| pubmed-article:17208001 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:17208001 | lifeskim:mentions | umls-concept:C0001480 | lld:lifeskim |
| pubmed-article:17208001 | lifeskim:mentions | umls-concept:C1947953 | lld:lifeskim |
| pubmed-article:17208001 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:17208001 | lifeskim:mentions | umls-concept:C2700372 | lld:lifeskim |
| pubmed-article:17208001 | lifeskim:mentions | umls-concept:C1063749 | lld:lifeskim |
| pubmed-article:17208001 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:17208001 | pubmed:dateCreated | 2007-2-9 | lld:pubmed |
| pubmed-article:17208001 | pubmed:abstractText | ATP synthase synthesizes ATP from ADP and inorganic phosphate using a unique rotary mechanism whereby two subcomplexes move relative to each other, powered by a proton or sodium gradient. The non-rotating parts of the machinery are held together by the "stator stalk". The recent resolution of the structure of a major portion of the stator stalk of mitochondrial ATP synthase represents an important step towards a structural model for the ATP synthase holoenzyme. | lld:pubmed |
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| pubmed-article:17208001 | pubmed:language | eng | lld:pubmed |
| pubmed-article:17208001 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17208001 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:17208001 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:17208001 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:17208001 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:17208001 | pubmed:issn | 0968-0004 | lld:pubmed |
| pubmed-article:17208001 | pubmed:author | pubmed-author:WeberJoachimJ | lld:pubmed |
| pubmed-article:17208001 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:17208001 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:17208001 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:17208001 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:17208001 | pubmed:pagination | 53-6 | lld:pubmed |
| pubmed-article:17208001 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:17208001 | pubmed:meshHeading | pubmed-meshheading:17208001... | lld:pubmed |
| pubmed-article:17208001 | pubmed:meshHeading | pubmed-meshheading:17208001... | lld:pubmed |
| pubmed-article:17208001 | pubmed:meshHeading | pubmed-meshheading:17208001... | lld:pubmed |
| pubmed-article:17208001 | pubmed:year | 2007 | lld:pubmed |
| pubmed-article:17208001 | pubmed:articleTitle | ATP synthase--the structure of the stator stalk. | lld:pubmed |
| pubmed-article:17208001 | pubmed:affiliation | Department of Chemistry and Biochemistry, Texas Tech University, Box 41061, Lubbock, TX 79409-1061, USA. joachim.weber@ttuhsc.edu | lld:pubmed |
| pubmed-article:17208001 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:17208001 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:17208001 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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