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Journal article

Globular and pre-fibrillar prion aggregates are toxic to neuronal cells and perturb their electrophysiology.

Abstract:

Prion diseases are characterised at autopsy by neuronal loss and accumulation of amorphous protein aggregates and/or amyloid fibrils in the brains of humans and animals. These protein deposits result from the conversion of the cellular, mainly alpha-helical prion protein (PrP(C)) to the beta-sheet-rich isoform (PrP(Sc)). Although the pathogenic mechanism of prion diseases is not fully understood, it appears that protein aggregation is itself neurotoxic and not the product of cell death. The p...

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Publication status:
Published

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Journal:
Biochimica et biophysica acta
Volume:
1784
Issue:
6
Pages:
873-881
Publication date:
2008-06-05
DOI:
ISSN:
0006-3002
URN:
uuid:1b6f88b2-c312-4f73-9fda-aceba7854df1
Source identifiers:
99996
Local pid:
pubs:99996

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