pubmed-article:3542568 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3542568 | lifeskim:mentions | umls-concept:C0242275 | lld:lifeskim |
pubmed-article:3542568 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
pubmed-article:3542568 | lifeskim:mentions | umls-concept:C0021641 | lld:lifeskim |
pubmed-article:3542568 | lifeskim:mentions | umls-concept:C1882726 | lld:lifeskim |
pubmed-article:3542568 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
pubmed-article:3542568 | lifeskim:mentions | umls-concept:C0017968 | lld:lifeskim |
pubmed-article:3542568 | lifeskim:mentions | umls-concept:C0033681 | lld:lifeskim |
pubmed-article:3542568 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
pubmed-article:3542568 | lifeskim:mentions | umls-concept:C2700400 | lld:lifeskim |
pubmed-article:3542568 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:3542568 | pubmed:dateCreated | 1987-3-23 | lld:pubmed |
pubmed-article:3542568 | pubmed:abstractText | The receptors for insulin and epidermal growth factor possess tyrosine-specific protein kinase activity which may play a role in mediating the biological actions of these two peptides. We have identified a 120 kDa glycoprotein (pp120) in rat liver plasma membranes which can be phosphorylated by the insulin receptor in a cell-free system and in intact cultured hepatoma cells. In the present report, we have demonstrated in a cell-free system that solubilized epidermal growth factor receptors can phosphorylate tyrosine residues in pp120. | lld:pubmed |
pubmed-article:3542568 | pubmed:language | eng | lld:pubmed |
pubmed-article:3542568 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3542568 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3542568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3542568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:3542568 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3542568 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3542568 | pubmed:month | Feb | lld:pubmed |
pubmed-article:3542568 | pubmed:issn | 0014-5793 | lld:pubmed |
pubmed-article:3542568 | pubmed:author | pubmed-author:TaylorS ISI | lld:pubmed |
pubmed-article:3542568 | pubmed:author | pubmed-author:PerrottiNN | lld:pubmed |
pubmed-article:3542568 | pubmed:author | pubmed-author:PhillipsS ASA | lld:pubmed |
pubmed-article:3542568 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3542568 | pubmed:day | 9 | lld:pubmed |
pubmed-article:3542568 | pubmed:volume | 212 | lld:pubmed |
pubmed-article:3542568 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3542568 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3542568 | pubmed:pagination | 141-4 | lld:pubmed |
pubmed-article:3542568 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
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pubmed-article:3542568 | pubmed:meshHeading | pubmed-meshheading:3542568-... | lld:pubmed |
pubmed-article:3542568 | pubmed:year | 1987 | lld:pubmed |
pubmed-article:3542568 | pubmed:articleTitle | Rat liver membranes contain a 120 kDa glycoprotein which serves as a substrate for the tyrosine kinases of the receptors for insulin and epidermal growth factor. | lld:pubmed |
pubmed-article:3542568 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3542568 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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