Pub. Date : 2000 Jul 7
PMID : 10801877
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Conformational reorganization of the amino-terminal four-helix bundle (22-kDa fragment) of apolipoprotein E (apoE) in binding to the phospholipid dimyristoylphosphatidylcholine (DMPC) to form discoidal particles was investigated by introducing single, double, and triple interhelical disulfide bonds to restrict the opening of the bundle. | Dimyristoylphosphatidylcholine | apolipoprotein E | Homo sapiens |
| 2 | Conformational reorganization of the amino-terminal four-helix bundle (22-kDa fragment) of apolipoprotein E (apoE) in binding to the phospholipid dimyristoylphosphatidylcholine (DMPC) to form discoidal particles was investigated by introducing single, double, and triple interhelical disulfide bonds to restrict the opening of the bundle. | Dimyristoylphosphatidylcholine | apolipoprotein E | Homo sapiens |
| 3 | Interaction of apoE with DMPC was assessed by vesicle disruption, turbidimetric clearing, and gel filtration assays. | Dimyristoylphosphatidylcholine | apolipoprotein E | Homo sapiens |
| 4 | The results indicate that the formation of apoE.DMPC discoidal particles occurs in a series of steps. | Dimyristoylphosphatidylcholine | apolipoprotein E | Homo sapiens |