{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Gilbert MAG"],"funding":["Medical Research Council","Wellcome Trust"],"pagination":["913-919"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11269202"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["631(8022)"],"pubmed_abstract":["A defining pathological feature of most neurodegenerative diseases is the assembly of proteins into amyloid that form disease-specific structures<sup>1</sup>. In Alzheimer's disease, this is characterized by the deposition of β-amyloid and tau with disease-specific conformations. The in situ structure of amyloid in the human brain is unknown. Here, using cryo-fluorescence microscopy-targeted cryo-sectioning, cryo-focused ion beam-scanning electron microscopy lift-out and cryo-electron tomography, we determined in-tissue architectures of β-amyloid and tau pathology in a postmortem Alzheimer's disease donor brain. β-amyloid plaques contained a mixture of fibrils, some of which were branched, and protofilaments, arranged in parallel arrays and lattice-like structures. Extracellular vesicles a"],"journal":["Nature"],"pubmed_title":["CryoET of β-amyloid and tau within postmortem Alzheimer's disease brain."],"pmcid":["PMC11269202"],"funding_grant_id":["MR/T011149/1","204963/Z/16/Z","208395","108466","MR/V022644/1","209407/Z/17/Z","221524"],"pubmed_authors":["Geibel M","Radford SE","O'Sullivan TJ","Halfon Y","Hoozemans JJM","Schertel A","Fatima N","Wilkinson M","Gilbert MAG","Morrema THJ","Ranson NA","Frank RAW","Jenkins J","Read RJ"],"additional_accession":[]},"is_claimable":false,"name":"CryoET of β-amyloid and tau within postmortem Alzheimer's disease brain.","description":"A defining pathological feature of most neurodegenerative diseases is the assembly of proteins into amyloid that form disease-specific structures<sup>1</sup>. In Alzheimer's disease, this is characterized by the deposition of β-amyloid and tau with disease-specific conformations. The in situ structure of amyloid in the human brain is unknown. Here, using cryo-fluorescence microscopy-targeted cryo-sectioning, cryo-focused ion beam-scanning electron microscopy lift-out and cryo-electron tomography, we determined in-tissue architectures of β-amyloid and tau pathology in a postmortem Alzheimer's disease donor brain. β-amyloid plaques contained a mixture of fibrils, some of which were branched, and protofilaments, arranged in parallel arrays and lattice-like structures. Extracellular vesicles a","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Jul","modification":"2026-05-04T06:38:28.993Z","creation":"2025-04-19T13:14:35.291Z"},"accession":"S-EPMC11269202","cross_references":{"pubmed":["38987603"],"doi":["10.1038/s41586-024-07680-x"]}}