Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core
Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core
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New York: Nature Publishing Group US
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English
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New York: Nature Publishing Group US
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Self-templating assemblies of the human prion protein are clinically associated with transmissible spongiform encephalopathies. Here we present the cryo-EM structure of a denaturant- and protease-resistant fibril formed in vitro spontaneously by a 9.7-kDa unglycosylated fragment of the human prion protein. This human prion fibril contains two proto...
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Cryo-EM structure of a human prion fibril with a hydrophobic, protease-resistant core
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7338044
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_7338044
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ISSN
1545-9993,1545-9985
E-ISSN
1545-9985
DOI
10.1038/s41594-020-0403-y
