PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
8724896-9	1996	Phospholipase A2 increased the erythrocyte anion-carrier protein phosphorylation and the oxalate exchange.	Oxalates	89-96	phospholipase A2 group IB	Homo sapiens	0-16	
16284883-2	2005	Oxalate exposure activates phospholipase A2 (PLA2), which increases two lipid signaling molecules, arachidonic acid and lysophosphatidylcholine (Lyso-PC).	Oxalates	0-7	phospholipase A2 group IB	Homo sapiens	27-43	
7241575-2	1981	Cleavage of 55% of the lecithin in intact human erythrocytes by phospholipase A2 (bee venom) markedly inhibits the mediated transport of L-lactate (via the monocarboxylate carrier) and of L-arabinose (via the monosaccharide carrier), while the major anion exchange system (probed by oxalate) and diffusion via the lipid domain (probed by erythritol) remain essentially unaltered.	Oxalates	283-290	phospholipase A2 group IB	Homo sapiens	64-80	
16284883-2	2005	Oxalate exposure activates phospholipase A2 (PLA2), which increases two lipid signaling molecules, arachidonic acid and lysophosphatidylcholine (Lyso-PC).	Oxalates	0-7	phospholipase A2 group IB	Homo sapiens	45-49	
16284883-3	2005	PLA2 inhibition blocks, whereas exogenous Lyso-PC or arachidonic acid reproduce many of the effects of oxalate on mitochondrial function, gene expression and cell viability, suggesting that PLA2 activation plays a role in mediating oxalate toxicity.	Oxalates	103-110	phospholipase A2 group IB	Homo sapiens	190-194	
16284883-3	2005	PLA2 inhibition blocks, whereas exogenous Lyso-PC or arachidonic acid reproduce many of the effects of oxalate on mitochondrial function, gene expression and cell viability, suggesting that PLA2 activation plays a role in mediating oxalate toxicity.	Oxalates	232-239	phospholipase A2 group IB	Homo sapiens	190-194