coli DnaJ molelcular chaperone: Secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain
    • Szyperski, T., Pellecchia, M., Wall, D., Georgopoulos, C., and Wüthrich, K. (1994). NMR structure determination of the Escherichia coli DnaJ molelcular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain. Proc. Natl. Acad. Sci. USA 91, 11343-11347.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11343-11347
    • Szyperski, T.1    Pellecchia, M.2    Wall, D.3    Georgopoulos, C.4    Wüthrich, K.5
  • 95
    • 0028855745 scopus 로고
    • Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin
    • Taguchi, H., and Yoshida, M. (1995). Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin. FEBS Lett. 359, 195-198.
    • (1995) FEBS Lett. , vol.359 , pp. 195-198
    • Taguchi, H.1    Yoshida, M.2
  • 96
    • 0030589149 scopus 로고    scopus 로고
    • The second step of ATP binding to DnaK induces peptide release
    • Theyssen, H., Schuster, H.-P., Bukau, B., and Reinstein, J. (1996). The second step of ATP binding to DnaK induces peptide release. J. Mol. Biol. 263, 657-670.
    • (1996) J. Mol. Biol. , vol.263 , pp. 657-670
    • Theyssen, H.1    Schuster, H.-P.2    Bukau, B.3    Reinstein, J.4
  • 97
    • 0028989966 scopus 로고
    • Specificity in chaperonin-mediated protein folding
    • Tian, G., Vainberg, I.E., Tap, W.D., Lewis, S.A., and Cowan, N.J. (1995). Specificity in chaperonin-mediated protein folding. Nature 375, 250-253.
    • (1995) Nature , vol.375 , pp. 250-253
    • Tian, G.1    Vainberg, I.E.2    Tap, W.D.3    Lewis, S.A.4    Cowan, N.J.5
  • 98
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • Todd, M.J., Viitanen, P.V., and Lorimer, G.H. (1994). Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 265, 659-666.
    • (1994) Science , vol.265 , pp. 659-666
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 99
    • 0030006212 scopus 로고    scopus 로고
    • Chaperonin-facilitated protein folding: Optimization of rate and yield by an iterative annealing mechanism
    • Todd, M.J., Lorimer, G.H., and Thirumalai, D. (1996). Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc. Natl. Acad. Sci. USA 93, 4030-4035.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4030-4035
    • Todd, M.J.1    Lorimer, G.H.2    Thirumalai, D.3
  • 100
    • 0028170215 scopus 로고
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication
    • 2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for λ replication. J. Biol. Chem. 269, 5446-5451.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5446-5451
    • Wall, D.1    Zylicz, M.2    Georgopoulos, C.3
  • 101
    • 0029837424 scopus 로고    scopus 로고
    • A thermodynamic coupling mechanism for GroEL-mediated unfolding
    • Walter, S., Lorimer, G.H., and Schmid, F.X. (1996). A thermodynamic coupling mechanism for GroEL-mediated unfolding. Proc. Natl. Acad. Sci. USA 93, 9425-9430.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9425-9430
    • Walter, S.1    Lorimer, G.H.2    Schmid, F.X.3
  • 102
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
    • Weissman, J.S., Kashi, Y., Fenton, W.A., and Horwich, A.L. (1994). GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms. Cell 78, 693-702.
    • (1994) Cell , vol.78 , pp. 693-702
    • Weissman, J.S.1    Kashi, Y.2    Fenton, W.A.3    Horwich, A.L.4
  • 104
    • 0030056969 scopus 로고    scopus 로고
    • Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction
    • Weissman, J.S., Rye, H.S., Fenton, W.A., Beechem, J.M., and Horwich, A.L. (1996). Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 84, 481-490.
    • (1996) Cell , vol.84 , pp. 481-490
    • Weissman, J.S.1    Rye, H.S.2    Fenton, W.A.3    Beechem, J.M.4    Horwich, A.L.5
  • 105
    • 0028980922 scopus 로고
    • Solution small-angle X-ray scattering study of the molecular chaperone hsc70 and its subfragments
    • Wilbanks, S.M., Chen, L., Tsuruta, H., Hodgson, K.O., and McKay, D.B. (1995). Solution small-angle X-ray scattering study of the molecular chaperone hsc70 and its subfragments. Biochemistry 34, 12095-12106.
    • (1995) Biochemistry , vol.34 , pp. 12095-12106
    • Wilbanks, S.M.1    Chen, L.2    Tsuruta, H.3    Hodgson, K.O.4    McKay, D.B.5
  • 108
    • 0029004759 scopus 로고
    • Nested cooperativity in the AT-Pase activity of the oligomeric chaperonin GroEL
    • Yifrach, O., and Horovitz, A. (1995). Nested cooperativity in the AT-Pase activity of the oligomeric chaperonin GroEL. Biochemistry 34, 5303-5308.
    • (1995) Biochemistry , vol.34 , pp. 5303-5308
    • Yifrach, O.1    Horovitz, A.2
  • 109
    • 0028260023 scopus 로고
    • Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
    • Zahn, R., Spitzfaden, C., Ottiger, M., Wüthrich, K., and Plückthun, A. (1994). Destabilization of the complete protein secondary structure on binding to the chaperone GroEL. Nature 368, 261-265.
    • (1994) Nature , vol.368 , pp. 261-265
    • Zahn, R.1    Spitzfaden, C.2    Ottiger, M.3    Wüthrich, K.4    Plückthun, A.5
  • 110
    • 0030061845 scopus 로고    scopus 로고
    • Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB
    • Zahn, R., Perrett, S., Stenberg, G., and Fersht, A.R. (1996). Catalysis of amide proton exchange by the molecular chaperones GroEL and SecB. Science 271, 642-645.
    • (1996) Science , vol.271 , pp. 642-645
    • Zahn, R.1    Perrett, S.2    Stenberg, G.3    Fersht, A.R.4
  • 112
    • 0028921261 scopus 로고
    • The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates
    • Ziegelhoffer, T., Lopez-Buesa, P., and Craig, E. (1995). The dissociation of ATP from hsp70 of Saccharomyces cerevisiae is stimulated by both Ydj1p and peptide substrates. J. Biol. Chem. 270, 10412-10419.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10412-10419
    • Ziegelhoffer, T.1    Lopez-Buesa, P.2    Craig, E.3


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