| pubmed-article:6489332 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:6489332 | lifeskim:mentions | umls-concept:C0003591 | lld:lifeskim |
| pubmed-article:6489332 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:6489332 | lifeskim:mentions | umls-concept:C1416804 | lld:lifeskim |
| pubmed-article:6489332 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:6489332 | pubmed:dateCreated | 1984-12-12 | lld:pubmed |
| pubmed-article:6489332 | pubmed:abstractText | Apolipoprotein A-IGiessen is a variant form of apo A-I that is displaced from the corresponding normal A-I isoforms on isoelectric focusing gels by a single charge unit towards the cathode [Utermann et al. (1982) J. Biol. Chem. 257, 501-507]. Three subjects heterozygous for the variant were detected in one family. The percentage of the total A-I in plasma represented by the A-IGiessen in these subjects ranged over 25-30%. The variant and normal major A-I isoforms from the proband (Y.J.) were purified by preparative isoelectric focusing and cleaved with CNBr. Analytical focusing of CNBr fragments demonstrated a charge difference between CB3Giessen and normal CB3. Sequence analysis of CB3Giessen revealed that a proline existing in normal A-I was replaced by an arginine in the variant A-I at residue 143. The ability of the mutant A-I to activate purified lecithin:cholesterol acyltransferase was determined in vitro. The cofactor activity of [Arg143]apolipoprotein A-I was about 60-70% of that demonstrated by control A-I. Residue 143 is in a putative beta-turn between two of the repeating amphiphilic helices in apolipoprotein A-I and may be a critical determinant of the protein's structure and function. | lld:pubmed |
| pubmed-article:6489332 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6489332 | pubmed:language | eng | lld:pubmed |
| pubmed-article:6489332 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6489332 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:6489332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6489332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6489332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6489332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6489332 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:6489332 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:6489332 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:6489332 | pubmed:issn | 0014-2956 | lld:pubmed |
| pubmed-article:6489332 | pubmed:author | pubmed-author:MahleyR WRW | lld:pubmed |
| pubmed-article:6489332 | pubmed:author | pubmed-author:SteinmetzAA | lld:pubmed |
| pubmed-article:6489332 | pubmed:author | pubmed-author:UtermannGG | lld:pubmed |
| pubmed-article:6489332 | pubmed:author | pubmed-author:WeisgraberK... | lld:pubmed |
| pubmed-article:6489332 | pubmed:author | pubmed-author:HaasJJ | lld:pubmed |
| pubmed-article:6489332 | pubmed:author | pubmed-author:RallS CSCJr | lld:pubmed |
| pubmed-article:6489332 | pubmed:author | pubmed-author:PaetzoldRR | lld:pubmed |
| pubmed-article:6489332 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:6489332 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:6489332 | pubmed:volume | 144 | lld:pubmed |
| pubmed-article:6489332 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:6489332 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:6489332 | pubmed:pagination | 325-31 | lld:pubmed |
| pubmed-article:6489332 | pubmed:dateRevised | 2008-11-21 | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:meshHeading | pubmed-meshheading:6489332-... | lld:pubmed |
| pubmed-article:6489332 | pubmed:year | 1984 | lld:pubmed |
| pubmed-article:6489332 | pubmed:articleTitle | Apolipoprotein A-IGiessen (Pro143----Arg). A mutant that is defective in activating lecithin:cholesterol acyltransferase. | lld:pubmed |
| pubmed-article:6489332 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:6489332 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:6489332 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:6489332 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:335 | entrezgene:pubmed | pubmed-article:6489332 | lld:entrezgene |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6489332 | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:6489332 | lld:pubmed |
