PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17698511-1 2007 Some organophosphorus compounds are toxic because they inhibit acetylcholinesterase (AChE) by phosphylation of the active site serine, forming a stable conjugate: Ser-O-P(O)-(Y)-(XR) (where X can be O, N, or S and Y can be methyl, OR, or SR). Serine 127-133 acetylcholinesterase (Cartwright blood group) Homo sapiens 63-83 19761810-1 2009 The nerve agent tabun inhibits the essential enzyme acetylcholinesterase (AChE) by a rapid phosphoramidation of the catalytic serine residue. Serine 126-132 acetylcholinesterase (Cartwright blood group) Homo sapiens 52-72 19761810-1 2009 The nerve agent tabun inhibits the essential enzyme acetylcholinesterase (AChE) by a rapid phosphoramidation of the catalytic serine residue. Serine 126-132 acetylcholinesterase (Cartwright blood group) Homo sapiens 74-78 19536291-1 2009 Organophosphonates such as isopropyl metylphosphonofluoridate (sarin) are extremely toxic as they phosphonylate the catalytic serine residue of acetylcholinesterase (AChE), an enzyme essential to humans and other species. Serine 126-132 acetylcholinesterase (Cartwright blood group) Homo sapiens 144-164 19536291-1 2009 Organophosphonates such as isopropyl metylphosphonofluoridate (sarin) are extremely toxic as they phosphonylate the catalytic serine residue of acetylcholinesterase (AChE), an enzyme essential to humans and other species. Serine 126-132 acetylcholinesterase (Cartwright blood group) Homo sapiens 166-170 19194505-1 2009 Aphids, among the most destructive insects to world agriculture, are mainly controlled by organophosphate insecticides that disable the catalytic serine residue of acetylcholinesterase (AChE). Serine 146-152 acetylcholinesterase (Cartwright blood group) Homo sapiens 164-184 19194505-1 2009 Aphids, among the most destructive insects to world agriculture, are mainly controlled by organophosphate insecticides that disable the catalytic serine residue of acetylcholinesterase (AChE). Serine 146-152 acetylcholinesterase (Cartwright blood group) Homo sapiens 186-190 18565503-1 2008 Exposure to the organophosphorus nerve agents such as sarin, soman, cyclosarin, and VX causes acute intoxication by inhibiting acetylcholinesterase (AChE), where the serine residue of the active site can attack the phosphorous atom of the organophosphorus agents to form a strong P-O bond. Serine 166-172 acetylcholinesterase (Cartwright blood group) Homo sapiens 127-147 18565503-1 2008 Exposure to the organophosphorus nerve agents such as sarin, soman, cyclosarin, and VX causes acute intoxication by inhibiting acetylcholinesterase (AChE), where the serine residue of the active site can attack the phosphorous atom of the organophosphorus agents to form a strong P-O bond. Serine 166-172 acetylcholinesterase (Cartwright blood group) Homo sapiens 149-153 18975951-2 2008 Organophosphates (OPs) exert their acute toxicity through inhibition of acetylcholinesterase (AChE) by phosphorylation of the catalytic serine. Serine 136-142 acetylcholinesterase (Cartwright blood group) Homo sapiens 72-92 18975951-2 2008 Organophosphates (OPs) exert their acute toxicity through inhibition of acetylcholinesterase (AChE) by phosphorylation of the catalytic serine. Serine 136-142 acetylcholinesterase (Cartwright blood group) Homo sapiens 94-98 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. Serine 314-320 acetylcholinesterase (Cartwright blood group) Homo sapiens 36-40 17698511-1 2007 Some organophosphorus compounds are toxic because they inhibit acetylcholinesterase (AChE) by phosphylation of the active site serine, forming a stable conjugate: Ser-O-P(O)-(Y)-(XR) (where X can be O, N, or S and Y can be methyl, OR, or SR). Serine 127-133 acetylcholinesterase (Cartwright blood group) Homo sapiens 85-89 16341717-4 2006 The crystal structure of the AChE-Mf268 complex, however, proves that eseroline has escaped from the enzyme, despite the fact that the Ser-bound inhibitor fragment blocks the gorge entrance. Serine 135-138 acetylcholinesterase (Cartwright blood group) Homo sapiens 29-33 16769211-4 2006 The underlying mechanism is that paraoxon prevents acetylcholine chloride (ACh) reacting with AChE by destroying the OH bond of serine in AChE. Serine 128-134 acetylcholinesterase (Cartwright blood group) Homo sapiens 94-98 16769211-4 2006 The underlying mechanism is that paraoxon prevents acetylcholine chloride (ACh) reacting with AChE by destroying the OH bond of serine in AChE. Serine 128-134 acetylcholinesterase (Cartwright blood group) Homo sapiens 138-142 16403852-1 2006 For decades the interaction of the anticholinesterase organophosphorus compounds with acetylcholinesterase has been characterized as a straightforward phosphylation of the active site serine (Ser-203) which can be described kinetically by the inhibitory rate constant k(i). Serine 184-190 acetylcholinesterase (Cartwright blood group) Homo sapiens 86-106 16403852-1 2006 For decades the interaction of the anticholinesterase organophosphorus compounds with acetylcholinesterase has been characterized as a straightforward phosphylation of the active site serine (Ser-203) which can be described kinetically by the inhibitory rate constant k(i). Serine 192-195 acetylcholinesterase (Cartwright blood group) Homo sapiens 86-106 16515465-2 2006 These compounds inhibit enzyme acetylcholinesterase (AChE, EC 3.1.1.7) via its phosphorylation or phosphonylation at the serine hydroxy group in its active site. Serine 121-127 acetylcholinesterase (Cartwright blood group) Homo sapiens 31-51 16515465-2 2006 These compounds inhibit enzyme acetylcholinesterase (AChE, EC 3.1.1.7) via its phosphorylation or phosphonylation at the serine hydroxy group in its active site. Serine 121-127 acetylcholinesterase (Cartwright blood group) Homo sapiens 53-57 11275256-5 2000 The antibodies recognised AchE and were capable of hydrolysing acetylthiocholine and the larger butyrylthiocholine substrate, and were inactivated by phenylmethylsulphonyl fluoride (PMSF), indicating a serine residue in the active site. Serine 202-208 acetylcholinesterase (Cartwright blood group) Homo sapiens 26-30 12851386-2 2003 AChE is inactivated by organophosphates as they pass through the P-site and phosphorylate the catalytic serine in the A-site. Serine 104-110 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-4 11453739-7 2001 For methamidophos, we show that phosphylation of AChE involves elimination of the thiomethyl moiety and that the spontaneous reactivation of the resulting organophosphate adduct generates the phosphorus free AChE active site Ser-peptide. Serine 225-228 acetylcholinesterase (Cartwright blood group) Homo sapiens 208-212 1517212-2 1992 Evidence for the involvement of Ser-203, His-447, and Glu-334 in the catalytic triad of human acetylcholinesterase was provided by substitution of these amino acids by alanine residues. Serine 32-35 acetylcholinesterase (Cartwright blood group) Homo sapiens 94-114 10072953-5 1997 The synthesized 24-peptide containing the active serine residue of the AChE active center did not react with McAb 3F3. Serine 49-55 acetylcholinesterase (Cartwright blood group) Homo sapiens 71-75 8951236-0 1996 Synthesis and 31P chemical shift identification of tripeptide active site models that represent human serum acetylcholinesterase covalently modified at serine by certain organophosphates. Serine 152-158 acetylcholinesterase (Cartwright blood group) Homo sapiens 108-128 10801325-1 2000 Organophosphates inactivate acetylcholinesterase by reacting covalently with the active center serine. Serine 95-101 acetylcholinesterase (Cartwright blood group) Homo sapiens 28-48 7794533-1 1995 A large-scale preparation of a recombinant human acetylcholinesterase (rhAChE) mutant harbouring a CyS580-->Ser substitution, expressed in Escherichia coli, was refolded following solubilization of the inclusion bodies. Serine 111-114 acetylcholinesterase (Cartwright blood group) Homo sapiens 49-69 34820662-1 2021 Intoxication by organophosphorus (OP) poisons, like nerve agents and pesticides, is characterized by the life-threatening inhibition of acetylcholinesterase (AChE) caused by covalent reaction with the serine residue of the active site of the enzyme (phosphylation). Serine 201-207 acetylcholinesterase (Cartwright blood group) Homo sapiens 136-156 34353435-1 2021 The enzyme acetylcholinesterase (AChE) is a serine hydrolase whose primary function is to degrade acetylcholine (ACh) and terminate neurotransmission. Serine 44-50 acetylcholinesterase (Cartwright blood group) Homo sapiens 11-31 34353435-1 2021 The enzyme acetylcholinesterase (AChE) is a serine hydrolase whose primary function is to degrade acetylcholine (ACh) and terminate neurotransmission. Serine 44-50 acetylcholinesterase (Cartwright blood group) Homo sapiens 33-37 35489467-2 2022 Once inside the human body, those chemicals act similarly to the classic nerve agents, by binding to the catalytic residue Serine 203 (Ser203) of human acetylcholinesterase (HssAChE) and thus preventing the proper function of this enzyme. Serine 123-129 acetylcholinesterase (Cartwright blood group) Homo sapiens 152-172 35489467-2 2022 Once inside the human body, those chemicals act similarly to the classic nerve agents, by binding to the catalytic residue Serine 203 (Ser203) of human acetylcholinesterase (HssAChE) and thus preventing the proper function of this enzyme. Serine 123-129 acetylcholinesterase (Cartwright blood group) Homo sapiens 174-181 34820662-1 2021 Intoxication by organophosphorus (OP) poisons, like nerve agents and pesticides, is characterized by the life-threatening inhibition of acetylcholinesterase (AChE) caused by covalent reaction with the serine residue of the active site of the enzyme (phosphylation). Serine 201-207 acetylcholinesterase (Cartwright blood group) Homo sapiens 158-162 32305437-1 2020 Human Cathepsin A (CatA) is a lysosomal serine carboxypeptidase of the renin-angiotensin system (RAS) and is structurally similar to acetylcholinesterase (AChE). Serine 40-46 acetylcholinesterase (Cartwright blood group) Homo sapiens 133-153 2917984-8 1989 These studies indicate that the active center of AchE comprises at least two kinetically distinct environments separate from the esteratic region but located within 5 A of the nucleophilic serine and differing in dipolar characteristics that promote charge separation and general acid catalysis. Serine 189-195 acetylcholinesterase (Cartwright blood group) Homo sapiens 49-53 3755763-5 1986 However, a consensus organophosphate-binding hexapeptide sequence Phe-Gly-Glu-Ser-Ala-Gly was found both in "true" acetylcholinesterase from the electric organ of Torpedo [McPhee-Quigley et al: J Biol Chem 260:12185-12189, 1985] and in "pseudocholinesterase" (butyrylcholinesterase) from human serum [Lockridge: "Cholinesterases--Fundamental and Applied Aspects." Serine 78-81 acetylcholinesterase (Cartwright blood group) Homo sapiens 115-135 6530433-1 1984 A series of affinity chromatography packings for the purification of serine and sulfhydryl esterases (acetylcholinesterase, alkaline phosphatase, urokinase and papain) have been synthesized using commercially available agarose, glass and acrylate parent matrices. Serine 69-75 acetylcholinesterase (Cartwright blood group) Homo sapiens 102-122 32992925-1 2020 Organophosphates (OPs) are esters of substituted phosphates, phosphonates or phosphoramidates that react with acetylcholinesterase (AChE) by initially transferring the organophosphityl group to a serine residue in the enzyme active site, concomitant with loss of an alcohol or halide leaving group. Serine 196-202 acetylcholinesterase (Cartwright blood group) Homo sapiens 110-130 31175846-1 2019 Carbamates are esters of substituted carbamic acids that react with acetylcholinesterase (AChE) by initially transferring the carbamoyl group to a serine residue in the enzyme active site accompanied by loss of the carbamate leaving group followed by hydrolysis of the carbamoyl enzyme. Serine 147-153 acetylcholinesterase (Cartwright blood group) Homo sapiens 68-88 31675671-2 2019 Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are known to be serine hydrolase enzymes responsible for the hydrolysis of acetylcholine (ACh). Serine 77-83 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 31175846-1 2019 Carbamates are esters of substituted carbamic acids that react with acetylcholinesterase (AChE) by initially transferring the carbamoyl group to a serine residue in the enzyme active site accompanied by loss of the carbamate leaving group followed by hydrolysis of the carbamoyl enzyme. Serine 147-153 acetylcholinesterase (Cartwright blood group) Homo sapiens 90-94 29870665-1 2018 After the inhibition of acetylcholinesterase (AChE) by organophosphorus (OP) nerve agents, a dealkylation reaction of the phosphylated serine, referred to as aging, can occur. Serine 135-141 acetylcholinesterase (Cartwright blood group) Homo sapiens 24-44 31138650-2 2019 OPs inactivate acetylcholinesterase (AChE) by covalently modifying its catalytic serine. Serine 81-87 acetylcholinesterase (Cartwright blood group) Homo sapiens 15-35 31138650-2 2019 OPs inactivate acetylcholinesterase (AChE) by covalently modifying its catalytic serine. Serine 81-87 acetylcholinesterase (Cartwright blood group) Homo sapiens 37-41 30098983-1 2018 Carbamates are esters of substituted carbamic acids that react with acetylcholinesterase (AChE) by initially transferring the carbamoyl group to a serine residue in the enzyme active site accompanied by loss of the carbamate leaving group followed by hydrolysis of the carbamoyl enzyme. Serine 147-153 acetylcholinesterase (Cartwright blood group) Homo sapiens 68-88 30098983-1 2018 Carbamates are esters of substituted carbamic acids that react with acetylcholinesterase (AChE) by initially transferring the carbamoyl group to a serine residue in the enzyme active site accompanied by loss of the carbamate leaving group followed by hydrolysis of the carbamoyl enzyme. Serine 147-153 acetylcholinesterase (Cartwright blood group) Homo sapiens 90-94 30110162-1 2018 Organophosphorus agents such as sarin and soman that phosphylate the active site serine of the enzyme acetylcholinesterase are notorious and pernicious, not only because they have been used by tyrants to effect mass murder of their own populations but also because they are sought by terrorists to inflict mass casualties on civilian populations. Serine 81-87 acetylcholinesterase (Cartwright blood group) Homo sapiens 102-122 30096649-1 2018 Organophosphorous (OP) compounds (such as nerve agents) inhibit the enzyme acetylcholinesterase (AChE) by covalent phosphylation of a key serine residue in the active site of the enzyme resulting in severe symptoms and ultimately death. Serine 138-144 acetylcholinesterase (Cartwright blood group) Homo sapiens 75-95 30096649-1 2018 Organophosphorous (OP) compounds (such as nerve agents) inhibit the enzyme acetylcholinesterase (AChE) by covalent phosphylation of a key serine residue in the active site of the enzyme resulting in severe symptoms and ultimately death. Serine 138-144 acetylcholinesterase (Cartwright blood group) Homo sapiens 97-101 30096649-3 2018 The presently fielded oximes reactivate OP-inhibited AChE by liberating the phosphylated serine. Serine 89-95 acetylcholinesterase (Cartwright blood group) Homo sapiens 53-57 29870665-1 2018 After the inhibition of acetylcholinesterase (AChE) by organophosphorus (OP) nerve agents, a dealkylation reaction of the phosphylated serine, referred to as aging, can occur. Serine 135-141 acetylcholinesterase (Cartwright blood group) Homo sapiens 46-50 28892361-1 2017 Nerve agents and organophosphorus pesticides make a covalent bond with the active site serine of acetylcholinesterase (AChE), resulting in inhibition of AChE activity and toxic symptoms. Serine 87-93 acetylcholinesterase (Cartwright blood group) Homo sapiens 97-117 29137457-1 2017 Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are irreversibly inhibited by organophosphorus pesticides through formation of a covalent bond with the active site serine. Serine 177-183 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 29137457-1 2017 Acetylcholinesterase (AChE) and butyrylcholinesterase (BChE) are irreversibly inhibited by organophosphorus pesticides through formation of a covalent bond with the active site serine. Serine 177-183 acetylcholinesterase (Cartwright blood group) Homo sapiens 22-26 28892361-1 2017 Nerve agents and organophosphorus pesticides make a covalent bond with the active site serine of acetylcholinesterase (AChE), resulting in inhibition of AChE activity and toxic symptoms. Serine 87-93 acetylcholinesterase (Cartwright blood group) Homo sapiens 119-123 28892361-1 2017 Nerve agents and organophosphorus pesticides make a covalent bond with the active site serine of acetylcholinesterase (AChE), resulting in inhibition of AChE activity and toxic symptoms. Serine 87-93 acetylcholinesterase (Cartwright blood group) Homo sapiens 153-157 28892361-12 2017 It was concluded that all 6 monoclonal antibodies could be used to immunopurify RBC AChE and that exposure to nerve agents could be detected as adducts on the active site serine of RBC AChE. Serine 171-177 acetylcholinesterase (Cartwright blood group) Homo sapiens 185-189 27371941-2 2016 Catalytically inactive OP-AChE conjugates formed between the active-center serine and phosphorus of OPs can, in principle, be reactivated by nucleophilic oxime antidotes. Serine 75-81 acetylcholinesterase (Cartwright blood group) Homo sapiens 26-30 27109753-2 2016 Because of the central role of acetylcholinesterase cholinergic neurotransmission in humans, one of the main purposes for using OPs is inactivation of the enzyme by phosphorylation of the nucleophilic serine residue in the active center. Serine 201-207 acetylcholinesterase (Cartwright blood group) Homo sapiens 31-51 27311923-8 2017 Mass spectrometry for AChE, BChE and APH have characterized the active site serine adducts with OPs being useful to detect biomarkers of OPs exposure and inhibitory and postinhibitory reactions of esterases and OPs. Serine 76-82 acetylcholinesterase (Cartwright blood group) Homo sapiens 22-26 28061690-1 2017 Originally, organophosphorus (OP) toxicology consisted of acetylcholinesterase inhibition by insecticides and chemical threat agents acting as phosphorylating agents for serine in the catalytic triad, but this is no longer the case. Serine 170-176 acetylcholinesterase (Cartwright blood group) Homo sapiens 58-78 27371941-3 2016 Antidote efficacy is limited by the structural diversity of OP-AChE conjugates resulting from differences in the structure of the conjugated OP, the different active-center volumes they occupy when conjugated to the active-center serine of AChE, and the distinct chemical characteristics of both OPs and oximes documented in numerous X-ray structures of OP-conjugated AChEs. Serine 230-236 acetylcholinesterase (Cartwright blood group) Homo sapiens 63-67 27371941-3 2016 Antidote efficacy is limited by the structural diversity of OP-AChE conjugates resulting from differences in the structure of the conjugated OP, the different active-center volumes they occupy when conjugated to the active-center serine of AChE, and the distinct chemical characteristics of both OPs and oximes documented in numerous X-ray structures of OP-conjugated AChEs. Serine 230-236 acetylcholinesterase (Cartwright blood group) Homo sapiens 240-244 25743373-2 2016 Inhibited AChE can be reactivated by cleavage of the Ser-phosphorus bond either spontaneously or through a reaction with nucleophilic agents, such as oximes. Serine 53-56 acetylcholinesterase (Cartwright blood group) Homo sapiens 10-14 27055524-1 2016 Organophosphate (OP) and carbamate esters can inhibit acetylcholinesterase (AChE) by binding covalently to a serine residue in the enzyme active site, and their inhibitory potency depends largely on affinity for the enzyme and the reactivity of the ester. Serine 109-115 acetylcholinesterase (Cartwright blood group) Homo sapiens 54-74 27055524-1 2016 Organophosphate (OP) and carbamate esters can inhibit acetylcholinesterase (AChE) by binding covalently to a serine residue in the enzyme active site, and their inhibitory potency depends largely on affinity for the enzyme and the reactivity of the ester. Serine 109-115 acetylcholinesterase (Cartwright blood group) Homo sapiens 76-80 25743373-1 2016 The hydroxyl oxygen of the catalytic triad serine in the active center of serine hydrolase acetylcholinesterase (AChE) attacks organophosphorus compounds (OPs) at the phosphorus atom to displace the primary leaving group and to form a covalent bond. Serine 43-49 acetylcholinesterase (Cartwright blood group) Homo sapiens 91-111 25743373-1 2016 The hydroxyl oxygen of the catalytic triad serine in the active center of serine hydrolase acetylcholinesterase (AChE) attacks organophosphorus compounds (OPs) at the phosphorus atom to displace the primary leaving group and to form a covalent bond. Serine 43-49 acetylcholinesterase (Cartwright blood group) Homo sapiens 113-117 27101948-1 2016 Organophosphate (OP)-based pesticides and nerve agents are highly toxic compounds which interrupt the catalytic mechanism of acetylcholinesterase (AChE) by phosphorylating the hydroxyl moiety of serine residue. Serine 195-201 acetylcholinesterase (Cartwright blood group) Homo sapiens 125-145 27101948-1 2016 Organophosphate (OP)-based pesticides and nerve agents are highly toxic compounds which interrupt the catalytic mechanism of acetylcholinesterase (AChE) by phosphorylating the hydroxyl moiety of serine residue. Serine 195-201 acetylcholinesterase (Cartwright blood group) Homo sapiens 147-151 25743373-8 2016 A peptide fingerprinted mass spectrometry (MS) method, which clearly distinguished the peptide with the active serine (active center peptide, ACP) of the human AChE adducted with OPs, was developed by MALDI-TOF and MALDI-TOF/TOF. Serine 111-117 acetylcholinesterase (Cartwright blood group) Homo sapiens 160-164 25407587-2 2015 The inhibition of AChE by an organophosphate can be reversed by a nucleophilic agent able to dephosphorylate a serine residue in the active site of AChE. Serine 111-117 acetylcholinesterase (Cartwright blood group) Homo sapiens 18-22 27040140-1 2016 The serine hydrolase butyrylcholinesterase (BChE), like the related enzyme acetylcholinesterase (AChE), co-regulates metabolism of the neurotransmitter acetylcholine. Serine 4-10 acetylcholinesterase (Cartwright blood group) Homo sapiens 75-95 27040140-1 2016 The serine hydrolase butyrylcholinesterase (BChE), like the related enzyme acetylcholinesterase (AChE), co-regulates metabolism of the neurotransmitter acetylcholine. Serine 4-10 acetylcholinesterase (Cartwright blood group) Homo sapiens 97-101 26520174-3 2015 The non-target toxicity and resistance problem of organophosphate and carbamate have become of growing concern, which may be due to the fact that they target the ubiquitous catalytic serine residue of acetylcholinesterase (AChE) in mammals, birds, and beneficial insects. Serine 183-189 acetylcholinesterase (Cartwright blood group) Homo sapiens 223-227 25407587-2 2015 The inhibition of AChE by an organophosphate can be reversed by a nucleophilic agent able to dephosphorylate a serine residue in the active site of AChE. Serine 111-117 acetylcholinesterase (Cartwright blood group) Homo sapiens 148-152 24805972-0 2015 Oxime-dipeptides as anticholinesterase, reactivator of phosphonylated-serine of AChE catalytic triad: probing the mechanistic insight by MM-GBSA, dynamics simulations and DFT analysis. Serine 70-76 acetylcholinesterase (Cartwright blood group) Homo sapiens 80-84 26563788-3 2015 With OP insecticides (but not carbamates), "aging" may also occur by partial dealkylation of the serine group at the active site of AChE; recovery of AChE activity requires synthesis of new enzyme in the liver. Serine 97-103 acetylcholinesterase (Cartwright blood group) Homo sapiens 132-136 25874456-2 2015 We present data from quantum mechanics/molecular mechanics (QM/MM) and 80 classical molecular dynamics (MD) simulations of the apo and soman-adducted forms of hAChE to investigate the effects on the dynamics and protein structure when the catalytic Serine 203 is phosphonylated. Serine 249-255 acetylcholinesterase (Cartwright blood group) Homo sapiens 159-164 25441834-2 2015 The acute toxicity of nerve agents leads to progressive inhibition of the enzyme acetylcholinesterase (AChE) by phosphylation of serine residue at the active site of gorge. Serine 129-135 acetylcholinesterase (Cartwright blood group) Homo sapiens 103-107 24652148-2 2014 Most often binding to serine, tyrosine, or threonine residues is described as being of relevance for toxicological effects (e.g., acetylcholinesterase and neuropathy target esterase) or as biomarkers for post-exposure analysis (verification, e.g., albumin and butyrylcholinesterase). Serine 22-28 acetylcholinesterase (Cartwright blood group) Homo sapiens 130-150 25441834-2 2015 The acute toxicity of nerve agents leads to progressive inhibition of the enzyme acetylcholinesterase (AChE) by phosphylation of serine residue at the active site of gorge. Serine 129-135 acetylcholinesterase (Cartwright blood group) Homo sapiens 81-101 24040835-4 2013 A potential long-term strategy for preventing AChE inactivation by OPs is based on evidence that OPs must pass through a peripheral site or P-site near the mouth of the AChE active site gorge before reacting with a catalytic serine in an acylation site or A-site at the base of the gorge. Serine 225-231 acetylcholinesterase (Cartwright blood group) Homo sapiens 46-50 23747845-2 2013 The catalytic serine of AChE can be phosphonylated by the nerve agent soman, and subsequently can undergo an aging process. Serine 14-20 acetylcholinesterase (Cartwright blood group) Homo sapiens 24-28 23111374-2 2013 They cause an irreversible inhibition of acetylcholinesterase (AChE), by the formation of a covalent P-O bond with the catalytic serine. Serine 129-135 acetylcholinesterase (Cartwright blood group) Homo sapiens 41-61 23631528-1 2013 Amphiphilic peptides were designed to fold into a beta-sheet monolayer structure while presenting the catalytic triad residues of the enzyme, acetylcholinesterase (Glu, His, and Ser), to a solution containing the organophosphate, paraoxon. Serine 178-181 acetylcholinesterase (Cartwright blood group) Homo sapiens 142-162 23631528-6 2013 Circular dichroism revealed that the peptide most sensitive to interactions with paraoxon was that with the triad residues in the order Glu, Ser, and His, which appears to be appropriate for supporting a catalytic mechanism similar to that in the acetylcholinesterase enzyme. Serine 141-144 acetylcholinesterase (Cartwright blood group) Homo sapiens 247-267 23679855-5 2013 Huprine W forms additional interactions with hAChE, which explains its superior affinity: the isoquinoline moiety is associated with a group of aromatic residues (Tyr337, Phe338 and Phe295 not present in hBChE) in addition to Trp86; the hydroxyl group is hydrogen bonded to both the catalytic serine residue and residues in the oxyanion hole; and the chlorine substituent is nested in a hydrophobic pocket interacting strongly with Trp439. Serine 293-299 acetylcholinesterase (Cartwright blood group) Homo sapiens 45-50 23376121-1 2013 Nerve agents such as tabun, cyclosarin and Russian VX inhibit the essential enzyme acetylcholinesterase (AChE) by organophosphorylating the catalytic serine residue. Serine 150-156 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. Serine 150-156 acetylcholinesterase (Cartwright blood group) Homo sapiens 105-109 23111374-2 2013 They cause an irreversible inhibition of acetylcholinesterase (AChE), by the formation of a covalent P-O bond with the catalytic serine. Serine 129-135 acetylcholinesterase (Cartwright blood group) Homo sapiens 63-67 20882513-1 2010 Poisoning with organophosphorus compounds (OP), e.g. pesticides and nerve agents, causes inhibition of acetylcholinesterase (AChE) by phosphylation of the active site serine residue. Serine 167-173 acetylcholinesterase (Cartwright blood group) Homo sapiens 103-123 22703537-2 2012 It acts via phosphorylation of a serine residue in the active site of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), leading to enzyme inactivation. Serine 33-39 acetylcholinesterase (Cartwright blood group) Homo sapiens 70-90 22703537-2 2012 It acts via phosphorylation of a serine residue in the active site of acetylcholinesterase (AChE) and butyrylcholinesterase (BChE), leading to enzyme inactivation. Serine 33-39 acetylcholinesterase (Cartwright blood group) Homo sapiens 92-96 22280344-6 2012 These data are used to discuss the differences between targeting the insect-specific cysteine residue and targeting the ubiquitous catalytic serine residue of acetylcholinesterase from the perspective of reducing off-target toxicity and insect resistance. Serine 141-147 acetylcholinesterase (Cartwright blood group) Homo sapiens 159-179 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. Serine 89-95 acetylcholinesterase (Cartwright blood group) Homo sapiens 73-77 22984913-2 2012 The catalytic serine of AChE can be phosphonylated by soman, one of the most potent nerve agents, and subsequently undergo an aging reaction. Serine 14-20 acetylcholinesterase (Cartwright blood group) Homo sapiens 24-28 20882513-1 2010 Poisoning with organophosphorus compounds (OP), e.g. pesticides and nerve agents, causes inhibition of acetylcholinesterase (AChE) by phosphylation of the active site serine residue. Serine 167-173 acetylcholinesterase (Cartwright blood group) Homo sapiens 125-129 20408548-1 2010 Tabun is a warfare agent that inhibits human acetylcholinesterase (hAChE) by rapid phosphylation of the catalytic serine. Serine 114-120 acetylcholinesterase (Cartwright blood group) Homo sapiens 67-72