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- W2328162512 endingPage "657" @default.
- W2328162512 startingPage "650" @default.
- W2328162512 abstract "Accumulation of misfolded proteins is a hallmark of many human diseases, including several incurable neurological disorders, such as Huntington's disease (HD). In HD, expansion of a polyglutamine stretch within the first exon of the Huntingtin protein (Htt) leads to Htt misfolding, aberrant protein aggregation, and progressive appearance of disease symptoms. Several studies in various organisms (from yeast to humans) have identified the accumulation of misfolded secretory proteins in the endoplasmic reticulum (ER stress) as a crucial determinant of cellular toxicity in HD. In this review, we highlight the recent research linking HD to ER stress. We also discuss how the modulation of signaling pathways responsible for coping with misfolded protein accumulation in the ER may constitute attractive methods to reduce toxicity and identify new therapeutic targets for treatment of HD. This article is part of a Special Issue entitled SI:ER stress." @default.
- W2328162512 created "2016-06-24" @default.
- W2328162512 creator A5008573382 @default.
- W2328162512 creator A5028612880 @default.
- W2328162512 creator A5077175091 @default.
- W2328162512 date "2016-10-01" @default.
- W2328162512 modified "2023-10-18" @default.
- W2328162512 title "Endoplasmic reticulum stress: The cause and solution to Huntington's disease?" @default.
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