| pubmed-article:12507758 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12507758 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:12507758 | lifeskim:mentions | umls-concept:C1705810 | lld:lifeskim |
| pubmed-article:12507758 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:12507758 | lifeskim:mentions | umls-concept:C0182537 | lld:lifeskim |
| pubmed-article:12507758 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:12507758 | pubmed:dateCreated | 2002-12-31 | lld:pubmed |
| pubmed-article:12507758 | pubmed:abstractText | The N-terminus of the Na(+),K(+)-ATPase alpha-subunit shows some homology to that of Shaker-B K(+) channels; the latter has been shown to mediate the N-type channel inactivation in a ball-and-chain mechanism. When the Torpedo Na(+),K(+)-ATPase is expressed in Xenopus oocytes and the pump is transformed into an ion channel with palytoxin (PTX), the channel exhibits a time-dependent inactivation gating at positive potentials. The inactivation gating is eliminated when the N-terminus is truncated by deleting the first 35 amino acids after the initial methionine. The inactivation gating is restored when a synthetic N-terminal peptide is applied to the truncated pumps at the intracellular surface. Truncated pumps generate no electrogenic current and exhibit an altered stoichiometry for active transport. Thus, the N-terminus of the alpha-subunit appears to act like an inactivation gate and performs a critical step in the Na(+),K(+)-ATPase pumping function. | lld:pubmed |
| pubmed-article:12507758 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12507758 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12507758 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12507758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12507758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12507758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12507758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12507758 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12507758 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12507758 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:12507758 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:12507758 | pubmed:author | pubmed-author:TakedaKazuoK | lld:pubmed |
| pubmed-article:12507758 | pubmed:author | pubmed-author:VasiletsLaris... | lld:pubmed |
| pubmed-article:12507758 | pubmed:author | pubmed-author:SchwarzWolfga... | lld:pubmed |
| pubmed-article:12507758 | pubmed:author | pubmed-author:KawamuraMasar... | lld:pubmed |
| pubmed-article:12507758 | pubmed:author | pubmed-author:WuChau HCH | lld:pubmed |
| pubmed-article:12507758 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12507758 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:12507758 | pubmed:volume | 1609 | lld:pubmed |
| pubmed-article:12507758 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12507758 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12507758 | pubmed:pagination | 55-62 | lld:pubmed |
| pubmed-article:12507758 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:meshHeading | pubmed-meshheading:12507758... | lld:pubmed |
| pubmed-article:12507758 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12507758 | pubmed:articleTitle | Functional role of the N-terminus of Na(+),K(+)-ATPase alpha-subunit as an inactivation gate of palytoxin-induced pump channel. | lld:pubmed |
| pubmed-article:12507758 | pubmed:affiliation | Department of Molecular Pharmacology and Biological Chemistry (S-215), The Feinberg School of Medicine, Northwestern University, Chicago, IL 60611-3008, USA. c-wu@northwestern.edu | lld:pubmed |
| pubmed-article:12507758 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12507758 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12507758 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12507758 | lld:pubmed |
