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- W2791226658 abstract "Transmissible spongiform encephalopathies (TSEs) are a group of fatal and rare neurodegenerative diseases that affect mammals, including humans. The infectious agent in TSEs is a proteinaceous entity, termed prion, which is devoid of nucleic acids and capable of replication, infectivity, and toxicity. The main component of the prion agent is the prion protein PrPSc, which results from the autocatalytic misfolding of the host-encoded cellular form of the prion protein PrPC. The molecular factors that determine PrPC to PrPSc conversion are not well understood. The secondary structure of the globular-shaped C-terminal of PrPC is well conserved across mammal species in spite of the presence of gene polymorphisms. Our structural bioinformatics study examines the effect of the polymorphisms on the dynamic network of prion protein residue interactions and on prion protein - model cell membrane interactions for a number of mammal species. We will discuss the outcomes of our study in relation to the initial steps of PrPC to PrPSc conversion." @default.
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- W2791226658 date "2018-02-01" @default.
- W2791226658 modified "2023-09-27" @default.
- W2791226658 title "Effect of Gene Polymorphisms on the Structural Dynamics of Prion Proteins: A Comparative Study" @default.
- W2791226658 doi "https://doi.org/10.1016/j.bpj.2017.11.2296" @default.
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