ReviewInternational journal of cell biology2013
Prions Ex Vivo: What Cell Culture Models Tell Us about Infectious Proteins.
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 15 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed.
- A Neuronal Cell Line Model for Studying Camel Prions.Pathogens (Basel, Switzerland) · 2026Article
- Enhanced lysosomal activity prevents infection with PrPThe Journal of biological chemistry · 2026Article
- Effect of incineration, co-incineration and combustion on TSE hazards in category 1 animal by-products.EFSA journal. European Food Safety Authority · 2025Article
- Propagation and Dissemination Strategies of Transmissible Spongiform Encephalopathy Agents in Mammalian Cells.International journal of molecular sciences · 2022Review
- Invited Review: The role of prion-like mechanisms in neurodegenerative diseases.Neuropathology and applied neurobiology · 2020Review
- An astrocyte cell line that differentially propagates murine prions.The Journal of biological chemistry · 2020Article
- Prion infection, transmission, and cytopathology modeled in a low-biohazard human cell line.Life science alliance · 2020Article
- Evaluation of an alternative method for production of biodiesel from processed fats derived from Category 1, 2 and 3 animal by-products (submitted by College Proteins).EFSA journal. European Food Safety Authority · 2020Article
- Entropic Bristles Tune the Seeding Efficiency of Prion-Nucleating Fragments.Cell reports · 2020Article
- Prion Replication in the Mammalian Cytosol: Functional Regions within a Prion Domain Driving Induction, Propagation, and Inheritance.Molecular and cellular biology · 2018Article
- Cellular mechanisms responsible for cell-to-cell spreading of prions.Cellular and molecular life sciences : CMLS · 2018Review
- Recombinant PrP and Its Contribution to Research on Transmissible Spongiform Encephalopathies.Pathogens (Basel, Switzerland) · 2017Review
- The relevance of contact-independent cell-to-cell transfer of TDP-43 and SOD1 in amyotrophic lateral sclerosis.Biochimica et biophysica acta. Molecular basis of disease · 2017Review
- Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.PLoS genetics · 2016Article
- Neurodegenerative diseases: expanding the prion concept.Annual review of neuroscience · 2015Review
Corrections and comments
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prions are unconventional infectious agents that are composed of misfolded aggregated prion protein. Prions replicate their conformation by template-assisted conversion of the endogenous prion protein PrP. Templated conversion of soluble proteins into protein aggregates is also a hallmark of other neurodegenerative diseases. Alzheimer's disease or Parkinson's disease are not considered infectious diseases, although aggregate pathology appears to progress in a stereotypical fashion reminiscent of the spreading behavior ofmammalian prions. While basic principles of prion formation have been studied extensively, it is still unclear what exactly drives PrP molecules into an infectious, self-templating conformation. In this review, we discuss crucial steps in the life cycle of prions that have been revealed in ex vivo models. Importantly, the persistent propagation of prions in mitotically active cells argues that cellular processes are in place that not only allow recruitment of cellular PrP into growing prion aggregates but also enable the multiplication of infectious seeds that are transmitted to daughter cells. Comparison of prions with other protein aggregates demonstrates that not all the characteristics of prions are equally shared by prion-like aggregates. Future experiments may reveal to which extent aggregation-prone proteins associated with other neurodegenerative diseases can copy the replication strategies of prions.
Identifiers
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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.