| pubmed-article:16935875 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16935875 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:16935875 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:16935875 | lifeskim:mentions | umls-concept:C0920283 | lld:lifeskim |
| pubmed-article:16935875 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:16935875 | lifeskim:mentions | umls-concept:C1335843 | lld:lifeskim |
| pubmed-article:16935875 | lifeskim:mentions | umls-concept:C1335841 | lld:lifeskim |
| pubmed-article:16935875 | lifeskim:mentions | umls-concept:C0178566 | lld:lifeskim |
| pubmed-article:16935875 | lifeskim:mentions | umls-concept:C0179400 | lld:lifeskim |
| pubmed-article:16935875 | lifeskim:mentions | umls-concept:C1705241 | lld:lifeskim |
| pubmed-article:16935875 | lifeskim:mentions | umls-concept:C1705242 | lld:lifeskim |
| pubmed-article:16935875 | pubmed:issue | 15 | lld:pubmed |
| pubmed-article:16935875 | pubmed:dateCreated | 2006-9-26 | lld:pubmed |
| pubmed-article:16935875 | pubmed:abstractText | Proteins with sequence similarity to the yeast Snf2 protein form a large family of ATPases that act to alter the structure of a diverse range of DNA-protein structures including chromatin. Snf2 family enzymes are related in sequence to DExx box helicases, yet they do not possess helicase activity. Recent biochemical and structural studies suggest that the mechanism by which these enzymes act involves ATP-dependent translocation on DNA. Crystal structures suggest that these enzymes travel along the minor groove, a process that can generate the torque or energy in remodelling processes. We review the recent structural and biochemical findings which suggest a common mechanistic basis underlies the action of many of both Snf2 family and DExx box helicases. | lld:pubmed |
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