PMID-sentid	Pub_year	Sent_text		comp_official_name	comp_offsetprotein_name	organism	prot_offset
9271331-5	1997	Substitution of glutamine for glutamate (E199) located at the amino-terminal to the active-site serine (S200) in Torpedo AChE generated an enzyme largely resistant to aging.	Serine	96-102	acetylcholinesterase	Mus musculus	121-125	
26494532-5	2015	The SMD simulations showed that the active pyridinium ring of K048 is directed towards the phosphorus atom conjugated to the active serine (SUN203) of tabun-mAChE(wild-type).	Serine	132-138	acetylcholinesterase	Mus musculus	157-162	
31226285-7	2019	Whereas benzenesulfonyl fluoride closely approaches the active-site serine in both mouse and Torpedo acetylcholinesterase in such simulations, phenylmethylsulfonyl fluoride is able to approach the active-site serine of mouse acetylcholinesterase, but remains trapped above the bottleneck in the Torpedo enzyme.	Serine	68-74	acetylcholinesterase	Mus musculus	101-121	
8530502-7	1995	The time course analysis reveals that the increase in serine/threonine activity precedes the effect of T3 on AChE mRNAs.	Serine	54-60	acetylcholinesterase	Mus musculus	109-113	
26494532-9	2015	Such displacement is causing the inaccessibility of the drug towards the phosphorus atom conjugated to the active serine (SUN203) of tabun-mutant mAChE(Y337A).	Serine	114-120	acetylcholinesterase	Mus musculus	146-151	
26494532-10	2015	Furthermore, the unbinding of the K048 with SMD studies showed that the active pyridinium ring of the drug undergoes a complete turn along the gorge axis and is directed away from the phosphorus atom conjugated to the active serine of the tabun-mutant mAChE(Y337A).	Serine	225-231	acetylcholinesterase	Mus musculus	252-257	
17192653-1	2006	The progressive inhibition of acetylcholinesterase (AChE [EC 3.1.1.7]) by organophosphates (OPs), such as the nerve agents tabun and soman, is due to phosphorylation of the active center serine characterized by the formation of conjugates and inactivation of this essential enzyme involved in neurotransmission.	Serine	187-193	acetylcholinesterase	Mus musculus	30-50	
22425525-2	2012	CPO is also responsible for the acetylcholinesterase (AChE) inhibition associated with CPF exposures; CPF is converted by liver CYP450 enzymes to CPO, which binds to and inhibits AChE and other serine active-site esterases, lipases and proteases.	Serine	194-200	acetylcholinesterase	Mus musculus	54-58	
22425525-2	2012	CPO is also responsible for the acetylcholinesterase (AChE) inhibition associated with CPF exposures; CPF is converted by liver CYP450 enzymes to CPO, which binds to and inhibits AChE and other serine active-site esterases, lipases and proteases.	Serine	194-200	acetylcholinesterase	Mus musculus	32-52	
20408548-1	2010	Tabun is a warfare agent that inhibits human acetylcholinesterase (hAChE) by rapid phosphylation of the catalytic serine.	Serine	114-120	acetylcholinesterase	Mus musculus	45-65	
19732756-1	2010	Organophosphorus insecticides and nerve agents inhibit the vital enzyme acetylcholinesterase by covalently bonding to the catalytic serine residue of the enzyme.	Serine	132-138	acetylcholinesterase	Mus musculus	72-92	
18215127-8	2008	Docking showed the major component of the interaction site on AChE to be the acidic sequence Arg(90)-Glu-Leu-Ser-Glu-Asp(95) on the omega loop, and also the involvement of Pro(40)-Pro-Val(42), Arg(46) (linked to Glu(94) by a salt bridge) and the hexapeptide Asp(61)-Ala-Thr-Thr-Phe-Gln(66).	Serine	109-112	acetylcholinesterase	Mus musculus	62-66	
16388582-1	2006	Organophosphorus compounds (OPs) interfere with the catalytic mechanism of acetylcholinesterase (AChE) by rapidly phosphorylating the catalytic serine residue.	Serine	144-150	acetylcholinesterase	Mus musculus	75-95	
16388582-1	2006	Organophosphorus compounds (OPs) interfere with the catalytic mechanism of acetylcholinesterase (AChE) by rapidly phosphorylating the catalytic serine residue.	Serine	144-150	acetylcholinesterase	Mus musculus	97-101	
17192653-1	2006	The progressive inhibition of acetylcholinesterase (AChE [EC 3.1.1.7]) by organophosphates (OPs), such as the nerve agents tabun and soman, is due to phosphorylation of the active center serine characterized by the formation of conjugates and inactivation of this essential enzyme involved in neurotransmission.	Serine	187-193	acetylcholinesterase	Mus musculus	52-56	
10898598-7	2000	Most importantly, POCl(3)-induced electric eel AChE inhibition prevents postlabeling with [(3)H]diisopropyl phosphorofluoridate; i.e., both compounds phosphorylate at Ser-200 in the catalytic triad.	Serine	167-170	acetylcholinesterase	Mus musculus	47-51	
12933813-1	2003	Two types of polyclonal antibodies were generated from (a) a decapeptide sequence that includes the active site serine of acetylcholinesterase (anti-AChE10S) and (b) the identical decapeptide sequence phosphorylated at the active site serine of acetylcholinesterase (anti-AChE10SP).	Serine	112-118	acetylcholinesterase	Mus musculus	122-142	
12974645-3	2003	The tryptic peptide of mAChE that contains the active center serine residue resolves to a molecular mass of 4331.0 Da.	Serine	61-67	acetylcholinesterase	Mus musculus	23-28	
12974645-5	2003	The relative abundance of AChE peptides containing a modified active center serine strongly correlates with the fractional inhibition of the enzyme, achieving a detection range of phosphorylated to nonphosphorylated enzyme of 5-95%.	Serine	76-82	acetylcholinesterase	Mus musculus	26-30	
12974645-8	2003	Further, the tryptic peptide containing the active center serine of AChE, isolated from mouse brain by anion-exchange and affinity chromatography, has been monitored by mass spectrometry.	Serine	58-64	acetylcholinesterase	Mus musculus	68-72