ReviewPhilosophical transactions of the Royal Society of London. Series B, Biological sciences2015
Outer membrane protein biogenesis in Gram-negative bacteria.
Review in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 134 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
134 citing papers in PubMed, 1 synthesis or guideline pooled it, 249 citations in OpenAlex.
- Drug-resistantClinical microbiology reviews · 2025Pooled it
- Article
- Is faster always better? A critical assessment of Vibrio natriegens as microbial host for recombinant protein production.Bioprocess and biosystems engineering · 2026Review
- Akkermansia muciniphila : A next-generation gut probiotic supporting neurorepair and functional recovery.Neural regeneration research · 2026Article
- An mRNA-Lipid Nanoparticle Platform Encoding the Conserved Outer Membrane Protein BamA Elicits Broadly Cross-Reactive Systemic and Mucosal Antibodies Against Antimicrobial-ResistantbioRxiv : the preprint server for biology · 2026Article
- DeepPath: overcoming data scarcity for protein transition pathway prediction using physics-based deep learning.Chemical science · 2026Article
- Negative design enables cell-free expression and folding of designed transmembrane β-barrels.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- The Omp85 family protein, TamA, exhibits characteristics of a suitable drug target againstMicrobiology (Reading, England) · 2026Article
- Carbapenem-ResistantAntibiotics (Basel, Switzerland) · 2026Review
- Ultrastructure Analysis by Cryo-Electron Tomography Revealed Mesosomes in the Gram-negative Delftia Acidovorans.Microbial ecology · 2026Article
- Molecular mechanisms of antibiotic resistance in Gram-positive and Gram-negative bacteria - a narrative review.Frontiers in cellular and infection microbiology · 2026Review
- Construction and characterization of a nanopore derived from the transmembrane domain of a trimeric autotransporter adhesin.Frontiers in bioengineering and biotechnology · 2026Article
- Review
- Molecular insights into how the motions of the β-barrel and POTRA domains of BamA are coupled for efficient function.Nature communications · 2025Article
- Article
- The Extracytoplasmic Protein Quality Control System in Pathogenic Campylobacterota: Its Role in Bacterial Virulence and Maintaining Cellular Envelope Proteostasis.International journal of molecular sciences · 2025Review
- Barrel expansion of outer membrane protein G nanopore through β-hairpin duplication.Protein science : a publication of the Protein Society · 2025Article
- Understanding phage BX-1 resistance inMicrobiology spectrum · 2025Article
- Airborne Escherichia coli bacteria biosynthesize lipids in response to aerosolization stress.Scientific reports · 2025Article
- Microbial adaptive pathogenicity strategies to the host inflammatory environment.FEMS microbiology reviews · 2025Review
74 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Gram-negative bacteria contain a double membrane which serves for both protection and for providing nutrients for viability. The outermost of these membranes is called the outer membrane (OM), and it contains a host of fully integrated membrane proteins which serve essential functions for the cell, including nutrient uptake, cell adhesion, cell signalling and waste export. For pathogenic strains, many of these outer membrane proteins (OMPs) also serve as virulence factors for nutrient scavenging and evasion of host defence mechanisms. OMPs are unique membrane proteins in that they have a β-barrel fold and can range in size from 8 to 26 strands, yet can still serve many different functions for the cell. Despite their essential roles in cell survival and virulence, the exact mechanism for the biogenesis of these OMPs into the OM has remained largely unknown. However, the past decade has witnessed significant progress towards unravelling the pathways and mechanisms necessary for moulding a nascent polypeptide into a functional OMP within the OM. Here, we will review some of these recent discoveries that have advanced our understanding of the biogenesis of OMPs in Gram-negative bacteria, starting with synthesis in the cytoplasm to folding and insertion into the OM.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.