ArticleProceedings of the National Academy of Sciences of the United States of America2009
Highly sensitive, quantitative cell-based assay for prions adsorbed to solid surfaces.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
What it found
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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
28 citing papers in PubMed, 61 citations in OpenAlex.
- Population screening for variant Creutzfeldt-Jakob disease using a novel blood test: diagnostic accuracy and feasibility study.JAMA neurology · 2014Trial
- A scalable, dividing cell model for the robust propagation and quantification of human sporadic Creutzfeldt-Jakob disease prions.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Rapid and sensitive determination of residual prion infectivity from prion-decontaminated surfaces.mSphere · 2024Article
- Article
- A structural basis for prion strain diversity.Nature chemical biology · 2023Article
- Improving the Predictive Value of Prion Inactivation Validation Methods to Minimize the Risks of Iatrogenic Transmission With Medical Instruments.Frontiers in bioengineering and biotechnology · 2020Review
- Enhanced detection of prion infectivity from blood by preanalytical enrichment with peptoid-conjugated beads.PloS one · 2019Article
- Article
- Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Pathogens (Basel, Switzerland) · 2017Review
- Diagnosing Sporadic Creutzfeldt-Jakob Disease by the Detection of Abnormal Prion Protein in Patient Urine.JAMA neurology · 2016Article
- Inactivation of Prions and Amyloid Seeds with Hypochlorous Acid.PLoS pathogens · 2016Article
- Temporal Resolution of Misfolded Prion Protein Transport, Accumulation, Glial Activation, and Neuronal Death in the Retinas of Mice Inoculated with Scrapie.The American journal of pathology · 2016Article
- Ex vivo mammalian prions are formed of paired double helical prion protein fibrils.Open biology · 2016Article
- 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
- Rapid chemical decontamination of infectious CJD and scrapie particles parallels treatments known to disrupt microbes and biofilms.Virulence · 2015Article
- Identification of misfolded proteins in body fluids for the diagnosis of prion diseases.International journal of cell biology · 2013Review
- Fast and ultrasensitive method for quantitating prion infectivity titre.Nature communications · 2012Article
- Plasmacytoid dendritic cells sequester high prion titres at early stages of prion infection.PLoS pathogens · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Prions are comprised principally of aggregates of a misfolded host protein and cause fatal transmissible neurodegenerative disorders of humans and animals, such as variant Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Prions pose significant public health concerns, including contamination of blood products and surgical instruments; require laborious and often insensitive animal bioassay to detect; and resist conventional hospital sterilization methods. A major experimental advance was the cell culture-based scrapie cell assay, allowing prion titres to be estimated more precisely and an order of magnitude faster than by animal bioassays. Here we describe a bioassay method that exploits the marked binding affinity of prions to steel surfaces. Using steel wires as a concentrating and sensitization tool and combining with an adapted scrapie cell endpoint assay we can achieve, for mouse prions, a sensitivity 100x higher than that achieved in standard mouse bioassays. The rapidity and sensitivity of this assay offers a major advance over small animal bioassay in many aspects of prion research. In addition, its specific application in assay of metal-bound prions allows evaluation of novel prion decontamination methods.
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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.