{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,10,23]],"date-time":"2025-10-23T16:57:53Z","timestamp":1761238673846,"version":"3.44.0"},"reference-count":52,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2019,12,1]],"date-time":"2019-12-01T00:00:00Z","timestamp":1575158400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,12,1]],"date-time":"2019-12-01T00:00:00Z","timestamp":1575158400000},"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":[[2019,12]]},"DOI":"10.1016\/j.cbi.2019.108845","type":"journal-article","created":{"date-parts":[[2019,10,5]],"date-time":"2019-10-05T10:34:58Z","timestamp":1570271698000},"page":"108845","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":4,"special_numbering":"C","title":["The kinetics of inhibition of human acetylcholinesterase and butyrylcholinesterase by methylene violet 3RAX"],"prefix":"10.1016","volume":"314","author":[{"given":"Seda","family":"Onder","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kevser","family":"Biberoglu","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ozden","family":"Tacal","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"78","reference":[{"key":"10.1016\/j.cbi.2019.108845_bib1","doi-asserted-by":"crossref","first-page":"281","DOI":"10.1146\/annurev.pa.34.040194.001433","article-title":"The cholinesterases: from genes to proteins","volume":"34","author":"Taylor","year":"1994","journal-title":"Annu. Rev. Pharmacol. Toxicol."},{"key":"10.1016\/j.cbi.2019.108845_bib2","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1042\/bj2600625","article-title":"Comparison of butyrylcholinesterase and acetylcholinesterase","volume":"260","author":"Chatonnet","year":"1989","journal-title":"Biochem. J."},{"key":"10.1016\/j.cbi.2019.108845_bib3","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/0959-440X(92)90207-N","article-title":"Acetylcholinesterase: structure and use as a model for specific cation\u2014protein interactions","volume":"2","author":"Sussman","year":"1992","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.cbi.2019.108845_bib4","doi-asserted-by":"crossref","first-page":"1294","DOI":"10.2174\/1871527313666140917121132","article-title":"Cholinergic system dysfunction and neurodegenerative diseases: cause or effect?","volume":"13","author":"Tata","year":"2014","journal-title":"CNS Neurol. Disord. - Drug Targets"},{"key":"10.1016\/j.cbi.2019.108845_bib5","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."},{"key":"10.1016\/j.cbi.2019.108845_bib6","doi-asserted-by":"crossref","first-page":"101","DOI":"10.2174\/1570159X13666150716165726","article-title":"Alzheimer's disease: targeting the cholinergic system","volume":"14","author":"Ferreira-Vieira","year":"2016","journal-title":"Curr. Neuropharmacol."},{"key":"10.1016\/j.cbi.2019.108845_bib7","doi-asserted-by":"crossref","first-page":"1917","DOI":"10.1093\/brain\/awy132","article-title":"The cholinergic system in the pathophysiology and treatment of Alzheimer's disease","volume":"141","author":"Hampel","year":"2018","journal-title":"Brain"},{"key":"10.1016\/j.cbi.2019.108845_bib8","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1056\/NEJMra0909142","article-title":"Mechanisms of disease Alzheimer's disease","volume":"362","author":"Henry","year":"2010","journal-title":"N. Engl. J. Med."},{"key":"10.1016\/j.cbi.2019.108845_bib9","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1517\/14728222.11.2.161","article-title":"Targeting acetylcholinesterase to treat neurodegeneration","volume":"11","author":"Holzgrabe","year":"2007","journal-title":"Expert Opin. Ther. Targets"},{"key":"10.1016\/j.cbi.2019.108845_bib10","doi-asserted-by":"crossref","first-page":"S12","DOI":"10.1097\/01.wad.0000213804.59187.2d","article-title":"Mechanisms behind the neuroprotective actions of cholinesterase inhibitors in Alzheimer disease","volume":"20","author":"Nordberg","year":"2006","journal-title":"Alzheimers Dis. Assoc. Disord."},{"key":"10.1016\/j.cbi.2019.108845_bib11","first-page":"1479","article-title":"Cholinesterase inhibitors as Alzheimer's therapeutics","volume":"20","author":"Sharma","year":"2019","journal-title":"Mol. Med. Rep."},{"key":"10.1016\/j.cbi.2019.108845_bib12","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1097\/NEN.0b013e31823cc7a6","article-title":"Butyrylcholinesterase is associated with \u03b2-amyloid plaques in the transgenic APPSWE\/PSEN1dE9 mouse model of Alzheimer disease","volume":"71","author":"Darvesh","year":"2012","journal-title":"J. Neuropathol. Exp. Neurol."},{"key":"10.1016\/j.cbi.2019.108845_bib13","first-page":"909","article-title":"Butyrylcholinesterase in the life cycle of amyloid plaques","volume":"42","author":"Guillozet","year":"1997","journal-title":"Ann. Neurol. Off. J. Am. Neurol. Assoc. Child Neurol. Soc."},{"key":"10.1016\/j.cbi.2019.108845_bib14","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1016\/S0896-6273(00)80108-7","article-title":"Acetylcholinesterase accelerates assembly of amyloid-\u03b2-peptides into Alzheimer's fibrils: possible role of the peripheral site of the enzyme","volume":"16","author":"Inestrosa","year":"1996","journal-title":"Neuron"},{"key":"10.1016\/j.cbi.2019.108845_bib15","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1016\/0304-3940(94)12127-C","article-title":"Acetylcholinesterase, a senile plaque component, affects the fibrillogenesis of amyloid-\u03b2-peptides","volume":"201","author":"Alvarez","year":"1995","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.cbi.2019.108845_bib16","doi-asserted-by":"crossref","first-page":"1825","DOI":"10.2174\/092986710791111206","article-title":"Tacrine derivatives and Alzheimer's disease","volume":"17","author":"Tumiatti","year":"2010","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.cbi.2019.108845_bib17","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/S0011-393X(03)00059-6","article-title":"Cholinesterase inhibitors for the treatment of Alzheimer's disease:: getting on and staying on","volume":"64","author":"Grossberg","year":"2003","journal-title":"Curr. Ther. Res."},{"key":"10.1016\/j.cbi.2019.108845_bib18","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pmed.0040338","article-title":"Cholinesterase inhibitors in mild cognitive impairment: a systematic review of randomised trials","volume":"4","author":"Raschetti","year":"2007","journal-title":"PLoS Med."},{"key":"10.1016\/j.cbi.2019.108845_bib19","doi-asserted-by":"crossref","first-page":"852","DOI":"10.1021\/acschemneuro.8b00391","article-title":"Reconsideration of anticholinesterase therapeutic strategies against Alzheimer's disease","volume":"10","author":"Wang","year":"2018","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.cbi.2019.108845_bib20","first-page":"211","article-title":"Efficacy and safety of donepezil, galantamine, and rivastigmine for the treatment of Alzheimer's disease: a systematic review and meta-analysis","volume":"3","author":"Hansen","year":"2008","journal-title":"Clin. Interv. Aging"},{"key":"10.1016\/j.cbi.2019.108845_bib21","doi-asserted-by":"crossref","first-page":"472","DOI":"10.3389\/fnins.2019.00472","article-title":"Meta-analysis of randomized controlled trials on the efficacy and safety of donepezil, galantamine, rivastigmine, and memantine for the treatment of Alzheimer's disease","volume":"13","author":"Li","year":"2019","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.cbi.2019.108845_bib22","doi-asserted-by":"crossref","first-page":"364","DOI":"10.2174\/1570159X14666160119094820","article-title":"AChE inhibition-based multi-target-directed ligands, a novel pharmacological approach for the symptomatic and disease-modifying therapy of Alzheimer's disease","volume":"14","author":"Wang","year":"2016","journal-title":"Curr. Neuropharmacol."},{"key":"10.1016\/j.cbi.2019.108845_bib23","series-title":"The Biosynthesis of Phenazines","first-page":"1","author":"Blankenfeldt","year":"2013"},{"key":"10.1016\/j.cbi.2019.108845_bib24","first-page":"215","article-title":"Recherches sur la mati\u00e8re colorante des suppurations bleues: pyocyanine","volume":"51","author":"Fordos","year":"1860","journal-title":"C. R. Hebd. Seances Acad. Sci."},{"key":"10.1016\/j.cbi.2019.108845_bib25","doi-asserted-by":"crossref","first-page":"26","DOI":"10.1016\/j.sbi.2014.08.013","article-title":"The structural biology of phenazine biosynthesis","volume":"29","author":"Blankenfeldt","year":"2014","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.cbi.2019.108845_bib26","doi-asserted-by":"crossref","first-page":"1659","DOI":"10.1007\/s00253-010-2509-3","article-title":"Metabolism and function of phenazines in bacteria: impacts on the behavior of bacteria in the environment and biotechnological processes","volume":"86","author":"Pierson","year":"2010","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"10.1016\/j.cbi.2019.108845_bib27","first-page":"175","article-title":"Studies on antitumor activity of phenazine derivatives against S 180 in mice.(VII). On phenazinequinone derivatives, the science reports of the research institutes, Tohoku University. Ser. C, Medicine","volume":"14","author":"Endo","year":"1967","journal-title":"Tohoku Daigaku"},{"key":"10.1016\/j.cbi.2019.108845_bib28","doi-asserted-by":"crossref","first-page":"1145","DOI":"10.1016\/j.bmcl.2003.12.069","article-title":"Antimalarial activity of phenazines from lapachol, \u03b2-lapachone and its derivatives against Plasmodium falciparum in vitro and Plasmodium berghei in vivo","volume":"14","author":"de Andrade-Neto","year":"2004","journal-title":"Bioorg. Med. Chem. Lett"},{"key":"10.1016\/j.cbi.2019.108845_bib29","doi-asserted-by":"crossref","first-page":"3499","DOI":"10.1128\/jb.170.8.3499-3508.1988","article-title":"Role of a phenazine antibiotic from Pseudomonas fluorescens in biological control of Gaeumannomyces graminis var. tritici","volume":"170","author":"Thomashow","year":"1988","journal-title":"J. Bacteriol."},{"key":"10.1016\/j.cbi.2019.108845_bib30","doi-asserted-by":"crossref","first-page":"477","DOI":"10.7124\/bc.00013A","article-title":"Evaluation of antibacterial and antiviral activity of N-arylamides of 9-methyl and 9-methoxyphenazine-1-carboxylic acids\u2013inhibitors of the phage T7 model transctiption","volume":"28","author":"Hovorun","year":"2012","journal-title":"Biopolym. Cell"},{"key":"10.1016\/j.cbi.2019.108845_bib31","doi-asserted-by":"crossref","first-page":"1663","DOI":"10.1021\/cr020473j","article-title":"Phenazine natural products: biosynthesis, synthetic analogues, and biological activity","volume":"104","author":"Laursen","year":"2004","journal-title":"Chem. Rev."},{"key":"10.1016\/j.cbi.2019.108845_bib32","doi-asserted-by":"crossref","first-page":"1400","DOI":"10.1021\/np2009626","article-title":"Geranylphenazinediol, an acetylcholinesterase inhibitor produced by a Streptomyces species","volume":"75","author":"Ohlendorf","year":"2012","journal-title":"J. Nat. Prod."},{"key":"10.1016\/j.cbi.2019.108845_bib33","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1016\/j.abb.2011.04.007","article-title":"The role of Phe329 in binding of cationic triarylmethane dyes to human butyrylcholinesterase","volume":"511","author":"Biberoglu","year":"2011","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.cbi.2019.108845_bib34","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."},{"year":"1975","author":"Segel","series-title":"Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady State Enzyme Systems","key":"10.1016\/j.cbi.2019.108845_bib35"},{"key":"10.1016\/j.cbi.2019.108845_bib36","doi-asserted-by":"crossref","first-page":"4472","DOI":"10.1039\/C7RA13176C","article-title":"Methylene violet 3RAX-conjugated porphyrin for photodynamic therapy: synthesis, DNA photocleavage, and cell study","volume":"8","author":"Yao","year":"2018","journal-title":"RSC Adv."},{"key":"10.1016\/j.cbi.2019.108845_bib37","doi-asserted-by":"crossref","DOI":"10.4161\/cib.23570","article-title":"Phenazine production enhances extracellular DNA release via hydrogen peroxide generation in Pseudomonas aeruginosa","volume":"6","author":"Das","year":"2013","journal-title":"Commun. Integr. Biol."},{"year":"2013","author":"Neuwelt","series-title":"Implications of the Blood-Brain Barrier and its Manipulation: Volume 1 Basic Science Aspects","key":"10.1016\/j.cbi.2019.108845_bib38"},{"key":"10.1016\/j.cbi.2019.108845_bib39","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1002\/med.20177","article-title":"Cellular and molecular actions of methylene blue in the nervous system","volume":"31","author":"Oz","year":"2011","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.cbi.2019.108845_bib40","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1055\/s-0028-1139684","article-title":"Ueber die Methylenblaureaction der lebenden Nervensubstanz","volume":"12","author":"Ehrlich","year":"1886","journal-title":"Dtsch. Med. Wochenschr."},{"key":"10.1016\/j.cbi.2019.108845_bib41","doi-asserted-by":"crossref","first-page":"927","DOI":"10.1016\/j.bcp.2009.04.034","article-title":"Methylene blue and Alzheimer's disease","volume":"78","author":"Oz","year":"2009","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.cbi.2019.108845_bib42","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1016\/j.abb.2013.01.003","article-title":"Determination of binding points of methylene blue and cationic phenoxazine dyes on human butyrylcholinesterase","volume":"532","author":"Sezgin","year":"2013","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.cbi.2019.108845_bib43","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.abb.2008.07.006","article-title":"Comparative effects of cationic triarylmethane, phenoxazine and phenothiazine dyes on horse serum butyrylcholinesterase","volume":"478","author":"Y\u00fccel","year":"2008","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.cbi.2019.108845_bib44","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1016\/j.abb.2016.06.005","article-title":"Toluidine blue O is a potent inhibitor of human cholinesterases","volume":"604","author":"Biberoglu","year":"2016","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.cbi.2019.108845_bib45","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.biochi.2017.04.012","article-title":"Effects of phenothiazine-structured compounds on APP processing in Alzheimer's disease cellular model","volume":"138","author":"Yuksel","year":"2017","journal-title":"Biochimie"},{"key":"10.1016\/j.cbi.2019.108845_bib46","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.biochi.2017.12.004","article-title":"Toluidine blue O modifies hippocampal amyloid pathology in a transgenic mouse model of Alzheimer's disease","volume":"146","author":"Yuksel","year":"2018","journal-title":"Biochimie"},{"key":"10.1016\/j.cbi.2019.108845_bib47","doi-asserted-by":"crossref","first-page":"98","DOI":"10.3109\/14756366.2014.889127","article-title":"Discovery of butyrylcholinesterase inhibitors among derivatives of azaphenothiazines","volume":"30","author":"Lodarski","year":"2015","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.cbi.2019.108845_bib48","doi-asserted-by":"crossref","first-page":"488","DOI":"10.1016\/j.taap.2013.10.014","article-title":"The interactions of azure B, a metabolite of methylene blue, with acetylcholinesterase and butyrylcholinesterase","volume":"274","author":"Petzer","year":"2014","journal-title":"Toxicol. Appl. Pharmacol."},{"key":"10.1016\/j.cbi.2019.108845_bib49","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1111\/j.1432-1033.1996.00036.x","article-title":"Asp70 in the peripheral anionic site of human butyrylcholinesterase","volume":"235","author":"Masson","year":"1996","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.cbi.2019.108845_bib50","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1006\/abbi.2000.2188","article-title":"Inhibition effects of benactyzine and drofenine on human serum butyrylcholinesterase","volume":"386","author":"Bodur","year":"2001","journal-title":"Arch. Biochem. Biophys."},{"key":"10.1016\/j.cbi.2019.108845_bib51","doi-asserted-by":"crossref","first-page":"561","DOI":"10.1016\/S0006-2952(00)00330-0","article-title":"Kinetics of human acetylcholinesterase inhibition by the novel experimental Alzheimer therapeutic agent, tolserine","volume":"60","author":"Kamal","year":"2000","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.cbi.2019.108845_bib52","doi-asserted-by":"crossref","first-page":"14642","DOI":"10.1021\/bi971425+","article-title":"Differences in active site gorge dimensions of cholinesterases revealed by binding of inhibitors to human butyrylcholinesterase","volume":"36","author":"Saxena","year":"1997","journal-title":"Biochemistry"}],"container-title":["Chemico-Biological Interactions"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279719311354?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0009279719311354?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,14]],"date-time":"2025-09-14T13:55:36Z","timestamp":1757858136000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0009279719311354"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,12]]},"references-count":52,"alternative-id":["S0009279719311354"],"URL":"https:\/\/doi.org\/10.1016\/j.cbi.2019.108845","relation":{},"ISSN":["0009-2797"],"issn-type":[{"type":"print","value":"0009-2797"}],"subject":[],"published":{"date-parts":[[2019,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The kinetics of inhibition of human acetylcholinesterase and butyrylcholinesterase by methylene violet 3RAX","name":"articletitle","label":"Article Title"},{"value":"Chemico-Biological Interactions","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.cbi.2019.108845","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 Elsevier B.V. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"108845"}}