ArticleJournal of neuropathology and experimental neurology2015
Transmission of Soluble and Insoluble α-Synuclein to Mice.
Article in Journal of neuropathology and experimental neurology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
18 citing papers in PubMed, 27 citations in OpenAlex.
- Safety and Tolerability of Multiple Ascending Doses of PRX002/RG7935, an Anti-α-Synuclein Monoclonal Antibody, in Patients With Parkinson Disease: A Randomized Clinical Trial.JAMA neurology · 2018Trial
- Imaging nanoscopic co-assemblies of α-synuclein and Tau in human samples.Nature communications · 2026Article
- Advancements in Genetic and Biochemical Insights: Unraveling the Etiopathogenesis of Neurodegeneration in Parkinson's Disease.Biomolecules · 2024Review
- Advanced human iPSC-based preclinical model for Parkinson's disease with optogenetic alpha-synuclein aggregation.Cell stem cell · 2023Article
- Intrastriatal injection of Parkinson's disease intestine and vagus lysates initiates α-synucleinopathy in rat brain.Cell death & disease · 2023Article
- Prion-like properties of the mutant huntingtin protein in living organisms: the evidence and the relevance.Molecular psychiatry · 2022Review
- Decreased AQP4 Expression Aggravates ɑ-Synuclein Pathology in Parkinson's Disease Mice, Possibly via Impaired Glymphatic Clearance.Journal of molecular neuroscience : MN · 2021Article
- Autonomic ganglionic injection of α-synuclein fibrils as a model of pure autonomic failure α-synucleinopathy.Nature communications · 2020Article
- FGF2 Affects Parkinson's Disease-Associated Molecular Networks Through Exosomal Rab8b/Rab31.Frontiers in genetics · 2020Article
- LRRK2 Kinase Inhibition Rescues Deficits in Lysosome Function Due to HeterozygousFrontiers in neuroscience · 2020Article
- Absence of Uptake and Prion-Like Spreading of Alpha-Synuclein and Tau After Intravitreal Injection of Preformed Fibrils.Frontiers in aging neuroscience · 2020Article
- Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved.Frontiers in molecular neuroscience · 2019Review
- Alpha-synuclein overexpression in the olfactory bulb initiates prodromal symptoms and pathology of Parkinson's disease.Translational neurodegeneration · 2018Article
- Neurodegenerative Disease Transmission and Transgenesis in Mice.Cold Spring Harbor perspectives in biology · 2017Review
- Brain-derived exosomes from dementia with Lewy bodies propagate α-synuclein pathology.Acta neuropathologica communications · 2017Article
- Calcium and Parkinson's disease.Biochemical and biophysical research communications · 2017Review
- Anti-α-synuclein immunotherapy reduces α-synuclein propagation in the axon and degeneration in a combined viral vector and transgenic model of synucleinopathy.Acta neuropathologica communications · 2017Article
- Transmission of α-synucleinopathy from olfactory structures deep into the temporal lobe.Molecular neurodegeneration · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
The neurodegenerative synucleinopathies, which include Parkinson disease, multiple-system atrophy, and Lewy body disease, are characterized by the presence of abundant neuronal inclusions called Lewy bodies and Lewy neurites. These disorders remain incurable, and a greater understanding of the pathologic processes is needed for effective treatment strategies to be developed. Recent data suggest that pathogenic misfolding of the presynaptic protein, α-synuclein (α-syn), and subsequent aggregation and accumulation are fundamental to the disease process. It is hypothesized that the misfolded isoform is able to induce misfolding of normal endogenous α-syn, much like what occurs in the prion diseases. Recent work highlighting the seeding effect of pathogenic α-syn has largely focused on the detergent-insoluble species of the protein. In this study, we performed intracerebral inoculations of the sarkosyl-insoluble or sarkosyl-soluble fractions of human Lewy body disease brain homogenate and show that both fractions induce CNS pathology in mice at 4 months after injection. Disease-associated deposits accumulated both near and distal to the site of the injection, suggesting a cell-to-cell spread via recruitment of α-syn. These results provide further insight into the prion-like mechanisms of α-syn and suggest that disease-associated α-syn is not homogeneous within a single patient but might exist in both soluble and insoluble isoforms.
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.