ArticleNature communications2026
Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.
Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- In vitro reconstitution implicates multiple OMP assembly factors in CdiAThe Journal of biological chemistry · 2026Article
- Dark Side ofJournal of the American Chemical Society · 2026Article
- Mechanism of phospholipid transport to the bacterial outer membrane by TAM.bioRxiv : the preprint server for biology · 2026Article
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Authors and funding
5 authors.
Funding
Abstract
Virtually all integral outer membrane proteins (OMPs) produced by Gram-negative bacteria contain a unique 'β barrel' structure that serves as a membrane spanning domain. The universal barrel assembly machine (BAM) catalyzes OMP assembly (folding and membrane insertion) in vivo, and purified Escherichia coli BAM that is reconstituted into proteoliposomes catalyzes OMP assembly in vitro. Here we show that BAM also catalyzes the assembly of OMPs into outer membrane fractions ('native OMs') that are purified by optimized conventional methods. Interestingly, we found that OMP assembly was moderately impaired when native OMs were isolated from a mlaA
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