ReviewCurrent neuropharmacology2016
Modulating the Amyloidogenesis of α-Synuclein.
Review in Current neuropharmacology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT04250376 (The Use of Transcranial Focused Ultrasound for the Treatment of Neurodegenerative Dementias), which is not on this map. Cited by 6 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.
The Use of Transcranial Focused Ultrasound for the Treatment of Neurodegenerative Dementias
Who cites it
6 citing papers in PubMed.
- Nucleolar aggregation of key neuropathological proteins in the postmortem neurodegenerative brain.Acta neuropathologica · 2025Article
- Pelargonium graveolens Attenuates Rotenone-Induced Parkinson's Disease in a Rat Model: Role of MAO-B Inhibition and In Silico Study.Molecular neurobiology · 2025Article
- Polymorphic Alpha-Synuclein Oligomers: Characterization and Differential Detection with Novel Corresponding Antibodies.Molecular neurobiology · 2023Article
- Phytochemicals Bridging Autophagy Induction and Alpha-Synuclein Degradation in Parkinsonism.International journal of molecular sciences · 2019Review
- Natural polyphenols effects on protein aggregates in Alzheimer's and Parkinson's prion-like diseases.Neural regeneration research · 2018Review
- Plant Extracts and Phytochemicals TargetingFrontiers in pharmacology · 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
2 authors.
Funding
Abstract
Alpha-Synuclein is found in the neuronal cells but its native function is not well known. While α -synuclein is an intrinsically disordered protein that adopts a helical conformation upon membrane binding, numerous studies have shown that oligomeric β-forms of this protein are cytotoxic. This response to misfolded species contributes to Parkinson's Disease etiology and symptoms. The resulting amyloid fibrils are an established diagnostic in Parkinson's Disease. In this review, we focus on strategies that have been used to inhibit the amyloidogenesis of α -synuclein either by stabilizing the native state, or by redirecting the pathway to less toxic aggregates. Small molecules such as polyphenols, peptides as well as large proteins have proven effective at protecting cells against the cytotoxicity of α-synuclein. These strategies may lead to the development of therapeutic agents that could prove useful in combating this disease.
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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.