ArticleJournal of virology2016
Assessment of the PrPc Amino-Terminal Domain in Prion Species Barriers.
Article in Journal of virology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
8 citing papers in PubMed, 12 citations in OpenAlex.
- Development of a sensitive real-time quaking-induced conversion (RT-QuIC) assay for application in prion-infected blood.PloS one · 2023Article
- Identification of a homology-independent linchpin domain controlling mouse and bank vole prion protein conversion.PLoS pathogens · 2020Article
- Cellulose ether treatment in vivo generates chronic wasting disease prions with reduced protease resistance and delayed disease progression.Journal of neurochemistry · 2020Article
- Article
- Mutations in Prion Protein Gene: Pathogenic Mechanisms in C-Terminal vs. N-Terminal Domain, a Review.International journal of molecular sciences · 2019Review
- Modified Protein Misfolding Cyclic Amplification Overcomes Real-Time Quaking-Induced Conversion Assay Inhibitors in Deer Saliva To Detect Chronic Wasting Disease Prions.Journal of clinical microbiology · 2018Article
- Endogenous Brain Lipids Inhibit Prion Amyloid FormationJournal of virology · 2017Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Chronic wasting disease (CWD) in cervids and bovine spongiform encephalopathy (BSE) in cattle are prion diseases that are caused by the same protein-misfolding mechanism, but they appear to pose different risks to humans. We are interested in understanding the differences between the species barriers of CWD and BSE. We used real-time, quaking-induced conversion (RT-QuIC) to model the central molecular event in prion disease, the templated misfolding of the normal prion protein, PrP IMPORTANCE: We demonstrate that the amino-terminal domain of the normal prion protein, 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.