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Volumn 10, Issue 5, 2009, Pages 2066-2083

GroEL-assisted protein folding: Does it occur within the chaperonin inner cavity?

Author keywords

Chaperones; GroEL ES chaperonin system; Protein aggregation; Protein folding

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; LIGAND; POLYPEPTIDE;

EID: 67049087960     PISSN: None     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms10052066     Document Type: Review
Times cited : (25)

References (114)
  • 1
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. Principles that govern the folding of protein chains. Science 1973, 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 2
    • 0026700861 scopus 로고
    • Protein folding and protein refolding
    • Seckler, R.; Jaenicke, R. Protein folding and protein refolding. FASEB J. 1992, 6, 2545-2552.
    • (1992) FASEB J , vol.6 , pp. 2545-2552
    • Seckler, R.1    Jaenicke, R.2
  • 3
    • 0023668329 scopus 로고
    • Proteins as molecular chaperones
    • Ellis, J. Proteins as molecular chaperones. Nature 1987, 328, 378-379.
    • (1987) Nature , vol.328 , pp. 378-379
    • Ellis, J.1
  • 4
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M.J.; Sambrook, J. Protein folding in the cell. Nature 1992, 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 5
    • 0023761756 scopus 로고
    • Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein
    • Bochkareva, E.S.; Lissin, N.M.; Girshovich, A.S. Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein. Nature 1988, 336, 254-257.
    • (1988) Nature , vol.336 , pp. 254-257
    • Bochkareva, E.S.1    Lissin, N.M.2    Girshovich, A.S.3
  • 6
    • 0030052910 scopus 로고    scopus 로고
    • Roles of molecular chaperones in protein degradation
    • Hayes, S.A.; Dice, J.F. Roles of molecular chaperones in protein degradation. J. Cell Biol. 1996, 132, 255-258.
    • (1996) J. Cell Biol , vol.132 , pp. 255-258
    • Hayes, S.A.1    Dice, J.F.2
  • 7
    • 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.; Goldberg, A. Rapid degradation of an abnormal protein in Escherichia coli proceeds through repeated cycles of association with GroEL. J.Biol.Chem. 1999, 274, 37743-37749.
    • (1999) J.Biol.Chem , vol.274 , pp. 37743-37749
    • Kandror, O.1    Sherman, M.2    Goldberg, A.3
  • 8
    • 0030844524 scopus 로고    scopus 로고
    • Protein folding. The difference with prokaryotes
    • Gething, M.J. Protein folding. The difference with prokaryotes. Nature 1997, 388, 329-331.
    • (1997) Nature , vol.388 , pp. 329-331
    • Gething, M.J.1
  • 10
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B.; Horwich, A.L. The Hsp70 and Hsp60 chaperone machines. Cell 1998, 92, 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 11
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • Fink, A.L. Chaperone-mediated protein folding. Physiol. Rev. 1999, 79, 425-449.
    • (1999) Physiol. Rev , vol.79 , pp. 425-449
    • Fink, A.L.1
  • 13
    • 0027925678 scopus 로고
    • What does protein refolding in vitro tell us about protein folding in the cell?
    • Jaenicke, R. What does protein refolding in vitro tell us about protein folding in the cell? Philos. Trans. R. Soc. Lond B Biol. Sci. 1993, 339, 287-294.
    • (1993) Philos. Trans. R. Soc. Lond B Biol. Sci , vol.339 , pp. 287-294
    • Jaenicke, R.1
  • 14
    • 0034646559 scopus 로고    scopus 로고
    • A thermodynamic coupling mechanism can explain the GroELmediated acceleration of the folding of barstar
    • Bhutani, N.; Udgaonkar, J.B. A thermodynamic coupling mechanism can explain the GroELmediated acceleration of the folding of barstar. J. Mol. Biol. 2000, 297, 1037-1044.
    • (2000) J. Mol. Biol , vol.297 , pp. 1037-1044
    • Bhutani, N.1    Udgaonkar, J.B.2
  • 16
    • 0034695615 scopus 로고    scopus 로고
    • GroEL-substrate interactions: Molding the fold, or folding the mold?
    • Feltham, J.L.; Gierasch, L.M. GroEL-substrate interactions: molding the fold, or folding the mold? Cell 2000, 100, 193-196.
    • (2000) Cell , vol.100 , pp. 193-196
    • Feltham, J.L.1    Gierasch, L.M.2
  • 17
    • 0027970179 scopus 로고
    • Protein folding. Secrets of a double-doughnut
    • Hartl, F.U. Protein folding. Secrets of a double-doughnut. Nature 1994, 371, 557-559.
    • (1994) Nature , vol.371 , pp. 557-559
    • Hartl, F.U.1
  • 18
    • 0029664944 scopus 로고    scopus 로고
    • The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S
    • Boisvert, D.C.; Wang, J.; Otwinowski, Z.; Horwich, A.L.; Sigler, P.B. The 2.4 Å crystal structure of the bacterial chaperonin GroEL complexed with ATP gamma S. Nat. Struct. Biol. 1996, 3, 170-177.
    • (1996) Nat. 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
  • 21
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution
    • Braig, K.; Adams, P.D.; Brunger, A.T. Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nat. Struct. Biol. 1995, 2, 1083-1094.
    • (1995) Nat. Struct. Biol , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brunger, A.T.3
  • 22
    • 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.; Saibil, H.R. Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy. Nature 1994, 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
  • 23
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton, W.A.; Kashi, Y.; Furtak, K.; Horwich, A.L. Residues in chaperonin GroEL required for polypeptide binding and release. Nature 1994, 371, 614-619.
    • (1994) Nature , vol.371 , pp. 614-619
    • Fenton, W.A.1    Kashi, Y.2    Furtak, K.3    Horwich, A.L.4
  • 24
    • 0027214204 scopus 로고
    • Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
    • Horwich, A.L.; Low, K.B.; Fenton, W.A.; Hirshfield, I.N.; Furtak, K. Folding in vivo of bacterial cytoplasmic proteins: role of GroEL. Cell 1993, 74, 909-917.
    • (1993) Cell , vol.74 , pp. 909-917
    • Horwich, A.L.1    Low, K.B.2    Fenton, W.A.3    Hirshfield, I.N.4    Furtak, K.5
  • 26
    • 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.; Deisenhofer, J. The crystal structure of the GroES co-chaperonin at 2.8 Å resolution. Nature 1996, 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
  • 27
    • 0028220199 scopus 로고
    • Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody
    • Ishii, N.; Taguchi, H.; Sasabe, H.; Yoshida, M. Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody. J. Mol. Biol. 1994, 236, 691-696.
    • (1994) J. Mol. Biol , vol.236 , pp. 691-696
    • Ishii, N.1    Taguchi, H.2    Sasabe, H.3    Yoshida, M.4
  • 28
    • 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.; Hartl, F.U. Chaperonin-mediated protein folding: GroES binds to one end of the GroEL cylinder, which accommodates the protein substrate within its central cavity. EMBO J. 1992, 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
  • 29
    • 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.; Saibil, H.R. The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL. Cell 1996, 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
  • 30
    • 0029643911 scopus 로고    scopus 로고
    • Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering
    • Thiyagarajan, P.; Henderson, S.J.; Joachimiak, A. Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering. Structure. 1996, 4, 79-88.
    • (1996) Structure , vol.4 , pp. 79-88
    • Thiyagarajan, P.1    Henderson, S.J.2    Joachimiak, A.3
  • 31
    • 0027065105 scopus 로고
    • Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins
    • Viitanen, P.V.; Gatenby, A.A.; Lorimer, G.H. Purified chaperonin 60 (groEL) interacts with the nonnative states of a multitude of Escherichia coli proteins. Protein Sci. 1992, 1, 363-369.
    • (1992) Protein Sci , vol.1 , pp. 363-369
    • Viitanen, P.V.1    Gatenby, A.A.2    Lorimer, G.H.3
  • 32
    • 0030870719 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES- (ADP)7 chaperonin complex
    • Xu, Z.; Horwich, A.L.; Sigler, P.B. The crystal structure of the asymmetric GroEL-GroES- (ADP)7 chaperonin complex. Nature 1997, 388, 741-750.
    • (1997) Nature , vol.388 , pp. 741-750
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 33
    • 58149229533 scopus 로고    scopus 로고
    • Chaperonin complex with a newly folded protein encapsulated in the folding chamber
    • Clare, D.K.; Bakkes, P.J.; van Heerikhuizen H.; van der Vies, S.M.; Saibil, H.R. Chaperonin complex with a newly folded protein encapsulated in the folding chamber. Nature 2009, 457, 107-110.
    • (2009) Nature , vol.457 , pp. 107-110
    • Clare, D.K.1    Bakkes, P.J.2    van Heerikhuizen, H.3    van der Vies, S.M.4    Saibil, H.R.5
  • 36
    • 0032822103 scopus 로고    scopus 로고
    • Principles of protein folding in the cellular environment
    • Ellis, R.J.; Hartl, F.U. Principles of protein folding in the cellular environment. Curr. Opin. Struct. Biol. 1999, 9, 102-110.
    • (1999) Curr. Opin. Struct. Biol , vol.9 , pp. 102-110
    • Ellis, R.J.1    Hartl, F.U.2
  • 37
    • 0027427326 scopus 로고
    • The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
    • Martin, J.; Mayhew, M.; Langer, T.; Hartl, F.U. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature 1993, 366, 228-233.
    • (1993) Nature , vol.366 , pp. 228-233
    • Martin, J.1    Mayhew, M.2    Langer, T.3    Hartl, F.U.4
  • 39
    • 33646945039 scopus 로고    scopus 로고
    • More than Just a folding cage
    • Radford, S.E. GroEL: More than Just a folding cage. Cell 2006, 125, 831-833.
    • (2006) Cell , vol.125 , pp. 831-833
    • Radford1    GroEL, S.E.2
  • 40
    • 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.; Horwich, A.L. Characterization of the active intermediate of a GroEL-GroES-mediated protein folding reaction. Cell 1996, 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
  • 41
    • 0033598941 scopus 로고    scopus 로고
    • The crystal structure of a GroEL/peptide complex: Plasticity as a basis for substrate diversity
    • Chen, L.; Sigler, P.B. The crystal structure of a GroEL/peptide complex: plasticity as a basis for substrate diversity. Cell 1999, 99, 757-768.
    • (1999) Cell , vol.99 , pp. 757-768
    • Chen, L.1    Sigler, P.B.2
  • 42
    • 0030750584 scopus 로고    scopus 로고
    • In vivo observation of polypeptide flux through the bacterial chaperonin system
    • Ewalt, K.L.; Hendrick, J.P.; Houry, W.A.; Hartl, F.U. In vivo observation of polypeptide flux through the bacterial chaperonin system. Cell 1997, 90, 491-500.
    • (1997) Cell , vol.90 , pp. 491-500
    • Ewalt, K.L.1    Hendrick, J.P.2    Houry, W.A.3    Hartl, F.U.4
  • 43
    • 0032920145 scopus 로고    scopus 로고
    • Binding of polylysine to GroEL. Inhibition of the refolding of mMDH
    • Lau, C.K.; Churchich, J.E. Binding of polylysine to GroEL. Inhibition of the refolding of mMDH. Biochim. Biophys. Acta 1999, 1431, 282-289.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 282-289
    • Lau, C.K.1    Churchich, J.E.2
  • 44
    • 0027509618 scopus 로고
    • Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro
    • Brunschier, R.; Danner, M.; Seckler, R. Interactions of phage P22 tailspike protein with GroE molecular chaperones during refolding in vitro. J. Biol. Chem. 1993, 268, 2767-2772.
    • (1993) J. Biol. Chem , vol.268 , pp. 2767-2772
    • Brunschier, R.1    Danner, M.2    Seckler, R.3
  • 45
    • 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.; King, J. Selective in vivo rescue by GroEL/ES of thermolabile folding intermediates to phage P22 structural proteins. J. Biol. Chem. 1994, 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
  • 46
    • 0034698058 scopus 로고    scopus 로고
    • Interactions of GroEL/GroES with a heterodimeric intermediate during ?2?2 assembly of mitochondrial branched-chain ?-ketoacid dehydrogenase. cis Capping of the native-like 86-kDa intermediate by GroES
    • Song, J.L.; Wynn, R.M.; Chuang, D.T. Interactions of GroEL/GroES with a heterodimeric intermediate during ?2?2 assembly of mitochondrial branched-chain ?-ketoacid dehydrogenase. cis Capping of the native-like 86-kDa intermediate by GroES. J. Biol. Chem. 2000, 275, 22305-22312.
    • (2000) J. Biol. Chem , vol.275 , pp. 22305-22312
    • Song, J.L.1    Wynn, R.M.2    Chuang, D.T.3
  • 47
    • 0035913910 scopus 로고    scopus 로고
    • GroEL/GroES-mediated folding of a protein too large to be encapsulated
    • Chaudhuri, T.K.; Farr, G.W.; Fenton, W.A.; Rospert, S.; Horwich, A.L. GroEL/GroES-mediated folding of a protein too large to be encapsulated. Cell 2001, 107, 235-246.
    • (2001) Cell , vol.107 , pp. 235-246
    • Chaudhuri, T.K.1    Farr, G.W.2    Fenton, W.A.3    Rospert, S.4    Horwich, A.L.5
  • 48
    • 35748954020 scopus 로고    scopus 로고
    • Chaperone-assisted refolding of Escherichia coli maltodextrin glucosidase
    • Paul, S.; Punam, S.; Chaudhuri, T.K. Chaperone-assisted refolding of Escherichia coli maltodextrin glucosidase. FEBS J. 2007, 274, 6000-6010.
    • (2007) FEBS J , vol.274 , pp. 6000-6010
    • Paul, S.1    Punam, S.2    Chaudhuri, T.K.3
  • 49
    • 0037926429 scopus 로고    scopus 로고
    • Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes
    • Farr, G.W.; Fenton, W.A.; Chaudhuri, T.K.; Clare, D.K.; Saibil, H.R.; Horwich, A.L. Folding with and without encapsulation by cis- and trans-only GroEL-GroES complexes. EMBO J. 2003, 22, 3220-3230.
    • (2003) EMBO J , vol.22 , pp. 3220-3230
    • Farr, G.W.1    Fenton, W.A.2    Chaudhuri, T.K.3    Clare, D.K.4    Saibil, H.R.5    Horwich, A.L.6
  • 50
    • 0024820705 scopus 로고
    • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP
    • Goloubinoff, P.; Christeller, J.T.; Gatenby, A.A.; Lorimer, G.H. Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and Mg-ATP. Nature 1989, 342, 884-889.
    • (1989) Nature , vol.342 , pp. 884-889
    • Goloubinoff, P.1    Christeller, J.T.2    Gatenby, A.A.3    Lorimer, G.H.4
  • 51
    • 0027447796 scopus 로고
    • Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES) do not catalyse the refolding of mitochondrial malate dehydrogenase
    • Miller, A.D.; Maghlaoui, K.; Albanese, G.; Kleinjan, D.A.; Smith, C. Escherichia coli chaperonins cpn60 (groEL) and cpn10 (groES) do not catalyse the refolding of mitochondrial malate dehydrogenase. Biochem. J. 1993, 291, 139-144.
    • (1993) Biochem. J , vol.291 , pp. 139-144
    • Miller, A.D.1    Maghlaoui, K.2    Albanese, G.3    Kleinjan, D.A.4    Smith, C.5
  • 53
    • 0029664316 scopus 로고    scopus 로고
    • Toward a mechanism for GroEL.GroES chaperone activity: An ATPase-gated and -pulsed folding and annealing cage
    • Corrales, F.J.; Fersht, A.R. Toward a mechanism for GroEL.GroES chaperone activity: an ATPase-gated and -pulsed folding and annealing cage. Proc. Natl. Acad. Sci. USA 1996, 93, 4509-4512.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4509-4512
    • Corrales, F.J.1    Fersht, A.R.2
  • 54
    • 0028307452 scopus 로고
    • Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivation
    • Kawata, Y.; Nosaka, K.; Hongo, K.; Mizobata, T.; Nagai, J. Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivation. FEBS Lett. 1994, 345, 229-232.
    • (1994) FEBS Lett , vol.345 , pp. 229-232
    • Kawata, Y.1    Nosaka, K.2    Hongo, K.3    Mizobata, T.4    Nagai, J.5
  • 55
    • 0029975103 scopus 로고    scopus 로고
    • Dynamics of the GroEL-protein complex: Effects of nucleotides and folding mutants
    • Sparrer, H.; Lilie, H.; Buchner, J. Dynamics of the GroEL-protein complex: effects of nucleotides and folding mutants. J. Mol. Biol. 1996, 258, 74-87.
    • (1996) J. Mol. Biol , vol.258 , pp. 74-87
    • Sparrer, H.1    Lilie, H.2    Buchner, J.3
  • 56
    • 0025940841 scopus 로고
    • Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase
    • Viitanen, P.V.; Donaldson, G.K.; Lorimer, G.H.; Lubben, T.H.; Gatenby, A.A. Complex interactions between the chaperonin 60 molecular chaperone and dihydrofolate reductase. Biochemistry 1991, 30, 9716-9723.
    • (1991) Biochemistry , vol.30 , pp. 9716-9723
    • Viitanen, P.V.1    Donaldson, G.K.2    Lorimer, G.H.3    Lubben, T.H.4    Gatenby, A.A.5
  • 57
    • 0029858706 scopus 로고    scopus 로고
    • Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis
    • Hayer-Hartl, M.K.; Weber, F.; Hartl, F.U. Mechanism of chaperonin action: GroES binding and release can drive GroEL-mediated protein folding in the absence of ATP hydrolysis. EMBO J. 1996, 15, 6111-6121.
    • (1996) EMBO J , vol.15 , pp. 6111-6121
    • Hayer-Hartl, M.K.1    Weber, F.2    Hartl, F.U.3
  • 58
    • 0028231826 scopus 로고
    • Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10
    • Staniforth, R.A.; Burston, S.G.; Atkinson, T.; Clarke, A.R. Affinity of chaperonin-60 for a protein substrate and its modulation by nucleotides and chaperonin-10. Biochem. J. 1994, 300, 651-658.
    • (1994) Biochem. J , vol.300 , pp. 651-658
    • Staniforth, R.A.1    Burston, S.G.2    Atkinson, T.3    Clarke, A.R.4
  • 59
    • 0030059690 scopus 로고    scopus 로고
    • The molten globule state of alpha-lactalbumin
    • Kuwajima, K. The molten globule state of alpha-lactalbumin. FASEB J. 1996, 10, 102-109.
    • (1996) FASEB J , vol.10 , pp. 102-109
    • Kuwajima, K.1
  • 60
    • 0026416043 scopus 로고
    • Chaperoninmediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
    • Martin, J.; Langer, T.; Boteva, R.; Schramel, A.; Horwich, A.L.; Hartl, F.U. Chaperoninmediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 1991, 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
  • 62
    • 0029926871 scopus 로고    scopus 로고
    • Effect of GroEL on the re-folding kinetics of alphalactalbumin
    • Katsumata, K.; Okazaki, A.; Kuwajima, K. Effect of GroEL on the re-folding kinetics of alphalactalbumin. J. Mol. Biol. 1996, 258, 827-838.
    • (1996) J. Mol. Biol , vol.258 , pp. 827-838
    • Katsumata, K.1    Okazaki, A.2    Kuwajima, K.3
  • 63
    • 21644446654 scopus 로고    scopus 로고
    • The interaction of the GroEL chaperone with early kinetic intermediates of renaturing proteins inhibits the formation of their native structure
    • Marchenkov, V.V.; Sokolovskii, I.V.; Kotova, N.V.; Galzitskaya, O.V.; Bochkareva, E.S.; Girshovich, A.S.; Semisotnov, G.V. The interaction of the GroEL chaperone with early kinetic intermediates of renaturing proteins inhibits the formation of their native structure. Biofizika 2004, 49, 987-994.
    • (2004) Biofizika , vol.49 , pp. 987-994
    • Marchenkov, V.V.1    Sokolovskii, I.V.2    Kotova, N.V.3    Galzitskaya, O.V.4    Bochkareva, E.S.5    Girshovich, A.S.6    Semisotnov, G.V.7
  • 64
    • 0031588017 scopus 로고    scopus 로고
    • Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL
    • Perrett, S.; Zahn, R.; Stenberg, G.; Fersht, A.R. Importance of electrostatic interactions in the rapid binding of polypeptides to GroEL. J. Mol. Biol. 1997, 269, 892-901.
    • (1997) J. Mol. Biol , vol.269 , pp. 892-901
    • Perrett, S.1    Zahn, R.2    Stenberg, G.3    Fersht, A.R.4
  • 65
    • 0028334547 scopus 로고
    • Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin
    • Hayer-Hartl, M.K.; Ewbank, J.J.; Creighton, T.E.; Hartl, F.U. Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin. EMBO J. 1994, 13, 3192-3202.
    • (1994) EMBO J , vol.13 , pp. 3192-3202
    • Hayer-Hartl, M.K.1    Ewbank, J.J.2    Creighton, T.E.3    Hartl, F.U.4
  • 66
    • 0030582682 scopus 로고    scopus 로고
    • Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL
    • Katsumata, K.; Okazaki, A.; Tsurupa, G.P.; Kuwajima, K. Dominant forces in the recognition of a transient folding intermediate of alpha-lactalbumin by GroEL. J. Mol. Biol. 1996, 264, 643-649.
    • (1996) J. Mol. Biol , vol.264 , pp. 643-649
    • Katsumata, K.1    Okazaki, A.2    Tsurupa, G.P.3    Kuwajima, K.4
  • 68
    • 33845651724 scopus 로고    scopus 로고
    • Affinity chromatography of GroEL chaperonin based on denatured proteins: Role of electrostatic interactions in regulation of GroEL affinity for protein substrates
    • Marchenko, N.I.; Marchenkov, V.V.; Kaisheva, A.L.; Kashparov, I.A.; Kotova, N.V.; Kaliman, P.A.; Semisotnov, G.V. Affinity chromatography of GroEL chaperonin based on denatured proteins: role of electrostatic interactions in regulation of GroEL affinity for protein substrates. Biochemistry (Moscow) 2006, 71, 1357-1364.
    • (2006) Biochemistry (Moscow) , vol.71 , pp. 1357-1364
    • Marchenko, N.I.1    Marchenkov, V.V.2    Kaisheva, A.L.3    Kashparov, I.A.4    Kotova, N.V.5    Kaliman, P.A.6    Semisotnov, G.V.7
  • 69
    • 0025331905 scopus 로고
    • Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent
    • Viitanen, P.V.; Lubben, T.H.; Reed, J.; Goloubinoff, P.; O'Keefe, D.P.; Lorimer, G.H. Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groEL) are K+ dependent. Biochemistry 1990, 29, 5665-5671.
    • (1990) Biochemistry , vol.29 , pp. 5665-5671
    • Viitanen, P.V.1    Lubben, T.H.2    Reed, J.3    Goloubinoff, P.4    O'Keefe, D.P.5    Lorimer, G.H.6
  • 70
    • 0031547963 scopus 로고    scopus 로고
    • GroEL-mediated folding of structurally homologous dihydrofolate reductases
    • Clark, A.C.; Frieden, C. GroEL-mediated folding of structurally homologous dihydrofolate reductases. J. Mol. Biol. 1997, 268, 512-525.
    • (1997) J. Mol. Biol , vol.268 , pp. 512-525
    • Clark, A.C.1    Frieden, C.2
  • 73
    • 33746792363 scopus 로고    scopus 로고
    • Co-translational binding of GroEL to nascent polypeptides is followed by post-translational encapsulation by GroES to mediate protein folding
    • Ying, B.W.; Taguchi, H.; Ueda, T. Co-translational binding of GroEL to nascent polypeptides is followed by post-translational encapsulation by GroES to mediate protein folding. J. Biol. Chem. 2006, 281, 21813-21819.
    • (2006) J. Biol. Chem , vol.281 , pp. 21813-21819
    • Ying, B.W.1    Taguchi, H.2    Ueda, T.3
  • 75
    • 0024311503 scopus 로고
    • Molecular cloning of a Chinese hamster mitochondrial protein related to the "chaperonin" family of bacterial and plant proteins
    • Picketts, D.J.; Mayanil, C.S.; Gupta, R.S. Molecular cloning of a Chinese hamster mitochondrial protein related to the "chaperonin" family of bacterial and plant proteins. J. Biol. Chem. 1989, 264, 12001-12008.
    • (1989) J. Biol. Chem , vol.264 , pp. 12001-12008
    • Picketts, D.J.1    Mayanil, C.S.2    Gupta, R.S.3
  • 76
    • 0032113635 scopus 로고    scopus 로고
    • A single ring is sufficient for productive chaperonin-mediated folding In Vivo
    • Nielsen, K.L.; Cowan, N.J. A single ring is sufficient for productive chaperonin-mediated folding In Vivo. Mol. Cell 1998, 2, 93-99.
    • (1998) Mol. Cell , vol.2 , pp. 93-99
    • Nielsen, K.L.1    Cowan, N.J.2
  • 78
    • 0034671453 scopus 로고    scopus 로고
    • From minichaperone to GroEL 3: Properties of an active single-ring mutant of GroEL
    • Chatellier, J.; Hill, F.; Foster, N.W.; Goloubinoff, P.; Fersht, A.R. From minichaperone to GroEL 3: properties of an active single-ring mutant of GroEL. J. Mol. Biol. 2000, 304, 897-910.
    • (2000) J. Mol. Biol , vol.304 , pp. 897-910
    • Chatellier, J.1    Hill, F.2    Foster, N.W.3    Goloubinoff, P.4    Fersht, A.R.5
  • 79
    • 0027144068 scopus 로고
    • Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP
    • Makino, Y.; Taguchi, H.; Yoshida, M. Truncated GroEL monomer has the ability to promote folding of rhodanese without GroES and ATP. FEBS Lett. 1993, 336, 363-367.
    • (1993) FEBS Lett , vol.336 , pp. 363-367
    • Makino, Y.1    Taguchi, H.2    Yoshida, M.3
  • 80
    • 0028366080 scopus 로고
    • Monomeric chaperonin-60 and its 50-kDa fragment possess the ability to interact with non-native proteins, to suppress aggregation; to promote protein folding
    • Taguchi, H.; Makino, Y.; Yoshida, M. Monomeric chaperonin-60 and its 50-kDa fragment possess the ability to interact with non-native proteins, to suppress aggregation; to promote protein folding. J. Biol. Chem. 1994, 269, 8529-8534.
    • (1994) J. Biol. Chem , vol.269 , pp. 8529-8534
    • Taguchi, H.1    Makino, Y.2    Yoshida, M.3
  • 81
    • 0030910349 scopus 로고    scopus 로고
    • GroEL-mediated protein folding
    • Fenton, W.A.; Horwich, A.L. GroEL-mediated protein folding. Protein Sci. 1997, 6, 743-760.
    • (1997) Protein Sci , vol.6 , pp. 743-760
    • Fenton, W.A.1    Horwich, A.L.2
  • 82
    • 0026773208 scopus 로고
    • Protein folding in the cell: The role of molecular chaperones Hsp70 and Hsp60
    • Hartl, F.U.; Martin, J.; Neupert, W. Protein folding in the cell: the role of molecular chaperones Hsp70 and Hsp60. Annu. Rev. Biophys. Biomol. Struct. 1992, 21, 293-322.
    • (1992) Annu. Rev. Biophys. Biomol. Struct , vol.21 , pp. 293-322
    • Hartl, F.U.1    Martin, J.2    Neupert, W.3
  • 84
  • 85
    • 34248349952 scopus 로고    scopus 로고
    • Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL
    • Farr, G.W.; Fenton, W.A.; Horwich, A.L. Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL. Proc. Natl. Acad. Sci. USA 2007, 104, 5342-5347.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 5342-5347
    • Farr, G.W.1    Fenton, W.A.2    Horwich, A.L.3
  • 86
    • 59649106114 scopus 로고    scopus 로고
    • Cryo-EM structure of the native GroEL-GroES complex from Thermus thermophilus encapsulating substrate inside the cavity
    • Kanno, R.; Koike-Takeshita, A.; Yokoyama, K.; Taguchi, H.; Mitsuoka, K. Cryo-EM structure of the native GroEL-GroES complex from Thermus thermophilus encapsulating substrate inside the cavity. Structure 2009, 17, 287-293.
    • (2009) Structure , vol.17 , pp. 287-293
    • Kanno, R.1    Koike-Takeshita, A.2    Yokoyama, K.3    Taguchi, H.4    Mitsuoka, K.5
  • 87
    • 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.; Thirumalai, D. Chaperonin-facilitated protein folding: optimization of rate and yield by an iterative annealing mechanism. Proc. Natl. Acad. Sci. USA 1996, 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
  • 88
    • 0031436142 scopus 로고    scopus 로고
    • Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction
    • Aoki, K.; Taguchi, H.; Shindo, Y.; Yoshida, M.; Ogasahara, K.; Yutani, K.; Tanaka, N. Calorimetric observation of a GroEL-protein binding reaction with little contribution of hydrophobic interaction. J. Biol. Chem. 1997, 272, 32158-32162.
    • (1997) J. Biol. Chem , vol.272 , pp. 32158-32162
    • Aoki, K.1    Taguchi, H.2    Shindo, Y.3    Yoshida, M.4    Ogasahara, K.5    Yutani, K.6    Tanaka, N.7
  • 89
    • 0028838951 scopus 로고
    • The hydrophobic nature of GroEL-substrate binding
    • Lin, Z.; Schwartz, F.P.; Eisenstein, E. The hydrophobic nature of GroEL-substrate binding. J. Biol. Chem. 1995, 270, 1011-1014.
    • (1995) J. Biol. Chem , vol.270 , pp. 1011-1014
    • Lin, Z.1    Schwartz, F.P.2    Eisenstein, E.3
  • 90
    • 0032478538 scopus 로고    scopus 로고
    • Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL
    • Tsurupa, G.P.; Ikura, T.; Makio, T.; Kuwajima, K. Refolding kinetics of staphylococcal nuclease and its mutants in the presence of the chaperonin GroEL. J. Mol. Biol. 1998, 277, 733-745.
    • (1998) J. Mol. Biol , vol.277 , pp. 733-745
    • Tsurupa, G.P.1    Ikura, T.2    Makio, T.3    Kuwajima, K.4
  • 91
    • 0029019467 scopus 로고
    • The folding of GroEL-bound barnase as a model for chaperoninmediated protein folding
    • Corrales, F.J.; Fersht, A.R. The folding of GroEL-bound barnase as a model for chaperoninmediated protein folding. Proc. Natl. Acad. Sci. USA 1995, 92, 5326-5330.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 5326-5330
    • Corrales, F.J.1    Fersht, A.R.2
  • 92
    • 0029882517 scopus 로고    scopus 로고
    • Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL
    • Clark, A.C.; Hugo, E.; Frieden, C. Determination of regions in the dihydrofolate reductase structure that interact with the molecular chaperonin GroEL. Biochemistry 1996, 35, 5893-5901.
    • (1996) Biochemistry , vol.35 , pp. 5893-5901
    • Clark, A.C.1    Hugo, E.2    Frieden, C.3
  • 93
    • 1442306202 scopus 로고    scopus 로고
    • Functional bacteriorhodopsin is efficiently solubilized and delivered to membranes by the chaperonin GroEL
    • Deaton, J.; Sun, J.; Holzenburg, A.; Struck, D.K.; Berry, J.; Young, R. Functional bacteriorhodopsin is efficiently solubilized and delivered to membranes by the chaperonin GroEL. Proc. Natl. Acad. Sci. USA 2004, 101, 2281-2286.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2281-2286
    • Deaton, J.1    Sun, J.2    Holzenburg, A.3    Struck, D.K.4    Berry, J.5    Young, R.6
  • 94
    • 3042533402 scopus 로고    scopus 로고
    • Solubilization and delivery by GroEL of megadalton complexes of the lambda holin
    • Deaton, J.; Savva, C.G.; Sun, J.; Holzenburg, A.; Berry, J.; Young, R. Solubilization and delivery by GroEL of megadalton complexes of the lambda holin. Protein Sci. 2004, 13, 1778-1786.
    • (2004) Protein Sci , vol.13 , pp. 1778-1786
    • Deaton, J.1    Savva, C.G.2    Sun, J.3    Holzenburg, A.4    Berry, J.5    Young, R.6
  • 95
    • 0031918147 scopus 로고    scopus 로고
    • Purification of GroEL with low fluorescence background
    • Clark, A.C.; Ramanathan, R.; Frieden, C. Purification of GroEL with low fluorescence background. Methods Enzymol. 1998, 290, 100-118.
    • (1998) Methods Enzymol , vol.290 , pp. 100-118
    • Clark, A.C.1    Ramanathan, R.2    Frieden, C.3
  • 96
    • 0034490988 scopus 로고    scopus 로고
    • Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: Off-pathway aggregation propensity does not determine the cochaperonin requirement
    • Voziyan, P.A.; Fisher, M.T. Chaperonin-assisted folding of glutamine synthetase under nonpermissive conditions: off-pathway aggregation propensity does not determine the cochaperonin requirement. Protein Sci. 2000, 9, 2405-2412.
    • (2000) Protein Sci , vol.9 , pp. 2405-2412
    • Voziyan, P.A.1    Fisher, M.T.2
  • 97
    • 0028169935 scopus 로고
    • Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer
    • Azem, A.; Kessel, M.; Goloubinoff, P. Characterization of a functional GroEL14(GroES7)2 chaperonin hetero-oligomer. Science 1994, 265, 653-656.
    • (1994) Science , vol.265 , pp. 653-656
    • Azem, A.1    Kessel, M.2    Goloubinoff, P.3
  • 99
    • 0030049296 scopus 로고    scopus 로고
    • Biochemical characterization of symmetric GroELGroES complexes. Evidence for a role in protein folding
    • Llorca, O.; Carrascosa, J.L.; Valpuesta, J.M. Biochemical characterization of symmetric GroELGroES complexes. Evidence for a role in protein folding. J. Biol. Chem. 1996, 271, 68-76.
    • (1996) J. Biol. Chem , vol.271 , pp. 68-76
    • Llorca, O.1    Carrascosa, J.L.2    Valpuesta, J.M.3
  • 100
    • 0031037687 scopus 로고    scopus 로고
    • Catalysis of protein folding by symmetric chaperone complexes
    • Sparrer, H.; Rutkat, K.; Buchner, J. Catalysis of protein folding by symmetric chaperone complexes. Proc. Natl. Acad. Sci. USA 1997, 94, 1096-1100.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1096-1100
    • Sparrer, H.1    Rutkat, K.2    Buchner, J.3
  • 101
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • Todd, M.J.; Viitanen, P.V.; Lorimer, G.H. Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science 1994, 265, 659-666.
    • (1994) Science , vol.265 , pp. 659-666
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 102
    • 0030018794 scopus 로고    scopus 로고
    • Fluorescence detection of symmetric GroEL14(GroES7)2 heterooligomers involved in protein release during the chaperonin cycle
    • Torok, Z.; Vigh, L.; Goloubinoff, P. Fluorescence detection of symmetric GroEL14(GroES7)2 heterooligomers involved in protein release during the chaperonin cycle. J. Biol. Chem. 1996, 271, 16180-16186.
    • (1996) J. Biol. Chem , vol.271 , pp. 16180-16186
    • Torok, Z.1    Vigh, L.2    Goloubinoff, P.3
  • 105
    • 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.; Horwich, A.L. Distinct actions of cis and trans ATP within the double ring of the chaperonin GroEL. Nature 1997, 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
  • 106
    • 0029016593 scopus 로고
    • The origins and consequences of asymmetry in the chaperonin reaction cycle
    • Burston, S.G.; Ranson, N.A.; Clarke, A.R. The origins and consequences of asymmetry in the chaperonin reaction cycle. J. Mol. Biol. 1995, 249, 138-152.
    • (1995) J. Mol. Biol , vol.249 , pp. 138-152
    • Burston, S.G.1    Ranson, N.A.2    Clarke, A.R.3
  • 107
    • 0031557387 scopus 로고    scopus 로고
    • Binding, encapsulation and ejection: Substrate dynamics during a chaperonin-assisted folding reaction
    • Ranson, N.A.; Burston, S.G.; Clarke, A.R. Binding, encapsulation and ejection: substrate dynamics during a chaperonin-assisted folding reaction. J. Mol. Biol. 1997, 266, 656-664.
    • (1997) J. Mol. Biol , vol.266 , pp. 656-664
    • Ranson, N.A.1    Burston, S.G.2    Clarke, A.R.3
  • 109
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N.; Peitsch, M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 110
    • 0034681443 scopus 로고    scopus 로고
    • Partial occlusion of both cavities of the eukaryotic chaperonin with antibody has no effect upon the rates of beta-actin or alpha-tubulin folding
    • Grantham, J.; Llorca, O.; Valpuesta, J.M.; Willison, K.R. Partial occlusion of both cavities of the eukaryotic chaperonin with antibody has no effect upon the rates of beta-actin or alpha-tubulin folding. J. Biol. Chem. 2000, 275, 4587-4591.
    • (2000) J. Biol. Chem , vol.275 , pp. 4587-4591
    • Grantham, J.1    Llorca, O.2    Valpuesta, J.M.3    Willison, K.R.4
  • 111
    • 0033648639 scopus 로고    scopus 로고
    • Analysis of chaperone properties of small Hsp's
    • Ehrnsperger, M.; Gaestel, M.; Buchner, J. Analysis of chaperone properties of small Hsp's. Methods Mol. Biol. 2000, 99, 421-429.
    • (2000) Methods Mol. Biol , vol.99 , pp. 421-429
    • Ehrnsperger, M.1    Gaestel, M.2    Buchner, J.3
  • 112
    • 63449134763 scopus 로고    scopus 로고
    • Mechanism of Suppression of Protein Aggregation by ?-Crystallin
    • Markossian, K.A.; Yudin, I.K.; Kurganov, B.I. Mechanism of Suppression of Protein Aggregation by ?-Crystallin. Int. J. Mol. Sci. 2009, 10, 1314-1345.
    • (2009) Int. J. Mol. Sci , vol.10 , pp. 1314-1345
    • Markossian, K.A.1    Yudin, I.K.2    Kurganov, B.I.3
  • 113
    • 0027426041 scopus 로고
    • ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis
    • Palleros, D.R.; Reid, K.L.; Shi, L., Welch, W.J.; Fink, A.L. ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis. Nature 1993, 365, 664-666.
    • (1993) Nature , vol.365 , pp. 664-666
    • Palleros, D.R.1    Reid, K.L.2    Shi, L.3    Welch, W.J.4    Fink, A.L.5


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