PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
32777483-15	2020	This suggests that there is an esterification pathway of side-chain oxysterols via LPLA2.	Oxysterols	68-78	phospholipase A2, group XV	Mus musculus	83-88	
32777483-4	2020	First, esterification of side-chain oxysterols by LPLA2 was investigated using recombinant mouse LPLA2 and dioleoyl-PC/sulfatide/oxysterol liposomes under acidic conditions.	Oxysterols	36-46	phospholipase A2, group XV	Mus musculus	50-55	
32777483-4	2020	First, esterification of side-chain oxysterols by LPLA2 was investigated using recombinant mouse LPLA2 and dioleoyl-PC/sulfatide/oxysterol liposomes under acidic conditions.	Oxysterols	36-46	phospholipase A2, group XV	Mus musculus	97-102	
32777483-4	2020	First, esterification of side-chain oxysterols by LPLA2 was investigated using recombinant mouse LPLA2 and dioleoyl-PC/sulfatide/oxysterol liposomes under acidic conditions.	Oxysterols	36-45	phospholipase A2, group XV	Mus musculus	50-55	
32777483-4	2020	First, esterification of side-chain oxysterols by LPLA2 was investigated using recombinant mouse LPLA2 and dioleoyl-PC/sulfatide/oxysterol liposomes under acidic conditions.	Oxysterols	36-45	phospholipase A2, group XV	Mus musculus	97-102	
32777483-9	2020	N-acetylsphingosine (NAS) acting as an acyl acceptor in LPLA2 transacylation inhibited the side-chain oxysterol esterification by LPLA2.	Oxysterols	102-111	phospholipase A2, group XV	Mus musculus	56-61	
32777483-9	2020	N-acetylsphingosine (NAS) acting as an acyl acceptor in LPLA2 transacylation inhibited the side-chain oxysterol esterification by LPLA2.	Oxysterols	102-111	phospholipase A2, group XV	Mus musculus	130-135	
32777483-13	2020	The docking model of acyl-LPLA2 intermediate and side-chain oxysterol provided new insight to elucidate the transacylation mechanism of sterols by LPLA2.	Oxysterols	60-69	phospholipase A2, group XV	Mus musculus	147-152