ArticleNature communications2025
Structure of ATTRv-F64S fibrils isolated from skin tissue of a living patient.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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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
1 citing paper in PubMed.
- Cryo-EM structures of biopsy-derived TTR fibrils in hereditary transthyretin amyloidosis.Nature communications · 2026Article
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Authors and funding
8 authors.
Funding
Abstract
Amyloid transthyretin-derived (ATTR) amyloidosis is a degenerative, systemic disease characterized by transthyretin fibril deposition in organs like the heart, kidneys, liver, and skin. In this study, we report the cryo-EM structure of transthyretin fibrils isolated from skin tissue of a living patient carrying a rare genetic mutation (ATTRv F64S). The structure adopts a highly conserved fold previously observed in other ATTR fibrils from various tissues or different genetic variants. Mass spectrometry was used to evaluate fibril content and to identify common post-translational modifications. The structural consistency between ATTR filaments from different tissues or patients validates non-invasive skin biopsy as a diagnostic tool.
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