| pubmed-article:1540178 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1540178 | lifeskim:mentions | umls-concept:C0078058 | lld:lifeskim |
| pubmed-article:1540178 | lifeskim:mentions | umls-concept:C0017982 | lld:lifeskim |
| pubmed-article:1540178 | lifeskim:mentions | umls-concept:C1171892 | lld:lifeskim |
| pubmed-article:1540178 | lifeskim:mentions | umls-concept:C1752930 | lld:lifeskim |
| pubmed-article:1540178 | lifeskim:mentions | umls-concept:C1611645 | lld:lifeskim |
| pubmed-article:1540178 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:1540178 | pubmed:dateCreated | 1992-3-27 | lld:pubmed |
| pubmed-article:1540178 | pubmed:abstractText | We have stably expressed the cDNA encoding the 165 amino-acid long form of human vascular endothelial growth factor (VEGF) in BHK-21 cells. VEGF was partially purified from the conditioned medium of transfected cells using heparin-sepharose affinity chromatography. The partially purified VEGF was mitogenic for various types of endothelial cells and inhibited the binding of pure [125I]VEGF to its receptors. Western blot analysis, using anti-VEGF antibodies, revealed a 47 kDa VEGF homodimer in the partially purified VEGF fraction. Preincubation of the transfected cells with the N-glycosylation inhibitor tunicamycin resulted in the conversion of the 47 kDa VEGF homodimer into a smaller, deglycosylated form of 42 kDa. Partially purified preparations of the deglycosylated VEGF displayed a mitogenic activity that was similar to that of the glycosylated form and efficiently inhibited the binding of native [125I]VEGF to the VEGF receptors of bovine aortic arch derived endothelial cells. | lld:pubmed |
| pubmed-article:1540178 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1540178 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540178 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1540178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540178 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1540178 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1540178 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:1540178 | pubmed:issn | 0006-291X | lld:pubmed |
| pubmed-article:1540178 | pubmed:author | pubmed-author:Gospodarowicz... | lld:pubmed |
| pubmed-article:1540178 | pubmed:author | pubmed-author:NeufeldGG | lld:pubmed |
| pubmed-article:1540178 | pubmed:author | pubmed-author:Gitay-GorenHH | lld:pubmed |
| pubmed-article:1540178 | pubmed:author | pubmed-author:SafranMM | lld:pubmed |
| pubmed-article:1540178 | pubmed:author | pubmed-author:PeretzDD | lld:pubmed |
| pubmed-article:1540178 | pubmed:author | pubmed-author:KimmelNN | lld:pubmed |
| pubmed-article:1540178 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1540178 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:1540178 | pubmed:volume | 182 | lld:pubmed |
| pubmed-article:1540178 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1540178 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1540178 | pubmed:pagination | 1340-7 | lld:pubmed |
| pubmed-article:1540178 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:1540178 | pubmed:meshHeading | pubmed-meshheading:1540178-... | lld:pubmed |
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| pubmed-article:1540178 | pubmed:meshHeading | pubmed-meshheading:1540178-... | lld:pubmed |
| pubmed-article:1540178 | pubmed:meshHeading | pubmed-meshheading:1540178-... | lld:pubmed |
| pubmed-article:1540178 | pubmed:meshHeading | pubmed-meshheading:1540178-... | lld:pubmed |
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| pubmed-article:1540178 | pubmed:meshHeading | pubmed-meshheading:1540178-... | lld:pubmed |
| pubmed-article:1540178 | pubmed:meshHeading | pubmed-meshheading:1540178-... | lld:pubmed |
| pubmed-article:1540178 | pubmed:meshHeading | pubmed-meshheading:1540178-... | lld:pubmed |
| pubmed-article:1540178 | pubmed:meshHeading | pubmed-meshheading:1540178-... | lld:pubmed |
| pubmed-article:1540178 | pubmed:meshHeading | pubmed-meshheading:1540178-... | lld:pubmed |
| pubmed-article:1540178 | pubmed:meshHeading | pubmed-meshheading:1540178-... | lld:pubmed |
| pubmed-article:1540178 | pubmed:meshHeading | pubmed-meshheading:1540178-... | lld:pubmed |
| pubmed-article:1540178 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1540178 | pubmed:articleTitle | Glycosylation of vascular endothelial growth factor is not required for its mitogenic activity. | lld:pubmed |
| pubmed-article:1540178 | pubmed:affiliation | Department of Biology, Israel Institute of Technology, Technion City, Haifa. | lld:pubmed |
| pubmed-article:1540178 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1540178 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:1540178 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1540178 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:1540178 | lld:pubmed |
