Abstract
Many neurodegenerative diseases feature templated conversion of natively folded proteins into misfolded isoforms. However, such prion-like propagation of misfolding has never been observed directly in any protein, hindering efforts to decipher conversion mechanisms and develop countermeasures. We observed prion-like conversion in single molecules of superoxide dismutase-1 (SOD1), which misfolds in amyotrophic lateral sclerosis (ALS), by tethering misfolded mutants associated with familial ALS to wild-type molecules held in optical tweezers.
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