Reversible unfolding of infectious prion assemblies reveals the existence of an oligomeric elementary brick.
Mammalian prions, the pathogens that cause transmissible spongiform encephalopathies, propagate by self-perpetuating the structural information stored in the abnormally folded, aggregated conformer (PrPSc) of the host-encoded prion protein (PrPC).To date, no structural model related to prion assembly organization satisfactorily describes how strain