Pub. Date : 2020 Oct
PMID : 32777483
8 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | First, esterification of side-chain oxysterols by LPLA2 was investigated using recombinant mouse LPLA2 and dioleoyl-PC/sulfatide/oxysterol liposomes under acidic conditions. | Oxysterols | phospholipase A2, group XV | Mus musculus |
| 2 | First, esterification of side-chain oxysterols by LPLA2 was investigated using recombinant mouse LPLA2 and dioleoyl-PC/sulfatide/oxysterol liposomes under acidic conditions. | Oxysterols | phospholipase A2, group XV | Mus musculus |
| 3 | First, esterification of side-chain oxysterols by LPLA2 was investigated using recombinant mouse LPLA2 and dioleoyl-PC/sulfatide/oxysterol liposomes under acidic conditions. | Oxysterols | phospholipase A2, group XV | Mus musculus |
| 4 | First, esterification of side-chain oxysterols by LPLA2 was investigated using recombinant mouse LPLA2 and dioleoyl-PC/sulfatide/oxysterol liposomes under acidic conditions. | Oxysterols | phospholipase A2, group XV | Mus musculus |
| 5 | N-acetylsphingosine (NAS) acting as an acyl acceptor in LPLA2 transacylation inhibited the side-chain oxysterol esterification by LPLA2. | Oxysterols | phospholipase A2, group XV | Mus musculus |
| 6 | N-acetylsphingosine (NAS) acting as an acyl acceptor in LPLA2 transacylation inhibited the side-chain oxysterol esterification by LPLA2. | Oxysterols | phospholipase A2, group XV | Mus musculus |
| 7 | The docking model of acyl-LPLA2 intermediate and side-chain oxysterol provided new insight to elucidate the transacylation mechanism of sterols by LPLA2. | Oxysterols | phospholipase A2, group XV | Mus musculus |
| 8 | This suggests that there is an esterification pathway of side-chain oxysterols via LPLA2. | Oxysterols | phospholipase A2, group XV | Mus musculus |