ArticleBiophysical journal2013
Human AQP1 is a constitutively open channel that closes by a membrane-tension-mediated mechanism.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 47 citations in OpenAlex.
- A Lumped Parameter Model Suggests That Infusion Studies Overestimate the Cerebrospinal Fluid Outflow Resistance in Normal Pressure Hydrocephalus.Brain sciences · 2024Article
- Membrane tension-dependent conformational change of Isoleucine 106 of loop B diminishes water permeability in FaPIP2;1.Protein science : a publication of the Protein Society · 2024Article
- Article
- Synergetic Effects of Aloe Vera Extract with Trimethylglycine for Targeted Aquaporin 3 Regulation and Long-Term Skin Hydration.Molecules (Basel, Switzerland) · 2024Article
- Mechanosensitive aquaporins.Biophysical reviews · 2023Review
- The multifaceted role of aquaporins in physiological cell migration.American journal of physiology. Cell physiology · 2023Review
- Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022Review
- Relevance of Aquaporins for Gamete Function and Cryopreservation.Animals : an open access journal from MDPI · 2022Review
- FungalBiomolecules · 2021Article
- Mechanical Activation of MscL Revealed by a Locally Distributed Tension Molecular Dynamics Approach.Biophysical journal · 2021Article
- Hydrogen, Bicarbonate, and Their Associated Exchangers in Cell Volume Regulation.Frontiers in cell and developmental biology · 2021Article
- Aquaporin 1 mediates early responses to osmotic stimuli in endothelial cells via the calmodulin pathway.FEBS open bio · 2021Article
- The quagga mussel genome and the evolution of freshwater tolerance.DNA research : an international journal for rapid publication of reports on genes and genomes · 2019Article
- Water transport, perception, and response in plants.Journal of plant research · 2019Review
- Review
- Article
- Plant and animal aquaporins crosstalk: what can be revealed from distinct perspectives.Biophysical reviews · 2017Review
- Rat Aquaporin-5 Is pH-Gated Induced by Phosphorylation and Is Implicated in Oxidative Stress.International journal of molecular sciences · 2016Article
- Role of Aquaporins in a Composite Model of Water Transport in the Leaf.International journal of molecular sciences · 2016Review
- The Water to Solute Permeability Ratio Governs the Osmotic Volume Dynamics in Beetroot Vacuoles.Frontiers in plant science · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This work presents experimental results combined with model-dependent predictions regarding the osmotic-permeability regulation of human aquaporin 1 (hAQP1) expressed in Xenopus oocyte membranes. Membrane elastic properties were studied under fully controlled conditions to obtain a function that relates internal volume and pressure. This function was used to design a model in which osmotic permeability could be studied as a pressure-dependent variable. The model states that hAQP1 closes with membrane-tension increments. It is important to emphasize that the only parameter of the model is the initial osmotic permeability coefficient, which was obtained by model-dependent fitting. The model was contrasted with experimental records from emptied-out Xenopus laevis oocytes expressing hAQP1. Simulated results reproduce and predict volume changes in high-water-permeability membranes under hypoosmotic gradients of different magnitude, as well as under consecutive hypo- and hyperosmotic conditions. In all cases, the simulated permeability coefficients are similar to experimental values. Predicted pressure, volume, and permeability changes indicate that hAQP1 water channels can transit from a high-water-permeability state to a closed state. This behavior is reversible and occurs in a cooperative manner among monomers. We conclude that hAQP1 is a constitutively open channel that closes mediated by membrane-tension increments.
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.