PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 28446076-7 2018 In contrast, HI 6 and 2-PAM showed high binding energy values with great contribution of the amino acid Asp74, demonstrating the importance of the quaternary nitrogen to the affinity and interaction of the oximes/AChE tabun-inhibited complexes. Nitrogen 158-166 acetylcholinesterase (Cartwright blood group) Homo sapiens 213-217 26159481-1 2015 A computational docking study of a series of de novo structural analogs of the highly potent, non-nitrogen containing, acetylcholinesterase inhibitor (+)-arisugacin A is presented. Nitrogen 98-106 acetylcholinesterase (Cartwright blood group) Homo sapiens 119-139 26186269-0 2016 Design, synthesis and preliminary structure-activity relationship investigation of nitrogen-containing chalcone derivatives as acetylcholinesterase and butyrylcholinesterase inhibitors: a further study based on Flavokawain B Mannich base derivatives. Nitrogen 83-91 acetylcholinesterase (Cartwright blood group) Homo sapiens 127-147 27055393-1 2016 This work presents a novel fluorescent sensor for the determination of tacrine by combining the magnificent fluorescence properties of nitrogen-doped graphene quantum dots (N-GQDs) with the high potential of acetylcholinesterase (AChE) enzyme for screening its inhibitors. Nitrogen 135-143 acetylcholinesterase (Cartwright blood group) Homo sapiens 230-234 26231935-0 2015 Three N-Glycosylation Sites of Human Acetylcholinesterase Shares Similar Glycan Composition. Nitrogen 6-7 acetylcholinesterase (Cartwright blood group) Homo sapiens 37-57 26231935-1 2015 Acetylcholinesterase (AChE; EC 3.1.1.7) is a glycoprotein possessing three conserved N-linked glycosylation sites in mammalian species, locating at 296, 381, and 495 residues of the human sequence. Nitrogen 85-86 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 26231935-1 2015 Acetylcholinesterase (AChE; EC 3.1.1.7) is a glycoprotein possessing three conserved N-linked glycosylation sites in mammalian species, locating at 296, 381, and 495 residues of the human sequence. Nitrogen 85-86 acetylcholinesterase (Cartwright blood group) Homo sapiens 22-26 26231935-2 2015 Several lines of evidence demonstrated that N-glycosylation of AChE affected the enzymatic activity, as well as its biosynthesis. Nitrogen 44-45 acetylcholinesterase (Cartwright blood group) Homo sapiens 63-67 29534488-4 2018 Both quaternization upon methylation of the quinoline nitrogen atom, and tethering of a triazole ring, with, in some cases, the additional incorporation of a polyphenol-like moiety, result in more polar compounds with higher inhibitory activity against human AChE (up to 190-fold) and butyrylcholinesterase (up to 40-fold) than pyridostigmine, the standard drug for symptomatic treatment of myasthenia gravis. Nitrogen 54-62 acetylcholinesterase (Cartwright blood group) Homo sapiens 259-263 27506355-12 2016 In addition, we further applied our method to reveal, for the first time, the site-specific N-glycosylation profile of recombinant human acetylcholinesterase expressed in HEK293 cells. Nitrogen 92-93 acetylcholinesterase (Cartwright blood group) Homo sapiens 137-157 27252617-3 2016 MTDL-2 showed more high affinity toward the four enzymes than MTDL-1.MTDL-3 and MTDL-4, were designed containing the N-benzylpiperidinium moiety from Donepezil, a metal- chelating 8-hydroxyquinoline group and linked to a N-propargyl core and they were pharmacologically evaluated.The presence of the cyano group in MTDL-3, enhanced binding to AChE, BuChE and MAO A. Nitrogen 117-118 acetylcholinesterase (Cartwright blood group) Homo sapiens 343-347 12049482-10 2001 Overall, our experiments reveal that nitrogenous substitutions at the permissive C-10 of the camptothecin backbone may lead to AchE inhibition, particularly if they involve a quaternary nitrogen. Nitrogen 37-45 acetylcholinesterase (Cartwright blood group) Homo sapiens 127-131 24422467-3 2014 In this work, we designed and synthesized two novel classes of tri- and tetracyclic nitrogen-bridgehead compounds acting as dual AChE inhibitors and histamine H3 antagonists by combining the nitrogen-bridgehead moiety of novel AChE inhibitors with a second N-basic fragment based on the piperidinylpropoxy pharmacophore with different spacer lengths. Nitrogen 191-199 acetylcholinesterase (Cartwright blood group) Homo sapiens 129-133 24422467-3 2014 In this work, we designed and synthesized two novel classes of tri- and tetracyclic nitrogen-bridgehead compounds acting as dual AChE inhibitors and histamine H3 antagonists by combining the nitrogen-bridgehead moiety of novel AChE inhibitors with a second N-basic fragment based on the piperidinylpropoxy pharmacophore with different spacer lengths. Nitrogen 191-199 acetylcholinesterase (Cartwright blood group) Homo sapiens 227-231 22343626-1 2012 We present a systematic structural optimization of uncharged but ionizable N-substituted 2-hydroxyiminoacetamido alkylamine reactivators of phosphylated human acetylcholinesterase (hAChE) intended to catalyze the hydrolysis of organophosphate (OP)-inhibited hAChE in the CNS. Nitrogen 75-76 acetylcholinesterase (Cartwright blood group) Homo sapiens 181-186 22343626-1 2012 We present a systematic structural optimization of uncharged but ionizable N-substituted 2-hydroxyiminoacetamido alkylamine reactivators of phosphylated human acetylcholinesterase (hAChE) intended to catalyze the hydrolysis of organophosphate (OP)-inhibited hAChE in the CNS. Nitrogen 75-76 acetylcholinesterase (Cartwright blood group) Homo sapiens 258-263 21795704-4 2011 Here, several lines of evidence indicate that the N-linked glycosylation of AChE(T) plays a major role for acquisition of AChE full enzymatic activity but does not affect its oligomerization. Nitrogen 50-51 acetylcholinesterase (Cartwright blood group) Homo sapiens 76-80 21795704-4 2011 Here, several lines of evidence indicate that the N-linked glycosylation of AChE(T) plays a major role for acquisition of AChE full enzymatic activity but does not affect its oligomerization. Nitrogen 50-51 acetylcholinesterase (Cartwright blood group) Homo sapiens 122-126 21795704-5 2011 The expression of the AChE(T) mutant, in which all N-glycosylation sites were deleted, together with PRiMA in HEK293T cells produced a glycan-depleted PRiMA-linked AChE tetramer but with a much higher K(m) value as compared with the wild type. Nitrogen 51-52 acetylcholinesterase (Cartwright blood group) Homo sapiens 22-26 21795704-5 2011 The expression of the AChE(T) mutant, in which all N-glycosylation sites were deleted, together with PRiMA in HEK293T cells produced a glycan-depleted PRiMA-linked AChE tetramer but with a much higher K(m) value as compared with the wild type. Nitrogen 51-52 acetylcholinesterase (Cartwright blood group) Homo sapiens 164-168 19240946-1 2009 Alkaloids from the plants of Amaryllidaceae family consists of an unique class of nitrogen-containing compounds showing diverse and significant biological activities, including anticancer and acetylcholinesterase (AChE) inhibitory activities. Nitrogen 82-90 acetylcholinesterase (Cartwright blood group) Homo sapiens 192-212 19240946-1 2009 Alkaloids from the plants of Amaryllidaceae family consists of an unique class of nitrogen-containing compounds showing diverse and significant biological activities, including anticancer and acetylcholinesterase (AChE) inhibitory activities. Nitrogen 82-90 acetylcholinesterase (Cartwright blood group) Homo sapiens 214-218 18769671-8 2008 CONCLUSIONS: Together, these findings attribute an apoptogenic role to N-AChE-S and outline a potential value to AChE inhibitor therapeutics in early AD. Nitrogen 2-3 acetylcholinesterase (Cartwright blood group) Homo sapiens 73-77 18769671-8 2008 CONCLUSIONS: Together, these findings attribute an apoptogenic role to N-AChE-S and outline a potential value to AChE inhibitor therapeutics in early AD. Nitrogen 2-3 acetylcholinesterase (Cartwright blood group) Homo sapiens 113-117 16289855-1 2006 Tetracyclic nitrogen bridgehead compounds, dibenzodiazecines and tricyclic quinazolinimines, in which the size of the alicyclic ring system and the length of the alkyl chain between the quinazolinimine moiety and a phenyl ring connected to the imine nitrogen atom were changed systematically, were synthesized and their ability to inhibit acetyl- and butyrylcholinesterase (AChE/BChE), respectively, was evaluated. Nitrogen 12-20 acetylcholinesterase (Cartwright blood group) Homo sapiens 374-378 16366609-6 2005 The introduction of a tetrahydropyrido ring with bulky hydrophobic substituents at the basic nitrogen provided inhibitors of AChE which were completely inactive toward CEase. Nitrogen 93-101 acetylcholinesterase (Cartwright blood group) Homo sapiens 125-129 11964163-0 2002 Overloading and removal of N-glycosylation targets on human acetylcholinesterase: effects on glycan composition and circulatory residence time. Nitrogen 27-28 acetylcholinesterase (Cartwright blood group) Homo sapiens 60-80 24422467-0 2014 Synthesis, biological evaluation, and computational studies of Tri- and tetracyclic nitrogen-bridgehead compounds as potent dual-acting AChE inhibitors and hH3 receptor antagonists. Nitrogen 84-92 acetylcholinesterase (Cartwright blood group) Homo sapiens 136-140 24422467-3 2014 In this work, we designed and synthesized two novel classes of tri- and tetracyclic nitrogen-bridgehead compounds acting as dual AChE inhibitors and histamine H3 antagonists by combining the nitrogen-bridgehead moiety of novel AChE inhibitors with a second N-basic fragment based on the piperidinylpropoxy pharmacophore with different spacer lengths. Nitrogen 84-92 acetylcholinesterase (Cartwright blood group) Homo sapiens 129-133 24422467-3 2014 In this work, we designed and synthesized two novel classes of tri- and tetracyclic nitrogen-bridgehead compounds acting as dual AChE inhibitors and histamine H3 antagonists by combining the nitrogen-bridgehead moiety of novel AChE inhibitors with a second N-basic fragment based on the piperidinylpropoxy pharmacophore with different spacer lengths. Nitrogen 84-92 acetylcholinesterase (Cartwright blood group) Homo sapiens 227-231 24594013-5 2014 Moreover, when expressed in human embryonic kidney 293 cells, N-glycosylated AChE co-immunoprecipitated with non-O-glycosylated neurexin-1beta, with N-glycosylation of the AChE being required for this co-precipitation to occur. Nitrogen 62-63 acetylcholinesterase (Cartwright blood group) Homo sapiens 77-81 24594013-5 2014 Moreover, when expressed in human embryonic kidney 293 cells, N-glycosylated AChE co-immunoprecipitated with non-O-glycosylated neurexin-1beta, with N-glycosylation of the AChE being required for this co-precipitation to occur. Nitrogen 62-63 acetylcholinesterase (Cartwright blood group) Homo sapiens 172-176 24594013-5 2014 Moreover, when expressed in human embryonic kidney 293 cells, N-glycosylated AChE co-immunoprecipitated with non-O-glycosylated neurexin-1beta, with N-glycosylation of the AChE being required for this co-precipitation to occur. Nitrogen 149-150 acetylcholinesterase (Cartwright blood group) Homo sapiens 77-81 23073222-7 2012 MIFs calculated with the N1 (pyridinium nitrogen) and the DRY GRID probes in the AChE active site enabled us to establish the relationship between amino acid residues within AChE active site and the variables having high impact on models. Nitrogen 40-48 acetylcholinesterase (Cartwright blood group) Homo sapiens 81-85 23073222-7 2012 MIFs calculated with the N1 (pyridinium nitrogen) and the DRY GRID probes in the AChE active site enabled us to establish the relationship between amino acid residues within AChE active site and the variables having high impact on models. Nitrogen 40-48 acetylcholinesterase (Cartwright blood group) Homo sapiens 174-178 21999734-1 2011 This study describes the interaction between human acetylcholinesterase (AChE), a key regulator of central and peripheral cholinergic function, and the widely used nitrogen mustard alkylating agent, cyclophosphamide (CP). Nitrogen 164-172 acetylcholinesterase (Cartwright blood group) Homo sapiens 51-71 21999734-1 2011 This study describes the interaction between human acetylcholinesterase (AChE), a key regulator of central and peripheral cholinergic function, and the widely used nitrogen mustard alkylating agent, cyclophosphamide (CP). Nitrogen 164-172 acetylcholinesterase (Cartwright blood group) Homo sapiens 73-77 18550228-2 2009 All of the new compounds prepared showed high AChE inhibitory activities, with compound 3e that has an N-hexyl-benzyl piperidine substituent on the nitrogen atom reaching the best inhibitory activity for AChE (IC(50)=5.62 nM). Nitrogen 148-156 acetylcholinesterase (Cartwright blood group) Homo sapiens 204-208 12502352-4 2003 The nitrogen-containing homobivalent ligands 3e,g and the sulfur-containing 3h validated the hypothesis of extra sites of interaction in the AChE and BuChE active site gorges. Nitrogen 4-12 acetylcholinesterase (Cartwright blood group) Homo sapiens 141-145 34783117-3 2022 The synthesized nitrogen-based novel heterocyclic compounds were evaluated against the human carbonic anhydrase isoenzymes I and II (hCA I and hCA II), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) enzymes. Nitrogen 16-24 acetylcholinesterase (Cartwright blood group) Homo sapiens 152-172 2003276-4 1991 A structural feature common to these compounds is the N-methyl determinant of the pyrrolidine ring which may be important in binding to the AChE. Nitrogen 54-55 acetylcholinesterase (Cartwright blood group) Homo sapiens 140-144 33243025-1 2021 A series of C4-substituted tertiary nitrogen-bearing 2"-hydroxychalcones were designed and synthesised based on a previous mixed type acetylcholinesterase inhibitor. Nitrogen 36-44 acetylcholinesterase (Cartwright blood group) Homo sapiens 134-154 10637365-4 2000 It is concluded that hydrophobicity and the presence of an ionizable nitrogen are the pre-requisites for the inhibitors to interact with AChE. Nitrogen 69-77 acetylcholinesterase (Cartwright blood group) Homo sapiens 137-141 34666020-0 2022 Cytotoxic activity and influence on acetylcholinesterase of series dinuclear platinum(II) complexes with aromatic nitrogen-containing heterocyclic bridging ligands: Insights in the mechanisms of action. Nitrogen 114-122 acetylcholinesterase (Cartwright blood group) Homo sapiens 36-56 34783117-3 2022 The synthesized nitrogen-based novel heterocyclic compounds were evaluated against the human carbonic anhydrase isoenzymes I and II (hCA I and hCA II), acetylcholinesterase (AChE), and butyrylcholinesterase (BChE) enzymes. Nitrogen 16-24 acetylcholinesterase (Cartwright blood group) Homo sapiens 174-178 34783117-4 2022 The synthesized nitrogen-based novel heterocyclic compounds showed IC50 values in the range of 2.69-7.01 against hCA I, 2.40-4.59 against hCA II, 0.81-1.32 microM against AChE, and 20.83-1.70 microM against BChE enzymes. Nitrogen 16-24 acetylcholinesterase (Cartwright blood group) Homo sapiens 171-175 34783117-5 2022 On the contrary, nitrogen-based novel heterocyclic compounds demonstrated Ki values between 2.93 +- 0.59-8.61 +- 1.39 against hCA I, 2.05 +- 0.62-4.97 +- 0.95 against hCA II, 0.34 +- 0.02-0.92 +- 0.17 nM against AChE, and 0.50 +- 0.04-1.20 +- 0.16 microM against BChE enzymes. Nitrogen 17-25 acetylcholinesterase (Cartwright blood group) Homo sapiens 212-216 34203347-0 2021 1,3,5-Triazine Nitrogen Mustards with Different Peptide Group as Innovative Candidates for AChE and BACE1 Inhibitors. Nitrogen 15-23 acetylcholinesterase (Cartwright blood group) Homo sapiens 91-95 34203347-1 2021 A series of new analogs of nitrogen mustards (4a-4h) containing the 1,3,5-triazine ring substituted with dipeptide residue were synthesized and evaluated for the inhibition of both acetylcholinesterase (AChE) and beta-secretase (BACE1) enzymes. Nitrogen 27-35 acetylcholinesterase (Cartwright blood group) Homo sapiens 181-201 34203347-1 2021 A series of new analogs of nitrogen mustards (4a-4h) containing the 1,3,5-triazine ring substituted with dipeptide residue were synthesized and evaluated for the inhibition of both acetylcholinesterase (AChE) and beta-secretase (BACE1) enzymes. Nitrogen 27-35 acetylcholinesterase (Cartwright blood group) Homo sapiens 203-207 592327-8 1977 A bis-quaternary ammonium compound with a flexible bridge that links the two nitrogen atoms was found to be more potent in inhibiting AcChE and less potent in inhibiting BuChE than a bis-quaternary ammonium compound with a rigid bridge. Nitrogen 77-85 acetylcholinesterase (Cartwright blood group) Homo sapiens 134-139 2605196-3 1989 The compound (5,5,5-trifluoro-4-oxopentyl)trimethylammonium bicarbonate (1) inhibits acetylcholinesterase with Ki = 0.06 X 10(-9)M and pseudocholinesterase with Ki = 70 X 10(-9)M. Replacement of the nitrogen of 1 by carbon (compound 2) increases Ki for 1 200-fold for acetylcholinesterase but does not significantly alter Ki for pseudocholinesterase. Nitrogen 199-207 acetylcholinesterase (Cartwright blood group) Homo sapiens 85-105 2917018-5 1989 HLo-7 is also much more active than HI-6 when used as a reactivator for electric eel AChE inhibited by some N-unsubstituted derivatives of tabun. Nitrogen 108-109 acetylcholinesterase (Cartwright blood group) Homo sapiens 85-89 19873643-4 1969 Two classes of sites on AChE molecule account for the binding of these quaternary nitrogen containing compounds: (1) the anionic site of the active center and (2) noncatalytic "peripheral anionic centers" located outside the active center. Nitrogen 82-90 acetylcholinesterase (Cartwright blood group) Homo sapiens 24-28 32175496-9 2020 In contrast, HI-6 and 2-PAM showed higher affinities with more negative binding energy values and larger contribution of the amino acid Asp74, demonstrating the importance of the quaternary nitrogen to the affinity and interaction of oximes with AChE-GB and AChE-VX conjugates. Nitrogen 190-198 acetylcholinesterase (Cartwright blood group) Homo sapiens 246-250 14098449-0 1963 EFFECT OF NITROGEN MUSTARD ON ERYTHROCYTE ACETYLCHOLINESTERASE. Nitrogen 10-18 acetylcholinesterase (Cartwright blood group) Homo sapiens 42-62 32891857-0 2020 Synthesis of nitrogen, phosphorus, selenium and sulfur-containing heterocyclic compounds - Determination of their carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase and alpha-glycosidase inhibition properties. Nitrogen 13-21 acetylcholinesterase (Cartwright blood group) Homo sapiens 134-154 32754990-0 2020 Nitrogen-containing flavonoid and their analogs with diverse B-ring in acetylcholinesterase and butyrylcholinesterase inhibition. Nitrogen 0-8 acetylcholinesterase (Cartwright blood group) Homo sapiens 71-91 31532667-0 2019 One-Step Facile Synthesis of Nitrogen-Doped Carbon Dots: A Ratiometric Fluorescent Probe for Evaluation of Acetylcholinesterase Activity and Detection of Organophosphorus Pesticides in Tap Water and Food. Nitrogen 29-37 acetylcholinesterase (Cartwright blood group) Homo sapiens 107-127 31532667-2 2019 In this study, a highly selective and sensitive ratiometric fluorescent probe was innovatively fabricated for the evaluation of AChE activity and the determination of OPs in tap water and food on the basis of the inner filter effect (IFE) between nitrogen-doped carbon dots (N-CDs) and 2,3-diaminophenazine (DAP). Nitrogen 247-255 acetylcholinesterase (Cartwright blood group) Homo sapiens 128-132 31175846-5 2019 We also review data showing that solvent deuterium oxide isotope effects for decarbamoylation decreased from 2.8 for N-monomethylcarbamoyl AChE to 1.1 for N,N-diethylcarbamoyl AChE, indicating a shift in the rate-limiting step from general acid-base catalysis to a likely conformational change in the distorted active site in N,N-diethylcarbamoyl AChE. Nitrogen 117-118 acetylcholinesterase (Cartwright blood group) Homo sapiens 139-143 31175846-5 2019 We also review data showing that solvent deuterium oxide isotope effects for decarbamoylation decreased from 2.8 for N-monomethylcarbamoyl AChE to 1.1 for N,N-diethylcarbamoyl AChE, indicating a shift in the rate-limiting step from general acid-base catalysis to a likely conformational change in the distorted active site in N,N-diethylcarbamoyl AChE. Nitrogen 117-118 acetylcholinesterase (Cartwright blood group) Homo sapiens 176-180 31175846-5 2019 We also review data showing that solvent deuterium oxide isotope effects for decarbamoylation decreased from 2.8 for N-monomethylcarbamoyl AChE to 1.1 for N,N-diethylcarbamoyl AChE, indicating a shift in the rate-limiting step from general acid-base catalysis to a likely conformational change in the distorted active site in N,N-diethylcarbamoyl AChE. Nitrogen 117-118 acetylcholinesterase (Cartwright blood group) Homo sapiens 176-180 31363918-0 2019 Carbon dots co-doped with nitrogen and chlorine for "off-on" fluorometric determination of the activity of acetylcholinesterase and for quantification of organophosphate pesticides. Nitrogen 26-34 acetylcholinesterase (Cartwright blood group) Homo sapiens 107-127