Université de Fribourg

Protein folding activity of ribosomal rna is a selective target of two unrelated antiprion drugs

Tribouillard-Tanvier, Déborah ; Reis, Suzana Dos ; Gug, Fabienne ; Voisset, Cécile ; Béringue, Vincent ; Sabate, Raimon ; Kikovska, Ema ; Talarek, Nicolas ; Bach, Stéphane ; Huang, Chenhui ; Desban, Nathalie ; Saupe, Sven J. ; Supattapone, Surachai ; Thuret, Jean-Yves ; Chédin, Stéphane ; Vilette, Didier ; Galons, Hervé ; Sanyal, Suparna ; Blondel, Marc

In: PLoS ONE, 2008, vol. 3, no. 5, p. e2174

Background: 6-Aminophenanthridine (6AP) and Guanabenz (GA, a drug currently in use for the treatment of hypertension) were isolated as antiprion drugs using a yeast-based assay. These structurally unrelated molecules are also active against mammalian prion in several cell-based assays and in vivo in a mouse model for prion-based diseases.Methodology/Principal Findings: Here we report the...