Proteolysis of prion protein by cathepsin S generates a soluble b-structured intermediate oligomeric...
Proteolysis of prion protein by cathepsin S generates a soluble b-structured intermediate oligomeric form, with potential implications for neurotoxic mechanisms
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English
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Formation of PrP aggregates is considered to be a characteristic event in the pathogenesis of TSE diseases, accompanied by brain inflammation and neurodegeneration. Factors identified as contributing to aggregate formation are of interest as potential therapeutic targets. We report that in vitro proteolysis of ovine PrP sub(94-233) (at neutral pH a...
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Proteolysis of prion protein by cathepsin S generates a soluble b-structured intermediate oligomeric form, with potential implications for neurotoxic mechanisms
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TN_cdi_proquest_miscellaneous_21233703
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_21233703
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0175-7571
E-ISSN
1432-1017
DOI
10.1007/s00249-008-0371-3
