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The accumulation of abnormal prion protein (PrP Sc ) converted from the normal cellular isoform of PrP (PrP C ) is assumed to induce pathogenesis in prion diseases. Therefore, drug discovery studies for these diseases have focused on the protein conversion process. We used a structure-based drug discovery algorithm (termed Nagasaki University Docking Engine: NUDE) that ran on an intensive supercomputer with a graphic-processing unit to identify several compounds with anti-prion effects. Amongdoi:10.1016/j.ebiom.2016.06.010 pmid:27333028 pmcid:PMC4972544 fatcat:mcj46kg4lbch7hp4kd2kdiqw74