ArticlePloS one2013
The gating mechanism of the human aquaporin 5 revealed by molecular dynamics simulations.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 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
27 citing papers in PubMed, 72 citations in OpenAlex.
- The Influence of AQP5 on the Response to Hydrogen Peroxide in Breast Cancer Cell Lines.International journal of molecular sciences · 2025Article
- The involvement of aquaporin 5 in the inflammatory response of primary Sjogren's syndrome dry eye: potential therapeutic targets exploration.Frontiers in medicine · 2024Review
- Expression Regulation and Trafficking of Aquaporins.Advances in experimental medicine and biology · 2023Review
- Multiple pore lining residues modulate water permeability of GlpF.Protein science : a publication of the Protein Society · 2022Article
- Aquaglyceroporin Modulators as Emergent Pharmacological Molecules for Human Diseases.Frontiers in molecular biosciences · 2022Review
- Human Aquaporins: Functional Diversity and Potential Roles in Infectious and Non-infectious Diseases.Frontiers in genetics · 2021Review
- Aquaporin-driven hydrogen peroxide transport: a case of molecular mimicry?RSC chemical biology · 2020Article
- Water in Nanopores and Biological Channels: A Molecular Simulation Perspective.Chemical reviews · 2020Review
- A novel molecular dynamics study of COThe European physical journal. E, Soft matter · 2019Article
- Human Aquaporin-5 Facilitates Hydrogen Peroxide Permeation Affecting Adaption to Oxidative Stress and Cancer Cell Migration.Cancers · 2019Article
- Inhibitors of Mammalian Aquaporin Water Channels.International journal of molecular sciences · 2019Review
- Peroxiporins in Cancer.International journal of molecular sciences · 2019Review
- Presence of Intra-helical Salt-Bridge in Loop E Half-Helix Can Influence the Transport Properties of AQP1 and GlpF Channels: Molecular Dynamics Simulations of In Silico Mutants.The Journal of membrane biology · 2019Article
- Article
- Cooperativity in Plant Plasma Membrane Intrinsic Proteins (PIPs): Mechanism of Increased Water Transport in Maize PIP1 Channels in Hetero-tetramers.Scientific reports · 2018Article
- Permeability and ammonia selectivity in aquaporin TIP2;1: linking structure to function.Scientific reports · 2018Article
- Forced diffusion of water molecules through aquaporin-5 biomembrane; a molecular dynamics study.Biophysics and physicobiology · 2018Article
- Computational Approaches for Revealing the Structure of Membrane Transporters: Case Study on Bilitranslocase.Computational and structural biotechnology journal · 2017Review
- Rat Aquaporin-5 Is pH-Gated Induced by Phosphorylation and Is Implicated in Oxidative Stress.International journal of molecular sciences · 2016Article
- Human Aquaporin-4 and Molecular Modeling: Historical Perspective and View to the Future.International journal of molecular sciences · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aquaporins are protein channels located across the cell membrane with the role of conducting water or other small sugar alcohol molecules (aquaglyceroporins). The high-resolution X-ray structure of the human aquaporin 5 (HsAQP5) shows that HsAQP5, as all the other known aquaporins, exhibits tetrameric structure. By means of molecular dynamics simulations we analyzed the role of spontaneous fluctuations on the structural behavior of the human AQP5. We found that different conformations within the tetramer lead to a distribution of monomeric channel structures, which can be characterized as open or closed. The switch between the two states of a channel is a tap-like mechanism at the cytoplasmic end which regulates the water passage through the pore. The channel is closed by a translation of the His67 residue inside the pore. Moreover, water permeation rate calculations revealed that the selectivity filter, located at the other end of the channel, regulates the flow rate of water molecules when the channel is open, by locally modifying the orientation of His173. Furthermore, the calculated permeation rates of a fully open channel are in good agreement with the reported experimental value.
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.