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Prion. 2011 Oct-Dec;5(4):250-7. doi: 10.4161/pri.17229. Epub 2011 Oct 1.

Modeling ALS and FTLD proteinopathies in yeast: an efficient approach for studying protein aggregation and toxicity.

Author information

1
Department of Pharmacology, Uniformed Services University of the Health Sciences, Bethesda, MD, USA. Dmitry.Kryndushkin@usuhs.mil

Abstract

In recent years there have been several reports of human neurodegenerative diseases that involve protein misfolding being modeled in the yeast Saccharomyces cerevisiae. This review summarizes recent advances in understanding the specific mechanisms underlying intracellular neuronal pathology during Amyotrophic Lateral Sclerosis (ALS) and Frontotemporal Lobar Degeneration (FTLD), including SOD1, TDP-43 and FUS protein inclusions and the potential of these proteins to be involved in pathogenic prion-like mechanisms. More specifically, we focus on findings from yeast systems that offer tremendous possibilities for screening for genetic and chemical modifiers of disease-related proteotoxicity.

PMID:
22052354
PMCID:
PMC4012400
DOI:
10.4161/pri.17229
[Indexed for MEDLINE]
Free PMC Article
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