Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid-Reference-Cited by-同舟云学术

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Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid

Published:2007-12 Issue:12 Volume:14 Page:1157-1164
ISSN:1545-9993
Container-title:Nature Structural & Molecular Biology
language:en
Short-container-title:Nat Struct Mol Biol

Author:

Chimon Sandra,Shaibat Medhat A,Jones Christopher R,Calero Diana C,Aizezi Buzulagu,Ishii Yoshitaka

Publisher

Springer Science and Business Media LLC

Subject

Molecular Biology,Structural Biology

Link

http://www.nature.com/articles/nsmb1345.pdf

Reference50 articles.

1. Selkoe, D.J. Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. Nat. Cell Biol. 6, 1054–1061 (2004).

2. Caughey, B. & Lansbury, P.T. Protofibrils, pores, fibrils, and neurodegeneration: Separating the responsible protein aggregates from the innocent bystanders. Annu. Rev. Neurosci. 26, 267–298 (2003).

3. Sunde, M. & Blake, C.C.F. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation. Q. Rev. Biophys. 31, 1–39 (1998).

4. Dobson, C.M. Protein folding and misfolding. Nature 426, 884–890 (2003).

5. Bucciantini, M. et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Nature 416, 507–511 (2002).

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