{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,9,16]],"date-time":"2025-09-16T19:56:56Z","timestamp":1758052616098,"version":"3.44.0"},"reference-count":47,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2015,12,1]],"date-time":"2015-12-01T00:00:00Z","timestamp":1448928000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2015,12,1]],"date-time":"2015-12-01T00:00:00Z","timestamp":1448928000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2015,12,1]],"date-time":"2015-12-01T00:00:00Z","timestamp":1448928000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2015,12,1]],"date-time":"2015-12-01T00:00:00Z","timestamp":1448928000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2015,12,1]],"date-time":"2015-12-01T00:00:00Z","timestamp":1448928000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2015,12,1]],"date-time":"2015-12-01T00:00:00Z","timestamp":1448928000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2015,12,1]],"date-time":"2015-12-01T00:00:00Z","timestamp":1448928000000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"name":"Department of Atomic Energy-Board of Research in Nuclear Sciences","award":["1096\/2013"],"award-info":[{"award-number":["1096\/2013"]}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Chemico-Biological Interactions"],"published-print":{"date-parts":[[2015,12]]},"DOI":"10.1016\/j.cbi.2015.10.016","type":"journal-article","created":{"date-parts":[[2015,10,23]],"date-time":"2015-10-23T14:32:12Z","timestamp":1445610732000},"page":"299-306","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":5,"special_numbering":"C","title":["In silico studies on the role of mutant Y337A to reactivate tabun inhibited mAChE with K048"],"prefix":"10.1016","volume":"242","author":[{"given":"Nellore Bhanu","family":"Chandar","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Shibaji","family":"Ghosh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Rabindranath","family":"Lo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Semire","family":"Banjo","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Bishwajit","family":"Ganguly","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.cbi.2015.10.016_bib1a","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.2015.10.016_bib1b","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.2015.10.016_bib1c","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1002\/jat.2550140502","article-title":"Review of oximes available for treatment of nerve agent poisoning","volume":"14","author":"Dawson","year":"1994","journal-title":"J.\u00a0Appl. Toxicol."},{"key":"10.1016\/j.cbi.2015.10.016_bib2","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1021\/ar2002864","article-title":"Reactivators of acetylcholinesterase inhibited by organophosphorus nerve agents","volume":"45","author":"Mercey","year":"2012","journal-title":"Acc. Chem. Res."},{"key":"10.1016\/j.cbi.2015.10.016_bib3","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1111\/j.1742-7843.2007.00085.x","article-title":"Bisquaternary oximes as reactivators of tabun-inhibited human brain cholinesterases: an in\u00a0vitro study","volume":"101","author":"Kuca","year":"2007","journal-title":"Basic Clin. Pharmacol. Toxicol."},{"key":"10.1016\/j.cbi.2015.10.016_bib4","doi-asserted-by":"crossref","first-page":"579","DOI":"10.1016\/S0140-6736(08)60270-6","article-title":"Multiple-dose activated charcoal in acute self-poisoning: a randomised controlled trial","volume":"371","author":"Eddleston","year":"2008","journal-title":"Lancet"},{"key":"10.1016\/j.cbi.2015.10.016_bib5","doi-asserted-by":"crossref","first-page":"1194","DOI":"10.1038\/nm1013-1194","article-title":"Syrian gas attack reinforces need for better anti-sarin drugs","volume":"19","author":"Dolgin","year":"2013","journal-title":"Nat. Med."},{"key":"10.1016\/j.cbi.2015.10.016_bib6","doi-asserted-by":"crossref","first-page":"9","DOI":"10.2174\/157340710790711764","article-title":"Cholinesterase interactions with oximes","volume":"6","author":"Kovarik","year":"2010","journal-title":"Curr. Bioact. Compd."},{"key":"10.1016\/j.cbi.2015.10.016_bib7","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1016\/j.cbi.2012.08.024","article-title":"A\u00a0common mechanism for resistance to oxime reactivation of acetylcholinesterase inhibited by organophosphorus compounds","volume":"203","author":"Maxwell","year":"2013","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2015.10.016_bib8","doi-asserted-by":"crossref","first-page":"413","DOI":"10.1016\/j.cbi.2008.04.031","article-title":"New bispyridinium oximes: in\u00a0vitro and in\u00a0vivo evaluation of their biological efficiency in soman and tabun poisoning","volume":"175","author":"Berend","year":"2008","journal-title":"Chem.Biol. Interact."},{"key":"10.1016\/j.cbi.2015.10.016_bib9","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/j.tox.2006.08.012","article-title":"Pretreatment with pyridinium oximes improves antidotal therapy against tabun poisoning","volume":"228","author":"Vrdoljak","year":"2006","journal-title":"Toxicology"},{"key":"10.1016\/j.cbi.2015.10.016_bib10","doi-asserted-by":"crossref","first-page":"531","DOI":"10.3109\/14756360903357593","article-title":"In\u00a0vivo experimental approach to treatment against tabun poisoning","volume":"25","author":"Berend","year":"2010","journal-title":"J.\u00a0Enzyme Inhib. Med. Chem."},{"key":"10.1016\/j.cbi.2015.10.016_bib11","doi-asserted-by":"crossref","first-page":"355","DOI":"10.3233\/MGC-2010-0023","article-title":"Development of promising oximes against nerve agent and\/or pesticide intoxication","volume":"9","author":"Musilek","year":"2010","journal-title":"Main Group Chem."},{"key":"10.1016\/j.cbi.2015.10.016_bib12","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/0163-7258(93)90066-M","article-title":"Organophosphate poisoning","volume":"58","author":"Marrs","year":"1993","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.cbi.2015.10.016_bib13","doi-asserted-by":"crossref","first-page":"41141","DOI":"10.1074\/jbc.M210241200","article-title":"Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products","volume":"278","author":"Nicolet","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.cbi.2015.10.016_bib14","doi-asserted-by":"crossref","first-page":"215","DOI":"10.1016\/0014-5793(93)81714-B","article-title":"Engineering resistance to 'aging' of phosphylated human acetylcholinesterase. Role of hydrogen bond network in the active center","volume":"334","author":"Ordentlich","year":"1993","journal-title":"FEBS Lett."},{"key":"10.1016\/j.cbi.2015.10.016_bib15","doi-asserted-by":"crossref","first-page":"102","DOI":"10.31482\/mmsl.2013.015","article-title":"Modeling the binding of CWAs to AChE and BuChE","volume":"82","author":"Bennion","year":"2013","journal-title":"Mil. Med. Sci. Lett. (Voj.Zdrav.Listy)"},{"key":"10.1016\/j.cbi.2015.10.016_bib16","doi-asserted-by":"crossref","DOI":"10.1103\/PhysRevE.63.041902","article-title":"Statistical analysis of the fractal gating motions of the enzyme acetylcholinesterase","volume":"63","author":"Shen","year":"2001","journal-title":"Phys. Rev. E"},{"key":"10.1016\/j.cbi.2015.10.016_bib17","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.2015.10.016_bib18","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1016\/j.cbi.2012.08.019","article-title":"Centrally acting oximes in reactivation of tabun-phosphoramidated AChE","volume":"203","author":"Kovarik","year":"2013","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2015.10.016_bib19","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.cbi.2010.03.050","article-title":"Investigating the structural influence of surface mutations on acetylcholinesterase inhibition by organophosphorus compounds and oxime reactivation","volume":"187","author":"K\u00fc\u00e7\u00fckkilin\u00e7","year":"2010","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2015.10.016_bib20","doi-asserted-by":"crossref","first-page":"388","DOI":"10.1016\/j.cbi.2005.10.069","article-title":"Acetylcholinesterase mutants: oxime-assisted catalytic scavengers of organophosphonates","volume":"157\u2013158","author":"Kovarik","year":"2005","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2015.10.016_bib21","doi-asserted-by":"crossref","first-page":"29718","DOI":"10.1074\/jbc.M111.264739","article-title":"Oxime-assisted acetylcholinesterase catalytic scavengers of organophosphates that resist aging","volume":"286","author":"Cochran","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.cbi.2015.10.016_bib22","doi-asserted-by":"crossref","first-page":"1036","DOI":"10.1021\/acs.chemrestox.5b00060","article-title":"Catalytic soman scavenging by the Y337A\/F338A acetylcholinesterase mutant assisted with novel site-directed aldoximes","volume":"28","author":"Kovarik","year":"2015","journal-title":"Chem. Res. Toxicol."},{"key":"10.1016\/j.cbi.2015.10.016_bib23","doi-asserted-by":"crossref","first-page":"3222","DOI":"10.1021\/bi036191a","article-title":"Mutant cholinesterases possessing enhanced capacity for reactivation of their phosphonylated conjugates","volume":"43","author":"Kovarik","year":"2004","journal-title":"Biochemistry"},{"key":"10.1016\/j.cbi.2015.10.016_bib24","doi-asserted-by":"crossref","first-page":"209","DOI":"10.5562\/cca1815","article-title":"Reactivation of tabun-inhibited acetylcholinesterase investigated by two oximes and mutagenesis","volume":"85","author":"Katalini\u0107","year":"2012","journal-title":"Croat. Chem. Acta"},{"key":"10.1016\/j.cbi.2015.10.016_bib25","doi-asserted-by":"crossref","first-page":"4002","DOI":"10.1021\/jm901853b","article-title":"Structural evidence that human acetylcholinesterase inhibited by tabun ages through o-dealkylation","volume":"53","author":"Carletti","year":"2010","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.cbi.2015.10.016_bib26","doi-asserted-by":"crossref","first-page":"16011","DOI":"10.1021\/ja804941z","article-title":"Aging of cholinesterases phosphylated by tabun proceeds through o-dealkylation","volume":"130","author":"Carletti","year":"2008","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2015.10.016_bib27","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.2015.10.016_bib28","doi-asserted-by":"crossref","first-page":"546","DOI":"10.1080\/07391102.2012.687521","article-title":"First principles calculations of thermodynamics and kinetic parameters and molecular dynamics simulations of acetylcholinesterase reactivators: can mouse data provide new insights into humans?","volume":"30","author":"Matos","year":"2012","journal-title":"J.\u00a0Biomol. Struct. Dyn."},{"key":"10.1016\/j.cbi.2015.10.016_bib29","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1111\/bcpt.12158","article-title":"In\u00a0vivo evaluation of cholinesterase activity, oxidative stress markers, cyto- and genotoxicity of K048 oxime\u2013a promising antidote against organophosphate poisoning","volume":"114","author":"\u017dunec","year":"2014","journal-title":"Basic Clin. Pharmacol. Toxicol."},{"key":"10.1016\/j.cbi.2015.10.016_bib30","doi-asserted-by":"crossref","first-page":"754","DOI":"10.1016\/j.bmc.2010.12.021","article-title":"Mono-oxime bisquaternary acetylcholinesterase reactivators with prop-1,3-diyl linkage-Preparation, in\u00a0vitro screening and molecular docking","volume":"19","author":"Musilek","year":"2011","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.cbi.2015.10.016_bib31","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1002\/jcc.540110405","article-title":"Macromodel\u2014an integrated software system for modeling organic and bioorganic molecules using molecular mechanics","volume":"11","author":"Mohamadi","year":"1990","journal-title":"J.\u00a0Comput. Chem."},{"key":"10.1016\/j.cbi.2015.10.016_bib32","doi-asserted-by":"crossref","DOI":"10.1002\/0471250953.bi0506s15","article-title":"Comparative protein structure modeling using modeller","author":"Eswar","year":"2006","journal-title":"Curr. Protoc. Bioinforma."},{"year":"2007","series-title":"Autodock, Version 4.2 ed.","key":"10.1016\/j.cbi.2015.10.016_bib33"},{"key":"10.1016\/j.cbi.2015.10.016_bib34","unstructured":"GROMACS 4.6.3 program package, freely available from the GROMACS Web site."},{"key":"10.1016\/j.cbi.2015.10.016_bib35","doi-asserted-by":"crossref","first-page":"10089","DOI":"10.1063\/1.464397","article-title":"Particle mesh Ewald: an N-log (N) method for Ewald sums in large systems","volume":"98","author":"Darden","year":"1993","journal-title":"J.\u00a0Chem. Phys."},{"key":"10.1016\/j.cbi.2015.10.016_bib36","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1093\/protein\/8.2.127","article-title":"LIGPLOT: a program to generate schematic diagrams of protein-ligand interactions","volume":"8","author":"Wallace","year":"1995","journal-title":"Protein Eng."},{"key":"10.1016\/j.cbi.2015.10.016_bib37","doi-asserted-by":"crossref","first-page":"1253","DOI":"10.1016\/j.jmb.2008.06.065","article-title":"Force-based analysis of multidimensional energy landscapes: application of dynamics force spectroscopy and steered molecular dynamics simulations to an antibody fragment-peptide complex","volume":"381","author":"Morfill","year":"2008","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.cbi.2015.10.016_bib38","doi-asserted-by":"crossref","first-page":"6126","DOI":"10.1103\/PhysRevLett.84.6126","article-title":"Dynamic force spectroscopy of molecular adhesion bonds","volume":"84","author":"Heymann","year":"2000","journal-title":"Phys. Rev. Lett."},{"key":"10.1016\/j.cbi.2015.10.016_bib39","doi-asserted-by":"crossref","first-page":"1174","DOI":"10.1021\/ci050343m","article-title":"A\u00a0QXP-based multistep docking procedure for accurate prediction of protein\u2013ligand complexes","volume":"46","author":"Alisaraie","year":"2006","journal-title":"J.\u00a0Chem. Inf. Model"},{"key":"10.1016\/j.cbi.2015.10.016_bib40","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.cbi.2014.08.015","article-title":"Quantum chemical and steered molecular dynamics studies for one pot solution to reactivate aged acetylcholinesterase with alkylator oxime","volume":"223","author":"Chandar","year":"2014","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2015.10.016_bib41","doi-asserted-by":"crossref","first-page":"429","DOI":"10.1016\/j.copbio.2009.08.003","article-title":"Docking and chemoinformatic screens for new ligands and targets","volume":"20","author":"Kolb","year":"2009","journal-title":"Curr. Opin. Biotechnol."},{"key":"10.1016\/j.cbi.2015.10.016_bib42","doi-asserted-by":"crossref","first-page":"2368","DOI":"10.1039\/C4MB00083H","article-title":"Can hydroxylamine be a more potent nucleophile for the reactivation of tabun-inhibited AChE than prototype oxime drugs? An answer derived from quantum chemical and steered molecular dynamics studies","volume":"10","author":"Lo","year":"2014","journal-title":"Mol. Biosyst."},{"key":"10.1016\/j.cbi.2015.10.016_bib43","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1021\/bi051286t","article-title":"Structural changes of phenylalanine 338 and histidine 447 revealed by the crystal structures of tabun-inhibited murine acetylcholinesterase","volume":"45","author":"Ekstr\u00f6m","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.cbi.2015.10.016_bib44","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1038\/aps.2009.193","article-title":"Differential binding of bispyridinium oxime drugs with acetylcholinesterase","volume":"31","author":"Kesharwani","year":"2010","journal-title":"Acta Pharmacol. Sin."},{"key":"10.1016\/j.cbi.2015.10.016_bib45","doi-asserted-by":"crossref","first-page":"e1000801","DOI":"10.1371\/journal.pcbi.1000801","article-title":"Symmetric allosteric mechanism of hexameric escherichia coli arginine repressor exploits competition between L-Arginine ligands and resident arginine residues","volume":"6","author":"Strawn","year":"2010","journal-title":"PloS Comput. Biol."}],"container-title":["Chemico-Biological Interactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279715300946?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279715300946?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,14]],"date-time":"2025-09-14T13:38:57Z","timestamp":1757857137000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0009279715300946"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2015,12]]},"references-count":47,"alternative-id":["S0009279715300946"],"URL":"https:\/\/doi.org\/10.1016\/j.cbi.2015.10.016","relation":{},"ISSN":["0009-2797"],"issn-type":[{"type":"print","value":"0009-2797"}],"subject":[],"published":{"date-parts":[[2015,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"In silico studies on the role of mutant Y337A to reactivate tabun inhibited mAChE with K048","name":"articletitle","label":"Article Title"},{"value":"Chemico-Biological Interactions","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbi.2015.10.016","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2015 Elsevier Ireland Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}