| pubmed-article:7638186 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7638186 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7638186 | lifeskim:mentions | umls-concept:C0123759 | lld:lifeskim |
| pubmed-article:7638186 | lifeskim:mentions | umls-concept:C1335874 | lld:lifeskim |
| pubmed-article:7638186 | lifeskim:mentions | umls-concept:C0024264 | lld:lifeskim |
| pubmed-article:7638186 | lifeskim:mentions | umls-concept:C1519726 | lld:lifeskim |
| pubmed-article:7638186 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:7638186 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:7638186 | pubmed:issue | 16 | lld:pubmed |
| pubmed-article:7638186 | pubmed:dateCreated | 1995-9-11 | lld:pubmed |
| pubmed-article:7638186 | pubmed:abstractText | Interleukin 12 (IL-12) is an important immunoregulatory cytokine whose receptor is a member of the hematopoietin receptor superfamily. We have recently demonstrated that stimulation of human T and natural killer cells with IL-12 induces tyrosine phosphorylation of the Janus family tyrosine kinase JAK2 and Tyk2, implicating these kinases in the immediate biochemical response to IL-12. Recently, transcription factors known as STATs (signal transducers and activators of transcription) have been shown to be tyrosine phosphorylated and activated in response to a number of cytokines that bind hematopoietin receptors and activate JAK kinases. In this report we demonstrate that IL-12 induces tyrosine phosphorylation of a recently identified STAT family member, STAT4, and show that STAT4 expression is regulated by T-cell activation. Furthermore, we show that IL-12 stimulates formation of a DNA-binding complex that recognizes a DNA sequence previously shown to bind STAT proteins and that this complex contains STAT4. These data, and the recent demonstration of JAK phosphorylation by IL-12, identify a rapid signal-transduction pathway likely to mediate IL-12-induced gene expression. | lld:pubmed |
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| pubmed-article:7638186 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7638186 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7638186 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7638186 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7638186 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7638186 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:7638186 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:7638186 | pubmed:author | pubmed-author:ReesR CRC | lld:pubmed |
| pubmed-article:7638186 | pubmed:author | pubmed-author:OrtaldoJ RJR | lld:pubmed |
| pubmed-article:7638186 | pubmed:author | pubmed-author:JohnstonJ AJA | lld:pubmed |
| pubmed-article:7638186 | pubmed:author | pubmed-author:O'SheaJ JJJ | lld:pubmed |
| pubmed-article:7638186 | pubmed:author | pubmed-author:LarnerA CAC | lld:pubmed |
| pubmed-article:7638186 | pubmed:author | pubmed-author:PetricoinE... | lld:pubmed |
| pubmed-article:7638186 | pubmed:author | pubmed-author:BaconC MCM | lld:pubmed |
| pubmed-article:7638186 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7638186 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:7638186 | pubmed:volume | 92 | lld:pubmed |
| pubmed-article:7638186 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7638186 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7638186 | pubmed:pagination | 7307-11 | lld:pubmed |
| pubmed-article:7638186 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
| pubmed-article:7638186 | pubmed:meshHeading | pubmed-meshheading:7638186-... | lld:pubmed |
| pubmed-article:7638186 | pubmed:meshHeading | pubmed-meshheading:7638186-... | lld:pubmed |
| pubmed-article:7638186 | pubmed:meshHeading | pubmed-meshheading:7638186-... | lld:pubmed |
| pubmed-article:7638186 | pubmed:meshHeading | pubmed-meshheading:7638186-... | lld:pubmed |
