ArticleACS chemical neuroscience2025
Divalent and Trivalent Metallic Ions Differentially Affect Alpha-Synuclein Aggregation.
Article in ACS chemical neuroscience, 2025. 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.
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Who cites it
3 citing papers in PubMed.
- Divergent effects of pathological α-synuclein truncations and mutations on phase separation.Nature communications · 2026Article
- Condensate State as Determinant of Amyloid Pathology in Neurodegeneration.Biomolecules · 2026Review
- Comparative Analysis of Aggregation of β- and γ-Synucleins in Vertebrates.Biomolecules · 2025Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alpha-synuclein (αSyn) is the constituent protein associated with neurodegenerative synucleinopathies such as Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. Recent studies have highlighted the potential role of altered metal ion homeostasis in influencing the aggregation and pathological behavior of αSyn, thereby affecting disease progression. We examined αSyn aggregation propensity in the presence of calcium (Ca
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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 Socratic graph.