pubmed-article:2710114 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2710114 | lifeskim:mentions | umls-concept:C0001271 | lld:lifeskim |
pubmed-article:2710114 | lifeskim:mentions | umls-concept:C0074398 | lld:lifeskim |
pubmed-article:2710114 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
pubmed-article:2710114 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:2710114 | pubmed:dateCreated | 1989-5-26 | lld:pubmed |
pubmed-article:2710114 | pubmed:abstractText | The c-fos serum response element (SRE) and a sarcomeric actin promoter element (CArG box) are similar in sequence and are recognized, respectively, by the serum response factor (SRF) and the CArG-binding factor (CBF). Although the transcriptional controls for the c-fos and sarcomeric actin genes are rather different, SRF and CBF have been found to be indistinguishable by all criteria tested. They exhibited similar chromatographic properties, sedimentation rates, and temperature stabilities. In mobility shift assays, the SRE competed more strongly than the actin CArG box for formation of either the SRF-SRE or the CBF-CArG complex. The symmetric inverted repeat of the left side of the Xenopus cytoskeletal actin SRE also competed, even more strongly, for each complex. The site-specific binding of each protein was inhibited both by orthophenanthroline, whose effects were reversed by zinc addition, and by treatment with potato acid phosphatase. Furthermore, immune serum raised against the c-fos SRF also recognized the actin CBF. We discuss how transcriptional control of these diverse genes might be obtained with a single similar factor. | lld:pubmed |
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pubmed-article:2710114 | pubmed:language | eng | lld:pubmed |
pubmed-article:2710114 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2710114 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2710114 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:2710114 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2710114 | pubmed:month | Feb | lld:pubmed |
pubmed-article:2710114 | pubmed:issn | 0270-7306 | lld:pubmed |
pubmed-article:2710114 | pubmed:author | pubmed-author:PrywesRR | lld:pubmed |
pubmed-article:2710114 | pubmed:author | pubmed-author:RoederR GRG | lld:pubmed |
pubmed-article:2710114 | pubmed:author | pubmed-author:BoxerL MLM | lld:pubmed |
pubmed-article:2710114 | pubmed:author | pubmed-author:KedesLL | lld:pubmed |
pubmed-article:2710114 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2710114 | pubmed:volume | 9 | lld:pubmed |
pubmed-article:2710114 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2710114 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2710114 | pubmed:pagination | 515-22 | lld:pubmed |
pubmed-article:2710114 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:2710114 | pubmed:year | 1989 | lld:pubmed |
pubmed-article:2710114 | pubmed:articleTitle | The sarcomeric actin CArG-binding factor is indistinguishable from the c-fos serum response factor. | lld:pubmed |
pubmed-article:2710114 | pubmed:affiliation | MEDIGEN Project, Department of Medicine, Stanford University School of Medicine, Palo Alto, California. | lld:pubmed |
pubmed-article:2710114 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2710114 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2710114 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:2710114 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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