ArticlePLoS genetics2013
Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans.
Article in PLoS genetics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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
41 citing papers in PubMed, 56 citations in OpenAlex.
- Differential proteostasis imbalance and the molecular basis of distinct synucleinopathies and tauopathies.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Form and function of actin impacts actin health and aging.iScience · 2026Article
- Brain rewired: Redox control of brain cell crosstalk via nanotubes and vesicles.Free radical biology & medicine · 2025Review
- A novelAutophagy · 2025Article
- Form and function of actin impacts actin health and aging.bioRxiv : the preprint server for biology · 2025Article
- Unraveling Molecular Targets for Neurodegenerative Diseases ThroughInternational journal of molecular sciences · 2025Review
- Increased mitochondrial CaFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023Article
- The cytoprotective sequestration activity of small heat shock proteins is evolutionarily conserved.The Journal of cell biology · 2022Article
- Stress increases in exopher-mediated neuronal extrusion require lipid biosynthesis, FGF, and EGF RAS/MAPK signaling.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Easy ultrastructural insight into the internal morphology of biological specimens by Atomic Force Microscopy.Scientific reports · 2021Article
- Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Quantitative Approaches for Scoring in vivo Neuronal Aggregate and Organelle Extrusion in Large Exopher Vesicles in C. elegans.Journal of visualized experiments : JoVE · 2020Article
- Review
- The HSP110/HSP70 disaggregation system generates spreading-competent toxic α-synuclein species.The EMBO journal · 2020Article
- Reducing INS-IGF1 signaling protects against non-cell autonomous vesicle rupture caused by SNCA spreading.Autophagy · 2020Article
- Article
- Prion Efficiently Replicates in α-Synuclein Knockout Mice.Molecular neurobiology · 2019Article
- Cellular clearance of circulating transthyretin decreases cell-nonautonomous proteotoxicity inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Quantitative Characterization of Metastability and Heterogeneity of Amyloid Aggregates.Biophysical journal · 2018Article
- Q&A: Trash talk: disposal and remote degradation of neuronal garbage.BMC biology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Prion proteins can adopt self-propagating alternative conformations that account for the infectious nature of transmissible spongiform encephalopathies (TSEs) and the epigenetic inheritance of certain traits in yeast. Recent evidence suggests a similar propagation of misfolded proteins in the spreading of pathology of neurodegenerative diseases including Alzheimer's or Parkinson's disease. Currently there is only a limited number of animal model systems available to study the mechanisms that underlie the cell-to-cell transmission of aggregation-prone proteins. Here, we have established a new metazoan model in Caenorhabditis elegans expressing the prion domain NM of the cytosolic yeast prion protein Sup35, in which aggregation and toxicity are dependent upon the length of oligopeptide repeats in the glutamine/asparagine (Q/N)-rich N-terminus. NM forms multiple classes of highly toxic aggregate species and co-localizes to autophagy-related vesicles that transport the prion domain from the site of expression to adjacent tissues. This is associated with a profound cell autonomous and cell non-autonomous disruption of mitochondrial integrity, embryonic and larval arrest, developmental delay, widespread tissue defects, and loss of organismal proteostasis. Our results reveal that the Sup35 prion domain exhibits prion-like properties when expressed in the multicellular organism C. elegans and adapts to different requirements for propagation that involve the autophagy-lysosome pathway to transmit cytosolic aggregation-prone proteins between tissues.
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.