ArticlePLoS pathogens2012
Biochemical properties of highly neuroinvasive prion strains.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
50 citing papers in PubMed, 66 citations in OpenAlex.
- Exposure of cells to prions induces prion strain-dependent changes in mitochondrial redox state and respiration.Journal of cell science · 2026Article
- Extraneural infection route restricts prion conformational variability and attenuates the impact of quaternary structure on infectivity.PLoS pathogens · 2024Article
- Misfolded protein oligomers: mechanisms of formation, cytotoxic effects, and pharmacological approaches against protein misfolding diseases.Molecular neurodegeneration · 2024Review
- Prion strains: shining new light on old concepts.Cell and tissue research · 2023Review
- Cryo-EM of prion strains from the same genotype of host identifies conformational determinants.PLoS pathogens · 2022Article
- Genetic prion disease-related mutation E196K displays a novel amyloid fibril structure revealed by cryo-EM.Science advances · 2021Article
- Environmental and host factors that contribute to prion strain evolution.Acta neuropathologica · 2021Review
- Bovine adapted transmissible mink encephalopathy is similar to L-BSE after passage through sheep with the VRQ/VRQ genotype but not VRQ/ARQ.BMC veterinary research · 2020Article
- Host prion protein expression levels impact prion tropism for the spleen.PLoS pathogens · 2020Article
- Crossing Species Barriers Relies on Structurally Distinct Prion Assemblies and Their Complementation.Molecular neurobiology · 2020Article
- Prion protein glycans reduce intracerebral fibril formation and spongiosis in prion disease.The Journal of clinical investigation · 2020Article
- Novel Strain of the Chronic Wasting Disease Agent Isolated From Experimentally Inoculated Elk With LL132 Prion Protein.Scientific reports · 2020Article
- Thermostability as a highly dependent prion strain feature.Scientific reports · 2019Article
- Review
- Protein-solvent interfaces in human Y145Stop prion protein amyloid fibrils probed by paramagnetic solid-state NMR spectroscopy.Journal of structural biology · 2019Article
- Synthetic Prion Selection and Adaptation.Molecular neurobiology · 2019Article
- Understanding Prion Strains: Evidence from Studies of the Disease Forms Affecting Humans.Viruses · 2019Review
- Cellular and Molecular Mechanisms of Prion Disease.Annual review of pathology · 2019Review
- Early stage prion assembly involves two subpopulations with different quaternary structures and a secondary templating pathway.Communications biology · 2019Article
- Generation of novel neuroinvasive prions following intravenous challenge.Brain pathology (Zurich, Switzerland) · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Infectious prions propagate from peripheral entry sites into the central nervous system (CNS), where they cause progressive neurodegeneration that ultimately leads to death. Yet the pathogenesis of prion disease can vary dramatically depending on the strain, or conformational variant of the aberrantly folded and aggregated protein, PrP(Sc). Although most prion strains invade the CNS, some prion strains cannot gain entry and do not cause clinical signs of disease. The conformational basis for this remarkable variation in the pathogenesis among strains is unclear. Using mouse-adapted prion strains, here we show that highly neuroinvasive prion strains primarily form diffuse aggregates in brain and are noncongophilic, conformationally unstable in denaturing conditions, and lead to rapidly lethal disease. These neuroinvasive strains efficiently generate PrP(Sc) over short incubation periods. In contrast, the weakly neuroinvasive prion strains form large fibrillary plaques and are stable, congophilic, and inefficiently generate PrP(Sc) over long incubation periods. Overall, these results indicate that the most neuroinvasive prion strains are also the least stable, and support the concept that the efficient replication and unstable nature of the most rapidly converting prions may be a feature linked to their efficient spread into the CNS.
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What OpenQuestion holds
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.