The emerging principles of mammalian prion propagation and transmissibility barriers: Insight from studies in vitro
Article Abstract:
The key molecular event in pathogenesis of transmissible spongiform encephalopathies group of disease is self-perpetuating conformational conversion of the cellular prion protein Pr[P.sup.C] into beta-sheet-rich 'scrapie' conformer (Pr[P.sup.Sc]) and misfolded protein is the sole cause of infection. The molecular-level insight into phenomena like inherited prion diseases, prion transmission barriers, and prion strains is provided by the observations about the prion protein structural rearrangement mechanism, the role of folding intermediates in conformational conversion, and ' conformational adaptability' in the propagation of prion amyloids in vitro.
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2006
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Prions and transmissible spongiform encephalopathy (TSE) chemotherapeutics: A common mechanism for anti-TSE compounds?
Article Abstract:
The persistent uncertainties regarding the nature of mammalian prions or transmissible spongiform encephalopathies (TSEs) and their pathogenic mechanisms have made existence of anti-TSE drugs or valid treatment in human or livestock difficult. The blocking of conversion of normal prion protein [Pr[P.sub.C]sub.1] to the TSE-associated isoform, Pr[P.sup.Sc] is regarded as a common mechanism of action for the anti-TSE compounds.
Publication Name: Accounts of Chemical Research
Subject: Science and technology
ISSN: 0001-4842
Year: 2006
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