PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 24059299-3 2014 Hydrophobic interactions and hydrogen bonds both play an equally important role in the correct positioning of Huperzine-B within the "catalytic site" of AChE to permit docking. Hydrogen 29-37 acetylcholinesterase (Cartwright blood group) Homo sapiens 153-157 24059300-3 2014 It was found that hydrophobic interactions play an important role in the correct positioning of BNC within the "catalytic site" of AChE, BuChE and 5-LPO to permit docking while hydrogen bonds are significant in case of cymserine for the same. Hydrogen 177-185 acetylcholinesterase (Cartwright blood group) Homo sapiens 131-135 23348103-4 2013 Contour map of variable coefficients showed that hydrogen bonding between the O atom in PO and the NH groups in acetylcholinesterase (AChE) played an important role in the interaction between OP and AChE. Hydrogen 49-57 acetylcholinesterase (Cartwright blood group) Homo sapiens 134-138 24059317-5 2014 Hydrophobic interactions and hydrogen bonds both play an equally important role in the correct positioning of Cisplatin within the "acyl pocket" as well as "catalytic site" of AChE to permit docking. Hydrogen 29-37 acetylcholinesterase (Cartwright blood group) Homo sapiens 176-180 24059317-7 2014 During "Cisplatin-CAS site of AChE enzyme" interaction, it was found that out of the three amino acids constituting the catalytic triad (S203, H447 and E334), two amino acid residues namely S203 and H447 interact with Cisplatin by hydrogen bonding and hydrophobic interaction, respectively. Hydrogen 231-239 acetylcholinesterase (Cartwright blood group) Homo sapiens 30-34 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. Hydrogen 255-263 acetylcholinesterase (Cartwright blood group) Homo sapiens 45-50 23796225-3 2013 Docking analysis showed that hydrophobic interaction and hydrogen bonding were created between the functional groups of Ace derivatives and the receptor sites of acetylcholinesterase. Hydrogen 57-65 acetylcholinesterase (Cartwright blood group) Homo sapiens 162-182 23348103-4 2013 Contour map of variable coefficients showed that hydrogen bonding between the O atom in PO and the NH groups in acetylcholinesterase (AChE) played an important role in the interaction between OP and AChE. Hydrogen 49-57 acetylcholinesterase (Cartwright blood group) Homo sapiens 199-203 21570330-6 2011 The key hydrogen bonding residues between hAChE and hCyt c proteins were found in Apo and Holo systems, as well as each Tyr341 and Trp286 residue of hAChE was participated in cation-pi (pi) interactions with Lys79 of hCyt c in Apo and Holo systems, respectively. Hydrogen 8-16 acetylcholinesterase (Cartwright blood group) Homo sapiens 42-47 23227542-7 2012 Icariin binds selectively to the AChE peripheral anionic site via hydrogen bonds and Van der Waals forces. Hydrogen 66-74 acetylcholinesterase (Cartwright blood group) Homo sapiens 33-37 21570330-6 2011 The key hydrogen bonding residues between hAChE and hCyt c proteins were found in Apo and Holo systems, as well as each Tyr341 and Trp286 residue of hAChE was participated in cation-pi (pi) interactions with Lys79 of hCyt c in Apo and Holo systems, respectively. Hydrogen 8-16 acetylcholinesterase (Cartwright blood group) Homo sapiens 149-154 20156428-6 2010 Hydrogen-bonding interactions between the fluoride leaving group of GB with Y124 in AChE are observed throughout the reaction profile. Hydrogen 0-8 acetylcholinesterase (Cartwright blood group) Homo sapiens 84-88 20839017-2 2011 The energies of the frontier orbitals and the distances between the more acidic hydrogen species were investigated to determine their contributions to the activity of a group of acetylcholinesterase inhibitors. Hydrogen 80-88 acetylcholinesterase (Cartwright blood group) Homo sapiens 178-198 20839017-7 2011 Desirable features for acetylcholinesterase inhibitor molecules include aromatic systems or groups that simulate the surface electrostatic potential of aromatic systems and the presence of a sufficient number of hydrogen acceptors and few hydrogen donors. Hydrogen 212-220 acetylcholinesterase (Cartwright blood group) Homo sapiens 23-43 20839017-7 2011 Desirable features for acetylcholinesterase inhibitor molecules include aromatic systems or groups that simulate the surface electrostatic potential of aromatic systems and the presence of a sufficient number of hydrogen acceptors and few hydrogen donors. Hydrogen 239-247 acetylcholinesterase (Cartwright blood group) Homo sapiens 23-43 21215642-8 2011 The docking results confirmed the apparent influence of pi-pi or cation-pi interactions and hydrogen bonding for reactivator binding within the hAChE active site cleft. Hydrogen 92-100 acetylcholinesterase (Cartwright blood group) Homo sapiens 144-149 20028185-10 2010 The in silico pharmacophore model of oxime affinity for binding to GA-inhibited AChE was found to require a hydrogen bond acceptor, a hydrogen bond donor at the two terminal regions, and an aromatic ring in the central region of the oximes. Hydrogen 108-116 acetylcholinesterase (Cartwright blood group) Homo sapiens 80-84 20028185-10 2010 The in silico pharmacophore model of oxime affinity for binding to GA-inhibited AChE was found to require a hydrogen bond acceptor, a hydrogen bond donor at the two terminal regions, and an aromatic ring in the central region of the oximes. Hydrogen 134-142 acetylcholinesterase (Cartwright blood group) Homo sapiens 80-84 16854005-1 2005 Molecular dynamics (MD) simulations and hydrogen bonding energy (HBE) calculations have been performed on the prereactive enzyme-substrate complexes (ES), transition states (TS1), and intermediates (INT1) for acetylcholinesterase (AChE)-catalyzed hydrolysis of acetylcholine (ACh), butyrylcholinesterase (BChE)-catalyzed hydrolysis of ACh, and BChE-catalyzed hydrolysis of (+)/(-)-cocaine to examine the protein environmental effects on the catalytic reactions. Hydrogen 40-48 acetylcholinesterase (Cartwright blood group) Homo sapiens 209-229 18343905-8 2008 The results indicated that substitution of halogen and methyl groups by hydrogen at aromatic ring of the benzothiazepine decreased the affinity of these molecules towards enzyme that may be due to the polar non-polar repulsions of these moieties with the amino acid residues in the active site of AChE. Hydrogen 72-80 acetylcholinesterase (Cartwright blood group) Homo sapiens 297-301 17601647-0 2007 Interactions of Lycopodium alkaloids with acetylcholinesterase investigated by 1H NMR relaxation rate. Hydrogen 79-81 acetylcholinesterase (Cartwright blood group) Homo sapiens 42-62 17601647-5 2007 The results indicate that investigation of 1H NMR relaxation data is a useful method to locate the new Lycopodium alkaloids as AchE inhibitors. Hydrogen 43-45 acetylcholinesterase (Cartwright blood group) Homo sapiens 127-131 17055616-4 2007 The results showed that all compounds act inside the AChE gorge, making pi-pi interactions and hydrogen bonds with Trp86 and Ser203 and by high HOMO energies of Ser2003 and high LUMO energies of N-aryl derivatives. Hydrogen 95-103 acetylcholinesterase (Cartwright blood group) Homo sapiens 53-57 16108094-7 2005 The affinity of ligands with AChE was found to be the cumulative effects of number of hydrophobic contacts and hydrogen bonding. Hydrogen 111-119 acetylcholinesterase (Cartwright blood group) Homo sapiens 29-33 16854005-3 2005 Whereas G121/G116, G122/G117, and A204/A199 of AChE/BChE all can form hydrogen bonds with ACh to stabilize the transition state during the ACh hydrolysis, BChE only uses G117 and A199 to form hydrogen bonds with cocaine. Hydrogen 70-78 acetylcholinesterase (Cartwright blood group) Homo sapiens 47-51 16854005-3 2005 Whereas G121/G116, G122/G117, and A204/A199 of AChE/BChE all can form hydrogen bonds with ACh to stabilize the transition state during the ACh hydrolysis, BChE only uses G117 and A199 to form hydrogen bonds with cocaine. Hydrogen 192-200 acetylcholinesterase (Cartwright blood group) Homo sapiens 47-51 16022504-7 2005 This result confirmed formation of 3-pronged hydrogen bonds for the oxyanion hole of butyrylcholinesterase and 2-pronged hydrogen bonds for the oxyanion hole of acetylcholinesterase. Hydrogen 45-53 acetylcholinesterase (Cartwright blood group) Homo sapiens 161-181 16022504-7 2005 This result confirmed formation of 3-pronged hydrogen bonds for the oxyanion hole of butyrylcholinesterase and 2-pronged hydrogen bonds for the oxyanion hole of acetylcholinesterase. Hydrogen 121-129 acetylcholinesterase (Cartwright blood group) Homo sapiens 161-181 12197759-6 2002 Our calculations indicate that, in the AChE-ACh Michaelis complex, only two hydrogen bonds are formed between the carbonyl oxygen of ACh and the peptidic NH groups of Gly121 and Gly122. Hydrogen 76-84 acetylcholinesterase (Cartwright blood group) Homo sapiens 39-43 15006409-0 2004 1H NMR relaxation investigation of acetylcholinesterase inhibitors from huperzine A and derivative. Hydrogen 0-2 acetylcholinesterase (Cartwright blood group) Homo sapiens 35-55 11341833-0 2001 Short, strong hydrogen bonds at the active site of human acetylcholinesterase: proton NMR studies. Hydrogen 14-22 acetylcholinesterase (Cartwright blood group) Homo sapiens 57-77 34808043-7 2021 The obtained thermodynamic parameters reveal interactions driven by van der Waals forces and hydrogen bonds in the lapatinib-AChE system (DeltaH and DeltaS < 0). Hydrogen 93-101 acetylcholinesterase (Cartwright blood group) Homo sapiens 125-129 9871590-2 1998 It was revealed that the methyl group at the three carbon bridge of (-)-huperzine A can form a weak hydrogen bond with the phenol hydroxyl oxygen of Tyr121 and the main-chain oxygen of Gly118 of AChE, respectively. Hydrogen 100-108 acetylcholinesterase (Cartwright blood group) Homo sapiens 195-199 9568380-17 1998 We propose that, similar to a previous model for cationic inhibitors of AChE (13), the P = O delta- group of Me forms hydrogen bonds within the oxyanion-hole causing the leaving group (-SCH3) to orient towards the "gorge" opening. Hydrogen 118-126 acetylcholinesterase (Cartwright blood group) Homo sapiens 72-76 34907850-12 2021 Amentoflavone has the ability to inhibit acetylcholinesterase when tested in vitro, having an IC50 of 8.68 +- 0.73 microg/mL, corroborating its effect in the in silico test, presenting four strong covalent hydrogen bonds for having a bond length up to 2.5 A. Hydrogen 206-214 acetylcholinesterase (Cartwright blood group) Homo sapiens 41-61 33557647-4 2021 Molecular docking study showed that 23 binds to the active site of AChE and interacts via extensive pi-pi stacking with the indole and phenol side chains of Trp86 and Tyr337, besides the hydrogen bonding with the hydration site and pi-pi interaction with the phenol side chain of Y72. Hydrogen 187-195 acetylcholinesterase (Cartwright blood group) Homo sapiens 67-71 34541552-9 2021 To map protonation states in the hAChE active site gorge we collected 3.5 A neutron diffraction data paving the way for obtaining higher resolution datasets that will be needed to determine locations of individual hydrogen atoms. Hydrogen 214-222 acetylcholinesterase (Cartwright blood group) Homo sapiens 33-38 34636548-4 2021 In addition, molecular docking results revealed that the cations and organic anions of ILs bound to specific amino acid residues of AChE through noncovalent interactions such as pi interactions and hydrogen bonds. Hydrogen 198-206 acetylcholinesterase (Cartwright blood group) Homo sapiens 132-136 35053900-6 2022 The binding constant between baicalein and AChE was an order of magnitude of 104 L mol-1, and hydrogen bonding and hydrophobic interaction were the major forces for forming the baicalein-AChE complex. Hydrogen 94-102 acetylcholinesterase (Cartwright blood group) Homo sapiens 43-47 34836871-4 2021 Two compounds of the series 1g and 1h were found to be active against AChE whereas no derivative was active against BChE while the whole series showed excellent 1, 1-diphenyl-2-picrylhydrazyl scavenging activity. Hydrogen 35-37 acetylcholinesterase (Cartwright blood group) Homo sapiens 70-74 35527546-10 2022 The number of hydrogen bonds was such that the flexibility of the enzyme protein structure due to inhibitor binding reduced AChE function. Hydrogen 14-22 acetylcholinesterase (Cartwright blood group) Homo sapiens 124-128 35346014-9 2022 The studied molecules interacted with the active site of AChE through hydrophobic and hydrogen bonds and with NOS through hydrogen interactions only but in a meaningful manner. Hydrogen 86-94 acetylcholinesterase (Cartwright blood group) Homo sapiens 57-61 35053900-6 2022 The binding constant between baicalein and AChE was an order of magnitude of 104 L mol-1, and hydrogen bonding and hydrophobic interaction were the major forces for forming the baicalein-AChE complex. Hydrogen 94-102 acetylcholinesterase (Cartwright blood group) Homo sapiens 187-191 2874096-3 1986 The potency of inhibitory activity of H2-antagonists on acetylcholinesterase estimated from median inhibitory dose were in the following order of decreasing activity: ranitidine greater than TZU-0460 greater than cimetidine greater than YM-11170, whereas that on pseudocholinesterase were TZU-0460 greater than ranitidine greater than cimetidine greater than YM-11170. Hydrogen 38-40 acetylcholinesterase (Cartwright blood group) Homo sapiens 56-76 6326400-6 1984 The inhibition of the acetylcholinesterase activity by H2-antagonists is of no practical relevance. Hydrogen 55-57 acetylcholinesterase (Cartwright blood group) Homo sapiens 22-42 33923726-6 2021 The molecular docking showed that most of the compounds bound to AChE through hydrogen bonds with residues of the catalytic triad and pi-stacking interactions between the main scaffold and the aromatic residues present in the binding pocket. Hydrogen 78-86 acetylcholinesterase (Cartwright blood group) Homo sapiens 65-69 33979725-4 2021 And, the binding model from molecular docking analysis of both BSA and AChE with these molecules clearly displayed non-covalent interactions (hydrogen bonding and hydrophobic interactions) which played a significant role in the binding mechanism. Hydrogen 142-150 acetylcholinesterase (Cartwright blood group) Homo sapiens 71-75 33320652-12 2021 Interaction analysis reveals that hydrophobic and hydrogen-bonding interactions are the primary driving forces responsible for the observed high affinity of the compound with AChE. Hydrogen 50-58 acetylcholinesterase (Cartwright blood group) Homo sapiens 175-179 33583373-6 2021 Structure-activity relationship of xanthones revealed that the type and position of substituent(s) attached to the xanthone moiety influenced their acetylcholinesterase inhibition activities where hydrophobic moiety will lead to an improved activity by contributing the pi-pi interactions, as well as the hydroxy substituent(s) by forming hydrogen-bond interactions. Hydrogen 339-347 acetylcholinesterase (Cartwright blood group) Homo sapiens 148-168 32048433-10 2020 These studies reveal that the benzodioxole moiety exhibits strong interactions due to hydrogen bonds that form with the Glu201 (AChE) and Tyr440 (BChE) residues, which is reflected in the IC 50 values. Hydrogen 86-94 acetylcholinesterase (Cartwright blood group) Homo sapiens 128-132 32118214-2 2020 Based on molecular docking analyses with AChE, the meta-hydroxyl group in DC, nonexistent in curcumin, showed the formation of hydrogen bonds with Ser293 and Tyr341 in the binding sites of AChE. Hydrogen 127-135 acetylcholinesterase (Cartwright blood group) Homo sapiens 41-45 32520690-9 2021 Molecular docking model for the most active molecule exhibited promising bindings with AChE and BChE"s active site pertained to hydrophobic hydrogen bonds and positive ionizable interactions. Hydrogen 140-148 acetylcholinesterase (Cartwright blood group) Homo sapiens 87-91 32118214-2 2020 Based on molecular docking analyses with AChE, the meta-hydroxyl group in DC, nonexistent in curcumin, showed the formation of hydrogen bonds with Ser293 and Tyr341 in the binding sites of AChE. Hydrogen 127-135 acetylcholinesterase (Cartwright blood group) Homo sapiens 189-193 30706763-7 2020 The inhibitor with multihydroxyl side chains shows an obviously large electrostatic interaction as it forms additional hydrogen bonds with AChE. Hydrogen 119-127 acetylcholinesterase (Cartwright blood group) Homo sapiens 139-143 31813875-3 2019 Series of new compounds were designed, synthesized and evaluated in this work, from which we identified 2-((4-(1,3-dioxoisoindolin-2-yl)benzyl)amino)-2-oxoethyl-2-(4-methoxyphenyl)acetate (1h) as a new dual cholinesterase and beta-secretase inhibitor without toxicity. Hydrogen 189-191 acetylcholinesterase (Cartwright blood group) Homo sapiens 207-221 31491736-6 2019 According to theoretical analysis, hydrogen bonding, van der Waals, and hydrophobic forces are the main binding interactions for each V(V) complex and AChE. Hydrogen 35-43 acetylcholinesterase (Cartwright blood group) Homo sapiens 151-155 31271801-8 2019 Docking simulations showed binding affinities of compounds 1 to 5 for hMAO-B were higher than those for hMAO-A or AChE and suggested these five chalcones form hydrogen bonds with MAO-B at Cys172 but that they do not form hydrogen bonds with hMAO-A or AChE. Hydrogen 159-167 acetylcholinesterase (Cartwright blood group) Homo sapiens 114-118 29697300-0 2019 Cooperative hydrogen bonds and mobility of the non-aromatic ring as selectivity determinants for human acetylcholinesterase to similar anti-Alzheimer"s galantaminics: a computational study. Hydrogen 12-20 acetylcholinesterase (Cartwright blood group) Homo sapiens 103-123 31100281-5 2019 Docking studies revealed that the quinoline group within the AChE active site was positioned in the choline binding site, while the C(4)-amino group substituents, depending on their lipophilicity, could establish hydrogen bonds or pi-interactions with residues of the peripheral anionic site. Hydrogen 213-221 acetylcholinesterase (Cartwright blood group) Homo sapiens 61-65 31173012-8 2019 The WTMtD simulations further reveal that the bridged water molecules are more ordered near the catalytic triad of AChE to deter the nucleophilicity of Ser203 through intermolecular hydrogen bonding when donepezil approaches near to the active site gorge of AChE. Hydrogen 182-190 acetylcholinesterase (Cartwright blood group) Homo sapiens 115-119 31173012-8 2019 The WTMtD simulations further reveal that the bridged water molecules are more ordered near the catalytic triad of AChE to deter the nucleophilicity of Ser203 through intermolecular hydrogen bonding when donepezil approaches near to the active site gorge of AChE. Hydrogen 182-190 acetylcholinesterase (Cartwright blood group) Homo sapiens 258-262 29980922-5 2018 The SMD simulations show that RS194B retains in more stable gauche conformation inside the active gorge of AChE during different time intervals that experiences more hydrogen bonding, hydrophobic interactions with the catalytic anionic site (CAS) residues and weaker interactions with the peripheral anionic site (PAS) residues compared to RS41A and RS69N. Hydrogen 166-174 acetylcholinesterase (Cartwright blood group) Homo sapiens 107-111 29966870-3 2018 Profiling of donepezil, a potent acetylcholinesterase (hAChE) inhibitor, into BACE-1 inhibition was achieved through introduction of backbone amide linkers to the designed compounds which are capable of hydrogen-bonding with BACE-1 catalytic site. Hydrogen 203-211 acetylcholinesterase (Cartwright blood group) Homo sapiens 55-60 29564983-7 2018 RESULTS: Ligplot analysis indicated that abietic acid had strong binding efficiency with AchE and HDAC3 receptors forming one and four hydrogen bonds respectively. Hydrogen 135-143 acetylcholinesterase (Cartwright blood group) Homo sapiens 89-93 28495556-1 2017 Pursuing the strategy of developing potent AChE inhibitors, we attempted to carry out the N1-substitution of 2,3-dihydroquinazolin-4(1H)-one core. Hydrogen 133-135 acetylcholinesterase (Cartwright blood group) Homo sapiens 43-47 28629119-7 2017 Molecular docking analyses were conducted for potential AChE and BChE inhibitors, and the results demonstrated that the peripheral anionic sites of target proteins were predominant binding sites for these compounds through hydrogen bonds and halogen interactions instead of hydrophobic interactions in the catalytic active site. Hydrogen 223-231 acetylcholinesterase (Cartwright blood group) Homo sapiens 56-60 27410776-10 2017 Isoalloxazine derivatives were docked against human AChE, which revealed critical residues implicated in hydrogen bonds as well as hydrophobic interactions. Hydrogen 105-113 acetylcholinesterase (Cartwright blood group) Homo sapiens 52-56 28406297-6 2017 Although several hydrogen bonds between ligands and AChE do appear, no significant values of BIEs have been recorded. Hydrogen 17-25 acetylcholinesterase (Cartwright blood group) Homo sapiens 52-56 26468911-2 2015 We present oxime (HI-6) unbinding from the active site gorge of AChE, known to be strongly influenced by intermolecular cation-pi, hydrogen bridge (HB) and water bridge (WB) interactions and by molecular simulations with effective polarization in polarizable mean-field model of TIP3P water. Hydrogen 131-139 acetylcholinesterase (Cartwright blood group) Homo sapiens 64-68 27602288-13 2016 Molecular docking revealed that compounds 13, 5 and 28 exhibited the lowest binding energies of -12.2, -12.0 and -12.0 kcal/mol, respectively, against human AChE, which is modulated by hydrogen bonding, pi-pi stacking and hydrophobic interaction inside the binding pocket. Hydrogen 185-193 acetylcholinesterase (Cartwright blood group) Homo sapiens 157-161 27697060-7 2016 Both, hydrogen bond and hydrophobic interactions were found to be involved in the proper positioning of these diabetic drugs within the catalytic site (CAS) of AChE and BACE enzymes to permit docking. Hydrogen 6-14 acetylcholinesterase (Cartwright blood group) Homo sapiens 160-164 26833077-9 2016 The compound forms strong hydrogen bonding at the peripheral anionic site of AChE whereas on BChE, it had hydrophobic and mild polar interactions. Hydrogen 26-34 acetylcholinesterase (Cartwright blood group) Homo sapiens 77-81 26584298-7 2015 Molecular docking revealed that compounds 6 and 7 interacted differently on AChE and BChE, by means of hydrophobic interactions and hydrogen bonding. Hydrogen 132-140 acetylcholinesterase (Cartwright blood group) Homo sapiens 76-80 26153025-2 2015 A multistep functionalization strategy was developed on a crystalline silicon surface: a carboxylic acid-terminated monolayer was grafted onto a hydrogen-terminated silicon surface by photochemical hydrosilylation, and then AChE was covalently attached through amide bonds using an activation EDC/NHS process. Hydrogen 145-153 acetylcholinesterase (Cartwright blood group) Homo sapiens 224-228 24836068-8 2014 Thorough docking calculations of the seven most potent AChE inhibitors from the set, showed that the hydrogen bond can be formed between amide -NH- moiety of compounds and -OH group of Tyr 124. Hydrogen 101-109 acetylcholinesterase (Cartwright blood group) Homo sapiens 55-59 25143139-8 2014 The molecular property-affinity relationship reveals that the hydrogen bond force plays an important role in binding flavonoids to AChE. Hydrogen 62-70 acetylcholinesterase (Cartwright blood group) Homo sapiens 131-135