pubmed-article:10319872 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10319872 | lifeskim:mentions | umls-concept:C0086661 | lld:lifeskim |
pubmed-article:10319872 | lifeskim:mentions | umls-concept:C0292369 | lld:lifeskim |
pubmed-article:10319872 | lifeskim:mentions | umls-concept:C1167093 | lld:lifeskim |
pubmed-article:10319872 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
pubmed-article:10319872 | lifeskim:mentions | umls-concept:C0040624 | lld:lifeskim |
pubmed-article:10319872 | lifeskim:mentions | umls-concept:C1546857 | lld:lifeskim |
pubmed-article:10319872 | pubmed:issue | 1 | lld:pubmed |
pubmed-article:10319872 | pubmed:dateCreated | 1999-5-25 | lld:pubmed |
pubmed-article:10319872 | pubmed:abstractText | Chromatin organization plays a key role in the regulation of gene expression. The evolutionarily conserved SWI/SNF complex is one of several multiprotein complexes that activate transcription by remodelling chromatin in an ATP-dependent manner. SWI2/SNF2 is an ATPase whose homologues, BRG1 and hBRM, mediate cell-cycle arrest; the SNF5 homologue, INI1/hSNF5, appears to be a tumour suppressor. A search for INI1-interacting proteins using the two-hybrid system led to the isolation of c-MYC, a transactivator. The c-MYC-INI1 interaction was observed both in vitro and in vivo. The c-MYC basic helix-loop-helix (bHLH) and leucine zipper (Zip) domains and the INI1 repeat 1 (Rpt1) region were required for this interaction. c-MYC-mediated transactivation was inhibited by a deletion fragment of INI1 and the ATPase mutant of BRG1/hSNF2 in a dominant-negative manner contingent upon the presence of the c-MYC bHLH-Zip domain. Our results suggest that the SWI/SNF complex is necessary for c-MYC-mediated transactivation and that the c-MYC-INI1 interaction helps recruit the complex. | lld:pubmed |
pubmed-article:10319872 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10319872 | pubmed:language | eng | lld:pubmed |
pubmed-article:10319872 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10319872 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10319872 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10319872 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10319872 | pubmed:month | May | lld:pubmed |
pubmed-article:10319872 | pubmed:issn | 1061-4036 | lld:pubmed |
pubmed-article:10319872 | pubmed:author | pubmed-author:YuJJ | lld:pubmed |
pubmed-article:10319872 | pubmed:author | pubmed-author:ChungC WCW | lld:pubmed |
pubmed-article:10319872 | pubmed:author | pubmed-author:DaviesK PKP | lld:pubmed |
pubmed-article:10319872 | pubmed:author | pubmed-author:KalpanaG VGV | lld:pubmed |
pubmed-article:10319872 | pubmed:author | pubmed-author:YunoMM | lld:pubmed |
pubmed-article:10319872 | pubmed:author | pubmed-author:BeltranR JRJ | lld:pubmed |
pubmed-article:10319872 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10319872 | pubmed:volume | 22 | lld:pubmed |
pubmed-article:10319872 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10319872 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10319872 | pubmed:pagination | 102-5 | lld:pubmed |
pubmed-article:10319872 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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pubmed-article:10319872 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10319872 | pubmed:articleTitle | c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for transactivation function. | lld:pubmed |
pubmed-article:10319872 | pubmed:affiliation | Department of Molecular Genetics, Albert Einstein College of Medicine, Bronx, New York 10461, USA. | lld:pubmed |
pubmed-article:10319872 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10319872 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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