ArticleProtein science : a publication of the Protein Society2014
Dopamine-induced α-synuclein oligomers show self- and cross-propagation properties.
Article in Protein science : a publication of the Protein Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 38 citations in OpenAlex.
- Facile generation of drug-like conformational antibodies specific for amyloid fibrils.Nature chemical biology · 2025Article
- Association betweenFrontiers in aging neuroscience · 2022Article
- αS Oligomers Generated from Interactions with a Polyunsaturated Fatty Acid and a Dopamine Metabolite Differentially Interact with Aβ to Enhance Neurotoxicity.ACS chemical neuroscience · 2021Article
- Prion-like C-Terminal Domain of TDP-43 and α-Synuclein Interact Synergistically to Generate Neurotoxic Hybrid Fibrils.Journal of molecular biology · 2021Article
- The contribution of Parkin, PINK1 and DJ-1 genes to selective neuronal degeneration in Parkinson's disease.The European journal of neuroscience · 2020Review
- Polymorphic α-Synuclein Strains Modified by Dopamine and Docosahexaenoic Acid Interact Differentially with Tau Protein.Molecular neurobiology · 2020Article
- Soluble tau aggregates, not large fibrils, are the toxic species that display seeding and cross-seeding behavior.Protein science : a publication of the Protein Society · 2018Article
- Disruption of Inferior Longitudinal Fasciculus Microstructure in Parkinson's Disease: A Systematic Review of Diffusion Tensor Imaging Studies.Frontiers in neurology · 2018Review
- High-Throughput Screening Methodology to Identify Alpha-Synuclein Aggregation Inhibitors.International journal of molecular sciences · 2017Article
- Site-Specific Fluorescence Polarization for Studying the Disaggregation of α-Synuclein Fibrils by Small Molecules.Biochemistry · 2017Article
- Acidic CaMessenger (Los Angeles, Calif. : Print) · 2016Article
- Structural and functional properties of prefibrillar α-synuclein oligomers.Scientific reports · 2016Article
- A hyperbranched dopamine-containing PEG-based polymer for the inhibition of α-synuclein fibrillation.Biochemical and biophysical research communications · 2016Article
- Manganese-induced Neurotoxicity: FromToxicology research · 2015Article
- Extracellular ATP induces intracellular alpha-synuclein accumulation via P2X1 receptor-mediated lysosomal dysfunction.Neurobiology of aging · 2015Article
- The N-terminal residues 43 to 60 form the interface for dopamine mediated α-synuclein dimerisation.PloS one · 2015Article
- Is Parkinson's disease truly a prion-like disorder? An appraisal of current evidence.Neurology research international · 2015Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Amyloid aggregates of α-synuclein (αS) protein are the predominant species present within the intracellular inclusions called Lewy bodies in Parkinson's disease (PD) patients. Among various aggregates, the low-molecular weight ones broadly ranging between 2 and 30 mers are known to be the primary neurotoxic agents responsible for the impairment of neuronal function. Recent research has indicated that the neurotransmitter dopamine (DA) is one of the key physiological agents promoting and augmenting αS aggregation, which is thought to be a significant event in PD pathologenesis. Specifically, DA is known to induce the formation of soluble oligomers of αS, which in turn are responsible for inducing several important cellular changes leading to cellular toxicity. In this report, we present the generation, isolation, and biophysical characterization of five different dopamine-derived αS oligomers (DSOs) ranging between 3 and 15 mers, corroborating previously published reports. More importantly, we establish that these DSOs are also capable of replication by self-propagation, which leads to the replication of DSOs upon interaction with αS monomers, a process similar to that observed in mammilian prions. In addition, DSOs are also able to cross-propagate amyloid-β (Aβ) aggregates involved in Alzheimer's disease (AD). Interestingly, while self-propagation of DSOs occur with no net gain in protein structure, cross-propagation proceeds with an overall gain in β-sheet conformation. These results implicate the involvement of DSOs in the progression of PD, and, in part, provide a molecular basis for the observed co-existence of AD-like pathology among PD patients.
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Registered trials
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