Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation-Reference-Cited by-同舟云学术

Kinetic analysis reveals the diversity of microscopic mechanisms through which molecular chaperones suppress amyloid formation

Published:2016-03-24 Issue:1 Volume:7 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Arosio Paolo,Michaels Thomas C. T.,Linse Sara,Månsson Cecilia,Emanuelsson Cecilia,Presto Jenny,Johansson Jan,Vendruscolo Michele,Dobson Christopher M.,Knowles Tuomas P. J.

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry

Link

http://www.nature.com/articles/ncomms10948.pdf

Reference50 articles.

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2. Knowles, T. P. J., Vendruscolo, M. & Dobson, C. M. The amyloid state and its association with protein misfolding diseases. Nat. Rev. Mol. Cell Biol. 15, 384–396 (2014).

3. Eisenberg, D. & Jucker, M. The amyloid state of proteins in human diseases. Cell 148, 1188–1203 (2012).

4. Hardy, J. & Selkoe, D. J. The amyloid hypothesis of Alzheimer’s disease: progress and problems on the road to therapeutics. Science 297, 353–356 (2002).

5. Lansbury, P. T. & Lashuel, H. A. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 443, 774–779 (2006).

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