| pubmed-article:18326568 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18326568 | lifeskim:mentions | umls-concept:C0014834 | lld:lifeskim |
| pubmed-article:18326568 | lifeskim:mentions | umls-concept:C0012854 | lld:lifeskim |
| pubmed-article:18326568 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:18326568 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:18326568 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:18326568 | pubmed:dateCreated | 2008-5-1 | lld:pubmed |
| pubmed-article:18326568 | pubmed:abstractText | Fluorescence microscopic observation of individual T4 DNA molecules revealed that the MukBEF complex (bacterial condensin) and its subunit, the MukB (a member of the SMC [structural maintenance of chromosomes] superfamily) homodimer, of Escherichia coli markedly shrunk large DNA molecules in the presence of hydrolyzable ATP. In contrast, in the presence of ADP or ATP-gammaS, the conformation of DNA was almost not changed. This suggests that the ATPase activity of subunit MukB is essential for shrinking large DNA molecules. Stretching experiments on the shrunken DNA molecules in the presence of ATP and MukBEF indicated a cross-bridging interaction between DNA molecules. | lld:pubmed |
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| pubmed-article:18326568 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:18326568 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:18326568 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18326568 | pubmed:month | May | lld:pubmed |
| pubmed-article:18326568 | pubmed:issn | 1098-5530 | lld:pubmed |
| pubmed-article:18326568 | pubmed:author | pubmed-author:HiragaSotaS | lld:pubmed |
| pubmed-article:18326568 | pubmed:author | pubmed-author:ChenNingN | lld:pubmed |
| pubmed-article:18326568 | pubmed:author | pubmed-author:YamazoeMitsuy... | lld:pubmed |
| pubmed-article:18326568 | pubmed:author | pubmed-author:YoshikawaKeni... | lld:pubmed |
| pubmed-article:18326568 | pubmed:author | pubmed-author:ZinchenkoAnat... | lld:pubmed |
| pubmed-article:18326568 | pubmed:author | pubmed-author:YoshikawaYuko... | lld:pubmed |
| pubmed-article:18326568 | pubmed:author | pubmed-author:AdachiShunS | lld:pubmed |
| pubmed-article:18326568 | pubmed:author | pubmed-author:ArakiSumikoS | lld:pubmed |
| pubmed-article:18326568 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18326568 | pubmed:volume | 190 | lld:pubmed |
| pubmed-article:18326568 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18326568 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18326568 | pubmed:pagination | 3731-7 | lld:pubmed |
| pubmed-article:18326568 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:18326568 | pubmed:meshHeading | pubmed-meshheading:18326568... | lld:pubmed |
| pubmed-article:18326568 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18326568 | pubmed:articleTitle | ATP-induced shrinkage of DNA with MukB protein and the MukBEF complex of Escherichia coli. | lld:pubmed |
| pubmed-article:18326568 | pubmed:affiliation | Department of Physics, Graduate School of Science, Kyoto University, Kyoto 606-8502, Japan. | lld:pubmed |
| pubmed-article:18326568 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18326568 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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