| pubmed-article:9722576 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9722576 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
| pubmed-article:9722576 | lifeskim:mentions | umls-concept:C0567416 | lld:lifeskim |
| pubmed-article:9722576 | lifeskim:mentions | umls-concept:C0378516 | lld:lifeskim |
| pubmed-article:9722576 | lifeskim:mentions | umls-concept:C1519727 | lld:lifeskim |
| pubmed-article:9722576 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:9722576 | pubmed:issue | 36 | lld:pubmed |
| pubmed-article:9722576 | pubmed:dateCreated | 1998-10-15 | lld:pubmed |
| pubmed-article:9722576 | pubmed:abstractText | Receptor tyrosine phosphorylation is crucial for signal transduction by creating high affinity binding sites for Src homology 2 domain-containing molecules. By expressing the intracellular domain of Flt-1/vascular endothelial growth factor receptor-1 in the baculosystem, we identified two major tyrosine phosphorylation sites at Tyr-1213 and Tyr-1242 and two minor tyrosine phosphorylation sites at Tyr-1327 and Tyr-1333 in this receptor. This pattern of phosphorylation of Flt-1 was also detected in vascular endothelial growth factor-stimulated cells expressing intact Flt-1. In vitro protein binding studies using synthetic peptides and immunoblotting showed that phospholipase C-gamma binds to both Y(p)1213 and Y(p)1333, whereas Grb2 and SH2-containing tyrosine protein phosphatase (SHP-2) bind to Y(p)1213, and Nck and Crk bind to Y(p)1333 in a phosphotyrosine-dependent manner. In addition, unidentified proteins with molecular masses around 74 and 27 kDa bound to Y(p)1213 and another of 75 kDa bound to Y(p)1333 in a phosphotyrosine-dependent manner. SHP-2, phospholipase C-gamma, and Grb2 could also be shown to bind to the intact Flt-1 intracellular domain. These results indicate that a spectrum of already known as well as novel phosphotyrosine-binding molecules are involved in signal transduction by Flt-1. | lld:pubmed |
| pubmed-article:9722576 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:9722576 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:9722576 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9722576 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:9722576 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9722576 | pubmed:author | pubmed-author:ItoNN | lld:pubmed |
| pubmed-article:9722576 | pubmed:author | pubmed-author:Claesson-Wels... | lld:pubmed |
| pubmed-article:9722576 | pubmed:author | pubmed-author:EngströmUU | lld:pubmed |
| pubmed-article:9722576 | pubmed:author | pubmed-author:WernstedtCC | lld:pubmed |
| pubmed-article:9722576 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9722576 | pubmed:day | 4 | lld:pubmed |
| pubmed-article:9722576 | pubmed:volume | 273 | lld:pubmed |
| pubmed-article:9722576 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9722576 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9722576 | pubmed:pagination | 23410-8 | lld:pubmed |
| pubmed-article:9722576 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:9722576 | pubmed:year | 1998 | lld:pubmed |
| pubmed-article:9722576 | pubmed:articleTitle | Identification of vascular endothelial growth factor receptor-1 tyrosine phosphorylation sites and binding of SH2 domain-containing molecules. | lld:pubmed |
| pubmed-article:9722576 | pubmed:affiliation | Department of Medical Biochemistry and Microbiology, Uppsala University, Biomedical Center, Box 575, S-751 23 Uppsala, Sweden. | lld:pubmed |
| pubmed-article:9722576 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9722576 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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