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Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery.
Molecules 2019; 24(18)M

Abstract

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 concentrations of the amyloidogenic proteins or via heterologous inducers of prions. Studies of environmental and physiological regulation of yeast prions open new possibilities for pharmacological intervention and/or prophylactic procedures aiming on common cellular systems rather than the properties of specific amyloids.

Authors+Show Affiliations

Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA. tcherno@emory.edu.School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA 30332, USA. yury.chernoff@biology.gatech.edu. Laboratory of Amyloid Biology, St. Petersburg State University, St. Petersburg 199034, Russia. yury.chernoff@biology.gatech.edu.Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA. genekdw@emory.edu.

Pub Type(s)

Journal Article
Review

Language

eng

PubMed ID

31540362

Citation

Chernova, Tatiana A., et al. "Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery." Molecules (Basel, Switzerland), vol. 24, no. 18, 2019.
Chernova TA, Chernoff YO, Wilkinson KD. Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery. Molecules. 2019;24(18).
Chernova, T. A., Chernoff, Y. O., & Wilkinson, K. D. (2019). Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery. Molecules (Basel, Switzerland), 24(18), doi:10.3390/molecules24183388.
Chernova TA, Chernoff YO, Wilkinson KD. Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery. Molecules. 2019 Sep 18;24(18) PubMed PMID: 31540362.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Yeast Models for Amyloids and Prions: Environmental Modulation and Drug Discovery. AU - Chernova,Tatiana A, AU - Chernoff,Yury O, AU - Wilkinson,Keith D, Y1 - 2019/09/18/ PY - 2019/07/30/received PY - 2019/09/10/revised PY - 2019/09/16/accepted PY - 2019/9/22/entrez KW - amyloid KW - chaperone KW - drug discovery KW - environmental factors KW - heat shock KW - neurodegenerative disease KW - prion KW - ubiquitin JF - Molecules (Basel, Switzerland) JO - Molecules VL - 24 IS - 18 N2 - 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 concentrations of the amyloidogenic proteins or via heterologous inducers of prions. Studies of environmental and physiological regulation of yeast prions open new possibilities for pharmacological intervention and/or prophylactic procedures aiming on common cellular systems rather than the properties of specific amyloids. SN - 1420-3049 UR - https://www.unboundmedicine.com/medline/citation/31540362/Yeast_Models_for_Amyloids_and_Prions:_Environmental_Modulation_and_Drug_Discovery L2 - http://www.mdpi.com/resolver?pii=molecules24183388 DB - PRIME DP - Unbound Medicine ER -
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