| pubmed-article:1851331 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1851331 | lifeskim:mentions | umls-concept:C0290068 | lld:lifeskim |
| pubmed-article:1851331 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:1851331 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:1851331 | lifeskim:mentions | umls-concept:C0021467 | lld:lifeskim |
| pubmed-article:1851331 | lifeskim:mentions | umls-concept:C0021469 | lld:lifeskim |
| pubmed-article:1851331 | pubmed:issue | 5007 | lld:pubmed |
| pubmed-article:1851331 | pubmed:dateCreated | 1991-6-11 | lld:pubmed |
| pubmed-article:1851331 | pubmed:abstractText | A mutated form of the platelet-derived growth factor (PDGF) beta receptor lacking most of its cytoplasmic domain was tested for its ability to block wild-type PDGF receptor function. PDGF induced the formation of complexes consisting of wild-type and truncated receptors. Such complexes were defective in autophosphorylation. When truncated receptors were expressed in excess compared to wild-type receptors, stimulation by PDGF of receptor autophosphorylation, association of phosphatidylinositol-3 kinase with the receptor, and calcium mobilization were blocked. Thus, a truncated receptor can inactivate wild-type receptor function by forming ligand-dependent receptor complexes (probably heterodimers) that are incapable of mediating the early steps of signal transduction. | lld:pubmed |
| pubmed-article:1851331 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1851331 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1851331 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1851331 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1851331 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1851331 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1851331 | pubmed:month | May | lld:pubmed |
| pubmed-article:1851331 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:1851331 | pubmed:author | pubmed-author:WilliamsL TLT | lld:pubmed |
| pubmed-article:1851331 | pubmed:author | pubmed-author:UenoHH | lld:pubmed |
| pubmed-article:1851331 | pubmed:author | pubmed-author:EscobedoJ AJA | lld:pubmed |
| pubmed-article:1851331 | pubmed:author | pubmed-author:ColbertHH | lld:pubmed |
| pubmed-article:1851331 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1851331 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:1851331 | pubmed:volume | 252 | lld:pubmed |
| pubmed-article:1851331 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1851331 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1851331 | pubmed:pagination | 844-8 | lld:pubmed |
| pubmed-article:1851331 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:1851331 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1851331 | pubmed:articleTitle | Inhibition of PDGF beta receptor signal transduction by coexpression of a truncated receptor. | lld:pubmed |
| pubmed-article:1851331 | pubmed:affiliation | Department of Medicine, University of California, San Francisco 94143. | lld:pubmed |
| pubmed-article:1851331 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1851331 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:1851331 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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