ArticleStructure (London, England : 1993)2025
Structural diversity and oligomerization of bacterial ubiquitin-like proteins.
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 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.
- A DNA damage-activated kinase phosphorylates a transcriptional repressor to control bacterial immune pathway expression.The EMBO journal · 2026Article
- A DNA damage-activated kinase controls bacterial immune pathway expression.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic basis for protein conjugation in a diverged bacterial ubiquitination pathway.Nature structural & molecular biology · 2026Article
- A ubiquitin-like protein controls assembly of a bacterial type VIIb secretion system.Science advances · 2025Article
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Abstract
Bacteria possess a variety of operons with homology to eukaryotic ubiquitination pathways that encode predicted E1, E2, E3, deubiquitinase, and ubiquitin-like proteins. Some of these pathways have recently been shown to function in anti-bacteriophage immunity, but the biological functions of others remain unknown. Here, we show that ubiquitin-like proteins in two bacterial operon families show surprising architectural diversity, possessing one to three β-grasp domains preceded by diverse N-terminal domains. We find that a large group of bacterial ubiquitin-like proteins possess three β-grasp domains and form homodimers and helical filaments mediated by conserved Ca
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