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Volumn , Issue , 2006, Pages 3-13

Protein folding, misfolding, stability, and aggregation: An overview

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Indexed keywords


EID: 84919835307     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-0-387-36063-8_1     Document Type: Editorial
Times cited : (5)

References (12)
  • 1
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • C. A. Ross and M. A. Poirier, Protein aggregation and neurodegenerative disease, Nature Med. 10, S10-S17 (2004).
    • (2004) Nature Med. , vol.10 , pp. S10-S17
    • Ross, C.A.1    Poirier, M.A.2
  • 2
    • 0036407227 scopus 로고    scopus 로고
    • Peptide aggregation in neurodegenerative disease
    • R. M. Murphy, Peptide aggregation in neurodegenerative disease, Annu. Rev. Biomed. Eng. 4, 155-174 (2002).
    • (2002) Annu. Rev. Biomed. Eng. , vol.4 , pp. 155-174
    • Murphy, R.M.1
  • 5
    • 0004176971 scopus 로고
    • New York: Harper and Row
    • J. D. Rawn, Biochemistry (New York: Harper and Row, 1983).
    • (1983) Biochemistry
    • Rawn, J.D.1
  • 7
    • 0032993447 scopus 로고    scopus 로고
    • Polymer principles and protein folding
    • K. A. Dill, Polymer principles and protein folding, Protein Sci. 8, 1166-1180 (1999).
    • (1999) Protein Sci. , vol.8 , pp. 1166-1180
    • Dill, K.A.1
  • 8
    • 0028801832 scopus 로고
    • Role of hydrophobic and hydrophilic forces in peptide-protein interaction: New advances
    • T. Cserhati and M. Szogyi, Role of hydrophobic and hydrophilic forces in peptide-protein interaction: new advances, Peptides 16, 165-173 (1995).
    • (1995) Peptides , vol.16 , pp. 165-173
    • Cserhati, T.1    Szogyi, M.2
  • 9
    • 0030727624 scopus 로고    scopus 로고
    • The Hofmeister series: Salt and solvent effects on interfacial phenomena
    • M. G. Cacace, E. M. Landau, and J. J Ramsden, The Hofmeister series: salt and solvent effects on interfacial phenomena, Q. Rev. Biophys. 30, 241-277 (1997).
    • (1997) Q. Rev. Biophys. , vol.30 , pp. 241-277
    • Cacace, M.G.1    Landau, E.M.2    Ramsden, J.J.3
  • 10
    • 0026299965 scopus 로고
    • Protein stability and protein folding
    • R. Jaenicki, Protein stability and protein folding, Ciba Foundation Symposium 161, 206-221 (1991).
    • (1991) Ciba Foundation Symposium , vol.161 , pp. 206-221
    • Jaenicki, R.1
  • 11
    • 4444362186 scopus 로고    scopus 로고
    • New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies
    • D. Foguel and J. L. Silva, New insights into the mechanisms of protein misfolding and aggregation in amyloidogenic diseases derived from pressure studies, Biochemistry 43, 11361-11370 (2004).
    • (2004) Biochemistry , vol.43 , pp. 11361-11370
    • Foguel, D.1    Silva, J.L.2
  • 12
    • 0035957228 scopus 로고    scopus 로고
    • Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates
    • R. Khurana, J. R. Gillespie, A. Talaptra, L. J. Minert, C. Ionescu-Zanetti, I. Millett, and A. L. Fink, Partially folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates, Biochemistry 40, 3525-3535 (2001).
    • (2001) Biochemistry , vol.40 , pp. 3525-3535
    • Khurana, R.1    Gillespie, J.R.2    Talaptra, A.3    Minert, L.J.4    Ionescu-Zanetti, C.5    Millett, I.6    Fink, A.L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.