ArticleActa neuropathologica2021
Structure of Tau filaments in Prion protein amyloidoses.
Article in Acta neuropathologica, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 78 citations in OpenAlex.
- Distinctive properties of the prion protein in the brain and retina in the amyloidosis associated with the PRNP F198S mutation.Acta neuropathologica · 2026Article
- Distinctive properties of the prion protein in the brain and retina in the amyloidosis associated with the PRNP F198S Mutation.Research square · 2026Article
- Structural and mechanistic characterization of heparin interactions with tau fibrils.The Journal of biological chemistry · 2026Article
- The Many Lives of a Single Sequence: Functional Plasticity Through Amyloid Polymorphism.Sub-cellular biochemistry · 2026Review
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- Seeding biosensor cell line that reproduces the Alzheimer tau fold.The Journal of biological chemistry · 2025Article
- Validation of helical symmetry parameters in the EMDB.Acta crystallographica. Section D, Structural biology · 2025Article
- Disrupting Amyloid Filaments of Tau by Means of Electric Fields.The journal of physical chemistry. B · 2025Article
- Tau filaments with the Alzheimer fold in human MAPT mutants V337M and R406W.Nature structural & molecular biology · 2025Article
- Ligands for Protein Fibrils of Amyloid-β, α-Synuclein, and Tau.Chemical reviews · 2025Review
- Cryo-EM evidence for a common factor in Alzheimer's and other neurodegenerations.bioRxiv : the preprint server for biology · 2025Article
- PRNP E146G mutation inherited prion disease: distinctive clinical, pathological and fluid biomarker features.Journal of neurology · 2025Article
- Recent Advances in Co-Condensation and Co-Aggregation of Amyloid Proteins Linked to Neurodegenerative Diseases.Current protein & peptide science · 2025Review
- Cryo-EM structures of cotton wool plaques' amyloid β and of tau filaments in dominantly inherited Alzheimer disease.Acta neuropathologica · 2024Article
- Cryo-EM structures of pathogenic fibrils and their impact on neurodegenerative disease research.Neuron · 2024Review
- Cryo-EM structures of amyloid-β and tau filaments in Down syndrome.Nature structural & molecular biology · 2024Article
- The structural line between prion and "prion-like": Insights from prion protein and tau.Current opinion in neurobiology · 2024Review
- The Enigma of Tau Protein Aggregation: Mechanistic Insights and Future Challenges.International journal of molecular sciences · 2024Review
- Tau filaments with the Alzheimer fold in cases withbioRxiv : the preprint server for biology · 2024Article
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9 authors at 2 institutions in 1 country.
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Abstract
In human neurodegenerative diseases associated with the intracellular aggregation of Tau protein, the ordered cores of Tau filaments adopt distinct folds. Here, we analyze Tau filaments isolated from the brain of individuals affected by Prion-Protein cerebral amyloid angiopathy (PrP-CAA) with a nonsense mutation in the PRNP gene that leads to early termination of translation of PrP (Q160Ter or Q160X), and Gerstmann-Sträussler-Scheinker (GSS) disease, with a missense mutation in the PRNP gene that leads to an amino acid substitution at residue 198 (F198S) of PrP. The clinical and neuropathologic phenotypes associated with these two mutations in PRNP are different; however, the neuropathologic analyses of these two genetic variants have consistently shown the presence of numerous neurofibrillary tangles (NFTs) made of filamentous Tau aggregates in neurons. We report that Tau filaments in PrP-CAA (Q160X) and GSS (F198S) are composed of 3-repeat and 4-repeat Tau isoforms, having a striking similarity to NFTs in Alzheimer disease (AD). In PrP-CAA (Q160X), Tau filaments are made of both paired helical filaments (PHFs) and straight filaments (SFs), while in GSS (F198S), only PHFs were found. Mass spectrometry analyses of Tau filaments extracted from PrP-CAA (Q160X) and GSS (F198S) brains show the presence of post-translational modifications that are comparable to those seen in Tau aggregates from AD. Cryo-EM analysis reveals that the atomic models of the Tau filaments obtained from PrP-CAA (Q160X) and GSS (F198S) are identical to those of the Tau filaments from AD, and are therefore distinct from those of Pick disease, chronic traumatic encephalopathy, and corticobasal degeneration. Our data support the hypothesis that in the presence of extracellular amyloid deposits and regardless of the primary amino acid sequence of the amyloid protein, similar molecular mechanisms are at play in the formation of identical Tau filaments.
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