pubmed-article:21428945 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:21428945 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
pubmed-article:21428945 | lifeskim:mentions | umls-concept:C0009452 | lld:lifeskim |
pubmed-article:21428945 | lifeskim:mentions | umls-concept:C0035647 | lld:lifeskim |
pubmed-article:21428945 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
pubmed-article:21428945 | lifeskim:mentions | umls-concept:C0040715 | lld:lifeskim |
pubmed-article:21428945 | lifeskim:mentions | umls-concept:C0001480 | lld:lifeskim |
pubmed-article:21428945 | lifeskim:mentions | umls-concept:C0011525 | lld:lifeskim |
pubmed-article:21428945 | lifeskim:mentions | umls-concept:C1522702 | lld:lifeskim |
pubmed-article:21428945 | lifeskim:mentions | umls-concept:C0599718 | lld:lifeskim |
pubmed-article:21428945 | lifeskim:mentions | umls-concept:C0599813 | lld:lifeskim |
pubmed-article:21428945 | lifeskim:mentions | umls-concept:C0599893 | lld:lifeskim |
pubmed-article:21428945 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:21428945 | pubmed:dateCreated | 2011-3-24 | lld:pubmed |
pubmed-article:21428945 | pubmed:abstractText | To cleave DNA, the Type III RM (restriction-modification) enzymes must communicate the relative orientation of two recognition sequences, which may be separated by many thousands of base pairs. This long-range interaction requires ATP hydrolysis by a helicase domain, and both active (DNA translocation) and passive (DNA sliding) modes of motion along DNA have been proposed. Potential roles for ATP binding and hydrolysis by the helicase domains are discussed, with a focus on bipartite ATPases that act as molecular switches. | lld:pubmed |
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pubmed-article:21428945 | pubmed:language | eng | lld:pubmed |
pubmed-article:21428945 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21428945 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:21428945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:21428945 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:21428945 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:21428945 | pubmed:month | Apr | lld:pubmed |
pubmed-article:21428945 | pubmed:issn | 1470-8752 | lld:pubmed |
pubmed-article:21428945 | pubmed:author | pubmed-author:SzczelkunMark... | lld:pubmed |
pubmed-article:21428945 | pubmed:issnType | Electronic | lld:pubmed |
pubmed-article:21428945 | pubmed:volume | 39 | lld:pubmed |
pubmed-article:21428945 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:21428945 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:21428945 | pubmed:pagination | 589-94 | lld:pubmed |
pubmed-article:21428945 | pubmed:dateRevised | 2011-10-27 | lld:pubmed |
pubmed-article:21428945 | pubmed:meshHeading | pubmed-meshheading:21428945... | lld:pubmed |
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pubmed-article:21428945 | pubmed:meshHeading | pubmed-meshheading:21428945... | lld:pubmed |
pubmed-article:21428945 | pubmed:year | 2011 | lld:pubmed |
pubmed-article:21428945 | pubmed:articleTitle | Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases. | lld:pubmed |
pubmed-article:21428945 | pubmed:affiliation | DNA-Protein Interactions Unit, School of Biochemistry, Medical Sciences Building, University of Bristol, Bristol BS8 1TD, UK. mark.szczelkun@bristol.ac.uk | lld:pubmed |
pubmed-article:21428945 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:21428945 | pubmed:publicationType | Review | lld:pubmed |
pubmed-article:21428945 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |