| pubmed-article:1982072 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1982072 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:1982072 | lifeskim:mentions | umls-concept:C1510411 | lld:lifeskim |
| pubmed-article:1982072 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:1982072 | lifeskim:mentions | umls-concept:C0813988 | lld:lifeskim |
| pubmed-article:1982072 | lifeskim:mentions | umls-concept:C1709059 | lld:lifeskim |
| pubmed-article:1982072 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1982072 | pubmed:dateCreated | 1991-5-16 | lld:pubmed |
| pubmed-article:1982072 | pubmed:abstractText | The product of the erbB-2 gene is a 185-kD receptor-like glycoprotein. erbB-2 gp185 displays constitutive tyrosine kinase activity and transforms NIH 3T3 cells when expressed 100-fold over the normal levels. We have analyzed the role of tyrosine kinase function and of receptor autophosphorylation in the regulation of erbB-2 biological activity. Abolition of erbB-2 gp185 tyrosine kinase function resulted in complete loss of its transforming activity and the absence of in vivo tyrosine phosphorylation. The steady-state content of phosphotyrosine in erbB-2 gp185 was found to be solely dependent on receptor autophosphorylation and to be dependent on the specific enzymatic activity of the erbB-2 protein. The major sites of erbB-2 autophosphorylation were shown to be in its COOH-terminal domain. Biological analysis of erbB-2 mutants containing either individual or multiple Tyr----Phe substitutions at the potential sites of autophosphorylation revealed that autophosphorylation upregulates erbB-2 gp185 transforming activity. Autophosphorylation did not modulate receptor turnover. A Tyr----Phe substitution of erbB-2 Tyr-877 homologous to pp60c-src Tyr-416 did not alter erbB-2 biological and biochemical properties, thus excluding the possibility that phosphorylation of this residue, located in the kinase domain, modulates erbB-2 gp185 catalytic function. Hence, autophosphorylation of tyrosine residues localized in its COOH terminus appears to be required for optimal coupling of erbB-2 gp185 with its mitogenic pathway. | lld:pubmed |
| pubmed-article:1982072 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1982072 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1982072 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1982072 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1982072 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:1982072 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1982072 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1982072 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1982072 | pubmed:issn | 1043-4674 | lld:pubmed |
| pubmed-article:1982072 | pubmed:author | pubmed-author:BottaroD PDP | lld:pubmed |
| pubmed-article:1982072 | pubmed:author | pubmed-author:PierceJ HJH | lld:pubmed |
| pubmed-article:1982072 | pubmed:author | pubmed-author:Di FioreP PPP | lld:pubmed |
| pubmed-article:1982072 | pubmed:author | pubmed-author:SegattoOO | lld:pubmed |
| pubmed-article:1982072 | pubmed:author | pubmed-author:LonardoFF | lld:pubmed |
| pubmed-article:1982072 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1982072 | pubmed:volume | 2 | lld:pubmed |
| pubmed-article:1982072 | pubmed:geneSymbol | erbB-2 | lld:pubmed |
| pubmed-article:1982072 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1982072 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1982072 | pubmed:pagination | 187-95 | lld:pubmed |
| pubmed-article:1982072 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:1982072 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:1982072 | pubmed:articleTitle | The role of autophosphorylation in modulation of erbB-2 transforming function. | lld:pubmed |
| pubmed-article:1982072 | pubmed:affiliation | National Institutes of Health, National Cancer Institute, Bethesda, MD 20892. | lld:pubmed |
| pubmed-article:1982072 | pubmed:publicationType | Journal Article | lld:pubmed |
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