pubmed-article:10619019 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10619019 | lifeskim:mentions | umls-concept:C1412592 | lld:lifeskim |
pubmed-article:10619019 | lifeskim:mentions | umls-concept:C0949662 | lld:lifeskim |
pubmed-article:10619019 | lifeskim:mentions | umls-concept:C1511331 | lld:lifeskim |
pubmed-article:10619019 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
pubmed-article:10619019 | lifeskim:mentions | umls-concept:C0376315 | lld:lifeskim |
pubmed-article:10619019 | lifeskim:mentions | umls-concept:C0332256 | lld:lifeskim |
pubmed-article:10619019 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
pubmed-article:10619019 | lifeskim:mentions | umls-concept:C1335651 | lld:lifeskim |
pubmed-article:10619019 | pubmed:issue | 5 | lld:pubmed |
pubmed-article:10619019 | pubmed:dateCreated | 2000-1-14 | lld:pubmed |
pubmed-article:10619019 | pubmed:abstractText | RSC is an essential 15 protein nucleosome-remodeling complex from S. cerevisiae. We have identified two closely related RSC members, Rsc1 and Rsc2. Biochemical analysis revealed Rsc1 and Rsc2 in distinct complexes, defining two forms of RSC. Genetic analysis has shown that Rsc1 and Rsc2 possess shared and unique functions. Rsc1 and Rsc2 each contain two bromodomains, a bromo-adjacent homology (BAH) domain, and an AT hook. One of the bromodomains, the BAH domain, and the AT hook are each essential for Rsc1 and Rsc2 functions, although they are not required for assembly into RSC complexes. Therefore, these domains are required for RSC function. Additional genetic analysis provides further evidence that RSC function is related to transcriptional control. | lld:pubmed |
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pubmed-article:10619019 | pubmed:language | eng | lld:pubmed |
pubmed-article:10619019 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10619019 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:10619019 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:10619019 | pubmed:month | Nov | lld:pubmed |
pubmed-article:10619019 | pubmed:issn | 1097-2765 | lld:pubmed |
pubmed-article:10619019 | pubmed:author | pubmed-author:KornbergR DRD | lld:pubmed |
pubmed-article:10619019 | pubmed:author | pubmed-author:WinstonFF | lld:pubmed |
pubmed-article:10619019 | pubmed:author | pubmed-author:TempstPP | lld:pubmed |
pubmed-article:10619019 | pubmed:author | pubmed-author:Erdjument-Bro... | lld:pubmed |
pubmed-article:10619019 | pubmed:author | pubmed-author:CairnsB RBR | lld:pubmed |
pubmed-article:10619019 | pubmed:author | pubmed-author:SchlichterAA | lld:pubmed |
pubmed-article:10619019 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:10619019 | pubmed:volume | 4 | lld:pubmed |
pubmed-article:10619019 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:10619019 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:10619019 | pubmed:pagination | 715-23 | lld:pubmed |
pubmed-article:10619019 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:10619019 | pubmed:year | 1999 | lld:pubmed |
pubmed-article:10619019 | pubmed:articleTitle | Two functionally distinct forms of the RSC nucleosome-remodeling complex, containing essential AT hook, BAH, and bromodomains. | lld:pubmed |
pubmed-article:10619019 | pubmed:affiliation | Huntsman Cancer Institute, University of Utah School of Medicine, Salt Lake City 84112, USA. brad.caims@hci.utah.edu | lld:pubmed |
pubmed-article:10619019 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:10619019 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:10619019 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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