Source:http://linkedlifedata.com/resource/pubmed/id/10881750
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7
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pubmed:dateCreated |
2000-8-9
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pubmed:abstractText |
High density lipoproteins are produced by the liver as protein-lipid complexes with a characteristic discoidal shape. A crystal structure is available for the chief protein component of these complexes, apolipoprotein A-I, but controversy about how this protein is situated with respect to the lipid components has flourished for lack of experimental techniques that can characterize protein structure in a lipid environment. New spectroscopic techniques developed to address this problem now indicate that apolipoprotein A-I is arranged as a helical belt around a bilayer of phospholipids. This is an important step towards understanding how these lipoproteins regulate cholesterol transport.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1050-1738
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
192-5
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pubmed:dateRevised |
2005-11-16
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pubmed:meshHeading | |
pubmed:year |
1999
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pubmed:articleTitle |
Lipoprotein A-I structure.
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pubmed:affiliation |
Department of Pharmacology, University of Pennsylvania, Philadelphia 19104-6084, USA.
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pubmed:publicationType |
Journal Article,
Review
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