<p> A high-throughput screening was used to identify protein aggregation inhibitors in vitro and in cell culture. Compounds selected in the primary screens were validated in dilution series in order to identify compounds active at very low concentrations. Clustering of the compound hits subsequently revealed a consensus structure common to active protein aggregation inhibitors. This lead structure was further modified to optimize its medicinal-chemical properties. The resulting candidates strongly reduced scrapie prion proteins in cell culture at nanomolar concentrations. They also revealed high therapeutic potential in mice infected with scrapie prions. The same compounds also inhibit formation
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New Lithium Salts of Pentafluorophenylamide Anions as Electrolytes in Lithium Ionic Batteries
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