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PrP(Sc)

Candidate: concept label1 source documents5 linked claims
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Aliases

disease associated, fibril-forming isoform PrP(Sc)

Evidence Snippets

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).
Evidence 1Source 1DOIPubMedprovenance

Supporting Sources

Linked Claims

Claim 1knowledge gapsupports2009Source 1DOIPubMed

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.
Claim 2mechanistic summarysupports2009Source 1DOIPubMed

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).
Claim 3pathogenesis summarysupports2009Source 1DOIPubMed

The review states that this conformational transition initiates an autocatalytic reaction leading to amyloid fibril accumulation in the CNS and neurodegeneration.

Quoted textsource-backed
This conformational transition from the alpha-helix-rich cellular form into the mainly beta-sheet containing counterpart initiates an 'autocatalytic' reaction which leads to the accumulation of amyloid fibrils in the central nervous system (CNS) and to neurodegeneration
Claim 4review focussupports2009Source 1DOIPubMed

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)
Claim 5structural transition summarysupports2009Source 1DOIPubMed

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