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. Available under: doi: 10.1007/s00232-005-0767-2

@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:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dc:contributor>Apell, Hans-Jürgen</dc:contributor> <dc:rights>terms-of-use</dc:rights> <dc:language>eng</dc:language> <dc:date rdf:datatype="">2011-03-24T17:45:07Z</dc:date> <dcterms:rights rdf:resource=""/> <dcterms:issued>2005</dcterms:issued> <dspace:isPartOfCollection rdf:resource=""/> <dspace:hasBitstream rdf:resource=""/> <dc:creator>Stimac, Robert</dc:creator> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <bibo:uri rdf:resource=""/> <dc:contributor>Kerek, Franz</dc:contributor> <dc:creator>Apell, Hans-Jürgen</dc:creator> <dc:creator>Kerek, Franz</dc:creator> <dcterms:bibliographicCitation>First publ. in: The Journal of Membrane Biology 205 (2005), 2, pp. 89-101</dcterms:bibliographicCitation> <dc:format>application/pdf</dc:format> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <dcterms:title>Mechanism of the Na,K-ATPase Inhibition by MCS Derivatives</dcterms:title> <dcterms:hasPart rdf:resource=""/> <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="">2011-03-24T17:45:07Z</dcterms:available> <dcterms:isPartOf rdf:resource=""/> </rdf:Description> </rdf:RDF>

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