메뉴 건너뛰기




Volumn 4, Issue 5, 1997, Pages 345-355

Kinetics and mechanism of amyloid formation by the prion protein H1 peptide as determined by time-dependent ESR

Author keywords

Aggregation; Amyloid; Electron spin resonance; Kinetics; Prion protein

Indexed keywords


EID: 0031149603     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(97)90125-3     Document Type: Article
Times cited : (53)

References (38)
  • 3
    • 0027001034 scopus 로고
    • Chemistry and biology of prions
    • Prusiner, S.B. (1992). Chemistry and biology of prions. Biochemistry 31, 12277-12288.
    • (1992) Biochemistry , vol.31 , pp. 12277-12288
    • Prusiner, S.B.1
  • 4
    • 0025910229 scopus 로고
    • Molecular biology of prion diseases
    • Prusiner, S.B. (1991). Molecular biology of prion diseases. Science 252, 1515-1522.
    • (1991) Science , vol.252 , pp. 1515-1522
    • Prusiner, S.B.1
  • 5
    • 0025244011 scopus 로고
    • Transgenetic studies implicate interactions between homologous prp isoforms in scrapie prion replication
    • Prusiner, S.B., et al., & Dearmond, S.J. (1990). Transgenetic studies implicate interactions between homologous prp isoforms in scrapie prion replication. Cell 63, 673-686.
    • (1990) Cell , vol.63 , pp. 673-686
    • Prusiner, S.B.1    Dearmond, S.J.2
  • 6
    • 12644272790 scopus 로고    scopus 로고
    • Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity
    • Telling, G.C., et al., & Prusiner, S.B. (1996). Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274, 2079-2082.
    • (1996) Science , vol.274 , pp. 2079-2082
    • Telling, G.C.1    Prusiner, S.B.2
  • 7
    • 0025944507 scopus 로고
    • Secondary structure analysis of the scrapie-associated protein prp 27-30 in water by infrared spectroscopy
    • Caughey, B.W., Dong, A., Bhat, K.S., Ernst, D., Hayes, S.F. & Caughey, W.S. (1991). Secondary structure analysis of the scrapie-associated protein prp 27-30 in water by infrared spectroscopy. Biochemistry 30, 7672-7680.
    • (1991) Biochemistry , vol.30 , pp. 7672-7680
    • Caughey, B.W.1    Dong, A.2    Bhat, K.S.3    Ernst, D.4    Hayes, S.F.5    Caughey, W.S.6
  • 8
    • 0027332116 scopus 로고
    • Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins
    • Pan, K.M., et al., & Prusiner, S.B. (1993). Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc. Natl Acad. Sci. USA 90, 10962-10966.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10962-10966
    • Pan, K.M.1    Prusiner, S.B.2
  • 9
    • 0027182522 scopus 로고
    • Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein
    • Safar, J., Roller, P.P., Gajdusek, D.C. & Gibbs, C.J., Jr. (1993). Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J. Biol. Chem. 268, 20276-20284.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20276-20284
    • Safar, J.1    Roller, P.P.2    Gajdusek, D.C.3    Gibbs Jr., C.J.4
  • 10
    • 0029116625 scopus 로고
    • Conformational transitions in peptides containing two putative alpha-helices of the prion protein
    • Zhang, H, et al., & Prusiner, S.B. (1995). Conformational transitions in peptides containing two putative alpha-helices of the prion protein. J. Mol. Biol. 250, 514-526.
    • (1995) J. Mol. Biol. , vol.250 , pp. 514-526
    • Zhang, H.1    Prusiner, S.B.2
  • 11
    • 0030035952 scopus 로고    scopus 로고
    • Solid-state nmr studies of the prion protein h1 fragment
    • Heller, J., et al., & Wemmer, D.E. (1996). Solid-state nmr studies of the prion protein h1 fragment. Protein Sci. 5, 1655-1661.
    • (1996) Protein Sci. , vol.5 , pp. 1655-1661
    • Heller, J.1    Wemmer, D.E.2
  • 14
    • 0026442278 scopus 로고
    • Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid
    • Gasset, M., et al., & Prusiner, S.B. (1992). Predicted alpha-helical regions of the prion protein when synthesized as peptides form amyloid. Proc. Natl Acad. Sci. USA 89, 10940-10944.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 10940-10944
    • Gasset, M.1    Prusiner, S.B.2
  • 16
    • 0024473899 scopus 로고
    • Pro → Leu change at position-102 of prion protein is the most common but not the sole mutation related to Gerstmannstraussler syndrome
    • Dohura, K., Tateishi, J., Sasaki, H., Kitamoto, T. & Sakaki, Y. (1989). Pro → Leu change at position-102 of prion protein is the most common but not the sole mutation related to Gerstmannstraussler syndrome. Biochem. Biophys. Res. Commun. 163, 974-979.
    • (1989) Biochem. Biophys. Res. Commun. , vol.163 , pp. 974-979
    • Dohura, K.1    Tateishi, J.2    Sasaki, H.3    Kitamoto, T.4    Sakaki, Y.5
  • 17
    • 0030342679 scopus 로고    scopus 로고
    • Scrapie prions: A three-dimensional model of an infectious fragment
    • Huang, Z, Prusiner, S.B. & Cohen, F.E. (1996). Scrapie prions: a three-dimensional model of an infectious fragment. Fold. Des. 1, 13-19.
    • (1996) Fold. Des. , vol.1 , pp. 13-19
    • Huang, Z.1    Prusiner, S.B.2    Cohen, F.E.3
  • 18
    • 0015408029 scopus 로고
    • The relation of the properties of congo red-stained amyloid fibrils to the β conformation
    • Glenner, G.G., Eanes, E.D. & Page, D.L. (1972). The relation of the properties of congo red-stained amyloid fibrils to the β conformation. J. Histochem. Cytochem. 20, 821-826.
    • (1972) J. Histochem. Cytochem. , vol.20 , pp. 821-826
    • Glenner, G.G.1    Eanes, E.D.2    Page, D.L.3
  • 19
    • 0021019026 scopus 로고
    • Scrapie prions aggregate to form amyloid-like birfringent rods
    • Prusiner, S.B., et al., & Glenner, G.G. (1983). Scrapie prions aggregate to form amyloid-like birfringent rods. Cell 35, 349-358.
    • (1983) Cell , vol.35 , pp. 349-358
    • Prusiner, S.B.1    Glenner, G.G.2
  • 21
    • 0026045862 scopus 로고
    • Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation
    • Wisniewski, T., Ghiso, J. & Frangione, B. (1991). Peptides homologous to the amyloid protein of Alzheimer's disease containing a glutamine for glutamic acid substitution have accelerated amyloid fibril formation. Biochem. Biophys. Res. Commun. 179, 1247-1254.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 1247-1254
    • Wisniewski, T.1    Ghiso, J.2    Frangione, B.3
  • 22
    • 0027270578 scopus 로고
    • A kinetic model for amyloid formation in the prion diseases - Importance of seeding
    • Come, J.H., Fraser, P.E. & Lansbury, P.T. (1993). A kinetic model for amyloid formation in the prion diseases - importance of seeding. Proc. Natl Acad. Sci. USA 90, 5959-5963.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5959-5963
    • Come, J.H.1    Fraser, P.E.2    Lansbury, P.T.3
  • 23
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid beta-protein fibrils - Detection of nuclei and quantitation of rate constants
    • Lomakin, A., Chung, D.S., Benedek, G.B., Kirschner, D.A. & Teplow, D.B. (1996). On the nucleation and growth of amyloid beta-protein fibrils - detection of nuclei and quantitation of rate constants. Proc. Natl Acad. Sci. USA 93, 1125-1129.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 24
    • 0025776471 scopus 로고
    • ESR spectra reflect local and global mobility in a short spin-labeled peptide throughout the α-helix→coil transition
    • Todd, A.P. & Millhauser, G.L. (1991). ESR spectra reflect local and global mobility in a short spin-labeled peptide throughout the α-helix→coil transition. Biochemistry 30, 5515-5523.
    • (1991) Biochemistry , vol.30 , pp. 5515-5523
    • Todd, A.P.1    Millhauser, G.L.2
  • 28
    • 0026055737 scopus 로고
    • Position dependent local motions in spin-labeled analogues of a short α helical peptide determined by electron spin resonance
    • Muck, S.M., Todd, A.P. & Millhauser, G.L. (1991). Position dependent local motions in spin-labeled analogues of a short α helical peptide determined by electron spin resonance. Biochemistry 30, 9498-9503.
    • (1991) Biochemistry , vol.30 , pp. 9498-9503
    • Muck, S.M.1    Todd, A.P.2    Millhauser, G.L.3
  • 33
    • 0022335486 scopus 로고
    • Nucleation and growth of protein crystals: General principles and assays
    • Feher, G. & Kam, Z. (1985). Nucleation and growth of protein crystals: general principles and assays. Methods Enzymol. 114, 77-112.
    • (1985) Methods Enzymol. , vol.114 , pp. 77-112
    • Feher, G.1    Kam, Z.2
  • 34
    • 0027195933 scopus 로고
    • Seeding one dimensional crystallization of amyloid - A pathogenic mechanism in Alzheimer's disease and scrapie
    • Jarrett, J.T. & Lansbury, P.T. (1993). Seeding one dimensional crystallization of amyloid - a pathogenic mechanism in Alzheimer's disease and scrapie. Cell 73, 1055-1058.
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, P.T.2
  • 35
    • 0026062496 scopus 로고
    • Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis
    • Mckinley, M.P., et al., & Prusiner, S.B. (1991). Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virology 65, 1340-1351.
    • (1991) J. Virology , vol.65 , pp. 1340-1351
    • Mckinley, M.P.1    Prusiner, S.B.2
  • 36
  • 38
    • 0029583794 scopus 로고
    • Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state
    • Caughey, B., Kocisko, D.A., Raymond, G.J. & Lansbury, P.T. (1995). Aggregates of scrapie-associated prion protein induce the cell-free conversion of protease-sensitive prion protein to the protease-resistant state. Chem. Biol. 2, 807-817.
    • (1995) Chem. Biol. , vol.2 , pp. 807-817
    • Caughey, B.1    Kocisko, D.A.2    Raymond, G.J.3    Lansbury, P.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.