ArticleThe Journal of biological chemistry2010
Sequence-dependent prion protein misfolding and neurotoxicity.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- A Drosophila model of prion disease and its metabolic changes in the brain.Animal models and experimental medicine · 2025Article
- Genetic modulation of CWD prion propagation in cervid PrP Drosophila.The Biochemical journal · 2023Article
- Prion disease modelled in Drosophila.Cell and tissue research · 2023Review
- Intrinsic determinants of prion protein neurotoxicity inFrontiers in molecular neuroscience · 2023Review
- New Drosophila models to uncover the intrinsic and extrinsic factors that mediate the toxicity of the human prion protein.Disease models & mechanisms · 2022Article
- Insight From Animals Resistant to Prion Diseases: Deciphering the Genotype - Morphotype - Phenotype Code for the Prion Protein.Frontiers in cellular neuroscience · 2020Review
- D159 and S167 are protective residues in the prion protein from dog and horse, two prion-resistant animals.Neurobiology of disease · 2018Article
- Article
- Genetic human prion disease modelled in PrP transgenicThe Biochemical journal · 2017Article
- Drosophila models of prionopathies: insight into prion protein function, transmission, and neurotoxicity.Current opinion in genetics & development · 2017Review
- A single amino acid (Asp159) from the dog prion protein suppresses the toxicity of the mouse prion protein in Drosophila.Neurobiology of disease · 2016Article
- Progress on low susceptibility mechanisms of transmissible spongiform encephalopathies.Dong wu xue yan jiu = Zoological research · 2014Review
- Prion protein facilitates synaptic vesicle release by enhancing release probability.Human molecular genetics · 2014Article
- Cytosolic PrP can participate in prion-mediated toxicity.Journal of virology · 2014Article
- How does domain replacement affect fibril formation of the rabbit/human prion proteins.PloS one · 2014Article
- Polar substitutions in helix 3 of the prion protein produce transmembrane isoforms that disturb vesicle trafficking.Human molecular genetics · 2013Article
- Purification of transcripts and metabolites from Drosophila heads.Journal of visualized experiments : JoVE · 2013Article
- Drosophila models of proteinopathies: the little fly that could.Current pharmaceutical design · 2012Review
- Fibril formation of the rabbit/human/bovine prion proteins.Biophysical journal · 2011Article
- Pulling rabbits to reveal the secrets of the prion protein.Communicative & integrative biology · 2011Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Prion diseases are neurodegenerative disorders caused by misfolding of the normal prion protein (PrP) into a pathogenic "scrapie" conformation. To better understand the cellular and molecular mechanisms that govern the conformational changes (conversion) of PrP, we compared the dynamics of PrP from mammals susceptible (hamster and mouse) and resistant (rabbit) to prion diseases in transgenic flies. We recently showed that hamster PrP induces spongiform degeneration and accumulates into highly aggregated, scrapie-like conformers in transgenic flies. We show now that rabbit PrP does not induce spongiform degeneration and does not convert into scrapie-like conformers. Surprisingly, mouse PrP induces weak neurodegeneration and accumulates small amounts of scrapie-like conformers. Thus, the expression of three highly conserved mammalian prion proteins in transgenic flies uncovered prominent differences in their conformational dynamics. How these properties are encoded in the amino acid sequence remains to be elucidated.
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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.