| pubmed-article:2471190 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2471190 | lifeskim:mentions | umls-concept:C0206427 | lld:lifeskim |
| pubmed-article:2471190 | lifeskim:mentions | umls-concept:C0018338 | lld:lifeskim |
| pubmed-article:2471190 | lifeskim:mentions | umls-concept:C0031640 | lld:lifeskim |
| pubmed-article:2471190 | lifeskim:mentions | umls-concept:C0035331 | lld:lifeskim |
| pubmed-article:2471190 | lifeskim:mentions | umls-concept:C0439851 | lld:lifeskim |
| pubmed-article:2471190 | lifeskim:mentions | umls-concept:C0439799 | lld:lifeskim |
| pubmed-article:2471190 | lifeskim:mentions | umls-concept:C1552596 | lld:lifeskim |
| pubmed-article:2471190 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:2471190 | lifeskim:mentions | umls-concept:C1947931 | lld:lifeskim |
| pubmed-article:2471190 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:2471190 | pubmed:dateCreated | 1989-6-28 | lld:pubmed |
| pubmed-article:2471190 | pubmed:abstractText | The cationic conductances of purified bovine retinal rod membranes were studied by incorporation of vesicles into planar lipid bilayers. When the membranes were stripped of all peripheral proteins [guanine nucleotide-binding protein (G protein) and cGMP phosphodiesterase (3',5'-cyclic-GMP 5'-nucleotidohydrolase), EC 3.1.4.35], sodium and calcium fluxes were almost only observed in the presence of cGMP. Reconstitution experiments in which purified cGMP phosphodiesterase alone or with G protein were reassociated to the vesicles in proportions similar to those found in the native rod provide evidence for a direct interaction between the cGMP-dependent channel protein and the phosphodiesterase. (i) In its inhibited state, phosphodiesterase markedly stimulates the activity of the channels in the presence of cGMP (situation in the dark-adapted rod) but is not capable of activating the channels in the absence of cGMP. (ii) In the absence of cGMP, activation of the phosphodiesterase by G protein with GTP bound (equivalent to photoexcitation) induces the opening of cation channels that have the same conductance for sodium ions as cGMP-activated channels (20-22 pS, with two sublevels of about 7 pS and 13 pS). | lld:pubmed |
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| pubmed-article:2471190 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2471190 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2471190 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2471190 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2471190 | pubmed:month | May | lld:pubmed |
| pubmed-article:2471190 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2471190 | pubmed:author | pubmed-author:BennettNN | lld:pubmed |
| pubmed-article:2471190 | pubmed:author | pubmed-author:ChapronYY | lld:pubmed |
| pubmed-article:2471190 | pubmed:author | pubmed-author:IldefonseMM | lld:pubmed |
| pubmed-article:2471190 | pubmed:author | pubmed-author:ClercAA | lld:pubmed |
| pubmed-article:2471190 | pubmed:author | pubmed-author:CrouzySS | lld:pubmed |
| pubmed-article:2471190 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2471190 | pubmed:volume | 86 | lld:pubmed |
| pubmed-article:2471190 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2471190 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2471190 | pubmed:pagination | 3634-8 | lld:pubmed |
| pubmed-article:2471190 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:2471190 | pubmed:meshHeading | pubmed-meshheading:2471190-... | lld:pubmed |
| pubmed-article:2471190 | pubmed:year | 1989 | lld:pubmed |
| pubmed-article:2471190 | pubmed:articleTitle | Direct activation of cGMP-dependent channels of retinal rods by the cGMP phosphodiesterase. | lld:pubmed |
| pubmed-article:2471190 | pubmed:affiliation | Centre National de la Recherche Scentifique, URA 520, Centre d'Etudes Nucléaires de Grenoble, France. | lld:pubmed |
| pubmed-article:2471190 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2471190 | pubmed:publicationType | In Vitro | lld:pubmed |
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