| pubmed-article:10428816 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10428816 | lifeskim:mentions | umls-concept:C1882598 | lld:lifeskim |
| pubmed-article:10428816 | lifeskim:mentions | umls-concept:C0006685 | lld:lifeskim |
| pubmed-article:10428816 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:10428816 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:10428816 | lifeskim:mentions | umls-concept:C2003941 | lld:lifeskim |
| pubmed-article:10428816 | lifeskim:mentions | umls-concept:C0439064 | lld:lifeskim |
| pubmed-article:10428816 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:10428816 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:10428816 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:10428816 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:10428816 | pubmed:issue | 32 | lld:pubmed |
| pubmed-article:10428816 | pubmed:dateCreated | 1999-9-2 | lld:pubmed |
| pubmed-article:10428816 | pubmed:abstractText | We have investigated the molecular determinants that mediate the differences in voltage-dependent inactivation properties between rapidly inactivating (R-type) alpha(1E) and noninactivating (L-type) alpha(1C) calcium channels. When coexpressed in human embryonic kidney cells with ancillary beta(1b) and alpha(2)-delta subunits, the wild type channels exhibit dramatically different inactivation properties; the half-inactivation potential of alpha(1E) is 45 mV more negative than that observed with alpha(1C), and during a 150-ms test depolarization, alpha(1E) undergoes 65% inactivation compared with only about 15% for alpha(1C). To define the structural determinants that govern these intrinsic differences, we have created a series of chimeric calcium channel alpha(1) subunits that combine the major structural domains of the two wild type channels, and we investigated their voltage-dependent inactivation properties. Each of the four transmembrane domains significantly affected the half-inactivation potential, with domains II and III being most critical. In particular, substitution of alpha(1C) sequence in domains II or III with that of alpha(1E) resulted in 25-mV negative shifts in half-inactivation potential. Similarly, the differences in inactivation rate were predominantly governed by transmembrane domains II and III and to some extent by domain IV. Thus, voltage-dependent inactivation of alpha(1E) channels is a complex process that involves multiple structural domains and possibly a global conformational change in the channel protein. | lld:pubmed |
| pubmed-article:10428816 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10428816 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10428816 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10428816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10428816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10428816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10428816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10428816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10428816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10428816 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10428816 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10428816 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10428816 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:10428816 | pubmed:author | pubmed-author:ZamponiG WGW | lld:pubmed |
| pubmed-article:10428816 | pubmed:author | pubmed-author:SpaetgensR... | lld:pubmed |
| pubmed-article:10428816 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10428816 | pubmed:day | 6 | lld:pubmed |
| pubmed-article:10428816 | pubmed:volume | 274 | lld:pubmed |
| pubmed-article:10428816 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10428816 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10428816 | pubmed:pagination | 22428-36 | lld:pubmed |
| pubmed-article:10428816 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:meshHeading | pubmed-meshheading:10428816... | lld:pubmed |
| pubmed-article:10428816 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10428816 | pubmed:articleTitle | Multiple structural domains contribute to voltage-dependent inactivation of rat brain alpha(1E) calcium channels. | lld:pubmed |
| pubmed-article:10428816 | pubmed:affiliation | Department of Pharmacology and Therapeutics, Neuroscience Research Group, University of Calgary, Calgary, Alberta T2N 4N1, Canada. | lld:pubmed |
| pubmed-article:10428816 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10428816 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:10428816 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10428816 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10428816 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10428816 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10428816 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10428816 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10428816 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10428816 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:10428816 | lld:pubmed |
