ArticleACS infectious diseases2017
Reviving Antibiotics: Efflux Pump Inhibitors That Interact with AcrA, a Membrane Fusion Protein of the AcrAB-TolC Multidrug Efflux Pump.
Article in ACS infectious diseases, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
What it found
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Who cites it
63 citing papers in PubMed, 123 citations in OpenAlex.
- Substrate Specificity Checkpoints of the Multidrug Efflux Pump MexF fromACS infectious diseases · 2026Article
- Bovine Mastitis Therapy at a Crossroads: Pharmacokinetic Barriers, Biofilms, Antimicrobial Resistance, and Emerging Solutions.Pharmaceuticals (Basel, Switzerland) · 2026Review
- Subterranean synergies: termite bacterial diversity and eugenol-mediated selective dysbiosis.Frontiers in microbiology · 2026Article
- A review of research progress on periplasmic adaptor proteins in bacterial tripartite pumps.Frontiers in microbiology · 2026Review
- Targeting the AcrAB-TolC efflux pump by small molecules selectively addressing the outer membrane factor TolC.Frontiers in pharmacology · 2026Article
- Asiatic acid, a novel ciprofloxacin adjuvant inhibitsGut microbes · 2025Article
- A novel role for colistin as an efflux pump inhibitor in multidrug-resistant Klebsiella pneumoniae.Scientific reports · 2025Article
- Antimicrobial and Anti-Efflux Machinery of FDA-Approved Proton Pump Inhibitors and Vitamins AgainstMicroorganisms · 2025Article
- Diversity and functional features of the root-associated bacteriome are dependent on grapevine susceptibility to Plasmopara viticola.Environmental microbiome · 2025Article
- High throughput screening identifies potential inhibitors targeting trimethoprim resistant DfrA1 protein in Klebsiella pneumoniae and Escherichia coli.Scientific reports · 2025Article
- Review
- Efficacy of outer membrane permeabilization in promoting aromatic isothiocyanates-mediated eradication of multidrug resistant Gram-negative bacteria and bacterial persisters.Folia microbiologica · 2024Article
- Structural and functional diversity of Resistance-Nodulation-Division (RND) efflux pump transporters with implications for antimicrobial resistance.Microbiology and molecular biology reviews : MMBR · 2024Review
- MgbioRxiv : the preprint server for biology · 2024Article
- Extending the Potency and Lifespan of Antibiotics: Inhibitors of Gram-Negative Bacterial Efflux Pumps.ACS infectious diseases · 2024Review
- Predicting permeation of compounds across the outer membrane of P. aeruginosa using molecular descriptors.Communications chemistry · 2024Article
- Characterization of genes related to the efflux pump and porin in multidrug-resistant Escherichia coli strains isolated from patients with COVID-19 after secondary infection.BMC microbiology · 2024Article
- Fitness trade-offs of multidrug efflux pumps inApplied and environmental microbiology · 2024Article
- Molecular insights into the determinants of substrate specificity and efflux inhibition of the RND efflux pumps AcrB and AdeB.Microbiology (Reading, England) · 2024Review
- Development of pharmacophore models for AcrB protein and the identification of potential adjuvant candidates for overcoming efflux-mediated colistin resistance.RSC medicinal chemistry · 2024Article
3 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
Antibiotic resistance is a major threat to human welfare. Inhibitors of multidrug efflux pumps (EPIs) are promising alternative therapeutics that could revive activities of antibiotics and reduce bacterial virulence. Identification of new druggable sites for inhibition is critical for the development of effective EPIs, especially in light of constantly emerging resistance. Here, we describe EPIs that interact with periplasmic membrane fusion proteins, critical components of efflux pumps that are responsible for the activation of the transporter and the recruitment of the outer-membrane channel. The discovered EPIs bind to AcrA, a component of the prototypical AcrAB-TolC pump, change its structure in vivo, inhibit efflux of fluorescent probes, and potentiate the activities of antibiotics in Escherichia coli and other Gram-negative bacteria. Our findings expand the chemical and mechanistic diversity of EPIs, suggest the mechanism for regulation of the efflux pump assembly and activity, and provide a promising path for reviving the activities of antibiotics in resistant bacteria.
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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.