| pubmed-article:7865125 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7865125 | lifeskim:mentions | umls-concept:C0023768 | lld:lifeskim |
| pubmed-article:7865125 | lifeskim:mentions | umls-concept:C1442792 | lld:lifeskim |
| pubmed-article:7865125 | lifeskim:mentions | umls-concept:C0085732 | lld:lifeskim |
| pubmed-article:7865125 | lifeskim:mentions | umls-concept:C1707520 | lld:lifeskim |
| pubmed-article:7865125 | lifeskim:mentions | umls-concept:C2828386 | lld:lifeskim |
| pubmed-article:7865125 | lifeskim:mentions | umls-concept:C0052172 | lld:lifeskim |
| pubmed-article:7865125 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:7865125 | pubmed:dateCreated | 1995-3-27 | lld:pubmed |
| pubmed-article:7865125 | pubmed:abstractText | In contrast to the horse heart apocytochrome c, the chicken heart apocytochrome c underwent a conformational change from random coil to partial folding during a renaturation process. When the apocytochrome horse heart and that of chicken heart c were subjected to a translocation assay in vitro using large trypsin-enclosed unilamellar vesicles from soybean phospholipids, the ability of the chicken heart apocytochrome c to penetrate into the liposomes was found to decrease markedly with the renaturation procedure, while that of horse heart apocytochrome c remained relatively constant. Observations from circular dichroism measurement on the induction of secondary folding of these two species of apocytochrome c upon interaction with soybean phospholipid vesicles suggested that a more flexible structure of apocytochrome c embedded in the lipid matrix be required for its efficient translocation across the bilayer. | lld:pubmed |
| pubmed-article:7865125 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7865125 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7865125 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7865125 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7865125 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7865125 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7865125 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7865125 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7865125 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7865125 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:7865125 | pubmed:issn | 1001-652X | lld:pubmed |
| pubmed-article:7865125 | pubmed:author | pubmed-author:YangF YFY | lld:pubmed |
| pubmed-article:7865125 | pubmed:author | pubmed-author:YanG LGL | lld:pubmed |
| pubmed-article:7865125 | pubmed:author | pubmed-author:WangX SXS | lld:pubmed |
| pubmed-article:7865125 | pubmed:author | pubmed-author:TongJ CJC | lld:pubmed |
| pubmed-article:7865125 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7865125 | pubmed:volume | 37 | lld:pubmed |
| pubmed-article:7865125 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7865125 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7865125 | pubmed:pagination | 1341-9 | lld:pubmed |
| pubmed-article:7865125 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:meshHeading | pubmed-meshheading:7865125-... | lld:pubmed |
| pubmed-article:7865125 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7865125 | pubmed:articleTitle | Correlation between unfolded states of apocytochrome c and its ability to pass lipid bilayer. | lld:pubmed |
| pubmed-article:7865125 | pubmed:affiliation | National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing, PRC. | lld:pubmed |
| pubmed-article:7865125 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7865125 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:7865125 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
