PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
8128641-5	1993	Experiments in vivo have shown that even a high dose of tabun (12 mg/kg, 120 LD50), given with antidotes, which inhibited 67% of NTE activity did not initiate delayed neuropathic effects.	tabun	56-61	patatin like phospholipase domain containing 6	Gallus gallus	129-132
35526478-4	2022	Mono-fluorinated oximes showed comparable reactivation to non-halogenated (except asoxime) and mono-chlorinated oximes in case of AChE inhibited by sarin, cyclosarin, VX, and tabun, but were less efficient than di-chlorinated ones.	tabun	175-180	acetylcholinesterase (Cartwright blood group)	Homo sapiens	130-134
3341026-13	1988	Two birds which survived out of eight pretreated with tabun (12 mg/kg sc) had about as much NTE inhibited as after soman administration but it was all in the modified (aged) inhibited form; these birds were not protected against DFP-induced neuropathy.	tabun	54-59	patatin like phospholipase domain containing 6	Gallus gallus	92-95
2709438-1	1989	The LD50s and ED50s for inhibition of acetylcholinesterase (AChE) in whole mouse brain by DFP (diisopropylfluorophosphate), sarin (methylphosphonofluoridic acid 1-methyl ethyl ester), soman (methylphosphonofluoridic acid 1,2,2-trimethyl propyl ester), and tabun (dimethylphosphoramidocyanidic acid ethyl ester) were compared after iv administration.	tabun	256-261	acetylcholinesterase	Mus musculus	60-64
2709438-1	1989	The LD50s and ED50s for inhibition of acetylcholinesterase (AChE) in whole mouse brain by DFP (diisopropylfluorophosphate), sarin (methylphosphonofluoridic acid 1-methyl ethyl ester), soman (methylphosphonofluoridic acid 1,2,2-trimethyl propyl ester), and tabun (dimethylphosphoramidocyanidic acid ethyl ester) were compared after iv administration.	tabun	263-309	acetylcholinesterase	Mus musculus	60-64
5576158-2	1971	Tabun is a more potent inhibitor of acetylcholinesterase than is DFP, is both lipid-and water-soluble, and penetrates readily into the squid giant axon in its inhibitory form.	tabun	0-5	acetylcholinesterase (Cartwright blood group)	Homo sapiens	36-56
4083033-7	1985	The striatal AChE activity of the tabun-treated group was only 13% of control.	tabun	34-39	acetylcholinesterase	Rattus norvegicus	13-17
13079852-0	1953	Protective effect of phenothiazine derivatives against poisoning by the irreversible cholinesterase inhibitor dimethylamidoethoxyphosphoryl cyanide (tabun).	tabun	110-147	butyrylcholinesterase	Homo sapiens	85-99
13079852-0	1953	Protective effect of phenothiazine derivatives against poisoning by the irreversible cholinesterase inhibitor dimethylamidoethoxyphosphoryl cyanide (tabun).	tabun	149-154	butyrylcholinesterase	Homo sapiens	85-99
33538594-5	2021	To gain insight into this issue, the structures of hAChE inhibited by tabun, sarin, cyclosarin, soman, and GP were obtained along with the inhibition kinetics for these agents.	tabun	70-75	acetylcholinesterase (Cartwright blood group)	Homo sapiens	51-56
33538594-8	2021	To identify the structural underpinnings of this phenomenon, the structures of tabun, sarin, and soman-inhibited hAChE in complex with HI-6 were determined.	tabun	79-84	acetylcholinesterase (Cartwright blood group)	Homo sapiens	113-118
31791835-1	2020	Pellets with an immobilized enzyme (acetyl- or butyrylcholinesterase) are the up-to-date type of carriers used for the detection of nerve agents (soman, sarin, tabun, VX, Novichok) and other cholinesterase inhibitors such as organophosphate and carbamate insecticides (parathion, malathion).	tabun	160-165	butyrylcholinesterase	Homo sapiens	54-68
32454005-5	2020	All compounds were assessed for their ability to reactivate human acetylcholinesterase inhibited by the nerve agents VX, tabun, sarin, cyclosarin and paraoxon in vitro.	tabun	121-126	acetylcholinesterase (Cartwright blood group)	Homo sapiens	66-86
33517499-5	2021	More importantly, these reactivators exhibited wide-spectrum efficacy and were minutely investigated via determination of their reactivation kinetics in parallel with molecular dynamics simulations to study their mechanisms of reactivation of the tabun-inhibited AChE conjugate.	tabun	247-252	acetylcholinesterase	Mus musculus	263-267
26368669-1	2015	Tabun-inhibited acetylcholinesterase (AChE) is rather resistant towards reactivation by oximes in vitro while in vivo experiments showed some protection of animals poisoned by this chemical warfare nerve agent after treatment with an oxime and atropine.	tabun	0-5	acetylcholinesterase (Cartwright blood group)	Homo sapiens	16-36
31191210-9	2019	In vitro reactivation potency is high for ethyl-paraoxon-, methyl-paraoxon-, dichlorvos-, diisopropylfluorophosphate (DFP)- and tabun-inhibited cholinesterase.	tabun	128-133	butyrylcholinesterase	Homo sapiens	144-158
29772260-7	2018	Therefore, it seems that aromatic amino acids at the peripheral binding site presented a limitation in bispyridinium oxime reactivation efficiency of tabun-phosphorylated AChE.	tabun	150-155	acetylcholinesterase (Cartwright blood group)	Homo sapiens	171-175
28446076-1	2018	Tabun is one of the most dangerous nerve agents because it has deleterious effects like inhibition of the essential enzymes acetylcholinesterase (AChE) and butyrylcholinesterase.	tabun	0-5	acetylcholinesterase (Cartwright blood group)	Homo sapiens	124-144
28446076-1	2018	Tabun is one of the most dangerous nerve agents because it has deleterious effects like inhibition of the essential enzymes acetylcholinesterase (AChE) and butyrylcholinesterase.	tabun	0-5	acetylcholinesterase (Cartwright blood group)	Homo sapiens	146-150
31969483-3	2020	In the present study, we have demonstrated an adeno-associated virus 8 (AAV8)-mediated paraoxonase 1 variant IF-11 (PON1-IF11) gene therapy that offers asymptomatic prophylactic protection to mice against multiple lethal doses of G-type chemical warfare nerve agents, namely, tabun, sarin, cyclosarin, and soman, for up to 5 months in mice.	tabun	276-281	paraoxonase 1	Mus musculus	87-100
30978400-7	2019	Indeed, after initial screening of the triazole oxime library and its precursors for the reactivation efficacy on Y337A and Y337A/F338A human AChE mutants, we found potentially active oxime-mutant enzyme pairs capable of degrading tabun in cycles of inhibition and reactivation.	tabun	231-236	acetylcholinesterase (Cartwright blood group)	Homo sapiens	142-146
30978400-9	2019	Hence, although the use of mutant enzyme bio-scavengers in humans may be limited in practicality, bioscavenging and efficient neutralization of tabun itself or phosphoramidate mixtures of organophosphates might be achieved efficiently in vitro or ex vivo with these mutant AChE combinations.	tabun	144-149	acetylcholinesterase (Cartwright blood group)	Homo sapiens	273-277
30458057-0	2019	Reversal of Tabun Toxicity Enabled by a Triazole-Annulated Oxime Library-Reactivators of Acetylcholinesterase.	tabun	12-17	acetylcholinesterase (Cartwright blood group)	Homo sapiens	89-109
30458057-5	2019	We identified several oximes with significantly improved in vitro reactivating potential for tabun-inhibited human AChE, and in vivo antidotal efficacies in tabun-exposed mice.	tabun	93-98	acetylcholinesterase (Cartwright blood group)	Homo sapiens	115-119
30205495-5	2018	The novel compounds were prepared, evaluated in vitro on human AChE (HssAChE) inhibited by tabun, paraoxon, methylparaoxon or DFP and compared to commercial HssAChE reactivators (pralidoxime, methoxime, trimedoxime, obidoxime, asoxime) or previously prepared compounds (K048, K074, K075, K203).	tabun	91-96	acetylcholinesterase (Cartwright blood group)	Homo sapiens	63-67
29467029-8	2018	DISCUSSION: According to these results and previous studies, using K203, it appears that oxime K203 is the most effective reactivator of tabun-inhibited cholinesterase in several species including humans and should be considered as a possible medical countermeasure to tabun exposure.	tabun	137-142	butyrylcholinesterase	Homo sapiens	153-167
26368669-1	2015	Tabun-inhibited acetylcholinesterase (AChE) is rather resistant towards reactivation by oximes in vitro while in vivo experiments showed some protection of animals poisoned by this chemical warfare nerve agent after treatment with an oxime and atropine.	tabun	0-5	acetylcholinesterase (Cartwright blood group)	Homo sapiens	38-42
23527625-0	2014	Reactivation steps by 2-PAM of tabun-inhibited human acetylcholinesterase: reducing the computational cost in hybrid QM/MM methods.	tabun	31-36	peptidylglycine alpha-amidating monooxygenase	Homo sapiens	24-27
24443939-8	2014	The reactivation of AChE inactivated with either cyclosarin or tabun requires the oxime therapeutic to possess an overall polar-positive surface area.	tabun	63-68	acetylcholinesterase (Cartwright blood group)	Homo sapiens	20-24
23527625-0	2014	Reactivation steps by 2-PAM of tabun-inhibited human acetylcholinesterase: reducing the computational cost in hybrid QM/MM methods.	tabun	31-36	acetylcholinesterase (Cartwright blood group)	Homo sapiens	53-73
22343626-2	2012	Starting with the initial lead oxime RS41A identified in our earlier study and extending to the azepine analog RS194B, reactivation rates for OP-hAChE conjugates formed by sarin, cyclosarin, VX, paraoxon, and tabun are enhanced severalfold in vitro.	tabun	209-214	acetylcholinesterase (Cartwright blood group)	Homo sapiens	145-150
23220589-6	2013	The aim of the present study was to evaluate the efficacy of some ChE reactivators against OPC intoxication (tabun, paraoxon and dichlorvos) in in vitro experiments and to compare their activity to that known for some currently used oximes (obidoxime, HI-6, 2-PAM).	tabun	109-114	butyrylcholinesterase	Rattus norvegicus	66-69
23376121-1	2013	Nerve agents such as tabun, cyclosarin and Russian VX inhibit the essential enzyme acetylcholinesterase (AChE) by organophosphorylating the catalytic serine residue.	tabun	21-26	acetylcholinesterase (Cartwright blood group)	Homo sapiens	83-103
23376121-1	2013	Nerve agents such as tabun, cyclosarin and Russian VX inhibit the essential enzyme acetylcholinesterase (AChE) by organophosphorylating the catalytic serine residue.	tabun	21-26	acetylcholinesterase (Cartwright blood group)	Homo sapiens	105-109
22975155-1	2013	A library of more than 200 novel uncharged oxime reactivators was used to select and refine lead reactivators of human acetylcholinesterase (hAChE) covalently conjugated with sarin, cyclosarin, VX, paraoxon and tabun.	tabun	211-216	acetylcholinesterase (Cartwright blood group)	Homo sapiens	141-146
23148598-2	2012	Herein, we described a series of nine nonquaternary phenyltetrahydroisoquinoline-pyridinaldoxime conjugates more efficient than or as efficient as pyridinium oximes to reactivate VX-, tabun- and ethyl paraoxon-inhibited human AChE.	tabun	184-189	acetylcholinesterase (Cartwright blood group)	Homo sapiens	226-230
22808117-1	2012	Oxime drugs translocate through the 20 A active-site gorge of acetylcholinesterase in order to liberate the enzyme from organophosphorus compounds" (such as tabun) conjugation.	tabun	157-162	acetylcholinesterase (Cartwright blood group)	Homo sapiens	62-82
21767560-5	2011	The present report summarizes our observations on plasma acetylcholinesterase activity in mice treated with chlorpyrifos, chlorpyrifos oxon, diazinon, tri-ortho-cresyl phosphate, tri-cresyl phosphate, tabun thiocholine, parathion, dichlorvos, and diisopropylfluorophosphate.	tabun	201-206	acetylcholinesterase	Mus musculus	57-77
20408548-1	2010	Tabun is a warfare agent that inhibits human acetylcholinesterase (hAChE) by rapid phosphylation of the catalytic serine.	tabun	0-5	acetylcholinesterase	Mus musculus	45-65
21054236-0	2010	A comparison of tabun-inhibited rat brain acetylcholinesterase reactivation by three oximes (HI-6, obidoxime, and K048) in vivo detected by biochemical and histochemical techniques.	tabun	16-21	acetylcholinesterase	Rattus norvegicus	42-62
20408548-1	2010	Tabun is a warfare agent that inhibits human acetylcholinesterase (hAChE) by rapid phosphylation of the catalytic serine.	tabun	0-5	acetylcholinesterase (Cartwright blood group)	Homo sapiens	67-72
19329372-3	2009	Tabun-inhibited AChE was completely reactivated by K203, with the overall reactivation rate constant of 1806 L mol(-1) min(-1).	tabun	0-5	acetylcholinesterase	Rattus norvegicus	16-20
19746406-2	2010	The ability of two combinations of oximes (HI-6 + obidoxime and HI-6 + K203) to reactivate tabun-inhibited acetylcholinesterase and reduce acute toxicity of tabun was compared with the reactivating and therapeutic efficacy of antidotal treatment involving single oxime (HI-6, obidoxime, K203) using in vivo methods.	tabun	91-96	acetylcholinesterase	Rattus norvegicus	107-127
19746406-6	2010	Based on the obtained data, we can conclude that the antidotal treatment involving chosen combinations of oximes brings beneficial effects for the potency of antidotal treatment to reactivate tabun-inhibited acetylcholinesterase in rats and to reduce acute toxicity of tabun in mice.	tabun	192-197	acetylcholinesterase	Rattus norvegicus	208-228
18608751-1	2008	The potency of newly developed bispyridinium compounds (K206, K269) in reactivating tabun-inhibited acetylcholinesterase and eliminating tabun-induced lethal toxic effects was compared with commonly used oximes (obidoxime, trimedoxime, the oxime HI-6) using in vivo methods.	tabun	84-89	acetylcholinesterase	Rattus norvegicus	100-120
17910616-6	2007	HI-6 dichloride showed a somewhat higher potency to reactivate tabun-inhibited acetylcholinesterase in brain, and soman-inhibited acetylcholinesterase in blood and brain than HI-6 dimethanesulphonate but the differences were not significant.	tabun	63-68	acetylcholinesterase	Rattus norvegicus	79-99
18608751-7	2008	Both newly developed oximes (K206, K269) are significantly more efficacious in reactivating tabun-inhibited AChE in rats and to eliminate lethal toxic effects of tabun in mice than the oxime HI-6 but their reactivating and therapeutic potency does not prevail over the effectiveness of currently available obidoxime and trimedoxime and, therefore, they are not suitable for their replacement of commonly used oximes for the treatment of acute tabun poisoning.	tabun	92-97	acetylcholinesterase	Rattus norvegicus	108-112
18501341-0	2008	Oximes: Reactivators of phosphorylated acetylcholinesterase and antidotes in therapy against tabun poisoning.	tabun	93-98	acetylcholinesterase (Cartwright blood group)	Homo sapiens	39-59
18622871-1	2008	The potency of newly developed bispyridinium compounds (K117, K127) to reactivate tabun-inhibited acetylcholinesterase and reduce tabun-induced lethal toxic effects was compared with currently available oximes (obidoxime, trimedoxime, oxime HI-6) by using in vivo methods.	tabun	82-87	acetylcholinesterase	Rattus norvegicus	98-118
17924614-0	2007	Design of a potent reactivator of tabun-inhibited acetylcholinesterase--synthesis and evaluation of (E)-1-(4-carbamoylpyridinium)-4-(4-hydroxyiminomethylpyridinium)-but-2-ene dibromide (K203).	tabun	34-39	acetylcholinesterase (Cartwright blood group)	Homo sapiens	50-70
17370251-5	2007	In order to investigate the feasibility of combining obidoxime and HI 6, human AChE inhibited by sarin, cyclosarin, VX, tabun and paraoxon was reactivated by these oximes either alone or in combination.	tabun	120-125	acetylcholinesterase (Cartwright blood group)	Homo sapiens	79-83
17562604-3	2007	Tabun-inhibited human erythrocyte acetylcholinesterase was completely reactivated only by the most flexible bispyridinium aldoxime - TMB-4 with a propylene chain between two rings.	tabun	0-5	acetylcholinesterase (Cartwright blood group)	Homo sapiens	34-54
15379785-1	2004	The efficacy of various oximes to reactivate acetylcholinesterase phosphorylated by tabun (O-ethyl-N,N-dimethyl phosphoramidocyanidate) was tested by in vitro and in vivo methods.	tabun	84-89	acetylcholinesterase (Cartwright blood group)	Homo sapiens	45-65
17194020-1	2006	Nerve agents such as sarin, cyclosarin and tabun are organophosphorus substances able to inhibit the enzyme acetylcholinesterase (AChE; EC 3.1.1.7).	tabun	43-48	acetylcholinesterase (Cartwright blood group)	Homo sapiens	108-128
17194020-1	2006	Nerve agents such as sarin, cyclosarin and tabun are organophosphorus substances able to inhibit the enzyme acetylcholinesterase (AChE; EC 3.1.1.7).	tabun	43-48	acetylcholinesterase (Cartwright blood group)	Homo sapiens	130-134
16952906-2	2006	Studies determined the percent of reactivation of tabun-inhibited blood and tissue AChE in poisoned rats and showed that the reactivating efficacy of both newly developed oximes is comparable with obidoxime and trimedoxime, the most efficacious known reactivators of tabun-inhibited AChE.	tabun	50-55	acetylcholinesterase	Rattus norvegicus	83-87
16388582-0	2006	Structural changes of phenylalanine 338 and histidine 447 revealed by the crystal structures of tabun-inhibited murine acetylcholinesterase.	tabun	96-101	acetylcholinesterase	Mus musculus	119-139
16601802-3	2005	The potency of trimedoxime and other commonly used oximes (pralidoxime, obidoxime, the oxime HI-6) to reactivate tabun-inhibited acetylcholinesterase and to eliminate tabun-induced acute effects was evaluated using in vitro and in vivo methods.	tabun	113-118	acetylcholinesterase	Rattus norvegicus	129-149
15065394-0	2004	[Effect of acetylcholinesterase reactivator dosage on its effectiveness in the treatment of tabun poisoning in mice].	tabun	92-97	acetylcholinesterase	Mus musculus	11-31
15446360-4	2004	The therapeutic efficacy of antidotal treatment of tabun-induced acute poisoning depends on the time of its administration when obidoxime or the oxime HI-6 was used as an acetylcholinesterase reactivator.	tabun	51-56	acetylcholinesterase	Mus musculus	171-191
15065394-7	2004	The most suitable reactivator of acetylcholinesterase for the elimination of acute lethal toxic effects of tabun seems to be trimedoxime.	tabun	107-112	acetylcholinesterase	Mus musculus	33-53
15639788-1	2004	We investigated the relationship between the chemical structure of acetylcholinesterase (AChE; EC 3.1.1.7) reactivators and their potency in reactivating this enzyme, after prior inhibition by VX (O-ethyl-S-(2-diisopropylaminoethyl)-methylthiophosphonate), tabun, sarin, and cyclosarin.	tabun	257-262	acetylcholinesterase	Rattus norvegicus	67-87
15639788-1	2004	We investigated the relationship between the chemical structure of acetylcholinesterase (AChE; EC 3.1.1.7) reactivators and their potency in reactivating this enzyme, after prior inhibition by VX (O-ethyl-S-(2-diisopropylaminoethyl)-methylthiophosphonate), tabun, sarin, and cyclosarin.	tabun	257-262	acetylcholinesterase	Rattus norvegicus	89-93