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An unusual soluble beta-turn-rich conformation of prion is involved in fibril formation and toxic to neuronal cells.

Abstract:

A key molecular event in prion diseases is the conversion of the prion protein (PrP) from its normal cellular form (PrPC) to the disease-specific form (PrPSc). The transition from PrPC to PrPSc involves a major conformational change, resulting in amorphous protein aggregates and fibrillar amyloid deposits with increased beta-sheet structure. Using recombinant PrP refolded into a beta-sheet-rich form (beta-PrP) we have studied the fibrillization of beta-PrP both in solution and in association ...

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Publication status:
Published

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Publisher copy:
10.1016/j.bbrc.2004.12.172

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Journal:
Biochemical and biophysical research communications
Volume:
328
Issue:
1
Pages:
292-305
Publication date:
2005-03-01
DOI:
EISSN:
1090-2104
ISSN:
0006-291X
Source identifiers:
100187

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