ArticleBiophysical journal2017
Role of Pore-Lining Residues in Defining the Rate of Water Conduction by Aquaporin-0.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Major Intrinsic Proteins in Fungi: A Special Emphasis on the XIP Subfamily.Journal of fungi (Basel, Switzerland) · 2025Review
- Molecular Dynamics Simulations of the Eye Lens Water Channel Aquaporin 0 from Fish.The journal of physical chemistry. B · 2024Article
- The role of phosphorylation in calmodulin-mediated gating of human AQP0.The Biochemical journal · 2024Article
- Multiple pore lining residues modulate water permeability of GlpF.Protein science : a publication of the Protein Society · 2022Article
- The Transporter-Mediated Cellular Uptake and Efflux of Pharmaceutical Drugs and Biotechnology Products: How and Why Phospholipid Bilayer Transport Is Negligible in Real Biomembranes.Molecules (Basel, Switzerland) · 2021Review
- Modeling water purification by an aquaporin-inspired graphene-based nano-channel.Journal of molecular modeling · 2019Article
- Cooperativity and allostery in aquaporin 0 regulation by CaBiochimica et biophysica acta. Biomembranes · 2019Article
- Review
- Achieving high permeability and enhanced selectivity for Angstrom-scale separations using artificial water channel membranes.Nature communications · 2018Article
Corrections and comments
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
Abstract
Compared to other aquaporins (AQPs), lens-specific AQP0 is a poor water channel, and its permeability was reported to be pH-dependent. To date, most water conduction studies on AQP0 were performed on protein expressed in Xenopus oocytes, and the results may therefore also reflect effects introduced by the oocytes themselves. Experiments with purified AQP0 reconstituted into liposomes are challenging because the water permeability of AQP0 is only slightly higher than that of pure lipid bilayers. By reconstituting high amounts of AQP0 and using high concentrations of cholesterol to reduce the permeability of the lipid bilayer, we improved the signal-to-noise ratio of water permeability measurements on AQP0 proteoliposomes. Our measurements show that mutation of two pore-lining tyrosine residues, Tyr-23 and Tyr-149 in sheep AQP0, to the corresponding residues in the high-permeability water channel AQP1 have additive effects and together increase the water permeability of AQP0 40-fold to a level comparable to that of AQP1. Molecular dynamics simulations qualitatively support these experimental findings and suggest that mutation of Tyr-23 changes the pore profile at the gate formed by residue Arg-187.
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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.