| pubmed-article:9886942 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9886942 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:9886942 | lifeskim:mentions | umls-concept:C0242692 | lld:lifeskim |
| pubmed-article:9886942 | lifeskim:mentions | umls-concept:C0026882 | lld:lifeskim |
| pubmed-article:9886942 | lifeskim:mentions | umls-concept:C0238357 | lld:lifeskim |
| pubmed-article:9886942 | lifeskim:mentions | umls-concept:C0597484 | lld:lifeskim |
| pubmed-article:9886942 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:9886942 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:9886942 | pubmed:issue | 1 Pt 1 | lld:pubmed |
| pubmed-article:9886942 | pubmed:dateCreated | 1999-3-9 | lld:pubmed |
| pubmed-article:9886942 | pubmed:abstractText | Mutations in the human skeletal muscle Na+ channel underlie the autosomal dominant disease hyperkalemic periodic paralysis (HPP). Muscle fibers from affected individuals exhibit sustained Na+ currents thought to depolarize the sarcolemma and thus inactivate normal Na+ channels. We expressed human wild-type or M1592V mutant alpha-subunits with the beta1-subunit in Xenopus laevis oocytes and recorded Na+ currents using two-electrode and cut-open oocyte voltage-clamp techniques. The most prominent functional difference between M1592V mutant and wild-type channels is a 5- to 10-mV shift in the hyperpolarized direction of the steady-state activation curve. The shift in the activation curve for the mutant results in a larger overlap with the inactivation curve than that observed for wild-type channels. Accordingly, the current through M1592V channels displays a larger noninactivating component than does that through wild-type channels at membrane potentials near -40 mV. The functional properties of the M1592V mutant resemble those of the previously characterized HPP T704M mutant. Both clinically similar phenotypes arise from mutations located at a distance from the putative voltage sensor of the channel. | lld:pubmed |
| pubmed-article:9886942 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9886942 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9886942 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9886942 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9886942 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9886942 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:9886942 | pubmed:issn | 0002-9513 | lld:pubmed |
| pubmed-article:9886942 | pubmed:author | pubmed-author:PalmaVV | lld:pubmed |
| pubmed-article:9886942 | pubmed:author | pubmed-author:RojasC VCV | lld:pubmed |
| pubmed-article:9886942 | pubmed:author | pubmed-author:KukuljanMM | lld:pubmed |
| pubmed-article:9886942 | pubmed:author | pubmed-author:NeelyAA | lld:pubmed |
| pubmed-article:9886942 | pubmed:author | pubmed-author:Velasco-Loyde... | lld:pubmed |
| pubmed-article:9886942 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9886942 | pubmed:volume | 276 | lld:pubmed |
| pubmed-article:9886942 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9886942 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9886942 | pubmed:pagination | C259-66 | lld:pubmed |
| pubmed-article:9886942 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:meshHeading | pubmed-meshheading:9886942-... | lld:pubmed |
| pubmed-article:9886942 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:9886942 | pubmed:articleTitle | Hyperkalemic periodic paralysis M1592V mutation modifies activation in human skeletal muscle Na+ channel. | lld:pubmed |
| pubmed-article:9886942 | pubmed:affiliation | Instituto de Nutrición y Tecnología de los Alimentos, Universidad de Chile, Casilla 138-11, Santiago, Chile. | lld:pubmed |
| pubmed-article:9886942 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9886942 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:9886942 | lld:pubmed |
