{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,16]],"date-time":"2026-07-16T05:37:38Z","timestamp":1784180258201,"version":"3.55.0"},"reference-count":66,"publisher":"MDPI AG","issue":"17","license":[{"start":{"date-parts":[[2020,8,26]],"date-time":"2020-08-26T00:00:00Z","timestamp":1598400000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Cooperative Research Program for Agriculture Science and Technology Development","award":["PJ01319104"],"award-info":[{"award-number":["PJ01319104"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Molecules"],"abstract":"<jats:p>Eight compounds were isolated from the roots of Glycyrrhiza uralensis and tested for cholinesterase (ChE) and monoamine oxidase (MAO) inhibitory activities. The coumarin glycyrol (GC) effectively inhibited butyrylcholinesterase (BChE) and acetylcholinesterase (AChE) with IC50 values of 7.22 and 14.77 \u00b5M, respectively, and also moderately inhibited MAO-B (29.48 \u00b5M). Six of the other seven compounds only weakly inhibited AChE and BChE, whereas liquiritin apioside moderately inhibited AChE (IC50 = 36.68 \u00b5M). Liquiritigenin (LG) potently inhibited MAO-B (IC50 = 0.098 \u00b5M) and MAO-A (IC50 = 0.27 \u00b5M), and liquiritin, a glycoside of LG, weakly inhibited MAO-B (&gt;40 \u00b5M). GC was a reversible, noncompetitive inhibitor of BChE with a Ki value of 4.47 \u00b5M, and LG was a reversible competitive inhibitor of MAO-B with a Ki value of 0.024 \u00b5M. Docking simulations showed that the binding affinity of GC for BChE (\u22127.8 kcal\/mol) was greater than its affinity for AChE (\u22127.1 kcal\/mol), and suggested that GC interacted with BChE at Thr284 and Val288 by hydrogen bonds (distances: 2.42 and 1.92 \u00c5, respectively) beyond the ligand binding site of BChE, but that GC did not form hydrogen bond with AChE. The binding affinity of LG for MAO-B (\u22128.8 kcal\/mol) was greater than its affinity for MAO-A (\u22127.9 kcal\/mol). These findings suggest GC and LG should be considered promising compounds for the treatment of Alzheimer\u2019s disease with multi-targeting activities.<\/jats:p>","DOI":"10.3390\/molecules25173896","type":"journal-article","created":{"date-parts":[[2020,8,26]],"date-time":"2020-08-26T09:56:58Z","timestamp":1598435818000},"page":"3896","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":41,"title":["Inhibition of Butyrylcholinesterase and Human Monoamine Oxidase-B by the Coumarin Glycyrol and Liquiritigenin Isolated from Glycyrrhiza uralensis"],"prefix":"10.3390","volume":"25","author":[{"given":"Geum Seok","family":"Jeong","sequence":"first","affiliation":[{"name":"Department of Pharmacy, and Research Institute of Life Pharmaceutical Sciences, Sunchon National University, Suncheon 57922, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Myung-Gyun","family":"Kang","sequence":"additional","affiliation":[{"name":"Department of Predictive Toxicology, Korea Institute of Toxicology, Daejeon 34114, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joon Yeop","family":"Lee","sequence":"additional","affiliation":[{"name":"National Institute for Korean Medicine Development, Gyeongsan 38540, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sang Ryong","family":"Lee","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, and Research Institute of Life Pharmaceutical Sciences, Sunchon National University, Suncheon 57922, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9452-5849","authenticated-orcid":false,"given":"Daeui","family":"Park","sequence":"additional","affiliation":[{"name":"Department of Predictive Toxicology, Korea Institute of Toxicology, Daejeon 34114, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"MyoungLae","family":"Cho","sequence":"additional","affiliation":[{"name":"National Institute for Korean Medicine Development, Gyeongsan 38540, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-7203-3712","authenticated-orcid":false,"given":"Hoon","family":"Kim","sequence":"additional","affiliation":[{"name":"Department of Pharmacy, and Research Institute of Life Pharmaceutical Sciences, Sunchon National University, Suncheon 57922, Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2020,8,26]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1046\/j.1471-4159.1995.64020749.x","article-title":"Neurochemical correlates of dementia severity in Alzheimer\u2019s disease: Relative importance of the cholinergic deficits","volume":"64","author":"Bierer","year":"1995","journal-title":"J. Neurochem."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"315","DOI":"10.2174\/1570159X11311030006","article-title":"Acetylcholinesterase inhibitors: Pharmacology and toxicology","volume":"11","year":"2013","journal-title":"Curr. Neuropharmacol."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"375","DOI":"10.1007\/s12272-013-0036-3","article-title":"A review on cholinesterase inhibitors for Alzheimer\u2019s disease","volume":"36","author":"Anand","year":"2013","journal-title":"Arch. Pharm. Res."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Ghai, R., Nagarajan, K., Arora, M., Grover, P., Ali, N., and Kapoor, G. (2020). Current strategies and novel drug approaches for Alzheimer disease. CNS Neurol. Disord. Drug Targets.","DOI":"10.2174\/1871527319666200717091513"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"4424","DOI":"10.1038\/s41598-018-22747-2","article-title":"Novel 2-phenylbenzofuran derivatives as selective butyrylcholinesterase inhibitors for Alzheimer\u2019s disease","volume":"8","author":"Kumar","year":"2018","journal-title":"Sci. Rep."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/j.neuroscience.2017.06.034","article-title":"Newly developed drugs for Alzheimer\u2019s disease in relation to energy metabolism, cholinergic and monoaminergic neurotransmission","volume":"370","year":"2018","journal-title":"Neuroscience"},{"key":"ref_7","first-page":"197","article-title":"BChE reported to be associated with plaque level in Alzheimer\u2019s disease","volume":"7","author":"Lake","year":"2013","journal-title":"Biomark. Med."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"2189","DOI":"10.2174\/156802612805219978","article-title":"Monoamine oxidases: The biochemistry of the proteins as targets in medicinal chemistry and drug discovery","volume":"12","author":"Ramsay","year":"2012","journal-title":"Curr. Top. Med. Chem."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1038\/nrn1883","article-title":"The therapeutic potential of monoamine oxidase inhibitors","volume":"7","author":"Youdim","year":"2006","journal-title":"Nat. Rev. Neurosci."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1186\/s13195-017-0279-1","article-title":"Monoamine oxidase B is elevated in Alzheimer disease neurons, is associated with \u03b3-secretase and regulates neuronal amyloid \u03b2-peptide levels","volume":"9","author":"Inoue","year":"2017","journal-title":"Alzheimers Res. Ther."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Ramsay, R.R., and Tipton, K.F. (2017). Assessment of enzyme inhibition: A review with examples from the development of monoamine oxidase and cholinesterase inhibitory drugs. Molecules, 22.","DOI":"10.20944\/preprints201707.0019.v1"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"714","DOI":"10.1016\/j.bmc.2016.11.048","article-title":"Multitarget drug design strategy against Alzheimer\u2019s disease: Homoisoflavonoid mannich base derivatives serve as acetylcholinesterase and monoamine oxidase B dual inhibitors with multifunctional properties","volume":"25","author":"Li","year":"2017","journal-title":"Bioorg. Med. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/j.ejmech.2018.08.005","article-title":"Donepezil-butylated hydroxytoluene (BHT) hybrids as anti-Alzheimer\u2019s disease agents with cholinergic, antioxidant, and neuroprotective properties","volume":"157","author":"Cai","year":"2018","journal-title":"Eur. J. Med. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"512","DOI":"10.1016\/j.bioorg.2018.09.010","article-title":"Coumarin-dithiocarbamate hybrids as novel multitarget AChE and MAO-B inhibitors against Alzheimer\u2019s disease: Design, synthesis and biological evaluation","volume":"81","author":"He","year":"2018","journal-title":"Bioorg. Chem."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"292","DOI":"10.1016\/j.ejmech.2018.10.016","article-title":"Investigating alkyl nitrates as nitric oxide releasing precursors of multitarget acetylcholinesterase-monoamine oxidase B inhibitors","volume":"161","author":"Pisani","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Oh, J.M., Rangarajan, T.M., Chaudhary, R., Singh, R.P., Singh, M., Singh, R.P., Tondo, A.R., Gambacorta, N., Nicolotti, O., and Mathew, B. (2020). Novel class of chalcone oxime ethers as potent monoamine oxidase-B and acetylcholinesterase inhibitors. Molecules, 25.","DOI":"10.3390\/molecules25102356"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Mascarenhas, A.M.S., de Almeida, R.B.M., de Araujo Neto, M.F., Mendes, G.O., da Cruz, J.N., Dos Santos, C.B.R., Botura, M.B., and Leite, F.H.A. (2020). Pharmacophore-based virtual screening and molecular docking to identify promising dual inhibitors of human acetylcholinesterase and butyrylcholinesterase. J. Biomol. Struct. Dyn.","DOI":"10.1080\/07391102.2020.1796791"},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1111\/jphp.13244","article-title":"TV 3326 for Alzheimer\u2019s dementia: A novel multimodal ChE and MAO inhibitors to mitigate Alzheimer\u2019s-like neuropathology","volume":"72","author":"Uddin","year":"2020","journal-title":"J. Pharm. Pharmcol."},{"key":"ref_19","doi-asserted-by":"crossref","unstructured":"Purgatorio, R., Kulikova, L., Pisani, L., Catto, M., de Candia, M., Carrieri, A., Cellamare, S., De Palma, A., Beloglazkin, A., and Raesi, G.R. (2020). Scouting around 1,2,3,4-Tetrahydrochromeno[3,2-c]pyridin-10-ones for single- and multi-target ligands directed towards relevant Alzheimer\u2019s targets. ChemMedChem.","DOI":"10.1002\/cmdc.202000468"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1097\/CAD.0b013e3282fba582","article-title":"Gene induction by glycyrol to apoptosis through endonuclease G in tumor cells and prediction of oncogene function by microarray analysis","volume":"19","author":"Lee","year":"2008","journal-title":"Anticancer Drugs"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1016\/j.fct.2014.10.023","article-title":"Antitumor activity of glycyrol via induction of cell cycle arrest, apoptosis and defective autophagy","volume":"74","author":"Xu","year":"2014","journal-title":"Food Chem. Toxicol."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"104366","DOI":"10.1016\/j.phrs.2019.104366","article-title":"Glycyrol exerts potent therapeutic effect on lung cancer via directly inactivating T-LAK cell-originated protein kinase","volume":"147","author":"Lu","year":"2019","journal-title":"Pharmacol. Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1482","DOI":"10.1007\/s12272-016-0824-7","article-title":"Synergic effect of combination of glycyrol and fluconazole against experimental cutaneous candidiasis due to Candida albicans","volume":"39","author":"Rhew","year":"2016","journal-title":"Arch. Pharm. Res."},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"270","DOI":"10.3177\/jnsv.47.270","article-title":"Antibacterial compounds of licorice against upper airway respiratory tract pathogens","volume":"47","author":"Tanaka","year":"2001","journal-title":"J. Nutr. Sci. Vitaminol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"971","DOI":"10.1016\/j.bmcl.2009.12.106","article-title":"Inhibition of neuraminidase activity by polyphenol compounds isolated from the roots of Glycyrrhiza uralensis","volume":"20","author":"Ryu","year":"2010","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"180","DOI":"10.1111\/1348-0421.12127","article-title":"Anti-hepatitis C virus compounds obtained from Glycyrrhiza uralensis and other Glycyrrhiza species","volume":"58","author":"Adianti","year":"2014","journal-title":"Microbiol. Immunol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"1524","DOI":"10.1016\/j.intimp.2008.06.008","article-title":"Anti-inflammatory effects of glycyrol isolated from Glycyrrhiza uralensis in LPS-stimulated RAW264.7 macrophages","volume":"8","author":"Shin","year":"2008","journal-title":"Int. Immunopharmacol."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Fu, Y., Zhou, H., Wang, S., and Wei, Q. (2014). Glycyrol suppresses collagen-induced arthritis by regulating autoimmune and inflammatory responses. PLoS ONE, 9.","DOI":"10.1371\/journal.pone.0098137"},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"1593","DOI":"10.1002\/jssc.201901013","article-title":"Metabolomics study of different parts of licorice from different geographical origins and their anti-inflammatory activities","volume":"43","author":"Bai","year":"2020","journal-title":"J. Sep. Sci."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1177","DOI":"10.3109\/13880200903573169","article-title":"Immunosuppressive activity on the murine immune responses of glycyrol from Glycyrrhiza uralensis via inhibition of calcineurin activity","volume":"48","author":"Li","year":"2010","journal-title":"Pharm. Biol."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1055\/s-2006-962604","article-title":"Isolation of monoamine oxidase inhibitors from Glycyrrhiza uralensis roots and the structure-activity relationship","volume":"53","author":"Tanaka","year":"1987","journal-title":"Planta Med."},{"key":"ref_32","first-page":"949","article-title":"In vitro inhibition of rat monoamine oxidase by liquiritigenin and isoliquiritigenin isolated from Sinofranchetia chinensis","volume":"21","author":"Pan","year":"2000","journal-title":"Acta Pharmacol. Sin."},{"key":"ref_33","first-page":"33","article-title":"Tyrosinase inhibitors isolated from the roots of Glycyrrhiza glabra L.","volume":"34","author":"Lee","year":"2003","journal-title":"Korean J. Pharmacogn."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.phytochem.2009.09.014","article-title":"Bioactive microbial metabolites from glycyrrhetinic acid","volume":"71","author":"Maatooq","year":"2010","journal-title":"Phytochemistry"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"535","DOI":"10.1016\/j.jpba.2010.10.004","article-title":"Metabolic profiling of roots of liquorice (Glycyrrhiza glabra) from different geographical areas by ESI\/MS\/MS and determination of major metabolites by LC-ESI\/MS and LC-ESI\/MS\/MS","volume":"54","author":"Montoro","year":"2011","journal-title":"J. Pharm. Biomed. Anal."},{"key":"ref_36","first-page":"4155","article-title":"Study on active constituents from Glycyrrhizae Radix et Rhizoma against NO production in LPS-induced Raw 264.7 macrophages","volume":"47","author":"Wang","year":"2016","journal-title":"Chin. Tradit. Herb. Drugs"},{"key":"ref_37","first-page":"104","article-title":"NMR analysis and hydrolysis studies of glycyrrhizin acid, a major constituent of Glycyrrhia glabra","volume":"3","author":"Chaturvedula","year":"2014","journal-title":"Eur. Chem. Bull."},{"key":"ref_38","first-page":"11e23","article-title":"Coumarins as cholinesterase inhibitors: A review","volume":"254","author":"Renn","year":"2016","journal-title":"Chem. Biol. Interact."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1083","DOI":"10.1080\/14756366.2019.1615484","article-title":"Synthesis and biological evaluation of 3\u2013(4-aminophenyl)-coumarin derivatives as potential anti-Alzheimer\u2019s disease agents","volume":"34","author":"Hu","year":"2019","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"4248","DOI":"10.1016\/j.bmcl.2013.04.081","article-title":"New bioactive dihydrofuranocoumarins from the roots of the Tunisian Ferula lutea (Poir.) maire","volume":"23","author":"Salem","year":"2013","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"7873","DOI":"10.1016\/j.bmc.2010.09.044","article-title":"4-Phenylcoumarins from Mesua elegans with acetylcholinesterase inhibitory activity","volume":"18","author":"Awang","year":"2010","journal-title":"Bioorg. Med. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1192","DOI":"10.3389\/fphar.2018.01192","article-title":"Naturally occurring acetylcholinesterase inhibitors and their potential use for Alzheimer\u2019s disease therapy","volume":"9","author":"Gomes","year":"2018","journal-title":"Front. Pharmacol."},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1016\/j.bmcl.2019.01.016","article-title":"Osthenol, a prenylated coumarin, as a monoamine oxidase A inhibitor with high selectivity","volume":"29","author":"Baek","year":"2019","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_44","first-page":"675e683","article-title":"Anticholinesterase furocoumarins from heracleumplatytaenium, a species endemic to the Ida mountains","volume":"37","author":"Dincel","year":"2013","journal-title":"Turk. J. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"9634349","DOI":"10.1155\/2018\/9634349","article-title":"Inhibition of acetylcholinesterase and butyrylcholinesterase by a plant secondary metabolite boldine","volume":"2018","author":"Kostelnik","year":"2018","journal-title":"Biomed. Res. Int."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"e1900017","DOI":"10.1002\/cbdv.201900017","article-title":"Profiling auspicious butyrylcholinesterase inhibitory activity of two herbal molecules: Hyperforin and hyuganin C","volume":"16","author":"Orhan","year":"2019","journal-title":"Chem. Biodivers."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Liu, L., Yin, Q.M., Gao, Q., Li, J., Jiang, Y., and Tu, P.F. (2019). New biphenanthrenes with butyrylcholinesterase inhibitory activity from Cremastra appendiculata. Nat. Prod. Res., 1\u20137.","DOI":"10.1080\/14786419.2019.1601091"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2633105520937693","DOI":"10.1177\/2633105520937693","article-title":"Scopoletin: Antiamyloidogenic, anticholinesterase, and neuroprotective potential of a natural compound present in argyreia speciosa roots by in vitro and in silico study","volume":"15","author":"Kashyap","year":"2020","journal-title":"Neurosci. Insights"},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"103043","DOI":"10.1016\/j.bioorg.2019.103043","article-title":"Potent inhibition of acetylcholinesterase by sargachromanol I from Sargassum siliquastrum and by selected natural compounds","volume":"89","author":"Lee","year":"2019","journal-title":"Bioorg. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","unstructured":"\u015alusarczyk, S., Senol Deniz, F.S., Abel, R., Pecio, \u0141., P\u00e9rez-S\u00e1nchez, H., Cer\u00f3n-Carrasco, J.P., den-Haan, H., Banerjee, P., Preissner, R., and Krzy\u017cak, E. (2020). Norditerpenoids with selective anti-cholinesterase activity from the roots of perovskia atriplicifolia benth. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21124475"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"e22340","DOI":"10.1002\/jbt.22340","article-title":"Tannic acid as a natural antioxidant compound: Discovery of a potent metabolic enzyme inhibitor for a new therapeutic approach in diabetes and Alzheimer\u2019s disease","volume":"33","author":"Taslimi","year":"2019","journal-title":"J. Biochem. Mol. Toxicol."},{"key":"ref_52","doi-asserted-by":"crossref","unstructured":"Taslimi, P., Caglayan, C., and Gulcin, \u0130. (2017). The impact of some natural phenolic compounds on carbonic anhydrase, acetylcholinesterase, butyrylcholinesterase, and \u03b1-glycosidase enzymes: An antidiabetic, anticholinergic, and antiepileptic study. Biochem. Mol. Toxicol.","DOI":"10.1002\/jbt.21995"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1016\/j.ijbiomac.2017.06.076","article-title":"Potent inhibitions of monoamine oxidase A and B by acacetin and its 7-O-(6-O-malonylglucoside) derivative from Agastache rugosa","volume":"104","author":"Lee","year":"2017","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_54","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. Med. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"12074","DOI":"10.1021\/bi00096a018","article-title":"Three distinct domains in the cholinesterase molecule confer selectivity for acetyl- and butyrylcholinesterase inhibitors","volume":"32","author":"Radic","year":"1993","journal-title":"Biochemistry"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1038\/s12276-019-0205-7","article-title":"Inhibition of \u03b2-site amyloid precursor protein cleaving enzyme 1 and cholinesterases by pterosins via a specific structure-activity relationship with a strong BBB permeability","volume":"51","author":"Jannat","year":"2019","journal-title":"Exp. Mol. Med."},{"key":"ref_57","doi-asserted-by":"crossref","first-page":"e01552","DOI":"10.1016\/j.heliyon.2019.e01552","article-title":"Coumarin derivatives as acetyl- and butyrylcholinesterase inhibitors: An in vitro, molecular docking, and molecular dynamics simulations study","volume":"5","author":"Mustafa","year":"2019","journal-title":"Heliyon"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"317","DOI":"10.1016\/j.bioorg.2018.10.051","article-title":"Rhamnocitrin isolated from Prunus padus var. seoulensis: A potent and selective reversible inhibitor of human monoamine oxidase A","volume":"83","author":"Baek","year":"2019","journal-title":"Bioorg. Chem."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"584","DOI":"10.1016\/j.bmcl.2018.01.049","article-title":"Selective inhibition of monoamine oxidase A by hispidol","volume":"28","author":"Baek","year":"2018","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"4714","DOI":"10.1016\/j.bmcl.2016.08.044","article-title":"Potent selective monoamine oxidase B inhibition by maackiain, a pterocarpan from the roots of Sophora flavescens","volume":"26","author":"Lee","year":"2016","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"187","DOI":"10.3839\/jabc.2018.027","article-title":"Inhibition of monoamine oxidase A and B by demethoxycurcumin and bisdemethoxycurcumin","volume":"61","author":"Baek","year":"2018","journal-title":"J. Appl. Biol. Chem."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/0006-2952(61)90145-9","article-title":"A new and rapid colorimetric determination of acetylcholinesterase activity","volume":"7","author":"Ellman","year":"1961","journal-title":"Biochem. Pharmacol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1016\/j.ijbiomac.2019.06.167","article-title":"Potent and selective inhibition of human monoamine oxidase-B by 4-dimethylaminochalcone and selected chalcone derivatives","volume":"137","author":"Oh","year":"2019","journal-title":"Int. J. Biol. Macromol."},{"key":"ref_64","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1002\/jcc.21334","article-title":"AutoDock Vina: Improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading","volume":"31","author":"Trott","year":"2010","journal-title":"J. Comput. Chem."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1605","DOI":"10.1002\/jcc.20084","article-title":"UCSF Chimera\u2014A visualization system for exploratory research and analysis","volume":"25","author":"Pettersen","year":"2004","journal-title":"J. Comput. Chem."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"607","DOI":"10.1007\/BF00134183","article-title":"Three-dimensional hydrogen-bond geometry and probability information from a crystal survey","volume":"10","author":"Mills","year":"1996","journal-title":"J. Comput. Aided Mol. Des."}],"container-title":["Molecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1420-3049\/25\/17\/3896\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,11]],"date-time":"2025-10-11T10:07:10Z","timestamp":1760177230000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1420-3049\/25\/17\/3896"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2020,8,26]]},"references-count":66,"journal-issue":{"issue":"17","published-online":{"date-parts":[[2020,9]]}},"alternative-id":["molecules25173896"],"URL":"https:\/\/doi.org\/10.3390\/molecules25173896","relation":{"has-preprint":[{"id-type":"doi","id":"10.20944\/preprints202008.0306.v1","asserted-by":"object"}]},"ISSN":["1420-3049"],"issn-type":[{"value":"1420-3049","type":"electronic"}],"subject":[],"published":{"date-parts":[[2020,8,26]]}}}