ReviewInternational journal of molecular sciences2017
Aquaporin Protein-Protein Interactions.
Review in International journal of molecular sciences, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 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
50 citing papers in PubMed, 90 citations in OpenAlex.
- Kv2.1/Kv8.2 Channels Regulate Fluid Homeostasis in the Outer Retina.bioRxiv : the preprint server for biology · 2026Article
- Localization and Expression of Aquaporin 0 (AQP0/MIP) in the Tissues of the Spiny Dogfish (International journal of molecular sciences · 2026Article
- From biological surfaces to engineered systems: how synthetic and systems biology enable biomimetic design.Frontiers in systems biology · 2026Review
- CLIP2: a novel functional player in AQP5 trafficking dynamics and implications for Sjögren's disease.Cell communication and signaling : CCS · 2025Article
- AQP5 trafficking is regulated by its C-terminal tail and interaction with prolactin-inducible protein.Biology direct · 2025Article
- The Emerging Role of Water Loss in Dog Aging.Cells · 2025Review
- Exploring Aquaporins in Human Studies: Mechanisms and Therapeutic Potential in Critical Illness.Life (Basel, Switzerland) · 2024Review
- Aquaporin Modulation by Cations, a Review.Current issues in molecular biology · 2024Review
- Inhibition of aquaporin-4 and its subcellular localization attenuates below-level central neuropathic pain by regulating astrocyte activation in a rat spinal cord injury model.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2024Article
- Functional regulation of aquaporin dynamics by lipid bilayer composition.Nature communications · 2024Article
- Deciphering Molecular Mechanisms Involved in the Modulation of Human Aquaporins' Water Permeability by Zinc Cations: A Molecular Dynamics Approach.International journal of molecular sciences · 2024Article
- Thermodynamics andThe journal of physical chemistry. B · 2024Article
- The Versatile Role of Uromodulin in Renal Homeostasis and Its Relevance in Chronic Kidney Disease.Internal medicine (Tokyo, Japan) · 2024Review
- Aquaglyceroporins in Human Breast Cancer.Cells · 2023Article
- Aquaporin-5 Dynamic Regulation.International journal of molecular sciences · 2023Review
- Cortisol Interaction with Aquaporin-2 Modulates Its Water Permeability: Perspectives for Non-Genomic Effects of Corticosteroids.International journal of molecular sciences · 2023Article
- Methods for studying mammalian aquaporin biology.Biology methods & protocols · 2023Review
- Evaluation of the Relationship Between Aquaporin-1, Hepcidin, Zinc, Copper, and İron Levels and Oxidative Stress in the Serum of Critically Ill Patients with COVID-19.Biological trace element research · 2022Article
- Proteomic Analysis of Roots Response to Potassium Deficiency and the Effect of TaHAK1-4A on KInternational journal of molecular sciences · 2022Article
- Insight into the Mammalian Aquaporin Interactome.International journal of molecular sciences · 2022Review
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 tetrameric membrane-bound channels that facilitate transport of water and other small solutes across cell membranes. In eukaryotes, they are frequently regulated by gating or trafficking, allowing for the cell to control membrane permeability in a specific manner. Protein-protein interactions play crucial roles in both regulatory processes and also mediate alternative functions such as cell adhesion. In this review, we summarize recent knowledge about aquaporin protein-protein interactions; dividing the interactions into three types: (1) interactions between aquaporin tetramers; (2) interactions between aquaporin monomers within a tetramer (hetero-tetramerization); and (3) transient interactions with regulatory proteins. We particularly focus on the structural aspects of the interactions, discussing the small differences within a conserved overall fold that allow for aquaporins to be differentially regulated in an organism-, tissue- and trigger-specific manner. A deep knowledge about these differences is needed to fully understand aquaporin function and regulation in many physiological processes, and may enable design of compounds targeting specific aquaporins for treatment of human disease.
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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.