ReviewJournal of molecular biology2014
Competition as a way of life for H(+)-coupled antiporters.
Review in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 40 citations in OpenAlex.
- Energetic and structural control of polyspecificity in a multidrug transporter.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular basis of vesicular monoamine transport and neurological drug interactions.Cell reports · 2025Article
- Dynamics underlie the drug recognition mechanism by the efflux transporter EmrE.Nature communications · 2024Article
- Proton-coupled transport mechanism of the efflux pump NorA.Nature communications · 2024Article
- Article
- Review
- Cryo-EM structure of antibacterial efflux transporter QacA from Staphylococcus aureus reveals a novel extracellular loop with allosteric role.The EMBO journal · 2023Article
- Expression and mutagenesis studies in theFrontiers in plant science · 2023Article
- GPU-Accelerated All-Atom Particle-Mesh Ewald Continuous Constant pH Molecular Dynamics in Amber.Journal of chemical theory and computation · 2022Article
- Structural basis for inhibition of the drug efflux pump NorA from Staphylococcus aureus.Nature chemical biology · 2022Article
- Principles of Alternating Access in Multidrug and Toxin Extrusion (MATE) Transporters.Journal of molecular biology · 2021Review
- Characterization of the substrate binding site of an iron detoxifying membrane transporter from Plasmodium falciparum.Malaria journal · 2021Article
- Dissection of Protonation Sites for Antibacterial Recognition and Transport in QacA, a Multi-Drug Efflux Transporter.Journal of molecular biology · 2019Article
- Bioprospecting of Native Efflux Pumps To Enhance Furfural Tolerance in EthanologenicApplied and environmental microbiology · 2019Article
- The ins and outs of vesicular monoamine transporters.The Journal of general physiology · 2018Review
- A Loose Relationship: Incomplete HBiophysical journal · 2017Article
- Dissecting the proton transport pathway in electrogenic NaProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Differences in the phenotypic effects of mutations in homologous MrpA and MrpD subunits of the multi-subunit Mrp-type NaExtremophiles : life under extreme conditions · 2017Article
- Emulating proton-induced conformational changes in the vesicular monoamine transporter VMAT2 by mutagenesis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Simulating the Function of the MjNhaP1 Transporter.The journal of physical chemistry. B · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author at 1 institution in 1 country.
Funding
Abstract
Antiporters are ubiquitous membrane proteins that catalyze obligatory exchange between two or more substrates across a membrane in opposite directions. Some utilize proton electrochemical gradients generated by primary pumps by coupling the downhill movement of one or more protons to the movement of a substrate. Since the direction of the proton gradient usually favors proton movement toward the cytoplasm, their function results in removal of substrates other than protons from the cytoplasm, either into acidic intracellular compartments or out to the medium. H(+)-coupled antiporters play central roles in living organisms, for example, storage of neurotransmitter and other small molecules, resistance to antibiotics, homeostasis of ionic content and more. Biochemical and structural data support a general mechanism for H(+)-coupled antiporters whereby the substrate and the protons cannot bind simultaneously to the protein. In several cases, it was shown that the binding sites overlap, and therefore, there is a direct competition between the protons and the substrate. In others, the "competition" seems to be indirect and it is most likely achieved by allosteric mechanisms. The pKa of one or more carboxyls in the protein must be tuned appropriately in order to ensure the feasibility of such a mechanism. In this review, I discuss in detail the case of EmrE, a multidrug transporter from Escherichia coli and evaluate the information available for other H(+)-coupled antiporters.
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.