ArticlePLoS biology2016
Crystal Structure of an Ammonia-Permeable Aquaporin.
Article in PLoS biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 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
58 citing papers in PubMed, 123 citations in OpenAlex.
- Comprehensive DIA-MS Proteomics of Root Basal Nodes Elucidates Mechanisms of Salt Tolerance in Rice.Proteomics · 2026Article
- A Semi-Quantitative Yeast Complementation Platform for Characterizing Urea and Ammonia Transport by Membrane Channels.Current protocols · 2026Article
- Mechanism of COThe Journal of physiology · 2026Article
- Independent divergences of the aquaporins across different genera highlight the distinct adaptation mechanisms within Mytilida.BMC genomics · 2025Article
- Article
- Yeast Complementation Assays Demonstrating the Importance of the Affinity Tag Position in Membrane Protein Purification, as Exemplified bySmall science · 2025Article
- Molecular mechanism of anion permeation through aquaporin 6.Biophysical journal · 2024Article
- A charged existence: A century of transmembrane ion transport in plants.Plant physiology · 2024Review
- TIP aquaporins in Cyperus esculentus: genome-wide identification, expression profiles, subcellular localizations, and interaction patterns.BMC plant biology · 2024Article
- Enhanced Stomatal Conductance Supports Photosynthesis in Wheat to Improved NHPlants (Basel, Switzerland) · 2023Article
- Analysis ofPlants (Basel, Switzerland) · 2023Article
- Burning questions for a warming and changing world: 15 unknowns in plant abiotic stress.The Plant cell · 2023Article
- Aquaporins and COFrontiers in physiology · 2023Review
- Protein Structure and Modification of Aquaporins.Advances in experimental medicine and biology · 2023Article
- Yeast as a tool for membrane protein production and structure determination.FEMS yeast research · 2022Article
- Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022Review
- High-resolution structure of a fish aquaporin reveals a novel extracellular fold.Life science alliance · 2022Article
- Article
- Diversification of the aquaporin family in geographical isolated oyster species promote the adaptability to dynamic environments.BMC genomics · 2022Article
- Structure and function of a silicic acid channel Lsi1.Frontiers in plant science · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporins of the TIP subfamily (Tonoplast Intrinsic Proteins) have been suggested to facilitate permeation of water and ammonia across the vacuolar membrane of plants, allowing the vacuole to efficiently sequester ammonium ions and counteract cytosolic fluctuations of ammonia. Here, we report the structure determined at 1.18 Å resolution from twinned crystals of Arabidopsis thaliana aquaporin AtTIP2;1 and confirm water and ammonia permeability of the purified protein reconstituted in proteoliposomes as further substantiated by molecular dynamics simulations. The structure of AtTIP2;1 reveals an extended selectivity filter with the conserved arginine of the filter adopting a unique unpredicted position. The relatively wide pore and the polar nature of the selectivity filter clarify the ammonia permeability. By mutational studies, we show that the identified determinants in the extended selectivity filter region are sufficient to convert a strictly water-specific human aquaporin into an AtTIP2;1-like ammonia channel. A flexible histidine and a novel water-filled side pore are speculated to deprotonate ammonium ions, thereby possibly increasing permeation of ammonia. The molecular understanding of how aquaporins facilitate ammonia flux across membranes could potentially be used to modulate ammonia losses over the plasma membrane to the atmosphere, e.g., during photorespiration, and thereby to modify the nitrogen use efficiency of plants.
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.