ArticleScientific reports2024
Metal-binding amino acid ligands commonly found in metalloproteins differentially fractionate copper isotopes.
Article in Scientific reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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Who cites it
9 citing papers in PubMed, 14 citations in OpenAlex.
- Metal coordination at biological interfaces: Mechanisms, therapeutics, and translation.Materials today. Bio · 2026Review
- Toward diagnostically relevant isotope-ratio biomarkers: what does MC-ICP-MS still need for standardized measurements?Analytical and bioanalytical chemistry · 2026Review
- Elemental and Isotopic Profiles in Blood and Urine of Jordanian Children with Autism Spectrum Disorder: a Preliminary Comparative Study with Neurotypical Children.Biological trace element research · 2026Article
- Article
- Review
- Amino Acid Complexation Fractionates Nickel Isotopes: Implications for Tracing Nickel Cycling in the Environment.Environmental science & technology letters · 2025Article
- Desert dust improves the photophysiology of heat-stressed corals beyond iron.Scientific reports · 2024Article
- Stable potassium isotope ratios in human blood serum towards biomarker development in Alzheimer's disease.Metallomics : integrated biometal science · 2024Article
- Copper isotope shifts in biofluids track Alzheimer's pathology.Alzheimer's & dementia (Amsterdam, Netherlands)Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Copper (Cu) is a cofactor in numerous key proteins and, thus, an essential element for life. In biological systems, Cu isotope abundances shift with metabolic and homeostatic state. However, the mechanisms underpinning these isotopic shifts remain poorly understood, hampering use of Cu isotopes as biomarkers. Computational predictions suggest that isotope fractionation occurs when proteins bind Cu, with the magnitude of this effect dependent on the identity and arrangement of the coordinating amino acids. This study sought to constrain equilibrium isotope fractionation values for Cu bound by common amino acids at protein metal-binding sites. Free and bound metal ions were separated via Donnan dialysis using a cation-permeable membrane. Isotope ratios of pre- and post-dialysis solutions were measured by MC-ICP-MS following purification. Sulfur ligands (cysteine) preferentially bound the light isotope (
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Registered trials
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