| pubmed-article:2118682 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:2118682 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:2118682 | lifeskim:mentions | umls-concept:C0030012 | lld:lifeskim |
| pubmed-article:2118682 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:2118682 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
| pubmed-article:2118682 | pubmed:issue | 4973 | lld:pubmed |
| pubmed-article:2118682 | pubmed:dateCreated | 1990-10-10 | lld:pubmed |
| pubmed-article:2118682 | pubmed:abstractText | The proto-oncogenes c-fos and c-jun function cooperatively as inducible transcription factors in signal transduction processes. Their protein products, Fos and Jun, form a heterodimeric complex that interacts with the DNA regulatory element known as the activator protein-1 (AP-1) binding site. Dimerization occurs via interaction between leucine zipper domains and serves to bring into proper juxtaposition a region in each protein that is rich in basic amino acids and that forms a DNA-binding domain. DNA binding of the Fos-Jun heterodimer was modulated by reduction-oxidation (redox) of a single conserved cysteine residue in the DNA-binding domains of the two proteins. Furthermore, a nuclear protein was identified that reduced Fos and Jun and stimulated DNA-binding activity in vitro. These results suggest that transcriptional activity mediated by AP-1 binding factors may be regulated by a redox mechanism. | lld:pubmed |
| pubmed-article:2118682 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:2118682 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:2118682 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:2118682 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:2118682 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:2118682 | pubmed:author | pubmed-author:PatelLL | lld:pubmed |
| pubmed-article:2118682 | pubmed:author | pubmed-author:CurranTT | lld:pubmed |
| pubmed-article:2118682 | pubmed:author | pubmed-author:RauscherF... | lld:pubmed |
| pubmed-article:2118682 | pubmed:author | pubmed-author:AbateCC | lld:pubmed |
| pubmed-article:2118682 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:2118682 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:2118682 | pubmed:volume | 249 | lld:pubmed |
| pubmed-article:2118682 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:2118682 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:2118682 | pubmed:pagination | 1157-61 | lld:pubmed |
| pubmed-article:2118682 | pubmed:dateRevised | 2007-3-19 | lld:pubmed |
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| pubmed-article:2118682 | pubmed:year | 1990 | lld:pubmed |
| pubmed-article:2118682 | pubmed:articleTitle | Redox regulation of fos and jun DNA-binding activity in vitro. | lld:pubmed |
| pubmed-article:2118682 | pubmed:affiliation | Department of Molecular Oncology and Virology, Roche Institute of Molecular Biology, Nutley, NJ 07110. | lld:pubmed |
| pubmed-article:2118682 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:2118682 | pubmed:publicationType | In Vitro | lld:pubmed |
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