| pubmed-article:1831660 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1831660 | lifeskim:mentions | umls-concept:C0007452 | lld:lifeskim |
| pubmed-article:1831660 | lifeskim:mentions | umls-concept:C0026238 | lld:lifeskim |
| pubmed-article:1831660 | lifeskim:mentions | umls-concept:C0001473 | lld:lifeskim |
| pubmed-article:1831660 | lifeskim:mentions | umls-concept:C0001480 | lld:lifeskim |
| pubmed-article:1831660 | lifeskim:mentions | umls-concept:C0069436 | lld:lifeskim |
| pubmed-article:1831660 | lifeskim:mentions | umls-concept:C1412671 | lld:lifeskim |
| pubmed-article:1831660 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:1831660 | lifeskim:mentions | umls-concept:C0205224 | lld:lifeskim |
| pubmed-article:1831660 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:1831660 | pubmed:dateCreated | 1991-10-3 | lld:pubmed |
| pubmed-article:1831660 | pubmed:abstractText | The requirement of bovine heart mitochondrial oligomycin sensitivity conferring protein (OSCP) in conferring dicyclohexylcarbodiimide (DCCD)-sensitivity to membrane-bound F1 was investigated by using OSCP-depleted membrane fraction (UF0) of ATP synthase. The ATPase activity of UF0-F1 was completely insensitive to DCCD while that of UF0-F1-OSCP was inhibited 95% by 16 microM DCCD. Both UF0-F1 and UF0-F1-OSCP complexes bound 5 nmol [14C]DCCD/mg UF0, and all the radioactivity was found to be associated with the DCCD-binding proteolipid. The data suggest that OSCP may be necessary for transmitting not only energy-linked signals, but also signals induced by F0 inhibitory ligands in mitochondrial energy transduction. | lld:pubmed |
| pubmed-article:1831660 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1831660 | pubmed:language | eng | lld:pubmed |
| pubmed-article:1831660 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1831660 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:1831660 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1831660 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1831660 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1831660 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:1831660 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1831660 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:1831660 | pubmed:issn | 0006-3002 | lld:pubmed |
| pubmed-article:1831660 | pubmed:author | pubmed-author:JoshiSS | lld:pubmed |
| pubmed-article:1831660 | pubmed:author | pubmed-author:HuangY GYG | lld:pubmed |
| pubmed-article:1831660 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1831660 | pubmed:day | 26 | lld:pubmed |
| pubmed-article:1831660 | pubmed:volume | 1067 | lld:pubmed |
| pubmed-article:1831660 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1831660 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1831660 | pubmed:pagination | 255-8 | lld:pubmed |
| pubmed-article:1831660 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:1831660 | pubmed:meshHeading | pubmed-meshheading:1831660-... | lld:pubmed |
| pubmed-article:1831660 | pubmed:meshHeading | pubmed-meshheading:1831660-... | lld:pubmed |
| pubmed-article:1831660 | pubmed:meshHeading | pubmed-meshheading:1831660-... | lld:pubmed |
| pubmed-article:1831660 | pubmed:meshHeading | pubmed-meshheading:1831660-... | lld:pubmed |
| pubmed-article:1831660 | pubmed:meshHeading | pubmed-meshheading:1831660-... | lld:pubmed |
| pubmed-article:1831660 | pubmed:meshHeading | pubmed-meshheading:1831660-... | lld:pubmed |
| pubmed-article:1831660 | pubmed:meshHeading | pubmed-meshheading:1831660-... | lld:pubmed |
| pubmed-article:1831660 | pubmed:meshHeading | pubmed-meshheading:1831660-... | lld:pubmed |
| pubmed-article:1831660 | pubmed:year | 1991 | lld:pubmed |
| pubmed-article:1831660 | pubmed:articleTitle | ATP synthase complex from bovine heart mitochondria: the oligomycin sensitivity conferring protein is essential for dicyclohexyl carbodiimide-sensitive ATPase. | lld:pubmed |
| pubmed-article:1831660 | pubmed:affiliation | Department of Cell and Molecular Biology, Boston Biomedical Research institute 02114. | lld:pubmed |
| pubmed-article:1831660 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1831660 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
