ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006
Accelerated accumulation of misfolded prion protein and spongiform degeneration in a Drosophila model of Gerstmann-Sträussler-Scheinker syndrome.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 56 citations in OpenAlex.
- 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
- Review
- New Drosophila models to uncover the intrinsic and extrinsic factors that mediate the toxicity of the human prion protein.Disease models & mechanisms · 2022Article
- Article
- Insight From Animals Resistant to Prion Diseases: Deciphering the Genotype - Morphotype - Phenotype Code for the Prion Protein.Frontiers in cellular neuroscience · 2020Review
- 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
- Prion disease: experimental models and reality.Acta neuropathologica · 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
- Interallelic Transcriptional Enhancement as an in Vivo Measure of Transvection in Drosophila melanogaster.G3 (Bethesda, Md.) · 2016Article
- Review
- Prion protein facilitates synaptic vesicle release by enhancing release probability.Human molecular genetics · 2014Article
- Polar substitutions in helix 3 of the prion protein produce transmembrane isoforms that disturb vesicle trafficking.Human molecular genetics · 2013Article
- Drosophila models of proteinopathies: the little fly that could.Current pharmaceutical design · 2012Review
- Drosophila melanogaster as a model system for studies of islet amyloid polypeptide aggregation.PloS one · 2011Article
- Sequence-dependent prion protein misfolding and neurotoxicity.The Journal of biological chemistry · 2010Article
- A Drosophila model of GSS syndrome suggests defects in active zones are responsible for pathogenesis of GSS syndrome.Human molecular genetics · 2010Article
- Neuron dysfunction is induced by prion protein with an insertional mutation via a Fyn kinase and reversed by sirtuin activation in Caenorhabditis elegans.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
Corrections and comments
- Commented on byMad fly disease.2007
Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prion diseases are CNS disorders that can occur in sporadic, infectious, and inherited forms. Although all forms of prion disease are associated with the accumulation of pathogenic conformers of the prion protein, collectively termed PrP(Sc), the mechanisms by which PrP(Sc) molecules form and cause neuronal degeneration are unknown. Using the bipartite galactosidase-4-upstream activating sequence expression system, we generated transgenic Drosophila melanogaster heterologously expressing either wild-type (WT) or mutant, disease-associated (P101L) mouse PrP molecules in cholinergic neurons. Transgenic flies expressing neuronal P101L PrP molecules exhibited severe locomotor dysfunction and premature death as larvae and adults. These striking clinical abnormalities were accompanied by age-dependent accumulation of misfolded PrP molecules, intracellular PrP aggregates, and neuronal vacuoles. In contrast, transgenic flies expressing comparable levels of WT PrP displayed no clinical, pathological, or biochemical abnormalities. These results indicate that transgenic Drosophila expressing neuronal P101L PrP specifically exhibit several hallmark features of human Gerstmann-Sträussler-Scheinker (GSS) syndrome. Because the rates of abnormal PrP accumulation and clinical progression are highly accelerated in Drosophila compared with the rates of these processes in rodents or humans, the P101L mutant may be used for future genetic and pharmacologic studies as a novel invertebrate model of GSS.
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.