pubmed-article:2884992 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2884992 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:2884992 | lifeskim:mentions | umls-concept:C0005821 | lld:lifeskim |
pubmed-article:2884992 | lifeskim:mentions | umls-concept:C0006772 | lld:lifeskim |
pubmed-article:2884992 | lifeskim:mentions | umls-concept:C1261322 | lld:lifeskim |
pubmed-article:2884992 | lifeskim:mentions | umls-concept:C1151017 | lld:lifeskim |
pubmed-article:2884992 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
pubmed-article:2884992 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:2884992 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2884992 | pubmed:dateCreated | 1987-7-17 | lld:pubmed |
pubmed-article:2884992 | pubmed:abstractText | Both soluble and particulate forms of human platelet guanylate cyclase were found to be sensitive to sub-micromolar concentrations of free Ca2+; soluble enzyme activity increased as Ca2+ was increased from 10 nM to 1 microM; particulate enzyme activity showed a biphasic response to Ca2+, with maximal enzyme activity between 1 and 10 nM free Ca2+ and inhibition occurring at higher Ca2+ concentrations. Neither Ca2+-sensitivity appeared to be calmodulin-dependent. | lld:pubmed |
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pubmed-article:2884992 | pubmed:language | eng | lld:pubmed |
pubmed-article:2884992 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2884992 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2884992 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2884992 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2884992 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2884992 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2884992 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2884992 | pubmed:month | Mar | lld:pubmed |
pubmed-article:2884992 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:2884992 | pubmed:author | pubmed-author:Mac NeilSS | lld:pubmed |
pubmed-article:2884992 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2884992 | pubmed:day | 1 | lld:pubmed |
pubmed-article:2884992 | pubmed:volume | 242 | lld:pubmed |
pubmed-article:2884992 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2884992 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2884992 | pubmed:pagination | 607-10 | lld:pubmed |
pubmed-article:2884992 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
pubmed-article:2884992 | pubmed:meshHeading | pubmed-meshheading:2884992-... | lld:pubmed |
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pubmed-article:2884992 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:2884992 | pubmed:articleTitle | Investigation of the role of Ca2+ and calmodulin in the regulation of platelet guanylate cyclase activity. | lld:pubmed |
pubmed-article:2884992 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2884992 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |