{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Emendato A"],"funding":["European Research Council"],"pagination":["1704"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12657908"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(1)"],"pubmed_abstract":["The misfolding of the human prion protein (hPrP) and the consequent self-assembly into insoluble amyloid fibrils are associated with neurodegenerative diseases known as transmissible spongiform encephalopathies (TSEs). In this study, we investigated the stability and aggregation behaviour of the folded C-terminal domain of hPrP (hPrP<sup>C</sup><sub>125-230</sub>) and observed that, under specific experimental conditions, this region of the protein rapidly aggregates into round-shaped oligomers. The isolated oligomers exhibited hallmarks properties of amyloid aggregates, including a β-sheet-rich structure, enhanced hydrophobic exposure, and Thioflavin T (ThT)-induced fluorescence. When incubated with neural precursor cells these hPrP oligomers, unlike monomeric species, induced mitochondri"],"journal":["Communications biology"],"pubmed_title":["Structural and cellular properties of human prion protein oligomers."],"pmcid":["PMC12657908"],"funding_grant_id":["BioDisOrder - 819644"],"pubmed_authors":["Parisi S","Zizolfi MC","Mansueto S","Peltrini R","De Simone A","Emendato A","Divisato G","Giannino E"],"additional_accession":[]},"is_claimable":false,"name":"Structural and cellular properties of human prion protein oligomers.","description":"The misfolding of the human prion protein (hPrP) and the consequent self-assembly into insoluble amyloid fibrils are associated with neurodegenerative diseases known as transmissible spongiform encephalopathies (TSEs). In this study, we investigated the stability and aggregation behaviour of the folded C-terminal domain of hPrP (hPrP<sup>C</sup><sub>125-230</sub>) and observed that, under specific experimental conditions, this region of the protein rapidly aggregates into round-shaped oligomers. The isolated oligomers exhibited hallmarks properties of amyloid aggregates, including a β-sheet-rich structure, enhanced hydrophobic exposure, and Thioflavin T (ThT)-induced fluorescence. When incubated with neural precursor cells these hPrP oligomers, unlike monomeric species, induced mitochondri","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Nov","modification":"2026-06-07T04:32:59.83Z","creation":"2026-06-07T03:06:56.548Z"},"accession":"S-EPMC12657908","cross_references":{"pubmed":["41299034"],"doi":["10.1038/s42003-025-09105-5"]}}