| pubmed-article:10518221 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C0007226 | lld:lifeskim |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C0386040 | lld:lifeskim |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C0031437 | lld:lifeskim |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C1414431 | lld:lifeskim |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C1527148 | lld:lifeskim |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C0205369 | lld:lifeskim |
| pubmed-article:10518221 | lifeskim:mentions | umls-concept:C0332516 | lld:lifeskim |
| pubmed-article:10518221 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10518221 | pubmed:dateCreated | 1999-10-29 | lld:pubmed |
| pubmed-article:10518221 | pubmed:abstractText | Ephrin-B2 is a transmembrane ligand that is specifically expressed on arteries but not veins and that is essential for cardiovascular development. However, ephrin-B2 is also expressed in nonvascular tissues and interacts with multiple EphB class receptors expressed in both endothelial and nonendothelial cell types. Thus, the identity of the relevant receptor for ephrin-B2 and the site(s) where these molecules interact to control angiogenesis were not clear. Here we show that EphB4, a specific receptor for ephrin-B2, is exclusively expressed by vascular endothelial cells in embryos and is preferentially expressed on veins. A targeted mutation in EphB4 essentially phenocopies the mutation in ephrin-B2. These data indicate that ephrin-B2-EphB4 interactions are intrinsically required in vascular endothelial cells and are consistent with the idea that they mediate bidirectional signaling essential for angiogenesis. | lld:pubmed |
| pubmed-article:10518221 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10518221 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10518221 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10518221 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10518221 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10518221 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10518221 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10518221 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10518221 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10518221 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:10518221 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:10518221 | pubmed:author | pubmed-author:AndersonD JDJ | lld:pubmed |
| pubmed-article:10518221 | pubmed:author | pubmed-author:ChenZ FZF | lld:pubmed |
| pubmed-article:10518221 | pubmed:author | pubmed-author:WingP EPE | lld:pubmed |
| pubmed-article:10518221 | pubmed:author | pubmed-author:GeretyS SSS | lld:pubmed |
| pubmed-article:10518221 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10518221 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:10518221 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10518221 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10518221 | pubmed:pagination | 403-14 | lld:pubmed |
| pubmed-article:10518221 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:10518221 | pubmed:meshHeading | pubmed-meshheading:10518221... | lld:pubmed |
| pubmed-article:10518221 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10518221 | pubmed:articleTitle | Symmetrical mutant phenotypes of the receptor EphB4 and its specific transmembrane ligand ephrin-B2 in cardiovascular development. | lld:pubmed |
| pubmed-article:10518221 | pubmed:affiliation | Division of Biology, Howard Hughes Medical Institute, California Institute of Technology, Pasadena 91125, USA. | lld:pubmed |
| pubmed-article:10518221 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10518221 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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