PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
14996830-1	2004	Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (PI-PLC), a bacterial model for the catalytic domain of mammalian PI-PLC enzymes, was cross-linked by 1-ethyl-3-[3-dimethylaminopropyl]carbodiimide hydrochloride to probe for the aggregation and/or conformational changes of PI-PLC when bound to activating phosphatidylcholine (PC) interfaces.	1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride	171-230	phospholipase C beta 1	Homo sapiens	23-68	
14996830-1	2004	Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (PI-PLC), a bacterial model for the catalytic domain of mammalian PI-PLC enzymes, was cross-linked by 1-ethyl-3-[3-dimethylaminopropyl]carbodiimide hydrochloride to probe for the aggregation and/or conformational changes of PI-PLC when bound to activating phosphatidylcholine (PC) interfaces.	1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride	171-230	phospholipase C beta 1	Homo sapiens	70-76	
14996830-1	2004	Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (PI-PLC), a bacterial model for the catalytic domain of mammalian PI-PLC enzymes, was cross-linked by 1-ethyl-3-[3-dimethylaminopropyl]carbodiimide hydrochloride to probe for the aggregation and/or conformational changes of PI-PLC when bound to activating phosphatidylcholine (PC) interfaces.	1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride	171-230	phospholipase C beta 1	Homo sapiens	135-141	
14996830-1	2004	Bacillus thuringiensis phosphatidylinositol-specific phospholipase C (PI-PLC), a bacterial model for the catalytic domain of mammalian PI-PLC enzymes, was cross-linked by 1-ethyl-3-[3-dimethylaminopropyl]carbodiimide hydrochloride to probe for the aggregation and/or conformational changes of PI-PLC when bound to activating phosphatidylcholine (PC) interfaces.	1-ethyl-3-(3-dimethylaminopropyl)carbodiimide hydrochloride	171-230	phospholipase C beta 1	Homo sapiens	135-141