ReviewChemical Society reviews2017
Chemistry of mammalian metallothioneins and their interaction with amyloidogenic peptides and proteins.
Review in Chemical Society reviews, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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.
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Who cites it
29 citing papers in PubMed, 75 citations in OpenAlex.
- A Covalent Resveratrol-Polyoxometalate Hybrid for Synergistic Disassembly of Prion Protein Fragment 106-126 Aggregates and Catalytic Scavenging of Reactive Oxygen Species.Small (Weinheim an der Bergstrasse, Germany) · 2026Article
- Cuproptosis in Sepsis: Cell Type-Specific Mechanisms and Clinical Prospects.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
- Article
- Tau Liquid-Liquid Phase Separation in Alzheimer's Disease: Mechanisms, Pathogenesis, and Therapeutic Implications.Molecular neurobiology · 2025Review
- Emerging Roles of Metallothioneins in Human Pathophysiology: A Review.Health science reports · 2025Article
- Copper homeostasis and cuproptosis: implications for neurodegenerative diseases.Frontiers in aging neuroscience · 2025Review
- Metallothioneins in the Pathogenesis of Liver Diseases: A Review.International journal of hepatology · 2025Review
- Mixed-ligand copper(ii)-diimine complexes of 3-formylchromone-RSC advances · 2024Article
- Cellular zinc metabolism and zinc signaling: from biological functions to diseases and therapeutic targets.Signal transduction and targeted therapy · 2024Review
- Structural Characterization of Cu(I)/Zn(II)-metallothionein-3 by Ion Mobility Mass Spectrometry and Top-Down Mass Spectrometry.Analytical chemistry · 2023Article
- Article
- From Small Peptides to Large Proteins against Alzheimer'sDisease.Biomolecules · 2022Review
- 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
- Azepine-Indole Alkaloids FromFrontiers in neuroscience · 2022Article
- Machine learning-based characterization of cuprotosis-related biomarkers and immune infiltration in Parkinson's disease.Frontiers in genetics · 2022Article
- Advances in aptamers against Aβ and applications in Aβ detection and regulation for Alzheimer's disease.Theranostics · 2022Review
- Highly Dynamic Polynuclear Metal Cluster Revealed in a Single Metallothionein Molecule.Research (Washington, D.C.) · 2021Article
- Response of Cytoprotective and Detoxifying Proteins to Vanadate and/or Magnesium in the Rat Liver: The Nrf2-Keap1 System.Oxidative medicine and cellular longevity · 2021Article
Corrections and comments
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Authors and funding
6 authors at 5 institutions in 4 countries.
Funding
Abstract
Cu and Zn ions are essential in most living beings. Their metabolism is critical for health and mis-metabolism can be lethal. In the last two decades, a large body of evidence has reported the role of copper, zinc and iron, and oxidative stress in several neurodegenerative diseases like Alzheimer's, Parkinson's, prion diseases, etc. To what extent this mis-metabolism is causative or a consequence of these diseases is still a matter of research. In this context metallothioneins (MTs) appear to play a central gate-keeper role in controlling aberrant metal-protein interactions. MTs are small proteins that can bind high amounts of Zn(ii) and Cu(i) ions in metal-cluster arrangements via their cysteine thiolates. Moreover, MTs are well known antioxidants. The present tutorial outlines the chemistry underlying the interconnection between copper(i/ii) and zinc(ii) coordination to amyloidogenic proteins and MTs, and their redox properties in generation and/or silencing reactive oxygen species (overproduced in oxidative stress) and other reactants. These studies have revealed the coordination chemistry involved in neurodegenerative diseases and the interactions between MTs and amyloidogenic protein metal-complexes (like amyloid-β, α-synuclein and prion-protein). Overall, the protective role of MTs in neurodegenerative processes is emerging, serving as a foundation for exploring MT chemistry as inspiration for therapeutic approaches.
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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.