| pubmed-article:16819518 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16819518 | lifeskim:mentions | umls-concept:C0028623 | lld:lifeskim |
| pubmed-article:16819518 | lifeskim:mentions | umls-concept:C0733755 | lld:lifeskim |
| pubmed-article:16819518 | lifeskim:mentions | umls-concept:C0441722 | lld:lifeskim |
| pubmed-article:16819518 | lifeskim:mentions | umls-concept:C1515655 | lld:lifeskim |
| pubmed-article:16819518 | pubmed:issue | 7 | lld:pubmed |
| pubmed-article:16819518 | pubmed:dateCreated | 2006-7-7 | lld:pubmed |
| pubmed-article:16819518 | pubmed:abstractText | ATP-dependent chromatin remodeling complexes are implicated in many areas of chromosome biology. However, the physiological role of many of these enzymes is still unclear. In budding yeast, the Isw2 complex slides nucleosomes along DNA. By analyzing the native chromatin structure of Isw2 targets, we have found that nucleosomes adopt default, DNA-directed positions when ISW2 is deleted. We provide evidence that Isw2 targets contain DNA sequences that are inhibitory to nucleosome formation and that these sequences facilitate the formation of nuclease-accessible open chromatin in the absence of Isw2. Our data show that the biological function of Isw2 is to position nucleosomes onto unfavorable DNA. These results reveal that antagonistic forces of Isw2 and the DNA sequence can control nucleosome positioning and genomic access in vivo. | lld:pubmed |
| pubmed-article:16819518 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16819518 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16819518 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16819518 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:16819518 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16819518 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:16819518 | pubmed:issn | 1545-9993 | lld:pubmed |
| pubmed-article:16819518 | pubmed:author | pubmed-author:TsukiyamaTosh... | lld:pubmed |
| pubmed-article:16819518 | pubmed:author | pubmed-author:WhitehouseIes... | lld:pubmed |
| pubmed-article:16819518 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16819518 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:16819518 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16819518 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16819518 | pubmed:pagination | 633-40 | lld:pubmed |
| pubmed-article:16819518 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
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| pubmed-article:16819518 | pubmed:meshHeading | pubmed-meshheading:16819518... | lld:pubmed |
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| pubmed-article:16819518 | pubmed:meshHeading | pubmed-meshheading:16819518... | lld:pubmed |
| pubmed-article:16819518 | pubmed:meshHeading | pubmed-meshheading:16819518... | lld:pubmed |
| pubmed-article:16819518 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16819518 | pubmed:articleTitle | Antagonistic forces that position nucleosomes in vivo. | lld:pubmed |
| pubmed-article:16819518 | pubmed:affiliation | Division of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, Washington 98109, USA. | lld:pubmed |
| pubmed-article:16819518 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16819518 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| pubmed-article:16819518 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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