ArticleJournal of bacteriology2008
Site-directed mutagenesis reveals putative substrate binding residues in the Escherichia coli RND efflux pump AcrB.
Article in Journal of bacteriology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 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.
The trial behind it
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Who cites it
71 citing papers in PubMed.
- Conformational plasticity across phylogenetic clusters of RND multidrug efflux pumps and its impact on substrate specificity.Nature communications · 2025Article
- Insights into substrate recognition and export tunnel preferences in the efflux transporter AcrB.Protein science : a publication of the Protein Society · 2025Article
- Structural and functional diversity of Resistance-Nodulation-Division (RND) efflux pump transporters with implications for antimicrobial resistance.Microbiology and molecular biology reviews : MMBR · 2024Review
- Pyrrole-based inhibitors of RND-type efflux pumps reverse antibiotic resistance and display anti-virulence potential.PLoS pathogens · 2024Article
- Comparative reassessment of AcrB efflux inhibitors reveals differential impact of specific pump mutations on the activity of potent compounds.Microbiology spectrum · 2024Article
- Molecular insights into the determinants of substrate specificity and efflux inhibition of the RND efflux pumps AcrB and AdeB.Microbiology (Reading, England) · 2024Review
- Article
- Tripartite efflux pumps of the RND superfamily: what did we learn from computational studies?Microbiology (Reading, England) · 2023Review
- Update on the Discovery of Efflux Pump Inhibitors against Critical Priority Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2023Review
- Functionally distinct mutations within AcrB underpin antibiotic resistance in different lifestyles.npj antimicrobials and resistance · 2023Article
- Characterization and Molecular Determinants for β-Lactam Specificity of the Multidrug Efflux Pump AcrD fromAntibiotics (Basel, Switzerland) · 2021Article
- Structural and functional analysis of the promiscuous AcrB and AdeB efflux pumps suggests different drug binding mechanisms.Nature communications · 2021Article
- Mechanistic Duality of Bacterial Efflux Substrates and Inhibitors: Example of Simple Substituted Cinnamoyl and Naphthyl Amides.ACS infectious diseases · 2021Article
- Insight into the AcrAB-TolC Complex Assembly Process Learned from Competition Studies.Antibiotics (Basel, Switzerland) · 2021Article
- Ever-Adapting RND Efflux Pumps in Gram-Negative Multidrug-Resistant Pathogens: A Race against Time.Antibiotics (Basel, Switzerland) · 2021Review
- Physicochemical and Structural Parameters Contributing to the Antibacterial Activity and Efflux Susceptibility of Small-Molecule Inhibitors of Escherichia coli.Antimicrobial agents and chemotherapy · 2021Article
- New Topoisomerase Inhibitors: Evaluating the Potency of Gepotidacin and Zoliflodacin in Fluoroquinolone-Resistant Escherichia coli uponAntimicrobial agents and chemotherapy · 2021Article
- Cryo-EM Structure and Molecular Dynamics Analysis of the Fluoroquinolone Resistant Mutant of the AcrB Transporter fromMicroorganisms · 2020Article
- Molecular Interactions of Carbapenem Antibiotics with the Multidrug Efflux Transporter AcrB ofInternational journal of molecular sciences · 2020Article
- Loss of the Periplasmic Chaperone Skp and Mutations in the Efflux Pump AcrAB-TolC Play a Role in Acquired Resistance to Antimicrobial Peptides inFrontiers in microbiology · 2020Article
11 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
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli multidrug efflux pump protein AcrB has recently been cocrystallized with various substrates, suggesting that there is a phenylalanine-rich binding site around F178 and F615. We found that F610A was the point mutation that had the most significant impact on substrate MICs, while other targeted mutations, including conversion of phenylalanines 136, 178, 615, 617, and 628 to alanine, had smaller and more variable effects.
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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.