{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,7]],"date-time":"2026-08-07T17:15:50Z","timestamp":1786122950345,"version":"build-2736575974"},"reference-count":131,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:00:00Z","timestamp":1788220800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/100018255","name":"GLA University","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100018255","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Chemico-Biological Interactions"],"published-print":{"date-parts":[[2026,9]]},"DOI":"10.1016\/j.cbi.2026.112224","type":"journal-article","created":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T15:34:41Z","timestamp":1783006481000},"page":"112224","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":0,"special_numbering":"C","title":["Interactions-guided blueprint of acetylcholinesterase binding: A review on structural and molecular determinants"],"prefix":"10.1016","volume":"437","author":[{"ORCID":"https:\/\/orcid.org\/0009-0001-5478-626X","authenticated-orcid":false,"given":"Ram","family":"Kumar","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0009-0006-6147-3516","authenticated-orcid":false,"given":"Suman","family":"Sinha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6547-1637","authenticated-orcid":false,"given":"M. Arockia","family":"Babu","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cbi.2026.112224_bib1","first-page":"1","article-title":"Smily, aetiology and pathophysiology of neurodegenerative disorders, nanomedical drug deliv","author":"Sahoo","year":"2022","journal-title":"Neurodegener. Dis."},{"key":"10.1016\/j.cbi.2026.112224_bib2","doi-asserted-by":"crossref","DOI":"10.3390\/ijms23031851","article-title":"A review of the common neurodegenerative disorders: current therapeutic approaches and the potential role of nanotherapeutics","volume":"23","author":"Lamptey","year":"2022","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.cbi.2026.112224_bib3","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.1002\/psp4.12852","article-title":"Hallmarks of neurodegenerative disease: a systems pharmacology perspective","volume":"11","author":"Bloomingdale","year":"2022","journal-title":"CPT Pharmacometrics Syst. Pharmacol."},{"key":"10.1016\/j.cbi.2026.112224_bib4","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/j.cell.2022.12.032","article-title":"Hallmarks of neurodegenerative diseases","volume":"186","author":"Wilson","year":"2023","journal-title":"Cell"},{"key":"10.1016\/j.cbi.2026.112224_bib5","doi-asserted-by":"crossref","DOI":"10.3390\/ijms241310809","article-title":"Unraveling molecular and genetic insights into neurodegenerative diseases: advances in understanding alzheimer's, parkinson's, and Huntington's diseases and amyotrophic lateral sclerosis","volume":"24","author":"Ciurea","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.cbi.2026.112224_bib6","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.3390\/ijms22031273","article-title":"The cholinergic system, the adrenergic system and the neuropathology of alzheimer's disease","volume":"22","author":"Bekdash","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.cbi.2026.112224_bib7","article-title":"Role of cholinergic signaling in alzheimer's disease","volume":"27","author":"Chen","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.cbi.2026.112224_bib8","doi-asserted-by":"crossref","first-page":"2183","DOI":"10.1007\/s12035-020-02232-6","article-title":"Cholesterol metabolism in neurodegenerative diseases: molecular mechanisms and therapeutic targets","volume":"58","author":"Dai","year":"2021","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.cbi.2026.112224_bib9","doi-asserted-by":"crossref","first-page":"9290","DOI":"10.3390\/ijms22179290","article-title":"Acetylcholinesterase inhibitors in the treatment of neurodegenerative diseases and the role of acetylcholinesterase in their pathogenesis","volume":"22","author":"Walczak-Nowicka","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.cbi.2026.112224_bib10","doi-asserted-by":"crossref","first-page":"2709","DOI":"10.1007\/978-3-030-62059-2_418","article-title":"Acetylcholinesterase inhibitors (Galantamine, Rivastigmine, and Donepezil)","author":"Sridhar","year":"2022","journal-title":"NeuroPsychopharmacotherapy"},{"key":"10.1016\/j.cbi.2026.112224_bib11","doi-asserted-by":"crossref","DOI":"10.1016\/j.neuropharm.2020.108352","article-title":"Efficacy of acetylcholinesterase inhibitors in Alzheimer's disease","volume":"190","author":"Marucci","year":"2021","journal-title":"Neuropharmacology"},{"key":"10.1016\/j.cbi.2026.112224_bib12","article-title":"Acetylcholinesterase: a versatile template to coin potent modulators of multiple therapeutic targets","volume":"57","author":"Luque","year":"2023","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.cbi.2026.112224_bib13","first-page":"580","article-title":"A comprehensive review of cholinesterase modeling and simulation","volume":"11","author":"De Boer","year":"2021","journal-title":"Biomol"},{"key":"10.1016\/j.cbi.2026.112224_bib14","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2021.105354","article-title":"Dual targeting of acetylcholinesterase and tau aggregation: design, synthesis and evaluation of multifunctional deoxyvasicinone analogues for Alzheimer's disease","volume":"116","author":"Manzoor","year":"2021","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib15","doi-asserted-by":"crossref","first-page":"7303","DOI":"10.3390\/ijms25137303","article-title":"Ceanothanes derivatives as peripheric anionic site and catalytic active site inhibitors of acetylcholinesterase: insights for future drug design","volume":"25","author":"Pastene-Burgos","year":"2024","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.cbi.2026.112224_bib16","doi-asserted-by":"crossref","first-page":"1362","DOI":"10.3390\/antiox12071362","article-title":"Inhibition of acetylcholinesterase and Amyloid-\u03b2 aggregation by piceatannol and analogs: assessing in vitro and in vivo impact on a murine model of scopolamine-induced memory impairment","volume":"12","author":"Sie","year":"2023","journal-title":"Antioxidants"},{"key":"10.1016\/j.cbi.2026.112224_bib17","article-title":"Natural acetylcholinesterase inhibitors: a multi-targeted therapeutic potential in Alzheimer's disease","volume":"11","author":"Gajendra","year":"2024","journal-title":"Eur. J. Med. Chem. Reports"},{"key":"10.1016\/j.cbi.2026.112224_bib18","doi-asserted-by":"crossref","DOI":"10.3389\/fnmol.2016.00160","article-title":"Neuromuscular junction impairment in amyotrophic lateral sclerosis: reassessing the role of acetylcholinesterase","volume":"9","author":"Campanari","year":"2016","journal-title":"Front. Mol. Neurosci."},{"key":"10.1016\/j.cbi.2026.112224_bib19","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.cbi.2005.10.007","article-title":"Targeting acetylcholinesterase to the neuromuscular synapse","volume":"157\u2013158","author":"Rotundo","year":"2005","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2026.112224_bib20","doi-asserted-by":"crossref","first-page":"102","DOI":"10.1016\/j.jneuroim.2009.11.004","article-title":"Anti-acetylcholinesterase antibodies associate with ocular myasthenia gravis","volume":"218","author":"Provenzano","year":"2010","journal-title":"J. Neuroimmunol."},{"key":"10.1016\/j.cbi.2026.112224_bib21","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1021\/tx050090r","article-title":"Mechanistic insight into acetylcholinesterase inhibition and acute toxicity of organophosphorus compounds: a molecular modeling study","volume":"19","author":"Guo","year":"2006","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2026.112224_bib22","doi-asserted-by":"crossref","first-page":"1756","DOI":"10.1134\/S002209302305023X","article-title":"Organophospate-induced pathology: mechanisms of development, principles of therapy and features of experimental studies","volume":"59","author":"Goncharov","year":"2023","journal-title":"J. Evol. Biochem. Physiol."},{"key":"10.1016\/j.cbi.2026.112224_bib23","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1021\/cr00081a005","article-title":"Acetylcholinesterase: enzyme structure, reaction dynamics, and virtual transition states","volume":"87","author":"Quinn","year":"1987","journal-title":"Chem. Rev."},{"key":"10.1016\/j.cbi.2026.112224_bib24","unstructured":"RCSB PDB: Homepage, (n.d.). https:\/\/www.rcsb.org\/(accessed March 26, 2025)."},{"key":"10.1016\/j.cbi.2026.112224_bib25","doi-asserted-by":"crossref","first-page":"206","DOI":"10.1016\/j.crstbi.2021.08.003","article-title":"Room temperature crystallography of human acetylcholinesterase bound to a substrate analogue 4K-TMA: towards a neutron structure","volume":"3","author":"Gerlits","year":"2021","journal-title":"Curr. Res. Struct. Biol."},{"key":"10.1016\/j.cbi.2026.112224_bib26","doi-asserted-by":"crossref","first-page":"29256","DOI":"10.1074\/jbc.M603018200","article-title":"Substrate and product trafficking through the active center gorge of acetylcholinesterase analyzed by crystallography and equilibrium binding","volume":"281","author":"Bourne","year":"2006","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib27","doi-asserted-by":"crossref","first-page":"2746","DOI":"10.1038\/sj.emboj.7601175","article-title":"Structural insights into substrate traffic and inhibition in acetylcholinesterase","volume":"25","author":"Colletier","year":"2006","journal-title":"EMBO J."},{"key":"10.1016\/j.cbi.2026.112224_bib28","doi-asserted-by":"crossref","DOI":"10.1080\/14756366.2023.2270781","article-title":"Latest advances in dual inhibitors of acetylcholinesterase and monoamine oxidase B against Alzheimer's disease","volume":"38","author":"Zou","year":"2023","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib29","doi-asserted-by":"crossref","first-page":"1996","DOI":"10.1021\/acs.biochem.5c00024","article-title":"Protonation state insights into the influence of biocatalytic function for acetylcholinesterase mediated by neonicotinoids","volume":"64","author":"He","year":"2025","journal-title":"Biochemistry"},{"key":"10.1016\/j.cbi.2026.112224_bib30","doi-asserted-by":"crossref","DOI":"10.2174\/0929867324666170705123509","article-title":"Modulators of acetylcholinesterase activity: from alzheimer's disease to anti-cancer drugs","volume":"24","author":"Lazarevic-Pasti","year":"2017","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib31","doi-asserted-by":"crossref","first-page":"255","DOI":"10.2174\/1389557013406828","article-title":"Towards improved acetylcholinesterase inhibitors: a structural and computational approach","volume":"1","author":"Barril","year":"2001","journal-title":"Mini Rev. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib32","doi-asserted-by":"crossref","first-page":"9031","DOI":"10.1073\/pnas.90.19.9031","article-title":"Quaternary ligand binding to aromatic residues in the active-site gorge of acetylcholinesterase","volume":"90","author":"Harel","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.cbi.2026.112224_bib33","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0121092","article-title":"A wrench in the works of human acetylcholinesterase: soman induced conformational changes revealed by molecular dynamics simulations","volume":"10","author":"Bennion","year":"2015","journal-title":"PLoS One"},{"key":"10.1016\/j.cbi.2026.112224_bib34","article-title":"Binding interaction of acetylcholinesterase with steroidal pregnanes: insight from machine learning and atomistic simulation","author":"Ogunyemi","year":"2025","journal-title":"J. Biomol. Struct. Dyn."},{"key":"10.1016\/j.cbi.2026.112224_bib35","doi-asserted-by":"crossref","first-page":"1114","DOI":"10.1002\/pro.661","article-title":"Backdoor opening mechanism in acetylcholinesterase based on X-ray crystallography and molecular dynamics simulations","volume":"20","author":"Sanson","year":"2011","journal-title":"Protein Sci."},{"key":"10.1016\/j.cbi.2026.112224_bib36","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1007\/s00044-024-03278-0","article-title":"Synthesis, in vitro activity, and molecular docking of caffeic acid and resveratrol derivatives against Alzheimer's disease-related enzymes","volume":"33","author":"Mart\u00ednez","year":"2024","journal-title":"Med. Chem. Res."},{"key":"10.1016\/j.cbi.2026.112224_bib37","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.jmb.2016.12.004","article-title":"Arpeggio: a web server for calculating and visualising interatomic interactions in protein structures","volume":"429","author":"Jubb","year":"2017","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.cbi.2026.112224_bib38","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1038\/srep42717","article-title":"SwissADME: a free web tool to evaluate pharmacokinetics, drug-likeness and medicinal chemistry friendliness of small molecules","volume":"7","author":"Daina","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.cbi.2026.112224_bib39","doi-asserted-by":"crossref","first-page":"719","DOI":"10.2174\/1386207013330670","article-title":"BindingDB: a web-accessible molecular recognition database","volume":"4","author":"Chen","year":"2012","journal-title":"Comb. Chem. High Throughput Screen."},{"key":"10.1016\/j.cbi.2026.112224_bib40","doi-asserted-by":"crossref","first-page":"4111","DOI":"10.1021\/jm048957q","article-title":"The PDBbind database: methodologies and updates","volume":"48","author":"Wang","year":"2005","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib42","doi-asserted-by":"crossref","first-page":"1096","DOI":"10.1002\/pro.2923","article-title":"The impact of crystallization conditions on structure-based drug design: a case study on the methylene blue\/acetylcholinesterase complex","volume":"25","author":"Dym","year":"2016","journal-title":"Protein Sci."},{"key":"10.1016\/j.cbi.2026.112224_bib41","doi-asserted-by":"crossref","first-page":"2963","DOI":"10.1074\/jbc.274.5.2963","article-title":"Crystal structure of mouse acetylcholinesterase: a peripheral site- occluding loop in a tetrameric assembly","volume":"274","author":"Bourne","year":"1999","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib62","doi-asserted-by":"crossref","first-page":"18292","DOI":"10.1021\/ja106820e","article-title":"Conformational remodeling of femtomolar inhibitor-acetylcholinesterase complexes in the crystalline state","volume":"132","author":"Bourne","year":"2010","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2026.112224_bib43","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1038\/nsb0197-57","article-title":"Structure of acetylcholinesterase complexed with the nootropic alkaloid, (-)-huperzine A","volume":"4","author":"Raves","year":"1997","journal-title":"Nat. Struct. Biol."},{"key":"10.1016\/j.cbi.2026.112224_bib45","doi-asserted-by":"crossref","first-page":"10282","DOI":"10.1021\/jm300871x","article-title":"Structures of human acetylcholinesterase in complex with pharmacologically important ligands","volume":"55","author":"Cheung","year":"2012","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib44","doi-asserted-by":"crossref","first-page":"10810","DOI":"10.1021\/bi020151+","article-title":"X-ray structures of Torpedo californica acetylcholinesterase complexed with (+)-Huperzine A and (\u2212)-Huperzine B: structural evidence for an active site rearrangement, | biochemistry","volume":"41","author":"H Dvir","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.cbi.2026.112224_bib46","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1002\/1097-0134(20010201)42:2<182::AID-PROT50>3.0.CO;2-1","article-title":"Three-dimensional structure of a complex of galanthamine (Nivalin\u00ae) with acetylcholinesterase from Torpedo californica: implications for the design of new anti-alzheimer drugs","volume":"42","author":"Bartolucci","year":"2001","journal-title":"Proteins Struct. Funct. Genet."},{"key":"10.1016\/j.cbi.2026.112224_bib48","doi-asserted-by":"crossref","first-page":"15405","DOI":"10.1021\/ja0466154","article-title":"The complex of a bivalent derivative of galanthamine with Torpedo acetylcholinesterase displays drastic deformation of the active-site gorge: implications for structure-based drug design","volume":"126","author":"Greenblatt","year":"2004","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2026.112224_bib47","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1016\/S0014-5793(99)01637-3","article-title":"Structure of acetylcholinesterase complexed with (-)-galanthamine at 2.3 \u00c5 resolution","volume":"463","author":"Greenblatt","year":"1999","journal-title":"FEBS Lett."},{"key":"10.1016\/j.cbi.2026.112224_bib49","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1021\/jm901296p","article-title":"Probing Torpedo californica acetylcholinesterase catalytic Gorge with two novel bis-functional galanthamine derivatives","volume":"53","author":"Bartolucci","year":"2010","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib50","doi-asserted-by":"crossref","first-page":"2970","DOI":"10.1021\/bi011652i","article-title":"3D structure of Torpedo californica acetylcholinesterase complexed with huprine X at 2.1 \u00c5 resolution: kinetic and molecular dynamic correlates","volume":"41","author":"Dvir","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.cbi.2026.112224_bib52","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1042\/BJ20130013","article-title":"Crystal structures of human cholinesterases in complex with huprine W and tacrine: elements of specificity for anti-alzheimer\u2019s drugs targeting acetyl- and butyryl-cholinesterase","volume":"453","author":"Nachon","year":"2013","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2026.112224_bib53","doi-asserted-by":"crossref","DOI":"10.3390\/molecules23030634","article-title":"Increasing polarity in tacrine and huprine derivatives: potent anticholinesterase agents for the treatment of myasthenia gravis","volume":"23","author":"Galdeano","year":"2018","journal-title":"Molecules"},{"key":"10.1016\/j.cbi.2026.112224_bib54","doi-asserted-by":"crossref","first-page":"812","DOI":"10.1021\/acs.jmedchem.0c01775","article-title":"Discovery of a potent dual inhibitor of acetylcholinesterase and butyrylcholinesterase with antioxidant activity that alleviates alzheimer-like pathology in old APP\/PS1 mice","volume":"64","author":"Viayna","year":"2021","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib51","doi-asserted-by":"crossref","first-page":"400","DOI":"10.1002\/cmdc.201100438","article-title":"Huprine derivatives as sub-nanomolar human acetylcholinesterase inhibitors: from rational design to validation by X-ray crystallography","volume":"7","author":"Ronco","year":"2012","journal-title":"ChemMedChem"},{"key":"10.1016\/j.cbi.2026.112224_bib55","doi-asserted-by":"crossref","first-page":"3203","DOI":"10.1021\/jm010826r","article-title":"A structure-based design approach to the development of novel, reversible AChE inhibitors","volume":"44","author":"Doucet-Personeni","year":"2001","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib57","doi-asserted-by":"crossref","first-page":"1874","DOI":"10.1124\/mol.104.009944","article-title":"The crystal structure of the complex of the anticancer prodrug 7-ethyl-10-[4-(1-piperidino)-1-piperidino]-carbonyloxycamptothecin (CPT-11) with Torpedo californica acetylcholinesterase provides a molecular explanation for its cholinergic action","volume":"67","author":"Harel","year":"2005","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.cbi.2026.112224_bib56","doi-asserted-by":"crossref","first-page":"363","DOI":"10.1021\/ja021111w","article-title":"Acetylcholinesterase complexed with bivalent ligands related to Huperzine A: experimental evidence for species-dependent protein-ligand complementarity","volume":"125","author":"Wong","year":"2003","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2026.112224_bib69","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1016\/j.ijbiomac.2022.05.009","article-title":"Crystal structure of human acetylcholinesterase in complex with tacrine: implications for drug discovery","volume":"210","author":"Dileep","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.cbi.2026.112224_bib68","doi-asserted-by":"crossref","DOI":"10.1016\/j.cbi.2019.06.011","article-title":"A new crystal form of human acetylcholinesterase for exploratory room-temperature crystallography studies","volume":"309","author":"Gerlits","year":"2019","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2026.112224_bib60","doi-asserted-by":"crossref","first-page":"5491","DOI":"10.1021\/jm060164b","article-title":"Complexes of Alkylene-linked tacrine dimers with Torpedo californica acetylcholinesterase: binding of bis(5)-tacrine produces a dramatic rearrangement in the active-site gorge","volume":"49","author":"Rydberg","year":"2006","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib64","doi-asserted-by":"crossref","first-page":"1611","DOI":"10.1021\/jacs.5b11384","article-title":"Steric and dynamic parameters influencing in situ cycloadditions to form triazole inhibitors with crystalline acetylcholinesterase","volume":"138","author":"Bourne","year":"2016","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2026.112224_bib66","doi-asserted-by":"crossref","first-page":"7630","DOI":"10.1021\/acs.jmedchem.8b00592","article-title":"Structure-based optimization of nonquaternary reactivators of acetylcholinesterase inhibited by organophosphorus nerve agents","volume":"61","author":"Santoni","year":"2018","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib61","doi-asserted-by":"crossref","first-page":"4526","DOI":"10.1021\/ja058683b","article-title":"Conformational flexibility in the peripheral site of Torpedo californica acetylcholinesterase revealed by the complex structure with a bifunctional inhibitor","volume":"128","author":"Colletier","year":"2006","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2026.112224_bib67","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.ejmech.2018.12.063","article-title":"Design, biological evaluation and X-ray crystallography of nanomolar multifunctional ligands targeting simultaneously acetylcholinesterase and glycogen synthase kinase-3","volume":"168","author":"Oukoloff","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib58","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.1073\/pnas.0308206100","article-title":"Freeze-frame inhibitor captures acetylcholinesterase in a unique conformation","volume":"101","author":"Bourne","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.cbi.2026.112224_bib59","doi-asserted-by":"crossref","first-page":"11029","DOI":"10.1021\/ja051765f","article-title":"Crystal packing mediates enantioselective ligand recognition at the peripheral site of acetylcholinesterase","volume":"127","author":"Haviv","year":"2005","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2026.112224_bib120","doi-asserted-by":"crossref","DOI":"10.1002\/pro.4977","article-title":"Disentangling the formation, mechanism, and evolvement of the covalent methanesulfonyl fluoride acetylcholinesterase adduct: insights into an aged-like inactive complex susceptible to reactivation by a combination of nucleophiles","volume":"33","author":"Stojan","year":"2024","journal-title":"Protein Sci."},{"key":"10.1016\/j.cbi.2026.112224_bib63","doi-asserted-by":"crossref","first-page":"114","DOI":"10.1021\/acs.jmedchem.5b01119","article-title":"Novel tacrine-benzofuran hybrids as potent multitarget-directed ligands for the treatment of alzheimers disease: design, synthesis, biological evaluation, and X-ray crystallography","volume":"59","author":"Zha","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib65","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1016\/j.ejmech.2019.02.021","article-title":"Novel tacrine-tryptophan hybrids: multi-target directed ligands as potential treatment for Alzheimer's disease","volume":"168","author":"Chalupova","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib121","doi-asserted-by":"crossref","first-page":"8576","DOI":"10.1021\/jm5010804","article-title":"Multitarget drug design strategy: Quinone-tacrine hybrids designed to block amyloid-\u03b2 aggregation and to exert anticholinesterase and antioxidant effects","volume":"57","author":"Nepovimova","year":"2014","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib73","doi-asserted-by":"crossref","first-page":"794","DOI":"10.1080\/14756366.2018.1458030","article-title":"Kinetic and structural studies on the interactions of Torpedo californica acetylcholinesterase with two donepezil-like rigid analogues","volume":"33","author":"Caliandro","year":"2018","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib70","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1016\/S0969-2126(99)80040-9","article-title":"Structure of acetylcholinesterase complexed with E2020 (Aricept\u03c1): implications for the design of new anti-alzheimer drugs","volume":"7","author":"Kryger","year":"1999","journal-title":"Structure"},{"key":"10.1016\/j.cbi.2026.112224_bib71","doi-asserted-by":"crossref","first-page":"9409","DOI":"10.1021\/acs.jmedchem.6b00967","article-title":"Discovery of selective inhibitors targeting acetylcholinesterase 1 from disease-transmitting mosquitoes","volume":"59","author":"Engdahl","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib74","doi-asserted-by":"crossref","first-page":"10545","DOI":"10.1021\/acs.jmedchem.8b01060","article-title":"Noncovalent inhibitors of Mosquito acetylcholinesterase 1 with resistance-breaking potency","volume":"61","author":"Knutsson","year":"2018","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib72","doi-asserted-by":"crossref","first-page":"2672","DOI":"10.1002\/chem.201503973","article-title":"The nature of activated non-classical hydrogen bonds: a case study on acetylcholinesterase-ligand complexes","volume":"22","author":"Berg","year":"2016","journal-title":"Chem. Eur J."},{"key":"10.1016\/j.cbi.2026.112224_bib76","doi-asserted-by":"crossref","first-page":"1844","DOI":"10.1021\/acs.jmedchem.0c01863","article-title":"Kinetics-driven drug design strategy for next-generation acetylcholinesterase inhibitors to clinical candidate","volume":"64","author":"Zhou","year":"2021","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib75","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.ejmech.2018.10.064","article-title":"Novel multitarget-directed ligands targeting acetylcholinesterase and \u03c31 receptors as lead compounds for treatment of Alzheimer's disease: synthesis, evaluation, and structural characterization of their complexes with acetylcholinesterase","volume":"162","author":"Lalut","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib77","doi-asserted-by":"crossref","DOI":"10.1016\/j.cbi.2025.111649","article-title":"Kinetic and structural evidence for specific DMSO interference with reversible binding of uncharged bis-oximes to hAChE and their reactivation kinetics of OP-hAChE","volume":"419","author":"Koli\u0107","year":"2025","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2026.112224_bib81","doi-asserted-by":"crossref","first-page":"11742","DOI":"10.1073\/pnas.0804828105","article-title":"Shoot-and-trap: use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography","volume":"105","author":"Colletier","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.cbi.2026.112224_bib82","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0006851","article-title":"Selective and irreversible inhibitors of mosquito acetylcholinesterases for controlling malaria and other mosquito-borne diseases","volume":"4","author":"Pang","year":"2009","journal-title":"PLoS One"},{"key":"10.1016\/j.cbi.2026.112224_bib83","doi-asserted-by":"crossref","DOI":"10.1002\/cbic.202200456","article-title":"Grid-type Quaternary metallosupramolecular compounds inhibit human cholinesterases through dynamic multivalent interactions","volume":"23","author":"Nachon","year":"2022","journal-title":"Chembiochem"},{"key":"10.1016\/j.cbi.2026.112224_bib79","doi-asserted-by":"crossref","first-page":"1765","DOI":"10.1107\/S0907444902011642","article-title":"Structure of a complex of the potent and specific inhibitor BW284C51 with Torpedo californica acetylcholinesterase","volume":"58","author":"Felder","year":"2002","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.cbi.2026.112224_bib78","doi-asserted-by":"crossref","first-page":"2340","DOI":"10.1021\/ja952232h","article-title":"The X-ray structure of a transition state analog complex reveals the molecular origins of the catalytic power and substrate specificity of acetylcholinesterase","volume":"118","author":"Harel","year":"1996","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2026.112224_bib85","doi-asserted-by":"crossref","first-page":"282","DOI":"10.1038\/sj.clpt.6100151","article-title":"Novel nerve-agent antidote design based on crystallographic and mass spectrometric analyses of tabun-conjugated acetylcholinesterase in complex with antidotes","volume":"82","author":"Ekstr\u00f6m","year":"2007","journal-title":"Clin. Pharmacol. Ther."},{"key":"10.1016\/j.cbi.2026.112224_bib93","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1021\/acsmedchemlett.9b00021","article-title":"Synthesis and molecular properties of nerve agent reactivator HL\u00f6-7 dimethanesulfonate","volume":"10","author":"Hsu","year":"2019","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.cbi.2026.112224_bib90","doi-asserted-by":"crossref","first-page":"1246","DOI":"10.1002\/prot.25073","article-title":"Structures of paraoxon-inhibited human acetylcholinesterase reveal perturbations of the acyl loop and the dimer interface","volume":"84","author":"Franklin","year":"2016","journal-title":"Proteins: Struct., Funct., Bioinf."},{"key":"10.1016\/j.cbi.2026.112224_bib92","doi-asserted-by":"crossref","first-page":"1405","DOI":"10.1021\/acs.chemrestox.8b00294","article-title":"Structural insights of stereospecific inhibition of human acetylcholinesterase by VX and subsequent reactivation by HI-6","volume":"31","author":"Bester","year":"2018","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2026.112224_bib95","doi-asserted-by":"crossref","first-page":"804","DOI":"10.1021\/acs.chemrestox.0c00406","article-title":"Structural and biochemical insights into the inhibition of human acetylcholinesterase by G-Series nerve agents and subsequent reactivation by HI-6","volume":"34","author":"McGuire","year":"2021","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2026.112224_bib84","doi-asserted-by":"crossref","first-page":"597","DOI":"10.1016\/j.bcp.2006.05.027","article-title":"Crystal structures of acetylcholinesterase in complex with HI-6, Ortho-7 and obidoxime: structural basis for differences in the ability to reactivate tabun conjugates","volume":"72","author":"Ekstr\u00f6m","year":"2006","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.cbi.2026.112224_bib91","doi-asserted-by":"crossref","first-page":"5514","DOI":"10.1073\/pnas.1523362113","article-title":"Structure of a prereaction complex between the nerve agent sarin, its biological target acetylcholinesterase, and the antidote HI-6","volume":"113","author":"Allgardsson","year":"2016","journal-title":"Proc. Natl. Acad. Sci. U. S. A"},{"key":"10.1016\/j.cbi.2026.112224_bib86","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0005957","article-title":"Structure of HI-6-sarin-acetylcholinesterase determined by x-ray crystallography and molecular dynamics simulation: reactivator mechanism and design","volume":"4","author":"Ekstr\u00f6m","year":"2009","journal-title":"PLoS One"},{"key":"10.1016\/j.cbi.2026.112224_bib87","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1016\/j.bcp.2009.08.027","article-title":"Crystal structures of oxime-bound fenamiphos-acetylcholinesterases: reactivation involving flipping of the His447 ring to form a reactive Glu334-His447-oxime triad","volume":"79","author":"H\u00f6rnberg","year":"2010","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.cbi.2026.112224_bib88","doi-asserted-by":"crossref","first-page":"1389","DOI":"10.1016\/j.bcp.2013.01.016","article-title":"Catalytic-site conformational equilibrium in nerve-agent adducts of acetylcholinesterase: possible implications for the HI-6 antidote substrate specificity","volume":"85","author":"Artursson","year":"2013","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.cbi.2026.112224_bib97","doi-asserted-by":"crossref","first-page":"1538","DOI":"10.1016\/j.str.2022.09.006","article-title":"Structural and dynamic effects of paraoxon binding to human acetylcholinesterase by X-ray crystallography and inelastic neutron scattering","volume":"30","author":"Gerlits","year":"2022","journal-title":"Structure"},{"key":"10.1016\/j.cbi.2026.112224_bib89","doi-asserted-by":"crossref","first-page":"1788","DOI":"10.1107\/S1399004715011281","article-title":"A conformational change in the peripheral anionic site of Torpedo californica acetylcholinesterase induced by a bis-imidazolium oxime","volume":"71","author":"Legler","year":"2015","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.cbi.2026.112224_bib94","doi-asserted-by":"crossref","first-page":"10607","DOI":"10.1074\/jbc.RA119.008725","article-title":"Productive reorientation of a bound oxime reactivator revealed in room temperature X-ray structures of native and VX-inhibited human acetylcholinesterase","volume":"294","author":"Gerlits","year":"2019","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib96","doi-asserted-by":"crossref","DOI":"10.1002\/chem.202200678","article-title":"Broad-spectrum antidote discovery by untangling the reactivation mechanism of nerve-agent-inhibited acetylcholinesterase","volume":"28","author":"Lindgren","year":"2022","journal-title":"Chem. Eur J."},{"key":"10.1016\/j.cbi.2026.112224_bib98","doi-asserted-by":"crossref","first-page":"7593","DOI":"10.1021\/jm900433t","article-title":"Crystallographic snapshots of nonaged and aged conjugates of soman with acetylcholinesterase, and of a ternary complex of the aged conjugate with pralidoxime","volume":"52","author":"Sanson","year":"2009","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib99","doi-asserted-by":"crossref","first-page":"9675","DOI":"10.1002\/chem.201801394","article-title":"Potent 3-Hydroxy-2-Pyridine aldoxime reactivators of organophosphate-inhibited cholinesterases with predicted blood\u2013brain barrier penetration","volume":"24","author":"Zorbaz","year":"2018","journal-title":"Chem. Eur J."},{"key":"10.1016\/j.cbi.2026.112224_bib100","doi-asserted-by":"crossref","first-page":"7615","DOI":"10.1021\/jm400990p","article-title":"Divergent structure-activity relationships of structurally similar acetylcholinesterase inhibitors","volume":"56","author":"Andersson","year":"2013","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib101","doi-asserted-by":"crossref","first-page":"6529","DOI":"10.1021\/acs.jpcb.0c03778","article-title":"Physical mechanisms governing substituent effects on arene-arene interactions in a protein milieu","volume":"124","author":"Andersson","year":"2020","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.cbi.2026.112224_bib122","doi-asserted-by":"crossref","first-page":"1","DOI":"10.3390\/antiox10020329","article-title":"Fine\u2010tuning the biological profile of multitarget mitochondriotropic antioxidants for neurodegenerative diseases","volume":"10","author":"Chavarria","year":"2021","journal-title":"Antioxidants"},{"key":"10.1016\/j.cbi.2026.112224_bib112","doi-asserted-by":"crossref","first-page":"2205","DOI":"10.1002\/cbic.201500348","article-title":"Discovery of new classes of compounds that reactivate acetylcholinesterase inhibited by organophosphates","volume":"16","author":"Katz","year":"2015","journal-title":"Chembiochem"},{"key":"10.1016\/j.cbi.2026.112224_bib102","doi-asserted-by":"crossref","first-page":"5714","DOI":"10.1021\/bi982723p","article-title":"\u20191OCE","volume":"38","author":"Bartolucci","year":"1999","journal-title":"Biochemistry"},{"key":"10.1016\/j.cbi.2026.112224_bib106","doi-asserted-by":"crossref","first-page":"7856","DOI":"10.1021\/ja7109822","article-title":"Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site","volume":"130","author":"Harel","year":"2008","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2026.112224_bib103","doi-asserted-by":"crossref","first-page":"3555","DOI":"10.1021\/bi020016x","article-title":"Kinetic and structural studies on the interaction of cholinesterases with the anti-alzheimer drug rivastigmine","volume":"41","author":"Bar-On","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.cbi.2026.112224_bib109","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1042\/BJ20111675","article-title":"Kinetics of Torpedo californica acetylcholinesterase inhibition by bisnorcymserine and crystal structure of the complex with its leaving group","volume":"444","author":"Bartolucci","year":"2012","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2026.112224_bib111","doi-asserted-by":"crossref","first-page":"1091","DOI":"10.1021\/ml400304w","article-title":"Structures of human acetylcholinesterase bound to dihydrotanshinone i and territrem B show peripheral site flexibility","volume":"4","author":"Cheung","year":"2013","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.cbi.2026.112224_bib114","doi-asserted-by":"crossref","DOI":"10.3390\/molecules22091433","article-title":"An unusual dimeric inhibitor of acetylcholinesterase: cooperative binding of crystal violet","volume":"22","author":"Allgardsson","year":"2017","journal-title":"Molecules"},{"key":"10.1016\/j.cbi.2026.112224_bib105","doi-asserted-by":"crossref","first-page":"5051","DOI":"10.1021\/jm060293s","article-title":"Structural determinants of Torpedo californica acetylcholinesterase inhibition by the novel and orally active carbamate based anti-alzheimer drug ganstigmine (CHF-2819)","volume":"49","author":"Bartolucci","year":"2006","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib108","doi-asserted-by":"crossref","first-page":"2543","DOI":"10.1021\/jm801657v","article-title":"The crystal structure of a complex of acetylcholinesterase with a bis-(-)-nor-meptazinol derivative reveals disruption of the catalytic triad","volume":"52","author":"Paz","year":"2009","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib119","doi-asserted-by":"crossref","first-page":"4649","DOI":"10.1021\/acs.jmedchem.1c01748","article-title":"A new class of Bi- and trifunctional sugar oximes as antidotes against organophosphorus poisoning","volume":"65","author":"Da Silva","year":"2022","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib123","doi-asserted-by":"crossref","DOI":"10.1021\/acsinfecdis.4c00531","article-title":"Enzyme dynamics determine the potency and selectivity of inhibitors targeting disease-transmitting mosquitoes","volume":"10","author":"Kumari","year":"2024","journal-title":"ACS Infect. Dis."},{"key":"10.1016\/j.cbi.2026.112224_bib124","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0026039","article-title":"Targeting acetylcholinesterase: identification of chemical leads by high throughput screening, structure determination and molecular modeling","volume":"6","author":"Berg","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.cbi.2026.112224_bib104","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1093\/emboj\/cdg005","article-title":"Structural insights into ligand interactions at the acetylcholinesterase peripheral anionic site","volume":"22","author":"Bourne","year":"2003","journal-title":"EMBO J."},{"key":"10.1016\/j.cbi.2026.112224_bib115","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1016\/j.neuropharm.2019.05.025","article-title":"New evidence for dual binding site inhibitors of acetylcholinesterase as improved drugs for treatment of Alzheimer's disease","volume":"155","author":"Zueva","year":"2019","journal-title":"Neuropharmacology"},{"key":"10.1016\/j.cbi.2026.112224_bib113","doi-asserted-by":"crossref","first-page":"1225","DOI":"10.1042\/BCJ20160084","article-title":"Slow-binding inhibition of acetylcholinesterase by an alkylammonium derivative of 6-methyluracil: mechanism and possible advantages for myasthenia gravis treatment","volume":"473","author":"Kharlamova","year":"2016","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2026.112224_bib116","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1021\/acsmedchemlett.9b00656","article-title":"Chiral separation, X-ray structure, and biological evaluation of a potent and reversible dual binding site ache inhibitor","volume":"11","author":"Catto","year":"2020","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.cbi.2026.112224_bib118","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1021\/acsmedchemlett.2c00001","article-title":"Dual reversible coumarin inhibitors mutually bound to monoamine oxidase B and acetylcholinesterase crystal structures","volume":"13","author":"Ekstr\u00f6m","year":"2022","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.cbi.2026.112224_bib117","doi-asserted-by":"crossref","first-page":"4079","DOI":"10.1074\/jbc.RA119.012400","article-title":"Rational design, synthesis, and evaluation of uncharged, \u201csmart\u201d bis-oxime antidotes of organophosphate-inhibited human acetylcholinesterase","volume":"295","author":"Gorecki","year":"2020","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2026.112224_bib110","doi-asserted-by":"crossref","first-page":"12716","DOI":"10.1002\/anie.201205113","article-title":"Similar but different: thermodynamic and structural characterization of a pair of enantiomers binding to acetylcholinesterase","volume":"51","author":"Berg","year":"2012","journal-title":"Angew. Chem. Int. Ed."},{"key":"10.1016\/j.cbi.2026.112224_bib107","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1107\/S0907444907044472","article-title":"Use of a \u201ccaged\u201d analogue to study the traffic of choline within acetylcholinesterase by kinetic crystallography","volume":"63","author":"Colletier","year":"2007","journal-title":"Acta Crystallogr. Sect. D Biol. Crystallogr."},{"key":"10.1016\/j.cbi.2026.112224_bib80","doi-asserted-by":"crossref","first-page":"2746","DOI":"10.1038\/sj.emboj.7601175","article-title":"Structural insights into substrate traffic and inhibition in acetylcholinesterase","volume":"25","author":"Colletier","year":"2006","journal-title":"EMBO J."},{"key":"10.1016\/j.cbi.2026.112224_bib125","doi-asserted-by":"crossref","first-page":"2500","DOI":"10.1529\/biophysj.108.129601","article-title":"Flexibility of aromatic residues in the active-site gorge of acetylcholinesterase: X-ray versus molecular dynamics","volume":"95","author":"Xu","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.cbi.2026.112224_bib126","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/j.cbi.2005.10.018","article-title":"Structural insights into conformational flexibility at the peripheral site and within the active center gorge of AChE","volume":"157\u2013158","author":"Bourne","year":"2005","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2026.112224_bib127","doi-asserted-by":"crossref","first-page":"8797","DOI":"10.1021\/jp112030p","article-title":"Active site gating and substrate specificity of butyrylcholinesterase and acetylcholinesterase: insights from molecular dynamics simulations","volume":"115","author":"Fang","year":"2011","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.cbi.2026.112224_bib128","doi-asserted-by":"crossref","first-page":"872","DOI":"10.1126\/science.1678899","article-title":"Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein","volume":"253","author":"Sussman","year":"1991","journal-title":"Science"},{"key":"10.1016\/j.cbi.2026.112224_bib129","doi-asserted-by":"crossref","DOI":"10.1016\/j.neuropharm.2020.108236","article-title":"Slow-binding inhibitors of acetylcholinesterase of medical interest","volume":"177","author":"Lushchekina","year":"2020","journal-title":"Neuropharmacology"},{"key":"10.1016\/j.cbi.2026.112224_bib130","article-title":"Novel small molecule-based acetylcholinesterase (AChE) inhibitors: from biological perspective to recent developments","volume":"12","author":"Sobha","year":"2024","journal-title":"Eur. J. Med. Chem. Reports"},{"key":"10.1016\/j.cbi.2026.112224_bib131","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1021\/cn200100h","article-title":"Knowledge-based, central nervous system (CNS) lead selection and lead optimization for CNS drug discovery","volume":"3","author":"Ghose","year":"2011","journal-title":"ACS Chem. Neurosci."}],"container-title":["Chemico-Biological Interactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279726003327?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279726003327?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,8,7]],"date-time":"2026-08-07T12:57:29Z","timestamp":1786107449000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0009279726003327"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,9]]},"references-count":131,"alternative-id":["S0009279726003327"],"URL":"https:\/\/doi.org\/10.1016\/j.cbi.2026.112224","relation":{},"ISSN":["0009-2797"],"issn-type":[{"value":"0009-2797","type":"print"}],"subject":[],"published":{"date-parts":[[2026,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Interactions-guided blueprint of acetylcholinesterase binding: A review on structural and molecular determinants","name":"articletitle","label":"Article Title"},{"value":"Chemico-Biological Interactions","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbi.2026.112224","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 Elsevier B.V. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"112224"}}