| pubmed-article:8994623 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8994623 | lifeskim:mentions | umls-concept:C0025255 | lld:lifeskim |
| pubmed-article:8994623 | lifeskim:mentions | umls-concept:C0015450 | lld:lifeskim |
| pubmed-article:8994623 | lifeskim:mentions | umls-concept:C0015127 | lld:lifeskim |
| pubmed-article:8994623 | lifeskim:mentions | umls-concept:C0103403 | lld:lifeskim |
| pubmed-article:8994623 | lifeskim:mentions | umls-concept:C1314792 | lld:lifeskim |
| pubmed-article:8994623 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:8994623 | lifeskim:mentions | umls-concept:C0301704 | lld:lifeskim |
| pubmed-article:8994623 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:8994623 | lifeskim:mentions | umls-concept:C0443172 | lld:lifeskim |
| pubmed-article:8994623 | pubmed:issue | 1 | lld:pubmed |
| pubmed-article:8994623 | pubmed:dateCreated | 1997-5-27 | lld:pubmed |
| pubmed-article:8994623 | pubmed:abstractText | Recent studies have revealed that binding of annexin I to phospholipids induces the formation of a second phospholipid binding site. It is shown that the N terminus on the concave side of membrane-bound annexin I is cleaved much faster by trypsin or cathepsin than the N terminus of the free protein. The reactivity of the unique disulfide bond located near the concave face was similarly increased by membrane binding. These results demonstrate that Ca(2+)-dependent membrane binding induces a conformational change on the concave side of the annexin I molecule and support the notion that this face of the molecule may contribute to the formation of the secondary membrane-binding site. | lld:pubmed |
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| pubmed-article:8994623 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8994623 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8994623 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8994623 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8994623 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:8994623 | pubmed:issn | 0006-3495 | lld:pubmed |
| pubmed-article:8994623 | pubmed:author | pubmed-author:de la... | lld:pubmed |
| pubmed-article:8994623 | pubmed:author | pubmed-author:OssaC GCG | lld:pubmed |
| pubmed-article:8994623 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8994623 | pubmed:volume | 72 | lld:pubmed |
| pubmed-article:8994623 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8994623 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8994623 | pubmed:pagination | 383-7 | lld:pubmed |
| pubmed-article:8994623 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:8994623 | pubmed:meshHeading | pubmed-meshheading:8994623-... | lld:pubmed |
| pubmed-article:8994623 | pubmed:meshHeading | pubmed-meshheading:8994623-... | lld:pubmed |
| pubmed-article:8994623 | pubmed:meshHeading | pubmed-meshheading:8994623-... | lld:pubmed |
| pubmed-article:8994623 | pubmed:meshHeading | pubmed-meshheading:8994623-... | lld:pubmed |
| pubmed-article:8994623 | pubmed:meshHeading | pubmed-meshheading:8994623-... | lld:pubmed |
| pubmed-article:8994623 | pubmed:meshHeading | pubmed-meshheading:8994623-... | lld:pubmed |
| pubmed-article:8994623 | pubmed:meshHeading | pubmed-meshheading:8994623-... | lld:pubmed |
| pubmed-article:8994623 | pubmed:meshHeading | pubmed-meshheading:8994623-... | lld:pubmed |
| pubmed-article:8994623 | pubmed:meshHeading | pubmed-meshheading:8994623-... | lld:pubmed |
| pubmed-article:8994623 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:8994623 | pubmed:articleTitle | Binding to phosphatidyl serine membranes causes a conformational change in the concave face of annexin I. | lld:pubmed |
| pubmed-article:8994623 | pubmed:affiliation | Departamento de Fislología y Biofísica, Facultad de Medicina, Universidad de Chile, Santiago, Chile. mdelafue@machi.med.uchile.cl | lld:pubmed |
| pubmed-article:8994623 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8994623 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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