ReviewThe FEBS journal2012
Insights into the structure and assembly of Escherichia coli outer membrane protein A.
Review in The FEBS journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 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.
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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
37 citing papers in PubMed, 56 citations in OpenAlex.
- metaRLK 2.0: An updated database of plant receptor-like kinases developed with structure- and deep learning-based functional annotation and classification.Plant communications · 2026Article
- From Hue to Health: Exploring the Therapeutic Potential of Plant-Pigment-Enriched Extracts.Microorganisms · 2025Article
- Autonomous division of the outer membrane in Gram-negative bacteria.bioRxiv : the preprint server for biology · 2025Article
- Optimizing phage therapy for carbapenem-resistantAntimicrobial agents and chemotherapy · 2025Article
- Synergistic effects of polymyxin and vancomycin combinations on carbapenem- and polymyxin-resistantMicrobiology spectrum · 2023Article
- Identification and characterisation of a major outer membrane protein from Methylacidiphilum fumariolicum SolV.Antonie van Leeuwenhoek · 2023Article
- Envelope-Stress Sensing Mechanism of Rcs and Cpx Signaling Pathways in Gram-Negative Bacteria.Journal of microbiology (Seoul, Korea) · 2023Review
- Article
- Subcellular localization of Type VI secretion system assembly in response to cell-cell contact.The EMBO journal · 2022Article
- Human Monoclonal Antibodies to Escherichia coli Outer Membrane Protein A Porin Domain Cause Aggregation but Do Not AlterInfection and immunity · 2022Article
- Article
- Phase separation in the outer membrane ofProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Extraintestinal PathogenicPathogens (Basel, Switzerland) · 2021Review
- Roles of ompA of Citrobacter werkmanii in bacterial growth, biocide resistance, biofilm formation and swimming motility.Applied microbiology and biotechnology · 2021Article
- Article
- Article
- How the assembly and protection of the bacterial cell envelope depend on cysteine residues.The Journal of biological chemistry · 2020Review
- Trigger factor is a bona fide secretory pathway chaperone that interacts with SecB and the translocase.EMBO reports · 2020Article
- Article
- Pushing beyond the Envelope: the Potential Roles of OprF inJournal of bacteriology · 2019Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Outer membrane protein A (OmpA) of Escherichia coli is a paradigm for the biogenesis of outer membrane proteins; however, the structure and assembly of OmpA have remained controversial. A review of studies to date supports the hypothesis that native OmpA is a single-domain large pore, while a two-domain narrow-pore structure is a folding intermediate or minor conformer. The in vitro refolding of OmpA to the large-pore conformation requires isolation of the protein from outer membranes with retention of an intact disulfide bond followed by sufficient incubation in lipids at temperatures of ≥ 26 °C to overcome the high energy of activation for refolding. The in vivo maturation of the protein involves covalent modification of serines in the eighth β-barrel of the N-terminal domain by oligo-(R)-3-hydroxybutyrates as the protein is escorted across the cytoplasm by SecB for post-translational secretion across the secretory translocase in the inner membrane. After cleavage of the signal sequence, protein chaperones, such as Skp, DegP and SurA, guide OmpA across the periplasm to the β-barrel assembly machinery (BAM) complex in the outer membrane. During this passage, a disulfide bond is formed between C290 and C302 by DsbA, and the hydrophobicity of segments of the C-terminal domain, which are destined for incorporation as β-barrels in the outer membrane bilayer, is increased by covalent attachment of oligo-(R)-3-hydroxybutyrates. With the aid of the BAM complex, OmpA is then assembled into the outer membrane as a single-domain large pore.
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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.