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Volumn 262, Issue 4, 1996, Pages 575-587

Interaction of GroEL with conformational states of horse cytochrome c

Author keywords

Cytochrome c; GroEL; Hydrophobic interaction; Molecular chaperone; Molten globule

Indexed keywords

CHAPERONE; CYTOCHROME C; HEME; PHOSPHOLIPID; PORPHYRIN DERIVATIVE;

EID: 0030569019     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0536     Document Type: Article
Times cited : (35)

References (64)
  • 1
    • 0029249945 scopus 로고
    • The nature of protein folding pathways: The classical versus the new view
    • Baldwin, R. L. (1995). The nature of protein folding pathways: the classical versus the new view. J. Biomol. NMR, 5, 103-109.
    • (1995) J. Biomol. NMR , vol.5 , pp. 103-109
    • Baldwin, R.L.1
  • 3
    • 0028885711 scopus 로고
    • Conformational variability in the refined structure of the chaperonin GroEL at 2.8 å resolution
    • Braig, K., Adams, P. D. & Brünger, A. T. (1995). Conformational variability in the refined structure of the chaperonin GroEL at 2.8 Å resolution. Nature Struct. Biol. 2, 1083-1094.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 1083-1094
    • Braig, K.1    Adams, P.D.2    Brünger, A.T.3
  • 5
    • 0025007598 scopus 로고
    • High-resolution three-dimensional structure of horse heart cytochrome c
    • Bushnell, G. W., Louie, G. V. & Brayer, G. D. (1990). High-resolution three-dimensional structure of horse heart cytochrome c. J. Mol. Biol. 214, 585-595.
    • (1990) J. Mol. Biol. , vol.214 , pp. 585-595
    • Bushnell, G.W.1    Louie, G.V.2    Brayer, G.D.3
  • 6
    • 0025324326 scopus 로고
    • Stabilization of helical structure in two 17-residue amphipathic analogues of the C-terminal peptide of cytochrome c
    • Collawn, J. F. & Paterson, Y. (1990). Stabilization of helical structure in two 17-residue amphipathic analogues of the C-terminal peptide of cytochrome c. Biopolymers, 29, 1289-1296.
    • (1990) Biopolymers , vol.29 , pp. 1289-1296
    • Collawn, J.F.1    Paterson, Y.2
  • 7
    • 0027155642 scopus 로고
    • Redesign of the interior hydrophobic region of mitochondrial cytochrome c by site-directed mutagenesis
    • Davies, A. M., Guillemette, J. G., Smith, M., Greenwood, C., Thurgood, A. G. P., Mauk, A. G. & Moore, G. R. (1993). Redesign of the interior hydrophobic region of mitochondrial cytochrome c by site-directed mutagenesis. Biochemistry, 32, 5431-5435.
    • (1993) Biochemistry , vol.32 , pp. 5431-5435
    • Davies, A.M.1    Guillemette, J.G.2    Smith, M.3    Greenwood, C.4    Thurgood, A.G.P.5    Mauk, A.G.6    Moore, G.R.7
  • 8
    • 0025092697 scopus 로고
    • The conformational changes of apocytochrome c upon binding to phospholipid vesicles and micelles of phospholipid based detergents: A circular dichroism study
    • de Jongh, H. H. J. & de Kruijff, B. (1990). The conformational changes of apocytochrome c upon binding to phospholipid vesicles and micelles of phospholipid based detergents: a circular dichroism study. Biochim. Biophys. Acta, 1029, 105-112.
    • (1990) Biochim. Biophys. Acta , vol.1029 , pp. 105-112
    • De Jongh, H.H.J.1    De Kruijff, B.2
  • 9
    • 0026603603 scopus 로고
    • A water-lipid interface induces a highly dynamic folded state in apocytochrome c and cytochrome c, which may represent a common folding intermediate
    • de Jongh, H. H. J., Killian, J. A. & de Kruijff, B. (1992). A water-lipid interface induces a highly dynamic folded state in apocytochrome c and cytochrome c, which may represent a common folding intermediate. Biochemistry, 31, 1636-1643.
    • (1992) Biochemistry , vol.31 , pp. 1636-1643
    • De Jongh, H.H.J.1    Killian, J.A.2    De Kruijff, B.3
  • 11
    • 0030347863 scopus 로고    scopus 로고
    • Revisiting the Anfinsen cage
    • Ellis, R. J. (1996). Revisiting the Anfinsen cage. Fold. Des. 1, R9-R15.
    • (1996) Fold. Des. , vol.1
    • Ellis, R.J.1
  • 13
    • 0028113299 scopus 로고
    • Residues in chaperonin GroEL required for polypeptide binding and release
    • Fenton, W. A., Kashi, Y., Furtak, K. & 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
  • 14
    • 0028034428 scopus 로고
    • The rates of commitment to denaturation of rhodanese and glutamine synthetase in the presence of the GroE chaperonins
    • Fisher, M. T. & Yuan, X. (1994). The rates of commitment to denaturation of rhodanese and glutamine synthetase in the presence of the GroE chaperonins. J. Biol. Chem. 269, 29598-29601.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29598-29601
    • Fisher, M.T.1    Yuan, X.2
  • 15
    • 0015919686 scopus 로고
    • On the role of heme in the formation of the structure of cytochrome c
    • Fisher, W. R., Taniuchi, H. & Anfinsen, C. B. (1973). On the role of heme in the formation of the structure of cytochrome c. J. Biol. Chem. 248, 3188-3195.
    • (1973) J. Biol. Chem. , vol.248 , pp. 3188-3195
    • Fisher, W.R.1    Taniuchi, H.2    Anfinsen, C.B.3
  • 16
    • 0026584271 scopus 로고
    • Protein folding in the cell
    • Gething, M. J. & Sambrook, J. (1992). Protein folding in the cell. Nature, 355, 33-45.
    • (1992) Nature , vol.355 , pp. 33-45
    • Gething, M.J.1    Sambrook, J.2
  • 17
    • 0027179284 scopus 로고
    • Refolding of barnase in the presence of GroE
    • Gray, T. E. & Fersht, A. R. (1993). Refolding of barnase in the presence of GroE. J. Mol. Biol. 232, 1197-1207.
    • (1993) J. Mol. Biol. , vol.232 , pp. 1197-1207
    • Gray, T.E.1    Fersht, A.R.2
  • 18
    • 0027433511 scopus 로고
    • Intermediate conformational states of apocytochrome c
    • Hamada, D., Hoshino, M., Kataoka, M., Fink, A. L. & Goto, Y. (1993). Intermediate conformational states of apocytochrome c. Biochemistry, 32, 10351-10358.
    • (1993) Biochemistry , vol.32 , pp. 10351-10358
    • Hamada, D.1    Hoshino, M.2    Kataoka, M.3    Fink, A.L.4    Goto, Y.5
  • 19
    • 0029863253 scopus 로고    scopus 로고
    • Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c
    • Hamada, D., Kuroda, Y., Kataoka, M., Aimoto, S., Yoshimura, T. & Goto, Y. (1996). Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c. J. Mol. Biol. 256, 172-186.
    • (1996) J. Mol. Biol. , vol.256 , pp. 172-186
    • Hamada, D.1    Kuroda, Y.2    Kataoka, M.3    Aimoto, S.4    Yoshimura, T.5    Goto, Y.6
  • 20
    • 0017337750 scopus 로고
    • Formation of a biologically active, ordered complex from two overlapping fragments of cytochrome c
    • Hantgan, R. R. & Taniuchi, H. (1977). Formation of a biologically active, ordered complex from two overlapping fragments of cytochrome c. J. Biol. Chem. 252, 1367-1374.
    • (1977) J. Biol. Chem. , vol.252 , pp. 1367-1374
    • Hantgan, R.R.1    Taniuchi, H.2
  • 21
    • 0028334547 scopus 로고
    • Conformational specificity of the chaperonin GroEL for the compact folding intermediates of α-lactalbumin
    • Hayer-Hartl, M. K., Ewbank, J. J., Creighton, T. E. & Hartl, F. U. (1994). Conformational specificity of the chaperonin GroEL for the compact folding intermediates of α-lactalbumin. EMBO J. 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
  • 22
    • 0029127242 scopus 로고
    • Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding
    • Hlodan, R., Tempst, P. & Hartl, F. U. (1995). Binding of defined regions of a polypeptide to GroEL and its implications for chaperonin-mediated protein folding. Nature Struct. Biol. 2, 587-595.
    • (1995) Nature Struct. Biol. , vol.2 , pp. 587-595
    • Hlodan, R.1    Tempst, P.2    Hartl, F.U.3
  • 23
    • 0030067634 scopus 로고    scopus 로고
    • The crystal structure of the GroES co-chaperonin at 2.8 å resolution
    • Hunt, J. F., Weaver, A. L., Landry, S. J., Gierasch, L. & 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.L.2    Landry, S.J.3    Gierasch, L.D.J.4
  • 24
    • 0028792612 scopus 로고
    • Nature and consequence of groel-protein interactions
    • Itzhaki, L. S., Otzen, D. E. & Fersht, A. R. (1995). Nature and consequence of GroEL-protein interactions. Biochemistry, 34, 14581-14587.
    • (1995) Biochemistry , vol.34 , pp. 14581-14587
    • Itzhaki, L.S.1    Otzen, D.E.2    Fersht, A.R.3
  • 25
    • 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. & 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
  • 26
    • 0023184951 scopus 로고
    • The spontaneous incorporation of proteins into preformed bilayers
    • Jain, M. K. & Zakim, D. (1987). The spontaneous incorporation of proteins into preformed bilayers. Biochim. Biophys. Acta, 906, 33-68.
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 33-68
    • Jain, M.K.1    Zakim, D.2
  • 27
    • 0024600228 scopus 로고
    • The importance of the amino terminus of the mitochondrial precursor protein apocytochrome c for translocation across model membranes
    • Jordi, W., Lin-Xin, Z., Pilon, M., Demel, R. A. & de Kruijff, B. (1989). The importance of the amino terminus of the mitochondrial precursor protein apocytochrome c for translocation across model membranes. J. Biol. Chem. 264, 2292-2301.
    • (1989) J. Biol. Chem. , vol.264 , pp. 2292-2301
    • Jordi, W.1    Lin-Xin, Z.2    Pilon, M.3    Demel, R.A.4    De Kruijff, B.5
  • 28
    • 0019320701 scopus 로고
    • A biologically active, three-fragment complex of horse heart cytochrome c
    • Juillerat, M., Parr, G. R. & Taniuchi, H. (1980). A biologically active, three-fragment complex of horse heart cytochrome c. J. Biol. Chem. 255, 845-853.
    • (1980) J. Biol. Chem. , vol.255 , pp. 845-853
    • Juillerat, M.1    Parr, G.R.2    Taniuchi, H.3
  • 29
    • 0029926871 scopus 로고    scopus 로고
    • Effect of GroEL on the refolding kinetics of α-lactalbumin
    • Katsumata, K., Okazaki, A. & Kuwajima, K. (1996). Effect of GroEL on the refolding kinetics of α-lactalbumin. J. Mol. Biol. 258, 828-838.
    • (1996) J. Mol. Biol. , vol.258 , pp. 828-838
    • Katsumata, K.1    Okazaki, A.2    Kuwajima, K.3
  • 30
    • 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. (1994). Chaperonin GroE and ADP facilitate the folding of various proteins and protect against heat inactivation. FEBS Letters, 345, 229-232.
    • (1994) FEBS Letters , vol.345 , pp. 229-232
    • Kawata, Y.1    Nosaka, K.2    Hongo, K.3    Mizobata, T.4    Nagai, J.5
  • 31
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 32
    • 0027182927 scopus 로고
    • Refolding of yeast enolase in the presence of the chaperonin GroE
    • Kubo, T., Mizobata, T. & Kawata, Y. (1993). Refolding of yeast enolase in the presence of the chaperonin GroE. J. Biol. Chem. 268, 19346-19351.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19346-19351
    • Kubo, T.1    Mizobata, T.2    Kawata, Y.3
  • 33
    • 0024417964 scopus 로고
    • The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
    • Kuwajima (1989). The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure. Proteins: Struct. Funct. Genet. 6, 87-103.
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 87-103
    • Kuwajima1
  • 34
    • 0025840379 scopus 로고
    • The chaperonin GroEL binds a polypeptide in an α-helical conformation
    • Landry, S. J. & Gierasch, L. M. (1991). The chaperonin GroEL binds a polypeptide in an α-helical conformation. Biochemistry, 30, 7359-7362.
    • (1991) Biochemistry , vol.30 , pp. 7359-7362
    • Landry, S.J.1    Gierasch, L.M.2
  • 35
    • 0028228564 scopus 로고
    • Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding
    • Landry, S. J. & Gierasch, L. M. (1994). Polypeptide interactions with molecular chaperones and their relationship to in vivo protein folding. Annu. Rev. Biophys. Biomol. Struct. 23, 645-669.
    • (1994) Annu. Rev. Biophys. Biomol. Struct. , vol.23 , pp. 645-669
    • Landry, S.J.1    Gierasch, L.M.2
  • 36
    • 0026595140 scopus 로고
    • Different conformations for the same polypeptide bound to chaperones DnaK and GroEL
    • Landry, S. J., Jordan, R., McMacken, R. & Gierasch, L. M. (1992). Different conformations for the same polypeptide bound to chaperones DnaK and GroEL. Nature, 355, 455-457.
    • (1992) Nature , vol.355 , pp. 455-457
    • Landry, S.J.1    Jordan, R.2    McMacken, R.3    Gierasch, L.M.4
  • 37
    • 0029115482 scopus 로고
    • Interaction of GroEL with a highly structured folding intermediate: Iterative binding cycles do not involve unfolding
    • Lilie, H. & Buchner, J. (1995). Interaction of GroEL with a highly structured folding intermediate: Iterative binding cycles do not involve unfolding. Proc. Natl Acad. Sci. USA, 92, 8100-8104.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8100-8104
    • Lilie, H.1    Buchner, J.2
  • 38
    • 0028838951 scopus 로고
    • The hydrophobic nature of GroEL-substrate binding
    • Lin, Z., Schwarz, F. P. & 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, Z.1    Schwarz, F.P.2    Eisenstein, E.3
  • 39
    • 0030024540 scopus 로고    scopus 로고
    • Structure of the heat shock protein chaperonin-10 of Mycobacterium leprae
    • Mande, S. C., Mehra, V., Bloom, B. R. & 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
  • 40
    • 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. & 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
  • 41
    • 0030043488 scopus 로고    scopus 로고
    • Lord of the rings: GroES structure
    • Mayhew, M. & Hartl, F. U. (1996). Lord of the rings: GroES structure. Science, 271, 161-162.
    • (1996) Science , vol.271 , pp. 161-162
    • Mayhew, M.1    Hartl, F.U.2
  • 42
    • 0026489533 scopus 로고
    • Characterization of a stable, reactivatable complex between chaperonin 60 and mitochondrial rhodanese
    • Mendoza, J. A., Butler, M. C. & 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
  • 43
    • 0028057108 scopus 로고
    • Raster3D version 2.0. A program for photorealistic molecular graphics
    • Merritt, E. A. & Murphy, M. E. P. (1994). Raster3D version 2.0. A program for photorealistic molecular graphics. Acta Crystallog. sect. D, 50, 869-873.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 869-873
    • Merritt, E.A.1    Murphy, M.E.P.2
  • 44
    • 0026640258 scopus 로고
    • Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli
    • Mizobata, T., Akiyama, Y., Ito, K., Yumoto, N. & Kawata, Y. (1992). Effects of the chaperonin GroE on the refolding of tryptophanase from Escherichia coli. J. Biol. Chem. 267, 17773-17779.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17773-17779
    • Mizobata, T.1    Akiyama, Y.2    Ito, K.3    Yumoto, N.4    Kawata, Y.5
  • 45
    • 0025877054 scopus 로고
    • Apocytochrome c interaction with phospholipid membranes studied by Fourier-transform infrared spectroscopy
    • Muga, A., Mantsch, H. H. & Surewicz, W. K. (1991). Apocytochrome c interaction with phospholipid membranes studied by Fourier-transform infrared spectroscopy. Biochemistry, 30, 2629-2635.
    • (1991) Biochemistry , vol.30 , pp. 2629-2635
    • Muga, A.1    Mantsch, H.H.2    Surewicz, W.K.3
  • 46
    • 0029090130 scopus 로고
    • Kinetic analysis of interactions between GroEL and reduced α-lactalbumin
    • Murai, N., Taguchi, H. & Yoshida, M. (1995). Kinetic analysis of interactions between GroEL and reduced α-lactalbumin. J. Biol Chem. 270, 19957-19963.
    • (1995) J. Biol Chem. , vol.270 , pp. 19957-19963
    • Murai, N.1    Taguchi, H.2    Yoshida, M.3
  • 47
    • 0028243107 scopus 로고
    • Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding
    • Nishii, I., Kataoka, M., Tokunaga, F. & Goto, Y. (1994). Cold denaturation of the molten globule states of apomyoglobin and a profile for protein folding. Biochemistry, 33, 4903-4909.
    • (1994) Biochemistry , vol.33 , pp. 4903-4909
    • Nishii, I.1    Kataoka, M.2    Tokunaga, F.3    Goto, Y.4
  • 48
    • 0028466392 scopus 로고
    • The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state
    • Okazaki, A., Ikura, T., Nikaido, K. & Kuwajima, K. (1994). The chaperonin GroEL does not recognize apo-α-lactalbumin in the molten globule state. Nature Struct. Biol. 1, 439-446.
    • (1994) Nature Struct. Biol. , vol.1 , pp. 439-446
    • Okazaki, A.1    Ikura, T.2    Nikaido, K.3    Kuwajima, K.4
  • 50
    • 0017814312 scopus 로고
    • Formation of two alternative complementing structures from a cytochrome c heme fragment (residues 1 to 38) and the apoprotein
    • Parr, G. R., Hantgan, R. R. & Taniuchi, H. (1978). Formation of two alternative complementing structures from a cytochrome c heme fragment (residues 1 to 38) and the apoprotein. J. Biol Chem. 253, 5381-5388.
    • (1978) J. Biol Chem. , vol.253 , pp. 5381-5388
    • Parr, G.R.1    Hantgan, R.R.2    Taniuchi, H.3
  • 51
    • 0011902301 scopus 로고
    • On the preparation and mössbauer properties of some heme peptides of cytochrome c
    • Peterson, J., Saleem, M. M. M., Silver, J. & Wilson, M. T. (1983). On the preparation and mössbauer properties of some heme peptides of cytochrome c. J. Inorg. Biochem. 19, 165-178.
    • (1983) J. Inorg. Biochem. , vol.19 , pp. 165-178
    • Peterson, J.1    Saleem, M.M.M.2    Silver, J.3    Wilson, M.T.4
  • 52
    • 0002940127 scopus 로고
    • The molten globule state
    • (Creighton, T. E., ed.), W. H. Freeman and Co., New York
    • Ptitsyn, O. B. (1992). The molten globule state. In Protein Folding (Creighton, T. E., ed.), pp. 243-300, W. H. Freeman and Co., New York.
    • (1992) Protein Folding , pp. 243-300
    • Ptitsyn, O.B.1
  • 53
    • 0029087065 scopus 로고
    • Chaperonins can catalyse the reversal of early aggregation steps when a protein misfolds
    • Ranson, N. A., Dunster, N. J., Burston, S. G. & Clarke, A. R. (1995). Chaperonins can catalyse 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
  • 55
    • 0026801563 scopus 로고
    • Interaction of GroE with an all-β-protein
    • Schmidt, M. & Buchner, J. (1992). Interaction of GroE with an all-β-protein. J. Biol. Chem. 267, 16829-16833.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16829-16833
    • Schmidt, M.1    Buchner, J.2
  • 56
    • 0029157314 scopus 로고
    • Interaction between the GroE chaperonins and rhodanese
    • Smith, K. E. & Fisher, M. T. (1995). Interaction between the GroE chaperonins and rhodanese. J. Biol. Chem. 270, 21517-21523.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21517-21523
    • Smith, K.E.1    Fisher, M.T.2
  • 57
    • 0025910862 scopus 로고
    • Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements
    • Spooner, P. J. R. & Watts, A. (1991a). Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 1. Evidence from deuterium NMR measurements. Biochemistry, 30, 3871-3879.
    • (1991) Biochemistry , vol.30 , pp. 3871-3879
    • Spooner, P.J.R.1    Watts, A.2
  • 58
    • 0025761403 scopus 로고
    • Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements
    • Spooner, P. J. R. & Watts, A. (1991b). Reversible unfolding of cytochrome c upon interaction with cardiolipin bilayers. 2. Evidence from phosphorus-31 NMR measurements. Biochemistry, 30, 3880-3885.
    • (1991) Biochemistry , vol.30 , pp. 3880-3885
    • Spooner, P.J.R.1    Watts, A.2
  • 59
    • 0028855745 scopus 로고
    • Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin
    • Taguchi, H. & Yoshida, M. (1995). Chaperonin releases the substrate protein in a form with tendency to aggregate and ability to rebind to chaperonin. FEBS Letters, 359, 195-198.
    • (1995) FEBS Letters , vol.359 , pp. 195-198
    • Taguchi, H.1    Yoshida, M.2
  • 60
    • 0028031345 scopus 로고
    • Dynamics of the chaperonin ATPase cycle: Implications for facilitated protein folding
    • Todd, M. J., Viitanen, P. V. & Lorimer, G. H. (1994). Dynamics of the chaperonin ATPase cycle: implications for facilitated protein folding. Science, 265, 659-665.
    • (1994) Science , vol.265 , pp. 659-665
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 61
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of normative forms
    • Weissman, J. S., Kashi, Y., Fenton, W. A. & Horwich, A. L. (1994). GroEL-mediated protein folding proceeds by multiple rounds of binding and release of normative 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
  • 64
    • 0028260023 scopus 로고
    • Destabilization of the complete protein secondary structure on binding to the chaperone GroEL
    • Zahn, R., Spitzfaden, C., Otti ger, M., Wüthrich, K. & 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    Otti Ger, M.3    Wüthrich, K.4    Plückthun, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.