ReviewChemical reviews2026
Integration of Membrane Proteins into the Outer Membrane of Diderm Bacteria by the BAM Complex.
Review in Chemical reviews, 2026. 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.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
3 citing papers in PubMed.
- In vitro reconstitution implicates multiple OMP assembly factors in CdiAThe Journal of biological chemistry · 2026Article
- BAM-BepA complexes in outer membrane protein quality control.Nature communications · 2026Article
- Membrane Protein Insertion in Cells: Principles, Pathways, and Quality Control.Chemical reviews · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Assembly of the outer membrane (OM) of diderm bacteria is coordinated by the essential β-barrel assembly machinery (BAM) and is critical for cellular survival and pathogenicity. BAM operates in a membrane environment that is highly rigid and spatiotemporally organized, and functions without ready access to an energy source. In addition, BAM interacts with many other proteins to efficiently fold outer membrane proteins (OMP), assemble complexes in the OM, and maintain cell envelope homeostasis. In recent years, great strides have been made toward understanding the molecular mechanism of BAM-mediated (OMP) folding, with structural biology used to visualize the different stages of the pathways of OMP folding and membrane insertion. The conformational cycling of BAM and its ability to transiently form hybrid barrels with substrate OMPs facilitates their folding. Both these mechanistic features appear to be well conserved and are attractive targets for antimicrobials.
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Registered trials
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