Abstract
Polyglutamine (polyQ) diseases are inherited neurodegenerative disorders caused by proteins with expanded polyQ regions. Although the pathological mechanisms of these diseases have not yet been elucidated, the processes of protein misfolding and aggregation seem to be a direct cause of neurodegeneration. Detailed structural information on polyQ proteins is therefore essential in order to understand the mechanisms underlying pathogenesis and to design therapeutic strategies. In the past decade, several studies have investigated the structural properties of polyQ proteins and the molecular basis of aggregation and fibre formation. The results obtained in these studies are reviewed here.
Keywords: polyglutamine, aggregation, neurodegenerative diseases, structure, triplet expansion
Related Journals
Current Protein & Peptide Science
Related Books
Frontiers in Protein and Peptide Sciences
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