ArticleNature communications2016
Tripartite assembly of RND multidrug efflux pumps.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 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
95 citing papers in PubMed, 204 citations in OpenAlex.
- Genome-wide network of antibiotic susceptibility in Pseudomonas aeruginosa.The Journal of antimicrobial chemotherapy · 2026Article
- Efflux-mediated carbapenem resistance: unveiling genetic drivers, clinical implications, and strategies for global antimicrobial stewardship.Antonie van Leeuwenhoek · 2026Review
- Broad synergistic effects of an AMP with multiple antibiotics against drug-resistant bacteria via multifaceted mechanisms.Science China. Life sciences · 2026Article
- Mutational analysis of multidrug efflux pump (AcrAB-TolC) in Enterobacter cloacae isolates from clinical samples.Scientific reports · 2026Article
- Operonic architecture of bacterial metal response: envelope constraints, evolutionary mobility, and bioremediation design rules.World journal of microbiology & biotechnology · 2026Review
- Medicinal Plants: A Promising Therapeutic Approach for Addressing Antimicrobial Resistance.International journal of molecular sciences · 2026Review
- A model for drug transport across two membranes of Gram-negative bacteria by an MFS tripartite assembly.Nature communications · 2026Article
- Genetic variants of AcrAB and OqxAB and the impact of efflux pump inhibition on ciprofloxacin and amikacin resistance in clinical isolates of Klebsiella pneumoniae from Lima, Peru.BMC microbiology · 2026Article
- Structure-Based Drug Design Targeting the Substrate-Binding Pocket of MexB.The protein journal · 2026Review
- RND efflux pump inhibitor-like natural products as antibiotic adjuvants against multidrug-resistant gram-negative bacteria: a graded-evidence review.Frontiers in microbiology · 2026Review
- Antibiotic resistance inFrontiers in microbiology · 2026Article
- Computer Simulations of Multidrug Efflux Pumps of the Resistance-Nodulation-Cell Division Superfamily.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Labeling of Specific Residues of the Multidrug Transporter AcrB with Its Fluorescent Substrate.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Unveiling structural dynamics and allosteric vulnerabilities in Klebsiella pneumoniae KPHS_11890: an integrated DRKG-MD study.Journal of computer-aided molecular design · 2025Article
- Assembly and inhibition of transferable TMexCD1-TOprJ1 efflux pump.Nature communications · 2025Article
- A novel role for colistin as an efflux pump inhibitor in multidrug-resistant Klebsiella pneumoniae.Scientific reports · 2025Article
- Surface protein machineries in Gram-negative bacteria.Journal of cell science · 2025Review
- Evaluation of Biofilm Formation, Alginate Production, Pattern of Drug Resistance, and the Presence of Efflux PumpTanaffos · 2025Article
- Quantifying bacterial efflux within subcellular domains ofApplied and environmental microbiology · 2024Article
- Article
35 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
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Tripartite multidrug efflux systems of Gram-negative bacteria are composed of an inner membrane transporter, an outer membrane channel and a periplasmic adaptor protein. They are assumed to form ducts inside the periplasm facilitating drug exit across the outer membrane. Here we present the reconstitution of native Pseudomonas aeruginosa MexAB-OprM and Escherichia coli AcrAB-TolC tripartite Resistance Nodulation and cell Division (RND) efflux systems in a lipid nanodisc system. Single-particle analysis by electron microscopy reveals the inner and outer membrane protein components linked together via the periplasmic adaptor protein. This intrinsic ability of the native components to self-assemble also leads to the formation of a stable interspecies AcrA-MexB-TolC complex suggesting a common mechanism of tripartite assembly. Projection structures of all three complexes emphasize the role of the periplasmic adaptor protein as part of the exit duct with no physical interaction between the inner and outer membrane components.
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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.