Title : Apolipoprotein E isoforms and rare mutations: parallel reduction in binding to cells and to heparin reflects severity of associated type III hyperlipoproteinemia.

Pub. Date : 1995 Mar

PMID : 7775863






6 Functional Relationships(s)
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Protein Name
Organism
1 Apolipoprotein E isoforms and rare mutations: parallel reduction in binding to cells and to heparin reflects severity of associated type III hyperlipoproteinemia. Heparin apolipoprotein E Homo sapiens
2 Heparin binding studies with the same variants showed a parallel reduction in proteoglycan binding (apoE-2(158), 58.2% of apoE-3; apoE-1(127,158), 37.9%; apoE-1(146), 20.6%). Heparin apolipoprotein E Homo sapiens
3 Heparin binding studies with the same variants showed a parallel reduction in proteoglycan binding (apoE-2(158), 58.2% of apoE-3; apoE-1(127,158), 37.9%; apoE-1(146), 20.6%). Heparin apolipoprotein E Homo sapiens
4 Heparin binding studies with the same variants showed a parallel reduction in proteoglycan binding (apoE-2(158), 58.2% of apoE-3; apoE-1(127,158), 37.9%; apoE-1(146), 20.6%). Heparin apolipoprotein E Homo sapiens
5 Heparin binding studies with the same variants showed a parallel reduction in proteoglycan binding (apoE-2(158), 58.2% of apoE-3; apoE-1(127,158), 37.9%; apoE-1(146), 20.6%). Heparin apolipoprotein E Homo sapiens
6 The functionally dominant mutation apoE-1(146) was most defective in heparin binding studies in vitro. Heparin apolipoprotein E Homo sapiens