Mechanism of misfolding of the human prion protein revealed by a pathological mutation
Mechanism of misfolding of the human prion protein revealed by a pathological mutation
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United States: National Academy of Sciences
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Language
English
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Publisher
United States: National Academy of Sciences
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Contents
The misfolding and aggregation of the human prion protein (PrP) is associated with transmissible spongiform encephalopathies (TSEs). Intermediate conformations forming during the conversion of the cellular form of PrP into its pathological scrapie conformation are key drivers of the misfolding process. Here, we analyzed the properties of the C-term...
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Full title
Mechanism of misfolding of the human prion protein revealed by a pathological mutation
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7999870
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7999870
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ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.2019631118
