
pmid: 15491795
Prions are self-perpetuating protein isoforms that are responsible for infectious diseases in mammals and for heritable traits in fungi. Most known prion proteins form amyloids--self-seeded fiber-like aggregates. Prion propagation ('replication') could be described as a sequence of repetitive cycles of aggregate 'shearing' into smaller seeds followed by the growth of these seeds into full-size polymers. Recent work shows that the ability to form aggregates and to propagate them is controlled by distinct regions of the composite prion domains (PrDs).
Models, Molecular, Binding Sites, Models, Genetic, Prions, Protein Conformation, Molecular Conformation, Models, Biological, Prion Diseases, Protein Structure, Tertiary, Evolution, Molecular, Structure-Activity Relationship, Models, Chemical, Multiprotein Complexes, Animals, Humans, Dimerization, Protein Binding
Models, Molecular, Binding Sites, Models, Genetic, Prions, Protein Conformation, Molecular Conformation, Models, Biological, Prion Diseases, Protein Structure, Tertiary, Evolution, Molecular, Structure-Activity Relationship, Models, Chemical, Multiprotein Complexes, Animals, Humans, Dimerization, Protein Binding
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