| pubmed-article:2100196 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C0521119 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C0017262 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C1442161 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C1517880 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C0392756 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C0449719 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C2911684 | lld:lifeskim |
| pubmed-article:2100196 | lifeskim:mentions | umls-concept:C0185117 | lld:lifeskim |
| pubmed-article:2100196 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:2100196 | pubmed:dateCreated | 1991-8-22 | lld:pubmed |
| pubmed-article:2100196 | pubmed:abstractText | Cultured NIH-3T3 cells were transfected with cDNA constructs encoding human epidermal growth factor-receptor (EGF-R)* and two deletion mutants in the extracellular portion of the receptor molecule. One mutant is devoid of 124 amino-terminal amino acids, and the other lacks 76 residues. Mutant receptors were not delivered to the cell surface unless the transfected cells contained also endogenous EGF-Rs, suggesting that receptor interaction complements the mutation and allows surface display of mutant receptors. Immunoprecipitation experiments revealed an association between mutant and endogenous EGF-Rs when both proteins were expressed in the same cell. Hence, receptor-oligomers may exist in the plane of the membrane even in the absence of ligand binding, and oligomerization may play a role in normal trafficking of EGF-Rs to the cell surface. Mutant receptors retained partial ligand binding activity as 125I-labeled EGF was covalently cross-linked to both mutant receptors, and EGF stimulated, albeit weakly, their protein tyrosine kinase activity. Both mutant EGF-Rs bind EGF with a 10-fold lower affinity than that of the solubilized wild type EGF-R. These results provide further evidence that the region flanked by the two cysteine-rich domains plays a crucial role in defining ligand-binding specificity of EGF-R. | lld:pubmed |
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| pubmed-article:2100196 | pubmed:language | eng | lld:pubmed |
| pubmed-article:2100196 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2100196 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:2100196 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2100196 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:2100196 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:2100196 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2100196 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:2100196 | pubmed:issn | 1044-2030 | lld:pubmed |
| pubmed-article:2100196 | pubmed:author | pubmed-author:GivolDD | lld:pubmed |
| pubmed-article:2100196 | pubmed:author | pubmed-author:SchlessingerJ... | lld:pubmed |
| pubmed-article:2100196 | pubmed:author | pubmed-author:SchmidtAA | lld:pubmed |
| pubmed-article:2100196 | pubmed:author | pubmed-author:UllrichAA | lld:pubmed |
| pubmed-article:2100196 | pubmed:author | pubmed-author:LawHH | lld:pubmed |
| pubmed-article:2100196 | pubmed:author | pubmed-author:BelloyCC | lld:pubmed |
| pubmed-article:2100196 | pubmed:author | pubmed-author:HoneggerA MAM | lld:pubmed |
| pubmed-article:2100196 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2100196 | pubmed:volume | 1 | lld:pubmed |
| pubmed-article:2100196 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2100196 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2100196 | pubmed:pagination | 173-88 | lld:pubmed |
| pubmed-article:2100196 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:2100196 | pubmed:meshHeading | pubmed-meshheading:2100196-... | lld:pubmed |
| pubmed-article:2100196 | pubmed:meshHeading | pubmed-meshheading:2100196-... | lld:pubmed |
