| pubmed-article:2000401 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2000401 | lifeskim:mentions | umls-concept:C1273518 | lld:lifeskim |
| pubmed-article:2000401 | lifeskim:mentions | umls-concept:C1155437 | lld:lifeskim |
| pubmed-article:2000401 | lifeskim:mentions | umls-concept:C0599740 | lld:lifeskim |
| pubmed-article:2000401 | lifeskim:mentions | umls-concept:C0057224 | lld:lifeskim |
| pubmed-article:2000401 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:2000401 | pubmed:dateCreated | 1991-4-11 | lld:pubmed |
| pubmed-article:2000401 | pubmed:abstractText | Protein kinase C is physiologically activated by 1,2-diacyl-sn-glycerol in the S configuration. The enzyme is also powerfully activated by structurally diverse tumor promotors. A model has been developed that demonstrates how the various tumor promotors and diacylglycerols can all be accommodated by the same binding site of the kinase. One prediction of this model concerns the structural nature of the pharmacophore in the tumor promotor debromoaplysiatoxin. This prediction is realized by synthesizing the analogs with the deduced pharmacophore and demonstrating that they are potent activators of protein kinase C. These findings provide strong experimental support for our structural model of protein kinase C activation. | lld:pubmed |
| pubmed-article:2000401 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2000401 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2000401 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2000401 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2000401 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2000401 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2000401 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2000401 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2000401 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:2000401 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:2000401 | pubmed:author | pubmed-author:RandoR RRR | lld:pubmed |
| pubmed-article:2000401 | pubmed:author | pubmed-author:KishiYY | lld:pubmed |
| pubmed-article:2000401 | pubmed:author | pubmed-author:KongF HFH | lld:pubmed |
| pubmed-article:2000401 | pubmed:author | pubmed-author:Perez-SalaDD | lld:pubmed |
| pubmed-article:2000401 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2000401 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:2000401 | pubmed:volume | 88 | lld:pubmed |
| pubmed-article:2000401 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2000401 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2000401 | pubmed:pagination | 1973-6 | lld:pubmed |
| pubmed-article:2000401 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:2000401 | pubmed:meshHeading | pubmed-meshheading:2000401-... | lld:pubmed |
| pubmed-article:2000401 | pubmed:meshHeading | pubmed-meshheading:2000401-... | lld:pubmed |
| pubmed-article:2000401 | pubmed:meshHeading | pubmed-meshheading:2000401-... | lld:pubmed |
| pubmed-article:2000401 | pubmed:meshHeading | pubmed-meshheading:2000401-... | lld:pubmed |
| pubmed-article:2000401 | pubmed:meshHeading | pubmed-meshheading:2000401-... | lld:pubmed |
| pubmed-article:2000401 | pubmed:meshHeading | pubmed-meshheading:2000401-... | lld:pubmed |
| pubmed-article:2000401 | pubmed:meshHeading | pubmed-meshheading:2000401-... | lld:pubmed |
| pubmed-article:2000401 | pubmed:meshHeading | pubmed-meshheading:2000401-... | lld:pubmed |
| pubmed-article:2000401 | pubmed:meshHeading | pubmed-meshheading:2000401-... | lld:pubmed |
| pubmed-article:2000401 | pubmed:meshHeading | pubmed-meshheading:2000401-... | lld:pubmed |
| pubmed-article:2000401 | pubmed:meshHeading | pubmed-meshheading:2000401-... | lld:pubmed |
| pubmed-article:2000401 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:2000401 | pubmed:articleTitle | The pharmacophore of debromoaplysiatoxin responsible for protein kinase C activation. | lld:pubmed |
| pubmed-article:2000401 | pubmed:affiliation | Department of Chemistry, Harvard University, Cambridge, MA 02138. | lld:pubmed |
| pubmed-article:2000401 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2000401 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:2000401 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:2000401 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
