ArticleMolecular psychiatry2018
Treatment with a non-toxic, self-replicating anti-prion delays or prevents prion disease in vivo.
Article in Molecular psychiatry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 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
12 citing papers in PubMed, 28 citations in OpenAlex.
- Transmissible long-term neuroprotective and pro-cognitive effects of 1-42 beta-amyloid with A2T icelandic mutation in an Alzheimer's disease mouse model.Molecular psychiatry · 2024Article
- Therapeutic perspectives for prion diseases in humans and animals.PLoS pathogens · 2024Article
- Multiple aspects of amyloid dynamicsFrontiers in molecular neuroscience · 2024Article
- α-Synuclein Strains: Does Amyloid Conformation Explain the Heterogeneity of Synucleinopathies?Biomolecules · 2021Review
- Tau immunotherapies: Lessons learned, current status and future considerations.Neuropharmacology · 2020Review
- Review
- Protein misfolding, aggregation, and conformational strains in neurodegenerative diseases.Nature neuroscience · 2018Review
- Prions, prionoids and protein misfolding disorders.Nature reviews. Genetics · 2018Review
- Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Pathogens (Basel, Switzerland) · 2017Review
- How do PrPPathogens (Basel, Switzerland) · 2017Review
- Reduced Abundance and Subverted Functions of Proteins in Prion-Like Diseases: Gained Functions Fascinate but Lost Functions Affect Aetiology.International journal of molecular sciences · 2017Review
- Prion disease: 'Anti-prions' block prion disease onset.Nature reviews. Neurology · 2017Article
Corrections and comments
- Commented on by
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Transmissible spongiform encephalopathies (TSEs) are fatal neurological disorders caused by prions, which are composed of a misfolded protein (PrP
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.