{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,9]],"date-time":"2026-10-09T17:54:35Z","timestamp":1791568475608,"version":"4.3.4"},"reference-count":256,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2024,9,1]],"date-time":"2024-09-01T00:00:00Z","timestamp":1725148800000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"funder":[{"DOI":"10.13039\/501100004608","name":"Natural Science Foundation of Jiangsu Province","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100004608","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["82173652"],"award-info":[{"award-number":["82173652"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["81830105"],"award-info":[{"award-number":["81830105"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["BK20221522"],"award-info":[{"award-number":["BK20221522"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["BK20191411"],"award-info":[{"award-number":["BK20191411"]}],"id":[{"id":"10.13039\/501100001809","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":[[2024,9]]},"DOI":"10.1016\/j.ejmech.2024.116569","type":"journal-article","created":{"date-parts":[[2024,6,5]],"date-time":"2024-06-05T08:39:59Z","timestamp":1717576799000},"page":"116569","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":55,"special_numbering":"C","title":["New insights into butyrylcholinesterase: Pharmaceutical applications, selective inhibitors and multitarget-directed ligands"],"prefix":"10.1016","volume":"275","author":[{"given":"Tianyu","family":"Sun","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tengfei","family":"Zhen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chrisanta Hamis","family":"Harakandi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lei","family":"Wang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Huanchao","family":"Guo","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yao","family":"Chen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5109-0304","authenticated-orcid":false,"given":"Haopeng","family":"Sun","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ejmech.2024.116569_bib1","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.ejmech.2024.116569_bib2","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.ejmech.2024.116569_bib3","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1038\/sj.bjp.0705010","article-title":"Butyrylcholinesterase and acetylcholinesterase activity and quantal transmitter release at normal and acetylcholinesterase knockout mouse neuromuscular junctions: cholinesterases at mouse neuromuscular junctions","volume":"138","author":"Minic","year":"2003","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.ejmech.2024.116569_bib4","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":"17","author":"Greig","year":"2001","journal-title":"Curr. Med. Res. Opin."},{"key":"10.1016\/j.ejmech.2024.116569_bib5","doi-asserted-by":"crossref","first-page":"165","DOI":"10.1038\/s41397-020-00192-7","article-title":"Characterization of four BCHE mutations associated with prolonged effect of suxamethonium","volume":"21","author":"Brazzolotto","year":"2021","journal-title":"Pharmacogenomics J."},{"key":"10.1016\/j.ejmech.2024.116569_bib6","doi-asserted-by":"crossref","first-page":"34","DOI":"10.1016\/j.pharmthera.2014.11.011","article-title":"Review of human butyrylcholinesterase structure, function, genetic variants, history of use in the clinic, and potential therapeutic uses","volume":"148","author":"Lockridge","year":"2015","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.ejmech.2024.116569_bib7","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1584\/jpestics.D17-078","article-title":"Enzymatic detoxification of organophosphorus pesticides and related toxicants","volume":"43","author":"Alejo-Gonz\u00e1lez","year":"2018","journal-title":"J. Pestic. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib8","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1016\/S0376-8716(97)00119-1","article-title":"Enhancing cocaine metabolism with butyrylcholinesterase as a treatment strategy","volume":"48","author":"Gorelick","year":"1997","journal-title":"Drug Alcohol Depend."},{"key":"10.1016\/j.ejmech.2024.116569_bib9","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1002\/med.21745","article-title":"Structure and therapeutic uses of butyrylcholinesterase: application in detoxification, Alzheimer's disease, and fat metabolism","volume":"41","author":"Xing","year":"2021","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.ejmech.2024.116569_bib10","doi-asserted-by":"crossref","first-page":"11365","DOI":"10.1021\/acs.jmedchem.2c00944","article-title":"N -benzyl benzamide derivatives as selective sub-nanomolar butyrylcholinesterase inhibitors for possible treatment in advanced Alzheimer's disease","volume":"65","author":"Du","year":"2022","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib11","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1111\/jnc.15833","article-title":"Butyrylcholinesterase in lipid metabolism: a new outlook","volume":"168","author":"Gok","year":"2024","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ejmech.2024.116569_bib12","doi-asserted-by":"crossref","first-page":"2251","DOI":"10.1073\/pnas.1421536112","article-title":"Plasma butyrylcholinesterase regulates ghrelin to control aggression","volume":"112","author":"Chen","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ejmech.2024.116569_bib13","doi-asserted-by":"crossref","first-page":"6542","DOI":"10.7150\/thno.54589","article-title":"Longitudinal evaluation of a novel BChE PET tracer as an early in vivo biomarker in the brain of a mouse model for Alzheimer disease","volume":"11","author":"Rejc","year":"2021","journal-title":"Theranostics"},{"key":"10.1016\/j.ejmech.2024.116569_bib14","doi-asserted-by":"crossref","DOI":"10.1155\/2022\/6051092","article-title":"BCHE as a prognostic biomarker in endometrial cancer and its correlation with immunity","volume":"2022","author":"Liu","year":"2022","journal-title":"J. Immunol. Res."},{"key":"10.1016\/j.ejmech.2024.116569_bib15","article-title":"Progressions of the correlation between lipid metabolism and immune infiltration characteristics in gastric cancer and identification of BCHE as a potential biomarker","volume":"15","author":"Wang","year":"2024","journal-title":"Front. Immunol."},{"key":"10.1016\/j.ejmech.2024.116569_bib16","doi-asserted-by":"crossref","DOI":"10.3389\/fneur.2022.900997","article-title":"The role of butyrylcholinesterase in the regulation of cognitive dysfunction in minimal hepatic encephalopathy: a potential blood marker of disease evolution","volume":"13","author":"Yang","year":"2022","journal-title":"Front. Neurol."},{"key":"10.1016\/j.ejmech.2024.116569_bib17","first-page":"726","article-title":"Butyrylcholinesterase as a biochemical marker, Bratisl","volume":"114","author":"Pohanka","year":"2013","journal-title":"Med. J."},{"key":"10.1016\/j.ejmech.2024.116569_bib18","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.biochi.2018.10.017","article-title":"3D structure of the natural tetrameric form of human butyrylcholinesterase as revealed by cryoEM, SAXS and MD","volume":"156","author":"Boyko","year":"2019","journal-title":"Biochimie"},{"key":"10.1016\/j.ejmech.2024.116569_bib19","doi-asserted-by":"crossref","first-page":"7046","DOI":"10.1021\/bi300955k","article-title":"Probing the peripheral site of human butyrylcholinesterase","volume":"51","author":"Macdonald","year":"2012","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2024.116569_bib20","doi-asserted-by":"crossref","first-page":"7529","DOI":"10.1021\/bi052176p","article-title":"A computational study of the deacylation mechanism of human butyrylcholinesterase","volume":"45","author":"Su\u00e1rez","year":"2006","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2024.116569_bib21","doi-asserted-by":"crossref","DOI":"10.1016\/j.bbapap.2021.140733","article-title":"Steady-state kinetic analysis of human cholinesterases over wide concentration ranges of competing substrates","volume":"1870","author":"Mukhametgalieva","year":"2022","journal-title":"Biochim. Biophys. Acta, Proteins Proteomics"},{"key":"10.1016\/j.ejmech.2024.116569_bib22","doi-asserted-by":"crossref","first-page":"7433","DOI":"10.1021\/bi010181x","article-title":"Does \u201cButyrylization\u201d of acetylcholinesterase through substitution of the six divergent aromatic amino acids in the active center gorge generate an enzyme mimic of butyrylcholinesterase?","volume":"40","author":"Kaplan","year":"2001","journal-title":"Biochemistry"},{"key":"10.1016\/j.ejmech.2024.116569_bib23","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"},{"key":"10.1016\/j.ejmech.2024.116569_bib24","first-page":"63","article-title":"Exploring the active sites of cholinesterases by inhibition with bambuterol and haloxon","volume":"76","author":"Kovarik","year":"2003","journal-title":"Croat. Chem. Acta"},{"key":"10.1016\/j.ejmech.2024.116569_bib25","doi-asserted-by":"crossref","first-page":"9116","DOI":"10.1021\/acs.jmedchem.9b01012","article-title":"Highly selective butyrylcholinesterase inhibitors with tunable duration of action by chemical modification of transferable carbamate units exhibit pronounced neuroprotective effect in an Alzheimer's disease mouse model","volume":"62","author":"Hoffmann","year":"2019","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib26","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.ejmech.2024.116569_bib27","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1042\/bj3270747","article-title":"Tetramerization domain of human butyrylcholinesterase is at the C-terminus","volume":"327","author":"Blong","year":"1997","journal-title":"Biochem. J."},{"key":"10.1016\/j.ejmech.2024.116569_bib28","doi-asserted-by":"crossref","first-page":"8324","DOI":"10.1016\/S0021-9258(19)86892-8","article-title":"Interchain disulfide bonds and subunit organization in human serum cholinesterase","volume":"254","author":"Lockridge","year":"1979","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib29","doi-asserted-by":"crossref","first-page":"1236","DOI":"10.1111\/jnc.15245","article-title":"Cryo\u2010electron microscopy of cholinesterases, present and future","volume":"158","author":"Leung","year":"2021","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ejmech.2024.116569_bib30","doi-asserted-by":"crossref","first-page":"6543","DOI":"10.1021\/jp8114995","article-title":"Model of human butyrylcholinesterase tetramer by homology modeling and dynamics simulation","volume":"113","author":"Pan","year":"2009","journal-title":"J. Phys. Chem. B"},{"key":"10.1016\/j.ejmech.2024.116569_bib31","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/j.cbi.2016.02.007","article-title":"Origin of polyproline-rich peptides in human butyrylcholinesterase tetramers","volume":"259","author":"Peng","year":"2016","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.ejmech.2024.116569_bib32","doi-asserted-by":"crossref","first-page":"3844","DOI":"10.1111\/j.1742-4658.2012.08744.x","article-title":"The proline-rich tetramerization peptides in equine serum butyrylcholinesterase","volume":"279","author":"Biberoglu","year":"2012","journal-title":"FEBS J."},{"key":"10.1016\/j.ejmech.2024.116569_bib33","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1042\/BJ20140421","article-title":"Polyproline promotes tetramerization of recombinant human butyrylcholinesterase","volume":"462","author":"Larson","year":"2014","journal-title":"Biochem. J."},{"key":"10.1016\/j.ejmech.2024.116569_bib34","doi-asserted-by":"crossref","first-page":"a033118","DOI":"10.1101\/cshperspect.a033118","article-title":"Clinical neurology and epidemiology of the major neurodegenerative diseases","volume":"10","author":"Erkkinen","year":"2018","journal-title":"Cold Spring Harbor Perspect. Biol."},{"key":"10.1016\/j.ejmech.2024.116569_bib35","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.ejmech.2024.116569_bib36","doi-asserted-by":"crossref","first-page":"408","DOI":"10.1126\/science.7046051","article-title":"The cholinergic hypothesis of geriatric memory dysfunction","volume":"217","author":"Bartus","year":"1982","journal-title":"Science"},{"key":"10.1016\/j.ejmech.2024.116569_bib37","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1007\/s12272-013-0036-3","article-title":"A review on cholinesterase inhibitors for Alzheimer's disease","volume":"36","author":"Anand","year":"2013","journal-title":"Arch Pharm. Res. (Seoul)"},{"key":"10.1016\/j.ejmech.2024.116569_bib38","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.ejmech.2024.116569_bib39","doi-asserted-by":"crossref","first-page":"1457","DOI":"10.1136\/bmj.2.6150.1457","article-title":"Correlation of cholinergic abnormalities with senile plaques and mental test scores in senile dementia","volume":"2","author":"Perry","year":"1978","journal-title":"Br. Med. J."},{"key":"10.1016\/j.ejmech.2024.116569_bib40","doi-asserted-by":"crossref","first-page":"60","DOI":"10.1016\/j.tox.2006.11.069","article-title":"Sensitivity of butyrylcholinesterase knockout mice to (\u2212)-huperzine A and donepezil suggests humans with butyrylcholinesterase deficiency may not tolerate these Alzheimer's disease drugs and indicates butyrylcholinesterase function in neurotransmission","volume":"233","author":"Duysen","year":"2007","journal-title":"Toxicology"},{"key":"10.1016\/j.ejmech.2024.116569_bib41","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1016\/j.ejmech.2017.03.062","article-title":"Recent progress in the identification of selective butyrylcholinesterase inhibitors for Alzheimer's disease","volume":"132","author":"Li","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib42","article-title":"Conventional versus new treatment: comparing the effects of acetylcholinesterase inhibitors and N-Methyl-D-Aspartate receptor antagonist with aducanumab","volume":"14","author":"Chin","year":"2022","journal-title":"Cureus"},{"key":"10.1016\/j.ejmech.2024.116569_bib43","doi-asserted-by":"crossref","first-page":"17213","DOI":"10.1073\/pnas.0508575102","article-title":"Selective butyrylcholinesterase inhibition elevates brain acetylcholine, augments learning and lowers Alzheimer \u03b2-amyloid peptide in rodent","volume":"102","author":"Greig","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ejmech.2024.116569_bib44","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.2174\/1567205013666160404120542","article-title":"Butyrylcholinesterase as a diagnostic and therapeutic target for Alzheimer's disease","volume":"13","author":"Darvesh","year":"2016","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.ejmech.2024.116569_bib45","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1111\/j.1468-1331.2008.02059.x","article-title":"Gene\u2013gene interaction between 14-3-3 zeta and butyrylcholinesterase modulates Alzheimer's disease risk","volume":"15","author":"Mateo","year":"2008","journal-title":"Eur. J. Neurol."},{"key":"10.1016\/j.ejmech.2024.116569_bib46","doi-asserted-by":"crossref","first-page":"1239","DOI":"10.1007\/s00109-007-0226-x","article-title":"Cholinergic status modulations in human volunteers under acute inflammation","volume":"85","author":"Ofek","year":"2007","journal-title":"J. Mol. Med."},{"key":"10.1016\/j.ejmech.2024.116569_bib47","doi-asserted-by":"crossref","first-page":"458","DOI":"10.1038\/35013070","article-title":"Vagus nerve stimulation attenuates the systemic inflammatory response to endotoxin","volume":"405","author":"Borovikova","year":"2000","journal-title":"Nature"},{"key":"10.1016\/j.ejmech.2024.116569_bib48","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.pharmthera.2017.05.002","article-title":"Cholinergic modulation of the immune system presents new approaches for treating inflammation","volume":"179","author":"Hoover","year":"2017","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.ejmech.2024.116569_bib49","doi-asserted-by":"crossref","first-page":"125","DOI":"10.1007\/BF03402177","article-title":"The cholinergic anti-inflammatory pathway: a missing link in neuroimmunomodulation","volume":"9","author":"Pavlov","year":"2003","journal-title":"Mol. Med."},{"key":"10.1016\/j.ejmech.2024.116569_bib50","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1016\/j.bioorg.2017.04.018","article-title":"Novel multi-targeted agents for Alzheimer's disease: synthesis, biological evaluation, and molecular modeling of novel 2-[4-(4-substitutedpiperazin-1-yl)phenyl]benzimidazoles","volume":"72","author":"Ozadali-Sari","year":"2017","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib51","doi-asserted-by":"crossref","DOI":"10.1016\/j.intimp.2021.108083","article-title":"Attenuation of spatial memory in 5xFAD mice by targeting cholinesterases, oxidative stress and inflammatory signaling using 2-(hydroxyl-(2-nitrophenyl)methyl)cyclopentanone","volume":"100","author":"Ullah","year":"2021","journal-title":"Int. Immunopharm."},{"key":"10.1016\/j.ejmech.2024.116569_bib52","doi-asserted-by":"crossref","first-page":"406","DOI":"10.1016\/S1474-4422(14)70305-9","article-title":"Role of the innate and adaptive immune responses in the course of multiple sclerosis","volume":"14","author":"Hemmer","year":"2015","journal-title":"Lancet Neurol."},{"key":"10.1016\/j.ejmech.2024.116569_bib53","doi-asserted-by":"crossref","first-page":"1336","DOI":"10.1016\/S0140-6736(16)30959-X","article-title":"Diagnosis of multiple sclerosis: progress and challenges","volume":"389","author":"Brownlee","year":"2017","journal-title":"Lancet"},{"key":"10.1016\/j.ejmech.2024.116569_bib54","doi-asserted-by":"crossref","first-page":"12656","DOI":"10.3390\/ijms131012656","article-title":"Relation between pro-inflammatory cytokines and acetylcholine levels in relapsing-remitting multiple sclerosis patients","volume":"13","author":"Reale","year":"2012","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib55","doi-asserted-by":"crossref","first-page":"2009","DOI":"10.3390\/ijms17122009","article-title":"Dysregulated homeostasis of acetylcholine levels in immune cells of RR-multiple sclerosis patients","volume":"17","author":"Di Bari","year":"2016","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib56","doi-asserted-by":"crossref","first-page":"540","DOI":"10.1016\/j.neuropharm.2005.10.013","article-title":"Anti-inflammatory properties of cholinergic up-regulation: a new role for acetylcholinesterase inhibitors","volume":"50","author":"Nizri","year":"2006","journal-title":"Neuropharmacology"},{"key":"10.1016\/j.ejmech.2024.116569_bib57","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/j.jns.2005.08.021","article-title":"Effects of donepezil on memory and cognition in multiple sclerosis","volume":"245","author":"Christodoulou","year":"2006","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib58","doi-asserted-by":"crossref","first-page":"425","DOI":"10.1016\/j.cbi.2010.01.037","article-title":"Butyrylcholinesterase activity in multiple sclerosis neuropathology","volume":"187","author":"Darvesh","year":"2010","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.ejmech.2024.116569_bib59","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1046\/j.1471-4159.2001.00116.x","article-title":"Chemical deacylation reduces the adhesive properties of proteolipid protein and leads to decompaction of the myelin sheath","volume":"76","author":"Bizzozero","year":"2001","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ejmech.2024.116569_bib60","doi-asserted-by":"crossref","first-page":"151","DOI":"10.1021\/cn100090g","article-title":"Cysteine thioesters as myelin proteolipid protein analogues to examine the role of butyrylcholinesterase in myelin decompaction","volume":"2","author":"Pottie","year":"2011","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.ejmech.2024.116569_bib61","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1007\/s11307-020-01540-6","article-title":"Imaging butyrylcholinesterase in multiple sclerosis","volume":"23","author":"Thorne","year":"2021","journal-title":"Mol. Imag. Biol."},{"key":"10.1016\/j.ejmech.2024.116569_bib62","doi-asserted-by":"crossref","first-page":"1154","DOI":"10.1139\/y89-184","article-title":"Cocaine: pharmacokinetics and biotransformation in man, can","volume":"67","author":"Inaba","year":"1989","journal-title":"J. Physiol. Pharmacol."},{"key":"10.1016\/j.ejmech.2024.116569_bib63","doi-asserted-by":"crossref","first-page":"83","DOI":"10.1124\/mol.55.1.83","article-title":"An improved cocaine hydrolase: the A328Y mutant of human butyrylcholinesterase is 4-fold more efficient","volume":"55","author":"Xie","year":"1999","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.ejmech.2024.116569_bib64","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1039\/B716268E","article-title":"Structure-and-mechanism-based design and discovery of therapeutics for cocaine overdose and addiction","volume":"6","author":"Zheng","year":"2008","journal-title":"Org. Biomol. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib65","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1016\/0006-2952(91)90665-R","article-title":"Activities of the enantiomers of cocaine and some related compounds as substrates and inhibitors of plasma butyrylcholinesterase","volume":"41","author":"Gatley","year":"1991","journal-title":"Biochem. Pharmacol."},{"key":"10.1016\/j.ejmech.2024.116569_bib66","doi-asserted-by":"crossref","first-page":"220","DOI":"10.1124\/mol.62.2.220","article-title":"Re-Engineering butyrylcholinesterase as a cocaine hydrolase","volume":"62","author":"Sun","year":"2002","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.ejmech.2024.116569_bib67","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.cbi.2010.01.004","article-title":"Characterization of a high-activity mutant of human butyrylcholinesterase against (\u2212)-cocaine","volume":"187","author":"Yang","year":"2010","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.ejmech.2024.116569_bib68","doi-asserted-by":"crossref","first-page":"2715","DOI":"10.1038\/sj.npp.1301666","article-title":"A cocaine hydrolase engineered from human butyrylcholinesterase selectively blocks cocaine toxicity and reinstatement of drug seeking in rats","volume":"33","author":"Brimijoin","year":"2008","journal-title":"Neuropsychopharmacology"},{"key":"10.1016\/j.ejmech.2024.116569_bib69","doi-asserted-by":"crossref","first-page":"16656","DOI":"10.1073\/pnas.0507332102","article-title":"Computational redesign of human butyrylcholinesterase for anticocaine medication","volume":"102","author":"Pan","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.ejmech.2024.116569_bib70","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1042\/BJ20130549","article-title":"Preparation and in vivo characterization of a cocaine hydrolase engineered from human butyrylcholinesterase for metabolizing cocaine","volume":"453","author":"Xue","year":"2013","journal-title":"Biochem. J."},{"key":"10.1016\/j.ejmech.2024.116569_bib71","doi-asserted-by":"crossref","first-page":"66","DOI":"10.1016\/j.cca.2014.01.024","article-title":"Acute organophosphorus poisoning","volume":"431","author":"Chowdhary","year":"2014","journal-title":"Clin. Chim. Acta"},{"key":"10.1016\/j.ejmech.2024.116569_bib72","doi-asserted-by":"crossref","first-page":"2131","DOI":"10.1007\/s00204-016-1772-1","article-title":"Toxicology of organophosphorus compounds in view of an increasing terrorist threat","volume":"90","author":"Worek","year":"2016","journal-title":"Arch. Toxicol."},{"key":"10.1016\/j.ejmech.2024.116569_bib73","doi-asserted-by":"crossref","DOI":"10.1016\/j.bios.2019.111348","article-title":"Preety, Bio-sensing of organophosphorus pesticides: a review","volume":"140","author":"Pundir","year":"2019","journal-title":"Biosens. Bioelectron."},{"key":"10.1016\/j.ejmech.2024.116569_bib74","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1016\/j.tox.2018.07.020","article-title":"Catalytic bioscavengers against organophosphorus agents: mechanistic issues of self-reactivating cholinesterases","volume":"409","author":"Lushchekina","year":"2018","journal-title":"Toxicology"},{"key":"10.1016\/j.ejmech.2024.116569_bib75","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1016\/j.cbi.2005.10.024","article-title":"Bioscavengers for the protection of humans against organophosphate toxicity","volume":"157\u2013158","author":"Doctor","year":"2005","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.ejmech.2024.116569_bib76","doi-asserted-by":"crossref","first-page":"536","DOI":"10.1016\/j.cbi.2013.06.012","article-title":"Progress in the development of enzyme-based nerve agent bioscavengers","volume":"206","author":"Nachon","year":"2013","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.ejmech.2024.116569_bib77","doi-asserted-by":"crossref","first-page":"50","DOI":"10.1016\/j.cbi.2018.07.006","article-title":"Catalytic bioscavengers as countermeasures against organophosphate nerve agents","volume":"292","author":"Goldsmith","year":"2018","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.ejmech.2024.116569_bib78","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1016\/j.tox.2006.11.066","article-title":"Stoichiometric and catalytic scavengers as protection against nerve agent toxicity: a mini review","volume":"233","author":"Lenz","year":"2007","journal-title":"Toxicology"},{"key":"10.1016\/j.ejmech.2024.116569_bib79","doi-asserted-by":"crossref","first-page":"4997","DOI":"10.1210\/en.2004-0569","article-title":"Ghrelin degradation by serum and tissue homogenates: identification of the cleavage sites","volume":"145","author":"De Vriese","year":"2004","journal-title":"Endocrinology"},{"key":"10.1016\/j.ejmech.2024.116569_bib80","doi-asserted-by":"crossref","first-page":"798","DOI":"10.3390\/ijms18040798","article-title":"Therapeutic potential of targeting the ghrelin pathway","volume":"18","author":"Colld\u00e9n","year":"2017","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib81","doi-asserted-by":"crossref","first-page":"2175","DOI":"10.1016\/j.peptides.2011.07.024","article-title":"Structures and molecular forms of the ghrelin-family peptides","volume":"32","author":"Nishi","year":"2011","journal-title":"Peptides"},{"key":"10.1016\/j.ejmech.2024.116569_bib82","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1016\/j.molmet.2015.03.005","article-title":"Ghrelin","volume":"4","author":"M\u00fcller","year":"2015","journal-title":"Mol. Metabol."},{"key":"10.1016\/j.ejmech.2024.116569_bib83","doi-asserted-by":"crossref","DOI":"10.1042\/BSR20181061","article-title":"Ghrelin, a gastrointestinal hormone, regulates energy balance and lipid metabolism","volume":"38","author":"Lv","year":"2018","journal-title":"Biosci. Rep."},{"key":"10.1016\/j.ejmech.2024.116569_bib84","doi-asserted-by":"crossref","first-page":"3086","DOI":"10.1210\/en.2016-1166","article-title":"Butyrylcholinesterase deficiency promotes adipose tissue growth and hepatic lipid accumulation in male mice on high-fat diet","volume":"157","author":"Chen","year":"2016","journal-title":"Endocrinology"},{"key":"10.1016\/j.ejmech.2024.116569_bib85","doi-asserted-by":"crossref","first-page":"1144","DOI":"10.1007\/s12035-016-9729-1","article-title":"Ghrelin and neurodegenerative disorders\u2014a review","volume":"54","author":"Shi","year":"2017","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.ejmech.2024.116569_bib86","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/j.cbi.2016.04.029","article-title":"Butyrylcholinesterase expression is regulated by fatty acids in HepG2 cells","volume":"259","author":"Gok","year":"2016","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.ejmech.2024.116569_bib87","doi-asserted-by":"crossref","first-page":"283","DOI":"10.3390\/biom10020283","article-title":"Arachidonoylcholine and other unsaturated long-chain acylcholines are endogenous modulators of the acetylcholine signaling system","volume":"10","author":"Akimov","year":"2020","journal-title":"Biomolecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib88","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/j.biochi.2022.09.008","article-title":"Novel activity of human BChE: lipid hydrolysis","volume":"204","author":"Gok","year":"2023","journal-title":"Biochimie"},{"key":"10.1016\/j.ejmech.2024.116569_bib89","doi-asserted-by":"crossref","first-page":"1031","DOI":"10.1093\/clinchem\/29.6.1031","article-title":"Pseudocholinesterase\/high-density lipoprotein cholesterol ratio in serum of normal persons and of hyperlipoproteinemics","volume":"29","author":"Jain","year":"1983","journal-title":"Clin. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib90","doi-asserted-by":"crossref","DOI":"10.3389\/fped.2021.629346","article-title":"Liver enzymes correlate with metabolic syndrome, inflammation, and endothelial dysfunction in prepubertal children with obesity","volume":"9","author":"Valle-Martos","year":"2021","journal-title":"Front. Pediatr."},{"key":"10.1016\/j.ejmech.2024.116569_bib91","doi-asserted-by":"crossref","DOI":"10.1016\/j.lfs.2022.120336","article-title":"Hepatocellular BChE as a therapeutic target to ameliorate hypercholesterolemia through PRMT5 selective degradation to restore LDL receptor transcription","volume":"293","author":"Wang","year":"2022","journal-title":"Life Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib92","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1186\/s12881-018-0561-5","article-title":"A novel mutation in the BCHE gene and phenotype identified in a child with low butyrylcholinesterase activity: a case report","volume":"19","author":"Yu","year":"2018","journal-title":"BMC Med. Genet."},{"key":"10.1016\/j.ejmech.2024.116569_bib93","first-page":"307","article-title":"[Serum levels of pseudocholinesterase in alcoholic cirrhosis patients. Correlation with the extent of anatomo-functional damage. Unfavorable prognostic index]","volume":"138","author":"Sportiello","year":"1981","journal-title":"Arch. Sci. Med."},{"key":"10.1016\/j.ejmech.2024.116569_bib94","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1007\/s13539-012-0083-5","article-title":"Butyrylcholinesterase as a prognostic marker: a review of the literature","volume":"4","author":"Santarpia","year":"2013","journal-title":"J. Cachexia Sarcopenia Muscle"},{"key":"10.1016\/j.ejmech.2024.116569_bib95","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, neuropathol","volume":"4","author":"Perry","year":"1978","journal-title":"Appl. Neurobiol."},{"key":"10.1016\/j.ejmech.2024.116569_bib96","doi-asserted-by":"crossref","first-page":"362","DOI":"10.1007\/BF00334445","article-title":"Colocalization of cholinesterases with ? amyloid protein in aged and Alzheimer's brains","volume":"85","author":"Mor\u00e1n","year":"1993","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.ejmech.2024.116569_bib97","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1016\/j.neuroscience.2015.04.039","article-title":"Butyrylcholinesterase-knockout reduces brain deposition of fibrillar \u03b2-amyloid in an Alzheimer mouse model","volume":"298","author":"Reid","year":"2015","journal-title":"Neuroscience"},{"key":"10.1016\/j.ejmech.2024.116569_bib98","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1111\/j.1468-1331.2008.02059.x","article-title":"Gene\u2013gene interaction between 14-3-3 zeta and butyrylcholinesterase modulates Alzheimer's disease risk","volume":"15","author":"Mateo","year":"2008","journal-title":"Eur. J. Neurol."},{"key":"10.1016\/j.ejmech.2024.116569_bib99","doi-asserted-by":"crossref","first-page":"359","DOI":"10.1007\/s00401-007-0276-8","article-title":"Homozygosity for the K variant of BCHE gene increases the risk for development of neurofibrillary pathology but not amyloid deposits at young ages","volume":"114","author":"Ghebremedhin","year":"2007","journal-title":"Acta Neuropathol."},{"key":"10.1016\/j.ejmech.2024.116569_bib100","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1111\/neup.12241","article-title":"Immunohistochemical analysis of hippocampal butyrylcholinesterase: implications for regional vulnerability in Alzheimer's disease","volume":"36","author":"Mizukami","year":"2016","journal-title":"Neuropathology"},{"key":"10.1016\/j.ejmech.2024.116569_bib101","first-page":"374","article-title":"Significance of serum butyrylcholinesterase levels in oral cancer, Australas","volume":"4","author":"Prabhu","year":"2011","journal-title":"Med. J."},{"key":"10.1016\/j.ejmech.2024.116569_bib102","doi-asserted-by":"crossref","first-page":"367","DOI":"10.4103\/0973-1482.165869","article-title":"Serum butyrylcholinesterase and zinc in breast cancer","volume":"13","author":"Kumar","year":"2017","journal-title":"J. Cancer Res. Therapeut."},{"key":"10.1016\/j.ejmech.2024.116569_bib103","doi-asserted-by":"crossref","first-page":"1012","DOI":"10.1016\/j.tranon.2018.06.003","article-title":"Biphasic alteration of butyrylcholinesterase (BChE) during prostate cancer development","volume":"11","author":"Gu","year":"2018","journal-title":"Transl. Oncol."},{"key":"10.1016\/j.ejmech.2024.116569_bib104","doi-asserted-by":"crossref","first-page":"293","DOI":"10.1097\/MPH.0000000000002285","article-title":"Multifarious functions of butyrylcholinesterase in neuroblastoma: impact of BCHE deletion on the neuroblastoma growth in vitro and in vivo","volume":"44","author":"Baranowska-Kortylewicz","year":"2022","journal-title":"J. Pediatr. Hematol. Oncol."},{"key":"10.1016\/j.ejmech.2024.116569_bib105","doi-asserted-by":"crossref","DOI":"10.3389\/fmed.2022.940533","article-title":"Does serum butyrylcholinesterase level determine the severity and mortality of COVID-19 pneumonia?: prospective study","volume":"9","author":"Sipahioglu","year":"2022","journal-title":"Front. Med."},{"key":"10.1016\/j.ejmech.2024.116569_bib106","doi-asserted-by":"crossref","first-page":"2150","DOI":"10.3390\/diagnostics12092150","article-title":"Critically Ill COVID-19 patients show reduced point of care-measured butyrylcholinesterase activity\u2014a prospective, monocentric observational study","volume":"12","author":"Espeter","year":"2022","journal-title":"Diagnostics"},{"key":"10.1016\/j.ejmech.2024.116569_bib107","first-page":"108","article-title":"Side effects of approved antidementives","volume":"21","author":"Mimica","year":"2009","journal-title":"Psychiatr. Danub."},{"key":"10.1016\/j.ejmech.2024.116569_bib108","doi-asserted-by":"crossref","first-page":"1825","DOI":"10.2174\/092986710791111206","article-title":"Tacrine derivatives and alzheimers disease","volume":"17","author":"Tumiatti","year":"2010","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib109","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/j.biopha.2018.06.147","article-title":"A molecular approach in drug development for Alzheimer's disease","volume":"106","author":"Agatonovic-Kustrin","year":"2018","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.ejmech.2024.116569_bib110","doi-asserted-by":"crossref","DOI":"10.1002\/cmdc.202200080","article-title":"Conjugates of tacrine with salicylamide as promising multitarget agents for Alzheimer's disease","volume":"17","author":"Grishchenko","year":"2022","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2024.116569_bib111","doi-asserted-by":"crossref","first-page":"2285","DOI":"10.3390\/ijms24032285","article-title":"Conjugates of tacrine and salicylic acid derivatives as new promising multitarget agents for Alzheimer's disease","volume":"24","author":"Makhaeva","year":"2023","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib112","doi-asserted-by":"crossref","first-page":"1551","DOI":"10.3390\/biom12111551","article-title":"New multifunctional agents for potential Alzheimer's disease treatment based on tacrine conjugates with 2-arylhydrazinylidene-1,3-diketones","volume":"12","author":"Elkina","year":"2022","journal-title":"Biomolecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib113","doi-asserted-by":"crossref","first-page":"4972","DOI":"10.1021\/acs.jmedchem.1c00048","article-title":"Sustainable drug discovery of multi-target-directed ligands for Alzheimer's disease","volume":"64","author":"Rossi","year":"2021","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib114","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1155\/2013\/524806","article-title":"Quantification of amiridine in human plasma by high-performance liquid chromatography coupled with electrospray tandem mass spectrometry","volume":"2013","author":"Miroshnichenko","year":"2013","journal-title":"Chromatogr. Res. Int."},{"key":"10.1016\/j.ejmech.2024.116569_bib115","doi-asserted-by":"crossref","first-page":"1060","DOI":"10.3390\/molecules27031060","article-title":"Bis-amiridines as acetylcholinesterase and butyrylcholinesterase inhibitors: N-functionalization determines the multitarget anti-alzheimer\u2019s activity profile","volume":"27","author":"Makhaeva","year":"2022","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib116","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2021.104974","article-title":"Amiridine-piperazine hybrids as cholinesterase inhibitors and potential multitarget agents for Alzheimer's disease treatment","volume":"112","author":"Makhaeva","year":"2021","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib117","doi-asserted-by":"crossref","first-page":"5891","DOI":"10.3390\/molecules25245891","article-title":"New multifunctional agents based on conjugates of 4-Amino-2,3-polymethylenequinoline and butylated hydroxytoluene for Alzheimer's disease treatment","volume":"25","author":"Makhaeva","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib118","doi-asserted-by":"crossref","first-page":"606","DOI":"10.1016\/j.mencom.2021.09.005","article-title":"Novel conjugates of 4-amino-2,3-polymethylenequinolines and vanillin as potential multitarget agents for AD treatment","volume":"31","author":"Makhaeva","year":"2021","journal-title":"Mendeleev Commun."},{"key":"10.1016\/j.ejmech.2024.116569_bib119","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2022.114606","article-title":"Recent advance on carbamate-based cholinesterase inhibitors as potential multifunctional agents against Alzheimer's disease","volume":"240","author":"Zhang","year":"2022","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib120","doi-asserted-by":"crossref","first-page":"9447","DOI":"10.3390\/ijms22179447","article-title":"Novel sulfonamide-based carbamates as selective inhibitors of BChE","volume":"22","author":"Magar","year":"2021","journal-title":"Int. J. Mol. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib121","doi-asserted-by":"crossref","first-page":"2067","DOI":"10.1021\/acs.jmedchem.5b01674","article-title":"Discovery of highly selective and nanomolar carbamate-based butyrylcholinesterase inhibitors by rational investigation into their inhibition mode","volume":"59","author":"Sawatzky","year":"2016","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib122","doi-asserted-by":"crossref","first-page":"914","DOI":"10.1021\/ml3001825","article-title":"Neuroprotective tri- and tetracyclic BChE inhibitors releasing reversible inhibitors upon carbamate transfer","volume":"3","author":"Darras","year":"2012","journal-title":"ACS Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2024.116569_bib123","doi-asserted-by":"crossref","first-page":"1540","DOI":"10.1002\/cmdc.201600223","article-title":"A novel way to radiolabel human butyrylcholinesterase for positron emission tomography through irreversible transfer of the radiolabeled moiety","volume":"11","author":"Sawatzky","year":"2016","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2024.116569_bib124","doi-asserted-by":"crossref","first-page":"2382","DOI":"10.3390\/pharmaceutics15102382","article-title":"Conceptual framework of the design of pleiotropic drugs against Alzheimer's disease","volume":"15","author":"Guiselin","year":"2023","journal-title":"Pharmaceutics"},{"key":"10.1016\/j.ejmech.2024.116569_bib125","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.113059","article-title":"Pleiotropic prodrugs: design of a dual butyrylcholinesterase inhibitor and 5-HT6 receptor antagonist with therapeutic interest in Alzheimer's disease","volume":"210","author":"Toublet","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib126","doi-asserted-by":"crossref","first-page":"2786","DOI":"10.3390\/molecules24152786","article-title":"Inhibiting acetylcholinesterase to activate pleiotropic prodrugs with therapeutic interest in Alzheimer's disease","volume":"24","author":"Toublet","year":"2019","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib127","doi-asserted-by":"crossref","first-page":"9302","DOI":"10.1021\/acs.jmedchem.1c00534","article-title":"Selective pseudo-irreversible butyrylcholinesterase inhibitors transferring antioxidant moieties to the enzyme show pronounced neuroprotective efficacy in vitro and in vivo in an Alzheimer's disease mouse model","volume":"64","author":"Scheiner","year":"2021","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib128","doi-asserted-by":"crossref","first-page":"3279","DOI":"10.1021\/jacs.1c13492","article-title":"Photoswitchable pseudoirreversible butyrylcholinesterase inhibitors allow optical control of inhibition in vitro and enable restoration of cognition in an Alzheimer's disease mouse model upon irradiation","volume":"144","author":"Scheiner","year":"2022","journal-title":"J. Am. Chem. Soc."},{"key":"10.1016\/j.ejmech.2024.116569_bib129","doi-asserted-by":"crossref","first-page":"944","DOI":"10.1039\/D2MD00087C","article-title":"Novel benzimidazole-based pseudo-irreversible butyrylcholinesterase inhibitors with neuroprotective activity in an Alzheimer's disease mouse model","volume":"13","author":"Spatz","year":"2022","journal-title":"RSC Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib130","doi-asserted-by":"crossref","first-page":"1510","DOI":"10.3390\/biomedicines10071510","article-title":"Novel rivastigmine derivatives as promising multi-target compounds for potential treatment of Alzheimer's disease","volume":"10","author":"Vicente-Zurdo","year":"2022","journal-title":"Biomedicines"},{"key":"10.1016\/j.ejmech.2024.116569_bib131","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.114044","article-title":"Design, synthesis, and biological evaluation of carbamate derivatives of N-salicyloyl tryptamine as multifunctional agents for the treatment of Alzheimer's disease","volume":"229","author":"Liu","year":"2022","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib132","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2022.105844","article-title":"Carbamate-based N-Substituted tryptamine derivatives as novel pleiotropic molecules for Alzheimer's disease","volume":"125","author":"Zhang","year":"2022","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib133","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2022.105993","article-title":"Discovery of carbamate-based N-salicyloyl tryptamine derivatives as novel pleiotropic agents for the treatment of Alzheimer's disease","volume":"127","author":"Wang","year":"2022","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib134","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2022.134804","article-title":"Discovery of carbamate-based salicylic acid derivatives as novel cholinesterase inhibitor","volume":"1276","author":"Wang","year":"2023","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.ejmech.2024.116569_bib135","doi-asserted-by":"crossref","DOI":"10.1080\/14756366.2023.2231661","article-title":"Development of novel salicylic acid\u2013donepezil\u2013rivastigmine hybrids as multifunctional agents for the treatment of Alzheimer's disease","volume":"38","author":"Zhou","year":"2023","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib136","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2022.115048","article-title":"Pseudo-irreversible butyrylcholinesterase inhibitors: structure\u2013activity relationships, computational and crystallographic study of the N-dialkyl O-arylcarbamate warhead","volume":"247","author":"Meden","year":"2023","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib137","doi-asserted-by":"crossref","first-page":"192","DOI":"10.1016\/j.cbi.2008.04.050","article-title":"Stereoselective inhibition of human, mouse, and horse cholinesterases by bambuterol enantiomers","volume":"175","author":"Bosak","year":"2008","journal-title":"Chem. Biol. Interact."},{"key":"10.1016\/j.ejmech.2024.116569_bib138","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1124\/dmd.114.060251","article-title":"Stereoselective inhibition of human butyrylcholinesterase by the enantiomers of bambuterol and their intermediates","volume":"43","author":"Pistolozzi","year":"2015","journal-title":"Drug Metab. Dispos."},{"key":"10.1016\/j.ejmech.2024.116569_bib139","doi-asserted-by":"crossref","first-page":"1220","DOI":"10.3390\/ph15101220","article-title":"Design, synthesis and biological evaluation of biscarbamates as potential selective butyrylcholinesterase inhibitors for the treatment of Alzheimer's disease","volume":"15","author":"Mato\u0161evi\u0107","year":"2022","journal-title":"Pharmaceuticals"},{"key":"10.1016\/j.ejmech.2024.116569_bib140","doi-asserted-by":"crossref","first-page":"3839","DOI":"10.3390\/molecules24213839","article-title":"Heterocycles in medicinal chemistry","volume":"24","author":"Jampilek","year":"2019","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib141","doi-asserted-by":"crossref","first-page":"1256","DOI":"10.4103\/1673-5374.213541","article-title":"Heterocyclic compounds as key structures for the interaction with old and new targets in Alzheimer's disease therapy","volume":"12","author":"Hiremathad","year":"2017","journal-title":"Neural Regen. Res."},{"key":"10.1016\/j.ejmech.2024.116569_bib142","doi-asserted-by":"crossref","DOI":"10.15640\/jcb.v2n2a3","article-title":"Synthesis of imidazole derivatives and their biological activities","volume":"2","author":"Romero","year":"2014","journal-title":"J. Chem. Biochem."},{"key":"10.1016\/j.ejmech.2024.116569_bib143","doi-asserted-by":"crossref","DOI":"10.1016\/j.arabjc.2022.104384","article-title":"Exploring facile synthesis and cholinesterase inhibiting potential of heteroaryl substituted imidazole derivatives for the treatment of Alzheimer's disease","volume":"16","author":"Chaudhry","year":"2023","journal-title":"Arab. J. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib144","doi-asserted-by":"crossref","first-page":"419","DOI":"10.1016\/j.ejmech.2014.11.053","article-title":"Structure activity relationship (SAR) study of benzimidazole scaffold for different biological activities: a mini-review","volume":"97","author":"Yadav","year":"2015","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib145","doi-asserted-by":"crossref","first-page":"3260","DOI":"10.2174\/0929867326666190124123208","article-title":"Benzimidazole-derived compounds designed for different targets of Alzheimer's disease","volume":"26","author":"Gulcan","year":"2019","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib146","doi-asserted-by":"crossref","first-page":"2863","DOI":"10.1007\/s11030-022-10476-8","article-title":"Synthesis of novel carboxamide- and carbohydrazide-benzimidazoles as selective butyrylcholinesterase inhibitors","volume":"26","author":"Ozturk","year":"2022","journal-title":"Mol. Divers."},{"key":"10.1016\/j.ejmech.2024.116569_bib147","doi-asserted-by":"crossref","DOI":"10.1016\/j.ica.2021.120486","article-title":"Silver (I)-N-heterocyclic carbene complexes: synthesis and characterization, biological evaluation of Anti-Cholinesterase, anti-alpha-amylase, anti-lipase, and antibacterial activities, and molecular docking study","volume":"525","author":"Sandeli","year":"2021","journal-title":"Inorg. Chim. Acta."},{"key":"10.1016\/j.ejmech.2024.116569_bib148","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2021.130399","article-title":"New silver Nheterocyclic carbenes complexes: synthesis, molecular docking study and biological activities evaluation as cholinesterase inhibitors and antimicrobials","volume":"1238","author":"Lasmari","year":"2021","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.ejmech.2024.116569_bib149","doi-asserted-by":"crossref","first-page":"6856","DOI":"10.1021\/acs.jmedchem.1c00167","article-title":"Highly potent and selective butyrylcholinesterase inhibitors for cognitive improvement and neuroprotection","volume":"64","author":"Li","year":"2021","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib150","doi-asserted-by":"crossref","DOI":"10.1016\/j.arr.2019.100945","article-title":"Ghrelin in Alzheimer's disease: pathologic roles and therapeutic implications","volume":"55","author":"Jeon","year":"2019","journal-title":"Ageing Res. Rev."},{"key":"10.1016\/j.ejmech.2024.116569_bib151","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2022.114510","article-title":"A highly effective and stable butyrylcholinesterase inhibitor with multi-faceted neuroprotection and cognition improvement","volume":"239","author":"Li","year":"2022","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib152","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2024.116289","article-title":"Optimizing drug-like properties of selective butyrylcholinesterase inhibitors for cognitive improvement: enhancing aqueous solubility by disrupting molecular plane","volume":"268","author":"Xing","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib153","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.113124","article-title":"Design, synthesis and biological evaluation of new benzoxazolone\/benzothiazolone derivatives as multi-target agents against Alzheimer's disease","volume":"212","author":"Erdogan","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib154","doi-asserted-by":"crossref","first-page":"1872","DOI":"10.3390\/pr10091872","article-title":"Inhibition of cholinesterases by benzothiazolone derivatives","volume":"10","author":"Alag\u00f6z","year":"2022","journal-title":"Processes"},{"key":"10.1016\/j.ejmech.2024.116569_bib155","first-page":"864","article-title":"Medicinal perspective of indole derivatives: recent developments and structure-activity relationship studies","volume":"21","author":"Kumar","year":"2020","journal-title":"Curr. Drug Targets"},{"key":"10.1016\/j.ejmech.2024.116569_bib156","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.112506","article-title":"The importance of indole and azaindole scaffold in the development of antitumor agents","volume":"203","author":"Han","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib157","doi-asserted-by":"crossref","first-page":"1209","DOI":"10.2174\/092986708784310422","article-title":"Natural products and their derivatives as cholinesterase inhibitors in the treatment of neurodegenerative disorders: an update","volume":"15","author":"Loizzo","year":"2008","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib158","doi-asserted-by":"crossref","first-page":"570","DOI":"10.1007\/s43440-022-00370-3","article-title":"Recent progress in biologically active indole hybrids: a mini review","volume":"74","author":"Mahmoud","year":"2022","journal-title":"Pharmacol. Rep."},{"key":"10.1016\/j.ejmech.2024.116569_bib159","doi-asserted-by":"crossref","first-page":"769","DOI":"10.4155\/fmc-2020-0325","article-title":"Discovery, biological evaluation and molecular dynamic simulations of butyrylcholinesterase inhibitors through structure-based pharmacophore virtual screening","volume":"13","author":"Lu","year":"2021","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib160","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2022.105647","article-title":"Dimethoxyindoles based thiosemicarbazones as multi-target agents; synthesis, crystal interactions, biological activity and molecular modeling","volume":"120","author":"Y\u0131ld\u0131z","year":"2022","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib161","doi-asserted-by":"crossref","DOI":"10.1016\/j.phytochem.2021.113017","article-title":"Monoterpene indole alkaloids from Vinca minor L. (Apocynaceae): identification of new structural scaffold for treatment of Alzheimer's disease","volume":"194","author":"Vrabec","year":"2022","journal-title":"Phytochemistry"},{"key":"10.1016\/j.ejmech.2024.116569_bib162","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2023.106663","article-title":"Synthesis and biological evaluation of thieno[3,2-c]pyrazol-3-amine derivatives as potent glycogen synthase kinase 3\u03b2 inhibitors for Alzheimer's disease","volume":"138","author":"Yan","year":"2023","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib163","doi-asserted-by":"crossref","first-page":"2881","DOI":"10.2174\/1389557522666220420094317","article-title":"GSK-3\u03b2 and its inhibitors in Alzheimer's disease: a recent update","volume":"22","author":"Chauhan","year":"2022","journal-title":"Mini-Rev. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib164","doi-asserted-by":"crossref","DOI":"10.1002\/ardp.201900299","article-title":"Isatin dimers and their biological activities","volume":"353","author":"Zhang","year":"2020","journal-title":"Arch. Pharm. (Weinheim)"},{"key":"10.1016\/j.ejmech.2024.116569_bib165","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmcl.2022.129037","article-title":"Selective butyrylcholinesterase inhibition by isatin dimers and 3-indolyl-3-hydroxy-2-oxindole dimers","volume":"77","author":"Reiland","year":"2022","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2024.116569_bib166","doi-asserted-by":"crossref","first-page":"667","DOI":"10.1007\/s11030-016-9668-9","article-title":"Synthesis and preliminary biological evaluations of (+)-isocampholenic acid-derived amides","volume":"20","author":"Gro\u0161elj","year":"2016","journal-title":"Mol. Divers."},{"key":"10.1016\/j.ejmech.2024.116569_bib167","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2020.112766","article-title":"Structure-activity relationship study of tryptophan-based butyrylcholinesterase inhibitors","volume":"208","author":"Meden","year":"2020","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib168","doi-asserted-by":"crossref","first-page":"1821","DOI":"10.1002\/cjoc.202200096","article-title":"Discovery of tryptophan\u2010tetrahydroisoquinoline derivatives as multifunctional agents for treatment of Alzheimer's disease","volume":"40","author":"Lu","year":"2022","journal-title":"Chin. J. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib169","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.2174\/1570180819666220314144219","article-title":"Progress and development of carbazole scaffold based as potential anti-alzheimer agents using MTDL approach","volume":"19","author":"Kumar","year":"2022","journal-title":"Lett. Drug Des. Discov."},{"key":"10.1016\/j.ejmech.2024.116569_bib170","doi-asserted-by":"crossref","first-page":"9307","DOI":"10.3390\/molecules19079307","article-title":"N-alkyl carbazole derivatives as new tools for Alzheimer's disease: preliminary studies","volume":"19","author":"Saturnino","year":"2014","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib171","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1002\/med.21622","article-title":"BACE1 inhibitors: current status and future directions in treating Alzheimer's disease","volume":"40","author":"Moussa\u2010Pacha","year":"2020","journal-title":"Med. Res. Rev."},{"key":"10.1016\/j.ejmech.2024.116569_bib172","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2020.128793","article-title":"Design, synthesis and biological activity evaluation of novel carbazole-benzylpiperidine hybrids as potential anti Alzheimer agents","volume":"1221","author":"Sadeghian","year":"2020","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.ejmech.2024.116569_bib173","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1007\/s11030-019-09943-6","article-title":"Design, synthesis, in vivo and in vitro studies of 1,2,3,4-tetrahydro-9H-carbazole derivatives, highly selective and potent butyrylcholinesterase inhibitors","volume":"24","author":"Ghobadian","year":"2020","journal-title":"Mol. Divers."},{"key":"10.1016\/j.ejmech.2024.116569_bib174","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2023.106378","article-title":"Novel N or N modified \u03b1-carboline analogues as potential ligands in Alzheimer's disease therapy: synthesis and neurobiological activity evaluation","volume":"133","author":"Dan","year":"2023","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib175","doi-asserted-by":"crossref","first-page":"663","DOI":"10.3390\/molecules26030663","article-title":"Recent advances in the synthesis of \u03b2-carboline alkaloids","volume":"26","author":"Szab\u00f3","year":"2021","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib176","doi-asserted-by":"crossref","DOI":"10.1590\/s2175-97902022e19958","article-title":"Anticholinesterase activity of \u03b2-carboline-1,3,5-triazine hybrids","volume":"58","author":"Bar\u00e9a","year":"2022","journal-title":"Braz. J. Pharm. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib177","doi-asserted-by":"crossref","first-page":"2170","DOI":"10.1016\/j.ejmech.2011.02.071","article-title":"Quinolizidinyl derivatives of bi- and tricyclic systems as potent inhibitors of acetyl- and butyrylcholinesterase with potential in Alzheimer's disease","volume":"46","author":"Tasso","year":"2011","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib178","doi-asserted-by":"crossref","first-page":"1040","DOI":"10.1002\/cmdc.201500104","article-title":"Multitarget therapeutic leads for Alzheimer's disease: quinolizidinyl derivatives of Bi\u2010 and tricyclic systems as dual inhibitors of cholinesterases and \u03b2\u2010amyloid (A\u03b2) aggregation","volume":"10","author":"Tonelli","year":"2015","journal-title":"ChemMedChem"},{"key":"10.1016\/j.ejmech.2024.116569_bib179","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115169","article-title":"Thioxanthenone-based derivatives as multitarget therapeutic leads for Alzheimer's disease","volume":"250","author":"Tonelli","year":"2023","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib180","doi-asserted-by":"crossref","first-page":"6273","DOI":"10.1039\/C9CS00286C","article-title":"Catalytic reductive aminations using molecular hydrogen for synthesis of different kinds of amines","volume":"49","author":"Murugesan","year":"2020","journal-title":"Chem. Soc. Rev."},{"key":"10.1016\/j.ejmech.2024.116569_bib181","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1080\/14756366.2016.1243534","article-title":"Tertiary amine derivatives of chlorochalcone as acetylcholinesterase (AChE) and buthylcholinesterase (BuChE) inhibitors: the influence of chlorine, alkyl amine side chain and \u03b1,\u03b2-unsaturated ketone group","volume":"32","author":"Gao","year":"2017","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib182","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1016\/j.ejmech.2016.12.003","article-title":"Novel ferulic amide derivatives with tertiary amine side chain as acetylcholinesterase and butyrylcholinesterase inhibitors: the influence of carbon spacer length, alkylamine and aromatic group","volume":"126","author":"Liu","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib183","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2022.114729","article-title":"Design, synthesis, and biological evaluation of aromatic tertiary amine derivatives as selective butyrylcholinesterase inhibitors for the treatment of Alzheimer's disease","volume":"243","author":"Lu","year":"2022","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib184","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2023.115301","article-title":"Highly selective butyrylcholinesterase inhibitors related to Amaryllidaceae alkaloids - design, synthesis, and biological evaluation","volume":"252","author":"Pidany","year":"2023","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib185","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1007\/s11274-020-02978-0","article-title":"Biological activity of quaternary ammonium salts and resistance of microorganisms to these compounds","volume":"37","author":"Ob\u0142\u0105k","year":"2021","journal-title":"World J. Microbiol. Biotechnol."},{"key":"10.1016\/j.ejmech.2024.116569_bib186","doi-asserted-by":"crossref","first-page":"7645","DOI":"10.1021\/acs.est.2c08244","article-title":"Quaternary ammonium compounds: a chemical class of emerging concern","volume":"57","author":"Arnold","year":"2023","journal-title":"Environ. Sci. Technol."},{"key":"10.1016\/j.ejmech.2024.116569_bib187","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmcl.2023.129392","article-title":"Synthesis and evaluation of Fmoc-amino esters and amides bearing a substrate like quaternary ammonium group as selective butyrylcholinesterase inhibitors","volume":"92","author":"Godinez","year":"2023","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2024.116569_bib188","doi-asserted-by":"crossref","DOI":"10.1002\/slct.202201977","article-title":"6\u2010Methoxy\u20101\u2010tetralone derivatives bearing an N\u2010arylpyridinium moiety as cholinesterase inhibitors: design, synthesis, biological evaluation, and molecular docking study","volume":"7","author":"Chehardoli","year":"2022","journal-title":"ChemistrySelect"},{"key":"10.1016\/j.ejmech.2024.116569_bib189","doi-asserted-by":"crossref","first-page":"344","DOI":"10.1002\/asia.201801560","article-title":"Carbonyl compounds' journey to amide bond formation","volume":"14","author":"Narendar Reddy","year":"2019","journal-title":"Chem. Asian J."},{"key":"10.1016\/j.ejmech.2024.116569_bib190","doi-asserted-by":"crossref","DOI":"10.1016\/j.molstruc.2022.133307","article-title":"Synthesis multicomponent based on o\u2010tolyl\u2010isocyanide; cholinesterase inhibitors and computational studies","volume":"1264","author":"Camargo-Ayala","year":"2022","journal-title":"J. Mol. Struct."},{"key":"10.1016\/j.ejmech.2024.116569_bib191","article-title":"Piperine: a comprehensive review of methods of isolation, purification, and biological properties, Med","volume":"7","author":"Tiwari","year":"2020","journal-title":"Drug Discov."},{"key":"10.1016\/j.ejmech.2024.116569_bib192","doi-asserted-by":"crossref","first-page":"216","DOI":"10.1016\/j.phytol.2023.01.004","article-title":"Synthesis of piperine analogues as AChE and BChE inhibitors for the treatment of Alzheimer's disease","volume":"53","author":"Jaipea","year":"2023","journal-title":"Phytochem. Lett."},{"key":"10.1016\/j.ejmech.2024.116569_bib193","doi-asserted-by":"crossref","first-page":"1449","DOI":"10.1517\/13543770903185920","article-title":"The role of sulfamide derivatives in medicinal chemistry: a patent review (2006 \u2013 2008)","volume":"19","author":"Reitz","year":"2009","journal-title":"Expert Opin. Ther. Pat."},{"key":"10.1016\/j.ejmech.2024.116569_bib194","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/j.ijbiomac.2022.01.136","article-title":"Identification of sulfonamide based butyrylcholinesterase inhibitors through scaffold hopping approach","volume":"203","author":"Ganeshpurkar","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ejmech.2024.116569_bib195","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1016\/j.drudis.2018.11.014","article-title":"Artificial intelligence in drug development: present status and future prospects","volume":"24","author":"Mak","year":"2019","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.ejmech.2024.116569_bib196","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.4155\/fmc-2021-0325","article-title":"Identification of sulfonamide-based butyrylcholinesterase inhibitors using machine learning","volume":"14","author":"Ganeshpurkar","year":"2022","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib197","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1007\/s10930-023-10090-z","article-title":"Molecular and computational analysis identify statins as selective inhibitors of human butyrylcholinesterase","volume":"42","author":"Atay","year":"2023","journal-title":"Protein J."},{"key":"10.1016\/j.ejmech.2024.116569_bib198","doi-asserted-by":"crossref","first-page":"643","DOI":"10.1038\/s41598-022-27149-z","article-title":"In silico and in vitro studies confirm Ondansetron as a novel acetylcholinesterase and butyrylcholinesterase inhibitor","volume":"13","author":"Gholami","year":"2023","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2024.116569_bib199","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1038\/nrd.2018.168","article-title":"Drug repurposing: progress, challenges and recommendations","volume":"18","author":"Pushpakom","year":"2019","journal-title":"Nat. Rev. Drug Discov."},{"key":"10.1016\/j.ejmech.2024.116569_bib200","doi-asserted-by":"crossref","first-page":"2076","DOI":"10.1016\/j.drudis.2019.06.014","article-title":"Drug repurposing: a promising tool to accelerate the drug discovery process","volume":"24","author":"Parvathaneni","year":"2019","journal-title":"Drug Discov. Today"},{"key":"10.1016\/j.ejmech.2024.116569_bib201","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.tips.2021.01.003","article-title":"Drug repurposing for rare diseases","volume":"42","author":"Roessler","year":"2021","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib202","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1111\/j.1472-8206.2004.00299.x","article-title":"Chemical, pharmacokinetic and pharmacodynamic properties of statins: an update","volume":"19","author":"Schachter","year":"2005","journal-title":"Fundam. Clin. Pharmacol."},{"key":"10.1016\/j.ejmech.2024.116569_bib203","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1111\/j.1527-3458.2001.tb00195.x","article-title":"Ondansetron: a selective 5-HT3 receptor antagonist and its applications in CNS-related disorders","volume":"7","author":"Ye","year":"2006","journal-title":"CNS Drug Rev."},{"key":"10.1016\/j.ejmech.2024.116569_bib204","doi-asserted-by":"crossref","first-page":"1735","DOI":"10.3390\/antiox11091735","article-title":"Polyfunctionalized \u03b1-Phenyl-tert-butyl(benzyl)nitrones: multifunctional antioxidants for stroke treatment","volume":"11","author":"Diez-Iriepa","year":"2022","journal-title":"Antioxidants"},{"key":"10.1016\/j.ejmech.2024.116569_bib205","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. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib206","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2022.116742","article-title":"Advancements in the development of multi-target directed ligands for the treatment of Alzheimer's disease","volume":"61","author":"Kumar","year":"2022","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib207","doi-asserted-by":"crossref","DOI":"10.1038\/srep45627","article-title":"Novel conjugates of aminoadamantanes with carbazole derivatives as potential multitarget agents for AD treatment","volume":"7","author":"Bachurin","year":"2017","journal-title":"Sci. Rep."},{"key":"10.1016\/j.ejmech.2024.116569_bib208","doi-asserted-by":"crossref","first-page":"485","DOI":"10.4155\/fmc.14.25","article-title":"Polypharmacology: the rise of multitarget drugs over combination therapies","volume":"6","author":"Rosini","year":"2014","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib209","doi-asserted-by":"crossref","first-page":"S191","DOI":"10.33549\/physiolres.932678","article-title":"Structure, function, and pharmacology of NMDA receptor channels","author":"Vyklicky","year":"2014","journal-title":"Physiol. Res."},{"key":"10.1016\/j.ejmech.2024.116569_bib210","doi-asserted-by":"crossref","first-page":"1041","DOI":"10.3233\/JAD-160763","article-title":"Role of glutamate and NMDA receptors in Alzheimer's disease","volume":"57","author":"Wang","year":"2017","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.ejmech.2024.116569_bib211","doi-asserted-by":"crossref","first-page":"746","DOI":"10.2174\/156720512801322564","article-title":"N-methyl D-aspartate (NMDA) receptor antagonists and memantine treatment for Alzheimer's disease, vascular dementia and Parkinson's disease","volume":"9","author":"Olivares","year":"2012","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.ejmech.2024.116569_bib212","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113320","article-title":"Alzheimer's disease and its treatment by different approaches: a review","volume":"216","author":"Srivastava","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib213","doi-asserted-by":"crossref","first-page":"2722","DOI":"10.1021\/acschemneuro.8b00154","article-title":"Pharmacological and electrophysiological characterization of novel NMDA receptor antagonists","volume":"9","author":"Leiva","year":"2018","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.ejmech.2024.116569_bib214","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmcl.2023.129213","article-title":"Identification and in silicon binding study of a novel NR2B selective NMDAR antagonist","volume":"85","author":"Yang","year":"2023","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2024.116569_bib215","doi-asserted-by":"crossref","first-page":"5789","DOI":"10.3390\/molecules25245789","article-title":"Comprehensive review on Alzheimer's disease: causes and treatment","volume":"25","author":"Breijyeh","year":"2020","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib216","doi-asserted-by":"crossref","first-page":"3","DOI":"10.3390\/biom11010003","article-title":"Pursuing the complexity of Alzheimer's disease: discovery of fluoren-9-amines as selective butyrylcholinesterase inhibitors and N-Methyl-d-Aspartate receptor antagonists","volume":"11","author":"Konecny","year":"2020","journal-title":"Biomolecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib217","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmc.2021.116355","article-title":"Evaluation of \u03b3-carboline-phenothiazine conjugates as simultaneous NMDA receptor blockers and cholinesterase inhibitors","volume":"46","author":"Schwarthoff","year":"2021","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib218","doi-asserted-by":"crossref","first-page":"5527","DOI":"10.3390\/molecules26185527","article-title":"Conjugation of aminoadamantane and \u03b3-carboline pharmacophores gives rise to unexpected properties of multifunctional ligands","volume":"26","author":"Bachurin","year":"2021","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib219","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2021.105070","article-title":"Structural exploration of multifunctional monoamine oxidase B inhibitors as potential drug candidates against Alzheimer's disease","volume":"114","author":"Zhang","year":"2021","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib220","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1080\/17425255.2017.1273901","article-title":"Use of monoamine oxidase inhibitors in chronic neurodegeneration","volume":"13","author":"Riederer","year":"2017","journal-title":"Expet Opin. Drug Metabol. Toxicol."},{"key":"10.1016\/j.ejmech.2024.116569_bib221","doi-asserted-by":"crossref","first-page":"789","DOI":"10.1007\/s00702-003-0828-6","article-title":"Early and persistent alterations in prefrontal cortex MAO A and B in Alzheimer's disease","volume":"110","author":"Kennedy","year":"2003","journal-title":"J. Neural. Transm."},{"key":"10.1016\/j.ejmech.2024.116569_bib222","doi-asserted-by":"crossref","first-page":"22","DOI":"10.1017\/S1092852913000734","article-title":"A neuroscientific update on monoamine oxidase and its inhibitors","volume":"18","author":"Schwartz","year":"2013","journal-title":"CNS Spectr."},{"key":"10.1016\/j.ejmech.2024.116569_bib223","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1016\/S0161-813X(03)00106-2","article-title":"Monoamine oxidase-B inhibition in Alzheimer's disease","volume":"25","author":"Riederer","year":"2004","journal-title":"Neurotoxicology"},{"key":"10.1016\/j.ejmech.2024.116569_bib224","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1016\/j.tips.2004.11.007","article-title":"Multi-functional drugs for various CNS targets in the treatment of neurodegenerative disorders","volume":"26","author":"Youdim","year":"2005","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib225","doi-asserted-by":"crossref","first-page":"1533","DOI":"10.3892\/mmr.2014.2040","article-title":"Monoamine oxidase inhibitors: promising therapeutic agents for Alzheimer's disease","volume":"9","author":"Cai","year":"2014","journal-title":"Mol. Med. Rep."},{"key":"10.1016\/j.ejmech.2024.116569_bib226","doi-asserted-by":"crossref","first-page":"3724","DOI":"10.3390\/molecules26123724","article-title":"Role of monoamine oxidase activity in Alzheimer's disease: an insight into the therapeutic potential of inhibitors","volume":"26","author":"Behl","year":"2021","journal-title":"Molecules"},{"key":"10.1016\/j.ejmech.2024.116569_bib227","doi-asserted-by":"crossref","first-page":"28182","DOI":"10.1021\/acsomega.1c04252","article-title":"Halogenated coumarin\u2013chalcones as multifunctional monoamine oxidase-B and butyrylcholinesterase inhibitors","volume":"6","author":"Rehuman","year":"2021","journal-title":"ACS Omega"},{"key":"10.1016\/j.ejmech.2024.116569_bib228","doi-asserted-by":"crossref","first-page":"910","DOI":"10.1016\/j.ijbiomac.2022.07.178","article-title":"Synthesis of 4-substituted benzyl-2-triazole-linked-tryptamine-paeonol derivatives and evaluation of their selective inhibitions against butyrylcholinesterase and monoamine oxidase-B","volume":"217","author":"Oh","year":"2022","journal-title":"Int. J. Biol. Macromol."},{"key":"10.1016\/j.ejmech.2024.116569_bib229","doi-asserted-by":"crossref","first-page":"2152","DOI":"10.1016\/j.apsb.2023.01.013","article-title":"8-Hydroxyquinolylnitrones as multifunctional ligands for the therapy of neurodegenerative diseases","volume":"13","author":"Knez","year":"2023","journal-title":"Acta Pharm. Sin. B"},{"key":"10.1016\/j.ejmech.2024.116569_bib230","doi-asserted-by":"crossref","first-page":"336","DOI":"10.1016\/j.molmed.2013.02.007","article-title":"Tryptophan metabolism: entering the field of aging and age-related pathologies","volume":"19","author":"van der Goot","year":"2013","journal-title":"Trends Mol. Med."},{"key":"10.1016\/j.ejmech.2024.116569_bib231","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1007\/978-1-4615-4709-9_19","article-title":"Degradation of tryptophan in neurodegenerative disorders","volume":"467","author":"Widner","year":"1999","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.ejmech.2024.116569_bib232","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1007\/s007020050029","article-title":"Tryptophan degradation and immune activation in Alzheimer's disease","volume":"107","author":"Widner","year":"2000","journal-title":"J. Neural. Transm."},{"key":"10.1016\/j.ejmech.2024.116569_bib233","doi-asserted-by":"crossref","first-page":"204","DOI":"10.2478\/v10039-010-0023-6","article-title":"Kynurenine and its metabolites in Alzheimer's disease patients","volume":"55","author":"Gulaj","year":"2010","journal-title":"Adv. Med. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib234","doi-asserted-by":"crossref","first-page":"1665","DOI":"10.1016\/j.bmc.2018.02.014","article-title":"Investigation of multi-target-directed ligands (MTDLs) with butyrylcholinesterase (BuChE) and indoleamine 2,3-dioxygenase 1 (Ido1) inhibition: the design, synthesis of miconazole analogues targeting Alzheimer's disease","volume":"26","author":"Lu","year":"2018","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib235","doi-asserted-by":"crossref","first-page":"371","DOI":"10.1002\/glia.10175","article-title":"Quinolinic acid upregulates chemokine production and chemokine receptor expression in astrocytes","volume":"41","author":"Guillemin","year":"2003","journal-title":"Glia"},{"key":"10.1016\/j.ejmech.2024.116569_bib236","doi-asserted-by":"crossref","first-page":"291","DOI":"10.3233\/JAD-140414","article-title":"The Ido inhibitor coptisine ameliorates cognitive impairment in a mouse model of Alzheimer's disease","volume":"43","author":"Yu","year":"2014","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.ejmech.2024.116569_bib237","doi-asserted-by":"crossref","first-page":"1105","DOI":"10.4155\/fmc-2021-0039","article-title":"Synthesis and activity of miconazole derivatives as dual BChE\/Ido1 inhibitors for the treatment of Alzheimer's disease","volume":"13","author":"Lu","year":"2021","journal-title":"Future Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib238","doi-asserted-by":"crossref","DOI":"10.1016\/j.bmcl.2020.127756","article-title":"Novel BuChE-Ido1 inhibitors from sertaconazole: virtual screening, chemical optimization and molecular modeling studies","volume":"34","author":"Zhou","year":"2021","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.ejmech.2024.116569_bib239","doi-asserted-by":"crossref","first-page":"3226","DOI":"10.1021\/acschemneuro.3c00358","article-title":"Design, synthesis, and proof of concept of balanced dual inhibitors of butyrylcholinesterase (BChE) and histone deacetylase 6 (HDAC6) for the treatment of Alzheimer's disease","volume":"14","author":"Wang","year":"2023","journal-title":"ACS Chem. Neurosci."},{"key":"10.1016\/j.ejmech.2024.116569_bib240","doi-asserted-by":"crossref","first-page":"158","DOI":"10.2174\/1570159X19666210609160017","article-title":"Understanding the role of histone deacetylase and their inhibitors in neurodegenerative disorders: current targets and future perspective","volume":"20","author":"Kumar","year":"2022","journal-title":"Curr. Neuropharmacol."},{"key":"10.1016\/j.ejmech.2024.116569_bib241","doi-asserted-by":"crossref","first-page":"2119","DOI":"10.1111\/j.1471-4159.2008.05564.x","article-title":"Histone deacetylase 6 interacts with the microtubule-associated protein tau","volume":"106","author":"Ding","year":"2008","journal-title":"J. Neurochem."},{"key":"10.1016\/j.ejmech.2024.116569_bib242","doi-asserted-by":"crossref","first-page":"283","DOI":"10.3233\/JAD-2012-120727","article-title":"The role of HDAC6 in Alzheimer's disease","volume":"33","author":"Zhang","year":"2012","journal-title":"J. Alzheimers Dis."},{"key":"10.1016\/j.ejmech.2024.116569_bib243","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2021.113874","article-title":"Inhibition of Histone Deacetylase 6 (HDAC6) as a therapeutic strategy for Alzheimer's disease: a review (2010\u20132020)","volume":"226","author":"Li","year":"2021","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib244","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1080\/13880209.2018.1563620","article-title":"Inhibition of HDAC6 alleviating lipopolysaccharide-induced p38MAPK phosphorylation and neuroinflammation in mice","volume":"57","author":"Song","year":"2019","journal-title":"Pharm. Biol."},{"key":"10.1016\/j.ejmech.2024.116569_bib245","doi-asserted-by":"crossref","first-page":"243","DOI":"10.3389\/fnins.2016.00243","article-title":"CB2 cannabinoid receptor as potential target against Alzheimer's disease","volume":"10","author":"Aso","year":"2016","journal-title":"Front. Neurosci."},{"key":"10.1016\/j.ejmech.2024.116569_bib246","doi-asserted-by":"crossref","first-page":"9913","DOI":"10.1021\/acs.jmedchem.7b00155","article-title":"Perspectives of cannabinoid type 2 receptor (CB2R) ligands in neurodegenerative disorders: structure\u2013affinity relationship (SAfiR) and structure\u2013activity relationship (SAR) studies: miniperspective","volume":"60","author":"Spinelli","year":"2017","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib247","doi-asserted-by":"crossref","first-page":"2888","DOI":"10.1002\/jnr.24933","article-title":"Cannabinoid receptor 2 selective agonists and Alzheimer's disease: an insight into the therapeutic potentials","volume":"99","author":"Magham","year":"2021","journal-title":"J. Neurosci. Res."},{"key":"10.1016\/j.ejmech.2024.116569_bib248","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1016\/j.neurobiolaging.2012.06.005","article-title":"CB2 receptor and amyloid pathology in frontal cortex of Alzheimer's disease patients","volume":"34","author":"Solas","year":"2013","journal-title":"Neurobiol. Aging"},{"key":"10.1016\/j.ejmech.2024.116569_bib249","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.tips.2006.11.001","article-title":"Cannabinoid CB2 receptor: a new target for controlling neural cell survival?","volume":"28","author":"Fern\u00e1ndez-Ruiz","year":"2007","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.ejmech.2024.116569_bib250","doi-asserted-by":"crossref","first-page":"4731","DOI":"10.1007\/s12035-017-0676-2","article-title":"Deletion of type-2 cannabinoid receptor induces Alzheimer's disease-like tau pathology and memory impairment through AMPK\/GSK3\u03b2 pathway","volume":"55","author":"Wang","year":"2018","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.ejmech.2024.116569_bib251","doi-asserted-by":"crossref","first-page":"29","DOI":"10.2119\/molmed.2013.00140.revised","article-title":"CB2 receptor deficiency increases amyloid pathology and alters tau processing in a transgenic mouse model of Alzheimer's disease","volume":"20","author":"Koppel","year":"2014","journal-title":"Mol. Med."},{"key":"10.1016\/j.ejmech.2024.116569_bib252","doi-asserted-by":"crossref","DOI":"10.1016\/j.neulet.2019.134286","article-title":"CB2 cannabinoid receptor agonist ameliorates novel object recognition but not spatial memory in transgenic APP\/PS1 mice","volume":"707","author":"Li","year":"2019","journal-title":"Neurosci. Lett."},{"key":"10.1016\/j.ejmech.2024.116569_bib253","doi-asserted-by":"crossref","first-page":"1938","DOI":"10.1007\/s12035-019-01813-4","article-title":"Targeting cannabinoid receptor activation and BACE-1 activity counteracts TgAPP mice memory impairment and Alzheimer's disease lymphoblast alterations","volume":"57","author":"Nu\u00f1ez-Borque","year":"2020","journal-title":"Mol. Neurobiol."},{"key":"10.1016\/j.ejmech.2024.116569_bib254","doi-asserted-by":"crossref","first-page":"9078","DOI":"10.1021\/acs.jmedchem.9b00623","article-title":"Dual-acting cholinesterase\u2013human cannabinoid receptor 2 ligands show pronounced neuroprotection in vitro and overadditive and disease-modifying neuroprotective effects in vivo","volume":"62","author":"Scheiner","year":"2019","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.ejmech.2024.116569_bib255","doi-asserted-by":"crossref","first-page":"721","DOI":"10.1016\/j.phrs.2016.07.021","article-title":"Type-2 cannabinoid receptors in neurodegeneration","volume":"111","author":"Bisogno","year":"2016","journal-title":"Pharmacol. Res."},{"key":"10.1016\/j.ejmech.2024.116569_bib256","doi-asserted-by":"crossref","first-page":"6414","DOI":"10.1021\/acs.jmedchem.3c00541","article-title":"Dual-acting small molecules: subtype-selective cannabinoid receptor 2 agonist\/butyrylcholinesterase inhibitor hybrids show neuroprotection in an Alzheimer's disease mouse model","volume":"66","author":"Spatz","year":"2023","journal-title":"J. Med. Chem."}],"container-title":["European Journal of Medicinal Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523424004495?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0223523424004495?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,7,8]],"date-time":"2024-07-08T13:25:25Z","timestamp":1720445125000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0223523424004495"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,9]]},"references-count":256,"alternative-id":["S0223523424004495"],"URL":"https:\/\/doi.org\/10.1016\/j.ejmech.2024.116569","relation":{},"ISSN":["0223-5234"],"issn-type":[{"value":"0223-5234","type":"print"}],"subject":[],"published":{"date-parts":[[2024,9]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"New insights into butyrylcholinesterase: Pharmaceutical applications, selective inhibitors and multitarget-directed ligands","name":"articletitle","label":"Article Title"},{"value":"European Journal of Medicinal Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ejmech.2024.116569","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2024 Elsevier Masson SAS. All rights are reserved, including those for text and data mining, AI training, and similar technologies.","name":"copyright","label":"Copyright"}],"article-number":"116569"}}