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Volumn 1764, Issue 3, 2006, Pages 443-451

Protein folding and aggregation: Two sides of the same coin in the condensation of proteins revealed by pressure studies

Author keywords

Amyloidogenic protein; Hydrostatic pressure; Neurodegenerative disease; Parkinson's disease; Prion; Protein folding

Indexed keywords

AMYLOID; CELL PROTEIN; PROTEIN;

EID: 33645985795     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.11.012     Document Type: Review
Times cited : (48)

References (80)
  • 1
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim P.S., and Baldwin R.L. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59 (1990) 631-660
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631-660
    • Kim, P.S.1    Baldwin, R.L.2
  • 2
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: a synthesis
    • Bryngelson J.D., Onuchic J.N., Socci N.D., and Wolynes P.G. Funnels, pathways, and the energy landscape of protein folding: a synthesis. Proteins 21 (1995) 167-195
    • (1995) Proteins , vol.21 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 3
    • 1842298212 scopus 로고    scopus 로고
    • From Levinthal to pathways to funnels
    • Dill K.A., and Chan H.S. From Levinthal to pathways to funnels. Nat. Struct. Biol. 4 (1997) 10-19
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 10-19
    • Dill, K.A.1    Chan, H.S.2
  • 4
    • 0036023918 scopus 로고    scopus 로고
    • Understanding protein folding with energy landscape theory: Part I. Basic concepts
    • Plotkin S.S., and Onuchic J.N. Understanding protein folding with energy landscape theory: Part I. Basic concepts. Q. Rev. Biophys. 35 (2002) 111-167
    • (2002) Q. Rev. Biophys. , vol.35 , pp. 111-167
    • Plotkin, S.S.1    Onuchic, J.N.2
  • 5
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24 (1999) 329-332
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 6
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myoglobin
    • Fändrich M., Fletcher M.A., and Dobson C.M. Amyloid fibrils from muscle myoglobin. Nature 410 (2001) 165-166
    • (2001) Nature , vol.410 , pp. 165-166
    • Fändrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 7
    • 0035496607 scopus 로고    scopus 로고
    • Rescuing the function of mutant p53
    • Bullock A.N., and Fersht A.R. Rescuing the function of mutant p53. Nat. Rev., Cancer 1 (2001) 68-76
    • (2001) Nat. Rev., Cancer , vol.1 , pp. 68-76
    • Bullock, A.N.1    Fersht, A.R.2
  • 8
    • 0035966046 scopus 로고    scopus 로고
    • DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation
    • Cordeiro Y., Machado F., Juliano L., Juliano M.A., Brentani R.R., Foguel D., and Silva J.L. DNA converts cellular prion protein into the beta-sheet conformation and inhibits prion peptide aggregation. J. Biol. Chem. 276 (2001) 49400-49409
    • (2001) J. Biol. Chem. , vol.276 , pp. 49400-49409
    • Cordeiro, Y.1    Machado, F.2    Juliano, L.3    Juliano, M.A.4    Brentani, R.R.5    Foguel, D.6    Silva, J.L.7
  • 9
    • 0036527699 scopus 로고    scopus 로고
    • Therapeutic strategies for human amyloid diseases
    • Sacchettini J.C., and Kelly J.W. Therapeutic strategies for human amyloid diseases. Nat. Rev., Drug Discov. 1 (2002) 267-275
    • (2002) Nat. Rev., Drug Discov. , vol.1 , pp. 267-275
    • Sacchettini, J.C.1    Kelly, J.W.2
  • 10
    • 0032558978 scopus 로고    scopus 로고
    • Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation
    • Lashuel H.A., Lai Z., and Kelly J.W. Characterization of the transthyretin acid denaturation pathways by analytical ultracentrifugation: implications for wild-type, V30M, and L55P amyloid fibril formation. Biochemistry 37 (1998) 17851-17864
    • (1998) Biochemistry , vol.37 , pp. 17851-17864
    • Lashuel, H.A.1    Lai, Z.2    Kelly, J.W.3
  • 12
    • 0036841958 scopus 로고    scopus 로고
    • Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions
    • Horwich A. Protein aggregation in disease: a role for folding intermediates forming specific multimeric interactions. J. Clin. Invest. 110 (2002) 1221-1232
    • (2002) J. Clin. Invest. , vol.110 , pp. 1221-1232
    • Horwich, A.1
  • 13
    • 0037551741 scopus 로고    scopus 로고
    • Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders
    • Caughey B., and Lansbury P.T. Protofibrils, pores, fibrils, and neurodegeneration: separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26 (2003) 267-298
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 267-298
    • Caughey, B.1    Lansbury, P.T.2
  • 14
    • 4444362186 scopus 로고    scopus 로고
    • New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies
    • Foguel D., and Silva J.L. New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies. Biochemistry 43 (2004) 11361-11370
    • (2004) Biochemistry , vol.43 , pp. 11361-11370
    • Foguel, D.1    Silva, J.L.2
  • 15
    • 10644225416 scopus 로고    scopus 로고
    • Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world
    • Stefani M. Protein misfolding and aggregation: new examples in medicine and biology of the dark side of the protein world. Biochim. Biophys. Acta 1739 (2004) 5-25
    • (2004) Biochim. Biophys. Acta , vol.1739 , pp. 5-25
    • Stefani, M.1
  • 16
    • 0000109395 scopus 로고
    • Thermodynamics of the association and the pressure dissociation of oligomeric proteins
    • Weber G. Thermodynamics of the association and the pressure dissociation of oligomeric proteins. J. Phys. Chem. 97 (1993) 7108-7115
    • (1993) J. Phys. Chem. , vol.97 , pp. 7108-7115
    • Weber, G.1
  • 17
    • 33645970613 scopus 로고    scopus 로고
    • Thermodynamic concepts in protein condensation
    • Weber G. Thermodynamic concepts in protein condensation. Comments Mol. Cell. Biophys. 9 (1999) 201-218
    • (1999) Comments Mol. Cell. Biophys. , vol.9 , pp. 201-218
    • Weber, G.1
  • 18
    • 0034612254 scopus 로고    scopus 로고
    • The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state
    • Ferrão-Gonzales A.D., Souto S.O., Silva J.L., and Foguel D. The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 6445-6450
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 6445-6450
    • Ferrão-Gonzales, A.D.1    Souto, S.O.2    Silva, J.L.3    Foguel, D.4
  • 19
    • 0043018095 scopus 로고    scopus 로고
    • Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease
    • Ferrão-Gonzales A.D., Palmieri L., Valory M., Silva J.L., Lashuel H., Kelly J.W., and Foguel D. Hydration and packing are crucial to amyloidogenesis as revealed by pressure studies on transthyretin variants that either protect or worsen amyloid disease. J. Mol. Biol. 328 (2003) 963-974
    • (2003) J. Mol. Biol. , vol.328 , pp. 963-974
    • Ferrão-Gonzales, A.D.1    Palmieri, L.2    Valory, M.3    Silva, J.L.4    Lashuel, H.5    Kelly, J.W.6    Foguel, D.7
  • 20
    • 0042357191 scopus 로고    scopus 로고
    • Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature
    • Marchal S., Shehi E., Harricane M.C., Fusi P., Heitz F., Tortora P., and Lange R. Structural instability and fibrillar aggregation of non-expanded human ataxin-3 revealed under high pressure and temperature. J. Biol. Chem. 278 (2003) 31554-31563
    • (2003) J. Biol. Chem. , vol.278 , pp. 31554-31563
    • Marchal, S.1    Shehi, E.2    Harricane, M.C.3    Fusi, P.4    Heitz, F.5    Tortora, P.6    Lange, R.7
  • 22
    • 1642488929 scopus 로고    scopus 로고
    • Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils
    • Niraula T.N., Konno T., Li H., Yamada H., Akasaka K., and Tachibana H. Pressure-dissociable reversible assembly of intrinsically denatured lysozyme is a precursor for amyloid fibrils. Proc. Natl. Acad. Sci. U. S. A. 23 (2004) 4089-4093
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.23 , pp. 4089-4093
    • Niraula, T.N.1    Konno, T.2    Li, H.3    Yamada, H.4    Akasaka, K.5    Tachibana, H.6
  • 24
  • 25
    • 0035478292 scopus 로고    scopus 로고
    • Pressure provides new insights into protein folding, dynamics and structure
    • Silva J.L., Foguel D., and Royer C.A. Pressure provides new insights into protein folding, dynamics and structure. Trends Biochem. Sci. 26 (2001) 612-618
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 612-618
    • Silva, J.L.1    Foguel, D.2    Royer, C.A.3
  • 26
    • 0141567910 scopus 로고    scopus 로고
    • Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy
    • Dzwolak W., Ravindra R., Lendermann J., and Winter R. Aggregation of bovine insulin probed by DSC/PPC calorimetry and FTIR spectroscopy. Biochemistry 42 (2003) 11347-11355
    • (2003) Biochemistry , vol.42 , pp. 11347-11355
    • Dzwolak, W.1    Ravindra, R.2    Lendermann, J.3    Winter, R.4
  • 27
    • 1842557395 scopus 로고    scopus 로고
    • High pressure promotes circularly shaped insulin amyloid
    • Jansen R., Grudzielanek S., Dzwolak W., and Winter R. High pressure promotes circularly shaped insulin amyloid. J. Mol. Biol. 338 (2004) 203-206
    • (2004) J. Mol. Biol. , vol.338 , pp. 203-206
    • Jansen, R.1    Grudzielanek, S.2    Dzwolak, W.3    Winter, R.4
  • 28
    • 0035912726 scopus 로고    scopus 로고
    • Partial molar volume, surface area, and hydration changes for equilibrium unfolding and formation of aggregation transition state: high-pressure and cosolute studies on recombinant human IFN-γ
    • Webb J.N., Webb S.D., Cleland J.L., Carpenter J.F., and Randolph T.W. Partial molar volume, surface area, and hydration changes for equilibrium unfolding and formation of aggregation transition state: high-pressure and cosolute studies on recombinant human IFN-γ. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 7259-7264
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 7259-7264
    • Webb, J.N.1    Webb, S.D.2    Cleland, J.L.3    Carpenter, J.F.4    Randolph, T.W.5
  • 29
    • 0033596963 scopus 로고    scopus 로고
    • Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin
    • Smeller L., Rubens P., and Heremans K. Pressure effect on the temperature-induced unfolding and tendency to aggregate of myoglobin. Biochemistry 38 (1999) 3816-3820
    • (1999) Biochemistry , vol.38 , pp. 3816-3820
    • Smeller, L.1    Rubens, P.2    Heremans, K.3
  • 30
    • 0036231272 scopus 로고    scopus 로고
    • Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin
    • Meersman F., Smeller L., and Heremans K. Comparative Fourier transform infrared spectroscopy study of cold-, pressure-, and heat-induced unfolding and aggregation of myoglobin. Biophys. J. 82 (2002) 2635-2644
    • (2002) Biophys. J. , vol.82 , pp. 2635-2644
    • Meersman, F.1    Smeller, L.2    Heremans, K.3
  • 32
    • 0037108168 scopus 로고    scopus 로고
    • Locally disordered conformer of the hamster prion protein: a crucial intermediate to PrPSc?
    • Kuwata K., Li H., Yamada H., Legname G., Prusiner S.B., Akasaka K., and James T.L. Locally disordered conformer of the hamster prion protein: a crucial intermediate to PrPSc?. Biochemistry 41 (2002) 12277-12283
    • (2002) Biochemistry , vol.41 , pp. 12277-12283
    • Kuwata, K.1    Li, H.2    Yamada, H.3    Legname, G.4    Prusiner, S.B.5    Akasaka, K.6    James, T.L.7
  • 33
    • 0346118882 scopus 로고    scopus 로고
    • Folding intermediates of the prion protein stabilized by hydrostatic pressure and low temperature
    • Martins S.M., Chapeaurouge A., and Ferreira S.T. Folding intermediates of the prion protein stabilized by hydrostatic pressure and low temperature. J. Biol. Chem. 278 (2003) 50449-50455
    • (2003) J. Biol. Chem. , vol.278 , pp. 50449-50455
    • Martins, S.M.1    Chapeaurouge, A.2    Ferreira, S.T.3
  • 35
    • 3543030409 scopus 로고    scopus 로고
    • Hydration and packing effects on prion folding and beta-sheet conversion: high-pressure spectroscopy and pressure perturbation calorimetry studies
    • Cordeiro Y., Kraineva J., Ravindra R., Lima L.M.T.R., Gomes M.P.B., Foguel D., Winter R., and Silva J.L. Hydration and packing effects on prion folding and beta-sheet conversion: high-pressure spectroscopy and pressure perturbation calorimetry studies. J. Biol. Chem. 279 (2004) 32354-32359
    • (2004) J. Biol. Chem. , vol.279 , pp. 32354-32359
    • Cordeiro, Y.1    Kraineva, J.2    Ravindra, R.3    Lima, L.M.T.R.4    Gomes, M.P.B.5    Foguel, D.6    Winter, R.7    Silva, J.L.8
  • 36
    • 0032574760 scopus 로고    scopus 로고
    • High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure
    • Gorovits B.M., and Horowitz P.M. High hydrostatic pressure can reverse aggregation of protein folding intermediates and facilitate acquisition of native structure. Biochemistry 37 (1998) 6132-6135
    • (1998) Biochemistry , vol.37 , pp. 6132-6135
    • Gorovits, B.M.1    Horowitz, P.M.2
  • 38
    • 0037420910 scopus 로고    scopus 로고
    • Pressure treatment of tailspike aggregates rapidly produces on-pathway folding intermediates
    • Lefebvre B.G., and Robinson A.S. Pressure treatment of tailspike aggregates rapidly produces on-pathway folding intermediates. Biotechnol. Bioeng. 82 (2003) 595-604
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 595-604
    • Lefebvre, B.G.1    Robinson, A.S.2
  • 39
    • 0036295569 scopus 로고    scopus 로고
    • Decreased thermodynamic stability as a crucial factor for familial amyloidotic polyneuropathy
    • Niraula T.N., Haraoka K., Ando Y., Li H., Yamada H., and Akasaka K. Decreased thermodynamic stability as a crucial factor for familial amyloidotic polyneuropathy. J. Mol. Biol. 320 (2002) 333-342
    • (2002) J. Mol. Biol. , vol.320 , pp. 333-342
    • Niraula, T.N.1    Haraoka, K.2    Ando, Y.3    Li, H.4    Yamada, H.5    Akasaka, K.6
  • 40
    • 15244356060 scopus 로고    scopus 로고
    • High hydrostatic pressure dissociates early aggregates of TTR105-115, but not the mature amyloid fibrils
    • Dirix C., Meersman F., MacPhee C.E., Dobson C.M., and Heremans K. High hydrostatic pressure dissociates early aggregates of TTR105-115, but not the mature amyloid fibrils. J. Mol. Biol. 347 (2005) 903-909
    • (2005) J. Mol. Biol. , vol.347 , pp. 903-909
    • Dirix, C.1    Meersman, F.2    MacPhee, C.E.3    Dobson, C.M.4    Heremans, K.5
  • 41
    • 0028071439 scopus 로고
    • Arc repressor will not denature under pressure in the absence of water
    • Oliveira A.C., Gaspar L.P., Da Poian A.T., and Silva J.L. Arc repressor will not denature under pressure in the absence of water. J. Mol. Biol. 240 (1994) 184-187
    • (1994) J. Mol. Biol. , vol.240 , pp. 184-187
    • Oliveira, A.C.1    Gaspar, L.P.2    Da Poian, A.T.3    Silva, J.L.4
  • 42
    • 0032539604 scopus 로고    scopus 로고
    • The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins
    • Hummer G., Garde S., Garcia A.E., Paulaitis M.E., and Pratt L.R. The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 1552-1555
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 1552-1555
    • Hummer, G.1    Garde, S.2    Garcia, A.E.3    Paulaitis, M.E.4    Pratt, L.R.5
  • 43
    • 18744415073 scopus 로고    scopus 로고
    • Simulations of the pressure and temperature unfolding of an alpha-helical peptide
    • Paschek D., Gnanakaran S., and Garcia A.E. Simulations of the pressure and temperature unfolding of an alpha-helical peptide. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 6765-6770
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6765-6770
    • Paschek, D.1    Gnanakaran, S.2    Garcia, A.E.3
  • 45
    • 0037171140 scopus 로고    scopus 로고
    • Revisiting volume changes in pressure-induced protein unfolding
    • Royer C.A. Revisiting volume changes in pressure-induced protein unfolding. Biochim. Biophys. Acta 1595 (2002) 201-209
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 201-209
    • Royer, C.A.1
  • 46
    • 0028016323 scopus 로고
    • Cold denaturation of a repressor-operator complex: the role of entropy in protein-DNA recognition
    • Foguel D., and Silva J.L. Cold denaturation of a repressor-operator complex: the role of entropy in protein-DNA recognition. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 8244-8247
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 8244-8247
    • Foguel, D.1    Silva, J.L.2
  • 47
    • 0030664959 scopus 로고    scopus 로고
    • Structure of pressure-assisted cold denatured lysozyme and comparison with lysozyme folding intermediates
    • Nash D.P., and Jonas J. Structure of pressure-assisted cold denatured lysozyme and comparison with lysozyme folding intermediates. Biochemistry 36 (1997) 14375-14383
    • (1997) Biochemistry , vol.36 , pp. 14375-14383
    • Nash, D.P.1    Jonas, J.2
  • 49
    • 0026608757 scopus 로고
    • Effects of hydrostatic pressure on a membrane-enveloped virus: high immunogenicity of the pressure-inactivated virus
    • Silva J.L., Luan P., Glaser M., Voss E.W., and Weber G. Effects of hydrostatic pressure on a membrane-enveloped virus: high immunogenicity of the pressure-inactivated virus. J. Virol. 66 (1992) 2111-2117
    • (1992) J. Virol. , vol.66 , pp. 2111-2117
    • Silva, J.L.1    Luan, P.2    Glaser, M.3    Voss, E.W.4    Weber, G.5
  • 50
    • 0027405350 scopus 로고
    • Molten-globule conformation of Arc repressor monomers determined by high-pressure 1H NMR spectroscopy
    • Peng X.D., Jonas J., and Silva J.L. Molten-globule conformation of Arc repressor monomers determined by high-pressure 1H NMR spectroscopy. Proc. Natl. Acad. Sci. U. S. A. 90 (1993) 1776-1780
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 1776-1780
    • Peng, X.D.1    Jonas, J.2    Silva, J.L.3
  • 52
    • 0034687674 scopus 로고    scopus 로고
    • DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume
    • Lima L.M.T.R., Foguel D., and Silva J.L. DNA tightens the dimeric DNA-binding domain of human papillomavirus E2 protein without changes in volume. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 14289-14294
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 14289-14294
    • Lima, L.M.T.R.1    Foguel, D.2    Silva, J.L.3
  • 53
    • 23844540599 scopus 로고    scopus 로고
    • Volume and energy folding landscape of prion protein revealed by pressure
    • Cordeiro Y., Kraineva J., Winter R., and Silva J.L. Volume and energy folding landscape of prion protein revealed by pressure. Braz. J. Med. Biol. Res. 38 (2005) 1195-1201
    • (2005) Braz. J. Med. Biol. Res. , vol.38 , pp. 1195-1201
    • Cordeiro, Y.1    Kraineva, J.2    Winter, R.3    Silva, J.L.4
  • 55
    • 0033539596 scopus 로고    scopus 로고
    • High pressure refolding of recombinant human growth hormone from insoluble aggregates
    • St John R.J., Carpenter J.F., and Randolph T.W. High pressure refolding of recombinant human growth hormone from insoluble aggregates. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 13029-13033
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 13029-13033
    • St John, R.J.1    Carpenter, J.F.2    Randolph, T.W.3
  • 56
    • 0037171154 scopus 로고    scopus 로고
    • High hydrostatic pressure as a tool to study protein aggregation and amyloidosis
    • Randolph T.W., Seefeldt M., and Carpenter J.F. High hydrostatic pressure as a tool to study protein aggregation and amyloidosis. Biochim. Biophys. Acta. 1595 (2002) 224-234
    • (2002) Biochim. Biophys. Acta. , vol.1595 , pp. 224-234
    • Randolph, T.W.1    Seefeldt, M.2    Carpenter, J.F.3
  • 57
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • Kelly J.W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8 (1998) 101-106
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 58
    • 0035827318 scopus 로고    scopus 로고
    • Protein misfolding and disease; protein refolding and therapy
    • Soto C. Protein misfolding and disease; protein refolding and therapy. FEBS Lett. 498 (2001) 204-207
    • (2001) FEBS Lett. , vol.498 , pp. 204-207
    • Soto, C.1
  • 59
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson C.M. Protein folding and misfolding. Nature 426 (2003) 884-890
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 62
    • 15944410327 scopus 로고    scopus 로고
    • High pressure studies on transthyretin
    • Foguel D. High pressure studies on transthyretin. Prot. Peptide Letters 12 (2005) 245-249
    • (2005) Prot. Peptide Letters , vol.12 , pp. 245-249
    • Foguel, D.1
  • 65
    • 0032923522 scopus 로고    scopus 로고
    • Molecular genetics of transmissible spongiform encephalopathies
    • Weissmann C. Molecular genetics of transmissible spongiform encephalopathies. J. Biol. Chem. 274 (1999) 3-6
    • (1999) J. Biol. Chem. , vol.274 , pp. 3-6
    • Weissmann, C.1
  • 66
    • 0035312586 scopus 로고    scopus 로고
    • Interactions between prion protein isoforms: the kiss of death?
    • Caughey B. Interactions between prion protein isoforms: the kiss of death?. Trends Biochem. Sci. 26 (2001) 235-242
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 235-242
    • Caughey, B.1
  • 67
    • 0022691315 scopus 로고
    • Examination of the secondary structure of proteins by deconvolved FTIR spectra
    • Byler D.M., and Susi H. Examination of the secondary structure of proteins by deconvolved FTIR spectra. Biopolymers 25 (1986) 469-487
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 68
    • 0033580649 scopus 로고    scopus 로고
    • Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering
    • Panick G., Malessa R., and Winter R. Differences between the pressure- and temperature-induced denaturation and aggregation of beta-lactoglobulin A, B, and AB monitored by FT-IR spectroscopy and small-angle X-ray scattering. Biochemistry 38 (1999) 6512-6519
    • (1999) Biochemistry , vol.38 , pp. 6512-6519
    • Panick, G.1    Malessa, R.2    Winter, R.3
  • 71
    • 0037171132 scopus 로고    scopus 로고
    • Pressure-temperature phase diagrams of biomolecules
    • Smeller L. Pressure-temperature phase diagrams of biomolecules. Biochim. Biophys. Acta 1595 (2002) 11-29
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 11-29
    • Smeller, L.1
  • 72
    • 0030874395 scopus 로고    scopus 로고
    • Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers
    • Lai Z., McCulloch J., Lashuel H.A., and Kelly J.W. Guanidine hydrochloride-induced denaturation and refolding of transthyretin exhibits a marked hysteresis: equilibria with high kinetic barriers. Biochemistry 36 (1997) 10230-10239
    • (1997) Biochemistry , vol.36 , pp. 10230-10239
    • Lai, Z.1    McCulloch, J.2    Lashuel, H.A.3    Kelly, J.W.4
  • 73
    • 0023051838 scopus 로고
    • Phenomenological description of the association of protein subunits subjected to conformational drift. Effects of dilution and of hydrostatic pressure
    • Weber G. Phenomenological description of the association of protein subunits subjected to conformational drift. Effects of dilution and of hydrostatic pressure. Biochemistry 25 (1986) 3231-3626
    • (1986) Biochemistry , vol.25 , pp. 3231-3626
    • Weber, G.1
  • 74
    • 0023055734 scopus 로고
    • Pressure dissociation and conformational drift of the beta dimer of tryptophan synthase
    • Silva J.L., Miles E.W., and Weber G. Pressure dissociation and conformational drift of the beta dimer of tryptophan synthase. Biochemistry 25 (1986) 5780-5786
    • (1986) Biochemistry , vol.25 , pp. 5780-5786
    • Silva, J.L.1    Miles, E.W.2    Weber, G.3
  • 76
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • Cohen F.E., and Kelly J.W. Therapeutic approaches to protein-misfolding diseases. Nature 426 (2003) 905-909
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 77
    • 0034614370 scopus 로고    scopus 로고
    • Productive and nonproductive intermediates in the folding of denatured rhodanese
    • Panda M., Gorovits B.M., and Horowitz P.M. Productive and nonproductive intermediates in the folding of denatured rhodanese. J. Biol. Chem. 275 (2000) 63-70
    • (2000) J. Biol. Chem. , vol.275 , pp. 63-70
    • Panda, M.1    Gorovits, B.M.2    Horowitz, P.M.3
  • 78
    • 24644500617 scopus 로고    scopus 로고
    • Main-chain dominated amyloid structures demonstrated by the effect of high pressure
    • Chatani E., Kato M., Kawai T., Naiki H., and Goto Y. Main-chain dominated amyloid structures demonstrated by the effect of high pressure. J. Mol. Biol. 352 (2005) 941-951
    • (2005) J. Mol. Biol. , vol.352 , pp. 941-951
    • Chatani, E.1    Kato, M.2    Kawai, T.3    Naiki, H.4    Goto, Y.5
  • 79
    • 0142184333 scopus 로고    scopus 로고
    • RNA molecules stimulate prion protein conversion
    • Deleault N.R., Lucassen R.W., and Supattapone S. RNA molecules stimulate prion protein conversion. Nature 425 (2003) 717-720
    • (2003) Nature , vol.425 , pp. 717-720
    • Deleault, N.R.1    Lucassen, R.W.2    Supattapone, S.3


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