Molecules, Vol. 24, Pages 3388: Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery

Molecules, Vol. 24, Pages 3388: Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery Molecules doi: 10.3390/molecules24183388 Authors: Tatiana A. Chernova Yury O. Chernoff Keith D. Wilkinson Amyloids are self-perpetuating protein aggregates causing neurodegenerative diseases in mammals. Prions are transmissible protein isoforms (usually of amyloid nature). Prion features were recently reported for various proteins involved in amyloid and neural inclusion disorders. Heritable yeast prions share molecular properties (and in the case of polyglutamines, amino acid composition) with human disease-related amyloids. Fundamental protein quality control pathways, including chaperones, the ubiquitin proteasome system and autophagy are highly conserved between yeast and human cells. Crucial cellular proteins and conditions influencing amyloids and prions were uncovered in the yeast model. The treatments available for neurodegenerative amyloid-associated diseases are few and their efficiency is limited. Yeast models of amyloid-related neurodegenerative diseases have become powerful tools for high-throughput screening for chemical compounds and FDA-approved drugs that reduce aggregation and toxicity of amyloids. Although some environmental agents have been linked to certain amyloid diseases, the molecular basis of their action remains unclear. Environmental stresses trigger amyloid formation and loss, acting either via influencing intracellular con...
Source: Molecules - Category: Chemistry Authors: Tags: Review Source Type: research