ArticleThe Journal of biological chemistry
Conserved binding site in the N-lobe of prokaryotic MATE transporters suggests a role for Na
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Types and Mechanisms of Efflux Pump Systems and the Potential of Efflux Pump Inhibitors in the Restoration of Antimicrobial Susceptibility, with a Special Reference toPathogens (Basel, Switzerland) · 2024Review
- Review
- Molecular Basis for the Cation Selectivity of Salmonella typhimurium Melibiose Permease.Journal of molecular biology · 2022Article
- Membrane Efflux Pumps of PathogenicMicroorganisms · 2022Review
- Principles of Alternating Access in Multidrug and Toxin Extrusion (MATE) Transporters.Journal of molecular biology · 2021Review
- Engineered MATE multidrug transporters reveal two functionally distinct ion-coupling pathways in NorM from Vibrio cholerae.Communications biology · 2021Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
In both prokaryotes and eukaryotes, multidrug and toxic-compound extrusion (MATE) transporters catalyze the efflux of a broad range of cytotoxic compounds, including human-made antibiotics and anticancer drugs. MATEs are secondary-active antiporters, i.e., their drug-efflux activity is coupled to, and powered by, the uptake of ions down a preexisting transmembrane electrochemical gradient. Key aspects of this mechanism, however, remain to be delineated, such as its ion specificity and stoichiometry. We previously revealed the existence of a Na
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