ArticleInternational journal of molecular sciences2016
Human Aquaporin 4 Gating Dynamics under Perpendicularly-Oriented Electric-Field Impulses: A Molecular Dynamics Study.
Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Aquaporin Modulation by Cations, a Review.Current issues in molecular biology · 2024Review
- Aqp4a and Trpv4 mediate regulatory cell volume increase for swimming maintenance of marine fish spermatozoa.Cellular and molecular life sciences : CMLS · 2024Article
- Water in Nanopores and Biological Channels: A Molecular Simulation Perspective.Chemical reviews · 2020Review
- Molecular dynamics simulation of the nanosecond pulsed electric field effect on kinesin nanomotor.Scientific reports · 2019Article
- Tubulin response to intense nanosecond-scale electric field in molecular dynamics simulation.Scientific reports · 2019Article
- Transprotein-Electropore Characterization: A Molecular Dynamics Investigation on Human AQP4.ACS omega · 2018Article
- Stimulation Strategies for Tinnitus Suppression in a Neuron Model.Computational and mathematical methods in medicine · 2018Article
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Authors and funding
8 authors.
Funding
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Abstract
Human aquaporin 4 has been studied using molecular dynamics (MD) simulations in the absence and presence of pulses of external static electric fields. The pulses were 10 ns in duration and 0.012-0.065 V/Å in intensity acting along both directions perpendicular to the pores. Water permeability and the dipolar response of all residues of interest (including the selectivity filter) within the pores have been studied. Results showed decreased levels of water osmotic permeability within aquaporin channels during orthogonally-oriented field impulses, although care must be taken with regard to statistical certainty. This can be explained observing enhanced "dipolar flipping" of certain key residues, especially serine 211, histidine 201, arginine 216, histidine 95 and cysteine 178. These residues are placed at the extracellular end of the pore (serine 211, histidine 201, and arginine 216) and at the cytoplasm end (histidine 95 and cysteine 178), with the key role in gating mechanism, hence influencing water permeability.
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