ArticleBiophysical reports2023
Proteoliposomes reconstituted with human aquaporin-1 reveal novel single-ion-channel properties.
Article in Biophysical reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 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
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Who cites it
4 citing papers in PubMed.
- Structural Domains Associated with Permeation, Gating, and Selectivity of Aquaporin Ion Channels Found Across Phyla.Advances in experimental medicine and biology · 2026Review
- Post-translational modification acts as a digital like switch influencing AtPIP2;1 water and cation permeability.Scientific reports · 2025Article
- Molecular mechanism of anion permeation through aquaporin 6.Biophysical journal · 2024Article
- Article
Corrections and comments
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Authors and funding
9 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human aquaporin 1 (hAQP1) forms homotetrameric channels that facilitate fluxes of water and small solutes across cell membranes. In addition to water channel activity, hAQP1 displays non-selective monovalent cation-channel activity gated by intracellular cyclic GMP. Dual water and ion-channel activity of hAQP1, thought to regulate cell shape and volume, could offer a target for novel therapeutics relevant to controlling cancer cell invasiveness. This study probed properties of hAQP1 ion channels using proteoliposomes, which, unlike conventional cell-based systems such as
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Registered trials
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