The crucial event in the development of transmissible spongiform encephalopathies (TSEs) is the conformational change of a host-encoded membrane protein - the cellular PrP(C) - into a disease associated, fibril-forming isoform PrP(Sc).
First-pass extracted concept
PrP(C)
Candidate: concept label1 source documents4 linked claims
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Aliases
cellular prion protein, cellular PrP(C)
Evidence Snippets
Supporting Sources
Linked Claims
The review states that the exact molecular mechanisms leading to prion protein conformational change remain unknown.
Quoted textsource-backed
The exact molecular mechanisms which lead to the conformational change are still unknown.
The review states that the key event in transmissible spongiform encephalopathy development is conformational conversion of PrP(C) into fibril-forming PrP(Sc).
Quoted textsource-backed
The crucial event in the development of transmissible spongiform encephalopathies (TSEs) is the conformational change of a host-encoded membrane protein - the cellular PrP(C) - into a disease associated, fibril-forming isoform PrP(Sc).
The review focuses on structural aspects of prion protein, protein-protein interactions, and protein regions that may contribute to initiation of PrP misfolding.
Quoted textsource-backed
This review focuses on structural aspects of the prion protein with regard to protein-protein interactions and the initiation of prion protein misfolding. It therefore highlights parts of the protein which might play a notable role in the conformational transition from PrP(C) to PrP(Sc)
The review describes PrP(C)-to-PrP(Sc) conversion as a transition from an alpha-helix-rich form to a mainly beta-sheet-containing form.
Quoted textsource-backed
This conformational transition from the alpha-helix-rich cellular form into the mainly beta-sheet containing counterpart initiates an 'autocatalytic' reaction