Hydrolysis of the Amyloid Prion Protein and Nonpathogenic Meat and Bone Meal by Anaerobic Thermophilic Prokaryotes and Streptomyces Subspecies von Tsiroulnikov, Kirill, Rezai, Human, Bonch-Osmolovskaya, Elisaveta, Nedkov, Peter, Gousterova, Adriana, Cueff, Valérie, Godfroy, Anne, Barbier, Georges, Métro, François, Chobert, Jean-Marc, Clayette, Pascal, Dormont, Dominique, Grosclaude, Jeanne, Haertlé, Thomas

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Phospholipids influence the aggregation of recombinant ovine prions: From rapid extensive aggregation to amyloidogenic conversion von Tsiroulnikov, Kirill, Shchutskaya, Yuliya, Muronetz, Vladimir, Chobert, Jean-Marc, Haertle, Thomas

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Cu(II) induces small-size aggregates with amyloid characteristics in two alleles of recombinant ovine prion proteins von Tsiroulnikov, Kirill, Rezaei, Human, Dalgalarrondo, Michèle, Chobert, Jean-Marc, Grosclaude, Jeanne, Haertlé, Thomas

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Phospholipids influence the aggregation of recombinant ovine prions von Tsiroulnikov, Kirill, Shchutskaya, Yuliya, Muronetz, Vladimir, Chobert, Jean-Marc, Haertlé, Thomas

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Copper-dependent degradation of recombinant ovine prion protein. Phosphatidylinositol stimulates aggregation and copper-driven disappearance of prion protein von Tsiroulnikov, Kirill, Chobert, Jean-Marc, Haertlé, Thomas

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Copper‐dependent degradation of recombinant ovine prion protein von Tsiroulnikov, Kirill, Chobert, Jean‐Marc, Haertlé, Thomas

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