ReviewPflugers Archiv : European journal of physiology2006
Amt/MEP/Rh proteins conduct ammonia.
Review in Pflugers Archiv : European journal of physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
36 citing papers in PubMed, 84 citations in OpenAlex.
- Proteobacteria with chemosynthetic potential are highly prevalent in the gills of Hypoplectrus reef fishes.PLoS genetics · 2026Article
- Ammonia and Nematode Ascaroside Are Synergistic in Trap Formation inPathogens (Basel, Switzerland) · 2023Article
- Prokaryotic ammonium transporters: what has three decades of research revealed?Microbiology (Reading, England) · 2023Article
- Local Attraction of Substrates and Co-Substrates Enhances Weak Acid and Base Transmembrane Transport.Biomolecules · 2022Review
- Volatile-Mediated Inhibitory Activity of Rhizobacteria as a Result of Multiple Factors Interaction: The Case ofMicroorganisms · 2020Article
- Genomic Insights of "Frontiers in microbiology · 2020Article
- Ranking network mechanisms by how they fit diverse experiments and deciding onNPJ systems biology and applications · 2019Article
- Parallel substrate supply and pH stabilization for optimal screening of E. coli with the membrane-based fed-batch shake flask.Microbial cell factories · 2018Article
- Horizontal gene transfer drives the evolution of Rh50 permeases in prokaryotes.BMC evolutionary biology · 2017Article
- Structural determinants of NH3 and NH4+ transport by mouse Rhbg, a renal Rh glycoprotein.American journal of physiology. Renal physiology · 2016Article
- Article
- Evidence for the functional involvement of members of the TRP channel family in the uptake of Na(+) and NH4 (+) by the ruminal epithelium.Pflugers Archiv : European journal of physiology · 2016Article
- Ammonia-Oligotrophic and Diazotrophic Heavy Metal-Resistant Serratia liquefaciens Strains from Pioneer Plants and Mine Tailings.Microbial ecology · 2016Article
- Evolution of Electrogenic Ammonium Transporters (AMTs).Frontiers in plant science · 2016Article
- Article
- Article
- Human SLC4A11 Is a Novel NH3/H+ Co-transporter.The Journal of biological chemistry · 2015Article
- Gene Deletions Resulting in Increased Nitrogen Release by Azotobacter vinelandii: Application of a Novel Nitrogen Biosensor.Applied and environmental microbiology · 2015Article
- Direct observation of electrogenic NH4(+) transport in ammonium transport (Amt) proteins.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Nitrogen assimilation in Escherichia coli: putting molecular data into a systems perspective.Microbiology and molecular biology reviews : MMBR · 2013Review
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
No grant is acknowledged in the PubMed record.
Abstract
The structure determination of the ammonium transport protein AmtB from Escherichia coli strongly indicates that the members of the ubiquitous ammonium transporter/methylamine permease/Rhesus (Amt/MEP/Rh) protein family are ammonia-conducting channels rather than ammonium ion transporters. The most conserved part of these proteins, apart from the common overall structure with 11 transmembrane helices, is the pore lined by hydrophobic side chains except for two highly conserved histidine residues. A high-affinity ion-binding site specific for ammonium is present at the extracellular pore entry of the Amt/MEP proteins. It is proposed to play an important role in enhancing net transport at very low external ammonium concentrations and to provide discrimination against water. The site is not conserved in the animal Rhesus proteins which are implicated in ammonium homeostasis and saturate at millimolar ammonium concentrations. Many aspects of the biological function of these ammonia channels are still poorly understood and further studies in cellular systems are needed. Likewise, studies with purified, reconstituted Amt/MEP/Rh proteins will be needed to resolve open mechanistic questions and gain a more quantitative understanding of the conduction mechanism in general and for different subfamily representatives.
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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.