ArticleNature structural & molecular biology2022
Cryo-EM structure of disease-related prion fibrils provides insights into seeding barriers.
Article in Nature structural & molecular biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- PrPStem cell reports · 2026Article
- In vitro, cellular and in vivo studies of amyloid oligomers structure and toxicity: Challenges and advances.Protein science : a publication of the Protein Society · 2026Review
- Prions and protein aggregates as pathogens, self-propagating structures, biomarkers, and therapeutic targets.Microbiology and molecular biology reviews : MMBR · 2025Review
- The Glycine-Rich Region as a Flexible Molecular Glue Promoting hPrPJournal of chemical information and modeling · 2025Article
- Prion protein E219K polymorphism: from the discovery of the KANNO blood group to interventions for human prion disease.Frontiers in neurology · 2024Review
- Mechanisms and pathology of protein misfolding and aggregation.Nature reviews. Molecular cell biology · 2023Review
- Classification of helical polymers with deep-learning language models.Journal of structural biology · 2023Article
- Recent advances in infectious disease research using cryo-electron tomography.Frontiers in molecular biosciences · 2023Review
- Development of a methodology for large-scale production of prions for biological and structural studies.Frontiers in molecular biosciences · 2023Article
- Cryo-EM structures of prion protein filaments from Gerstmann-Sträussler-Scheinker disease.Acta neuropathologica · 2022Article
- Structural biology of ex vivo mammalian prions.The Journal of biological chemistry · 2022Review
- Pathogenic prion structures at high resolution.PLoS pathogens · 2022Article
- Structural consequences of sequence variation in mammalian prion β2α2 loop segments.Frontiers in neuroscience · 2022Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
One of the least understood aspects of prion diseases is the structure of infectious prion protein aggregates. Here we report a high-resolution cryo-EM structure of amyloid fibrils formed by human prion protein with the Y145Stop mutation that is associated with a familial prion disease. This structural insight allows us not only to explain previous biochemical findings, but also provides direct support for the conformational adaptability model of prion transmissibility barriers.
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Registered trials
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