| pubmed-article:9020115 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9020115 | lifeskim:mentions | umls-concept:C0385463 | lld:lifeskim |
| pubmed-article:9020115 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:9020115 | lifeskim:mentions | umls-concept:C1511625 | lld:lifeskim |
| pubmed-article:9020115 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:9020115 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:9020115 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:9020115 | lifeskim:mentions | umls-concept:C0332120 | lld:lifeskim |
| pubmed-article:9020115 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:9020115 | pubmed:dateCreated | 1997-3-14 | lld:pubmed |
| pubmed-article:9020115 | pubmed:abstractText | The leptin receptor (OB-R) mediates the weight regulatory effects of the adipocyte secreted hormone leptin (OB). Previously we have shown that the long form of OB-R, expressed predominantly in the hypothalamus, can mediate ligand-induced activation of signal transducer and activator of transcription factors 1, 3, and 5 and stimulate transcription via interleukin-6 and hematopoietin receptor responsive gene elements. Here we report that deletion and tyrosine substitution mutagenesis of OB-R identifies two distinct regions of the intracellular domain important for signaling. In addition, granulocyte-colony stimulatory factor receptor/OB-R and OB-R/granulocyte-colony stimulatory factor receptor chimeras are signaling competent and provide evidence that aggregation of two OB-R intracellular domains is sufficient for ligand-induced receptor activation. However, signaling by full-length OB-R appears to be relatively resistant to dominant negative repression by signaling-incompetent OB-R, suggesting that mechanisms exist to permit signaling by the long form of OB-R even in the presence [corrected] of excess naturally occurring short form of OB-R. | lld:pubmed |
| pubmed-article:9020115 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9020115 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9020115 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9020115 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9020115 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9020115 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9020115 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:9020115 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9020115 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9020115 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9020115 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:9020115 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:9020115 | pubmed:author | pubmed-author:DevosRR | lld:pubmed |
| pubmed-article:9020115 | pubmed:author | pubmed-author:BaumannHH | lld:pubmed |
| pubmed-article:9020115 | pubmed:author | pubmed-author:WhiteD WDW | lld:pubmed |
| pubmed-article:9020115 | pubmed:author | pubmed-author:TartagliaL... | lld:pubmed |
| pubmed-article:9020115 | pubmed:author | pubmed-author:Kuropatwinski... | lld:pubmed |
| pubmed-article:9020115 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9020115 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:9020115 | pubmed:volume | 272 | lld:pubmed |
| pubmed-article:9020115 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9020115 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9020115 | pubmed:pagination | 4065-71 | lld:pubmed |
| pubmed-article:9020115 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
| pubmed-article:9020115 | pubmed:meshHeading | pubmed-meshheading:9020115-... | lld:pubmed |
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| pubmed-article:9020115 | pubmed:meshHeading | pubmed-meshheading:9020115-... | lld:pubmed |
| pubmed-article:9020115 | pubmed:meshHeading | pubmed-meshheading:9020115-... | lld:pubmed |
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| pubmed-article:9020115 | pubmed:meshHeading | pubmed-meshheading:9020115-... | lld:pubmed |
| pubmed-article:9020115 | pubmed:meshHeading | pubmed-meshheading:9020115-... | lld:pubmed |
| pubmed-article:9020115 | pubmed:meshHeading | pubmed-meshheading:9020115-... | lld:pubmed |
| pubmed-article:9020115 | pubmed:meshHeading | pubmed-meshheading:9020115-... | lld:pubmed |
| pubmed-article:9020115 | pubmed:meshHeading | pubmed-meshheading:9020115-... | lld:pubmed |
| pubmed-article:9020115 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9020115 | pubmed:articleTitle | Leptin receptor (OB-R) signaling. Cytoplasmic domain mutational analysis and evidence for receptor homo-oligomerization. | lld:pubmed |
| pubmed-article:9020115 | pubmed:affiliation | Millennium Pharmaceuticals, Cambridge, Massachusetts 02215-2406, USA. | lld:pubmed |
| pubmed-article:9020115 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9020115 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:9020115 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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