ReviewJournal of bioenergetics and biomembranes2007
Structures of the FXYD regulatory proteins in lipid micelles and membranes.
Review in Journal of bioenergetics and biomembranes, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 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
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
18 citing papers in PubMed, 28 citations in OpenAlex.
- The functions of FXYD family members in human health and disease.Genes & diseases · 2026Review
- Article
- FXYD proteins and sodium pump regulatory mechanisms.The Journal of general physiology · 2021Review
- FXYD6 overexpression in HBV-related hepatocellular carcinoma with cirrhosis.Open life sciences · 2020Article
- Abnormal Scn1b and Fxyd1 gene expression in the pulled-through ganglionic colon may influence functional outcome in patients with Hirschsprung's disease.Pediatric surgery international · 2019Article
- Na+/Ca2+ exchange and Na+/K+-ATPase in the heart.The Journal of physiology · 2015Review
- Expression and clinical significance of FXYD3 in endometrial cancer.Oncology letters · 2014Article
- Surface charges of the membrane crucially affect regulation of Na,K-ATPase by phospholemman (FXYD1).The Journal of membrane biology · 2013Article
- Regulation of the cardiac sodium pump.Cellular and molecular life sciences : CMLS · 2013Review
- Article
- The inhibitory effect of phospholemman on the sodium pump requires its palmitoylation.The Journal of biological chemistry · 2011Article
- Phosphomimetic mutations enhance oligomerization of phospholemman and modulate its interaction with the Na/K-ATPase.The Journal of biological chemistry · 2011Article
- Translocation of Pseudomonas aeruginosa from the intestinal tract is mediated by the binding of ExoS to an Na,K-ATPase regulator, FXYD3.Infection and immunity · 2010Article
- Down-regulation of FXYD3 expression in human lung cancers: its mechanism and potential role in carcinogenesis.The American journal of pathology · 2009Article
- Recent Advances in the Application of Solution NMR Spectroscopy to Multi-Span Integral Membrane Proteins.Progress in nuclear magnetic resonance spectroscopy · 2009Article
- Efficient and accurate estimation of relative order tensors from lambda-maps.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2009Article
- Regulation of epithelial Na+ transport by soluble adenylyl cyclase in kidney collecting duct cells.The Journal of biological chemistry · 2009Article
- Estimation of relative order tensors, and reconstruction of vectors in space using unassigned RDC data and its application.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2008Article
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
The FXYD membrane proteins constitute a family of conserved auxiliary subunits of the Na,K-ATPase, and have been the focus of recent attention due to their ability to finely regulate the activity of the enzyme complex in various physiological settings. In this review we describe the structures of the proteins, as well as their dynamics and their associations with the lipid bilayer membrane, which we have recently determined by NMR spectroscopy. Although the proteins are relatively small, their genes contain as many as six to nine small exons, and the coincidence of structured protein segments with their genetic elements suggests assembly from discrete structural modules through exon shuffling. The three-dimensional structures and backbone dynamics provide the foundation for understanding their intra-membrane association with the Na,K-ATPase alpha subunit, and the structure of FXYD1 suggests a mechanism whereby the phosphorylation of conserved Ser residues, by protein kinases A and C, could induce a conformational change in the cytoplasmic domain of the protein, to modulate its interaction with the alpha subunit.
Indexed as
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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.