ReviewProtein science : a publication of the Protein Society2015
Heavy metal transport by the CusCFBA efflux system.
Review in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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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.
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Who cites it
31 citing papers in PubMed, 64 citations in OpenAlex.
- Distinct sub-MIC kill kinetics of Cu and Ag inMicrobiology spectrum · 2026Article
- CuiT is a Cu importer required for metal homeostasis inBiochemistry and biophysics reports · 2026Article
- Operonic architecture of bacterial metal response: envelope constraints, evolutionary mobility, and bioremediation design rules.World journal of microbiology & biotechnology · 2026Review
- Discovery and cryoEM structure of FPM13, a periplasmic metalloprotein unique to Francisella.PLoS pathogens · 2026Article
- A correlation analysis between arsenic and mercury resistance and the spread of antibiotic resistance genes in bacteria isolated from a highly contaminated brownfield.Frontiers in microbiology · 2026Article
- Plant Responses to Heavy Metal Stresses: Mechanisms, Defense Strategies, and Nanoparticle-Assisted Remediation.Plants (Basel, Switzerland) · 2025Review
- Systematic and synthetic biology insights into copper homeostasis in Escherichia coli.iScience · 2025Article
- Long-read methylome analysis of Oleidesulfovibrio alaskensis G20 biofilm under copper stress.Scientific reports · 2025Article
- Bacteria Under Metal Stress-Molecular Mechanisms of Metal Tolerance.International journal of molecular sciences · 2025Review
- Enhancing 10-HDA production ofFrontiers in bioengineering and biotechnology · 2025Article
- Development of a two component system based biosensor with high sensitivity for the detection of copper ions.Communications biology · 2024Article
- Genomics and taxonomy of the glyphosate-degrading, copper-tolerant rhizospheric bacterium Achromobacter insolitus LCu2.Antonie van Leeuwenhoek · 2024Article
- Article
- Early transcriptional changes of heavy metal resistance and multiple efflux genes in Xanthomonas campestris pv. campestris under copper and heavy metal ion stress.BMC microbiology · 2024Article
- The Bradyrhizobium japonicum exporter ExsFGH is involved in efflux of ferric xenosiderophores from the periplasm.PloS one · 2024Article
- The divalent metal ion exporter IhpABC is required to maintain iron homeostasis under low to moderate environmental iron conditions in the bacterium Bradyrhizobium japonicum.Molecular microbiology · 2024Article
- The copper resistance mechanism in a newly isolated Pseudoxanthomonas spadix ZSY-33.Environmental microbiology reports · 2023Article
- Metal Messengers: Communication in the Bacterial World through Transition-Metal-Sensing Two-Component Systems.Biochemistry · 2023Review
- Five copper homeostasis gene clusters encode the Cu-efflux resistome of the highly copper-tolerantPeerJ · 2023Article
- Structural and functional mapping ofComputational and structural biotechnology journal · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It is widely accepted that the increased use of antibiotics has resulted in bacteria with developed resistance to such treatments. These organisms are capable of forming multi-protein structures that bridge both the inner and outer membrane to expel diverse toxic compounds directly from the cell. Proteins of the resistance nodulation cell division (RND) superfamily typically assemble as tripartite efflux pumps, composed of an inner membrane transporter, a periplasmic membrane fusion protein, and an outer membrane factor channel protein. These machines are the most powerful antimicrobial efflux machinery available to bacteria. In Escherichia coli, the CusCFBA complex is the only known RND transporter with a specificity for heavy metals, detoxifying both Cu(+) and Ag(+) ions. In this review, we discuss the known structural information for the CusCFBA proteins, with an emphasis on their assembly, interaction, and the relationship between structure and function.
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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.