ReviewChannels (Austin, Tex.)2014
Switching substrate specificity of AMT/MEP/ Rh proteins.
Review in Channels (Austin, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 28 citations in OpenAlex.
- Nitrogen Use Efficiency in Agriculture: Integrating Biotechnology, Microbiology, and Novel Delivery Systems for Sustainable Agriculture.Plants (Basel, Switzerland) · 2025Review
- Identification and analysis of pyroptosis-related key genes in heart failure.Journal of cardiothoracic surgery · 2025Article
- Biological ammonium transporters from the Amt/Mep/Rh superfamily: mechanism, energetics, and technical limitations.Bioscience reports · 2024Review
- 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
- Article
- The TRPV3 channel of the bovine rumen: localization and functional characterization of a protein relevant for ruminal ammonia transport.Pflugers Archiv : European journal of physiology · 2020Article
- A twin histidine motif is the core structure for high-affinity substrate selection in plant ammonium transporters.The Journal of biological chemistry · 2020Article
- Nutrient Limitation Causes Differential Expression of Transport- and Metabolism Genes in the Compartmentalized Anammox BacteriumFrontiers in microbiology · 2020Article
- Targeted metagenomic recovery of four divergent viruses reveals shared and distinctive characteristics of giant viruses of marine eukaryotes.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019Article
- A pore-occluding phenylalanine gate prevents ion slippage through plant ammonium transporters.Scientific reports · 2019Article
- The lipid environment determines the activity of the Escherichia coli ammonium transporter AmtB.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Ranking network mechanisms by how they fit diverse experiments and deciding onNPJ systems biology and applications · 2019Article
- Complete nitrification: insights into the ecophysiology of comammox Nitrospira.Applied microbiology and biotechnology · 2019Review
- Mechanism of formate-nitrite transporters by dielectric shift of substrate acidity.The EMBO journal · 2017Article
- Evolution of Electrogenic Ammonium Transporters (AMTs).Frontiers in plant science · 2016Article
Corrections and comments
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In organisms from all kingdoms of life, ammonia and its conjugated ion ammonium are transported across membranes by proteins of the AMT/Rh family. Efficient and successful growth often depends on sufficient ammonium nutrition. The proteins mediating this transport, the so called Ammonium Transporter (AMT) or Rhesus like (Rh) proteins, share a very similar trimeric overall structure and a high sequence similarity even throughout the kingdoms. Even though structural components of the transport mechanism, like an external substrate recruitment site, an essential twin histidine pore motif, a phenylalanine gate and the hydrophobic pore are strongly conserved and have been analyzed in detail by molecular dynamic simulations and mutational studies, the substrate(s), which pass the central pores of the AMT/Rh subunits, NH4(+), NH3 + H(+), NH4(+) + H(+) or NH3, are still a matter of debate for most proteins, including the best characterized AmtB protein from Escherichia coli. The lack of a robust expression system for functional analysis has hampered proof of structural and mutational studies, although the NH3 transport function for Rh-like proteins is rarely disputed. In plant transporters belonging to the subfamily AMT1, transport is associated with electrical currents, while some plant transporters, notably of the AMT2 type, were suggested to transport NH3 across the membrane, without associated ionic currents. Here we summarize data in favor of each substrate for the distinct AMT/Rh classes, discuss mutants and how they differ in structure and functionality. A common mechanism with deprotonation and subsequent NH3 transport through the central subunit pore is suggested.
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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.