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Volumn 12, Issue 4, 2003, Pages 672-680

Denaturation and reassembly of chaperonin GroEL studied by solution X-ray scattering

Author keywords

Denaturation; GroEL; Molecular chaperone; Protein folding; Reassembly; X ray scattering

Indexed keywords

ADENOSINE DERIVATIVE; AMMONIUM SULFATE; BACTERIAL PROTEIN; CHAPERONIN; MONOMER; UREA;

EID: 0037377494     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0233603     Document Type: Article
Times cited : (19)

References (63)
  • 2
    • 0029249356 scopus 로고
    • Large-aperture TV detector with a beryllium-windowed image intensifier for X-ray diffraction
    • Amemiya, Y., Ito, K., Yagi, N., Asano, Y., Wakabayashi, K., Ueki, T., and Endo, T. 1995. Large-aperture TV detector with a beryllium-windowed image intensifier for X-ray diffraction. Rev. Sci. Instrum. 66: 2290-2294.
    • (1995) Rev. Sci. Instrum. , vol.66 , pp. 2290-2294
    • Amemiya, Y.1    Ito, K.2    Yagi, N.3    Asano, Y.4    Wakabayashi, K.5    Ueki, T.6    Endo, T.7
  • 3
    • 0034581327 scopus 로고    scopus 로고
    • Role of the molten globule state in protein folding
    • Arai, M. and Kuwajima, K. 2000. Role of the molten globule state in protein folding. Adv. Protein Chem. 53: 209-282.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 209-282
    • Arai, M.1    Kuwajima, K.2
  • 4
    • 0032498226 scopus 로고    scopus 로고
    • Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy
    • Arai, M., Ikura, T., Semisotnov, G.V., Kihara, H., Amemiya, Y., and Kuwajima, K. 1998. Kinetic refolding of β-lactoglobulin. Studies by synchrotron X-ray scattering, and circular dichroism, absorption and fluorescence spectroscopy. J. Mol. Biol. 275: 149-162.
    • (1998) J. Mol. Biol. , vol.275 , pp. 149-162
    • Arai, M.1    Ikura, T.2    Semisotnov, G.V.3    Kihara, H.4    Amemiya, Y.5    Kuwajima, K.6
  • 6
    • 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. Nat. Struct. Biol. 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
  • 7
    • 0031563834 scopus 로고    scopus 로고
    • The structural stability of the cochaperonin GroES
    • Boudker, O., Todd, M.J., and Freire, E. 1997. The structural stability of the cochaperonin GroES. J. Mol. Biol. 272: 770-779.
    • (1997) J. Mol. Biol. , vol.272 , pp. 770-779
    • Boudker, O.1    Todd, M.J.2    Freire, E.3
  • 9
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B. and Horwich, A.L. 1998. The Hsp70 and Hsp60 chaperone machines. Cell 92: 351-366.
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 10
    • 0025258481 scopus 로고
    • The mitochondrial chaperonin hsp60 is required for its own assembly
    • Cheng, M.Y., Hartl, F.U., and Horwich, A.L. 1990. The mitochondrial chaperonin hsp60 is required for its own assembly. Nature 348: 455-458.
    • (1990) Nature , vol.348 , pp. 455-458
    • Cheng, M.Y.1    Hartl, F.U.2    Horwich, A.L.3
  • 12
    • 0035354585 scopus 로고    scopus 로고
    • Changes in biomolecular conformation seen by small angle X-ray scattering
    • Doniach, S. 2001. Changes in biomolecular conformation seen by small angle X-ray scattering. Chem. Rev. 101: 1763-1778.
    • (2001) Chem. Rev. , vol.101 , pp. 1763-1778
    • Doniach, S.1
  • 13
    • 0032531727 scopus 로고    scopus 로고
    • Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but nonidentical requirement for hsp60 and hsp10
    • Dubaquié, Y., Looser, R., Fünfschilling, U., Jenö, P., and Rospert, S. 1998. Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but nonidentical requirement for hsp60 and hsp10. EMBO J. 17: 5868-5876.
    • (1998) EMBO J. , vol.17 , pp. 5868-5876
    • Dubaquié, Y.1    Looser, R.2    Fünfschilling, U.3    Jenö, P.4    Rospert, S.5
  • 15
    • 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
  • 16
    • 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
  • 17
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman, J. 2001. Folding of newly translated proteins in vivo: The role of molecular chaperones. Annu. Rev. Biochem. 70: 603-647.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 603-647
    • Frydman, J.1
  • 18
    • 0035847097 scopus 로고    scopus 로고
    • Excluded volume effects on the refolding and assembly of an oligomeric protein, GroEL, a case study
    • Galan, A., Sot, B., Llorca, O., Carrascosa, J.L., Valpuesta, J.M., and Muga, A. 2001. Excluded volume effects on the refolding and assembly of an oligomeric protein. GroEL, a case study. J. Biol. Chem. 276: 957-964.
    • (2001) J. Biol. Chem. , vol.276 , pp. 957-964
    • Galan, A.1    Sot, B.2    Llorca, O.3    Carrascosa, J.L.4    Valpuesta, J.M.5    Muga, A.6
  • 20
    • 0028841921 scopus 로고
    • Residual structure in urea-denatured chaperonin GroEL
    • Gorovits, B.M., Seale, J.W., and Horowitz, P.M. 1995. Residual structure in urea-denatured chaperonin GroEL. Biochemistry 34: 13928-13933.
    • (1995) Biochemistry , vol.34 , pp. 13928-13933
    • Gorovits, B.M.1    Seale, J.W.2    Horowitz, P.M.3
  • 21
    • 0034489321 scopus 로고    scopus 로고
    • Reversible denaturation of oligomeric human chaperonin 10: Denatured state depends on chemical denaturant
    • Guidry, J.J., Moczygemba, C.K., Steede, N.K., Landry, S.J., and Wittung-Stafshede, P. 2000. Reversible denaturation of oligomeric human chaperonin 10: Denatured state depends on chemical denaturant. Protein Sci. 9: 2109-2117.
    • (2000) Protein Sci. , vol.9 , pp. 2109-2117
    • Guidry, J.J.1    Moczygemba, C.K.2    Steede, N.K.3    Landry, S.J.4    Wittung-Stafshede, P.5
  • 22
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: From nascent chain to folded protein
    • Hartl, F.U. and Hayer-Hartl, M. 2002. Molecular chaperones in the cytosol: From nascent chain to folded protein. Science 295: 1852-1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 23
    • 0033588259 scopus 로고    scopus 로고
    • Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model
    • Higurashi, T., Nosaka, K., Mizobata, T., Nagai, J., and Kawata, Y. 1999. Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model. J. Mol. Biol. 291: 703-713.
    • (1999) J. Mol. Biol. , vol.291 , pp. 703-713
    • Higurashi, T.1    Nosaka, K.2    Mizobata, T.3    Nagai, J.4    Kawata, Y.5
  • 24
    • 0033547324 scopus 로고    scopus 로고
    • Identification of in vivo substrates of the chaperonin GroEL
    • Houry, W.A., Frishman, D., Eckerskom, C., Lottspeich, F., and Hartl, F.U. 1999. Identification of in vivo substrates of the chaperonin GroEL. Nature 402: 147-154.
    • (1999) Nature , vol.402 , pp. 147-154
    • Houry, W.A.1    Frishman, D.2    Eckerskom, C.3    Lottspeich, F.4    Hartl, F.U.5
  • 26
    • 0035830681 scopus 로고    scopus 로고
    • Nucleotide binding to the chaperonin GroEL: Noncooperative binding of ATP analogs and ADP, and cooperative effect of ATP
    • Inobe, T., Makio, T., Takasu-Ishikawa, E., Terada, T.P., and Kuwajima, K. 2001. Nucleotide binding to the chaperonin GroEL: Noncooperative binding of ATP analogs and ADP, and cooperative effect of ATP. Biochim. Biophys. Acta 1545: 160-173.
    • (2001) Biochim. Biophys. Acta , vol.1545 , pp. 160-173
    • Inobe, T.1    Makio, T.2    Takasu-Ishikawa, E.3    Terada, T.P.4    Kuwajima, K.5
  • 27
    • 0037436402 scopus 로고    scopus 로고
    • Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy
    • in press
    • Inobe, T., Arai, M., Nakao, M., Ito, K., Kamagata, K., Makio, T., Amemiya, Y., Kihara, H., and Kuwajima, K. 2003. Equilibrium and kinetics of the allosteric transition of GroEL studied by solution X-ray scattering and fluorescence spectroscopy. J. Mol. Biol. (in press).
    • (2003) J. Mol. Biol.
    • Inobe, T.1    Arai, M.2    Nakao, M.3    Ito, K.4    Kamagata, K.5    Makio, T.6    Amemiya, Y.7    Kihara, H.8    Kuwajima, K.9
  • 28
    • 0025812217 scopus 로고
    • In vivo analysis of integration of membrane proteins in Escherichia coli
    • Ito, K. and Akiyama, Y. 1991. In vivo analysis of integration of membrane proteins in Escherichia coli. Mol. Microbiol. 5: 2243-2253.
    • (1991) Mol. Microbiol. , vol.5 , pp. 2243-2253
    • Ito, K.1    Akiyama, Y.2
  • 29
    • 0002740483 scopus 로고    scopus 로고
    • Oligomeric proteins
    • eds. A.L. Fink and Y. Goto. Marcel Dekker, Inc., New York
    • Jaenicke, R. 1998. Oligomeric proteins. In Molecular chaperones in the life cycle of proteins (eds. A.L. Fink and Y. Goto), pp. 35-70. Marcel Dekker, Inc., New York.
    • (1998) Molecular Chaperones in the Life Cycle of Proteins , pp. 35-70
    • Jaenicke, R.1
  • 30
    • 0034581324 scopus 로고    scopus 로고
    • Folding and association of oligomeric and multimeric proteins
    • Jaenicke, R. and Lilie, H. 2000. Folding and association of oligomeric and multimeric proteins. Adv. Protein Chem. 53: 329-401.
    • (2000) Adv. Protein Chem. , vol.53 , pp. 329-401
    • Jaenicke, R.1    Lilie, H.2
  • 31
    • 0030324821 scopus 로고    scopus 로고
    • X-ray solution scattering studies of protein folding
    • Kataoka, M. and Goto, Y. 1996. X-ray solution scattering studies of protein folding. Fold. Des. 1: 107-114.
    • (1996) Fold. Des. , vol.1 , pp. 107-114
    • Kataoka, M.1    Goto, Y.2
  • 32
    • 0027400842 scopus 로고
    • Molten globule of cytochrome c studied by small angle X-ray scattering
    • Kataoka, M., Hagihara, Y., Mihara, K., and Goto, Y. 1993. Molten globule of cytochrome c studied by small angle X-ray scattering. J. Mol. Biol. 229: 591-596.
    • (1993) J. Mol. Biol. , vol.229 , pp. 591-596
    • Kataoka, M.1    Hagihara, Y.2    Mihara, K.3    Goto, Y.4
  • 33
    • 0029032691 scopus 로고
    • Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
    • Kataoka, M., Nishii, I., Fujisawa, T., Ueki, T., Tokunaga, F., and Goto, Y. 1995. Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J. Mol. Biol. 249: 215-228.
    • (1995) J. Mol. Biol. , vol.249 , pp. 215-228
    • Kataoka, M.1    Nishii, I.2    Fujisawa, T.3    Ueki, T.4    Tokunaga, F.5    Goto, Y.6
  • 34
    • 0030582682 scopus 로고    scopus 로고
    • Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL
    • Katsumata, K., Okazaki, A., Tsurupa, G.P., and Kuwajima, K. 1996. Dominant forces in the recognition of a transient folding intermediate of α-lactalbumin by GroEL. J. Mol. Biol. 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
  • 35
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. 1996. MOLMOL: A program for display and analysis of macromolecular structures. J. Mol. Graphics 14: 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 36
    • 0034773339 scopus 로고    scopus 로고
    • Assembly of chaperonin complexes
    • Kusmierczyk, A.R. and Martin, J. 2001. Assembly of chaperonin complexes. Mol. Biotechnol. 19: 141-152.
    • (2001) Mol. Biotechnol. , vol.19 , pp. 141-152
    • Kusmierczyk, A.R.1    Martin, J.2
  • 37
    • 0001579510 scopus 로고    scopus 로고
    • The molten globule state: The physical picture and biological significance
    • ed. R.H. Pain. Oxford University Press, New York
    • Kuwajima, K. and Arai, M. 2000. The molten globule state: The physical picture and biological significance. In Mechanisms of protein folding, 2nd ed. (ed. R.H. Pain), pp. 138-174. Oxford University Press, New York.
    • (2000) Mechanisms of Protein Folding, 2nd Ed. , pp. 138-174
    • Kuwajima, K.1    Arai, M.2
  • 39
    • 0028933373 scopus 로고
    • In vitro dissociation of self-assembly of three chaperonin 60s: The role of ATP
    • Lissin, N.M. 1995. In vitro dissociation of self-assembly of three chaperonin 60s: The role of ATP. FEBS Lett. 361: 55-60.
    • (1995) FEBS Lett. , vol.361 , pp. 55-60
    • Lissin, N.M.1
  • 40
    • 0027243528 scopus 로고
    • Stabilization of a compact conformation of monomeric GroEL at low temperature by adenine nucleotides
    • Lissin, N.M. and Hemmingsen, S.M. 1993. Stabilization of a compact conformation of monomeric GroEL at low temperature by adenine nucleotides. FEBS Lett. 324: 41-44.
    • (1993) FEBS Lett. , vol.324 , pp. 41-44
    • Lissin, N.M.1    Hemmingsen, S.M.2
  • 41
    • 0025205189 scopus 로고
    • (Mg-ATP)-dependent self-assembly of molecular chaperone GroEL
    • Lissin, N.M., Venyaminov, S. Yu., and Girshovich, A.S. 1990. (Mg-ATP)-dependent self-assembly of molecular chaperone GroEL. Nature 348: 339-342.
    • (1990) Nature , vol.348 , pp. 339-342
    • Lissin, N.M.1    Venyaminov, Yu.S.2    Girshovich, A.S.3
  • 42
    • 0033569635 scopus 로고    scopus 로고
    • Chaperonin-affected refolding of α-lactalbumin: Effects of nucleotides and the cochaperonin GroES
    • Makio, T., Arai, M., and Kuwajima, K. 1999. Chaperonin-affected refolding of α-lactalbumin: Effects of nucleotides and the cochaperonin GroES. J. Mol. Biol. 293: 125-137.
    • (1999) J. Mol. Biol. , vol.293 , pp. 125-137
    • Makio, T.1    Arai, M.2    Kuwajima, K.3
  • 44
    • 0028933073 scopus 로고
    • Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent
    • Mendoza, J.A., Martinez, J.L., and Horowitz, P.M. 1995. Tetradecameric chaperonin 60 can be assembled in vitro from monomers in a process that is ATP independent. Biochim. Biophys. Acta 1247: 209-214.
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 209-214
    • Mendoza, J.A.1    Martinez, J.L.2    Horowitz, P.M.3
  • 45
    • 0022555885 scopus 로고
    • Determination and analysis of urea and guanidine hydrochloride denaturation curves
    • Pace, C.N. 1986. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131: 266-280.
    • (1986) Methods Enzymol. , vol.131 , pp. 266-280
    • Pace, C.N.1
  • 46
    • 0002101049 scopus 로고
    • Assembly of multi-subunit structures
    • ed. R.H. Pain. Oxford University Press, New York
    • Price, N.C. 1994. Assembly of multi-subunit structures. In Mechanisms of protein folding (ed. R.H. Pain), pp. 160-193. Oxford University Press, New York.
    • (1994) Mechanisms of Protein Folding , pp. 160-193
    • Price, N.C.1
  • 48
    • 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
  • 49
    • 0033617129 scopus 로고    scopus 로고
    • GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings
    • Rye, H.S., Roseman, A.M., Chen, S., Furtak. K., Fenton, W.A., Saibil, H.R., and Horwich, A.L. 1999. GroEL-GroES cycling: ATP and nonnative polypeptide direct alternation of folding-active rings. Cell 97: 325-338.
    • (1999) Cell , vol.97 , pp. 325-338
    • Rye, H.S.1    Roseman, A.M.2    Chen, S.3    Furtak, K.4    Fenton, W.A.5    Saibil, H.R.6    Horwich, A.L.7
  • 51
    • 0029974605 scopus 로고    scopus 로고
    • Reversible oligomerization and denaturation of the chaperonin GroES
    • Seale, J.W., Gorovits, B.M., Ybarra, J., and Horowitz, P.M. 1996. Reversible oligomerization and denaturation of the chaperonin GroES. Biochemistry 35: 4079-4083.
    • (1996) Biochemistry , vol.35 , pp. 4079-4083
    • Seale, J.W.1    Gorovits, B.M.2    Ybarra, J.3    Horowitz, P.M.4
  • 52
    • 0012551674 scopus 로고    scopus 로고
    • Assembly of multi-subunit structures
    • ed. R.H. Pain. Oxford University Press, New York
    • Seckler, R. 2000. Assembly of multi-subunit structures. In Mechanisms of protein folding, 2nd ed. (ed. R.H. Pain), pp. 279-308. Oxford University Press, New York.
    • (2000) Mechanisms of Protein Folding, 2nd Ed. , pp. 279-308
    • Seckler, R.1
  • 54
    • 0035815699 scopus 로고    scopus 로고
    • Synchronized domain-opening motion of GroEL is essential for communication between the two rings
    • Shiseki, K., Murai, N., Motojima, F., Hisabori, T., Yoshida. M., and Taguchi, H. 2001. Synchronized domain-opening motion of GroEL is essential for communication between the two rings. J. Biol. Chem. 276: 11335-11338.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11335-11338
    • Shiseki, K.1    Murai, N.2    Motojima, F.3    Hisabori, T.4    Yoshida, M.5    Taguchi, H.6
  • 56
  • 57
    • 0014364651 scopus 로고
    • Protein denaturation
    • Tanford, C. 1968. Protein denaturation. Adv. Protein Chem. 23: 121-282.
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121-282
    • Tanford, C.1
  • 58
    • 0032932922 scopus 로고    scopus 로고
    • Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for noncooperative nucleotide binding
    • Terada, T.P. and Kuwajima. K. 1999. Thermodynamics of nucleotide binding to the chaperonin GroEL studied by isothermal titration calorimetry: Evidence for noncooperative nucleotide binding. Biochim. Biophys. Acta 1431: 269-281.
    • (1999) Biochim. Biophys. Acta , vol.1431 , pp. 269-281
    • Terada, T.P.1    Kuwajima, K.2
  • 59
    • 0029643911 scopus 로고    scopus 로고
    • Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering
    • Thiyagarajan, P., Henderson, S.J., and Joachimiak, A. 1996. Solution structures of GroEL and its complex with rhodanese from small-angle neutron scattering. Structure 4: 79-88.
    • (1996) Structure , vol.4 , pp. 79-88
    • Thiyagarajan, P.1    Henderson, S.J.2    Joachimiak, A.3
  • 61
    • 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
  • 62
    • 0012545994 scopus 로고    scopus 로고
    • The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex
    • Xu, Z., Horwich, A.L., and Sigler. P.B. 1997. The crystal structure of the asymmetric GroEL-GroES-(ADP)7 chaperonin complex. Nature 3887: 41-50.
    • (1997) Nature , vol.3887 , pp. 41-50
    • Xu, Z.1    Horwich, A.L.2    Sigler, P.B.3
  • 63
    • 0029142612 scopus 로고
    • Refolding and reassembly of active chaperonin GroEL after denaturation
    • Ybarra, J. and Horowitz, P.M. 1995. Refolding and reassembly of active chaperonin GroEL after denaturation. J. Biol. Chem. 270: 22113-22115.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22113-22115
    • Ybarra, J.1    Horowitz, P.M.2


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