ArticleProceedings of the National Academy of Sciences of the United States of America2014
Direct observation of electrogenic NH4(+) transport in ammonium transport (Amt) proteins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. 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
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
36 citing papers in PubMed, 66 citations in OpenAlex.
- Ammonia oxidizers offset acidification stress via adaptive substrate affinity in aquatic ecosystems.Nature communications · 2026Article
- Ammonia as a parameter shaping habitability on icy moons.FEMS microbes · 2026Review
- Preparation of Plasma Membrane Vesicles, Lysosomes, Proteoliposomes and Alternative Sample Types for SSM-Based Electrophysiology.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Investigating the Effect of Membrane Composition on the Selective Ammonium Transport of Escherichia coli AmtB Membrane Proteins.ACS applied engineering materials · 2025Article
- Extensive paralogism in the environmental pangenome: a key factor in the ecological success of natural SAR11 populations.Microbiome · 2025Article
- Electrocatalytic nitrate reduction using iron single atoms for sustainable ammonium supplies to increase rice yield.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- How sensor Amt-like proteins integrate ammonium signals.Science advances · 2024Article
- Ammonia-oxidizing bacteria and archaea exhibit differential nitrogen source preferences.Nature microbiology · 2024Article
- Biological ammonium transporters from the Amt/Mep/Rh superfamily: mechanism, energetics, and technical limitations.Bioscience reports · 2024Review
- Nitrification and beyond: metabolic versatility of ammonia oxidising archaea.The ISME journal · 2023Review
- Microbially Induced Calcium Carbonate Precipitation byApplied and environmental microbiology · 2023Review
- Prokaryotic ammonium transporters: what has three decades of research revealed?Microbiology (Reading, England) · 2023Article
- Expression and Functional Analysis ofAnimals : an open access journal from MDPI · 2023Article
- Genome-Wide Comprehensive Analysis of the Nitrogen Metabolism Toolbox Reveals Its Evolution and Abiotic Stress Responsiveness in Rice (International journal of molecular sciences · 2022Article
- Exaggerated trans-membrane charge of ammonium transporters in nutrient-poor marine environments.Open biology · 2022Article
- Phylogenomic Analysis of Metagenome-Assembled Genomes Deciphered Novel Acetogenic Nitrogen-FixingMicrobiology spectrum · 2022Article
- Article
- The Oxoglutarate Binding Site and Regulatory Mechanism Are Conserved in Ammonium Transporter Inhibitors GlnKs fromInternational journal of molecular sciences · 2021Article
- An ammonium transporter is a non-canonical olfactory receptor for ammonia.Current biology : CB · 2021Article
- The CopA2-Type PFrontiers in microbiology · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ammonium transport (Amt) proteins form a ubiquitous family of integral membrane proteins that specifically shuttle ammonium across membranes. In prokaryotes, archaea, and plants, Amts are used as environmental NH4(+) scavengers for uptake and assimilation of nitrogen. In the eukaryotic homologs, the Rhesus proteins, NH4(+)/NH3 transport is used instead in acid-base and pH homeostasis in kidney or NH4(+)/NH3 (and eventually CO2) detoxification in erythrocytes. Crystal structures and variant proteins are available, but the inherent challenges associated with the unambiguous identification of substrate and monitoring of transport events severely inhibit further progress in the field. Here we report a reliable in vitro assay that allows us to quantify the electrogenic capacity of Amt proteins. Using solid-supported membrane (SSM)-based electrophysiology, we have investigated the three Amt orthologs from the euryarchaeon Archaeoglobus fulgidus. Af-Amt1 and Af-Amt3 are electrogenic and transport the ammonium and methylammonium cation with high specificity. Transport is pH-dependent, with a steep decline at pH values of ∼5.0. Despite significant sequence homologies, functional differences between the three proteins became apparent. SSM electrophysiology provides a long-sought-after functional assay for the ubiquitous ammonium transporters.
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.