ArticleEssays in biochemistry2022
Crossroads between copper ions and amyloid formation in Parkinson's disease.
Article in Essays in biochemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Copper Dyshomeostasis Affects α-Synuclein Clearance Mechanisms in Parkinson's Disease: Insights from In Vitro Models and Translational Evidence.International journal of molecular sciences · 2026Review
- Neuronal regulated cell death in aging-related neurodegenerative diseases: key pathways and therapeutic potentials.Neural regeneration research · 2025Article
- Cuproptosis and its potential role in musculoskeletal disease.Frontiers in cell and developmental biology · 2025Review
- Copper homeostasis and cuproptosis: implications for neurodegenerative diseases.Frontiers in aging neuroscience · 2025Review
- Cuproptosis, the novel type of oxidation-induced cell death in thoracic cancers: can it enhance the success of immunotherapy?Cell communication and signaling : CCS · 2024Review
- Primary Nucleation of Polymorphic α-Synuclein Dimers Depends on Copper Concentrations and Definite Copper-Binding Site.Biomolecules · 2024Article
- Copper ion incorporation in α-synuclein amyloids.Protein science : a publication of the Protein Society · 2024Article
- Copper binding and protein aggregation: a journey from the brain to the human lens.RSC chemical biology · 2023Article
- Chemical catalysis by biological amyloids.Biochemical Society transactions · 2023Article
- Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins.Molecules (Basel, Switzerland) · 2023Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Copper (Cu) ion dys-homeostasis and α-synclein amyloid deposits are two hallmarks of Parkinson's disease (PD). Here, I will discuss the connections between these features, with a major focus on the role of Cu in the α-synuclein (aS) amyloid formation process. The structurally disordered aS monomer can bind to both redox states of Cu (i.e., oxidized Cu(II) and reduced Cu(I)) with high affinity in vitro. Notably, the presence of Cu(II) (in absence of aS N-terminal acetylation) and Cu(I) (when in complex with the copper chaperone Atox1) modulate aS assembly into β-structured amyloids in opposite directions in vitro. Albeit the link to biological relevance is not fully unraveled, existing observations clearly emphasize the need for more knowledge on this interplay and its consequences to eventually combat destructive reactions that promote PD.
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