| pubmed-article:8709144 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8709144 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:8709144 | lifeskim:mentions | umls-concept:C0081594 | lld:lifeskim |
| pubmed-article:8709144 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8709144 | lifeskim:mentions | umls-concept:C1378554 | lld:lifeskim |
| pubmed-article:8709144 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:8709144 | pubmed:dateCreated | 1996-9-12 | lld:pubmed |
| pubmed-article:8709144 | pubmed:abstractText | The crystal structure of calcium-free recombinant human annexin VI was solved at a resolution of 3.2 A by using the annexin I model for Patterson search and refined to an R-factor of 19.0%. The molecule consists of two similar halves closely resembling annexin I connected by an alpha-helical segment and arranged perpendicular to each other. The calcium and membrane binding sites assigned by structural homology are therefore not located in the same plane. Analysis of the membrane-bound form of annexin VI by electron microscopy shows the two halves of the molecule coplanar with the membrane, but oriented differently to the crystal structure and suggesting a flexible arrangement. Ion channel activity has been found for annexin VI and the half molecules by electrophysiological experiments. | lld:pubmed |
| pubmed-article:8709144 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8709144 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8709144 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8709144 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8709144 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8709144 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:8709144 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:8709144 | pubmed:author | pubmed-author:HuberRR | lld:pubmed |
| pubmed-article:8709144 | pubmed:author | pubmed-author:HofmannAA | lld:pubmed |
| pubmed-article:8709144 | pubmed:author | pubmed-author:VogelMM | lld:pubmed |
| pubmed-article:8709144 | pubmed:author | pubmed-author:BergnerAA | lld:pubmed |
| pubmed-article:8709144 | pubmed:author | pubmed-author:BensMM | lld:pubmed |
| pubmed-article:8709144 | pubmed:author | pubmed-author:DemangePP | lld:pubmed |
| pubmed-article:8709144 | pubmed:author | pubmed-author:LiemannSS | lld:pubmed |
| pubmed-article:8709144 | pubmed:author | pubmed-author:GöttigPP | lld:pubmed |
| pubmed-article:8709144 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8709144 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:8709144 | pubmed:volume | 260 | lld:pubmed |
| pubmed-article:8709144 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8709144 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8709144 | pubmed:pagination | 638-43 | lld:pubmed |
| pubmed-article:8709144 | pubmed:dateRevised | 2004-11-17 | lld:pubmed |
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| pubmed-article:8709144 | pubmed:meshHeading | pubmed-meshheading:8709144-... | lld:pubmed |
| pubmed-article:8709144 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8709144 | pubmed:articleTitle | The structure of recombinant human annexin VI in crystals and membrane-bound. | lld:pubmed |
| pubmed-article:8709144 | pubmed:affiliation | Max-Planck-Institut für Biochemie, Abt. Strukturforschung, Martinsried, Germany. | lld:pubmed |
| pubmed-article:8709144 | pubmed:publicationType | Journal Article | lld:pubmed |
| entrez-gene:309 | entrezgene:pubmed | pubmed-article:8709144 | lld:entrezgene |
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