PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
18501885-3	2008	Both cholinesterases showed the highest affinity for K114 (K(i) was 0.01 mM for AChE and 0.06 mM for BChE).	K114	53-57	acetylcholinesterase (Cartwright blood group)	Homo sapiens	80-84	
18501885-6	2008	The reactivation of tabun-inhibited AChE assisted by K114 was slow and reached 90% after 20 h. Since the aldoxime binding affinity of tabun-inhibited AChE was similar for all tested aldoximes (and corresponded to their K(i)), the rate of the nucleophilic displacement of the phosphoryl-moiety from the active site serine was the limiting factor for AChE reactivation.	K114	53-57	acetylcholinesterase (Cartwright blood group)	Homo sapiens	36-40	
20417629-1	2010	Catalytic activity of acetylcholinesterase (AChE; EC 3.1.1.7) was studied in the presence of oximes HI-6, K114, K127 and K203, and inhibition constants were determined for the reversible enzyme-inhibitor complex (K(I)).	K114	106-110	acetylcholinesterase (Cartwright blood group)	Homo sapiens	22-42	
20417629-1	2010	Catalytic activity of acetylcholinesterase (AChE; EC 3.1.1.7) was studied in the presence of oximes HI-6, K114, K127 and K203, and inhibition constants were determined for the reversible enzyme-inhibitor complex (K(I)).	K114	106-110	acetylcholinesterase (Cartwright blood group)	Homo sapiens	44-48