ReviewProtein science : a publication of the Protein Society2018
Thermodynamic secrets of multidrug resistance: A new take on transport mechanisms of secondary active antiporters.
Review in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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
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
7 citing papers in PubMed.
- The resistome bridge between livestock and workers: novel frameworks for early detection and monitoring of antimicrobial resistance.Frontiers in public health · 2026Review
- Asymmetric protonation of glutamate residues drives a preferred transport pathway in EmrE.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- TrkA undergoes a tetramer-to-dimer conversion to open TrkH which enables changes in membrane potential.Nature communications · 2020Article
- smFRET Probing Reveals Substrate-Dependent Conformational Dynamics of E. coli Multidrug MdfA.Biophysical journal · 2019Article
- Dissection of Protonation Sites for Antibacterial Recognition and Transport in QacA, a Multi-Drug Efflux Transporter.Journal of molecular biology · 2019Article
- Interplay between the electrostatic membrane potential and conformational changes in membrane proteins.Protein science : a publication of the Protein Society · 2019Review
- Thermodynamics of voltage-gated ion channels.Biophysics reports · 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
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Multidrug resistance (MDR) presents a growing challenge to global public health. Drug extrusion transporters play a critical part in MDR; thus, their mechanisms of substrate recognition are being studied in great detail. In this work, we review common structural features of key transporters involved in MDR. Based on our membrane potential-driving hypothesis, we propose a general energy-coupling mechanism for secondary-active antiporters. This putative mechanism provides a common framework for understanding poly-specificity of most-if not all-MDR transporters.
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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.