Article
Driving amyloid toxicity in a yeast model by structural changes: a molecular approach.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Jul 2009
Berthelot Karine, Immel Françoise, Géan Julie, Lecomte Sophie, Oda Reiko, Kauffmann Brice, Cullin Christophe
Abstract excerpt
The amyloid aggregation pathway is a multistep process, and many in vitro studies have highlighted the role of particular intermediates in the cellular toxicity of various amyloid diseases. In a previous study, we generated a yeast toxic mutant (M8) of the harmless model amyloid protein Het-s(218-289). In this study, we compared the aggregation characteristics of the wild-type (WT) and the toxic mutant at the...
Topics
- Amyloid
- Amyloidosis
- Mutation
- Protein Folding
- Protein Multimerization
- Protein Structure, Secondary
- Spectroscopy, Fourier Transform Infrared
- X-Ray Diffraction
- Yeasts