{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,3]],"date-time":"2026-08-03T10:36:18Z","timestamp":1785753378847,"version":"3.56.0"},"reference-count":38,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2006,8,1]],"date-time":"2006-08-01T00:00:00Z","timestamp":1154390400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2006,8,1]],"date-time":"2006-08-01T00:00:00Z","timestamp":1154390400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Chemico-Biological Interactions"],"published-print":{"date-parts":[[2006,8]]},"DOI":"10.1016\/j.cbi.2006.06.002","type":"journal-article","created":{"date-parts":[[2006,6,18]],"date-time":"2006-06-18T07:21:00Z","timestamp":1150615260000},"page":"165-171","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":54,"title":["Inhibition of two different cholinesterases by tacrine"],"prefix":"10.1016","volume":"162","author":[{"given":"Mushtaq","family":"Ahmed","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jo\u00e3o Batista T.","family":"Rocha","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ma\u00edsa","family":"Corr\u00eaa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Cinthia M.","family":"Mazzanti","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rafael F.","family":"Zanin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Andr\u00e9 L.B.","family":"Morsch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Vera Maria","family":"Morsch","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria R.C.","family":"Schetinger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.cbi.2006.06.002_bib1","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1006\/taap.1996.0003","article-title":"Modification of acetylcholinesterase during adaptation to chronic, subacute paraoxon application in rat","volume":"136","author":"Milatovic","year":"1996","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"10.1016\/j.cbi.2006.06.002_bib2","doi-asserted-by":"crossref","first-page":"949","DOI":"10.1023\/A:1007500424392","article-title":"New benzodiazepines alter acetylcholinesterase and ATPase activities","volume":"25","author":"Schetinger","year":"2000","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.cbi.2006.06.002_bib3","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/0301-0082(93)90040-Y","article-title":"Molecular and cellular biology of cholinesterases","volume":"41","author":"Massouli\u00e9","year":"1993","journal-title":"Prog. Neurobiol."},{"key":"10.1016\/j.cbi.2006.06.002_bib4","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1016\/j.coph.2005.01.014","article-title":"Acetylcholinesterase: \u2018classical\u2019 and \u2018non-classical\u2019 functions and pharmacology","volume":"5","author":"Silman","year":"2005","journal-title":"Curr. Opin. Pharmacol."},{"key":"10.1016\/j.cbi.2006.06.002_bib5","doi-asserted-by":"crossref","first-page":"100","DOI":"10.1515\/znc-2000-1-219","article-title":"Tissue cholinesterases. A comparative study of their kinetic properties","volume":"55","author":"Dave","year":"2000","journal-title":"Z. Naturforsch."},{"key":"10.1016\/j.cbi.2006.06.002_bib6","doi-asserted-by":"crossref","first-page":"3555","DOI":"10.1073\/pnas.84.11.3555","article-title":"Isolation and characterization of full length cDNA clones coding for cholinesterase from fetal human tissues","volume":"84","author":"Prody","year":"1987","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1016\/j.cbi.2006.06.002_bib7","first-page":"29","article-title":"Pseudocholinesterase of mammalian plasma: physiochemical properties and organophosphate inhibition in eleven species","volume":"24","author":"Ecobicon","year":"1973","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"10.1016\/j.cbi.2006.06.002_bib8","doi-asserted-by":"crossref","first-page":"1320","DOI":"10.1046\/j.1471-4159.2000.751320.x","article-title":"Abundant tissue butyrylcholinesterase and its possible function in the acetylcholinesterase knockout mouse","volume":"75","author":"Li","year":"2000","journal-title":"J. Neurochem."},{"key":"10.1016\/j.cbi.2006.06.002_bib9","doi-asserted-by":"crossref","first-page":"1419","DOI":"10.1046\/j.1460-9568.2003.02867.x","article-title":"Respiratory survival mechanism in acetylcholinesterase knockout mouse","volume":"18","author":"Chatonnet","year":"2003","journal-title":"Eur. J. Neurosci."},{"issue":"2","key":"10.1016\/j.cbi.2006.06.002_bib10","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/0014-5793(89)81352-3","article-title":"Purification and partial amino acid sequence analysis of human erythrocyte acetylcholinesterase","volume":"247","author":"Chhaliani","year":"1989","journal-title":"FEBS. Lett."},{"key":"10.1016\/j.cbi.2006.06.002_bib11","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/0014-5793(96)00447-4","article-title":"Acetylcholinesterase from Bungarus venom: a monomeric species","volume":"387","author":"Cousin","year":"1996","journal-title":"FEBS. Lett."},{"key":"10.1016\/j.cbi.2006.06.002_bib12","first-page":"381","article-title":"Acetylcholinesterase from snake venom","volume":"191","author":"Cousin","year":"1997","journal-title":"C. R. Seances Soc. Biol. Fil."},{"key":"10.1016\/j.cbi.2006.06.002_bib13","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1580\/1080-6032(2004)015[0257:EBTCKB]2.0.CO;2","article-title":"Envenoming by the common krait (Bungarus caeruleus) and Asian cobra (Naja naja): clinical manifestations and their management in a rural setting","volume":"15","author":"Bawaskar","year":"2004","journal-title":"Wilderness Environ. Med."},{"key":"10.1016\/j.cbi.2006.06.002_bib14","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1016\/S0167-4838(97)00009-5","article-title":"Acetylcholinesterases from Elapidae snake venoms: biochemical, immunological and enzymatic characterization","volume":"23","author":"Frobert","year":"1997","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.cbi.2006.06.002_bib15","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1192\/bjp.160.1.36","article-title":"Tacrine in Alzhemer's disease. Time course of changes in cognitive function and practice effect","volume":"160","author":"Eagger","year":"1992","journal-title":"Br. J. Psychol."},{"key":"10.1016\/j.cbi.2006.06.002_bib16","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1002\/(SICI)1099-0461(1998)12:4<245::AID-JBT7>3.0.CO;2-L","article-title":"Sensitivity of bovine retinal acetylcholinesterase (E.C. 3.1.1.7) toward tacrine. Kinetic characterization","volume":"12","author":"Al-Jafari","year":"1998","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"10.1016\/j.cbi.2006.06.002_bib17","doi-asserted-by":"crossref","first-page":"412","DOI":"10.1016\/S0026-895X(25)08895-9","article-title":"Interaction of tetrahydroaminoacridine with acetylcholinesterase and butyrylcholinesterase","volume":"41","author":"Berman","year":"1992","journal-title":"Mol. Pharmacol."},{"issue":"2","key":"10.1016\/j.cbi.2006.06.002_bib18","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1016\/S0091-3057(97)00601-1","article-title":"Comparative studies of huperzine A, E2020, and tacrine on behavior and cholinesterase activity","volume":"60","author":"Cheng","year":"1998","journal-title":"Pharmacol. Biochem. Behav."},{"issue":"23","key":"10.1016\/j.cbi.2006.06.002_bib19","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1185\/03007990152673800","article-title":"A new therapeutic target in Alzheimer's disease treatment: attention to butyrylcholinesterase","volume":"3","author":"Greig","year":"2001","journal-title":"Curr. Med. Res. Opin."},{"key":"10.1016\/j.cbi.2006.06.002_bib20","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/0006-2952(61)90145-9","article-title":"A new and rapid colorimetric determination of acetylcholinesterase activity","volume":"7","author":"Ellman","year":"1961","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.cbi.2006.06.002_bib21","first-page":"431","article-title":"Effects of early under nutrition kinetic parameters of brain acetylcholinesterase from adult rats","volume":"53","author":"Rocha","year":"1993","journal-title":"Acta Neurobiol. Exp."},{"key":"10.1016\/j.cbi.2006.06.002_bib22","doi-asserted-by":"crossref","first-page":"248","DOI":"10.1016\/0003-2697(76)90527-3","article-title":"A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein dye binding","volume":"72","author":"Bradford","year":"1976","journal-title":"Anal. Biochem."},{"key":"10.1016\/j.cbi.2006.06.002_bib23","doi-asserted-by":"crossref","first-page":"658","DOI":"10.1021\/ja01318a036","article-title":"The determination of enzyme dissociation constants","volume":"56","author":"Lineweaver","year":"1934","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.cbi.2006.06.002_bib24","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1126\/science.116.3013.329","article-title":"On the evaluation of the constant Vm and constant Km enzyme reactions","volume":"116","author":"Hofstee","year":"1952","journal-title":"Science"},{"key":"10.1016\/j.cbi.2006.06.002_bib25","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1016\/S0021-9258(17)45254-9","article-title":"A comparison of estimates of Michaelis Menten kinetic constants from various linear transformations","volume":"240","author":"Dowd","year":"1965","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.cbi.2006.06.002_bib26","series-title":"Enzyme Kinetics","author":"Dixon","year":"1964"},{"key":"10.1016\/j.cbi.2006.06.002_bib27","doi-asserted-by":"crossref","first-page":"181","DOI":"10.1016\/j.cbi.2005.10.027","article-title":"Interaction between the peripheral site and the acylation site in acetylcholinesterase","volume":"157\/158","author":"Rosenberry","year":"2005","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.cbi.2006.06.002_bib28","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/S0300-483X(00)00177-3","article-title":"Kinetic analysis of the toxicology effect of tacrine (Cognex) on human retinal acetylcholinesterase activity","volume":"147","author":"Alhomida","year":"2000","journal-title":"Toxicology"},{"key":"10.1016\/j.cbi.2006.06.002_bib29","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1089\/jop.1996.12.503","article-title":"The nature of the inhibition of camel retina acetylcholinesterase (E.C. 3.1.1.7) activity by tetrahydroacridine","volume":"12","author":"Al-Jafari","year":"1996","journal-title":"J. Ocul. Pharmacol. Ther."},{"issue":"47","key":"10.1016\/j.cbi.2006.06.002_bib30","doi-asserted-by":"crossref","first-page":"17213","DOI":"10.1073\/pnas.0508575102","article-title":"Selective butyrylcholinesterase inhibition elevates brain acetylclholine, augments learning and lowers Alzheimer's \u03b2-amyloid peptide in rodent","volume":"102","author":"Greig","year":"2005","journal-title":"PNAS"},{"key":"10.1016\/j.cbi.2006.06.002_bib31","series-title":"Human Cholinesterase and Anti-cholinesterase","author":"Soreq","year":"1993"},{"issue":"4","key":"10.1016\/j.cbi.2006.06.002_bib32","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/S0306-4522(01)00613-3","article-title":"Acetylcholinesterase knockouts establish central cholinergic pathways and can use butyrylcholinesterase to hydrolyze acetylcholine","volume":"110","author":"Mesulam","year":"2002","journal-title":"Neuroscience"},{"issue":"3\/4","key":"10.1016\/j.cbi.2006.06.002_bib33","doi-asserted-by":"crossref","first-page":"515","DOI":"10.1023\/A:1022869222652","article-title":"Cholinesterases: new roles in brain function and in Alzheimer's disease","volume":"28","author":"Giacobini","year":"2003","journal-title":"Neurochem. Res."},{"issue":"3","key":"10.1016\/j.cbi.2006.06.002_bib34","doi-asserted-by":"crossref","first-page":"307","DOI":"10.2174\/1567205054367838","article-title":"Cholinesterases: roles in the brain during health and disease","volume":"2","author":"Ballard","year":"2005","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.cbi.2006.06.002_bib35","doi-asserted-by":"crossref","first-page":"308","DOI":"10.1016\/j.mehy.2004.02.031","article-title":"Brain cholinesterases: II. The molecular and cellular basis of Alzheimer's disease","volume":"63","author":"Shen","year":"2004","journal-title":"Med. Hypothesis"},{"key":"10.1016\/j.cbi.2006.06.002_bib36","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1017\/S1041610203008676","article-title":"Butyrylcholinesterase: an important new target in Alzheimer's disease therapy","volume":"14","author":"Greig","year":"2002","journal-title":"Int. Psychogeriatr."},{"key":"10.1016\/j.cbi.2006.06.002_bib37","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1038\/nrn1035","article-title":"Neurobiology of butyrylcholinesterase","volume":"4","author":"Darvesh","year":"2003","journal-title":"Nat. Rev. Neurosci."},{"key":"10.1016\/j.cbi.2006.06.002_bib38","doi-asserted-by":"crossref","first-page":"273","DOI":"10.1111\/j.1365-2990.1978.tb00545.x","article-title":"Changes in brain cholinesterases in senile dementia of Alzheimer type","volume":"4","author":"Perry","year":"1978","journal-title":"Neuropathol. Appl. Neurobiol."}],"container-title":["Chemico-Biological Interactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279706001463?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279706001463?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,14]],"date-time":"2025-09-14T13:12:33Z","timestamp":1757855553000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0009279706001463"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2006,8]]},"references-count":38,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2006,8]]}},"alternative-id":["S0009279706001463"],"URL":"https:\/\/doi.org\/10.1016\/j.cbi.2006.06.002","relation":{},"ISSN":["0009-2797"],"issn-type":[{"value":"0009-2797","type":"print"}],"subject":[],"published":{"date-parts":[[2006,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Inhibition of two different cholinesterases by tacrine","name":"articletitle","label":"Article Title"},{"value":"Chemico-Biological Interactions","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbi.2006.06.002","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2006 Elsevier Ireland Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}