| pubmed-article:7510216 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7510216 | lifeskim:mentions | umls-concept:C0376525 | lld:lifeskim |
| pubmed-article:7510216 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:7510216 | lifeskim:mentions | umls-concept:C0287920 | lld:lifeskim |
| pubmed-article:7510216 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:7510216 | lifeskim:mentions | umls-concept:C1512827 | lld:lifeskim |
| pubmed-article:7510216 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:7510216 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:7510216 | pubmed:dateCreated | 1994-4-12 | lld:pubmed |
| pubmed-article:7510216 | pubmed:abstractText | Stat91 (a 91 kd protein that acts as a signal transducer and activator of transcription) is inactive in the cytoplasm of untreated cells but is activated by phosphorylation on tyrosine in response to a number of polypeptide ligands, including interferon alpha (IFN-alpha) and IFN-gamma. We report here that the inactive Stat91 in the cytoplasm of untreated cells is a monomer and that upon IFN-gamma-induced phosphorylation it forms a stable homodimer. Only the dimer is capable of binding to a specific DNA sequence directing transcription. Through dissociation and reassociation assays, we show that dimerization of Stat91 is mediated through SH2-phosphotyrosyl peptide interactions. Dimerization involving SH2 recognition of specific phosphotyrosyl peptides may well provide a prototype for interactions among family members of STAT proteins to form different transcription complexes. | lld:pubmed |
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| pubmed-article:7510216 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7510216 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7510216 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7510216 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:7510216 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:7510216 | pubmed:author | pubmed-author:DarnellJ... | lld:pubmed |
| pubmed-article:7510216 | pubmed:author | pubmed-author:HuangL HLH | lld:pubmed |
| pubmed-article:7510216 | pubmed:author | pubmed-author:QureshiS ASA | lld:pubmed |
| pubmed-article:7510216 | pubmed:author | pubmed-author:CowburnDD | lld:pubmed |
| pubmed-article:7510216 | pubmed:author | pubmed-author:ShuaiKK | lld:pubmed |
| pubmed-article:7510216 | pubmed:author | pubmed-author:HorvathC MCM | lld:pubmed |
| pubmed-article:7510216 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7510216 | pubmed:day | 11 | lld:pubmed |
| pubmed-article:7510216 | pubmed:volume | 76 | lld:pubmed |
| pubmed-article:7510216 | pubmed:geneSymbol | src | lld:pubmed |
| pubmed-article:7510216 | pubmed:geneSymbol | lck | lld:pubmed |
| pubmed-article:7510216 | pubmed:geneSymbol | stat91 | lld:pubmed |
| pubmed-article:7510216 | pubmed:geneSymbol | p85&agr;N | lld:pubmed |
| pubmed-article:7510216 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7510216 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7510216 | pubmed:pagination | 821-8 | lld:pubmed |
| pubmed-article:7510216 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7510216 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7510216 | pubmed:articleTitle | Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions. | lld:pubmed |
| pubmed-article:7510216 | pubmed:affiliation | Laboratory of Molecular Cell Biology, Rockefeller University, New York, New York 10021. | lld:pubmed |
| pubmed-article:7510216 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7510216 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7510216 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7510216 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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