ReviewInternational journal of cell biology2013
Synaptic dysfunction in prion diseases: a trafficking problem?
Review in International journal of cell biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 27 citations in OpenAlex.
- Accurate genomic predictions for chronic wasting disease in North American elk.G3 (Bethesda, Md.) · 2026Article
- Bovine Spongiform Encephalopathy: An Integrated Review of Prion Mechanisms, Neuroanatomy, and Control.Veterinary sciences · 2026Review
- Time-dependent transcriptomic response to scrapie exposure in ovine MSC-derived neuron-like cells.Frontiers in cellular and infection microbiology · 2026Article
- Aberrance of GAP43/p-GAP43 Closely Associates with the Pathology of Neuron Loss in Prion-Infected Rodent Models.Molecular neurobiology · 2025Article
- Unwanted Exacerbation of the Immune Response in Neurodegenerative Disease: A Time to Review the Impact.Frontiers in cellular neuroscience · 2021Review
- Mutant prion proteins increase calcium permeability of AMPA receptors, exacerbating excitotoxicity.PLoS pathogens · 2020Article
- Melatonin regulates mitochondrial dynamics and alleviates neuron damage in prion diseases.Aging · 2020Article
- Analysis of RNA Expression Profiles Identifies Dysregulated Vesicle Trafficking Pathways in Creutzfeldt-Jakob Disease.Molecular neurobiology · 2019Article
- Protein Misfolding, Signaling Abnormalities and Altered Fast Axonal Transport: Implications for Alzheimer and Prion Diseases.Frontiers in cellular neuroscience · 2019Review
- Inhibition of IL-1β Signaling Normalizes NMDA-Dependent Neurotransmission and Reduces Seizure Susceptibility in a Mouse Model of Creutzfeldt-Jakob Disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Prion protein inhibits fast axonal transport through a mechanism involving casein kinase 2.PloS one · 2017Article
- Misfolding leads the way to unraveling signaling pathways in the pathophysiology of prion diseases.Prion · 2016Review
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- Prion Protein Modulates Monoaminergic Systems and Depressive-like Behavior in Mice.The Journal of biological chemistry · 2015Article
- The elusive role of the prion protein and the mechanism of toxicity in prion disease.PLoS pathogens · 2015Review
- Transgenic fatal familial insomnia mice indicate prion infectivity-independent mechanisms of pathogenesis and phenotypic expression of disease.PLoS pathogens · 2015Article
- Activation of Src family kinase ameliorates secretory trafficking in mutant prion protein cells.The Journal of biological chemistryArticle
- Disparity among neural injury models and the unfolded protein response.Journal of neurological disorders & strokeArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Synaptic dysfunction is an important cause of neurological symptoms in prion diseases, a class of clinically heterogeneous neurodegenerative disorders caused by misfolding of the cellular prion protein (PrP(C)). Experimental data suggest that accumulation of misfolded PrP(C) in the endoplasmic reticulum (ER) may be crucial in synaptic failure, possibly because of the activation of the translational repression pathway of the unfolded protein response. Here, we report that this pathway is not operative in mouse models of genetic prion disease, consistent with our previous observation that ER stress is not involved. Building on our recent finding that ER retention of mutant PrP(C) impairs the secretory trafficking of calcium channels essential for synaptic function, we propose a model of pathogenicity in which intracellular retention of misfolded PrP(C) results in loss of function or gain of toxicity of PrP(C)-interacting proteins. This neurotoxic modality may also explain the phenotypic heterogeneity of prion diseases.
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.