21219628

Source:http://linkedlifedata.com/resource/pubmed/id/21219628

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0003595, umls-concept:C0014406, umls-concept:C0023779, umls-concept:C0030956, umls-concept:C0086418, umls-concept:C0205245, umls-concept:C0599956, umls-concept:C0678594, umls-concept:C1880022
pubmed:dateCreated	2011-1-19
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.
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pubmed:language	eng
pubmed:journal	http://linkedlifedata.com/resource/pubmed/journal/9421567
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/1,2-hexanoylphosphatidylcholine, http://linkedlifedata.com/resource/pubmed/chemical/Apolipoproteins E, http://linkedlifedata.com/resource/pubmed/chemical/Dimyristoylphosphatidylcholine, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines, http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms
pubmed:status	MEDLINE
pubmed:issn	1423-0127
pubmed:author	pubmed-author:ChouChi-YuanCY, pubmed-author:HsiehYi-HuiYH
pubmed:issnType	Electronic
pubmed:volume	18
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	4
pubmed:dateRevised	2011-7-20
pubmed:meshHeading	pubmed-meshheading:21219628-Apolipoproteins E, pubmed-meshheading:21219628-Dimyristoylphosphatidylcholine, pubmed-meshheading:21219628-Humans, pubmed-meshheading:21219628-Peptides, pubmed-meshheading:21219628-Phosphatidylcholines, pubmed-meshheading:21219628-Protein Isoforms, pubmed-meshheading:21219628-Protein Structure, Tertiary, pubmed-meshheading:21219628-Structure-Activity Relationship
pubmed:year	2011
pubmed:articleTitle	Structural and functional characterization of human apolipoprotein E 72-166 peptides in both aqueous and lipid environments.
pubmed:affiliation	Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei 112, Taiwan.
pubmed:publicationType	Journal Article, Research Support, Non-U.S. Gov't