ReviewCells2018
Aquaporins: More Than Functional Monomers in a Tetrameric Arrangement.
Review in Cells, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 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
25 citing papers in PubMed, 49 citations in OpenAlex.
- Localization and Expression of Aquaporin 0 (AQP0/MIP) in the Tissues of the Spiny Dogfish (International journal of molecular sciences · 2026Article
- Diabetic Kidney Disease-Associated Pathological Angiogenesis: The Role of Aquaporin-1.Journal of diabetes · 2025Review
- Amino Acid Substitutions in Loop C of Arabidopsis PIP2 Aquaporins Alters the Permeability of COPlant, cell & environment · 2025Article
- In Silico Modelling of the AQP0 T138R Mutation and its' links to Potential Mechanisms of Cataractogenesis.Research square · 2025Article
- Major Intrinsic Proteins in Fungi: A Special Emphasis on the XIP Subfamily.Journal of fungi (Basel, Switzerland) · 2025Review
- Article
- Exploring Aquaporins in Human Studies: Mechanisms and Therapeutic Potential in Critical Illness.Life (Basel, Switzerland) · 2024Review
- 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
- Peroxiporins in Triple-Negative Breast Cancer: Biomarker Potential and Therapeutic Perspectives.International journal of molecular sciences · 2024Review
- Two aquaporins, PIP1;1 and PIP2;1, mediate the uptake of neonicotinoid pesticides in plants.Plant communications · 2024Article
- Important functions and molecular mechanisms of aquaporins family on respiratory diseases: potential translational values.Journal of Cancer · 2024Review
- Genome-Wide Identification and Expression Pattern Profiling of the Aquaporin Gene Family in Papaya (International journal of molecular sciences · 2023Article
- Mechanosensitive aquaporins.Biophysical reviews · 2023Review
- Evolution of the Concepts of Architecture and Supramolecular Dynamics of the Plasma Membrane.Membranes · 2023Review
- Ice plant root plasma membrane aquaporins are regulated by clathrin-coated vesicles in response to salt stress.Plant physiology · 2023Article
- Aquaporin Gating: A New Twist to Unravel Permeation through Water Channels.International journal of molecular sciences · 2022Review
- High-resolution structure of a fish aquaporin reveals a novel extracellular fold.Life science alliance · 2022Article
- Relevance of Aquaporins for Gamete Function and Cryopreservation.Animals : an open access journal from MDPI · 2022Review
- Aquaporins: New players in breast cancer progression and treatment response.Frontiers in oncology · 2022Review
- Genome-Wide Characterization of the Aquaporin Gene Family in Radish and Functional Analysis ofFrontiers in plant science · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Aquaporins (AQPs) function as tetrameric structures in which each monomer has its own permeable pathway. The combination of structural biology, molecular dynamics simulations, and experimental approaches has contributed to improve our knowledge of how protein conformational changes can challenge its transport capacity, rapidly altering the membrane permeability. This review is focused on evidence that highlights the functional relationship between the monomers and the tetramer. In this sense, we address AQP permeation capacity as well as regulatory mechanisms that affect the monomer, the tetramer, or tetramers combined in complex structures. We therefore explore: (i) water permeation and recent evidence on ion permeation, including the permeation pathway controversy-each monomer versus the central pore of the tetramer-and (ii) regulatory mechanisms that cannot be attributed to independent monomers. In particular, we discuss channel gating and AQPs that sense membrane tension. For the latter we propose a possible mechanism that includes the monomer (slight changes of pore shape, the number of possible H-bonds between water molecules and pore-lining residues) and the tetramer (interactions among monomers and a positive cooperative effect).
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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.