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http://purl.uniprot.org/citations/16403837http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16403837http://www.w3.org/2000/01/rdf-schema#comment"FXYD proteins belong to a family of small-membrane proteins. Recent experimental evidence suggests that at least five of the seven members of this family, FXYD1 (phospholemman), FXYD2 (gamma-subunit of Na-K-ATPase), FXYD3 (Mat-8), FXYD4 (CHIF), and FXYD7, are auxiliary subunits of Na-K-ATPase and regulate Na-K-ATPase activity in a tissue- and isoform-specific way. These results highlight the complexity of the regulation of Na+ and K+ handling by Na-K-ATPase, which is necessary to ensure appropriate tissue functions such as renal Na+ reabsorption, muscle contractility, and neuronal excitability. Moreover, a mutation in FXYD2 has been linked to cases of human hypomagnesemia, indicating that perturbations in the regulation of Na-K-ATPase by FXYD proteins may be critically involved in pathophysiological states. A better understanding of this novel regulatory mechanism of Na-K-ATPase should help in learning more about its role in pathophysiological states. This review summarizes the present knowledge of the role of FXYD proteins in the modulation of Na-K-ATPase as well as of other proteins, their regulation, and their structure-function relationship."xsd:string
http://purl.uniprot.org/citations/16403837http://purl.org/dc/terms/identifier"doi:10.1152/ajprenal.00126.2005"xsd:string
http://purl.uniprot.org/citations/16403837http://purl.uniprot.org/core/author"Geering K."xsd:string
http://purl.uniprot.org/citations/16403837http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16403837http://purl.uniprot.org/core/name"Am J Physiol Renal Physiol"xsd:string
http://purl.uniprot.org/citations/16403837http://purl.uniprot.org/core/pages"F241-50"xsd:string
http://purl.uniprot.org/citations/16403837http://purl.uniprot.org/core/title"FXYD proteins: new regulators of Na-K-ATPase."xsd:string
http://purl.uniprot.org/citations/16403837http://purl.uniprot.org/core/volume"290"xsd:string
http://purl.uniprot.org/citations/16403837http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16403837
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http://purl.uniprot.org/uniprot/#_A0A0J9YUX0-mappedCitation-16403837http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16403837
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http://purl.uniprot.org/uniprot/#_A0A0U1RPY2-mappedCitation-16403837http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16403837