| pubmed-article:1848515 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1848515 | lifeskim:mentions | umls-concept:C0332307 | lld:lifeskim |
| pubmed-article:1848515 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:1848515 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:1848515 | lifeskim:mentions | umls-concept:C0013935 | lld:lifeskim |
| pubmed-article:1848515 | lifeskim:mentions | umls-concept:C0016030 | lld:lifeskim |
| pubmed-article:1848515 | lifeskim:mentions | umls-concept:C0033634 | lld:lifeskim |
| pubmed-article:1848515 | lifeskim:mentions | umls-concept:C0282498 | lld:lifeskim |
| pubmed-article:1848515 | lifeskim:mentions | umls-concept:C1515926 | lld:lifeskim |
| pubmed-article:1848515 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1848515 | pubmed:dateCreated | 1991-4-22 | lld:pubmed |
| pubmed-article:1848515 | pubmed:abstractText | Heat shock treatment of rat embryo fibroblasts resulted in a 60% increase in cytosolic protein kinase C activity, in contrast to phorbol ester-induced translocation to the membrane. During reversal of the cells back to the normal temperature a decrease in cytosolic PKC activity was observed and paralleled by an increase in protamine kinase activity. Cell lysates prepared from heat shock-treated cells show a marked calcium/phospholipid-dependent phosphorylation of several endogenous PKC substrate proteins, while the 28-kDa stress protein was shown to be a PKC substrate. These cells express the TYPE III-alpha isoform of PKC and, thus, the alterations induced within cells exposed to hyperthermic treatment may reflect a functional significance with regard to the regulation of this specific isoform. | lld:pubmed |
| pubmed-article:1848515 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848515 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848515 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1848515 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848515 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1848515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848515 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1848515 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1848515 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:1848515 | pubmed:issn | 0014-4827 | lld:pubmed |
| pubmed-article:1848515 | pubmed:author | pubmed-author:WootenM WMW | lld:pubmed |
| pubmed-article:1848515 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1848515 | pubmed:volume | 193 | lld:pubmed |
| pubmed-article:1848515 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1848515 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1848515 | pubmed:pagination | 274-8 | lld:pubmed |
| pubmed-article:1848515 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:meshHeading | pubmed-meshheading:1848515-... | lld:pubmed |
| pubmed-article:1848515 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1848515 | pubmed:articleTitle | Alterations in protein kinase C type III-alpha during heat shock of rat embryo fibroblasts. | lld:pubmed |
| pubmed-article:1848515 | pubmed:affiliation | Auburn University, Department of Zoology & Wildlife Science, Alabama 36849-5414. | lld:pubmed |
| pubmed-article:1848515 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1848515 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:1848515 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1848515 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
