ReviewPrion2016
Protein aggregates stimulate macropinocytosis facilitating their propagation.
Review in Prion, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed.
- Membrane Ruffles: Composition, Function, Formation and Visualization.International journal of molecular sciences · 2024Review
- Cell-Penetrating Chaperone Nuc1 for Small- and Large-Molecule Delivery Into Retinal Cells and Tissues.Investigative ophthalmology & visual science · 2024Article
- Macropinocytosis as a potential mechanism driving neurotropism ofFrontiers in cellular and infection microbiology · 2023Review
- Six genetically linked mutations in the CD36 gene significantly delay the onset of Alzheimer's disease.Scientific reports · 2022Article
- Prionoids in amyotrophic lateral sclerosis.Brain communications · 2022Review
- Loss of MAPK8IP3 Affects Endocytosis in Neurons.Frontiers in cellular neuroscience · 2022Article
- Article
- Prospects on the nano-plastic particles internalization and induction of cellular response in human keratinocytes.Particle and fibre toxicology · 2021Article
- Visualizing Membrane Ruffle Formation using Scanning Electron Microscopy.Journal of visualized experiments : JoVE · 2021Article
- Proteostatic imbalance and protein spreading in amyotrophic lateral sclerosis.The EMBO journal · 2021Review
- Article
- Reovirus uses macropinocytosis-mediated entry and fast axonal transport to infect neurons.PLoS pathogens · 2020Article
- Self-triggered click reaction in an Alzheimer's disease model:Chemical science · 2019Article
- Crossing the blood-brain-barrier with nanoligand drug carriers self-assembled from a phage display peptide.Nature communications · 2019Article
- Prion-like protein aggregates exploit the RHO GTPase to cofilin-1 signaling pathway to enter cells.The EMBO journal · 2018Article
- Article
- Enhanced neuroinvasion by smaller, soluble prions.Acta neuropathologica communications · 2017Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Temporal and spatial patterns of pathological changes such as loss of neurons and presence of pathological protein aggregates are characteristic of neurodegenerative diseases such as Amyotrophic Lateral Sclerosis, Frontotemporal Dementia, Alzheimer's disease and Parkinson's disease. These patterns are consistent with the propagation of protein misfolding and aggregation reminiscent of the prion diseases. There is a surge of evidence that suggests that large protein aggregates of a range of proteins are able to enter cells via macropinocytosis. Our recent work suggests that this process is activated by the binding of aggregates to the neuron cell surface. The current review considers the potential role of cell surface receptors in the triggering of macropinocytosis by protein aggregates and the possibility of utilizing macropinocytosis pathways as a therapeutic target.
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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.