ReviewPrion
Prion-like propagation of cytosolic protein aggregates: insights from cell culture models.
Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 48 citations in OpenAlex.
- Internalized components of membrane attack complexes disrupt proteostasis and acquire alarmin-like properties.Nature communications · 2026Article
- Internalized Components of Membrane Attack Complexes Disrupt Proteostasis and Acquire Alarmin-Like Properties.bioRxiv : the preprint server for biology · 2026Article
- Energetic profiling reveals thermodynamic principles underlying amyloid fibril maturation.Nature communications · 2025Article
- Rational Modulation of Liquid-Liquid Phase Separation Offers Novel Ways to Combat Tauopathies.International journal of molecular sciences · 2025Review
- Membrane composition and lipid to protein ratio modulate amyloid kinetics of yeast prion protein.RSC chemical biology · 2021Article
- The HSP110/HSP70 disaggregation system generates spreading-competent toxic α-synuclein species.The EMBO journal · 2020Article
- Entropy-Based Strategies for Rapid Pre-Processing and Classification of Time Series Data from Single-Molecule Force Experiments.Entropy (Basel, Switzerland) · 2020Article
- Tau Fibril Formation in Cultured Cells Compatible with a Mouse Model of Tauopathy.International journal of molecular sciences · 2018Article
- Insights into Mechanisms of Chronic Neurodegeneration.International journal of molecular sciences · 2016Review
- Protein Transmission, Seeding and Degradation: Key Steps for α-Synuclein Prion-Like Propagation.Experimental neurobiology · 2014Review
- Caenorhabditis elegans as a model system for studying non-cell-autonomous mechanisms in protein-misfolding diseases.Disease models & mechanisms · 2014Review
- Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans.PLoS genetics · 2013Article
- Cellular aspects of prion replication in vitro.Viruses · 2013Review
- The emerging science of BMAA: do cyanobacteria contribute to neurodegenerative disease?Environmental health perspectives · 2012Article
- Dynamic reorganization of metabolic enzymes into intracellular bodies.Annual review of cell and developmental biology · 2012Review
- Multifaceted roles of tunneling nanotubes in intercellular communication.Frontiers in physiology · 2012Article
- A deadly spread: cellular mechanisms of α-synuclein transfer.Cell death and differentiation · 2011Review
- Prion-like propagation of mutant superoxide dismutase-1 misfolding in neuronal cells.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Human Tau isoforms assemble into ribbon-like fibrils that display polymorphic structure and stability.The Journal of biological chemistry · 2010Article
- Review
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
No grant is acknowledged in the PubMed record.
Abstract
Amyloid formation is a hallmark of several systemic and neurodegenerative diseases. Extracellular amyloid deposits or intracellular inclusions arise from the conformational transition of normally soluble proteins into highly ordered fibrillar aggregates. Amyloid fibrils are formed by nucleated polymerization, a process also shared by prions, proteinaceous infectious agents identified in mammals and fungi. Unlike so called non-infectious amyloids, the aggregation phenotype of prion proteins can be efficiently transmitted between cells and organisms. Recent discoveries in vivo now implicate that even disease-associated intracellular protein aggregates consisting of alpha-synuclein or Tau have the capacity to seed aggregation of homotypic native proteins and might propagate their amyloid states in a prion-like manner. Studies in tissue culture demonstrate that aggregation of diverse intracellular amyloidogenic proteins can be induced by exogenous fibrillar seeds. Still, a prerequisite for prion-like propagation is the fragmentation of proteinaceous aggregates into smaller seeds that can be transmitted to daughter cells. So far efficient propagation of the aggregation phenotype in the absence of exogenous seeds was only observed for a yeast prion domain expressed in tissue culture. Intrinsic properties of amyloidogenic protein aggregates and a suitable host environment likely determine if a protein polymer can propagate in a prion-like manner in the mammalian cytosol.
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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.