ArticleNeurobiology of disease2016
A single amino acid (Asp159) from the dog prion protein suppresses the toxicity of the mouse prion protein in Drosophila.
Article in Neurobiology of disease, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Prion Protein Codon Implicated in Resistance in Dogs Detected in Non-Domesticated Members of Mammalia.Animals : an open access journal from MDPI · 2026Article
- First report of novel single-nucleotide polymorphisms and genetic characteristics in the open reading frame of the prion protein gene (Frontiers in veterinary science · 2026Article
- Prion disease modelled in Drosophila.Cell and tissue research · 2023Review
- Intrinsic determinants of prion protein neurotoxicity inFrontiers in molecular neuroscience · 2023Review
- Novel Single Nucleotide Polymorphisms (SNPs) and Genetic Features of the Prion Protein Gene (Frontiers in veterinary science · 2022Article
- Insight From Animals Resistant to Prion Diseases: Deciphering the Genotype - Morphotype - Phenotype Code for the Prion Protein.Frontiers in cellular neuroscience · 2020Review
- The First Report of Polymorphisms and Genetic Features of theInternational journal of molecular sciences · 2019Article
- D159 and S167 are protective residues in the prion protein from dog and horse, two prion-resistant animals.Neurobiology of disease · 2018Article
- Unraveling the key to the resistance of canids to prion diseases.PLoS pathogens · 2017Article
- Drosophila models of prionopathies: insight into prion protein function, transmission, and neurotoxicity.Current opinion in genetics & development · 2017Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Misfolding of the prion protein (PrP) is the key step in the transmission of spongiform pathologies in humans and several animals. Although PrP is highly conserved in mammals, a few changes in the sequence of endogenous PrP are proposed to confer protection to dogs, which were highly exposed to prion during the mad-cow epidemics. D159 is a unique amino acid found in PrP from dogs and other canines that was shown to alter surface charge, but its functional relevance has never been tested in vivo. Here, we show in transgenic Drosophila that introducing the N159D substitution on mouse PrP decreases its turnover. Additionally, mouse PrP-N159D demonstrates no toxicity and accumulates no pathogenic conformations, suggesting that a single D159 substitution is sufficient to prevent PrP conformational change and pathogenesis. Understanding the mechanisms mediating the protective activity of D159 is likely to lessen the burden of prion diseases in humans and domestic animals.
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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.