pubmed-article:8749392 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8749392 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
pubmed-article:8749392 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
pubmed-article:8749392 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
pubmed-article:8749392 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
pubmed-article:8749392 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:8749392 | pubmed:dateCreated | 1997-2-6 | lld:pubmed |
pubmed-article:8749392 | pubmed:abstractText | Protein kinase Cs are a family of enzymes that transduce the plethora of signals promoting lipid hydrolysis. Here, we show that protein kinase C must first be processed by three distinct phosphorylations before it is competent to respond to second messengers. | lld:pubmed |
pubmed-article:8749392 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8749392 | pubmed:language | eng | lld:pubmed |
pubmed-article:8749392 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8749392 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8749392 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8749392 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8749392 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8749392 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8749392 | pubmed:month | Dec | lld:pubmed |
pubmed-article:8749392 | pubmed:issn | 0960-9822 | lld:pubmed |
pubmed-article:8749392 | pubmed:author | pubmed-author:NewtonA CAC | lld:pubmed |
pubmed-article:8749392 | pubmed:author | pubmed-author:KeranenL MLM | lld:pubmed |
pubmed-article:8749392 | pubmed:author | pubmed-author:DutilE MEM | lld:pubmed |
pubmed-article:8749392 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8749392 | pubmed:day | 1 | lld:pubmed |
pubmed-article:8749392 | pubmed:volume | 5 | lld:pubmed |
pubmed-article:8749392 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8749392 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8749392 | pubmed:pagination | 1394-1403 | lld:pubmed |
pubmed-article:8749392 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
pubmed-article:8749392 | pubmed:meshHeading | pubmed-meshheading:8749392-... | lld:pubmed |
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pubmed-article:8749392 | pubmed:meshHeading | pubmed-meshheading:8749392-... | lld:pubmed |
pubmed-article:8749392 | pubmed:year | 1995 | lld:pubmed |
pubmed-article:8749392 | pubmed:articleTitle | Protein kinase C is regulated in vivo by three functionally distinct phosphorylations. | lld:pubmed |
pubmed-article:8749392 | pubmed:affiliation | Department of Pharmacology, University of California at San Diego, La Jolla 92093-0640, USA. | lld:pubmed |
pubmed-article:8749392 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8749392 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8749392 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
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