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| pubmed-article:14536084 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:14536084 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:14536084 | lifeskim:mentions | umls-concept:C1335840 | lld:lifeskim |
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| pubmed-article:14536084 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:14536084 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:14536084 | lifeskim:mentions | umls-concept:C1709061 | lld:lifeskim |
| pubmed-article:14536084 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:14536084 | pubmed:dateCreated | 2003-10-10 | lld:pubmed |
| pubmed-article:14536084 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14536084 | pubmed:abstractText | Energy-dependent nucleosome remodeling emerges as a key process endowing chromatin with dynamic properties. However, the principles by which remodeling ATPases interact with their nucleosome substrate to alter histone-DNA interactions are only poorly understood. We have identified a substrate recognition domain in the C-terminal half of the remodeling ATPase ISWI and determined its structure by X-ray crystallography. The structure comprises three domains, a four-helix domain with a novel fold and two alpha-helical domains related to the modules of c-Myb, SANT and SLIDE, which are linked by a long helix. An integrated structural and functional analysis of these domains provides insight into how ISWI interacts with the nucleosomal substrate. | lld:pubmed |
| pubmed-article:14536084 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:14536084 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:14536084 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14536084 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:14536084 | pubmed:issn | 1097-2765 | lld:pubmed |
| pubmed-article:14536084 | pubmed:author | pubmed-author:ClapierCedric... | lld:pubmed |
| pubmed-article:14536084 | pubmed:author | pubmed-author:BeckerPeter... | lld:pubmed |
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| pubmed-article:14536084 | pubmed:author | pubmed-author:CoronaDavide... | lld:pubmed |
| pubmed-article:14536084 | pubmed:author | pubmed-author:MüllerChristo... | lld:pubmed |
| pubmed-article:14536084 | pubmed:author | pubmed-author:BrzeskiJanJ | lld:pubmed |
| pubmed-article:14536084 | pubmed:author | pubmed-author:GrüneTimT | lld:pubmed |
| pubmed-article:14536084 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14536084 | pubmed:volume | 12 | lld:pubmed |
| pubmed-article:14536084 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14536084 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14536084 | pubmed:pagination | 449-60 | lld:pubmed |
| pubmed-article:14536084 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:14536084 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:14536084 | pubmed:articleTitle | Crystal structure and functional analysis of a nucleosome recognition module of the remodeling factor ISWI. | lld:pubmed |
| pubmed-article:14536084 | pubmed:affiliation | European Molecular Biology Laboratory, Grenoble Outstation, B.P. 181, F 38042 Grenoble 9, France. | lld:pubmed |
| pubmed-article:14536084 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14536084 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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