Modulation of Prion-dependent Polyglutamine Aggregation and Toxicity by Chaperone Proteins in the Yeast Model

In yeast, aggregation and toxicity of the expanded polyglutamine fragment of human huntingtin strictly depend on the presence of the endogenous self-perpetuating aggregated proteins (prions), which contain glutamine/asparagine-rich domains. Some chaperones of the Hsp100/70/40 complex, modulating pro...

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Veröffentlicht in:	The Journal of biological chemistry 2005-06, Vol.280 (24), p.22809-22818
Hauptverfasser:	Gokhale, Kavita C, Newnam, Gary P, Sherman, Michael Y, Chernoff, Yury O
Format:	Artikel
Sprache:	eng
Schlagworte:	Alleles Centrifugation Endocytosis Green Fluorescent Proteins - chemistry Heat-Shock Proteins - chemistry HSP40 Heat-Shock Proteins HSP70 Heat-Shock Proteins - chemistry Microscopy, Fluorescence Microscopy, Phase-Contrast Molecular Chaperones - chemistry Mutation Peptides - chemistry Plasmids - metabolism Polyribonucleotides Prions - chemistry Protein Structure, Tertiary Saccharomyces cerevisiae - metabolism Time Factors
Online-Zugang:	Volltext
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