| pubmed-article:21219628 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:21219628 | lifeskim:mentions | umls-concept:C0003595 | lld:lifeskim |
| pubmed-article:21219628 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:21219628 | lifeskim:mentions | umls-concept:C0205245 | lld:lifeskim |
| pubmed-article:21219628 | lifeskim:mentions | umls-concept:C0014406 | lld:lifeskim |
| pubmed-article:21219628 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:21219628 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:21219628 | lifeskim:mentions | umls-concept:C0599956 | lld:lifeskim |
| pubmed-article:21219628 | pubmed:dateCreated | 2011-1-19 | lld:pubmed |
| pubmed-article:21219628 | pubmed:abstractText | There are three apolipoprotein E (apoE) isoforms involved in human lipid homeostasis. In the present study, truncated apoE2-, apoE3- and apoE4-(72-166) peptides that are tailored to lack domain interactions are expressed and elucidated the structural and functional consequences. | lld:pubmed |
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| pubmed-article:21219628 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21219628 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21219628 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:21219628 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21219628 | pubmed:issn | 1423-0127 | lld:pubmed |
| pubmed-article:21219628 | pubmed:author | pubmed-author:ChouChi-YuanC... | lld:pubmed |
| pubmed-article:21219628 | pubmed:author | pubmed-author:HsiehYi-HuiYH | lld:pubmed |
| pubmed-article:21219628 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21219628 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:21219628 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21219628 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21219628 | pubmed:pagination | 4 | lld:pubmed |
| pubmed-article:21219628 | pubmed:dateRevised | 2011-7-20 | lld:pubmed |
| pubmed-article:21219628 | pubmed:meshHeading | pubmed-meshheading:21219628... | lld:pubmed |
| pubmed-article:21219628 | pubmed:meshHeading | pubmed-meshheading:21219628... | lld:pubmed |
| pubmed-article:21219628 | pubmed:meshHeading | pubmed-meshheading:21219628... | lld:pubmed |
| pubmed-article:21219628 | pubmed:meshHeading | pubmed-meshheading:21219628... | lld:pubmed |
| pubmed-article:21219628 | pubmed:meshHeading | pubmed-meshheading:21219628... | lld:pubmed |
| pubmed-article:21219628 | pubmed:meshHeading | pubmed-meshheading:21219628... | lld:pubmed |
| pubmed-article:21219628 | pubmed:meshHeading | pubmed-meshheading:21219628... | lld:pubmed |
| pubmed-article:21219628 | pubmed:meshHeading | pubmed-meshheading:21219628... | lld:pubmed |
| pubmed-article:21219628 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21219628 | pubmed:articleTitle | Structural and functional characterization of human apolipoprotein E 72-166 peptides in both aqueous and lipid environments. | lld:pubmed |
| pubmed-article:21219628 | pubmed:affiliation | Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei 112, Taiwan. | lld:pubmed |
| pubmed-article:21219628 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21219628 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:348 | entrezgene:pubmed | pubmed-article:21219628 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21219628 | lld:entrezgene |
