ArticleGenome biology and evolution2025
Piecing Together the History of Protein Folds From a Fragmented Evolutionary Record.
Article in Genome biology and evolution, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- TEDLH: domain HMMs for sensitive detection of remote homologues.Bioinformatics (Oxford, England) · 2026Article
- Antimicrobial peptides: emerging next-generation strategy for sustainable plant disease management.Frontiers in antibiotics · 2026Review
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1 author.
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Abstract
Protein folds are structural units defined by the number, type, arrangement, and orientation of their core secondary structural elements. The universe of protein folds is highly interconnected. Local sequence similarities, referred to as sequence motifs, link structurally distinct folds. Sequence and structure motifs reveal deep evolutionary relationships that can help us understand the evolutionary mechanisms shaping protein structures over time. This work analyses structural divergence in folds that contain the β-hammerhead motif. Sequence and structure-based analyses reveal deep evolutionary relationships between 3-fold superfamilies: Beta Barrel (CATH superfamily 2.40.50.100); Distorted Sandwich (CATH superfamily 2.70.70.100); and Alpha-Beta Complex (CATH superfamily 3.90.1170.30). The patterns of fold divergence and motif degeneration are discussed in the context of fold evolution.
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