{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,23]],"date-time":"2026-08-23T14:48:49Z","timestamp":1787496529943,"version":"build-2736575974"},"reference-count":56,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2020,7,1]],"date-time":"2020-07-01T00:00:00Z","timestamp":1593561600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,7,1]],"date-time":"2020-07-01T00:00:00Z","timestamp":1593561600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"}],"funder":[{"DOI":"10.13039\/501100000921","name":"European Cooperation in Science and Technology","doi-asserted-by":"publisher","award":["CA15135"],"award-info":[{"award-number":["CA15135"]}],"id":[{"id":"10.13039\/501100000921","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003407","name":"Ministero dell\u00e2\u0080\u0099Istruzione, dell\u00e2\u0080\u0099Universit\u00c3\u00a0 e della Ricerca","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003407","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100004271","name":"Sapienza Universit\u00c3\u00a0 di Roma","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004271","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100003407","name":"Ministero dell\u00e2\u0080\u0099Istruzione, dell\u00e2\u0080\u0099Universit\u00c3\u00a0 e della Ricerca","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100003407","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["European Journal of Medicinal Chemistry"],"published-print":{"date-parts":[[2020,7]]},"DOI":"10.1016\/j.ejmech.2020.112350","type":"journal-article","created":{"date-parts":[[2020,4,27]],"date-time":"2020-04-27T05:00:19Z","timestamp":1587963619000},"page":"112350","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":48,"special_numbering":"C","title":["New deferiprone derivatives as multi-functional cholinesterase inhibitors: design, synthesis and in\u00a0vitro evaluation"],"prefix":"10.1016","volume":"198","author":[{"given":"Martina","family":"Bortolami","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fabiana","family":"Pandolfi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniela","family":"De Vita","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Camilla","family":"Carafa","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Antonella","family":"Messore","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roberto","family":"Di Santo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marta","family":"Feroci","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Roberta","family":"Costi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Isabella","family":"Chiarotto","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Donatella","family":"Bagetta","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefano","family":"Alcaro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marisa","family":"Colone","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Annarita","family":"Stringaro","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Luigi","family":"Scipione","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2020.112350_bib1","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1159\/000464422","article-title":"Molecular pathogenesis of Alzheimer\u2019s disease: an update","volume":"24","author":"Sanabria-Castro","year":"2017","journal-title":"Ann. Neurosci."},{"key":"10.1016\/j.ejmech.2020.112350_bib2","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.envres.2017.07.048","article-title":"Metals and neurodegenerative diseases. A systematic review","volume":"159","author":"Cicero","year":"2017","journal-title":"Environ. Res."},{"key":"10.1016\/j.ejmech.2020.112350_bib3","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/j.neuint.2012.08.014","article-title":"Metal dyshomeostasis and oxidative stress in Alzheimer\u2019s disease","volume":"62","author":"Bush","year":"2013","journal-title":"Neurochem. Int."},{"key":"10.1016\/j.ejmech.2020.112350_bib4","doi-asserted-by":"crossref","first-page":"1976","DOI":"10.1016\/j.bbamem.2007.02.002","article-title":"The redox chemistry of the Alzheimer\u2019s disease amyloid beta peptide","volume":"1768","author":"Smith","year":"2007","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.ejmech.2020.112350_bib5","doi-asserted-by":"crossref","first-page":"779","DOI":"10.3233\/JAD-180766","article-title":"Combinations for Alzheimer\u2019s disease: current and future pharmacotherapy options","volume":"67","author":"Cummings","year":"2019","journal-title":"J.\u00a0Alzheimers Dis."},{"issue":"19","key":"10.1016\/j.ejmech.2020.112350_bib6","doi-asserted-by":"crossref","first-page":"8167","DOI":"10.1021\/jm501195e","article-title":"Discovery, biological evaluation, and crystal structure of a novel nanomolar selective butyrylcholinesterase inhibitor","volume":"57","author":"Brus","year":"2014","journal-title":"J.\u00a0Med. Chem."},{"issue":"22","key":"10.1016\/j.ejmech.2020.112350_bib7","doi-asserted-by":"crossref","first-page":"10282","DOI":"10.1021\/jm300871x","article-title":"Height J.J. Structures of human acetylcholinesterase in complex with pharmacologically important ligands","volume":"55","author":"Cheung","year":"2012","journal-title":"J.\u00a0Med. Chem."},{"issue":"6","key":"10.1016\/j.ejmech.2020.112350_bib8","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1016\/S0197-4580(02)00230-0","article-title":"Acetylcholinesterase promotes beta-amyloid plaques in cerebral cortex","volume":"24","author":"Rees","year":"2003","journal-title":"Neurobiol. Aging"},{"issue":"3","key":"10.1016\/j.ejmech.2020.112350_bib9","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/S0006-2952(02)01514-9","article-title":"\u03b2-Amyloid aggregation induced by human acetylcholinesterase: inhibition studies","volume":"65","author":"Bartolini","year":"2003","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.ejmech.2020.112350_bib10","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1185\/03007990152673800","article-title":"A\u00a0new therapeutic target in Alzheimer\u2019s disease treatment: attention to butyrylcholinesterase","volume":"17","author":"Greig","year":"2001","journal-title":"Curr. Med. Res. Opin."},{"key":"10.1016\/j.ejmech.2020.112350_bib11","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","key":"10.1016\/j.ejmech.2020.112350_bib12","first-page":"367","article-title":"Alzheimer\u2019s disease facts and figures","volume":"14","year":"2018","journal-title":"Alzheimer\u2019s Dementia"},{"issue":"3","key":"10.1016\/j.ejmech.2020.112350_bib13","doi-asserted-by":"crossref","first-page":"347","DOI":"10.1021\/jm7009364","article-title":"Multi-target-directed ligands to combat neurodegenerative diseases","volume":"51","author":"Cavalli","year":"2008","journal-title":"J.\u00a0Med. Chem."},{"issue":"4","key":"10.1016\/j.ejmech.2020.112350_bib14","first-page":"239","article-title":"A\u00a0review on iron chelators in treatment of iron overload syndromes","volume":"10","author":"Mobarra","year":"2016","journal-title":"Int. J. Hematol. Oncol. Stem Cell Res."},{"issue":"5","key":"10.1016\/j.ejmech.2020.112350_bib15","doi-asserted-by":"crossref","first-page":"1070","DOI":"10.1093\/jac\/dkl350","article-title":"Deferiprone iron chelation as a novel therapy for experimental mucormycosis","volume":"58","author":"Ibrahim","year":"2006","journal-title":"J.\u00a0Antimicrob. Chemother."},{"issue":"9","key":"10.1016\/j.ejmech.2020.112350_bib16","doi-asserted-by":"crossref","first-page":"3436","DOI":"10.1182\/blood-2006-02-002394","article-title":"Oral chelators deferasirox and deferiprone for transfusional iron overload in thalassemia major: new data, new questions","volume":"107","author":"Neufeld","year":"2006","journal-title":"Blood"},{"issue":"1","key":"10.1016\/j.ejmech.2020.112350_bib17","doi-asserted-by":"crossref","first-page":"97","DOI":"10.2174\/0929867324666170330092304","article-title":"Hydroxypyridinone derivatives: a fascinating class of chelators with therapeutic applications - an update","volume":"25","author":"Chaves","year":"2018","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112350_bib18","doi-asserted-by":"crossref","first-page":"367","DOI":"10.1016\/j.ejmech.2019.07.031","article-title":"Design, synthesis and biological evaluation of hydroxypyridinone-coumarin hybrids as multimodal monoamine oxidase B inhibitors and iron chelates against Alzheimer\u2019s disease","volume":"180","author":"Zhang","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112350_bib19","doi-asserted-by":"crossref","first-page":"82","DOI":"10.1016\/j.jinorgbio.2017.11.015","article-title":"Hydroxypyridinone-benzofuran hybrids with potential protective roles for Alzheimer\u2019s disease therapy","volume":"179","author":"Hiremathad","year":"2018","journal-title":"J.\u00a0Inorg. Biochem."},{"issue":"1","key":"10.1016\/j.ejmech.2020.112350_bib20","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1021\/acschemneuro.5b00224","article-title":"Novel 1-Phenyl-3-hydroxy-4-pyridinone derivatives as multifunctional agents for the therapy of Alzheimer\u2019s disease","volume":"7","author":"Sheng","year":"2016","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.ejmech.2020.112350_bib21","doi-asserted-by":"crossref","first-page":"174","DOI":"10.1016\/j.ejmech.2016.12.045","article-title":"Synthesis and biological evaluation of deferiprone-resveratrol hybrids as antioxidants, A\u03b21-42 aggregation inhibitors and metal-chelating agents for Alzheimer\u2019s disease","volume":"127","author":"Xu","year":"2017","journal-title":"Eur. J. Med. Chem."},{"issue":"10","key":"10.1016\/j.ejmech.2020.112350_bib22","doi-asserted-by":"crossref","first-page":"1460","DOI":"10.1039\/c8mt00143j","article-title":"Tacrine-deferiprone hybrids as multi-target-directed metal chelators against Alzheimer\u2019s disease: a two-in-one drug","volume":"10","author":"Chand","year":"2018","journal-title":"Metall"},{"key":"10.1016\/j.ejmech.2020.112350_bib23","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.ejmech.2017.09.022","article-title":"New pyridine derivatives as inhibitors of acetylcholinesterase and amyloid aggregation","volume":"141","author":"Pandolfi","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112350_bib24","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1016\/j.ejmech.2015.12.024","article-title":"Cardanol-derived AChE inhibitors: towards the development of dual binding derivatives for Alzheimer\u2019s disease","volume":"108","author":"Lemes","year":"2016","journal-title":"Eur. J. Med. Chem."},{"issue":"20","key":"10.1016\/j.ejmech.2020.112350_bib25","doi-asserted-by":"crossref","first-page":"4882","DOI":"10.1021\/jm070559a","article-title":"Novel class of quinone-bearing polyamines as multi-target-directed ligands to combat Alzheimer\u2019s disease","volume":"50","author":"Bolognesi","year":"2007","journal-title":"J.\u00a0Med. Chem."},{"issue":"15","key":"10.1016\/j.ejmech.2020.112350_bib26","doi-asserted-by":"crossref","first-page":"4312","DOI":"10.1016\/j.bmcl.2009.05.087","article-title":"Structure-activity relationships of memoquin: influence of the chain chirality in the multi-target mechanism of action","volume":"19","author":"Bolognesi","year":"2009","journal-title":"Bioorg. Med. Chem. Lett"},{"issue":"27","key":"10.1016\/j.ejmech.2020.112350_bib27","doi-asserted-by":"crossref","first-page":"8742","DOI":"10.1021\/ja063063b","article-title":"Highly selective room-temperature copper-catalyzed C\u2212N coupling reactions","volume":"128","author":"Shafir","year":"2006","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2020.112350_bib28","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/0006-2952(61)90145-9","article-title":"A\u00a0new and rapid colorimetric determination of acetylcholinesterase activity","volume":"7","author":"Ellman","year":"1961","journal-title":"Biochem. Pharmacol."},{"issue":"1","key":"10.1016\/j.ejmech.2020.112350_bib29","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1042\/bj0550170","article-title":"The determination of enzyme inhibitor constants","volume":"55","author":"Dixon","year":"1953","journal-title":"Biochem. J."},{"issue":"17","key":"10.1016\/j.ejmech.2020.112350_bib30","doi-asserted-by":"crossref","first-page":"6058","DOI":"10.1039\/c3dt50406a","article-title":"Multifunctional iron-chelators with protective roles against neurodegenerative diseases","volume":"42","author":"Nunes","year":"2013","journal-title":"Dalton Trans."},{"issue":"6","key":"10.1016\/j.ejmech.2020.112350_bib31","doi-asserted-by":"crossref","first-page":"1624","DOI":"10.1016\/j.bmcl.2016.01.080","article-title":"In silico to in\u00a0vitro screening of hydroxypyridinones as acetylcholinesterase inhibitors","volume":"26","author":"Telpoukhovskaia","year":"2016","journal-title":"Bioorg. Med. Chem. Lett"},{"issue":"4","key":"10.1016\/j.ejmech.2020.112350_bib32","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1039\/c3mb25600f","article-title":"Exploring the multifunctionality of thioflavin- and deferiprone-based molecules as acetylcholinesterase inhibitors for potential application in Alzheimer\u2019s disease","volume":"9","author":"Telpoukhovskaia","year":"2013","journal-title":"Mol. Biosyst."},{"key":"10.1016\/j.ejmech.2020.112350_bib33","doi-asserted-by":"crossref","DOI":"10.1093\/nar\/gkp253","article-title":"IC50-to-Ki: a web-based tool for converting IC50 to Ki values for inhibitors of enzyme activity and ligand binding","volume":"37","author":"Cer","year":"2009","journal-title":"Nucleic Acids Res."},{"key":"10.1016\/j.ejmech.2020.112350_bib34","first-page":"113","article-title":"Formation and stability of inorganic complexes in solution","volume":"9","author":"Job","year":"1928","journal-title":"Ann. Chim."},{"issue":"1","key":"10.1016\/j.ejmech.2020.112350_bib35","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1093\/nar\/28.1.235","article-title":"The protein Data Bank","volume":"28","author":"Berman","year":"2000","journal-title":"Nucleic Acids Res."},{"issue":"1","key":"10.1016\/j.ejmech.2020.112350_bib36","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1021\/acs.jmedchem.7b01086","article-title":"The magic of crystal structure-based inhibitor optimization: development of a butyrylcholinesterase inhibitor with picomolar affinity and in\u00a0vivo activity","volume":"61","author":"Kosak","year":"2018","journal-title":"J.\u00a0Med. Chem."},{"issue":"43","key":"10.1016\/j.ejmech.2020.112350_bib37","doi-asserted-by":"crossref","first-page":"30370","DOI":"10.1074\/jbc.274.43.30370","article-title":"Conformational flexibility of the acetylcholinesterase tetramer suggested by x-ray crystallography","volume":"274","author":"Bourne","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"issue":"23\u201324","key":"10.1016\/j.ejmech.2020.112350_bib38","article-title":"Essential considerations for using protein-ligand structures in drug discovery","volume":"17","author":"Warren","year":"2012","journal-title":"Drug Discov. Today"},{"issue":"Pt 5","key":"10.1016\/j.ejmech.2020.112350_bib39","doi-asserted-by":"crossref","first-page":"792","DOI":"10.1107\/S0907444902003931","article-title":"Rearrangement of Cruickshank\u2019s formulae for the diffraction-component precision index","volume":"58","author":"Blow","year":"2002","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"issue":"1\u20133","key":"10.1016\/j.ejmech.2020.112350_bib40","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/0009-2797(93)90042-W","article-title":"Three-dimensional structure of acetylcholinesterase and its complexes with anticholinesterase drugs","volume":"87","author":"Sussman","year":"1993","journal-title":"Chem. Biol. Interact."},{"issue":"3","key":"10.1016\/j.ejmech.2020.112350_bib41","doi-asserted-by":"crossref","first-page":"758","DOI":"10.1006\/bbrc.1999.0705","article-title":"The adhesion function on acetylcholinesterase is located at the peripheral anionic site","volume":"258","author":"Johnson","year":"1999","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"3","key":"10.1016\/j.ejmech.2020.112350_bib42","doi-asserted-by":"crossref","first-page":"267","DOI":"10.2174\/1389557013406864","article-title":"Peripheral and dual binding site acetylcholinesterase inhibitors: implications in treatment of Alzheimer\u2019s disease","volume":"1","author":"Castro","year":"2001","journal-title":"Mini Rev. Med. Chem."},{"issue":"26","key":"10.1016\/j.ejmech.2020.112350_bib43","doi-asserted-by":"crossref","first-page":"7753","DOI":"10.1021\/bi000210o","article-title":"Acetylthiocholine binds to Asp74 at the peripheral site of human acetylcholinesterase as the first step in the catalytic pathway","volume":"39","author":"Mallender","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2020.112350_bib44","doi-asserted-by":"crossref","first-page":"42717","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."},{"issue":"1\u20133","key":"10.1016\/j.ejmech.2020.112350_bib45","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/S0169-409X(00)00129-0","article-title":"Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings","volume":"46","author":"Lipinski","year":"2001","journal-title":"Adv. Drug Deliv. Rev."},{"issue":"4","key":"10.1016\/j.ejmech.2020.112350_bib46","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1602\/neurorx.2.4.541","article-title":"Medicinal chemical properties of successful central nervous system drugs","volume":"2","author":"Pajouhesh","year":"2005","journal-title":"NeuroRx"},{"issue":"21","key":"10.1016\/j.ejmech.2020.112350_bib47","doi-asserted-by":"crossref","first-page":"9824","DOI":"10.1021\/acs.jmedchem.9b01220","article-title":"The blood-brain barrier (BBB) Score","volume":"62","author":"Gupta","year":"2019","journal-title":"J.\u00a0Med. Chem."},{"key":"10.1016\/j.ejmech.2020.112350_bib48","year":"2018"},{"issue":"45","key":"10.1016\/j.ejmech.2020.112350_bib49","doi-asserted-by":"crossref","first-page":"11225","DOI":"10.1021\/ja9621760","article-title":"Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids","volume":"118","author":"Jorgensen","year":"1996","journal-title":"J.\u00a0Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2020.112350_bib50","series-title":"Maestro","year":"2018"},{"issue":"2","key":"10.1016\/j.ejmech.2020.112350_bib51","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1016\/0898-5529(88)90015-2","article-title":"A\u00a0rapid approximation to the solvent accessible surface areas of atoms","volume":"1","author":"Hasel","year":"1988","journal-title":"Tetrahedon Comput. Methodol."},{"key":"10.1016\/j.ejmech.2020.112350_bib52","series-title":"Prime","year":"2018"},{"key":"10.1016\/j.ejmech.2020.112350_bib53","series-title":"Protein Preparation Wizard","year":"2018"},{"key":"10.1016\/j.ejmech.2020.112350_bib54","series-title":"Glide","year":"2018"},{"key":"10.1016\/j.ejmech.2020.112350_bib55","series-title":"Desmond Molecular Dynamics System","year":"2018"},{"key":"10.1016\/j.ejmech.2020.112350_bib56","series-title":"Epik","year":"2018"}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523420303202?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523420303202?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,10,1]],"date-time":"2025-10-01T14:09:35Z","timestamp":1759327775000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523420303202"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,7]]},"references-count":56,"alternative-id":["S0223523420303202"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2020.112350","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2020,7]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"New deferiprone derivatives as multi-functional cholinesterase inhibitors: design, synthesis and in\u00a0vitro evaluation","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2020.112350","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2020 Published by Elsevier Masson SAS.","name":"copyright","label":"Copyright"}],"article-number":"112350"}}