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Amyloid fibrils of human prion protein are spun and woven from morphologically disordered aggregates

Propagation and infectivity of prions in human prionopathies are likely associated with conversion of the mainly a-helical human prion protein, HuPrP, into an aggregated form with amyloid-like properties. Previous reports on efficient conversion of recombinant HuPrP have used mild to harsh denaturin...

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Bibliographische Detailangaben
Hauptverfasser: Almstedt, Karin, Nyström, Sofie, Peter, K, Nilsson, R, Hammarström, Per
Format: Artigo
Sprache:Inglês
Veröffentlicht: Landes Bioscience 2009
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Online Zugang:https://ncbi.nlm.nih.gov/pmc/articles/PMC2807696/
https://ncbi.nlm.nih.gov/pubmed/19923901
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