pubmed-article:3017977 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:3017977 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
pubmed-article:3017977 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:3017977 | lifeskim:mentions | umls-concept:C0010453 | lld:lifeskim |
pubmed-article:3017977 | lifeskim:mentions | umls-concept:C0018557 | lld:lifeskim |
pubmed-article:3017977 | lifeskim:mentions | umls-concept:C0034802 | lld:lifeskim |
pubmed-article:3017977 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
pubmed-article:3017977 | lifeskim:mentions | umls-concept:C1442161 | lld:lifeskim |
pubmed-article:3017977 | pubmed:issue | 27 | lld:pubmed |
pubmed-article:3017977 | pubmed:dateCreated | 1986-10-23 | lld:pubmed |
pubmed-article:3017977 | pubmed:abstractText | DNA sequences encoding the human epidermal growth factor (EGF) receptor and various EGF-receptor deletion mutants were transfected into chinese hamster ovary (CHO) cells devoid of endogenous EGF receptors. A functional human EGF-receptor is expressed on the surface of heterologous CHO cells with the following properties: it exhibits typical high affinity (10%; Kd = 3 X 10(-10) M) and low affinity (90%; Kd = 3 X 10(-9) M) binding sites for 125I-EGF; it is expressed as a polypeptide of 170,000 molecular weight with intrinsic protein tyrosine kinase activity. EGF stimulates the kinase activity leading to self-phosphorylation and to phosphorylation of exogenous substrate; 125I-EGF is rapidly internalized into the CHO cells by receptor mediated endocytosis and; EGF stimulates DNA synthesis in the cells expressing the human EGF-receptor. Deletion of 63 amino acids from the C-terminal end of EGF-receptor, which removes two autophosphorylation sites, abolishes the high affinity state of the receptor. Nevertheless, this receptor mutant is able to undergo endocytosis and to respond mitogenically to EGF to a similar extent as the "wild type" receptor. Further deletions from the cytoplasmic domain give rise to low affinity endocytosis-defective receptor mutants. Finally, deletion of the transmembrane domain of the human receptor yields an EGF-receptor ligand binding domain which is secreted from the cells. | lld:pubmed |
pubmed-article:3017977 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3017977 | pubmed:language | eng | lld:pubmed |
pubmed-article:3017977 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3017977 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:3017977 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3017977 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3017977 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3017977 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3017977 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3017977 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:3017977 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:3017977 | pubmed:month | Sep | lld:pubmed |
pubmed-article:3017977 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:3017977 | pubmed:author | pubmed-author:SchlessingerJ... | lld:pubmed |
pubmed-article:3017977 | pubmed:author | pubmed-author:PrywesRR | lld:pubmed |
pubmed-article:3017977 | pubmed:author | pubmed-author:UllrichAA | lld:pubmed |
pubmed-article:3017977 | pubmed:author | pubmed-author:LivnehEE | lld:pubmed |
pubmed-article:3017977 | pubmed:author | pubmed-author:PUCAF MFM | lld:pubmed |
pubmed-article:3017977 | pubmed:author | pubmed-author:ReiszEE | lld:pubmed |
pubmed-article:3017977 | pubmed:author | pubmed-author:KashlesOO | lld:pubmed |
pubmed-article:3017977 | pubmed:author | pubmed-author:SassonII | lld:pubmed |
pubmed-article:3017977 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:3017977 | pubmed:day | 25 | lld:pubmed |
pubmed-article:3017977 | pubmed:volume | 261 | lld:pubmed |
pubmed-article:3017977 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:3017977 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:3017977 | pubmed:pagination | 12490-7 | lld:pubmed |
pubmed-article:3017977 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:3017977 | pubmed:meshHeading | pubmed-meshheading:3017977-... | lld:pubmed |
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pubmed-article:3017977 | pubmed:meshHeading | pubmed-meshheading:3017977-... | lld:pubmed |
pubmed-article:3017977 | pubmed:year | 1986 | lld:pubmed |
pubmed-article:3017977 | pubmed:articleTitle | Reconstitution of human epidermal growth factor receptors and its deletion mutants in cultured hamster cells. | lld:pubmed |
pubmed-article:3017977 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:3017977 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:3017977 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:3017977 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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