ArticleProceedings of the National Academy of Sciences of the United States of America2010
Spontaneous generation of mammalian prions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 44 citations in OpenAlex.
- 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
- Neurotropic influenza A virus infection causes prion protein misfolding into infectious prions in neuroblastoma cells.Scientific reports · 2021Article
- Protective anti-prion antibodies in human immunoglobulin repertoires.EMBO molecular medicine · 2020Article
- The biofilm adhesion protein Aap fromThe Journal of biological chemistry · 2020Article
- A Novel, Reliable and Highly Versatile Method to Evaluate Different Prion Decontamination Procedures.Frontiers in bioengineering and biotechnology · 2020Article
- Enhanced detection of prion infectivity from blood by preanalytical enrichment with peptoid-conjugated beads.PloS one · 2019Article
- Prion Strains and Transmission Barrier Phenomena.Pathogens (Basel, Switzerland) · 2018Review
- Review
- Insights into Mechanisms of Chronic Neurodegeneration.International journal of molecular sciences · 2016Review
- Preclinical detection of infectivity and disease-specific PrP in blood throughout the incubation period of prion disease.Scientific reports · 2015Article
- A systematic investigation of production of synthetic prions from recombinant prion protein.Open biology · 2015Article
- Review
- Pathogenic mutations within the hydrophobic domain of the prion protein lead to the formation of protease-sensitive prion species with increased lethality.Journal of virology · 2014Article
- Polythiophenes inhibit prion propagation by stabilizing prion protein (PrP) aggregates.The Journal of biological chemistry · 2012Article
- Ubiquitous amyloids.Applied biochemistry and biotechnology · 2012Review
- Spontaneous generation of rapidly transmissible prions in transgenic mice expressing wild-type bank vole prion protein.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Ultra-efficient PrP(Sc) amplification highlights potentialities and pitfalls of PMCA technology.PLoS pathogens · 2011Article
- An auto-catalytic surface for conformational replication of amyloid fibrils--genesis of an amyloid world?Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2011Article
- Nuclease resistant circular DNAs copurify with infectivity in scrapie and CJD.Journal of neurovirology · 2011Article
- Superparamagnetic nanoparticle capture of prions for amplification.Journal of virology · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 6 institutions in 2 countries.
Funding
Abstract
Prions are transmissible agents that cause lethal neurodegeneration in humans and other mammals. Prions bind avidly to metal surfaces such as steel wires and, when surface-bound, can initiate infection of brain or cultured cells with remarkable efficiency. While investigating the properties of metal-bound prions by using the scrapie cell assay to measure infectivity, we observed, at low frequency, positive assay results in control groups in which metal wires had been coated with uninfected mouse brain homogenate. This phenomenon proved to be reproducible in rigorous and exhaustive control experiments designed to exclude prion contamination. The infectivity generated in cell culture could be readily transferred to mice and had strain characteristics distinct from the mouse-adapted prion strains used in the laboratory. The apparent "spontaneous generation" of prions from normal brain tissue could result if the metal surface, possibly with bound cofactors, catalyzed de novo formation of prions from normal cellular prion protein. Alternatively, if prions were naturally present in the brain at levels not detectable by conventional methods, metal surfaces might concentrate them to the extent that they become quantifiable by the scrapie cell assay.
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.