ArticleStructure (London, England : 1993)2025
Automated fibril structure calculations in Xplor-NIH.
Article in Structure (London, England : 1993), 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.
- In Vitro-Prepared A30P Alpha-Synuclein Fibrils Adopt the Conserved and Disease-Relevant Greek Key Fold.The journal of physical chemistry. B · 2026Article
- Protonated Structure of EmrE Reveals C-terminal Tail Gating Mechanism.bioRxiv : the preprint server for biology · 2026Article
- Article
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Authors and funding
7 authors.
Funding
Abstract
Amyloid fibrils are protein assemblies that are pathologically linked to neurodegenerative diseases. Fibril structures can aid development of highly specific ligands for diagnostic imaging and therapeutics. Solid-state NMR (SSNMR) is a viable approach to solving fibril structures; however, most SSNMR protocols require manual analysis of extensive spectral data, presenting a major bottleneck to determining structures. Standard automation; routines fall short for symmetric multimeric assemblies like amyloids due to high cross peak degeneracy and the need to account for multiple protein subunits. Here, we employ the probabilistic assignment for structure determination protocol in conjunction with strict; symmetry in Xplor-NIH structure determination software, demonstrating the methodology using data from a previous structure of an α-synuclein (Asyn) fibril implicated in Parkinson disease. The automated protocol generated a structure of comparable, if not superior, quality in a few days of computational time, reducing the manual effort required; to solve amyloid structures by SSNMR.
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Registered trials
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