PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
10802244-11	2000	We postulate that during cardiac cell differentiation, the observed elevation in lysophosphatidylethanolamine acyltransferase activity accompanies the elevation in phosphatidylethanolamine mass, possibly to maintain the fatty acyl composition of this phospholipid within the membrane.	Phospholipids	251-263	membrane bound O-acyltransferase domain containing 2	Homo sapiens	81-125	
10667352-16	1999	These clones will afford opportunity for defining the function of LPAAT in eukaryotic phospholipid metabolism.	Phospholipids	86-98	membrane bound O-acyltransferase domain containing 2	Homo sapiens	66-71	
24990952-4	2014	The LPAAT pathway is integral to de novo membrane phospholipid biosynthesis, whereas the PLD and DGK pathways are activated in response to growth factors and stress.	Phospholipids	50-62	membrane bound O-acyltransferase domain containing 2	Homo sapiens	4-9	
30180990-1	2018	Lysophosphatidic acid acyltransferases (LPAAT) play an essential role in generating phosphatidic acid (PA), a key intermediate for phospholipids and triacylglycerol synthesis.	Phospholipids	131-144	membrane bound O-acyltransferase domain containing 2	Homo sapiens	0-38	
30180990-1	2018	Lysophosphatidic acid acyltransferases (LPAAT) play an essential role in generating phosphatidic acid (PA), a key intermediate for phospholipids and triacylglycerol synthesis.	Phospholipids	131-144	membrane bound O-acyltransferase domain containing 2	Homo sapiens	40-45	
29373329-6	2018	Loss of any specific LPAAT can lead to alterations in cellular and organellar membrane phospholipid composition that can vary for a single enzyme in different tissues, with unique pathophysiological implications.	Phospholipids	87-99	membrane bound O-acyltransferase domain containing 2	Homo sapiens	21-26