ArticleOpen biology2016
Ex vivo mammalian prions are formed of paired double helical prion protein fibrils.
Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 62 citations in OpenAlex.
- Prion propagation is controlled by discrete structural regions of PrP rather than overall stability.The Journal of biological chemistry · 2026Article
- Effect of incineration, co-incineration and combustion on TSE hazards in category 1 animal by-products.EFSA journal. European Food Safety Authority · 2025Article
- Article
- BSE risk posed by ruminant collagen and gelatine derived from bones.EFSA journal. European Food Safety Authority · 2024Article
- Multiple aspects of amyloid dynamicsFrontiers in molecular neuroscience · 2024Article
- Prion protein conversion at two distinct cellular sites precedes fibrillisation.Nature communications · 2023Article
- Full-length prion protein incorporated into prion aggregates is a marker for prion strain-specific destabilization of aggregate structure following cellular uptake.Journal of biochemistry · 2023Article
- A structural basis for prion strain diversity.Nature chemical biology · 2023Article
- Prion strains viewed through the lens of cryo-EM.Cell and tissue research · 2023Review
- Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures.Viruses · 2022Review
- 2.7 Å cryo-EM structure of ex vivo RML prion fibrils.Nature communications · 2022Article
- Genetic prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM.Science advances · 2021Article
- From Kuru to Alzheimer: A personal outlook.Protein science : a publication of the Protein Society · 2021Review
- The ultrastructure of infectious L-type bovine spongiform encephalopathy prions constrains molecular models.PLoS pathogens · 2021Article
- Asymmetric-flow field-flow fractionation of prions reveals a strain-specific continuum of quaternary structures with protease resistance developing at a hydrodynamic radius of 15 nm.PLoS pathogens · 2021Article
- Scaling analysis reveals the mechanism and rates of prion replication in vivo.Nature structural & molecular biology · 2021Article
- Analysis of circulating protein aggregates as a route of investigation into neurodegenerative disorders.Brain communications · 2021Article
- Altered DNA methylation profiles in blood from patients with sporadic Creutzfeldt-Jakob disease.Acta neuropathologica · 2020Article
- Highly infectious prions are not directly neurotoxic.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural effects of the highly protective V127 polymorphism on human prion protein.Communications biology · 2020Article
Corrections and comments
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Authors and funding
12 authors at 2 institutions in 1 country.
Funding
Abstract
Mammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but structures observed to date have not been definitively correlated with infectivity and the three-dimensional structure of infectious prions has remained obscure. Recently, we developed novel methods to obtain exceptionally pure preparations of prions from mouse brain and showed that pathogenic PrP in these high-titre preparations is assembled into rod-like assemblies. Here, we have used precise cell culture-based prion infectivity assays to define the physical relationship between the PrP rods and prion infectivity and have used electron tomography to define their architecture. We show that infectious PrP rods isolated from multiple prion strains have a common hierarchical assembly comprising twisted pairs of short fibres with repeating substructure. The architecture of the PrP rods provides a new structural basis for understanding prion infectivity and can explain the inability to systematically generate high-titre synthetic prions from recombinant PrP.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.