{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hallinan GI"],"funding":["NCATS NIH HHS","NIA NIH HHS","NINDS NIH HHS","NCI NIH HHS","NIH","NIGMS NIH HHS"],"pagination":["509-520"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9381446"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["144(3)"],"pubmed_abstract":["Prion protein (PrP) aggregation and formation of PrP amyloid (APrP) are central events in the pathogenesis of prion diseases. In the dominantly inherited prion protein amyloidosis known as Gerstmann-Sträussler-Scheinker (GSS) disease, plaques made of PrP amyloid are present throughout the brain. The c.593t > c mutation in the prion protein gene (PRNP) results in a phenylalanine to serine amino acid substitution at PrP residue 198 (F198S) and causes the most severe amyloidosis among GSS variants. It has been shown that neurodegeneration in this disease is associated with the presence of extracellular APrP plaques and neuronal intracytoplasmic Tau inclusions, that have been shown to contain paired helical filaments identical to those found in Alzheimer disease. Using cryogenic electron micro"],"journal":["Acta neuropathologica"],"pubmed_title":["Cryo-EM structures of prion protein filaments from Gerstmann-Straussler-Scheinker disease."],"pmcid":["PMC9381446"],"funding_grant_id":["AG010133","P30 AG072976","T32 GM132024","P30 AG010133","U01 NS110437","P30 CA082709","RF1 AG071177","UL1 TR002529","RF1-AG071177","U01-NS110437"],"pubmed_authors":["Li D","Jacobsen M","Vago FS","Hallinan GI","Garringer HJ","Mosley AL","Ghetti B","Bharath SR","Fernandez A","Cracco L","Jiang W","Hoq MR","Doud EH","Vidal R","Ozcan KA"],"additional_accession":[]},"is_claimable":false,"name":"Cryo-EM structures of prion protein filaments from Gerstmann-Straussler-Scheinker disease.","description":"Prion protein (PrP) aggregation and formation of PrP amyloid (APrP) are central events in the pathogenesis of prion diseases. In the dominantly inherited prion protein amyloidosis known as Gerstmann-Sträussler-Scheinker (GSS) disease, plaques made of PrP amyloid are present throughout the brain. The c.593t > c mutation in the prion protein gene (PRNP) results in a phenylalanine to serine amino acid substitution at PrP residue 198 (F198S) and causes the most severe amyloidosis among GSS variants. It has been shown that neurodegeneration in this disease is associated with the presence of extracellular APrP plaques and neuronal intracytoplasmic Tau inclusions, that have been shown to contain paired helical filaments identical to those found in Alzheimer disease. Using cryogenic electron micro","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Sep","modification":"2026-06-01T02:15:32.15Z","creation":"2025-02-19T01:28:42.389Z"},"accession":"S-EPMC9381446","cross_references":{"pubmed":["35819518"],"doi":["10.1007/s00401-022-02461-0"]}}