| pubmed-article:1649701 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1649701 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:1649701 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:1649701 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:1649701 | lifeskim:mentions | umls-concept:C1422634 | lld:lifeskim |
| pubmed-article:1649701 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
| pubmed-article:1649701 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:1649701 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1649701 | pubmed:dateCreated | 1991-8-27 | lld:pubmed |
| pubmed-article:1649701 | pubmed:abstractText | In this report we provide four lines of evidence indicating that E12/E47-like proteins interact in vivo with the myogenic HLH proteins MyoD and myogenin. First, cotransfection of MyoD and E47 in COS cells indicates that these factors synergistically enhance transcription of a reporter gene containing an oligomerized MyoD-binding site. Second, mobility-shift assays of muscle cell nuclear extracts, "double shifted" with specific antisera, have identified complexes binding to the MEF1 site that contain either MyoD or myogenin in association with E12/E47-like proteins. Third, association with E47 alters the phosphorylation state of MyoD. Fourth, C3H10T1/2 cells expressing antisense E2A transcripts contain low levels of E2A gene products and display less terminal muscle differentiation when infected with retroviral MyoD or when challenged to differentiate with 5-azacytidine treatment. In addition we demonstrate that MyoD, in conjunction with E12/E47-like proteins, is functioning as a regulatory nodal point for activation of several other downstream muscle regulators. | lld:pubmed |
| pubmed-article:1649701 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1649701 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1649701 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1649701 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1649701 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:1649701 | pubmed:issn | 0092-8674 | lld:pubmed |
| pubmed-article:1649701 | pubmed:author | pubmed-author:BaltimoreDD | lld:pubmed |
| pubmed-article:1649701 | pubmed:author | pubmed-author:WrightW EWE | lld:pubmed |
| pubmed-article:1649701 | pubmed:author | pubmed-author:DavisR LRL | lld:pubmed |
| pubmed-article:1649701 | pubmed:author | pubmed-author:WeintraubHH | lld:pubmed |
| pubmed-article:1649701 | pubmed:author | pubmed-author:LassarA BAB | lld:pubmed |
| pubmed-article:1649701 | pubmed:author | pubmed-author:KadeschTT | lld:pubmed |
| pubmed-article:1649701 | pubmed:author | pubmed-author:MurreCC | lld:pubmed |
| pubmed-article:1649701 | pubmed:author | pubmed-author:VoronovaAA | lld:pubmed |
| pubmed-article:1649701 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1649701 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:1649701 | pubmed:volume | 66 | lld:pubmed |
| pubmed-article:1649701 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1649701 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1649701 | pubmed:pagination | 305-15 | lld:pubmed |
| pubmed-article:1649701 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:1649701 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1649701 | pubmed:articleTitle | Functional activity of myogenic HLH proteins requires hetero-oligomerization with E12/E47-like proteins in vivo. | lld:pubmed |
| pubmed-article:1649701 | pubmed:affiliation | Department of Genetics, Fred Hutchinson Cancer Research Center, Seattle, Washington 98104. | lld:pubmed |
| pubmed-article:1649701 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1649701 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1649701 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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