ArticlePrion
Comparison of 2 synthetically generated recombinant prions.
Article in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 20 citations in OpenAlex.
- The octapeptide repeats of prion protein play critical roles in the pathogenesis of prion diseases.Acta neuropathologica communications · 2026Article
- Soluble N-terminal region of prion protein causes rapid neurodegeneration in prion disease.Science advances · 2025Article
- Cofactors facilitate bona fide prion misfolding in vitro but are not necessary for the infectivity of recombinant murine prions.PLoS pathogens · 2025Article
- Understanding the key features of the spontaneous formation of bona fide prions through a novel methodology that enables their swift and consistent generation.Acta neuropathologica communications · 2023Article
- Review
- Oral Ingestion of Synthetically Generated Recombinant Prion Is Sufficient to Cause Prion Disease in Wild-Type Mice.Pathogens (Basel, Switzerland) · 2020Article
- Isolation of infectious, non-fibrillar and oligomeric prions from a genetic prion disease.Brain : a journal of neurology · 2020Article
- Development of a new largely scalable in vitro prion propagation method for the production of infectious recombinant prions for high resolution structural studies.PLoS pathogens · 2019Article
- Treatment with a non-toxic, self-replicating anti-prion delays or prevents prion disease in vivo.Molecular psychiatry · 2018Article
- Prion-like mechanisms in Alzheimer disease.Handbook of clinical neurology · 2018Review
- Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Pathogens (Basel, Switzerland) · 2017Review
- Downregulation of the Repressor Element 1-Silencing Transcription Factor (REST) Is Associated with Akt-mTOR and Wnt-β-Catenin Signaling in Prion Diseases Models.Frontiers in molecular neuroscience · 2017Article
- Heparan Sulfate and Heparin Promote Faithful Prion Replication in Vitro by Binding to Normal and Abnormal Prion Proteins in Protein Misfolding Cyclic Amplification.The Journal of biological chemistry · 2016Article
- Isolation of a Defective Prion Mutant from Natural Scrapie.PLoS pathogens · 2016Article
- The Prion-Like Properties of Amyloid-β Assemblies: Implications for Alzheimer's Disease.Cold Spring Harbor perspectives in medicine · 2016Review
- Article
- Neurodegenerative diseases: expanding the prion concept.Annual review of neuroscience · 2015Review
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 4 institutions in 3 countries.
Funding
Abstract
Prion is a protein-conformation-based infectious agent causing fatal neurodegenerative diseases in humans and animals. Our previous studies revealed that in the presence of cofactors, infectious prions can be synthetically generated in vitro with bacterially expressed recombinant prion protein (PrP). Once initiated, the recombinant prion is able to propagate indefinitely via serial protein misfolding cyclic amplification (sPMCA). In this study, we compared 2 separately initiated recombinant prions. Our results showed that these 2 recombinant prions had distinct biochemical properties and caused different patterns of spongiosis and PrP deposition in inoculated mice. Our findings indicate that various recombinant prions can be initiated in vitro and potential reasons for this variability are discussed.
Indexed as
Identifiers
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.