pubmed-article:9049300 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9049300 | lifeskim:mentions | umls-concept:C0242275 | lld:lifeskim |
pubmed-article:9049300 | lifeskim:mentions | umls-concept:C0035687 | lld:lifeskim |
pubmed-article:9049300 | lifeskim:mentions | umls-concept:C0597298 | lld:lifeskim |
pubmed-article:9049300 | lifeskim:mentions | umls-concept:C1280500 | lld:lifeskim |
pubmed-article:9049300 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
pubmed-article:9049300 | lifeskim:mentions | umls-concept:C1704259 | lld:lifeskim |
pubmed-article:9049300 | lifeskim:mentions | umls-concept:C1705987 | lld:lifeskim |
pubmed-article:9049300 | lifeskim:mentions | umls-concept:C1521805 | lld:lifeskim |
pubmed-article:9049300 | pubmed:issue | 4 | lld:pubmed |
pubmed-article:9049300 | pubmed:dateCreated | 1997-3-31 | lld:pubmed |
pubmed-article:9049300 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9049300 | pubmed:abstractText | Shc proteins are targets of activated tyrosine kinases and are implicated in the transmission of activation signals to Ras. The p46shc and p52shc isoforms share a C-terminal SH2 domain, a proline- and glycine-rich region (collagen homologous region 1; CH1) and a N-terminal PTB domain. We have isolated cDNAs encoding for a third Shc isoform, p66shc. The predicted amino acid sequence of p66shc overlaps that of p52shc and contains a unique N-terminal region which is also rich in glycines and prolines (CH2). p52shc/p46shc is found in every cell type with invariant reciprocal relationship, whereas p66shc expression varies from cell type to cell type. p66shc differs from p52shc/p46shc in its inability to transform mouse fibroblasts in vitro. Like p52shc/p46shc, p66shc is tyrosine-phosphorylated upon epidermal growth factor (EGF) stimulation, binds to activated EGF receptors (EGFRs) and forms stable complexes with Grb2. However, unlike p52shc/p46shc it does not increase EGF activation of MAP kinases, but inhibits fos promoter activation. The isolated CH2 domain retains the inhibitory effect of p66shc on the fos promoter. p52shc/p46shc and p66shc, therefore, appear to exert different effects on the EGFR-MAP kinase and other signalling pathways that control fos promoter activity. Regulation of p66shc expression might, therefore, influence the cellular response to growth factors. | lld:pubmed |
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pubmed-article:9049300 | pubmed:language | eng | lld:pubmed |
pubmed-article:9049300 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9049300 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9049300 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9049300 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9049300 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9049300 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9049300 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9049300 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9049300 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9049300 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9049300 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:9049300 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9049300 | pubmed:month | Feb | lld:pubmed |
pubmed-article:9049300 | pubmed:issn | 0261-4189 | lld:pubmed |
pubmed-article:9049300 | pubmed:author | pubmed-author:PawsonTT | lld:pubmed |
pubmed-article:9049300 | pubmed:author | pubmed-author:LaiK MKM | lld:pubmed |
pubmed-article:9049300 | pubmed:author | pubmed-author:LanfranconeLL | lld:pubmed |
pubmed-article:9049300 | pubmed:author | pubmed-author:PelicciP GPG | lld:pubmed |
pubmed-article:9049300 | pubmed:author | pubmed-author:Superti-Furga... | lld:pubmed |
pubmed-article:9049300 | pubmed:author | pubmed-author:Di FioreP PPP | lld:pubmed |
pubmed-article:9049300 | pubmed:author | pubmed-author:PelicciGG | lld:pubmed |
pubmed-article:9049300 | pubmed:author | pubmed-author:SalciniA EAE | lld:pubmed |
pubmed-article:9049300 | pubmed:author | pubmed-author:MigliaccioEE | lld:pubmed |
pubmed-article:9049300 | pubmed:author | pubmed-author:MeleSS | lld:pubmed |
pubmed-article:9049300 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9049300 | pubmed:day | 17 | lld:pubmed |
pubmed-article:9049300 | pubmed:volume | 16 | lld:pubmed |
pubmed-article:9049300 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9049300 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9049300 | pubmed:pagination | 706-16 | lld:pubmed |
pubmed-article:9049300 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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