Pub. Date : 2003 Apr 25
PMID : 12588864
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Characterization of the heparin binding sites in human apolipoprotein E. | Heparin | apolipoprotein E | Homo sapiens |
| 2 | Both the 22-kDa N-terminal domain and 10-kDa C-terminal domain of apoE contain a heparin binding site; the N-terminal site overlaps with the low density lipoprotein receptor binding region and the C-terminal site is undefined. | Heparin | apolipoprotein E | Homo sapiens |
| 3 | To understand the molecular details of the apoE-heparin interaction, we defined the microenvironments of all 12 lysine residues in intact apoE3 and examined their relative contributions to heparin binding. | Heparin | apolipoprotein E | Homo sapiens |
| 4 | With lipidated apoE3, it is confirmed that the Lys-233 site is completely masked and the N-terminal site mediates heparin binding. | Heparin | apolipoprotein E | Homo sapiens |
| 5 | In addition, mutations of the two heparin binding sites in intact apoE3 demonstrated the dominant role of the N-terminal site in the heparin binding of apoE even in the lipid-free state. | Heparin | apolipoprotein E | Homo sapiens |
| 6 | In addition, mutations of the two heparin binding sites in intact apoE3 demonstrated the dominant role of the N-terminal site in the heparin binding of apoE even in the lipid-free state. | Heparin | apolipoprotein E | Homo sapiens |
| 7 | In addition, mutations of the two heparin binding sites in intact apoE3 demonstrated the dominant role of the N-terminal site in the heparin binding of apoE even in the lipid-free state. | Heparin | apolipoprotein E | Homo sapiens |
| 8 | In addition, mutations of the two heparin binding sites in intact apoE3 demonstrated the dominant role of the N-terminal site in the heparin binding of apoE even in the lipid-free state. | Heparin | apolipoprotein E | Homo sapiens |