ReviewJournal of bioenergetics and biomembranes2005
Function of FXYD proteins, regulators of Na, K-ATPase.
Review in Journal of bioenergetics and biomembranes, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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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.
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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.
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Who cites it
57 citing papers in PubMed, 117 citations in OpenAlex.
- The functions of FXYD family members in human health and disease.Genes & diseases · 2026Review
- Post-translational modifications of na+/K+-atpase subunits: regulatory mechanisms and functional implications.Frontiers in cell and developmental biology · 2026Review
- Synovial joint cavitation during limb skeletogenesis entails Na/K-ATPase ion pump expression and osmoregulatory activity.Development (Cambridge, England) · 2025Article
- Article
- Na,K-ATPase mediated and cardiotonic induced signaling in health and disease.Frontiers in physiology · 2025Review
- NaInternational journal of molecular sciences · 2024Review
- Low-Salt Diet Regulates the Metabolic and Signal Transduction Genomic Fabrics, and Remodels the Cardiac Normal and Chronic Pathological Pathways.Current issues in molecular biology · 2024Article
- A century of exercise physiology: effects of muscle contraction and exercise on skeletal muscle NaEuropean journal of applied physiology · 2024Review
- FXYD3 facilitates NaAmerican journal of physiology. Cell physiology · 2022Article
- Integration of Single-Cell RNA- and CAGE-seq Reveals Tooth-Enriched Genes.Journal of dental research · 2022Article
- Fluorescence lifetime imaging microscopy reveals sodium pump dimers in live cells.The Journal of biological chemistry · 2022Article
- Fxyd5 activates the NF‑κB pathway and is involved in chondrocytes inflammation and extracellular matrix degradation.Molecular medicine reports · 2022Article
- Intestinal secretory mechanisms and diarrhea.American journal of physiology. Gastrointestinal and liver physiology · 2022Review
- Comparative description of the mRNA expression profile of NaThe Journal of comparative neurology · 2022Article
- Maturation of the Na,K-ATPase in the Endoplasmic Reticulum in Health and Disease.The Journal of membrane biology · 2021Article
- Clinical significance of P-class pumps in cancer.Oncology letters · 2021Review
- Role of endogenous ouabain in the etiology of bipolar disorder.International journal of bipolar disorders · 2021Review
- The MemMoRF database for recognizing disordered protein regions interacting with cellular membranes.Nucleic acids research · 2021Article
- Transcriptional and Epigenetic Bioinformatic Analysis of Claudin-9 Regulation in Gastric Cancer.Journal of oncology · 2021Article
- Overview on solubilization and lipid reconstitution of Na,K-ATPase: enzyme kinetic and biophysical characterization.Biophysical reviews · 2020Review
Corrections and comments
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In this short review, we summarize our work on the role of members of the FXYD protein family as tissue-specific modulators of Na, K-ATPase. FXYD1 or phospholemman, mainly expressed in heart and skeletal muscle increases the apparent affinity for intracellular Na(+) of Na, K-ATPase and may thus be important for appropriate muscle contractility. FXYD2 or gamma subunit and FXYD4 or CHIF modulate the apparent affinity for Na(+) of Na, K-ATPase in an opposite way, adapted to the physiological needs of Na(+) reabsorption in different segments of the renal tubule. FXYD3 expressed in stomach, colon, and numerous tumors also modulates the transport properties of Na, K-ATPase but it has a lower specificity of association than other FXYD proteins and an unusual membrane topology. Finally, FXYD7 is exclusively expressed in the brain and decreases the apparent affinity for extracellular K(+), which may be essential for proper neuronal excitability.
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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.