ReviewBBA advances2026
Hidden faces of alpha-synuclein: Cryo-EM revelation of fibril polymorphs driven by disease, mutations, and PTMs.
Review in BBA advances, 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
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
3 citing papers in PubMed.
- Reverse-engineering amyloid strains with generative protein design.bioRxiv : the preprint server for biology · 2026Article
- Distinct Molecular Mechanisms Underlie Modulation of Seeded α-Synuclein Aggregation and Toxicity by Salvianolic Acid B and Dihydromyricetin.International journal of molecular sciences · 2026Article
- Propagation of α-synuclein pathology: models, mechanisms and future goals.Molecular neurodegeneration advances · 2026Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Alpha-synuclein (α-Syn) is a neuronal protein implicated in the pathogenesis of several neurodegenerative disorders collectively known as synucleinopathies, including Parkinson's disease, dementia with Lewy bodies, and multiple system atrophy. This article provides a comprehensive overview of the structural characteristics of α-Syn, emphasizing its fibrillar aggregation and the resulting polymorphic fibril forms. Using advances in cryo-electron microscopy, a diverse range of α-Syn fibril polymorphs has been elucidated, both from
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Registered trials
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