ArticleNature communications2024
Substrate engagement by the intramembrane metalloprotease SpoIVFB.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- TMcin RiPP biosynthesis in the cellular membrane.bioRxiv : the preprint server for biology · 2026Article
- Inhibitory proteins ofJournal of bacteriology · 2025Article
- Structural characterization and biophysical analysis of recombinant SpoIVB variants: insights into PDZ and serine protease domain interactions.Microbiology spectrum · 2025Article
- Cryo-EM structure of the bacterial intramembrane metalloprotease RseP in the substrate-bound state.Science advances · 2025Article
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Authors and funding
5 authors.
Funding
Abstract
S2P intramembrane metalloproteases regulate diverse signaling pathways across all three domains of life. However, the mechanism by which S2P metalloproteases engage substrates and catalyze peptide hydrolysis within lipid membranes has remained elusive. Here we determine the cryo-EM structure of the S2P family intramembrane metalloprotease SpoIVFB from Bacillus subtilis bound to its native substrate Pro-σ
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Registered trials
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