PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
1412509-3	1992	The GSH adduct of EA (EA-GSH) was the most potent inhibitor of GSTs; EA-GSH was approximately one order of magnitude more potent than the parent EA, while L-cysteine conjugate of EA (EA-cysteine) and N-acetyl-L-cysteine conjugate of EA (EA-mercapturate) were approximately two orders of magnitude less potent than the parent EA.	ea-gsh	22-28	glutathione S-transferase kappa 1	Homo sapiens	63-67	
1412509-3	1992	The GSH adduct of EA (EA-GSH) was the most potent inhibitor of GSTs; EA-GSH was approximately one order of magnitude more potent than the parent EA, while L-cysteine conjugate of EA (EA-cysteine) and N-acetyl-L-cysteine conjugate of EA (EA-mercapturate) were approximately two orders of magnitude less potent than the parent EA.	ea-gsh	69-75	glutathione S-transferase kappa 1	Homo sapiens	63-67	
1412509-4	1992	Further metabolism of EA-GSH conjugate is suggested to be a detoxification process in terms of GST activities.	ea-gsh	22-28	glutathione S-transferase kappa 1	Homo sapiens	95-98