{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,3]],"date-time":"2026-09-03T11:06:46Z","timestamp":1788433606850,"version":"build-2803163510"},"reference-count":60,"publisher":"MDPI AG","issue":"19","license":[{"start":{"date-parts":[[2024,9,29]],"date-time":"2024-09-29T00:00:00Z","timestamp":1727568000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Ministry of Education, Science, and Technology","award":["RS-2023-00253188"],"award-info":[{"award-number":["RS-2023-00253188"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Amyloid \u03b2 protein (A\u03b2) deposition has been implicated as the molecular driver of Alzheimer\u2019s disease (AD) progression. The modulation of the formation of abnormal aggregates and their post-translational modification is strongly suggested as the most effective approach to anti-AD. Beta-site APP-cleaving enzyme 1 (BACE1) acts upstream in amyloidogenic processing to generate A\u03b2, which rapidly aggregates alone or in combination with acetylcholinesterase (AChE) to form fibrils. Accumulated A\u03b2 promotes BACE1 activation via glycogen synthase kinase-3\u03b2 (GSK-3\u03b2) and is post-translationally modified by glutaminyl cyclase (QC), resulting in increased neurotoxicity. A novel multi-target inhibitor as a potential AD agent was identified using an in silico approach and experimental validation. Magnolia officinalis, which showed the best anti-AD activity in our preliminary study, was subjected to analysis, and 82 compounds were studied. Among 23 compounds with drug-likeness, blood\u2013brain barrier penetration, and safety, honokiol emerged as a lead structure for the inhibition of BACE1, AChE, QC, and GSK-3\u03b2 in docking and molecular dynamics (MD) simulations. Furthermore, honokiol was found to be an excellent multi-target inhibitor of these enzymes with an IC50 of 6\u201390 \u03bcM, even when compared to other natural single-target inhibitors. Taken together, the present study is the first to demonstrate that honokiol acts as a multiple enzyme inhibitor with an excellent pharmacokinetic and safety profile which may provide inhibitory effects in broad-range areas including the overproduction, aggregation, and post-translational modification of A\u03b2. It also provides insight into novel structural features for the design and discovery of multi-target inhibitors for anti-AD.<\/jats:p>","DOI":"10.3390\/ijms251910507","type":"journal-article","created":{"date-parts":[[2024,9,30]],"date-time":"2024-09-30T03:12:28Z","timestamp":1727665948000},"page":"10507","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":6,"title":["Determination of Potential Lead Compound from Magnolia officinalis for Alzheimer\u2019s Disease through Pharmacokinetic Prediction, Molecular Docking, Dynamic Simulation, and Experimental Validation"],"prefix":"10.3390","volume":"25","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-3124-2665","authenticated-orcid":false,"given":"Kumju","family":"Youn","sequence":"first","affiliation":[{"name":"Department of Food Science and Nutrition, Dong-A University, Busan 49315, Republic of Korea"},{"name":"Center for Food & Bio Innovation, Dong-A University, Busan 49315, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mira","family":"Jun","sequence":"additional","affiliation":[{"name":"Department of Food Science and Nutrition, Dong-A University, Busan 49315, Republic of Korea"},{"name":"Center for Food & Bio Innovation, Dong-A University, Busan 49315, Republic of Korea"},{"name":"Department of Health Sciences, The Graduate School of Dong-A University, Busan 49315, Republic of Korea"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2024,9,29]]},"reference":[{"key":"ref_1","unstructured":"(2024, February 27). World Health Organization. Available online: https:\/\/www.who.int\/news-room\/fact-sheets\/detail\/dementia."},{"key":"ref_2","unstructured":"Lazarov, O., and Tesco, G. (2016). Molecular mechanisms of learning and memory. Genes, Environment and Alzheimer\u2019s Disease, Academic Press."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"258","DOI":"10.1016\/j.ejmech.2016.02.049","article-title":"Amyloid cascade in Alzheimer\u2019s disease: Recent advances in medicinal chemistry","volume":"113","author":"Mohamed","year":"2016","journal-title":"Eur. J. Med. Chem."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1080\/13543784.2019.1683160","article-title":"Investigational BACE inhibitors for the treatment of Alzheimer\u2019s disease","volume":"28","author":"Imbimbo","year":"2019","journal-title":"Expert Opin. Investig. Drugs"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1021\/cn500016p","article-title":"Acetylcholinesterase inhibitors with photoswitchable inhibition of beta-amyloid aggregation","volume":"5","author":"Chen","year":"2014","journal-title":"ACS Chem. Neurosci."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"32","DOI":"10.1186\/s13024-019-0333-5","article-title":"The neuropathological diagnosis of Alzheimer\u2019s disease","volume":"14","author":"Deture","year":"2019","journal-title":"Mol. Neurodegener."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"2158822","DOI":"10.1080\/14756366.2022.2158822","article-title":"New cyclopentaquinoline and 3,5-dichlorobenzoic acid hybrids with neuroprotection against oxidative stress for the treatment of Alzheimer\u2019s disease","volume":"38","author":"Czarnecka","year":"2023","journal-title":"J. Enzym. Inhib. Med. Chem."},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"100170","DOI":"10.1016\/j.snr.2023.100170","article-title":"Patterning amyloid-\u03b2 aggregation under the effect of acetylcholinesterase using a biological nanopore\u2014An in vitro study","volume":"6","author":"Subramanian","year":"2023","journal-title":"Sens. Actuators Rep."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"4","DOI":"10.1186\/1750-1326-5-4","article-title":"Amyloid-beta-acetylcholinesterase complexes potentiate neurodegenerative changes induced by the abeta peptide","volume":"5","author":"Dinamarca","year":"2010","journal-title":"Mol. Neurodegener."},{"key":"ref_10","doi-asserted-by":"crossref","unstructured":"Barykin, E.P., Mitkevich, V.A., Kozin, S.A., and Makarov, A.A. (2017). Amyloid \u03b2 modification: A key to the sporadic Alzheimer\u2019s Disease?. Front. Genet., 8.","DOI":"10.3389\/fgene.2017.00058"},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"6134","DOI":"10.1074\/jbc.M115.655183","article-title":"Amyloid-\u03b2 peptide a\u03b23pE-42 induces lipid peroxidation, membrane permeabilization, and calcium influx in neurons","volume":"291","author":"Gunn","year":"2016","journal-title":"J. Biol. Chem."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"4454","DOI":"10.1074\/jbc.M110.185819","article-title":"Overexpression of glutaminyl cyclase, the enzyme responsible for pyroglutamate A{beta} formation, induces behavioral deficits, and glutaminyl cyclase knock-out rescues the behavioral phenotype in 5XFAD mice","volume":"286","author":"Jawhar","year":"2011","journal-title":"J. Biol. Chem."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1186\/s13195-017-0317-z","article-title":"Neurons derived from sporadic Alzheimer\u2019s disease iPSCs reveal elevated TAU hyperphosphorylation, increased amyloid levels, and GSK3B activation","volume":"9","author":"Ochalek","year":"2017","journal-title":"Alzheimer\u2019s Res. Ther."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"1183","DOI":"10.1038\/s41593-020-0687-6","article-title":"Synergy between amyloid-\u03b2 and tau in Alzheimer\u2019s disease","volume":"23","author":"Busche","year":"2020","journal-title":"Nat. Neurosci."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1111\/j.1365-2990.2006.00795.x","article-title":"Increased level of active GSK-3beta in Alzheimer\u2019s disease and accumulation in argyrophilic grains and neurons at different stages of neurofibrillary degeneration","volume":"33","author":"Leroy","year":"2007","journal-title":"Neuropathol. Appl. Neurobiol."},{"key":"ref_16","doi-asserted-by":"crossref","unstructured":"Lauretti, E., Dincer, O., and Pratic\u00f2, D. (2020). Glycogen synthase kinase-3 signaling in Alzheimer\u2019s disease. Biochim. Biophys. Acta Mol. Cell Res., 1867.","DOI":"10.1016\/j.bbamcr.2020.118664"},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1017\/S1461145711000149","article-title":"Increased NF-\u03baB signalling up-regulates BACE1 expression and its therapeutic potential in Alzheimer\u2019s disease","volume":"15","author":"Chen","year":"2012","journal-title":"Int. J. Neuropsychopharmacol."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1172\/JCI64516","article-title":"Inhibition of GSK3\u03b2-mediated BACE1 expression reduces Alzheimer-associated phenotypes","volume":"123","author":"Ly","year":"2013","journal-title":"J. Clin. Investig."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"194","DOI":"10.1631\/jzus.B1600299","article-title":"Biological activity and toxicity of the Chinese herb Magnolia officinalis Rehder & E. Wilson (Houpo) and its constituents","volume":"18","author":"Poivre","year":"2017","journal-title":"J. Zhejiang Univ. Sci. B"},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"1210","DOI":"10.1093\/jaoac\/90.5.1219","article-title":"Liquid chromatographic determination of honokiol and magnolol in hou po (Magnolia officinalis) as the raw herb and dried aqueous extract","volume":"90","author":"Lee","year":"2007","journal-title":"J. AOAC Int."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"1151","DOI":"10.1055\/a-0642-1966","article-title":"Safety and toxicology of magnolol and honokiol","volume":"84","author":"Sarrica","year":"2018","journal-title":"Planta Med."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"438","DOI":"10.1002\/ptr.4740","article-title":"Ethanol extract of Magnolia officinalis prevents llipopolysaccharide-induced memory deficiency via its antineuroinflammatory and antiamyloidogenic effects","volume":"27","author":"Lee","year":"2013","journal-title":"Phytother. Res."},{"key":"ref_23","doi-asserted-by":"crossref","first-page":"1147","DOI":"10.1248\/yakushi.15-00197","article-title":"Search of neurotrophin-mimic natural products for prevention and treatment of neurodegenerative disease","volume":"135","author":"Kubo","year":"2015","journal-title":"Yakugaku Zasshi"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"102398","DOI":"10.1016\/j.arr.2024.102398","article-title":"Neolignans in Magnolia officinalis as natural anti-Alzheimer\u2019s disease agents: A systematic review","volume":"99","author":"Li","year":"2024","journal-title":"Ageing Res. Rev."},{"key":"ref_25","doi-asserted-by":"crossref","unstructured":"Zhu, S., Liu, F., Zhang, R., Xiong, Z., Zhang, Q., Hao, L., and Chen, S. (2022). Neuroprotective potency of neolignans in Magnolia officinalis cortex against brain disorders. Front. Pharmacol., 13.","DOI":"10.3389\/fphar.2022.857449"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1002\/biof.1385","article-title":"Neuroprotective effects of honokiol: From chemistry to medicine","volume":"43","author":"Talarek","year":"2017","journal-title":"Biofactors"},{"key":"ref_27","doi-asserted-by":"crossref","unstructured":"Kim, S.K., Lee, M.K., Jang, H., Lee, J.J., Lee, S., Jang, Y., Jang, H., and Kim, A. (2024). TM-MC 2.0: An enhanced chemical database of medicinal materials in Northeast Asian traditional medicine. BMC Complement. Med. Ther., 24.","DOI":"10.1186\/s12906-023-04331-y"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1186\/s12987-020-00230-3","article-title":"A blood-brain barrier overview on structure, function, impairment, and biomarkers of integrity","volume":"17","author":"Kadry","year":"2020","journal-title":"Fluids. Barriers. CNS"},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Shi, S., Zhao, S., Tian, X., Liu, F., Lu, X., Zang, H., Li, F., Xiang, L., Li, L., and Jiang, S. (2023). Molecular and metabolic mechanisms of bufalin against lung adenocarcinoma: New and comprehensive evidences from network pharmacology, metabolomics and molecular biology experiment. Comput. Biol. Med., 157.","DOI":"10.1016\/j.compbiomed.2023.106777"},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.jmgm.2012.12.010","article-title":"Elucidating the catalytic mechanism of \u03b2-secretase (BACE1): A quantum mechanics\/molecular mechanics (QM\/MM) approach","volume":"40","author":"Barman","year":"2013","journal-title":"J. Mol. Graph. Model."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"197","DOI":"10.1016\/j.ejmech.2017.09.022","article-title":"New pyridine derivatives as inhibitors of acetylcholinesterase and amyloid aggregation","volume":"141","author":"Pandolfi","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"13117","DOI":"10.1073\/pnas.0504184102","article-title":"Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation","volume":"102","author":"Huang","year":"2005","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_33","first-page":"381029","article-title":"Small-molecule inhibitors of GSK-3: Structural insights and their application to Alzheimer\u2019s disease models","volume":"2012","author":"Kramer","year":"2012","journal-title":"Int. J. Alzheimer\u2019s Dis."},{"key":"ref_34","doi-asserted-by":"crossref","unstructured":"Mart\u00ednez, L. (2015). Automatic identification of mobile and rigid substructures in molecular dynamics simulations and fractional structural fluctuation analysis. PLoS ONE, 10.","DOI":"10.1371\/journal.pone.0119264"},{"key":"ref_35","doi-asserted-by":"crossref","unstructured":"Baier, A., and Szyszka, R. (2020). Compounds from Natural Sources as Protein Kinase Inhibitors. Biomolecules, 10.","DOI":"10.3390\/biom10111546"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Paudel, P., Seong, S.H., Zhou, Y., Park, C.H., Yokozawa, T., Jung, H.A., and Choi, J.S. (2018). Rosmarinic acid derivatives\u2019 inhibition of glycogen synthase kinase-3\u03b2 is the pharmacological basis of Kangen-karyu in Alzheimer\u2019s Disease. Molecules, 23.","DOI":"10.3390\/molecules23112919"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"68","DOI":"10.1016\/j.biochi.2024.05.002","article-title":"Natural compound screening predicts novel GSK-3 isoform-specific inhibitors","volume":"225","author":"Ahmad","year":"2024","journal-title":"Biochimie"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"819","DOI":"10.1016\/j.bbagen.2008.01.017","article-title":"Flavonols and flavones as BACE-1 inhibitors: Structure-activity relationship in cell-free, cell-based and in silico studies reveal novel pharmacophore features","volume":"1780","author":"Shimmyo","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"1399","DOI":"10.1007\/s12272-009-2009-0","article-title":"Cholinesterase and BACE1 inhibitory diterpenoids from Aralia cordata","volume":"32","author":"Jung","year":"2009","journal-title":"Arch. Pharm. Res."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"1316","DOI":"10.1055\/a-1019-9819","article-title":"Natural compounds with anti-BACE1 activity as promising therapeutic drugs for treating Alzheimer\u2019s Disease","volume":"85","author":"Naushad","year":"2019","journal-title":"Planta Med."},{"key":"ref_41","first-page":"100154","article-title":"Natural acetylcholinesterase inhibitors: A multi-targeted therapeutic potential in Alzheimer\u2019s disease","volume":"11","author":"Gajendra","year":"2024","journal-title":"Eur. J. Med. Chem. Rep."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Chen, D., Chen, Q., Qin, X., Tong, P., Peng, L., Zhang, T., and Xia, C. (2023). Development and evolution of human glutaminyl cyclase inhibitors (QCIs): An alternative promising approach for disease-modifying treatment of Alzheimer\u2019s disease. Front. Aging Neurosci., 15.","DOI":"10.3389\/fnagi.2023.1209863"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Hielscher-Michael, S., Griehl, C., Buchholz, M., Demuth, H.U., Arnold, N., and Wessjohann, L.A. (2019). Natural products from microalgae with potential against Alzheimer\u2019s disease: Sulfolipids are potent glutaminyl cyclase inhibitors. Mar. Drugs, 14.","DOI":"10.3390\/md14110203"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"2280","DOI":"10.1016\/j.bmc.2016.03.064","article-title":"Inhibitory effect of flavonoids on human glutaminyl cyclase","volume":"24","author":"Li","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"239","DOI":"10.1080\/07391102.2015.1022603","article-title":"Molecular docking based virtual screening of natural compounds as potential BACE1 inhibitors: 3D QSAR pharmacophore mapping and molecular dynamics analysis","volume":"34","author":"Kumar","year":"2016","journal-title":"J. Biomol. Struct. Dyn."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"131425","DOI":"10.1016\/j.molstruc.2021.131425","article-title":"Synthesis, kinetic evaluation and molecular docking studies of donepezil-based acetylcholinesterase inhibitors","volume":"1247","author":"Makarian","year":"2022","journal-title":"J. Mol. Struct."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Mirza, F.J., Zahid, S., Amber, S., Jabeen, H., Asim, N., and Ali Shah, S.A. (2022). Multitargeted molecular docking and dynamic simulation studies of bioactive compounds from Rosmarinus officinalis against Alzheimer\u2019s Disease. Molecules, 27.","DOI":"10.3390\/molecules27217241"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"648","DOI":"10.1007\/s11418-020-01431-8","article-title":"The search for, and chemistry and mechanism of, neurotrophic natural products","volume":"74","author":"Fukuyama","year":"2020","journal-title":"J. Nat. Med."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"53647","DOI":"10.1016\/j.phymed.2021.153647","article-title":"Honokiol: A review of its pharmacological potential and therapeutic insights","volume":"90","author":"Rauf","year":"2021","journal-title":"Phytomedicine"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1080\/10790268.2021.1890878","article-title":"Honokiol exerts protective effects on neural myelin sheaths after compressed spinal cord injury by inhibiting oligodendrocyte apoptosis through regulation of ER-mitochondrial interactions","volume":"45","author":"Tan","year":"2022","journal-title":"J. Spinal Cord Med."},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"577","DOI":"10.1016\/j.apsb.2022.07.019","article-title":"Honokiol alleviated neurodegeneration by reducing oxidative stress and improving mitochondrial function in mutant SOD1 cellular and mouse models of amyotrophic lateral sclerosis","volume":"13","author":"Zhou","year":"2023","journal-title":"Acta Pharm. Sin. B"},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.brainres.2009.09.107","article-title":"Magnolol and honokiol prevent learning and memory impairment and cholinergic deficit in SAMP8 mice","volume":"1305","author":"Matsui","year":"2009","journal-title":"Brain Res."},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"88","DOI":"10.1016\/j.ejphar.2015.04.013","article-title":"Honokiol improves learning and memory impairments induced by scopolamine in mice","volume":"760","author":"Xian","year":"2015","journal-title":"Eur. J. Pharmacol."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.ejphar.2015.11.047","article-title":"Honokiol abrogates chronic restraint stress-induced cognitive impairment and depressive-like behavior by blocking endoplasmic reticulum stress in the hippocampus of mice","volume":"770","author":"Jangra","year":"2016","journal-title":"Eur. J. Pharmacol."},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Hou, M., Bao, W., Gao, Y., Chen, J., and Song, G. (2022). Honokiol improves cognitive impairment in APP\/PS1 mice through activating mitophagy and mitochondrial unfolded protein response. Chem. Biol. Interact., 351.","DOI":"10.1016\/j.cbi.2021.109741"},{"key":"ref_56","doi-asserted-by":"crossref","unstructured":"Hwang, J., Youn, K., Ji, Y., Lee, S., Lim, G., Lee, J., Ho, C.T., Leem, S.H., and Jun, M. (2020). Biological and computational studies for dual cholinesterases inhibitory effect of zerumbone. Nutrients, 12.","DOI":"10.3390\/nu12051215"},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Chen, L.L., Fan, Y.G., Zhao, L.X., Zhang, Q., and Wang, Z.Y. (2023). The metal ion hypothesis of Alzheimer\u2019s disease and the anti-neuroinflammatory effect of metal chelators. Bioorg. Chem., 131.","DOI":"10.1016\/j.bioorg.2022.106301"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"147216","DOI":"10.1016\/j.brainres.2020.147216","article-title":"Ferritin reduction is essential for cerebral ischemia-induced hippocampal neuronal death through p53\/SLC7A11-mediated ferroptosis","volume":"1752","author":"Chen","year":"2021","journal-title":"Brain Res."},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"69","DOI":"10.1159\/000480320","article-title":"Honokiol attenuates oligomeric amyloid \u03b21-42-induced Alzheimer\u2019s disease in mice through attenuating mitochondrial apoptosis and inhibiting the nuclear factor kappa-B signaling pathway","volume":"43","author":"Wang","year":"2017","journal-title":"Cell Physiol. Biochem."},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1901","DOI":"10.1021\/acschemneuro.7b00071","article-title":"Effect of the Biphenyl Neolignan Honokiol on A\u03b242-Induced Toxicity in Caenorhabditis elegans, A\u03b242 Fibrillation, Cholinesterase Activity, DPPH Radicals, and Iron(II) Chelation","volume":"8","author":"Kantham","year":"2017","journal-title":"ACS Chem. Neurosci."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/19\/10507\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T16:06:46Z","timestamp":1760112406000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/25\/19\/10507"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2024,9,29]]},"references-count":60,"journal-issue":{"issue":"19","published-online":{"date-parts":[[2024,10]]}},"alternative-id":["ijms251910507"],"URL":"https:\/\/doi.org\/10.3390\/ijms251910507","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2024,9,29]]}}}