ArticleFree radical biology & medicine2020
Membrane insertion exacerbates the α-Synuclein-Cu(II) dopamine oxidase activity: Metallothionein-3 targets and silences all α-synuclein-Cu(II) complexes.
Article in Free radical biology & medicine, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- Disease-specific tau polymorphs are associated with unique protein networks across proteinopathies.The EMBO journal · 2026Article
- Copper Homeostasis and Cuproptosis in Neurological Disorders.Drug design, development and therapy · 2026Review
- Redox reactivities of membrane-bound amyloid-β-Cu complexes and their targeting by metallothionein-3.Free radical biology & medicine · 2025Article
- Oxidative pathways of apo, partially, and fully Zn(II)- and Cd(II)-metalated human metallothionein-3 are dominated by disulfide bond formation.The FEBS journal · 2025Article
- Copper homeostasis and cuproptosis: implications for neurodegenerative diseases.Frontiers in aging neuroscience · 2025Review
- Metallothionein: A Comprehensive Review of Its Classification, Structure, Biological Functions, and Applications.Antioxidants (Basel, Switzerland) · 2024Review
- Arsenic binding to human metallothionein-3.Chemical science · 2023Article
- Multifunctional Metallothioneins as a Target for Neuroprotection in Parkinson's Disease.Antioxidants (Basel, Switzerland) · 2023Review
- Article
- Metal binding and interdomain thermodynamics of mammalian metallothionein-3: enthalpically favoured CuChemical science · 2022Article
- Evidence for a Long-Lived, Cu-Coupled and Oxygen-Inert Disulfide Radical Anion in the Assembly of Metallothionein-3 Cu(I)Journal of the American Chemical Society · 2022Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Copper binding to α-synuclein (α-Syn), the major component of intracellular Lewy body inclusions in substantia nigra dopaminergic neurons, potentiate its toxic redox-reactivity and plays a detrimental role in the etiology of Parkinson disease (PD). Soluble α-synuclein-Cu(II) complexes possess dopamine oxidase activity and catalyze ROS production in the presence of biological reducing agents via Cu(II)/Cu(I) redox cycling. These metal-centered redox reactivities harmfully promote the oxidation and oligomerization of α-Syn. While this chemistry has been investigated on recombinantly expressed soluble α-Syn, in vivo, α-Syn is acetylated at its N-terminus and is present in equilibrium between soluble and membrane-bound forms. This post-translational modification and membrane-binding alter the Cu(II) coordination environment and binding modes and are expected to affect the α-Syn-Cu(II) reactivity. In this work, we first investigated the reactivity of acetylated and membrane-bound complexes, and subsequently addressed whether the brain metalloprotein Zn
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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.