Mechanism of the Na,K-ATPase Inhibition by MCS Derivatives

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STIMAC, Robert, Franz KEREK, Hans-Jürgen APELL, 2005. Mechanism of the Na,K-ATPase Inhibition by MCS Derivatives. In: The Journal of Membrane Biology. 205(2), pp. 89-101. ISSN 0022-2631. eISSN 1432-1424

@article{Stimac2005Mecha-8615, title={Mechanism of the Na,K-ATPase Inhibition by MCS Derivatives}, year={2005}, doi={10.1007/s00232-005-0767-2}, number={2}, volume={205}, issn={0022-2631}, journal={The Journal of Membrane Biology}, pages={89--101}, author={Stimac, Robert and Kerek, Franz and Apell, Hans-Jürgen} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/8615"> <dc:contributor>Apell, Hans-Jürgen</dc:contributor> <dc:language>eng</dc:language> <dcterms:issued>2005</dcterms:issued> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:07Z</dc:date> <dc:creator>Stimac, Robert</dc:creator> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8615"/> <dc:contributor>Kerek, Franz</dc:contributor> <dc:creator>Apell, Hans-Jürgen</dc:creator> <dc:format>application/pdf</dc:format> <dcterms:bibliographicCitation>First publ. in: The Journal of Membrane Biology 205 (2005), 2, pp. 89-101</dcterms:bibliographicCitation> <dc:creator>Kerek, Franz</dc:creator> <dcterms:title>Mechanism of the Na,K-ATPase Inhibition by MCS Derivatives</dcterms:title> <dc:rights>deposit-license</dc:rights> <dcterms:abstract xml:lang="eng">The previously reported class of potent inorganic inhibitors of Na,K-ATPase, named MCS factors, was shown to inhibit not only Na,K-ATPase but several P-type ATPases with high potency in the sub-micromolar range. These MCS factors were found to bind to the intracellular side of the Na, K-ATPase. The inhibition is not competitive with ouabain binding, thus excluding its role as cardiac-steroid-like inhibitor of the Na,K-ATPase. The mechanism of inhibition of Na,K-ATPase was investigated with the fluorescent styryl dye RH421, a dye known to report changes of local electric fields in the membrane dielectric. MCS factors interact with the Na,K-ATPase in the E1 conformation of the ion pump and induce a conformational rearrangement that causes a change of the equilibrium dissociation constant for one of the first two intracellular cation binding sites. The MCS-inhibited state was found to have bound one cation (H+, Na+ or K+) in one of the two unspecific binding sites, and at high Na+ concentrations another Na+ ion was bound to the highly Na+-selective ion-binding site.</dcterms:abstract> <dc:contributor>Stimac, Robert</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:45:07Z</dcterms:available> </rdf:Description> </rdf:RDF>

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