| http://purl.uniprot.org/citations/10636900 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10636900 | http://www.w3.org/2000/01/rdf-schema#comment | "Na,K-ATPase plays a crucial role in cellular ion homeostasis and is the pharmacological receptor for digitalis in man. Nine different human Na,K-ATPase isozymes, composed of 3 alpha and beta isoforms, were expressed in Xenopus oocytes and were analyzed for their transport and pharmacological properties. According to ouabain binding and K(+)-activated pump current measurements, all human isozymes are functional but differ in their turnover rates depending on the alpha isoform. On the other hand, variations in external K(+) activation are determined by a cooperative interaction mechanism between alpha and beta isoforms with alpha2-beta2 complexes having the lowest apparent K(+) affinity. alpha Isoforms influence the apparent internal Na(+) affinity in the order alpha1 > alpha2 > alpha3 and the voltage dependence in the order alpha2 > alpha1 > alpha3. All human Na,K-ATPase isozymes have a similar, high affinity for ouabain. However, alpha2-beta isozymes exhibit more rapid ouabain association as well as dissociation rate constants than alpha1-beta and alpha3-beta isozymes. Finally, isoform-specific differences exist in the K(+)/ouabain antagonism which may protect alpha1 but not alpha2 or alpha3 from digitalis inhibition at physiological K(+) levels. In conclusion, our study reveals several new functional characteristics of human Na,K-ATPase isozymes which help to better understand their role in ion homeostasis in different tissues and in digitalis action and toxicity."xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.275.3.1976"xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/author | "Yu C."xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/author | "Modyanov N.N."xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/author | "Beggah A.T."xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/author | "Crambert G."xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/author | "Geering K."xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/author | "Horisberger J.D."xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/author | "Hasler U."xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/author | "Lelievre L."xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/pages | "1976-1986"xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/title | "Transport and pharmacological properties of nine different human Na, K-ATPase isozymes."xsd:string |
| http://purl.uniprot.org/citations/10636900 | http://purl.uniprot.org/core/volume | "275"xsd:string |
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| http://purl.uniprot.org/citations/10636900 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10636900 |
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| http://purl.uniprot.org/uniprot/P50993#attribution-40159F6EE4CBD61C73159943B045FF80 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/10636900 |
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