| pubmed-article:8362244 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8362244 | lifeskim:mentions | umls-concept:C0034721 | lld:lifeskim |
| pubmed-article:8362244 | lifeskim:mentions | umls-concept:C0034693 | lld:lifeskim |
| pubmed-article:8362244 | lifeskim:mentions | umls-concept:C0059249 | lld:lifeskim |
| pubmed-article:8362244 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:8362244 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:8362244 | lifeskim:mentions | umls-concept:C0205263 | lld:lifeskim |
| pubmed-article:8362244 | pubmed:issue | 5126 | lld:pubmed |
| pubmed-article:8362244 | pubmed:dateCreated | 1993-9-24 | lld:pubmed |
| pubmed-article:8362244 | pubmed:abstractText | Annexins are a family of calcium- and phospholipid-binding proteins implicated in mediating membrane-related processes such as secretion, signal transduction, and ion channel activity. The crystal structure of rat annexin V was solved to 1.9 angstrom resolution by multiple isomorphous replacement. Unlike previously solved annexin V structures, all four domains bound calcium in this structure. Calcium binding in the third domain induced a large relocation of the calcium-binding loop regions, exposing the single tryptophan residue to the solvent. These alterations in annexin V suggest a role for domain 3 in calcium-triggered interaction with phospholipid membranes. | lld:pubmed |
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| pubmed-article:8362244 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8362244 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8362244 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8362244 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8362244 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8362244 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:8362244 | pubmed:issn | 0036-8075 | lld:pubmed |
| pubmed-article:8362244 | pubmed:author | pubmed-author:DedmanJ RJR | lld:pubmed |
| pubmed-article:8362244 | pubmed:author | pubmed-author:HeadJ FJF | lld:pubmed |
| pubmed-article:8362244 | pubmed:author | pubmed-author:KaetzelM AMA | lld:pubmed |
| pubmed-article:8362244 | pubmed:author | pubmed-author:SeatonB ABA | lld:pubmed |
| pubmed-article:8362244 | pubmed:author | pubmed-author:ConchaN ONO | lld:pubmed |
| pubmed-article:8362244 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8362244 | pubmed:day | 3 | lld:pubmed |
| pubmed-article:8362244 | pubmed:volume | 261 | lld:pubmed |
| pubmed-article:8362244 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8362244 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8362244 | pubmed:pagination | 1321-4 | lld:pubmed |
| pubmed-article:8362244 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:8362244 | pubmed:meshHeading | pubmed-meshheading:8362244-... | lld:pubmed |
| pubmed-article:8362244 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8362244 | pubmed:articleTitle | Rat annexin V crystal structure: Ca(2+)-induced conformational changes. | lld:pubmed |
| pubmed-article:8362244 | pubmed:affiliation | Department of Physiology, Boston University School of Medicine, MA 02118. | lld:pubmed |
| pubmed-article:8362244 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8362244 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8362244 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:25673 | entrezgene:pubmed | pubmed-article:8362244 | lld:entrezgene |
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