Amyloid formation under physiological conditions proceeds via a native-like folding intermediate
Author:
Publisher
Springer Science and Business Media LLC
Subject
Molecular Biology,Structural Biology
Link
http://www.nature.com/articles/nsmb1058.pdf
Reference50 articles.
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3. Colon, W. & Kelly, J.W. Partial denaturation of transthyretin is sufficient for amyloid fibril formation in vitro. Biochemistry 31, 8654–8660 (1992).
4. Calamai, M., Chiti, F. & Dobson, C.M. Amyloid fibril formation can proceed from different conformations of a partially unfolded protein. Biophys. J. 89, 4201–4210 (2005).
5. Kelly, J.W. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8, 101–106 (1998).
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