ArticleNeurochemical research2015
Stabilization of Alpha-Synuclein Oligomers In Vitro by the Neurotransmitters, Dopamine and Norepinephrine: The Effect of Oxidized Catecholamines.
Article in Neurochemical research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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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.
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Who cites it
6 citing papers in PubMed, 19 citations in OpenAlex.
- Machine learning-assisted screening of small-molecule drugs for suppressing protein aggregation and ROS generation based on ECL and CV dual-mode signals amplified by DNA.Chemical science · 2026Article
- A Focus on the Link Between Metal Dyshomeostasis, Norepinephrine, and Protein Aggregation.Antioxidants (Basel, Switzerland) · 2025Review
- Modulation of cytotoxic amyloid fibrillation and mitochondrial damage of α-synuclein by catechols mediated conformational changes.Scientific reports · 2023Article
- Impaired Phasic Discharge of Locus Coeruleus Neurons Based on Persistent High Tonic Discharge-A New Hypothesis With Potential Implications for Neurodegenerative Diseases.Frontiers in neurology · 2020Article
- Enhanced mitochondrial inhibition by 3,4-dihydroxyphenyl-acetaldehyde (DOPAL)-oligomerized α-synuclein.Journal of neuroscience research · 2019Article
- A hyperbranched dopamine-containing PEG-based polymer for the inhibition of α-synuclein fibrillation.Biochemical and biophysical research communications · 2016Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aggregation of the protein alpha-synuclein has been identified in the pathogenesis of Parkinson's disease and is initiated by the folding of the protein monomer into an amyloid form of insoluble fibrils. The neurotransmitters dopamine and norepinephrine have been shown to both inhibit the formation of these fibrils and disaggregate existing fibrils, yielding the more toxic oligomeric form of α-synuclein. This study characterizes the stable oligomers formed through the aggregation and disaggregation processes in the presence of these catecholamines, and suggests differences in oligomer formation depending on the extent of oxidation of the neurotransmitter at the time of oligomerization. Unique oligomers are also stabilized, likely formed from the aggregation of monomeric α-synuclein and a proteolytic fragment of α-synuclein; however, proteolytic fragments do not form as readily in the presence of these neurotransmitters. These findings suggest novel pathways for the formation of α-synuclein oligomers in the presence of neurotransmitters, particularly oxidized forms.
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