Article
Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model.
The Journal of biological chemistry - 17 Jun 2005
Gokhale Kavita C, Newnam Gary P, Sherman Michael Y, Chernoff Yury O
Abstract excerpt
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 propagation of yeast prions, were also reported to influence polyglutamine aggregation in yeast, but it was not clear...
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