PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
27174897-0	2016	Methionine-choline deprivation alters liver and brain acetylcholinesterase activity in C57BL6 mice.	Choline	11-18	acetylcholinesterase	Mus musculus	54-74	
27174897-1	2016	Choline and methionine are precursors of acetylcholine, whose hydrolysis is catalyzed by acetylcholinesterase (AChE).	Choline	0-7	acetylcholinesterase	Mus musculus	89-109	
27174897-1	2016	Choline and methionine are precursors of acetylcholine, whose hydrolysis is catalyzed by acetylcholinesterase (AChE).	Choline	0-7	acetylcholinesterase	Mus musculus	111-115	
27174897-9	2016	Our findings indicate the increase of hepatic and brain AChE activity in mice caused by methionine-choline deprivation.	Choline	99-106	acetylcholinesterase	Mus musculus	56-60	
18023504-0	2008	Choline availability and acetylcholine synthesis in the hippocampus of acetylcholinesterase-deficient mice.	Choline	0-7	acetylcholinesterase	Mus musculus	71-91	
26879641-3	2016	Mutation of mAChE within the choline binding site by Y337A and F338A and its interaction with Ortho-7 has been investigated using steered molecular dynamics (SMD) and quantum chemical methods.	Choline	29-36	acetylcholinesterase	Mus musculus	12-17	
26250336-1	2015	Acetylcholinesterase (AChE) hydrolyzes acetylcholine (ACh) to acetate and choline and thereby terminates nerve impulse transmission.	Choline	6-13	acetylcholinesterase	Mus musculus	22-26	
24274995-1	2014	The hemicholinium-3 (HC-3) sensitive, high-affinity choline transporter (CHT) sustains cholinergic signaling via the presynaptic uptake of choline derived from dietary sources or from acetylcholinesterase (AChE)-mediated hydrolysis of acetylcholine (ACh).	Choline	52-59	acetylcholinesterase	Mus musculus	184-204	
24274995-1	2014	The hemicholinium-3 (HC-3) sensitive, high-affinity choline transporter (CHT) sustains cholinergic signaling via the presynaptic uptake of choline derived from dietary sources or from acetylcholinesterase (AChE)-mediated hydrolysis of acetylcholine (ACh).	Choline	52-59	acetylcholinesterase	Mus musculus	206-210	
26494532-7	2015	However, in the case of tabun-mutant mAChE(Y337A).K048 conjugate, the replacement of aromatic Tyr337 with the aliphatic alanine unit in the choline binding site, however, loses one of the pi-pi interaction between the active pyridinium ring of K048 and the Tyr337.	Choline	140-147	acetylcholinesterase	Mus musculus	37-42	
18023504-5	2008	Using microdialysis, we found that increased ACh levels are accompanied by decreased levels of extracellular choline which were 1.60 microM in AChE-deficient mice and 4.36 microM in wild-type mice.	Choline	109-116	acetylcholinesterase	Mus musculus	143-147	
18023504-6	2008	Addition of choline (10 microM) to the perfusion fluid, while ineffective in wild-type animals, more than doubled extracellular ACh levels in AChE-deficient mice.	Choline	12-19	acetylcholinesterase	Mus musculus	142-146	
18023504-7	2008	High-affinity choline uptake (HACU), as measured ex vivo in corticohippocampal synaptosomes, was more than doubled in AChE-deficient mice.	Choline	14-21	acetylcholinesterase	Mus musculus	118-122	
18023504-11	2008	In conclusion, absence of AChE causes dynamic changes in the ratio of choline to ACh.	Choline	70-77	acetylcholinesterase	Mus musculus	26-30	
18167304-7	2008	The enlargement of the AChE choline binding site and of the acyl pocket by single or double mutations (Y337A, F295L/Y337A and F297I/Y337A) increased, in comparison to w.t.	Choline	28-35	acetylcholinesterase	Mus musculus	23-27	
2569343-9	1989	In vitro concentrations of choline, MEC, and NAD, similar to the estimated concentration obtained in vivo in the acute toxicity study, produced mixed inhibition of mouse brain acetylcholinesterase.	Choline	27-34	acetylcholinesterase	Mus musculus	176-196	
11920914-5	2001	These observations suggest that peripheral site ligands are capable of allosterically affecting the conformation of residues in the choline binding site of AChE, thus optimizing the position of the leaving group of uncharged organophosphates during the inhibition reaction.	Choline	132-139	acetylcholinesterase	Mus musculus	156-160	
9851655-8	1998	AChE activity produces protons and choline, possible microglial activators.	Choline	35-42	acetylcholinesterase	Mus musculus	0-4	
10446376-8	1999	Replacement of tyrosine-337 in AChE with alanine (resembling the choline binding site of BChE) resulted in 630 times faster inhibition by bambuterol.	Choline	65-72	acetylcholinesterase	Mus musculus	31-35	
33666613-2	2021	Acetylcholinesterase (AChE) is one of the most important bioactive substances and plays a major part in choline changes in the aging process.	Choline	6-13	acetylcholinesterase	Mus musculus	22-26	
28286520-4	2017	AChE degrades acetylcholine into choline and acetic acid which causes color change of acid-base indicator.	Choline	20-27	acetylcholinesterase	Mus musculus	0-4	
27618041-3	2016	AChE splits acetylcholine into choline and acetic acid, which changes the pH of a medium, resulting in a phenol red color change.	Choline	18-25	acetylcholinesterase	Mus musculus	0-4