| pubmed-article:7774668 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7774668 | lifeskim:mentions | umls-concept:C0020291 | lld:lifeskim |
| pubmed-article:7774668 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:7774668 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:7774668 | lifeskim:mentions | umls-concept:C1334043 | lld:lifeskim |
| pubmed-article:7774668 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:7774668 | pubmed:dateCreated | 1995-7-11 | lld:pubmed |
| pubmed-article:7774668 | pubmed:abstractText | Signal transduction at a diverse range of pharmacologically distinct receptors is effected by the enhanced turnover of inositol phospholipids, with the attendant formation of inositol 1,4,5-trisphosphate and diacylglycerol. Although considerable progress has been made in recent years towards the identification and characterization of the individual components of this pathway, much less is known of mechanisms that may underlie its regulation. In this review, evidence is presented for the potential regulation of inositol lipid turnover at the level of receptor, phosphoinositide-specific phospholipase C and substrate availability in response to either homologous or heterologous stimuli. Available data indicate that the extent of receptor-stimulated inositol lipid hydrolysis is regulated by multiple mechanisms that operate at different levels of the signal transduction pathway. | lld:pubmed |
| pubmed-article:7774668 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7774668 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7774668 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7774668 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7774668 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7774668 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7774668 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7774668 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7774668 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7774668 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7774668 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7774668 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:7774668 | pubmed:issn | 0014-2999 | lld:pubmed |
| pubmed-article:7774668 | pubmed:author | pubmed-author:FisherS KSK | lld:pubmed |
| pubmed-article:7774668 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7774668 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:7774668 | pubmed:volume | 288 | lld:pubmed |
| pubmed-article:7774668 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7774668 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7774668 | pubmed:pagination | 231-50 | lld:pubmed |
| pubmed-article:7774668 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:7774668 | pubmed:meshHeading | pubmed-meshheading:7774668-... | lld:pubmed |
| pubmed-article:7774668 | pubmed:meshHeading | pubmed-meshheading:7774668-... | lld:pubmed |
| pubmed-article:7774668 | pubmed:meshHeading | pubmed-meshheading:7774668-... | lld:pubmed |
| pubmed-article:7774668 | pubmed:meshHeading | pubmed-meshheading:7774668-... | lld:pubmed |
| pubmed-article:7774668 | pubmed:meshHeading | pubmed-meshheading:7774668-... | lld:pubmed |
| pubmed-article:7774668 | pubmed:meshHeading | pubmed-meshheading:7774668-... | lld:pubmed |
| pubmed-article:7774668 | pubmed:meshHeading | pubmed-meshheading:7774668-... | lld:pubmed |
| pubmed-article:7774668 | pubmed:meshHeading | pubmed-meshheading:7774668-... | lld:pubmed |
| pubmed-article:7774668 | pubmed:meshHeading | pubmed-meshheading:7774668-... | lld:pubmed |
| pubmed-article:7774668 | pubmed:meshHeading | pubmed-meshheading:7774668-... | lld:pubmed |
| pubmed-article:7774668 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:7774668 | pubmed:articleTitle | Homologous and heterologous regulation of receptor-stimulated phosphoinositide hydrolysis. | lld:pubmed |
| pubmed-article:7774668 | pubmed:affiliation | Neuroscience Laboratory, University of Michigan, Ann Arbor 48104-1687, USA. | lld:pubmed |
| pubmed-article:7774668 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7774668 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7774668 | pubmed:publicationType | Review | lld:pubmed |
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