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Volumn 130, Issue 2-3, 2000, Pages 130-141

The Alzheimer's peptide Aβ adopts a collapsed coil structure in water

Author keywords

Alzheimer; Amyloid; Folding; Peptide; Structure

Indexed keywords

AMYLOID BETA PROTEIN;

EID: 0033855845     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1006/jsbi.2000.4288     Document Type: Article
Times cited : (321)

References (37)
  • 2
    • 0001926444 scopus 로고
    • The Peptides: Analysis, synthesis, biology
    • Gross, E., and Meienhofer J. (Eds.), The Peptides: Analysis, Synthesis, Biology, Academic Press, New York
    • (1980) , vol.2 , pp. 1-384
    • Barany, G.1    Merrifield, R.B.2
  • 5
    • 0029854533 scopus 로고    scopus 로고
    • Point substitution in the central hydrophobic cluster of a human β-amyloid congener disrupts peptide folding and abolishes plaque competence
    • (1996) Biochemistry , vol.35 , pp. 13914-13921
    • Esler, W.P.1
  • 8
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • (1998) Fold. Des. , vol.3
    • Fink, A.L.1
  • 9
    • 0031256658 scopus 로고    scopus 로고
    • The MaxFlux algorithm for calculating variationally optimized reaction paths for conformational transitions in many body systems at finite temperature
    • (1997) J. Chem. Phys. , vol.107 , pp. 5000-5006
    • Huo, S.1    Straub, J.E.2
  • 12
    • 0027195933 scopus 로고
    • Seeding 'one-dimensional crystallization' of amyloid: A pathogenic mechanism in Alzheimer's disease and Scrapie
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarret, J.T.1    Lansbury P.T., Jr.2
  • 13
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1
  • 17
    • 0028987233 scopus 로고
    • 1H NMR of Aβ amyloid peptide congeners in water solution: Conformational changes correlate with plaque competence
    • (1995) Biochemistry , vol.34 , pp. 5191-5200
    • Lee, J.P.1
  • 18
    • 0008339014 scopus 로고    scopus 로고
    • Protein folding intermediates and Alzheimer's disease
    • Kluwer Academic, Great Britain. Y. Shimonishi (ed.), 'Peptide Science: Present and Future'
    • (1998) , pp. 326-328
    • Lee, J.P.1    Peng, J.W.2
  • 20
    • 0019201754 scopus 로고
    • Effects of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes
    • (1980) Biophys. J. , vol.30 , pp. 489
    • Lipari, G.1    Szabo, A.2
  • 23
    • 0024362326 scopus 로고
    • Three-dimensional heteronuclear NMR of nitrogen-15 labeled proteins
    • (1989) Biochemistry , vol.28 , pp. 6150-6156
    • Marion, D.1
  • 24
    • 85031599197 scopus 로고    scopus 로고
    • Simulation study of the structure and dynamics of the Alzheimer's amyloid peptide cogener in solution. Submitted for publication
    • (2000)
    • Massi, F.1    Straub, J.E.2
  • 25
    • 0027184611 scopus 로고
    • Peptide compositions of the cerebrovascular and senile plaque core amyloid deposits of Alzheimer's disease
    • (1993) Arch. Biochem. Biophys. , vol.301 , pp. 41-52
    • Miller, D.L.1
  • 28
    • 0026784152 scopus 로고
    • Mapping of the spectral densities of the N-H bond motions in eglin C using heteronuclear relaxation experiments
    • (1992) Biochemistry , vol.31 , pp. 8571-8586
    • Peng, J.W.1    Wagner, G.W.2
  • 31
    • 0026646605 scopus 로고
    • Isolation and quantification of soluble Alzheimer's β-peptide from biological fluids
    • (1992) Nature , vol.359 , pp. 325-327
    • Seubert, P.1
  • 36
    • 85031607634 scopus 로고    scopus 로고
    • Studies of Beta Amyloid Congeners Directed Toward Understanding the Molecular Mechanism Underlying the Formation of Amyloid Deposits in Alzheimer's Disease, Ph.D. dissertation, Department of Chemistry, Boston University, Boston
    • (1999)
    • Zhang, S.1
  • 37


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.