ArticleStructure (London, England : 1993)2026
The amyloid packing difference: A pairwise comparison metric for amyloid structures.
Article in Structure (London, England : 1993), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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
4 citing papers in PubMed.
- Article
- The Pick fold in tau filaments from human MAPT mutants.Acta neuropathologica · 2026Article
- Transthyretin amyloid fibrils adopt distinct folds in the brain.bioRxiv : the preprint server for biology · 2026Article
- Reverse-engineering amyloid strains with generative protein design.bioRxiv : the preprint server for biology · 2026Article
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Abstract
Because a given protein may adopt different amyloid protofilament folds, it has become necessary to compare pairs of amyloid structures of a given protein. This article describes the amyloid packing difference (APD), which quantifies the difference between amyloid structures as the percentage of residues involved in unique cross-β packing interactions or side-chain orientations. Clustering of α-synuclein folds on APD values recapitulates clustering based on structural superpositions. Known protofilament folds of the prion protein, tau, α-synuclein, TDP-43, or TAF15 from different neurodegenerative diseases have APD values above 20%, whereas structures that have been associated with the same disease have APD values below 40%. Different individuals with peripheral amyloidosis have antibody light-chain structures with APDs above 60%, whereas transthyretin filaments are strikingly similar, with APDs below 25%. These observations provide context for the interpretation of APD values in future structure comparisons.
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