pubmed-article:1961249 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1961249 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
pubmed-article:1961249 | lifeskim:mentions | umls-concept:C0031760 | lld:lifeskim |
pubmed-article:1961249 | lifeskim:mentions | umls-concept:C0178702 | lld:lifeskim |
pubmed-article:1961249 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:1961249 | lifeskim:mentions | umls-concept:C0013138 | lld:lifeskim |
pubmed-article:1961249 | lifeskim:mentions | umls-concept:C0439831 | lld:lifeskim |
pubmed-article:1961249 | pubmed:issue | 6350 | lld:pubmed |
pubmed-article:1961249 | pubmed:dateCreated | 1992-1-7 | lld:pubmed |
pubmed-article:1961249 | pubmed:abstractText | CALCIUM is involved in the adaptation of vertebrate photoreceptors to light and may have a similar role in invertebrate phototransduction. But the molecular mechanisms mediating this stimulus-dependent regulation are not well understood in any G protein-coupled transduction system. We have developed a preparation of isolated Drosophila photoreceptors that has allowed us to carry out an electrophysiological characterization of the light-activated response in these sensory neurons using patch-clamp techniques. We report here that extracellular calcium entering through the light-activated conductance is a key regulator of both the activation and deactivation phases of the phototransduction cascade, and that inaC mutant photoreceptors are specifically defective in the calcium-dependent deactivation mechanism. These data suggest that the light-dependent calcium influx inactivates this cascade through a biochemical pathway that requires the inaC gene product, and that this mechanism represents a molecular basis for stimulus-dependent regulation of visual transduction in Drosophila photoreceptors. | lld:pubmed |
pubmed-article:1961249 | pubmed:language | eng | lld:pubmed |
pubmed-article:1961249 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1961249 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:1961249 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1961249 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1961249 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1961249 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1961249 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1961249 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1961249 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:1961249 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1961249 | pubmed:month | Nov | lld:pubmed |
pubmed-article:1961249 | pubmed:issn | 0028-0836 | lld:pubmed |
pubmed-article:1961249 | pubmed:author | pubmed-author:HarrisG LGL | lld:pubmed |
pubmed-article:1961249 | pubmed:author | pubmed-author:StevensC FCF | lld:pubmed |
pubmed-article:1961249 | pubmed:author | pubmed-author:RanganathanRR | lld:pubmed |
pubmed-article:1961249 | pubmed:author | pubmed-author:ZukerC SCS | lld:pubmed |
pubmed-article:1961249 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1961249 | pubmed:day | 21 | lld:pubmed |
pubmed-article:1961249 | pubmed:volume | 354 | lld:pubmed |
pubmed-article:1961249 | pubmed:geneSymbol | inaC | lld:pubmed |
pubmed-article:1961249 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1961249 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1961249 | pubmed:pagination | 230-2 | lld:pubmed |
pubmed-article:1961249 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
pubmed-article:1961249 | pubmed:meshHeading | pubmed-meshheading:1961249-... | lld:pubmed |
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pubmed-article:1961249 | pubmed:meshHeading | pubmed-meshheading:1961249-... | lld:pubmed |
pubmed-article:1961249 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1961249 | pubmed:articleTitle | A Drosophila mutant defective in extracellular calcium-dependent photoreceptor deactivation and rapid desensitization. | lld:pubmed |
pubmed-article:1961249 | pubmed:affiliation | Howard Hughes Medical Institute, San Diego, La Jolla, California. | lld:pubmed |
pubmed-article:1961249 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:1961249 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:1961249 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:1961249 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
entrez-gene:36897 | entrezgene:pubmed | pubmed-article:1961249 | lld:entrezgene |
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