| pubmed-article:18618700 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18618700 | lifeskim:mentions | umls-concept:C0018787 | lld:lifeskim |
| pubmed-article:18618700 | lifeskim:mentions | umls-concept:C0022009 | lld:lifeskim |
| pubmed-article:18618700 | lifeskim:mentions | umls-concept:C1419778 | lld:lifeskim |
| pubmed-article:18618700 | lifeskim:mentions | umls-concept:C0039808 | lld:lifeskim |
| pubmed-article:18618700 | lifeskim:mentions | umls-concept:C1149164 | lld:lifeskim |
| pubmed-article:18618700 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:18618700 | pubmed:dateCreated | 2008-12-17 | lld:pubmed |
| pubmed-article:18618700 | pubmed:abstractText | The skeletal muscle (RyR1) and cardiac muscle (RyR2) ryanodine receptor calcium release channels contain a single, conserved calmodulin (CaM) binding domain, yet are differentially regulated by CaM. Here, we report that high-affinity [(35)S]CaM binding to RyR1 is driven by favorable enthalpic and entropic contributions at Ca(2+) concentrations from <0.01 to 100 microM. At 0.15 microM Ca(2+), [(35)S]CaM bound to RyR2 with decreased affinity and binding enthalpy compared with RyR1. The rates of [(35)S]CaM dissociation from RyR1 increased as the temperature was raised, whereas at 0.15 microM Ca(2+) the rate from RyR2 was little affected. The results suggest major differences in the energetics of CaM binding to and dissociation from RyR1 and RyR2. | lld:pubmed |
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| pubmed-article:18618700 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18618700 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18618700 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18618700 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18618700 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18618700 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18618700 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18618700 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:18618700 | pubmed:issn | 1097-0134 | lld:pubmed |
| pubmed-article:18618700 | pubmed:author | pubmed-author:MeissnerGerha... | lld:pubmed |
| pubmed-article:18618700 | pubmed:author | pubmed-author:DokholyanNiko... | lld:pubmed |
| pubmed-article:18618700 | pubmed:author | pubmed-author:TripathyAshut... | lld:pubmed |
| pubmed-article:18618700 | pubmed:author | pubmed-author:YamaguchiNaoh... | lld:pubmed |
| pubmed-article:18618700 | pubmed:author | pubmed-author:PasekDaniel... | lld:pubmed |
| pubmed-article:18618700 | pubmed:author | pubmed-author:RamachandranS... | lld:pubmed |
| pubmed-article:18618700 | pubmed:copyrightInfo | (c) 2008 Wiley-Liss, Inc. | lld:pubmed |
| pubmed-article:18618700 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18618700 | pubmed:volume | 74 | lld:pubmed |
| pubmed-article:18618700 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18618700 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18618700 | pubmed:pagination | 207-11 | lld:pubmed |
| pubmed-article:18618700 | pubmed:dateRevised | 2011-11-14 | lld:pubmed |
| pubmed-article:18618700 | pubmed:meshHeading | pubmed-meshheading:18618700... | lld:pubmed |
| pubmed-article:18618700 | pubmed:meshHeading | pubmed-meshheading:18618700... | lld:pubmed |
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| pubmed-article:18618700 | pubmed:meshHeading | pubmed-meshheading:18618700... | lld:pubmed |
| pubmed-article:18618700 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:18618700 | pubmed:articleTitle | Thermodynamics of calmodulin binding to cardiac and skeletal muscle ryanodine receptor ion channels. | lld:pubmed |
| pubmed-article:18618700 | pubmed:affiliation | Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599-7260, USA. meissner@med.unc.edu | lld:pubmed |
| pubmed-article:18618700 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18618700 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:18618700 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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