PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
21605992-6	2011	The superiority of hydroxylamine anion to reactivate the sarin-inhibited AChE with sarin-serine adducts 3 and 4 compared to formoximate anion was observed in the presence and absence of hydrogen bonding interactions of Gly121 and Gly122.	formoximate anion	124-141	acetylcholinesterase (Cartwright blood group)	Homo sapiens	73-77	
21850569-3	2012	The calculated results suggest that the hydroxylamine anion is more efficient than the formoximate anion at reactivating VX-inhibited AChE.	formoximate anion	87-104	acetylcholinesterase (Cartwright blood group)	Homo sapiens	134-138	
21850569-4	2012	The reaction of formoximate anion and the VX-AChE adduct is a three-step process, while the reaction of hydroxylamine anion with the VX-AChE adduct seems to be a two-step process.	formoximate anion	16-33	acetylcholinesterase (Cartwright blood group)	Homo sapiens	45-49	
21850569-7	2012	The potential energy surface (PES) for the reaction of the VX-AChE adduct with hydroxylamine anion reveals that the reactivation process is facilitated by the lower free energy of activation (by a factor of 1.7 kcal mol(-1)) than that of the formoximate anion at the B3LYP/6-311 G(d,p) level of theory.	formoximate anion	242-259	acetylcholinesterase (Cartwright blood group)	Homo sapiens	62-66