| pubmed-article:12670943 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12670943 | lifeskim:mentions | umls-concept:C0035868 | lld:lifeskim |
| pubmed-article:12670943 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:12670943 | lifeskim:mentions | umls-concept:C0205345 | lld:lifeskim |
| pubmed-article:12670943 | lifeskim:mentions | umls-concept:C0033727 | lld:lifeskim |
| pubmed-article:12670943 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
| pubmed-article:12670943 | pubmed:issue | 26 | lld:pubmed |
| pubmed-article:12670943 | pubmed:dateCreated | 2003-6-23 | lld:pubmed |
| pubmed-article:12670943 | pubmed:abstractText | Vacuolar-type ATPases V1V0 (V-ATPases) are found ubiquitously in the endomembrane organelles of eukaryotic cells. In this study, we genetically introduced a His tag and a biotin tag onto the c and G subunits, respectively, of Saccharomyces cerevisiae V-ATPase. Using this engineered enzyme, we observed directly the continuous counter-clockwise rotation of an actin filament attached to the G subunit when the enzyme was immobilized on a glass surface through the c subunit. V-ATPase generated essentially the same torque as the F-ATPase (ATP synthase). The rotation was inhibited by concanamycin and nitrate but not by azide. These results demonstrated that the V- and F-ATPase carry out a common rotational catalysis. | lld:pubmed |
| pubmed-article:12670943 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12670943 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12670943 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12670943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12670943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12670943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:12670943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12670943 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12670943 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12670943 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:12670943 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:12670943 | pubmed:author | pubmed-author:OkajimaToshih... | lld:pubmed |
| pubmed-article:12670943 | pubmed:author | pubmed-author:HirataTomoyuk... | lld:pubmed |
| pubmed-article:12670943 | pubmed:author | pubmed-author:WadaYohY | lld:pubmed |
| pubmed-article:12670943 | pubmed:author | pubmed-author:FutaiMasamits... | lld:pubmed |
| pubmed-article:12670943 | pubmed:author | pubmed-author:Sun-WadaGe-Ho... | lld:pubmed |
| pubmed-article:12670943 | pubmed:author | pubmed-author:Iwamoto-Kihar... | lld:pubmed |
| pubmed-article:12670943 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12670943 | pubmed:day | 27 | lld:pubmed |
| pubmed-article:12670943 | pubmed:volume | 278 | lld:pubmed |
| pubmed-article:12670943 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12670943 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12670943 | pubmed:pagination | 23714-9 | lld:pubmed |
| pubmed-article:12670943 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:12670943 | pubmed:meshHeading | pubmed-meshheading:12670943... | lld:pubmed |
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| pubmed-article:12670943 | pubmed:meshHeading | pubmed-meshheading:12670943... | lld:pubmed |
| pubmed-article:12670943 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12670943 | pubmed:articleTitle | Subunit rotation of vacuolar-type proton pumping ATPase: relative rotation of the G and C subunits. | lld:pubmed |
| pubmed-article:12670943 | pubmed:affiliation | Division of Biological Sciences, Institute of Scientific and Industrial Research, Osaka University, Osaka 567-0047, Japan. | lld:pubmed |
| pubmed-article:12670943 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:526 | entrezgene:pubmed | pubmed-article:12670943 | lld:entrezgene |
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