PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
11080676-3	2000	gVPLA(2) is homologous to other group II PLA(2) family members but has distinctive enzymatic properties, including its activity to effectively hydrolyze phosphatidylcholine (PC) vesicles and the outer plasma membrane of mammalian cells.	Phosphatidylcholines	153-172	phospholipase A2 group V	Homo sapiens	0-8	
11080676-4	2000	Mutational studies showed that gVPLA(2) has a unique structure that allows effective binding to PC membranes and efficient catalysis of an active-site-bound PC substrate.	Phosphatidylcholines	96-98	phospholipase A2 group V	Homo sapiens	31-39	
11080676-4	2000	Mutational studies showed that gVPLA(2) has a unique structure that allows effective binding to PC membranes and efficient catalysis of an active-site-bound PC substrate.	Phosphatidylcholines	157-159	phospholipase A2 group V	Homo sapiens	31-39	
3099849-5	1987	Parallel to the liberation process, phosphatidylcholine underwent a rapid decrease of radioactivity with both agonists, suggesting the involvement of a Ca2+-dependent phospholipase A2.	Phosphatidylcholines	36-55	phospholipase A2 group V	Homo sapiens	152-183	
33383652-6	2020	Phosphatidylcholine (PC) was preferentially metabolized in (LPS+IFNgamma)BM-Macs and Phosphatidylethanolamine (PE) in (IL-4)BM-Macs, with Pla2g5 contributing mostly to metabolization of selected PE molecules.	Phosphatidylcholines	0-19	phospholipase A2 group V	Homo sapiens	138-144	
12796497-5	2003	As low a concentration as 10 nm exogenous hVPLA2 was able to elicit the significant release of AA and LTC4 from unstimulated eosinophils, which depended on its ability to act on phosphatidylcholine membranes.	Phosphatidylcholines	178-197	phospholipase A2 group V	Homo sapiens	42-48	
10839997-2	2000	We showed that hVPLA(2) can bind phosphatidylcholine membranes and hydrolyse phosphatidylcholine molecules much more efficiently than human group-IIa PLA(2), which accounts for its high activity on the outer plasma membrane of mammalian cells.	Phosphatidylcholines	33-52	phospholipase A2 group V	Homo sapiens	15-23	
10839997-2	2000	We showed that hVPLA(2) can bind phosphatidylcholine membranes and hydrolyse phosphatidylcholine molecules much more efficiently than human group-IIa PLA(2), which accounts for its high activity on the outer plasma membrane of mammalian cells.	Phosphatidylcholines	77-96	phospholipase A2 group V	Homo sapiens	15-23	
10839997-3	2000	To understand the molecular basis of the high phosphatidylcholine specificity of hVPLA(2), we mutated several residues (Gly-53, Glu-56 and Glu-57) that might be involved in interaction with an active-site-bound phospholipid molecule.	Phosphatidylcholines	46-65	phospholipase A2 group V	Homo sapiens	81-89	
10839997-6	2000	Together, these steric and electrostatic properties of the active site of hVPLA(2) allow for effective binding and hydrolysis of a bulky cationic choline head group of phosphatidylcholine, which is unique among mammalian secretory PLA(2)s.	Phosphatidylcholines	168-187	phospholipase A2 group V	Homo sapiens	74-82	
9531469-4	1998	First, hV-PLA2 can catalyse the hydrolysis of phosphatidylcholine more effectively than hIIa-PLA2 by two orders of magnitude.	Phosphatidylcholines	46-65	phospholipase A2 group V	Homo sapiens	7-14	
9531469-5	1998	Secondly, hV-PLA2 has much higher binding affinity and activity for compactly packed phosphatidylcholine bilayers than hIIa-PLA2.	Phosphatidylcholines	85-104	phospholipase A2 group V	Homo sapiens	10-17