Abstract
Many neurodegenerative diseases are associated with the formation of insoluble structures composed primarily of protein aggregates. Examples include Alzheimer disease (neurofibrillary tangles and amyloid plaques), Parkinson disease (Lewy bodies), and a class of diseases provoked by extension of the length of polyglutamine (polyQ) sequences in particular proteins. The extended polyQ sequences result from abnormal expansion of CAG repeats in the genes encoding the affected proteins, and they are thus inherited. In this issue, Popiel et al.1 tested a new therapeutic strategy to treat a Drosophila model of polyQ disease that involves feeding to the flies a fusion peptide designed to disrupt polyQ aggregates.
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