ArticleChemical science2026
Structural insights into copper and zinc binding to tau protein and the impact of metal binding on amyloid aggregation.
Article in Chemical science, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
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Who cites it
3 citing papers in PubMed.
- Metal Binding to Tau Protein: Physiological and Pathological Relevance.Biochemistry · 2026Review
- Zinc Differentially Modulates Tau Aggregation, Fibril Morphology, and Prion-like Seeding in a Construct-Dependent Manner.bioRxiv : the preprint server for biology · 2026Article
- Condensate State as Determinant of Amyloid Pathology in Neurodegeneration.Biomolecules · 2026Review
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tau protein is a microtubule-associated protein central to the pathogenesis of Alzheimer's disease (AD) and other tauopathies. While metal ion homeostasis is disrupted in AD, the presence of copper and zinc in neurofibrillary tangles suggests a pathological role for metal-tau interactions. In this study, the metal binding properties of Tau441 were probed using a wide range of spectroscopic tools. Specifically, electron paramagnetic resonance, circular dichroism, nuclear magnetic resonance (NMR) and X-ray absorption spectroscopy (XAS) results point to a single high-affinity Cu
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Registered trials
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