메뉴 건너뛰기




Volumn 1, Issue 1, 1996, Pages

Revisiting the Anfinsen cage

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONIN; DIHYDROFOLATE REDUCTASE;

EID: 0030347863     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(96)00004-1     Document Type: Article
Times cited : (46)

References (45)
  • 1
    • 0023900525 scopus 로고
    • Homologous plant and bacterial proteins chaperone oligomeric protein assembly
    • Hemmingsen, S.M., et al., & Ellis, RJ. (1988). Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 333, 330-334.
    • (1988) Nature , vol.333 , pp. 330-334
    • Hemmingsen, S.M.1    Ellis, R.J.2
  • 2
    • 0029062216 scopus 로고
    • The chaperonin containing t-complex polypeptide 1 (TCP-1)
    • Kubota, H., Hynes, G. & Willison, K. (1995). The chaperonin containing t-complex polypeptide 1 (TCP-1). Eur. J. Biochem. 230, 3-16.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 3-16
    • Kubota, H.1    Hynes, G.2    Willison, K.3
  • 3
    • 0030042460 scopus 로고    scopus 로고
    • Protein folding in the cell; competing models of chaperonin function
    • Ellis, RJ. & Hartl, F.-U. (1996). Protein folding in the cell; competing models of chaperonin function. FASEB J. 10, 20-26.
    • (1996) FASEB J. , vol.10 , pp. 20-26
    • Ellis, R.J.1    Hartl, F.-U.2
  • 4
    • 0029566336 scopus 로고
    • The role of molecular chaperones in protein folding
    • Hendrick, J.P. & Hartl, F.-U. (1995). The role of molecular chaperones in protein folding. FASEB J. 9, 1559-1569.
    • (1995) FASEB J. , vol.9 , pp. 1559-1569
    • Hendrick, J.P.1    Hartl, F.-U.2
  • 5
    • 0004167360 scopus 로고    scopus 로고
    • Ellis, R.J., ed. Academic Press, San Diego, in press
    • Ellis, R.J., ed. (1996). The Chaperonins. Academic Press, San Diego, in press.
    • (1996) The Chaperonins
  • 6
    • 0015859467 scopus 로고
    • Principles that govern the folding of protein chains
    • Anfinsen, C.B. (1973). Principles that govern the folding of protein chains. Science 181, 223-230.
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 7
    • 0024314918 scopus 로고
    • Molecular chaperones: Proteins essential for the biogenesis of some macromolecular structures
    • Ellis, RJ. & Hemmingsen, S.M. (1989). Molecular chaperones: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem. Sci. 14, 339-342.
    • (1989) Trends Biochem. Sci. , vol.14 , pp. 339-342
    • Ellis, R.J.1    Hemmingsen, S.M.2
  • 9
    • 0027184721 scopus 로고
    • Molecular chaperons functions of heat-shock proteins
    • Hendrick, J.P. & Hartl, F.-U. (1993). Molecular chaperons functions of heat-shock proteins. Annu. Rev. Biochem. 62, 349-384.
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 349-384
    • Hendrick, J.P.1    Hartl, F.-U.2
  • 10
    • 0642360467 scopus 로고
    • Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and ATP
    • Goloubinoff, P., Christeller, J.P., Gatenby, A.A. & Lorimer, G.G. (1989). Reconstitution of active dimeric ribulose bisphosphate carboxylase from an unfolded state depends on two chaperonin proteins and ATP. Nature 371, 578-586.
    • (1989) Nature , vol.371 , pp. 578-586
    • Goloubinoff, P.1    Christeller, J.P.2    Gatenby, A.A.3    Lorimer, G.G.4
  • 11
    • 0024972083 scopus 로고
    • Mitochondrial heat shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
    • Cheng, M.Y., et al., & Horwich, A.R. (1989). Mitochondrial heat shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria Nature 337, 620-625.
    • (1989) Nature , vol.337 , pp. 620-625
    • Cheng, M.Y.1    Horwich, A.R.2
  • 12
    • 0024458504 scopus 로고
    • Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis
    • Ostermann, J., Horwich, A.L., Neupert, W., & Hartl, F.-U. (1989). Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 341, 125-130.
    • (1989) Nature , vol.341 , pp. 125-130
    • Ostermann, J.1    Horwich, A.L.2    Neupert, W.3    Hartl, F.-U.4
  • 13
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
    • Martin, J., et al., & 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    Hartl, F.-U.2
  • 14
    • 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. (1988). Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein. Nature 336, 254-257.
    • (1988) Nature , vol.336 , pp. 254-257
    • Bochkareva, E.S.1    Lissin, N.M.2    Girshovich, A.S.3
  • 15
    • 0028465426 scopus 로고
    • Opening and closing the Anfinsen cage
    • Ellis, R.J. (1994). Opening and closing the Anfinsen cage. Curr. Biol. 4, 633-635.
    • (1994) Curr. Biol. , vol.4 , pp. 633-635
    • Ellis, R.J.1
  • 16
    • 0028822679 scopus 로고
    • Quasi-native chaperonin-bound intermediates in facilitated protein folding
    • Tian, G., Vainberg, I.E., Tap, W.D., Lewis, S.A. & Cowan, N.J. (1995). Quasi-native chaperonin-bound intermediates in facilitated protein folding. J. Biol. Chem. 270, 23910-23914.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23910-23914
    • Tian, G.1    Vainberg, I.E.2    Tap, W.D.3    Lewis, S.A.4    Cowan, N.J.5
  • 17
    • 0018791204 scopus 로고
    • Purification and properties of GroE, a host protein involved in bacteriophage assembly
    • Hendrix, R.W. (1979). Purification and properties of GroE, a host protein involved in bacteriophage assembly. J. Mol. Biol. 129, 375-392.
    • (1979) J. Mol. Biol. , vol.129 , pp. 375-392
    • Hendrix, R.W.1
  • 18
    • 0018791259 scopus 로고
    • Isolation and characterisation of the host protein GroE involved in bacteriophage lambda assembly
    • Hohn, T., Hohn, B., Engel, A., Wurtz, M., & Smith, P.R. (1979). Isolation and characterisation of the host protein GroE involved in bacteriophage lambda assembly. J. Mol. Biol. 129, 359-373.
    • (1979) J. Mol. Biol. , vol.129 , pp. 359-373
    • Hohn, T.1    Hohn, B.2    Engel, A.3    Wurtz, M.4    Smith, P.R.5
  • 20
    • 0019333950 scopus 로고
    • Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact chloroplasts
    • Barraclough, R., & Ellis, R.J. (1980). Protein synthesis in chloroplasts IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact chloroplasts. Biochim. Biophys. Acta 608, 19-31.
    • (1980) Biochim. Biophys. Acta , vol.608 , pp. 19-31
    • Barraclough, R.1    Ellis, R.J.2
  • 22
    • 0024396544 scopus 로고
    • Identification and electron microscopic analysis of a chaperonin oligomer from Neurospora crassa
    • Hutchinson, E.G., Tichelaar, W., Hofhaus, G., Weiss, H. & Leonard, K.R. (1989). Identification and electron microscopic analysis of a chaperonin oligomer from Neurospora crassa. EMBO J. 8, 1485-1490.
    • (1989) EMBO J. , vol.8 , pp. 1485-1490
    • Hutchinson, E.G.1    Tichelaar, W.2    Hofhaus, G.3    Weiss, H.4    Leonard, K.R.5
  • 23
    • 0023673510 scopus 로고
    • A highly evolutionary conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene
    • McMullin, T.W. & Hallberg, R.L. (1988). A highly evolutionary conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene. Mol. Cell Biol. 8, 371-380.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 371-380
    • McMullin, T.W.1    Hallberg, R.L.2
  • 24
    • 0022981315 scopus 로고
    • Purification and properties of the groES morphogenetic protein of Escherichia coli
    • Chandrasekhar, G.N., Tilly, K., Woolford, C., Hendrix, R., Georgopoulos, G.G. (1986). Purification and properties of the groES morphogenetic protein of Escherichia coli. J. Biol. Chem. 261, 12414-12419.
    • (1986) J. Biol. Chem. , vol.261 , pp. 12414-12419
    • Chandrasekhar, G.N.1    Tilly, K.2    Woolford, C.3    Hendrix, R.4    Georgopoulos, G.G.5
  • 26
    • 0025291463 scopus 로고
    • The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor
    • Laminet, A.A., Ziegelhoffer, T., Georgopoulos, G.C. & Pluckthun, A. (1990). The Escherichia coli heat shock proteins GroEL and GroES modulate the folding of the β-lactamase precursor, EMBO J. 9, 2315-2319.
    • (1990) EMBO J. , vol.9 , pp. 2315-2319
    • Laminet, A.A.1    Ziegelhoffer, T.2    Georgopoulos, G.C.3    Pluckthun, A.4
  • 27
    • 0025727072 scopus 로고
    • GroE facilitates the refolding of citrate synthase by suppressing aggregation
    • Buchner, J., et al., & Kiefhaber, T. (1991). GroE facilitates the refolding of citrate synthase by suppressing aggregation. Biochemistry 30, 1586-1591.
    • (1991) Biochemistry , vol.30 , pp. 1586-1591
    • Buchner, J.1    Kiefhaber, T.2
  • 28
    • 0025995773 scopus 로고
    • Cooperativity in ATP hydrolysis by GroEL is increased by GroES
    • Gray, T.E. & 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
  • 29
    • 0026416056 scopus 로고
    • Unfolding protein folding
    • Creighton, T.E. (1991). Unfolding protein folding. Nature 352, 17-18.
    • (1991) Nature , vol.352 , pp. 17-18
    • Creighton, T.E.1
  • 30
    • 0027318513 scopus 로고
    • Macromolecular crowding: Biophysical and physiological consequences
    • Zimmerman, S.B. & Minton, AP. (1993). Macromolecular crowding: biophysical and physiological consequences. Annu. Rev. Biophys. Biomol. Struct. 22, 27-65.
    • (1993) Annu. Rev. Biophys. Biomol. Struct. , vol.22 , pp. 27-65
    • Zimmerman, S.B.1    Minton, A.P.2
  • 31
    • 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
  • 32
    • 0028792612 scopus 로고
    • Nature and consequences of GroEL-protein interactions
    • Itzhaki, L.S., Otzen, D.E. & Fersht, A.R. (1995). Nature and consequences 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
  • 33
    • 13244295644 scopus 로고
    • ATP induces large quaternary rearrangements in a cage-like chaperonin structure
    • Saibil, H.R., et al., & Ellis, RJ. (1993). ATP induces large quaternary rearrangements in a cage-like chaperonin structure. Curr. Biol. 3, 265-273.
    • (1993) Curr. Biol. , vol.3 , pp. 265-273
    • Saibil, H.R.1    Ellis, R.J.2
  • 34
    • 0028027055 scopus 로고
    • Location of a folding protein and shape changes in GroEL-GroES complexes imaged by cryo-electron microscopy
    • Chen, S., et al., & 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    Saibil, H.R.2
  • 35
    • 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
  • 36
    • 0027943510 scopus 로고
    • The crystal structure of the bacterial chaperonin GroEL at 2.8Å
    • Braig, K., et al., & Sigler, P.B. (1994). The crystal structure of the bacterial chaperonin GroEL at 2.8Å. Nature 371, 578-586.
    • (1994) Nature , vol.371 , pp. 578-586
    • Braig, K.1    Sigler, P.B.2
  • 37
    • 0027214204 scopus 로고
    • Folding in vivo of bacterial cytoplasmic proteins: Role of GroEL
    • Horwich, A.L., Low, K.B., Fenton, F.A., Hirshfield, I.N. & Furtak, K. (1993). Folding in vivo of bacterial cytoplasmic proteins: role of GroEL Cell 74, 909-917.
    • (1993) Cell , vol.74 , pp. 909-917
    • Horwich, A.L.1    Low, K.B.2    Fenton, F.A.3    Hirshfield, I.N.4    Furtak, K.5
  • 38
    • 0027427326 scopus 로고
    • The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding
    • Martin, J., Mayhew, M., Langer, T., & Hartl F.-U. (1993). The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature 366, 228-233.
    • (1993) Nature , vol.366 , pp. 228-233
    • Martin, J.1    Mayhew, M.2    Langer, T.3    Hartl, F.-U.4
  • 39
    • 0028003639 scopus 로고
    • ATP induces non-identity of two rings in GroEL J
    • Bochkareva, E.S. & Girshovich, A.S. (1994). ATP induces non-identity of two rings in GroEL J. Biol. Chem. 269, 23869-23871.
    • (1994) Biol. Chem. , vol.269 , pp. 23869-23871
    • Bochkareva, E.S.1    Girshovich, A.S.2
  • 40
    • 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, 659-666.
    • (1994) Science , vol.265 , pp. 659-666
    • Todd, M.J.1    Viitanen, P.V.2    Lorimer, G.H.3
  • 41
    • 0027933369 scopus 로고
    • GroEL-mediated protein folding proceeds by multiple rounds of binding and release of nonnative forms
    • Weismann, J.S., Kashi, Y., Fenton, W.A. & Norwich, 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
    • Weismann, J.S.1    Kashi, Y.2    Fenton, W.A.3    Norwich, A.L.4
  • 42
    • 0029016593 scopus 로고
    • The origins and consequences of asymmetry in the chaperonin reaction cycle
    • Burston, S.G., Ranson, N.A. & 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
  • 43
    • 0028258634 scopus 로고
    • Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES
    • Peralta, D., Hartman, D.J., Hoogenraad, N.J. & Hoj, P.B. (1994). Generation of a stable folding intermediate which can be rescued by the chaperonins GroEL and GroES. FEBS Lett. 339, 45-49.
    • (1994) FEBS Lett. , vol.339 , pp. 45-49
    • Peralta, D.1    Hartman, D.J.2    Hoogenraad, N.J.3    Hoj, P.B.4
  • 44
    • 0026751786 scopus 로고
    • The folding of hen lysozyme involves partially structured intermediates
    • Radford, S.E., Dobson, C.M. & Evans, P.A. (1992). The folding of hen lysozyme involves partially structured intermediates. Nature 358, 302-307.
    • (1992) Nature , vol.358 , pp. 302-307
    • Radford, S.E.1    Dobson, C.M.2    Evans, P.A.3
  • 45
    • 0025303147 scopus 로고
    • Interaction of hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckman, R.P., Mizzen, L. & Welch, W.J. (1990). Interaction of hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science 248, 850-856.
    • (1990) Science , vol.248 , pp. 850-856
    • Beckman, R.P.1    Mizzen, L.2    Welch, W.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.