ArticleEuropean journal of inorganic chemistry2018
Cu(II) binding to various forms of amyloid-β peptides. Are they friends or foes?
Article in European journal of inorganic chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 48 citations in OpenAlex.
- Oxidative stress and inflammation in neurodegenerative disorders.Archives of toxicology · 2026Review
- 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
- Black phosphorus in theragenerative medicine: a multi-organ perspective on disease modulation and tissue repair.Bioactive materials · 2026Review
- Evaluation of a New Methylimidazole-Containing Thiosemicarbazone as a CuChemistry (Weinheim an der Bergstrasse, Germany) · 2026Article
- Redox reactivities of membrane-bound amyloid-β-Cu complexes and their targeting by metallothionein-3.Free radical biology & medicine · 2025Article
- Exploiting SpyTag/SpyCatcher Technology to Design New Artificial Catalytic Copper Proteins.Chembiochem : a European journal of chemical biology · 2025Article
- Multi-target-directed therapeutic strategies for Alzheimer's disease: controlling amyloid-β aggregation, metal ion homeostasis, and enzyme inhibition.Chemical science · 2025Review
- Tuning multispectral fluorescence quantum dot-based identification of short-length amyloid β peptides by applying Cu(II) ions.Mikrochimica acta · 2024Article
- Unveiling the Effects of Copper Ions in the Aggregation of Amyloidogenic Proteins.Molecules (Basel, Switzerland) · 2023Review
- Decoding the Roles of Amyloid-β (1-42)'s Key Oligomerization Domains toward Designing Epitope-Specific Aggregation Inhibitors.JACS Au · 2023Article
- Why the Ala-His-His Peptide Is an Appropriate Scaffold to Remove and Redox Silence Copper Ions from the Alzheimer's-Related Aβ Peptide.Biomolecules · 2022Article
- Amyloid β structural polymorphism, associated toxicity and therapeutic strategies.Cellular and molecular life sciences : CMLS · 2021Review
- Reassembling protein complexes after controlled disassembly by top-down mass spectrometry in native mode.International journal of mass spectrometry · 2021Article
- A catalytic antioxidant for limiting amyloid-beta peptide aggregation and reactive oxygen species generation.Chemical science · 2019Article
- Cu and Zn coordination to amyloid peptides: From fascinating chemistry to debated pathological relevance.Coordination chemistry reviews · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In the present micro-review, we describe the Cu(II) binding to several forms of amyloid-β peptides, the peptides involved in Alzheimer's disease. It has indeed been shown that in addition to the "full-length" peptide originating from the precursor protein after cleavage at position 1, several other shorter peptides do exist in large proportion and may be involved in the disease as well. Cu(II) binding to amyloid-β peptides is one of the key interactions that impact both the aggregating properties of the amyloid peptides and the Reactive Oxygen Species (ROS) production, two events linked to the etiology of the disease. Binding sites and affinity are described in correlation with Cu(II) induced ROS formation and Cu(II) altered aggregation, for amyloid peptides starting at position 1, 3, 4, 11 and for the corresponding pyroglutamate forms when they could be obtained (i.e. for peptides cleaved at positions 3 and 11). It appears that the current paradigm which points out a toxic role of the Cu(II) - amyloid-β interaction might well be shifted towards a possible protective role when the peptides considered are the N-terminally truncated ones.
Identifiers
What OpenQuestion holds
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.