Article
An aggregate-prone conformational epitope in trinucleotide repeat diseases.
Neuroreport - 19 Dec 2003
Sugaya Keizo, Matsubara Shiro, Miyamoto Kazuhito, Kawata Akihiro, Hayashi Hideaki
Abstract excerpt
A broad range of neurodegenerative disorders is associated with accumulation of misfolded protein that is toxic to the cells. Knowledge of the conformational structure of the protein implicated is essential for understanding how an aggregate-prone protein causes disease. Here we show that a conformational epitope associated with aggregation property and cell toxicity is preserved in homopolymeric amino acid...
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