| pubmed-article:7680109 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7680109 | lifeskim:mentions | umls-concept:C2752508 | lld:lifeskim |
| pubmed-article:7680109 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:7680109 | lifeskim:mentions | umls-concept:C1167322 | lld:lifeskim |
| pubmed-article:7680109 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:7680109 | lifeskim:mentions | umls-concept:C0231491 | lld:lifeskim |
| pubmed-article:7680109 | lifeskim:mentions | umls-concept:C1551336 | lld:lifeskim |
| pubmed-article:7680109 | lifeskim:mentions | umls-concept:C1517050 | lld:lifeskim |
| pubmed-article:7680109 | lifeskim:mentions | umls-concept:C0458216 | lld:lifeskim |
| pubmed-article:7680109 | pubmed:issue | 6414 | lld:pubmed |
| pubmed-article:7680109 | pubmed:dateCreated | 1993-3-29 | lld:pubmed |
| pubmed-article:7680109 | pubmed:abstractText | The fate of the R7 photoreceptor cell in the Drosophila compound eye is established by a specific inductive interaction between the R8 photoreceptor neuron and the R7 precursor cell. This induction is mediated by two cell-surface proteins: the ligand, bride of sevenless (boss), and sevenless (sev), a tyrosine-kinase receptor. The structure of boss is unique for a ligand of a tyrosine-kinase receptor. It contains a large extracellular domain, seven transmembrane segments, and a carboxy-terminal cytoplasmic tail. Here we report that: (1) boss activates tyrosine phosphorylation of the sev receptor; (2) the seven transmembrane domain of boss is necessary for its function; and (3) a soluble form of boss acts as an antagonist of the sev receptor both in vivo and in vitro. | lld:pubmed |
| pubmed-article:7680109 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7680109 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7680109 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7680109 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:7680109 | pubmed:issn | 0028-0836 | lld:pubmed |
| pubmed-article:7680109 | pubmed:author | pubmed-author:ZipurskyS LSL | lld:pubmed |
| pubmed-article:7680109 | pubmed:author | pubmed-author:HartA CAC | lld:pubmed |
| pubmed-article:7680109 | pubmed:author | pubmed-author:KrämerHH | lld:pubmed |
| pubmed-article:7680109 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7680109 | pubmed:day | 25 | lld:pubmed |
| pubmed-article:7680109 | pubmed:volume | 361 | lld:pubmed |
| pubmed-article:7680109 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7680109 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7680109 | pubmed:pagination | 732-6 | lld:pubmed |
| pubmed-article:7680109 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:7680109 | pubmed:meshHeading | pubmed-meshheading:7680109-... | lld:pubmed |
| pubmed-article:7680109 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:7680109 | pubmed:articleTitle | Extracellular domain of the boss transmembrane ligand acts as an antagonist of the sev receptor. | lld:pubmed |
| pubmed-article:7680109 | pubmed:affiliation | Howard Hughes Medical Institute, Department of Biological Chemistry, University of California, Los Angeles 90024. | lld:pubmed |
| pubmed-article:7680109 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7680109 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7680109 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:32039 | entrezgene:pubmed | pubmed-article:7680109 | lld:entrezgene |
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