ReviewThe FEBS journal2012
Alternative folding pathways of the major porin OprF of Pseudomonas aeruginosa.
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 29 papers, 1 of them a synthesis that pooled it.
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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
29 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Molecular exploration of host-pathogen interactions in severeFrontiers in medicine · 2025Pooled it
- Inhaled Antibiotic and Biologic Formulations TargetingPharmaceutics · 2026Review
- Antibiotic resistance of Pseudomonas aeruginosa strains-intracellular metabolomics analysis.The Journal of antimicrobial chemotherapy · 2026Article
- Broadly Defined Antibiotic Adjuvants forThe Canadian journal of infectious diseases & medical microbiology = Journal canadien des maladies infectieuses et de la microbiologie medicale · 2026Review
- Multidrug resistance in Pseudomonas aeruginosa: genetic control mechanisms and therapeutic advances.Molecular biomedicine · 2024Review
- Nisin Z Potential for the Control of Diabetic Foot Infections Promoted byAntibiotics (Basel, Switzerland) · 2023Article
- Review
- Exploring Oceans for Curative Compounds: Potential New Antimicrobial and Anti-Virulence Molecules againstMarine drugs · 2022Review
- Molecular Characterization and Designing of a Novel Multiepitope Vaccine Construct AgainstInternational journal of peptide research and therapeutics · 2022Article
- Outer membrane permeability: Antimicrobials and diverse nutrients bypass porins inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cell-free expression of the outer membrane protein OprF ofLife science alliance · 2021Article
- Iron Acquisition Systems of Gram-negative Bacterial Pathogens Define TonB-Dependent Pathways to Novel Antibiotics.Chemical reviews · 2021Review
- The Building Blocks of Antimicrobial Resistance inFrontiers in cellular and infection microbiology · 2021Review
- The Landscape ofCells · 2020Article
- Identification of the PA1113 Gene Product as an ABC Transporter Involved in the Uptake of Carbenicillin inAntibiotics (Basel, Switzerland) · 2020Article
- Microevolution in the major outer membrane protein OmpA ofMicrobial genomics · 2020Article
- Identification and characterization of phage protein and its activity against two strains of multidrug-resistant Pseudomonas aeruginosa.Scientific reports · 2019Article
- Mechanisms and Targeted Therapies for Pseudomonas aeruginosa Lung Infection.American journal of respiratory and critical care medicine · 2018Review
- PA0833 Is an OmpA C-Like Protein That Confers Protection AgainstFrontiers in microbiology · 2018Article
- Surface display for metabolic engineering of industrially important acetic acid bacteria.PeerJ · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
OprF is the major porin of Pseudomonas aeruginosa and allows very slow, nonspecific, diffusion of solutes. The low permeability of this porin channel is a major factor that enhances other types of resistance mechanisms and often creates strong multidrug resistance in this nosocomial pathogen. We have previously shown that the low permeability is caused by the folding of OprF into two conformers: a majority, two-domain closed-channel conformer containing the N-terminal transmembrane β-barrel and the C-terminal periplasmic, globular domain; and a minority, one-domain open-channel conformer comprising < 5% of the protein population. Our analysis of the bifurcate folding pathway using site-directed mutagenesis showed that slowing down the folding of the two-domain conformer increases the fraction of the open, one-domain conformer. Use of outer membrane protein assembly machinery mutants showed that the absence of the Skp chaperone led to an increased proportion of open conformers. As many environmental pathogens causing nosocomial infections appear to have outer membrane protein (OmpA)/OprF homologs as the major porin, efforts to understand the low permeability of these 'slow porins' are important in our fight against these organisms.
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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.