| pubmed-article:21150316 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21150316 | lifeskim:mentions | umls-concept:C0288263 | lld:lifeskim |
| pubmed-article:21150316 | lifeskim:mentions | umls-concept:C1413058 | lld:lifeskim |
| pubmed-article:21150316 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:21150316 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:21150316 | pubmed:dateCreated | 2011-1-13 | lld:pubmed |
| pubmed-article:21150316 | pubmed:abstractText | CaV1.3 L-type channels control inner hair cell (IHC) sensory and sinoatrial node (SAN) function, and excitability in central neurons by means of their low-voltage activation and inactivation properties. In SAN cells CaV1.3 inward calcium current (ICa) inactivates rapidly whereas in IHCs inactivation is slow. A candidate suggested in slowing CaV1.3 channel inactivation is the presynaptically located ribbon-synapse protein RIM that is expressed in immature IHCs in presynaptic compartments also expressing CaV1.3 channels. CaV1.3 channel gating is also modulated by an intramolecular C-terminal mechanism. This mechanism was elicited during analysis of human C-terminal splice variants that differ in the length of their C-terminus and that modulates the channel's negative activation range and slows calcium-dependent inactivation. | lld:pubmed |
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| pubmed-article:21150316 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21150316 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21150316 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21150316 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:21150316 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21150316 | pubmed:issn | 1933-6969 | lld:pubmed |
| pubmed-article:21150316 | pubmed:author | pubmed-author:KoschakAlexan... | lld:pubmed |
| pubmed-article:21150316 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21150316 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:21150316 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21150316 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21150316 | pubmed:pagination | 523-5 | lld:pubmed |
| pubmed-article:21150316 | pubmed:dateRevised | 2011-7-28 | lld:pubmed |
| pubmed-article:21150316 | pubmed:meshHeading | pubmed-meshheading:21150316... | lld:pubmed |
| pubmed-article:21150316 | pubmed:meshHeading | pubmed-meshheading:21150316... | lld:pubmed |
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| pubmed-article:21150316 | pubmed:meshHeading | pubmed-meshheading:21150316... | lld:pubmed |
| pubmed-article:21150316 | pubmed:meshHeading | pubmed-meshheading:21150316... | lld:pubmed |
| pubmed-article:21150316 | pubmed:meshHeading | pubmed-meshheading:21150316... | lld:pubmed |
| pubmed-article:21150316 | pubmed:meshHeading | pubmed-meshheading:21150316... | lld:pubmed |
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| pubmed-article:21150316 | pubmed:meshHeading | pubmed-meshheading:21150316... | lld:pubmed |
| pubmed-article:21150316 | pubmed:meshHeading | pubmed-meshheading:21150316... | lld:pubmed |
| pubmed-article:21150316 | pubmed:articleTitle | Impact of gating modulation in CaV1.3 L-type calcium channels. | lld:pubmed |
| pubmed-article:21150316 | pubmed:affiliation | Pharmacology and Toxicology, Institute of Pharmacy, University of Innsbruck, Innsbruck, Austria. alexandra.koschak@uibk.ac.at | lld:pubmed |
| pubmed-article:21150316 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21150316 | pubmed:publicationType | Review | lld:pubmed |
