| pubmed-article:3328613 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C0032043 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C0242275 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C0021641 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C1135936 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C2828366 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C1705851 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C0205227 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C1555707 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C0242759 | lld:lifeskim |
| pubmed-article:3328613 | lifeskim:mentions | umls-concept:C2752151 | lld:lifeskim |
| pubmed-article:3328613 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:3328613 | pubmed:dateCreated | 1988-5-12 | lld:pubmed |
| pubmed-article:3328613 | pubmed:abstractText | 1. Triton extracts of syncytiotrophoblast membranes were incubated with [gamma-32P]ATP, MgCl2 and MnCl2. Addition of epidermal growth factor (EGF) resulted in increased phosphorylation not only of the EGF receptor and a Mr-35,000 protein as previously described, but also a protein of Mr 95,000 on both tyrosine and serine residues. In addition, a small increase in the phosphorylation of a protein of Mr 105,000 was observed. Spermine had a similar effect on the phosphorylation of the Mr-95,000 protein, without affecting the phosphorylation of the other proteins. In the absence of MnCl2, the effect of spermine on the phosphorylation of Mr-95,000 protein was still evident, whereas that of EGF was greatly diminished. 2. The Mr-95,000 protein bound poorly to wheat-germ-lectin-Sepharose and was not precipitated by antisera specific for insulin and EGF receptors. The protein continued to exhibit serine and tyrosine phosphorylation on addition of [gamma-32P]ATP, MgCl2 and MnCl2 to a glycoprotein-depleted fraction prepared by chromatography on wheat-germ-lectin-Sepharose. The extent of phosphorylation was no longer increased by spermine or EGF, but was inhibited by heparin. 3. It is suggested that the Mr-95,000 protein not only is a possible direct substrate for the EGF-receptor (but not the insulin receptor) tyrosine kinase but is a substrate for other endogenous kinases, including a protein tyrosine kinase which is probably not a glycoprotein, and a protein serine kinase with properties similar to those of casein kinase II. | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3328613 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:3328613 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3328613 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3328613 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:3328613 | pubmed:issn | 0264-6021 | lld:pubmed |
| pubmed-article:3328613 | pubmed:author | pubmed-author:DentonR MRM | lld:pubmed |
| pubmed-article:3328613 | pubmed:author | pubmed-author:DiggleT ATA | lld:pubmed |
| pubmed-article:3328613 | pubmed:author | pubmed-author:TavaréJ MJM | lld:pubmed |
| pubmed-article:3328613 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3328613 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:3328613 | pubmed:volume | 244 | lld:pubmed |
| pubmed-article:3328613 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3328613 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3328613 | pubmed:pagination | 769-74 | lld:pubmed |
| pubmed-article:3328613 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:meshHeading | pubmed-meshheading:3328613-... | lld:pubmed |
| pubmed-article:3328613 | pubmed:year | 1987 | lld:pubmed |
| pubmed-article:3328613 | pubmed:articleTitle | Epidermal growth factor, but not insulin, stimulates tyrosine phosphorylation of an endogenous protein of Mr 95,000 in triton extracts of human placental syncytiotrophoblast membranes. | lld:pubmed |
| pubmed-article:3328613 | pubmed:affiliation | Department of Biochemistry, University of Bristol Medical School, U.K. | lld:pubmed |
| pubmed-article:3328613 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:3328613 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:3328613 | lld:pubmed |
