| pubmed-article:10576729 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10576729 | lifeskim:mentions | umls-concept:C0001480 | lld:lifeskim |
| pubmed-article:10576729 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:10576729 | lifeskim:mentions | umls-concept:C0003737 | lld:lifeskim |
| pubmed-article:10576729 | lifeskim:mentions | umls-concept:C1705994 | lld:lifeskim |
| pubmed-article:10576729 | lifeskim:mentions | umls-concept:C1513492 | lld:lifeskim |
| pubmed-article:10576729 | pubmed:issue | 5445 | lld:pubmed |
| pubmed-article:10576729 | pubmed:dateCreated | 1999-12-14 | lld:pubmed |
| pubmed-article:10576729 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10576729 | pubmed:abstractText | Adenosine triphosphate (ATP) synthase contains a rotary motor involved in biological energy conversion. Its membrane-embedded F0 sector has a rotation generator fueled by the proton-motive force, which provides the energy required for the synthesis of ATP by the F1 domain. An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits. Each c subunit forms an alpha-helical hairpin. The interhelical loops of six to seven of the c subunits are in close contact with the gamma and delta subunits of the central stalk. The extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis. | lld:pubmed |
| pubmed-article:10576729 | pubmed:commentsCorrections | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10576729 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10576729 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10576729 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:10576729 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:10576729 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10576729 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:10576729 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:10576729 | pubmed:author | pubmed-author:LeslieA GAG | lld:pubmed |
| pubmed-article:10576729 | pubmed:author | pubmed-author:WalkerJ EJE | lld:pubmed |
| pubmed-article:10576729 | pubmed:author | pubmed-author:StockDD | lld:pubmed |
| pubmed-article:10576729 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10576729 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:10576729 | pubmed:volume | 286 | lld:pubmed |
| pubmed-article:10576729 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10576729 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10576729 | pubmed:pagination | 1700-5 | lld:pubmed |
| pubmed-article:10576729 | pubmed:dateRevised | 2007-3-19 | lld:pubmed |
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| pubmed-article:10576729 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10576729 | pubmed:articleTitle | Molecular architecture of the rotary motor in ATP synthase. | lld:pubmed |
| pubmed-article:10576729 | pubmed:affiliation | Medical Research Council Dunn Human Nutrition Unit, Hills Road, Cambridge CB2 2XY, UK. | lld:pubmed |
| pubmed-article:10576729 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10576729 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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