PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 22975155-7 2013 Computational molecular modeling of RS41A and RS194B interactions with VX inhibited hAChE, bound reversibly in Michaelis type complex and covalently in the pentacoordinate reaction intermediate suggests that the faster reactivation reaction is a consequence of a tighter RS194B interactions with hAChE peripheral site (PAS) residues, in particular with D74, resulting in lower interaction energies for formation of both the binding and reactivation states. Aminosalicylic Acid 319-322 acetylcholinesterase (Cartwright blood group) Homo sapiens 84-89 21570330-4 2011 The hCyt c was bound to peripheral anionic site (PAS) on hAChE and binding mode of the docked conformation was very similar to the reported crystal structure of the AChE and fasciculin-II (Fas-II) complex. Aminosalicylic Acid 49-52 acetylcholinesterase (Cartwright blood group) Homo sapiens 57-62 23515568-1 2013 Atomic force microscopy (AFM) was applied for obtaining structural information about acetylcholinesterase (AChE) tetramer (AChE G(4)) before and after reaction with S-acetylcholine iodide (S-ACh), in the presence or absence of propidium iodide (PI), an inhibitor for peripheral anionic sites (PAS). Aminosalicylic Acid 293-296 acetylcholinesterase (Cartwright blood group) Homo sapiens 85-105 23515568-1 2013 Atomic force microscopy (AFM) was applied for obtaining structural information about acetylcholinesterase (AChE) tetramer (AChE G(4)) before and after reaction with S-acetylcholine iodide (S-ACh), in the presence or absence of propidium iodide (PI), an inhibitor for peripheral anionic sites (PAS). Aminosalicylic Acid 293-296 acetylcholinesterase (Cartwright blood group) Homo sapiens 107-111 23062825-7 2012 Using molecular docking studies, it was further proven that chelerythrine binds on both the catalytic site and the peripheral anionic site (PAS) of the AChE. Aminosalicylic Acid 140-143 acetylcholinesterase (Cartwright blood group) Homo sapiens 152-156 22467516-4 2012 These results support the outcome of docking studies which tested compounds targeting both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 156-159 acetylcholinesterase (Cartwright blood group) Homo sapiens 164-168 22229321-9 2011 CP displayed variable docking poses with the peripheral anionic site (PAS) of human AChE. Aminosalicylic Acid 70-73 acetylcholinesterase (Cartwright blood group) Homo sapiens 84-88 23353586-2 2013 The AD pathogenicity involved in AChE protein is mainly due to amyloid beta peptide aggregation, which is triggered specifically by peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 157-160 acetylcholinesterase (Cartwright blood group) Homo sapiens 33-37 23353586-2 2013 The AD pathogenicity involved in AChE protein is mainly due to amyloid beta peptide aggregation, which is triggered specifically by peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 157-160 acetylcholinesterase (Cartwright blood group) Homo sapiens 165-169 23353586-3 2013 In the present study, a workflow has been developed for the identification and prioritization of potential compounds that could interact not only with the catalytic site but also with the PAS of AChE. Aminosalicylic Acid 188-191 acetylcholinesterase (Cartwright blood group) Homo sapiens 195-199 23353586-10 2013 The knowledge gained from this study, could lead to the discovery of potential AChE inhibitors that are highly specific for AD treatment as they are bivalent lead molecules endowed with dual binding ability for both catalytic site and PAS of AChE. Aminosalicylic Acid 235-238 acetylcholinesterase (Cartwright blood group) Homo sapiens 79-83 23353586-10 2013 The knowledge gained from this study, could lead to the discovery of potential AChE inhibitors that are highly specific for AD treatment as they are bivalent lead molecules endowed with dual binding ability for both catalytic site and PAS of AChE. Aminosalicylic Acid 235-238 acetylcholinesterase (Cartwright blood group) Homo sapiens 242-246 21570330-4 2011 The hCyt c was bound to peripheral anionic site (PAS) on hAChE and binding mode of the docked conformation was very similar to the reported crystal structure of the AChE and fasciculin-II (Fas-II) complex. Aminosalicylic Acid 49-52 acetylcholinesterase (Cartwright blood group) Homo sapiens 58-62 11523986-2 2001 We have shown that AChE interacts with the amyloid beta-peptide (Abeta) and promotes amyloid fibril formation by a hydrophobic environment close to the peripheral anionic binding site (PAS) of the enzyme. Aminosalicylic Acid 185-188 acetylcholinesterase (Cartwright blood group) Homo sapiens 19-23 21211982-3 2011 A Lineweaver-Burk plot and molecular modeling study showed that these hybrids targeted both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 157-160 acetylcholinesterase (Cartwright blood group) Homo sapiens 165-169 20823602-3 2010 The inhibition mechanism revealed that the best active compound 4e displayed a mix-type mode of AChE and BChE by its dual-site interactions with the catalytic triad active center and the peripheral anionic site (PAS) of enzyme. Aminosalicylic Acid 212-215 acetylcholinesterase (Cartwright blood group) Homo sapiens 96-100 15974895-4 2005 Recently, novel dual inhibitors of AChE have been developed that target both the active site of the enzyme as well as the peripheral anionic site (PAS). Aminosalicylic Acid 147-150 acetylcholinesterase (Cartwright blood group) Homo sapiens 35-39 15483114-2 2004 The noncatalytic functions of AChE have been attributed to its peripheral anionic site (PAS)-mediated protein-protein interactions. Aminosalicylic Acid 88-91 acetylcholinesterase (Cartwright blood group) Homo sapiens 30-34 15483114-9 2004 Moreover, the PAS blockade-induced glutamatergic impairments were associated with a depressed expression of beta-neurexins and an accumulation of other synaptic proteins, including neuroligins, and were mostly preventable by antisense suppression of AChE expression. Aminosalicylic Acid 14-17 acetylcholinesterase (Cartwright blood group) Homo sapiens 250-254 11904227-9 2002 Excess substrate binds to the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 55-58 acetylcholinesterase (Cartwright blood group) Homo sapiens 63-67 11904227-10 2002 The finding that AChE is activated by excess substrate supports the idea that binding of a second substrate molecule to the PAS induces a conformational change that reorganizes the active site. Aminosalicylic Acid 124-127 acetylcholinesterase (Cartwright blood group) Homo sapiens 17-21 21397996-4 2011 These dual binding inhibitors, being able to interact both with the peripheral anionic site (PAS) of AChE and the catalytic subsite, proved to be able to inhibit the AChE-induced Abeta aggregation. Aminosalicylic Acid 93-96 acetylcholinesterase (Cartwright blood group) Homo sapiens 101-105 21397996-4 2011 These dual binding inhibitors, being able to interact both with the peripheral anionic site (PAS) of AChE and the catalytic subsite, proved to be able to inhibit the AChE-induced Abeta aggregation. Aminosalicylic Acid 93-96 acetylcholinesterase (Cartwright blood group) Homo sapiens 166-170 20056426-5 2010 Molecular modeling studies confirmed that these hybrids target both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 133-136 acetylcholinesterase (Cartwright blood group) Homo sapiens 141-145 19051205-9 2009 The non-catalytic antibodies, AE-2 and the Ab2, recognized AChE"s peripheral anionic site (PAS), in particular, the sequence (70)YQYVD, which contains two of the site"s residues. Aminosalicylic Acid 91-94 acetylcholinesterase (Cartwright blood group) Homo sapiens 59-63 17359933-7 2007 The peripheral anionic site (PAS) is encoded by invariant exons and represents the domain involved in non-cholinergic functions of AChE. Aminosalicylic Acid 29-32 acetylcholinesterase (Cartwright blood group) Homo sapiens 131-135 17359933-8 2007 Masking of PAS with fasciculin results in a significant decrease of neurite outgrowth in all clones overexpressing AChE. Aminosalicylic Acid 11-14 acetylcholinesterase (Cartwright blood group) Homo sapiens 115-119 17359933-13 2007 Our results indicate that PAS could directly or indirectly mediate AChE/fibronectin interactions. Aminosalicylic Acid 26-29 acetylcholinesterase (Cartwright blood group) Homo sapiens 67-71 17005406-4 2006 In addition, the propidium displacement experiments showed that these compounds bind AChE to the peripheral anionic site (PAS) of AChE and, consequently, are potential agents that can prevent the aggregation of beta-amyloid. Aminosalicylic Acid 122-125 acetylcholinesterase (Cartwright blood group) Homo sapiens 85-89 17005406-4 2006 In addition, the propidium displacement experiments showed that these compounds bind AChE to the peripheral anionic site (PAS) of AChE and, consequently, are potential agents that can prevent the aggregation of beta-amyloid. Aminosalicylic Acid 122-125 acetylcholinesterase (Cartwright blood group) Homo sapiens 130-134 15034934-1 2004 Acetylcholinesterase mediates cell adhesion and neurite outgrowth through a site associated with the peripheral anionic site (PAS). Aminosalicylic Acid 126-129 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-20 30890752-2 2019 In addition, we determined the ability of MB-gCs to bind to the peripheral anionic site (PAS) of Electrophorus electricus AChE (EeAChE) and competitively displace propidium iodide from this site. Aminosalicylic Acid 89-92 acetylcholinesterase (Cartwright blood group) Homo sapiens 122-126 10619655-4 1999 The action of AChE was not affected by edrophonium and tacrine both active site inhibitors, but it was abolished by propidium and gallamine, two peripheral anionic binding site (PAS) ligands. Aminosalicylic Acid 178-181 acetylcholinesterase (Cartwright blood group) Homo sapiens 14-18 10619655-5 1999 We conclude that the PAS domain of AChE is involved in the neurotrophic activity of the enzyme. Aminosalicylic Acid 21-24 acetylcholinesterase (Cartwright blood group) Homo sapiens 35-39 7492545-1 1995 Replacement of residues Asp74, Trp286, and Tyr72, which are constituents of the peripheral anionic site (PAS) of human acetylcholinesterase (HuAChE), affected similarly both the binding and the inhibition constants of the PAS-specific ligand propidium, demonstrating that changes in the inhibitory activity are a direct consequence of altered binding to the PAS. Aminosalicylic Acid 105-108 acetylcholinesterase (Cartwright blood group) Homo sapiens 119-139 7492545-1 1995 Replacement of residues Asp74, Trp286, and Tyr72, which are constituents of the peripheral anionic site (PAS) of human acetylcholinesterase (HuAChE), affected similarly both the binding and the inhibition constants of the PAS-specific ligand propidium, demonstrating that changes in the inhibitory activity are a direct consequence of altered binding to the PAS. Aminosalicylic Acid 222-225 acetylcholinesterase (Cartwright blood group) Homo sapiens 119-139 7492545-1 1995 Replacement of residues Asp74, Trp286, and Tyr72, which are constituents of the peripheral anionic site (PAS) of human acetylcholinesterase (HuAChE), affected similarly both the binding and the inhibition constants of the PAS-specific ligand propidium, demonstrating that changes in the inhibitory activity are a direct consequence of altered binding to the PAS. Aminosalicylic Acid 222-225 acetylcholinesterase (Cartwright blood group) Homo sapiens 119-139 31271946-6 2019 Compounds 44 and 67 produced significant displacement of propidium iodide from the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 108-111 acetylcholinesterase (Cartwright blood group) Homo sapiens 116-120 34662731-7 2022 In particular, it showed that binding of a competing ligand on PAS may affect the catalytic behavior of AChE and BChE in an opposite way, i.e. inhibition of AChE and activation of BChE, regardless the nature of the reporter substrate. Aminosalicylic Acid 63-66 acetylcholinesterase (Cartwright blood group) Homo sapiens 104-108 34662731-7 2022 In particular, it showed that binding of a competing ligand on PAS may affect the catalytic behavior of AChE and BChE in an opposite way, i.e. inhibition of AChE and activation of BChE, regardless the nature of the reporter substrate. Aminosalicylic Acid 63-66 acetylcholinesterase (Cartwright blood group) Homo sapiens 157-161 30928873-4 2019 Furthermore, the docking study of the compounds 7f and 7i showed that these compounds bound to both the catalytic site (CS) and peripheral anionic site (PAS) of AChE and BuChE, respectively. Aminosalicylic Acid 153-156 acetylcholinesterase (Cartwright blood group) Homo sapiens 161-165 29663860-6 2019 Both the coumarin derivatives were observed to bind to the peripheral anionic site (PAS) of AChE and also found to displace the fluorescence marker thioflavinT (ThT) from AChE binding pocket. Aminosalicylic Acid 84-87 acetylcholinesterase (Cartwright blood group) Homo sapiens 92-96 30890752-6 2019 Molecular docking results showed that the MB-gCs could bind both to the catalytic active site and to the PAS of human AChE and BChE. Aminosalicylic Acid 105-108 acetylcholinesterase (Cartwright blood group) Homo sapiens 118-122 29775949-8 2018 The Lineweaver-Burk plot and docking study showed that compound 5 h targeted both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 147-150 acetylcholinesterase (Cartwright blood group) Homo sapiens 155-159 30411689-9 2019 Molecular docking study indicated that the spirocyclohexadienone, 9e (IC50 = 0.12 microM), a mixedtype AChE inhibitor, showed a good interaction at active site of the enzyme, including the cationic (CAS) and the peripheral site (PAS). Aminosalicylic Acid 229-232 acetylcholinesterase (Cartwright blood group) Homo sapiens 103-107 30257474-5 2018 In a previous work, we performed an inedited theoretical investigation on the binding modes of these molecules on the peripheral anionic site (PAS) of human AChE (HssAChE), revealing that the metabolites can also bind in the PAS in the same way as AFB1. Aminosalicylic Acid 143-146 acetylcholinesterase (Cartwright blood group) Homo sapiens 157-161 30257474-5 2018 In a previous work, we performed an inedited theoretical investigation on the binding modes of these molecules on the peripheral anionic site (PAS) of human AChE (HssAChE), revealing that the metabolites can also bind in the PAS in the same way as AFB1. Aminosalicylic Acid 225-228 acetylcholinesterase (Cartwright blood group) Homo sapiens 157-161 27766908-6 2017 Molecular docking studies of the most active compound 7 in AChE showed that this compound can interact with both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 178-181 acetylcholinesterase (Cartwright blood group) Homo sapiens 59-63 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. Aminosalicylic Acid 314-317 acetylcholinesterase (Cartwright blood group) Homo sapiens 107-111 28617100-6 2018 Molecular docking study revealed that compound 7 could combine both catalytic active site (CAS) and peripheral active site (PAS) of AChE with four points (Trp84, Trp279, Tyr70 and Phe330), while it could bind with BuChE via only His 20. Aminosalicylic Acid 124-127 acetylcholinesterase (Cartwright blood group) Homo sapiens 132-136 28963904-5 2017 The synthetic xanthone 11 showed the best inhibitory effect on AChE and a molecular modeling study revealed that 11 targeted both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 195-198 acetylcholinesterase (Cartwright blood group) Homo sapiens 63-67 28963904-5 2017 The synthetic xanthone 11 showed the best inhibitory effect on AChE and a molecular modeling study revealed that 11 targeted both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 195-198 acetylcholinesterase (Cartwright blood group) Homo sapiens 203-207 29886321-6 2018 Pleasingly, whereas compound 4 showed to be a highly potent inhibitor of AChE (IC50 = 6 nM) and binds to AChE-PAS to the same extent as donepezil, its prodrug 3 revealed to be inactive (IC50 > 10 muM). Aminosalicylic Acid 110-113 acetylcholinesterase (Cartwright blood group) Homo sapiens 105-109 27801600-6 2017 Molecular docking and enzyme kinetic study on compound 4l suggested that it simultaneously binds to the catalytic active site (CAS) and peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 161-164 acetylcholinesterase (Cartwright blood group) Homo sapiens 169-173 27766908-6 2017 Molecular docking studies of the most active compound 7 in AChE showed that this compound can interact with both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 178-181 acetylcholinesterase (Cartwright blood group) Homo sapiens 186-190 28646405-6 2017 Such orientation of K203 experiences favorable interaction with the surrounding residues of catalytic anionic site (CAS) and peripheral anionic site (PAS) of tabun-inhibited AChE. Aminosalicylic Acid 150-153 acetylcholinesterase (Cartwright blood group) Homo sapiens 174-178 28374576-3 2017 The amyloid beta (Abeta) peptide binds in the peripheral anionic site (PAS) at the entrance of the binding gorge of AChE and initiates the formation of amyloid plaques. Aminosalicylic Acid 71-74 acetylcholinesterase (Cartwright blood group) Homo sapiens 116-120 28374576-4 2017 The blockade of PAS prevents from AChE-induced Abeta aggregation. Aminosalicylic Acid 16-19 acetylcholinesterase (Cartwright blood group) Homo sapiens 34-38 28374576-10 2017 The CAM fragment of the best binders fits in the same region, proximal to PAS, where the Omega-loop of Abeta binds to AChE. Aminosalicylic Acid 74-77 acetylcholinesterase (Cartwright blood group) Homo sapiens 118-122 27392529-3 2016 AChE molecular modeling studies of these hybrids indicated that tacrine moiety interacts in the bottom of the gorge with the catalytic active site (CAS) while tianeptine binds to peripheral anionic site (PAS). Aminosalicylic Acid 204-207 acetylcholinesterase (Cartwright blood group) Homo sapiens 0-4 28492309-8 2017 Specifically, the fullerene core covered the enzyme gorge as a lid through pi-pi stacking with Tyr72 and Trp286 in the PAS, while the hydrophobic ligands on the fullerene surface inserted into the AChE active site to provide further stability for the complexes. Aminosalicylic Acid 119-122 acetylcholinesterase (Cartwright blood group) Homo sapiens 197-201 27863370-5 2017 Also, molecular modeling and kinetic studies showed that compounds 5l and 5j bound simultaneously to the peripheral anionic site (PAS) and catalytic sites (CS) of the AChE and BChE. Aminosalicylic Acid 130-133 acetylcholinesterase (Cartwright blood group) Homo sapiens 167-171 27910192-6 2016 Also, kinetic and molecular docking studies of binding interactions elucidated that compound 6f bound to both the catalytic anionic site (CAS) and peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 172-175 acetylcholinesterase (Cartwright blood group) Homo sapiens 180-184 27214510-5 2016 Based on the docking study of AChE, the prototype compound 4o was laid across the active site and occupied both peripheral anionic site (PAS) and catalytic anionic site (CAS). Aminosalicylic Acid 137-140 acetylcholinesterase (Cartwright blood group) Homo sapiens 30-34 26579427-4 2015 Lineweaver-Burk plot and molecular modeling study showed that compound 4b targeted both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 153-156 acetylcholinesterase (Cartwright blood group) Homo sapiens 161-165 27492242-1 2016 The enzyme acetylcholinesterase is a key target in the treatment of Alzheimer"s disease because of its ability to hydrolyze acetylcholine via the catalytic binding site and to accelerate the aggregation of amyloid-beta peptide via the peripheral anionic site (PAS). Aminosalicylic Acid 260-263 acetylcholinesterase (Cartwright blood group) Homo sapiens 11-31 26752094-5 2016 Furthermore, molecular modeling study showed that 5q targeted both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 132-135 acetylcholinesterase (Cartwright blood group) Homo sapiens 140-144 24628027-3 2014 Compound 11b bearing an octylene linker exhibited interactions with both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 138-141 acetylcholinesterase (Cartwright blood group) Homo sapiens 146-150 26639720-14 2015 In the present study, taking acyclic derivatives of 6-methyluracil as a model AChE inhibitor, we attempted to develop AChE inhibitors that specifically bind to the PAS with weak binding to the active site of AChE. Aminosalicylic Acid 164-167 acetylcholinesterase (Cartwright blood group) Homo sapiens 78-82 26639720-14 2015 In the present study, taking acyclic derivatives of 6-methyluracil as a model AChE inhibitor, we attempted to develop AChE inhibitors that specifically bind to the PAS with weak binding to the active site of AChE. Aminosalicylic Acid 164-167 acetylcholinesterase (Cartwright blood group) Homo sapiens 118-122 26639720-14 2015 In the present study, taking acyclic derivatives of 6-methyluracil as a model AChE inhibitor, we attempted to develop AChE inhibitors that specifically bind to the PAS with weak binding to the active site of AChE. Aminosalicylic Acid 164-167 acetylcholinesterase (Cartwright blood group) Homo sapiens 118-122 26639720-15 2015 We attempted to increase the size of AChE ligands to restrict specific binding to the PAS of AChE. Aminosalicylic Acid 86-89 acetylcholinesterase (Cartwright blood group) Homo sapiens 37-41 26639720-15 2015 We attempted to increase the size of AChE ligands to restrict specific binding to the PAS of AChE. Aminosalicylic Acid 86-89 acetylcholinesterase (Cartwright blood group) Homo sapiens 93-97 26639720-18 2015 Based on molecular docking simulations, it was suggested that compounds bind AChE to the active center as well as to the PAS or only to the PAS. Aminosalicylic Acid 140-143 acetylcholinesterase (Cartwright blood group) Homo sapiens 77-81 26639721-14 2015 RESULTS: During unconstrained MD, C547 very rapidly binded to the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 91-94 acetylcholinesterase (Cartwright blood group) Homo sapiens 99-103 24628027-5 2014 The AChE-induced beta-amyloid (Abeta) aggregation assay gave further experimental support to this finding: Abeta1-40 aggregation catalyzed by the PAS of AChE might be inhibited by compound 11b in a concentration-dependent manner and seems to occur only with one photochromic form. Aminosalicylic Acid 146-149 acetylcholinesterase (Cartwright blood group) Homo sapiens 4-8 24628027-5 2014 The AChE-induced beta-amyloid (Abeta) aggregation assay gave further experimental support to this finding: Abeta1-40 aggregation catalyzed by the PAS of AChE might be inhibited by compound 11b in a concentration-dependent manner and seems to occur only with one photochromic form. Aminosalicylic Acid 146-149 acetylcholinesterase (Cartwright blood group) Homo sapiens 153-157 23984975-2 2013 The inhibitors" aromatic properties were varied to establish structure-activity relationships (SAR) between the inhibitors and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 156-159 acetylcholinesterase (Cartwright blood group) Homo sapiens 164-168 23981668-2 2014 The peripheral anionic site (PAS) of AChE has been indicated as the amyloid-beta (Abeta) binding domain. Aminosalicylic Acid 29-32 acetylcholinesterase (Cartwright blood group) Homo sapiens 37-41 24475704-3 2013 A Lineweaver-Burk plot and molecular modeling study showed that these derivatives targeted both the catalytic active site (CAS) and the peripheral anionic site (PAS) of AChE. Aminosalicylic Acid 161-164 acetylcholinesterase (Cartwright blood group) Homo sapiens 169-173