| pubmed-article:17499849 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17499849 | lifeskim:mentions | umls-concept:C0682969 | lld:lifeskim |
| pubmed-article:17499849 | lifeskim:mentions | umls-concept:C0063592 | lld:lifeskim |
| pubmed-article:17499849 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:17499849 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:17499849 | lifeskim:mentions | umls-concept:C0220905 | lld:lifeskim |
| pubmed-article:17499849 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:17499849 | pubmed:dateCreated | 2008-1-15 | lld:pubmed |
| pubmed-article:17499849 | pubmed:abstractText | The inositol 1,4,5-trisphosphate (IP(3)) receptor (IP(3)R) can be divided in three functionally distinct regions: a ligand-binding domain, a modulatory domain and a channel domain. Numerous regulatory mechanisms including inter- and intra-molecular protein-protein interactions and phosphorylation events act via these domains to regulate the function of the IP(3)R. Regulation at the level of the ligand-binding domain primarily affects the affinity for IP(3). The extent of IP(3)-induced Ca(2+) release (IICR) is, however, not only determined by the affinity for IP(3) but also by the effectiveness of the coupling between ligand binding and channel opening. As a result, regulation as well as malfunction of IICR may be affected by both steps in the activation mechanism. The 3D structures of the two subdomains of the ligand-binding domain have recently been determined by X-ray diffraction analysis. This allows a more detailed molecular explanation of the regulatory events situated at the ligand-binding domain of the IP(3)R. In this review, we will focus on recent structural and functional data on the ligand-binding domain that have extended and clarified the view on the molecular mechanisms of IP(3)R regulation. | lld:pubmed |
| pubmed-article:17499849 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17499849 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17499849 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17499849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17499849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17499849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17499849 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17499849 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17499849 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:17499849 | pubmed:issn | 0143-4160 | lld:pubmed |
| pubmed-article:17499849 | pubmed:author | pubmed-author:ParysJan BJB | lld:pubmed |
| pubmed-article:17499849 | pubmed:author | pubmed-author:MissiaenLudwi... | lld:pubmed |
| pubmed-article:17499849 | pubmed:author | pubmed-author:De... | lld:pubmed |
| pubmed-article:17499849 | pubmed:author | pubmed-author:DevogelaereBe... | lld:pubmed |
| pubmed-article:17499849 | pubmed:author | pubmed-author:VerbertLeenL | lld:pubmed |
| pubmed-article:17499849 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17499849 | pubmed:volume | 43 | lld:pubmed |
| pubmed-article:17499849 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17499849 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17499849 | pubmed:pagination | 17-27 | lld:pubmed |
| pubmed-article:17499849 | pubmed:meshHeading | pubmed-meshheading:17499849... | lld:pubmed |
| pubmed-article:17499849 | pubmed:meshHeading | pubmed-meshheading:17499849... | lld:pubmed |
| pubmed-article:17499849 | pubmed:meshHeading | pubmed-meshheading:17499849... | lld:pubmed |
| pubmed-article:17499849 | pubmed:meshHeading | pubmed-meshheading:17499849... | lld:pubmed |
| pubmed-article:17499849 | pubmed:meshHeading | pubmed-meshheading:17499849... | lld:pubmed |
| pubmed-article:17499849 | pubmed:meshHeading | pubmed-meshheading:17499849... | lld:pubmed |
| pubmed-article:17499849 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:17499849 | pubmed:articleTitle | The complex regulatory function of the ligand-binding domain of the inositol 1,4,5-trisphosphate receptor. | lld:pubmed |
| pubmed-article:17499849 | pubmed:affiliation | Laboratory of Molecular and Cellular Signalling, Division of Physiology, Department of Molecular Cell Biology, Katholieke Universiteit Leuven, Leuven, Belgium. | lld:pubmed |
| pubmed-article:17499849 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17499849 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:17499849 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:17499849 | lld:pubmed |
