ArticleJournal of bacteriology2006
Role of the novel OprD family of porins in nutrient uptake in Pseudomonas aeruginosa.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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
73 citing papers in PubMed, 150 citations in OpenAlex.
- Random Forest Modeling to Predict Small Molecule Accumulation in Gram-Negative Bacteria.ACS infectious diseases · 2026Article
- Adaptive Laboratory Evolution Unlocks Membrane Permeability as a Key Limitation in Long-Chain Alcohol Metabolism by Pseudomonas putida KT2440.Microbial biotechnology · 2026Article
- NV716 acts as an envelope-active adjuvant that enhances antibiotic accumulation in Pseudomonas aeruginosa.npj antimicrobials and resistance · 2026Article
- AMR-GNN: a multi-representation graph neural network framework to enable genomic antimicrobial resistance prediction.Nature communications · 2026Article
- Antibiotic resistance inFrontiers in microbiology · 2026Review
- Integron architecture and virulence-associated gene profiles in extensively drug-resistant high-riskFrontiers in microbiology · 2026Article
- The solute-binding proteins DppA1-5 of Pseudomonas aeruginosa have distinct substrate profiles.Scientific reports · 2025Article
- Cellular and molecular outcomes of Pseudomonas putida KT2440 exposure to aluminium.Folia microbiologica · 2025Article
- Vancomycin Sensitization inACS infectious diseases · 2025Article
- Proteomic profiling of zinc homeostasis mechanisms in Pseudomonas aeruginosa through data-dependent and data-independent acquisition mass spectrometry.Metallomics : integrated biometal science · 2025Article
- Evolution of Resistant Mutants inMicroorganisms · 2025Article
- Outer membrane permeability ofMicrobiology spectrum · 2025Article
- Interplay between porin deficiency, fitness, and virulence in carbapenem-non-susceptible Pseudomonas aeruginosa and Enterobacteriaceae.PLoS pathogens · 2025Review
- Proteomic profiling of zinc homeostasis mechanisms inbioRxiv : the preprint server for biology · 2025Article
- Antibiotic influx and efflux in Pseudomonas aeruginosa: Regulation and therapeutic implications.Microbial biotechnology · 2024Review
- Optimized preparation pipeline for emergency phage therapy against Pseudomonas aeruginosa at Yale University.Scientific reports · 2024Article
- Global transcriptome analysis of Pseudomonas aeruginosa NT06 response to potassium chloride, sodium lactate, sodium citrate, and microaerophilic conditions in a fish ecosystem.FEMS microbiology letters · 2024Article
- The Name Is Barrel, β-Barrel.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Article
- Genome-Wide Expression Analysis Unravels Fluoroalkane Metabolism inEnvironmental science & technology · 2023Article
13 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
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To circumvent the permeability barrier of its outer membrane, Pseudomonas aeruginosa has evolved a series of specific porins. These channels have binding sites for related classes of molecules that facilitate uptake under nutrient-limited conditions. Here, we report on the identification of a 19-member family of porins similar to the basic-amino-acid-specific porin OprD. The members of this family fell into one of two phylogenetically distinct clusters, one bearing high similarity to OprD and the other bearing most similarity to the putative phenylacetic acid uptake porin PhaK of Pseudomonas putida. Analysis of the genome context, operon arrangement, and regulation of the PhaK-like porin OpdK indicated that it might be involved in vanillate uptake. This result was confirmed by demonstrating that an opdK mutant had a deficiency in the ability to grow on vanillate as a carbon source. To extrapolate these data to other paralogues within this family, the substrate specificities of 6 of the 17 remaining OprD homologues were inferred using an approach similar to that used with opdK. The specificities determined were as follows: OpdP, glycine-glutamate; OpdC, histidine; OpdB, proline; OpdT, tyrosine; OpdH, cis-aconitate; and OpdO, pyroglutamate. Thus, members of the OprD subfamily took up amino acids and related molecules, and those characterized members most similar to PhaK were responsible for the uptake of a diverse array of organic acids. These results imply that there is a functional basis for the phylogenetic clustering of these proteins and provide a framework for studying OprD homologues in other organisms.
Indexed as
Identifiers
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.