| pubmed-article:3464946 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:3464946 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:3464946 | lifeskim:mentions | umls-concept:C0023884 | lld:lifeskim |
| pubmed-article:3464946 | lifeskim:mentions | umls-concept:C0028606 | lld:lifeskim |
| pubmed-article:3464946 | lifeskim:mentions | umls-concept:C0006556 | lld:lifeskim |
| pubmed-article:3464946 | lifeskim:mentions | umls-concept:C0205666 | lld:lifeskim |
| pubmed-article:3464946 | lifeskim:mentions | umls-concept:C0002518 | lld:lifeskim |
| pubmed-article:3464946 | lifeskim:mentions | umls-concept:C1441547 | lld:lifeskim |
| pubmed-article:3464946 | lifeskim:mentions | umls-concept:C0205197 | lld:lifeskim |
| pubmed-article:3464946 | pubmed:issue | 21 | lld:pubmed |
| pubmed-article:3464946 | pubmed:dateCreated | 1986-12-5 | lld:pubmed |
| pubmed-article:3464946 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3464946 | pubmed:abstractText | Human apolipoprotein B-100 (apoB-100), the ligand on low density lipoproteins that interacts with the low density lipoprotein receptor and initiates receptor-mediated endocytosis and low density lipoprotein catabolism, has been cloned, and the complete nucleic acid and derived amino acid sequences have been determined. ApoB-100 cDNAs were isolated from normal human liver cDNA libraries utilizing immunoscreening as well as filter hybridization with radiolabeled apoB-100 oligodeoxynucleotides. The apoB-100 mRNA is 14.1 kilobases long encoding a mature apoB-100 protein of 4536 amino acids with a calculated amino acid molecular weight of 512,723. ApoB-100 contains 20 potential glycosylation sites, and 12 of a total of 25 cysteine residues are located in the amino-terminal region of the apolipoprotein providing a potential globular structure of the amino terminus of the protein. ApoB-100 contains relatively few regions of amphipathic helices, but compared to other human apolipoproteins it is enriched in beta-structure. The delineation of the entire human apoB-100 sequence will now permit a detailed analysis of the conformation of the protein, the low density lipoprotein receptor binding domain(s), and the structural relationship between apoB-100 and apoB-48 and will provide the basis for the study of genetic defects in apoB-100 in patients with dyslipoproteinemias. | lld:pubmed |
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| pubmed-article:3464946 | pubmed:language | eng | lld:pubmed |
| pubmed-article:3464946 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:3464946 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:3464946 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:3464946 | pubmed:month | Nov | lld:pubmed |
| pubmed-article:3464946 | pubmed:issn | 0027-8424 | lld:pubmed |
| pubmed-article:3464946 | pubmed:author | pubmed-author:BrewerH BHBJr | lld:pubmed |
| pubmed-article:3464946 | pubmed:author | pubmed-author:LeeNN | lld:pubmed |
| pubmed-article:3464946 | pubmed:author | pubmed-author:LawS WSW | lld:pubmed |
| pubmed-article:3464946 | pubmed:author | pubmed-author:HiguchiKK | lld:pubmed |
| pubmed-article:3464946 | pubmed:author | pubmed-author:LacknerKK | lld:pubmed |
| pubmed-article:3464946 | pubmed:author | pubmed-author:GrantS MSM | lld:pubmed |
| pubmed-article:3464946 | pubmed:author | pubmed-author:HospattankarA... | lld:pubmed |
| pubmed-article:3464946 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:3464946 | pubmed:volume | 83 | lld:pubmed |
| pubmed-article:3464946 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:3464946 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:3464946 | pubmed:pagination | 8142-6 | lld:pubmed |
| pubmed-article:3464946 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:3464946 | pubmed:meshHeading | pubmed-meshheading:3464946-... | lld:pubmed |
| pubmed-article:3464946 | pubmed:year | 1986 | lld:pubmed |
| pubmed-article:3464946 | pubmed:articleTitle | Human liver apolipoprotein B-100 cDNA: complete nucleic acid and derived amino acid sequence. | lld:pubmed |
| pubmed-article:3464946 | pubmed:publicationType | Journal Article | lld:pubmed |
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