{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,4]],"date-time":"2026-11-04T22:20:03Z","timestamp":1793830803546,"version":"4.6.1"},"reference-count":163,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-017"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-037"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-012"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-029"},{"start":{"date-parts":[[2022,2,1]],"date-time":"2022-02-01T00:00:00Z","timestamp":1643673600000},"content-version":"stm-asf","delay-in-days":0,"URL":"https:\/\/doi.org\/10.15223\/policy-004"}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Bioorganic Chemistry"],"published-print":{"date-parts":[[2022,2]]},"DOI":"10.1016\/j.bioorg.2021.105562","type":"journal-article","created":{"date-parts":[[2021,12,15]],"date-time":"2021-12-15T21:07:25Z","timestamp":1639602445000},"page":"105562","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":53,"special_numbering":"C","title":["The molecular mechanism, targets, and novel molecules in the treatment of Alzheimer\u2019s disease"],"prefix":"10.1016","volume":"119","author":[{"given":"Akash","family":"Verma","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Digambar","family":"Kumar Waiker","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bhagwati","family":"Bhardwaj","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Poorvi","family":"Saraf","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sushant K.","family":"Shrivastava","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"5","key":"10.1016\/j.bioorg.2021.105562_b0005","doi-asserted-by":"crossref","first-page":"492","DOI":"10.1002\/ana.21509","article-title":"Prodromal Alzheimer's disease: successive emergence of the clinical symptoms","volume":"64","author":"Amieva","year":"2008","journal-title":"Ann. Neurol.: Off. J. Am. Neurol. Assoc. Child Neurol. Soc."},{"key":"10.1016\/j.bioorg.2021.105562_b0010","article-title":"The state of the art of dementia research: New frontiers","author":"Patterson","year":"2018","journal-title":"World Alzheimer Report"},{"key":"10.1016\/j.bioorg.2021.105562_b0015","doi-asserted-by":"crossref","unstructured":"C. Masters, et al., Sperling 559 RA, Cummings JL (2015) Alzheimer\u2019s disease, Nat. Rev. 560 Dis. Primers 1(15056) (2015) 561.","DOI":"10.1038\/nrdp.2015.56"},{"issue":"5","key":"10.1016\/j.bioorg.2021.105562_b0020","doi-asserted-by":"crossref","first-page":"1946","DOI":"10.1096\/fj.11-199851","article-title":"Identification of oligomers at early stages of tau aggregation in Alzheimer's disease","volume":"26","author":"Lasagna-Reeves","year":"2012","journal-title":"FASEB J."},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0025","doi-asserted-by":"crossref","first-page":"6","DOI":"10.3390\/biom6010006","article-title":"Tau protein hyperphosphorylation and aggregation in Alzheimer\u2019s disease and other tauopathies, and possible neuroprotective strategies","volume":"6","author":"\u0160imi\u0107","year":"2016","journal-title":"Biomolecules"},{"issue":"10","key":"10.1016\/j.bioorg.2021.105562_b0030","doi-asserted-by":"crossref","first-page":"1211","DOI":"10.1007\/BF01271206","article-title":"Cerebrospinal fluid acetylcholine and choline in vascular dementia of Binswanger and multiple small infarct types as compared with Alzheimer-type dementia","volume":"103","author":"Tohgi","year":"1996","journal-title":"J. Neural Transm."},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0035","doi-asserted-by":"crossref","first-page":"265","DOI":"10.1016\/S0306-4522(02)00241-5","article-title":"Characterization of neuronal dystrophy induced by fibrillar amyloid \u03b2: implications for Alzheimer\u2019s disease","volume":"114","author":"Grace","year":"2002","journal-title":"Neuroscience"},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0040","first-page":"24","article-title":"Alzheimer\u2019s disease: a clinical and basic science review","volume":"4","author":"Korolev","year":"2014","journal-title":"Med. Student Res. J."},{"issue":"2\u20133","key":"10.1016\/j.bioorg.2021.105562_b0045","doi-asserted-by":"crossref","first-page":"407","DOI":"10.1016\/0022-510X(82)90045-4","article-title":"Alzheimer's disease: correlation of cortical choline acetyltransferase activity with the severity of dementia and histological abnormalities","volume":"57","author":"Wilcock","year":"1982","journal-title":"J. Neurol. Sci."},{"key":"10.1016\/j.bioorg.2021.105562_b0050","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1016\/j.neuropharm.2014.11.018","article-title":"Role of the nicotinic acetylcholine receptor in Alzheimer's disease pathology and treatment","volume":"96","author":"Lombardo","year":"2015","journal-title":"Neuropharmacology"},{"issue":"6","key":"10.1016\/j.bioorg.2021.105562_b0055","doi-asserted-by":"crossref","first-page":"710","DOI":"10.1016\/j.conb.2006.09.002","article-title":"The role of acetylcholine in learning and memory","volume":"16","author":"Hasselmo","year":"2006","journal-title":"Curr. Opin. Neurobiol."},{"issue":"12","key":"10.1016\/j.bioorg.2021.105562_b0060","doi-asserted-by":"crossref","first-page":"1713","DOI":"10.1016\/j.bcp.2013.04.001","article-title":"Importance of the nicotinic acetylcholine receptor system in the prefrontal cortex","volume":"85","author":"Wallace","year":"2013","journal-title":"Biochem. Pharmacol."},{"issue":"6531","key":"10.1016\/j.bioorg.2021.105562_b0065","doi-asserted-by":"crossref","first-page":"484","DOI":"10.1038\/375484a0","article-title":"Essential role of neocortical acetylcholine in spatial memory","volume":"375","author":"Winkler","year":"1995","journal-title":"Nature"},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0070","doi-asserted-by":"crossref","first-page":"821","DOI":"10.1124\/jpet.102.041616","article-title":"The cholinergic hypothesis of age and Alzheimer's disease-related cognitive deficits: recent challenges and their implications for novel drug development","volume":"306","author":"Terry","year":"2003","journal-title":"J. Pharmacol. Exp. Ther."},{"issue":"9","key":"10.1016\/j.bioorg.2021.105562_b0075","doi-asserted-by":"crossref","first-page":"7565","DOI":"10.3390\/molecules16097565","article-title":"1, 3-Substituted imidazolidine-2, 4, 5-triones: synthesis and inhibition of cholinergic enzymes","volume":"16","author":"Pejchal","year":"2011","journal-title":"Molecules"},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0080","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1038\/nrn1035","article-title":"Neurobiology of butyrylcholinesterase","volume":"4","author":"Darvesh","year":"2003","journal-title":"Nat. Rev. Neurosci."},{"issue":"10","key":"10.1016\/j.bioorg.2021.105562_b0085","doi-asserted-by":"crossref","first-page":"1914","DOI":"10.1007\/s11064-014-1250-1","article-title":"Multi-target design strategies in the context of Alzheimer\u2019s disease: acetylcholinesterase inhibition and NMDA receptor antagonism as the driving forces","volume":"39","author":"Rosini","year":"2014","journal-title":"Neurochem. Res."},{"key":"10.1016\/j.bioorg.2021.105562_b0090","first-page":"183","article-title":"Activation of M1 and M4 muscarinic receptors as potential treatments for Alzheimer\u2019s disease and schizophrenia","volume":"10","author":"Foster","year":"2014","journal-title":"Neuropsychiatr. Dis. Treat."},{"issue":"8","key":"10.1016\/j.bioorg.2021.105562_b0095","doi-asserted-by":"crossref","first-page":"931","DOI":"10.1016\/j.bcp.2011.06.039","article-title":"Research update: Alpha7 nicotinic acetylcholine receptor mechanisms in Alzheimer's disease","volume":"82","author":"Parri","year":"2011","journal-title":"Biochem. Pharmacol."},{"issue":"5","key":"10.1016\/j.bioorg.2021.105562_b0100","doi-asserted-by":"crossref","first-page":"582","DOI":"10.1016\/j.conb.2004.08.001","article-title":"Amyloid-beta precursor protein processing in neurodegeneration","volume":"14","author":"Wilquet","year":"2004","journal-title":"Curr. Opin. Neurobiol."},{"key":"10.1016\/j.bioorg.2021.105562_b0105","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1111\/j.1749-6632.1991.tb00204.x","article-title":"Mechanisms of amyloid deposition in Alzheimer's disease","volume":"640","author":"Beyreuther","year":"1991","journal-title":"Ann. N. Y. Acad. Sci."},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0110","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1038\/nrm2101","article-title":"Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid \u03b2-peptide","volume":"8","author":"Haass","year":"2007","journal-title":"Nat. Rev. Mol. Cell Biol."},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0115","doi-asserted-by":"crossref","first-page":"10","DOI":"10.1111\/j.1471-4159.2010.07081.x","article-title":"Alpha-secretase in Alzheimer\u2019s disease: molecular identity, regulation and therapeutic potential","volume":"116","author":"Lichtenthaler","year":"2011","journal-title":"J. Neurochem."},{"issue":"41","key":"10.1016\/j.bioorg.2021.105562_b0120","doi-asserted-by":"crossref","first-page":"12787","DOI":"10.1523\/JNEUROSCI.3657-09.2009","article-title":"The \u03b2-secretase enzyme BACE in health and Alzheimer's disease: regulation, cell biology, function, and therapeutic potential","volume":"29","author":"Vassar","year":"2009","journal-title":"J. Neurosci."},{"issue":"10","key":"10.1016\/j.bioorg.2021.105562_b0125","doi-asserted-by":"crossref","first-page":"1493","DOI":"10.1016\/j.neurobiolaging.2006.06.023","article-title":"Alpha-and beta-secretase activity as a function of age and beta-amyloid in Down syndrome and normal brain","volume":"28","author":"Nistor","year":"2007","journal-title":"Neurobiol. Aging"},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0130","doi-asserted-by":"crossref","first-page":"99","DOI":"10.1038\/nrneurol.2009.218","article-title":"The secretases: enzymes with therapeutic potential in Alzheimer disease","volume":"6","author":"De Strooper","year":"2010","journal-title":"Nat. Rev. Neurol."},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0135","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1038\/sj.embor.7400897","article-title":"Loss-of-function presenilin mutations in Alzheimer disease: talking Point on the role of presenilin mutations in Alzheimer disease","volume":"8","author":"De Strooper","year":"2007","journal-title":"EMBO Rep."},{"issue":"6","key":"10.1016\/j.bioorg.2021.105562_b0140","doi-asserted-by":"crossref","first-page":"1615","DOI":"10.1016\/0896-6273(89)90050-0","article-title":"The microtubule binding domain of tau protein","volume":"2","author":"Lee","year":"1989","journal-title":"Neuron"},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0145","doi-asserted-by":"crossref","first-page":"1906","DOI":"10.1007\/s12035-016-9762-0","article-title":"Neuroprotective effect of nanodiamond in Alzheimer\u2019s disease rat model: a pivotal role for modulating NF-\u03baB and STAT3 signaling","volume":"54","author":"Alawdi","year":"2017","journal-title":"Mol. Neurobiol."},{"issue":"1\u20132","key":"10.1016\/j.bioorg.2021.105562_b0150","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0165-5728(01)00463-5","article-title":"GRO\u03b1\/KC, a chemokine receptor CXCR2 ligand, can be a potent trigger for neuronal ERK1\/2 and PI-3 kinase pathways and for tau hyperphosphorylation\u2014a role in Alzheimer's disease?","volume":"122","author":"Xia","year":"2002","journal-title":"J. Neuroimmunol."},{"issue":"11","key":"10.1016\/j.bioorg.2021.105562_b0155","doi-asserted-by":"crossref","first-page":"5053","DOI":"10.1523\/JNEUROSCI.4361-12.2013","article-title":"Sustained interleukin-1\u03b2 overexpression exacerbates tau pathology despite reduced amyloid burden in an Alzheimer's mouse model","volume":"33","author":"Ghosh","year":"2013","journal-title":"J. Neurosci."},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0160","doi-asserted-by":"crossref","first-page":"226","DOI":"10.1016\/j.arcmed.2010.03.007","article-title":"The revitalized tau hypothesis on Alzheimer's disease","volume":"41","author":"Maccioni","year":"2010","journal-title":"Arch. Med. Res."},{"issue":"6","key":"10.1016\/j.bioorg.2021.105562_b0165","doi-asserted-by":"crossref","first-page":"579","DOI":"10.2174\/156802606776743057","article-title":"Tau therapeutic strategies for the treatment of Alzheimer's disease","volume":"6","author":"Churcher","year":"2006","journal-title":"Curr. Top. Med. Chem."},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0170","doi-asserted-by":"crossref","first-page":"3","DOI":"10.2174\/1567205052772713","article-title":"Current advances on different kinases involved in tau phosphorylation, and implications in Alzheimer's disease and tauopathies","volume":"2","author":"Ferrer","year":"2005","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.bioorg.2021.105562_b0175","article-title":"Mechanism of oxidative stress in neurodegeneration","volume":"2012","author":"Gandhi","year":"2012","journal-title":"Oxid. Med. Cell. Long."},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0180","doi-asserted-by":"crossref","first-page":"1403","DOI":"10.3233\/JAD-170585","article-title":"Mitochondria and mitochondrial cascades in Alzheimer\u2019s disease","volume":"62","author":"Swerdlow","year":"2018","journal-title":"J. Alzheimers Dis."},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0185","doi-asserted-by":"crossref","first-page":"426","DOI":"10.1111\/j.1750-3639.2004.tb00087.x","article-title":"Amyloid \u03b2-peptide (1\u201342) contributes to the oxidative stress and neurodegeneration found in Alzheimer disease brain","volume":"14","author":"Butterfield","year":"2004","journal-title":"Brain Pathol."},{"issue":"6","key":"10.1016\/j.bioorg.2021.105562_b0190","doi-asserted-by":"crossref","first-page":"1936","DOI":"10.3390\/ph3061936","article-title":"Unlocking the door to neuronal woes in Alzheimer\u2019s disease: A\u03b2 and mitochondrial permeability transition pore","volume":"3","author":"Du","year":"2010","journal-title":"Pharmaceuticals"},{"issue":"6","key":"10.1016\/j.bioorg.2021.105562_b0195","doi-asserted-by":"crossref","first-page":"1173","DOI":"10.1023\/A:1014559331402","article-title":"Effect of beta-amyloid peptide fragment 25\u201335 on nonselective permeability of mitochondria","volume":"132","author":"Shevtzova","year":"2001","journal-title":"Bull. Exp. Biol. Med."},{"key":"10.1016\/j.bioorg.2021.105562_b0200","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1016\/j.cbi.2019.05.020","article-title":"Overview of novel multifunctional agents based on conjugates of \u03b3-carbolines, carbazoles, tetrahydrocarbazoles, phenothiazines, and aminoadamantanes for treatment of Alzheimer's disease","volume":"308","author":"Makhaeva","year":"2019","journal-title":"Chem. Biol. Interact."},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0205","doi-asserted-by":"crossref","first-page":"803","DOI":"10.1002\/med.21715","article-title":"Mitochondria as a promising target for developing novel agents for treating Alzheimer's disease","volume":"41","author":"Shevtsova","year":"2021","journal-title":"Med. Res. Rev."},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0210","first-page":"218","article-title":"Free radicals and oxidative stress in neurodegenerative diseases: relevance of dietary antioxidants","volume":"5","author":"Singh","year":"2004","journal-title":"J. Indian Acad. Clin. Med."},{"issue":"1\u20132","key":"10.1016\/j.bioorg.2021.105562_b0215","doi-asserted-by":"crossref","first-page":"254","DOI":"10.1016\/j.jns.2012.05.030","article-title":"Mitochondria, oxidative stress and neurodegeneration","volume":"322","author":"Federico","year":"2012","journal-title":"J. Neurol. Sci."},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0220","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1007\/s12640-012-9331-x","article-title":"Oxidative damage to RNA in aging and neurodegenerative disorders","volume":"22","author":"Nunomura","year":"2012","journal-title":"Neurotox. Res."},{"issue":"9","key":"10.1016\/j.bioorg.2021.105562_b0225","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pbio.1000479","article-title":"Post-stroke inhibition of induced NADPH oxidase type 4 prevents oxidative stress and neurodegeneration","volume":"8","author":"Kleinschnitz","year":"2010","journal-title":"PLoS Biol."},{"issue":"6","key":"10.1016\/j.bioorg.2021.105562_b0230","doi-asserted-by":"crossref","first-page":"1634","DOI":"10.1111\/j.1471-4159.2006.03907.x","article-title":"Oxidative stress and neurodegeneration: where are we now?","volume":"97","author":"Halliwell","year":"2006","journal-title":"J. Neurochem."},{"key":"10.1016\/j.bioorg.2021.105562_b0235","series-title":"Detection of Mitochondrial Diseases","first-page":"189","article-title":"Nitric oxide inhibition of cytochrome oxidase and mitochondrial respiration: implications for inflammatory, neurodegenerative and ischaemic pathologies","author":"Brown","year":"1997"},{"issue":"5","key":"10.1016\/j.bioorg.2021.105562_b0240","doi-asserted-by":"crossref","first-page":"1655","DOI":"10.1016\/S0002-9440(10)63724-8","article-title":"12\/15-lipoxygenase is increased in Alzheimer's disease: possible involvement in brain oxidative stress","volume":"164","author":"Pratico","year":"2004","journal-title":"Am. J. Pathol."},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0245","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1016\/j.brainresrev.2006.02.002","article-title":"Cyclooxygenases, lipoxygenases, and epoxygenases in CNS: their role and involvement in neurological disorders","volume":"52","author":"Phillis","year":"2006","journal-title":"Brain Res. Rev."},{"key":"10.1016\/j.bioorg.2021.105562_b0250","article-title":"Oxidative stress in neurodegenerative diseases: mechanisms and therapeutic perspectives","volume":"2011","author":"Melo","year":"2011","journal-title":"Oxid. Med. Cell. Long."},{"issue":"7","key":"10.1016\/j.bioorg.2021.105562_b0255","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."},{"issue":"25","key":"10.1016\/j.bioorg.2021.105562_b0260","doi-asserted-by":"crossref","first-page":"3167","DOI":"10.2174\/1381612043383421","article-title":"Recent approaches to novel anti-Alzheimer therapy","volume":"10","author":"Carreiras","year":"2004","journal-title":"Curr. Pharm. Des."},{"issue":"12","key":"10.1016\/j.bioorg.2021.105562_b0265","doi-asserted-by":"crossref","first-page":"1304","DOI":"10.1001\/archgenpsychiatry.2009.156","article-title":"Brain monoamine oxidase A binding in major depressive disorder: relationship to selective serotonin reuptake inhibitor treatment, recovery, and recurrence","volume":"66","author":"Meyer","year":"2009","journal-title":"Arch. Gen. Psychiatry"},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0270","doi-asserted-by":"crossref","first-page":"327","DOI":"10.1016\/j.neulet.2005.03.028","article-title":"1-N-Substituted thiocarbamoyl-3-phenyl-5-thienyl-2-pyrazolines: a novel cholinesterase and selective monoamine oxidase B inhibitors for the treatment of Parkinson's and Alzheimer's diseases","volume":"382","author":"Ucar","year":"2005","journal-title":"Neurosci. Lett."},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0275","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1016\/j.neuron.2008.07.013","article-title":"Linking calcium to A\u03b2 and Alzheimer's disease","volume":"59","author":"Green","year":"2008","journal-title":"Neuron"},{"issue":"6453","key":"10.1016\/j.bioorg.2021.105562_b0280","doi-asserted-by":"crossref","first-page":"559","DOI":"10.1126\/science.aay0198","article-title":"A vicious cycle of \u03b2 amyloid\u2013dependent neuronal hyperactivation","volume":"365","author":"Zott","year":"2019","journal-title":"Science"},{"issue":"20","key":"10.1016\/j.bioorg.2021.105562_b0285","doi-asserted-by":"crossref","first-page":"2059","DOI":"10.2174\/0929867033456800","article-title":"Ionotropic glutamate receptor biology: effect on synaptic connectivity and function in neurological disease","volume":"10","author":"Barnes","year":"2003","journal-title":"Curr. Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0290","doi-asserted-by":"crossref","first-page":"43","DOI":"10.3389\/fnins.2019.00043","article-title":"The role of NMDA receptors in Alzheimer\u2019s disease","volume":"13","author":"Liu","year":"2019","journal-title":"Front. Neurosci."},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0295","doi-asserted-by":"crossref","first-page":"511","DOI":"10.1002\/cmdc.201300444","article-title":"Lysine deacetylase (KDAC) regulatory pathways: an alternative approach to selective modulation","volume":"9","author":"Van Dyke","year":"2014","journal-title":"ChemMedChem"},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0300","doi-asserted-by":"crossref","first-page":"737","DOI":"10.1042\/bj20021321","article-title":"Histone deacetylases (HDACs): characterization of the classical HDAC family","volume":"370","author":"Ruijter","year":"2003","journal-title":"Biochem. J"},{"issue":"6887","key":"10.1016\/j.bioorg.2021.105562_b0305","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1038\/417455a","article-title":"HDAC6 is a microtubule-associated deacetylase","volume":"417","author":"Hubbert","year":"2002","journal-title":"Nature"},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0310","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":"2013","journal-title":"J. Alzheimers Dis."},{"issue":"29","key":"10.1016\/j.bioorg.2021.105562_b0315","doi-asserted-by":"crossref","first-page":"7072","DOI":"10.1021\/bi900818a","article-title":"Pyroglutamate formation influences solubility and amyloidogenicity of amyloid peptides","volume":"48","author":"Schlenzig","year":"2009","journal-title":"Biochemistry"},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0320","doi-asserted-by":"crossref","first-page":"385","DOI":"10.3233\/JAD-131535","article-title":"Glutaminyl cyclase in human cortex: correlation with (pGlu)-amyloid-\u03b2 load and cognitive decline in Alzheimer's disease","volume":"39","author":"Morawski","year":"2014","journal-title":"J. Alzheimers Dis."},{"issue":"8","key":"10.1016\/j.bioorg.2021.105562_b0325","article-title":"Cathepsin B in neurodegeneration of Alzheimer's disease, traumatic brain injury, and related brain disorders","volume":"1868","author":"Hook","year":"2020","journal-title":"Biochim. Biophys. Acta (BBA)-Prot. Proteom."},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0330","doi-asserted-by":"crossref","first-page":"287","DOI":"10.1016\/j.neuron.2009.06.026","article-title":"The role of apolipoprotein E in Alzheimer's disease","volume":"63","author":"Kim","year":"2009","journal-title":"Neuron"},{"key":"10.1016\/j.bioorg.2021.105562_b0335","series-title":"Seminars in Cell & Developmental Biology","article-title":"Cholesterol homeostasis in neurons and glial cells","author":"Vance","year":"2005"},{"issue":"8","key":"10.1016\/j.bioorg.2021.105562_b0340","first-page":"960","article-title":"ACAT inhibition and amyloid beta reduction","volume":"1801","author":"Bhattacharyya","year":"2010","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Cell Biol. Lipids"},{"issue":"5","key":"10.1016\/j.bioorg.2021.105562_b0345","doi-asserted-by":"crossref","first-page":"284","DOI":"10.1038\/nrn3012","article-title":"Linking lipids to Alzheimer's disease: cholesterol and beyond","volume":"12","author":"Di Paolo","year":"2011","journal-title":"Nat. Rev. Neurosci."},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0350","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.neurobiolaging.2014.10.038","article-title":"Periodontal disease associates with higher brain amyloid load in normal elderly","volume":"36","author":"Kamer","year":"2015","journal-title":"Neurobiol. Aging"},{"issue":"5","key":"10.1016\/j.bioorg.2021.105562_b0355","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1111\/omi.12134","article-title":"Spheres of influence: porphyromonas gingivalis outer membrane vesicles","volume":"31","author":"Gui","year":"2016","journal-title":"Mol. Oral Microbiol."},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0360","doi-asserted-by":"crossref","first-page":"eaau3333","DOI":"10.1126\/sciadv.aau3333","article-title":"Porphyromonas gingivalis in Alzheimer\u2019s disease brains: evidence for disease causation and treatment with small-molecule inhibitors","volume":"5","author":"Dominy","year":"2019","journal-title":"Sci. Adv."},{"issue":"suppl_2","key":"10.1016\/j.bioorg.2021.105562_b0365","doi-asserted-by":"crossref","first-page":"S74","DOI":"10.1111\/j.1753-4887.2010.00352.x","article-title":"Vascular basis for brain degeneration: faltering controls and risk factors for dementia","volume":"68","author":"Kalaria","year":"2010","journal-title":"Nutr. Rev."},{"issue":"7","key":"10.1016\/j.bioorg.2021.105562_b0370","doi-asserted-by":"crossref","first-page":"977","DOI":"10.1016\/j.neurobiolaging.2006.05.016","article-title":"Microvascular injury and blood\u2013brain barrier leakage in Alzheimer's disease","volume":"28","author":"Zipser","year":"2007","journal-title":"Neurobiol. Aging"},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0375","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1016\/j.tins.2005.02.001","article-title":"Neurovascular mechanisms of Alzheimer's neurodegeneration","volume":"28","author":"Zlokovic","year":"2005","journal-title":"Trends Neurosci."},{"issue":"12","key":"10.1016\/j.bioorg.2021.105562_b0380","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1038\/nrn3114","article-title":"Neurovascular pathways to neurodegeneration in Alzheimer's disease and other disorders","volume":"12","author":"Zlokovic","year":"2011","journal-title":"Nat. Rev. Neurosci."},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0385","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1016\/j.bmc.2008.11.068","article-title":"New pyrazoline bearing 4 (3H)-quinazolinone inhibitors of monoamine oxidase: Synthesis, biological evaluation, and structural determinants of MAO-A and MAO-B selectivity","volume":"17","author":"G\u00f6khan-Kelek\u00e7i","year":"2009","journal-title":"Bioorg. Med. Chem."},{"issue":"50","key":"10.1016\/j.bioorg.2021.105562_b0390","doi-asserted-by":"crossref","first-page":"10365","DOI":"10.1016\/j.tet.2012.09.086","article-title":"Synthesis and configurational assignment of 1, 2-dihydroimidazo [5, 1-b] quinazoline-3, 9-diones: novel NMDA receptor antagonists","volume":"68","author":"V\u00e1radi","year":"2012","journal-title":"Tetrahedron"},{"issue":"17","key":"10.1016\/j.bioorg.2021.105562_b0395","doi-asserted-by":"crossref","first-page":"6775","DOI":"10.1021\/jm400564j","article-title":"Quinazolin-4-one derivatives as selective histone deacetylase-6 inhibitors for the treatment of Alzheimer\u2019s disease","volume":"56","author":"Yu","year":"2013","journal-title":"J. Med. Chem."},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0400","doi-asserted-by":"crossref","first-page":"74","DOI":"10.2174\/1573406411666150708111417","article-title":"Biological evaluation of azomethine-dihydroquinazolinone conjugates as cancer and cholinesterase inhibitors","volume":"12","author":"Iqbal","year":"2016","journal-title":"Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0405","doi-asserted-by":"crossref","first-page":"823","DOI":"10.1016\/j.ejmech.2016.12.005","article-title":"2, 4-Disubstituted quinazolines as amyloid-\u03b2 aggregation inhibitors with dual cholinesterase inhibition and antioxidant properties: development and structure-activity relationship (SAR) studies","volume":"126","author":"Mohamed","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0410","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.bioorg.2017.07.014","article-title":"Synthesis and biological evaluation of quinazolinone-based hydrazones with potential use in Alzheimer\u2019s disease","volume":"74","author":"Haghighijoo","year":"2017","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0415","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1016\/j.ejmech.2017.09.008","article-title":"Novel deoxyvasicinone derivatives as potent multitarget-directed ligands for the treatment of Alzheimer's disease: design, synthesis, and biological evaluation","volume":"140","author":"Ma","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0420","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/j.bioorg.2017.01.004","article-title":"Synthesis, biological evaluation and docking studies of 2, 3-dihydroquinazolin-4 (1H)-one derivatives as inhibitors of cholinesterases","volume":"70","author":"Sarfraz","year":"2017","journal-title":"Bioorg. Chem."},{"issue":"36","key":"10.1016\/j.bioorg.2021.105562_b0425","doi-asserted-by":"crossref","first-page":"22360","DOI":"10.1039\/C7RA02889J","article-title":"Application of quinazoline and pyrido [3, 2-d] pyrimidine templates to design multi-targeting agents in Alzheimer's disease","volume":"7","author":"Mohamed","year":"2017","journal-title":"RSC Adv."},{"key":"10.1016\/j.bioorg.2021.105562_b0430","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/j.ejmech.2013.09.024","article-title":"Multifunctional tacrine\u2013flavonoid hybrids with cholinergic, \u03b2-amyloid-reducing, and metal chelating properties for the treatment of Alzheimer's disease","volume":"69","author":"Li","year":"2013","journal-title":"Eur. J. Med. Chem."},{"issue":"9","key":"10.1016\/j.bioorg.2021.105562_b0435","doi-asserted-by":"crossref","first-page":"2636","DOI":"10.1016\/j.bmcl.2013.02.095","article-title":"Design, synthesis and evaluation of flavonoid derivatives as potential multifunctional acetylcholinesterase inhibitors against Alzheimer\u2019s disease","volume":"23","author":"Li","year":"2013","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"10","key":"10.1016\/j.bioorg.2021.105562_b0440","doi-asserted-by":"crossref","first-page":"1354","DOI":"10.1007\/s12272-014-0351-3","article-title":"The effects of C-glycosylation of luteolin on its antioxidant, anti-Alzheimer\u2019s disease, anti-diabetic, and anti-inflammatory activities","volume":"37","author":"Choi","year":"2014","journal-title":"Arch. Pharmacal Res."},{"issue":"24","key":"10.1016\/j.bioorg.2021.105562_b0445","doi-asserted-by":"crossref","first-page":"6273","DOI":"10.1016\/j.bmc.2017.09.012","article-title":"Exploration of multi-target potential of chromen-4-one based compounds in Alzheimer\u2019s disease: design, synthesis and biological evaluations","volume":"25","author":"Singh","year":"2017","journal-title":"Bioorg. Med. Chem."},{"issue":"23","key":"10.1016\/j.bioorg.2021.105562_b0450","doi-asserted-by":"crossref","first-page":"7275","DOI":"10.1016\/j.bmc.2013.09.061","article-title":"Design, synthesis and evaluation of novel 4-dimethylamine flavonoid derivatives as potential multi-functional anti-Alzheimer agents","volume":"21","author":"Luo","year":"2013","journal-title":"Bioorg. Med. Chem."},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0455","doi-asserted-by":"crossref","first-page":"672","DOI":"10.1016\/j.bmc.2015.12.031","article-title":"Design, synthesis and evaluation of novel 7-aminoalkyl-substituted flavonoid derivatives with improved cholinesterase inhibitory activities","volume":"24","author":"Luo","year":"2016","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0460","doi-asserted-by":"crossref","DOI":"10.1155\/2017\/8587260","article-title":"Xanthone and flavone derivatives as dual agents with acetylcholinesterase inhibition and antioxidant activity as potential anti-alzheimer agents","volume":"2017","author":"Cruz","year":"2017","journal-title":"J. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0465","doi-asserted-by":"crossref","first-page":"751","DOI":"10.1016\/j.ejmech.2013.03.025","article-title":"Synthesis and biological evaluation of phosphorylated flavonoids as potent and selective inhibitors of cholesterol esterase","volume":"74","author":"Wei","year":"2014","journal-title":"Eur. J. Med. Chem."},{"issue":"21","key":"10.1016\/j.bioorg.2021.105562_b0470","doi-asserted-by":"crossref","first-page":"6124","DOI":"10.1016\/j.bmc.2014.08.033","article-title":"Design, synthesis and pharmacological evaluation of chalcone derivatives as acetylcholinesterase inhibitors","volume":"22","author":"Liu","year":"2014","journal-title":"Bioorg. Med. Chem."},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0475","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1111\/cbdd.12514","article-title":"Novel potent and selective acetylcholinesterase inhibitors as potential drugs for the treatment of Alzheimer's disease: synthesis, pharmacological evaluation, and molecular modeling of amino-alkyl-substituted fluoro-chalcones derivatives","volume":"86","author":"Liu","year":"2015","journal-title":"Chem. Biol. Drug Des."},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0480","doi-asserted-by":"crossref","first-page":"580","DOI":"10.3109\/14756366.2015.1050009","article-title":"Design, synthesis and preliminary structure\u2013activity relationship investigation of nitrogen-containing chalcone derivatives as acetylcholinesterase and butyrylcholinesterase inhibitors: a further study based on Flavokawain B Mannich base derivatives","volume":"31","author":"Liu","year":"2016","journal-title":"J. Enzyme Inhib. Med. Chem."},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0485","doi-asserted-by":"crossref","first-page":"615","DOI":"10.1016\/j.bbrc.2016.11.082","article-title":"Cholinesterases inhibition and molecular modeling studies of piperidyl-thienyl and 2-pyrazoline derivatives of chalcones","volume":"482","author":"Shah","year":"2017","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1016\/j.bioorg.2021.105562_b0490","doi-asserted-by":"crossref","first-page":"238","DOI":"10.1016\/j.ejmech.2019.07.021","article-title":"Design, synthesis, in-silico and biological evaluation of novel chalcone derivatives as multi-function agents for the treatment of Alzheimer's disease","volume":"180","author":"Sang","year":"2019","journal-title":"Eur. J. Med. Chem."},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0495","doi-asserted-by":"crossref","first-page":"893","DOI":"10.1007\/s11030-018-9839-y","article-title":"Structure\u2013activity relationship investigation of coumarin\u2013chalcone hybrids with diverse side-chains as acetylcholinesterase and butyrylcholinesterase inhibitors","volume":"22","author":"Kang","year":"2018","journal-title":"Mol. Diversity"},{"issue":"7","key":"10.1016\/j.bioorg.2021.105562_b0500","doi-asserted-by":"crossref","first-page":"955","DOI":"10.3390\/molecules21070955","article-title":"Synthesis, biological evaluation and molecular modelling of 2\u2032-hydroxychalcones as acetylcholinesterase inhibitors","volume":"21","author":"Sukumaran","year":"2016","journal-title":"Molecules"},{"key":"10.1016\/j.bioorg.2021.105562_b0505","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2019.103477","article-title":"Flurbiprofen-chalcone hybrid Mannich base derivatives as balanced multifunctional agents against Alzheimer\u2019s disease: design, synthesis and biological evaluation","volume":"94","author":"Tian","year":"2020","journal-title":"Bioorg. Chem."},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0510","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1016\/j.bmc.2016.11.002","article-title":"Design, synthesis, biological evaluation, and molecular modeling studies of chalcone-rivastigmine hybrids as cholinesterase inhibitors","volume":"25","author":"Wang","year":"2017","journal-title":"Bioorg. Med. Chem."},{"issue":"9","key":"10.1016\/j.bioorg.2021.105562_b0515","doi-asserted-by":"crossref","first-page":"2614","DOI":"10.1016\/j.bmcl.2013.02.103","article-title":"Design, synthesis and biological activity of multifunctional \u03b1, \u03b2-unsaturated carbonyl scaffolds for Alzheimer\u2019s disease","volume":"23","author":"Bag","year":"2013","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0520","doi-asserted-by":"crossref","first-page":"213","DOI":"10.1039\/C1MD00221J","article-title":"3-Substituted coumarins as dual inhibitors of AChE and MAO for the treatment of Alzheimer's disease","volume":"3","author":"Vi\u00f1a","year":"2012","journal-title":"MedChemComm"},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0525","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.1016\/j.bmc.2014.01.010","article-title":"Synthesis of aminoalkyl-substituted coumarin derivatives as acetylcholinesterase inhibitors","volume":"22","author":"Nam","year":"2014","journal-title":"Bioorg. Med. Chem."},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0530","doi-asserted-by":"crossref","first-page":"508","DOI":"10.1016\/j.bmcl.2014.12.034","article-title":"Multifunctional coumarin derivatives: monoamine oxidase B (MAO-B) inhibition, anti-\u03b2-amyloid (A\u03b2) aggregation and metal chelation properties against Alzheimer\u2019s disease","volume":"25","author":"Huang","year":"2015","journal-title":"Bioorg. Med. Chem. Lett."},{"key":"10.1016\/j.bioorg.2021.105562_b0535","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.jinorgbio.2016.05.001","article-title":"Targeting copper (II)-induced oxidative stress and the acetylcholinesterase system in Alzheimer's disease using multifunctional tacrine-coumarin hybrid molecules","volume":"161","author":"Hamulakova","year":"2016","journal-title":"J. Inorg. Biochem."},{"key":"10.1016\/j.bioorg.2021.105562_b0540","doi-asserted-by":"crossref","first-page":"853","DOI":"10.1016\/j.ejmech.2016.09.041","article-title":"Synthesis and evaluation of 7-substituted coumarin derivatives as multimodal monoamine oxidase-B and cholinesterase inhibitors for the treatment of Alzheimer's disease","volume":"125","author":"Joubert","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0545","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.ejmech.2015.10.046","article-title":"Synthesis, pharmacological assessment, molecular modeling and in silico studies of fused tricyclic coumarin derivatives as a new family of multifunctional anti-Alzheimer agents","volume":"107","author":"Shaik","year":"2016","journal-title":"Eur. J. Med. Chem."},{"issue":"9","key":"10.1016\/j.bioorg.2021.105562_b0550","doi-asserted-by":"crossref","first-page":"2886","DOI":"10.1016\/j.bbagen.2014.05.005","article-title":"Synthesis and characterization of 1H-phenanthro [9, 10-d] imidazole derivatives as multifunctional agents for treatment of Alzheimer's disease","volume":"1840","author":"Liu","year":"2014","journal-title":"Biochim. Biophys. Acta (BBA)-Gen. Subj."},{"key":"10.1016\/j.bioorg.2021.105562_b0555","doi-asserted-by":"crossref","first-page":"1172","DOI":"10.1016\/j.ejmech.2016.11.017","article-title":"Discovery of benzimidazole derivatives as modulators of mitochondrial function: a potential treatment for Alzheimer's disease","volume":"125","author":"Kim","year":"2017","journal-title":"Eur. J. Med. Chem."},{"issue":"15","key":"10.1016\/j.bioorg.2021.105562_b0560","doi-asserted-by":"crossref","first-page":"6664","DOI":"10.1021\/acs.jmedchem.7b00648","article-title":"Synthesis and evaluation of diphenyl conjugated imidazole derivatives as potential glutaminyl cyclase inhibitors for treatment of Alzheimer\u2019s disease","volume":"60","author":"Li","year":"2017","journal-title":"J. Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0565","doi-asserted-by":"crossref","first-page":"1213","DOI":"10.1016\/j.ejmech.2016.11.021","article-title":"Design, synthesis and SAR analysis of potent BACE1 inhibitors: possible lead drug candidates for Alzheimer's disease","volume":"125","author":"Tarazi","year":"2017","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0570","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.ejmech.2017.08.025","article-title":"Discovery of novel propargylamine-modified 4-aminoalkyl imidazole substituted pyrimidinylthiourea derivatives as multifunctional agents for the treatment of Alzheimer's disease","volume":"143","author":"Xu","year":"2018","journal-title":"Eur. J. Med. Chem."},{"issue":"8","key":"10.1016\/j.bioorg.2021.105562_b0575","doi-asserted-by":"crossref","first-page":"1511","DOI":"10.1016\/j.bmc.2018.01.029","article-title":"In silico studies, synthesis and pharmacological evaluation to explore multi-targeted approach for imidazole analogues as potential cholinesterase inhibitors with neuroprotective role for Alzheimer\u2019s disease","volume":"26","author":"Gurjar","year":"2018","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0580","doi-asserted-by":"crossref","first-page":"187","DOI":"10.1016\/j.bioorg.2019.01.044","article-title":"Mono-or di-substituted imidazole derivatives for inhibition of acetylcholine and butyrylcholine esterases","volume":"86","author":"Kuzu","year":"2019","journal-title":"Bioorg. Chem."},{"issue":"7","key":"10.1016\/j.bioorg.2021.105562_b0585","doi-asserted-by":"crossref","first-page":"1506","DOI":"10.1007\/s00044-017-1874-1","article-title":"Novel 2-Arylbenzimidazole derivatives as multi-targeting agents to treat Alzheimer\u2019s disease","volume":"26","author":"Unsal-Tan","year":"2017","journal-title":"Med. Chem. Res."},{"key":"10.1016\/j.bioorg.2021.105562_b0590","doi-asserted-by":"crossref","first-page":"33","DOI":"10.1016\/j.bioorg.2013.06.008","article-title":"Synthesis, characterization, and molecular docking analysis of novel benzimidazole derivatives as cholinesterase inhibitors","volume":"49","author":"Yoon","year":"2013","journal-title":"Bioorg. Chem."},{"issue":"8","key":"10.1016\/j.bioorg.2021.105562_b0595","doi-asserted-by":"crossref","first-page":"1215","DOI":"10.1002\/cmdc.201000086","article-title":"Bis (7)-tacrine derivatives as multitarget-directed ligands: focus on anticholinesterase and antiamyloid activities","volume":"5","author":"Bolognesi","year":"2010","journal-title":"ChemMedChem"},{"issue":"6","key":"10.1016\/j.bioorg.2021.105562_b0600","doi-asserted-by":"crossref","first-page":"2609","DOI":"10.1016\/j.ejmech.2011.03.058","article-title":"Synthesis and evaluation of heterobivalent tacrine derivatives as potential multi-functional anti-Alzheimer agents","volume":"46","author":"Luo","year":"2011","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0605","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.ejmech.2012.06.051","article-title":"Synthesis, design and biological evaluation of novel highly potent tacrine congeners for the treatment of Alzheimer's disease","volume":"55","author":"Hamulakova","year":"2012","journal-title":"Eur. J. Med. Chem."},{"issue":"7","key":"10.1016\/j.bioorg.2021.105562_b0610","doi-asserted-by":"crossref","first-page":"3588","DOI":"10.1021\/jm300124p","article-title":"Multifunctional mercapto-tacrine derivatives for treatment of age-related neurodegenerative diseases","volume":"55","author":"Wang","year":"2012","journal-title":"J. Med. Chem."},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0615","doi-asserted-by":"crossref","first-page":"807","DOI":"10.1016\/j.bmcl.2014.12.084","article-title":"Synthesis and pharmacological evaluation of multifunctional tacrine derivatives against several disease pathways of AD","volume":"25","author":"Digiacomo","year":"2015","journal-title":"Bioorg. Med. Chem. Lett."},{"issue":"16","key":"10.1016\/j.bioorg.2021.105562_b0620","doi-asserted-by":"crossref","first-page":"7073","DOI":"10.1021\/jm5008648","article-title":"Synthesis and biological evaluation of novel tacrine derivatives and tacrine\u2013coumarin hybrids as cholinesterase inhibitors","volume":"57","author":"Hamulakova","year":"2014","journal-title":"J. Med. Chem."},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0625","doi-asserted-by":"crossref","first-page":"1338","DOI":"10.1021\/jm901614b","article-title":"Design, synthesis, biological properties, and molecular modeling investigations of novel tacrine derivatives with a combination of acetylcholinesterase inhibition and cannabinoid CB1 receptor antagonism","volume":"53","author":"Lange","year":"2010","journal-title":"J. Med. Chem."},{"issue":"6","key":"10.1016\/j.bioorg.2021.105562_b0630","doi-asserted-by":"crossref","first-page":"1425","DOI":"10.1111\/cbdd.12609","article-title":"Design, synthesis, biological evaluation, and docking study of acetylcholinesterase inhibitors: new acridone-1, 2, 4-oxadiazole-1, 2, 3-triazole hybrids","volume":"86","author":"Mohammadi-Khanaposhtani","year":"2015","journal-title":"Chem. Biol. Drug Des."},{"issue":"10","key":"10.1016\/j.bioorg.2021.105562_b0635","doi-asserted-by":"crossref","first-page":"1807","DOI":"10.1007\/s00706-017-1993-x","article-title":"Synthesis and biological evaluation of benzothiazol-based 1, 3, 4-oxadiazole derivatives as amyloid \u03b2-targeted compounds against Alzheimer\u2019s disease","volume":"148","author":"Mei","year":"2017","journal-title":"Monatshefte f\u00fcr Chemie-Chemical Monthly"},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0640","doi-asserted-by":"crossref","first-page":"1472197","DOI":"10.1080\/23312009.2018.1472197","article-title":"Synthesis of new heterocyclic 3-piperidinyl-1, 3, 4-oxadiazole derivatives as potential drug candidate for the treatment of Alzheimer\u2019s disease","volume":"4","author":"Rehman","year":"2018","journal-title":"Cogent Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0645","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2019.103506","article-title":"Design, synthesis, and biological evaluation of ferulic acid based 1, 3, 4-oxadiazole hybrids as multifunctional therapeutics for the treatment of Alzheimer\u2019s disease","volume":"95","author":"Tripathi","year":"2020","journal-title":"Bioorg. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0650","doi-asserted-by":"crossref","DOI":"10.1016\/j.bioorg.2019.103025","article-title":"Design and development of 1, 3, 4-oxadiazole derivatives as potential inhibitors of acetylcholinesterase to ameliorate scopolamine-induced cognitive dysfunctions","volume":"89","author":"Mishra","year":"2019","journal-title":"Bioorg. Chem."},{"issue":"10","key":"10.1016\/j.bioorg.2021.105562_b0655","doi-asserted-by":"crossref","first-page":"4361","DOI":"10.1021\/acschemneuro.9b00430","article-title":"Novel molecular hybrids of n-benzylpiperidine and 1, 3, 4-oxadiazole as multitargeted therapeutics to treat Alzheimer\u2019s disease","volume":"10","author":"Sharma","year":"2019","journal-title":"ACS Chem. Neurosci."},{"issue":"7","key":"10.1016\/j.bioorg.2021.105562_b0660","doi-asserted-by":"crossref","first-page":"1327","DOI":"10.1016\/j.bmc.2019.02.031","article-title":"Design and development of novel N-(pyrimidin-2-yl)-1, 3, 4-oxadiazole hybrids to treat cognitive dysfunctions","volume":"27","author":"Tripathi","year":"2019","journal-title":"Bioorg. Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0665","doi-asserted-by":"crossref","DOI":"10.1016\/j.ejmech.2019.111707","article-title":"Design and development of molecular hybrids of 2-pyridylpiperazine and 5-phenyl-1, 3, 4-oxadiazoles as potential multifunctional agents to treat Alzheimer's disease","volume":"183","author":"Tripathi","year":"2019","journal-title":"Eur. J. Med. Chem."},{"key":"10.1016\/j.bioorg.2021.105562_b0670","article-title":"Alzheimer's disease and the amyloid cascade hypothesis: a critical review","volume":"2012","author":"Reitz","year":"2012","journal-title":"Int. J. Alzheimer\u2019s Dis."},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0675","doi-asserted-by":"crossref","first-page":"47","DOI":"10.1186\/s12929-017-0355-7","article-title":"Drug candidates in clinical trials for Alzheimer\u2019s disease","volume":"24","author":"Hung","year":"2017","journal-title":"J. Biomed. Sci."},{"key":"10.1016\/j.bioorg.2021.105562_b0680","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.trci.2018.11.001","article-title":"A phase 1 clinical trial of the sigma-2 receptor complex allosteric antagonist CT1812, a novel therapeutic candidate for Alzheimer's disease","volume":"5","author":"Grundman","year":"2019","journal-title":"Alzheimer's & Dementia: Transl. Res. Clin. Intervent."},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0685","doi-asserted-by":"crossref","first-page":"262","DOI":"10.1016\/j.trci.2017.03.005","article-title":"UB-311, a novel UBITh\u00ae amyloid \u03b2 peptide vaccine for mild Alzheimer's disease","volume":"3","author":"Wang","year":"2017","journal-title":"Alzheimer's & Dementia: Transl. Res. Clin. Intervent."},{"issue":"3","key":"10.1016\/j.bioorg.2021.105562_b0690","doi-asserted-by":"crossref","first-page":"959","DOI":"10.3233\/JAD-140291","article-title":"A randomized study of H3 antagonist ABT-288 in mild-to-moderate Alzheimer's dementia","volume":"42","author":"Haig","year":"2014","journal-title":"J. Alzheimers Dis."},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0695","doi-asserted-by":"crossref","first-page":"47","DOI":"10.2174\/1567205010666131212110148","article-title":"A randomized, double-blind, placebo-controlled, 16-week study of the H3 receptor antagonist, GSK239512 as a monotherapy in subjects with mild-to-moderate Alzheimer\u2019s disease","volume":"11","author":"Grove","year":"2014","journal-title":"Curr. Alzheimer Res."},{"key":"10.1016\/j.bioorg.2021.105562_b0700","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.biopha.2016.12.067","article-title":"Riluzole ameliorates learning and memory deficits in A\u03b225-35-induced rat model of Alzheimer\u2019s disease and is independent of cholinoceptor activation","volume":"87","author":"Mokhtari","year":"2017","journal-title":"Biomed. Pharmacother."},{"key":"10.1016\/j.bioorg.2021.105562_b0705","first-page":"1471","article-title":"Disease-modifying drugs in Alzheimer\u2019s disease","volume":"7","author":"Ghezzi","year":"2013","journal-title":"Drug Des., Dev. Therapy"},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0710","doi-asserted-by":"crossref","first-page":"3","DOI":"10.3233\/JAD-180145","article-title":"Alzheimer\u2019s disease: advances in drug development","volume":"65","author":"Piton","year":"2018","journal-title":"J. Alzheimers Dis."},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0715","doi-asserted-by":"crossref","first-page":"144","DOI":"10.2174\/156802610790410983","article-title":"Neuronal nicotinic acetylcholine receptors-targets for the development of drugs to treat cognitive impairment associated with schizophrenia and Alzheimer's disease","volume":"10","author":"Haydar","year":"2010","journal-title":"Curr. Top. Med. Chem."},{"issue":"5","key":"10.1016\/j.bioorg.2021.105562_b0720","doi-asserted-by":"crossref","first-page":"631","DOI":"10.1016\/j.bbadis.2011.10.006","article-title":"Antioxidant clinical trials in mild cognitive impairment and Alzheimer's disease","volume":"1822","author":"Mecocci","year":"2012","journal-title":"Biochim. Biophys. Acta (BBA)-Mol. Basis Dis."},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0725","doi-asserted-by":"crossref","first-page":"429","DOI":"10.4155\/ppa.14.22","article-title":"Advances in recent patent and clinical trial drug development for Alzheimer\u2019s disease","volume":"3","author":"Liu","year":"2014","journal-title":"Pharm. Pat. Anal."},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0730","first-page":"288","article-title":"Cautious optimism for growth in Alzheimer\u2019s disease treatments","volume":"40","author":"Cherian","year":"2015","journal-title":"Pharm. Therap."},{"issue":"1","key":"10.1016\/j.bioorg.2021.105562_b0735","doi-asserted-by":"crossref","first-page":"102","DOI":"10.5114\/aoms.2011.20612","article-title":"Tramiprosate in mild-to-moderate Alzheimer\u2019s disease\u2013a randomized, double-blind, placebo-controlled, multi-centre study (the Alphase Study)","volume":"7","author":"Aisen","year":"2011","journal-title":"Arch. Med. Sci.: AMS"},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0740","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1001\/jama.2017.19700","article-title":"Lack of benefit with idalopirdine for Alzheimer disease: another therapeutic failure in a complex disease process","volume":"319","author":"Bennett","year":"2018","journal-title":"JAMA"},{"issue":"13","key":"10.1016\/j.bioorg.2021.105562_b0745","doi-asserted-by":"crossref","first-page":"3053","DOI":"10.1038\/npp.2015.176","article-title":"Randomized, double-blind, placebo-controlled study of encenicline, an \u03b1 7 nicotinic acetylcholine receptor agonist, as a treatment for cognitive impairment in schizophrenia","volume":"40","author":"Keefe","year":"2015","journal-title":"Neuropsychopharmacology"},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0750","doi-asserted-by":"crossref","first-page":"322","DOI":"10.1056\/NEJMoa1304839","article-title":"Two phase 3 trials of bapineuzumab in mild-to-moderate Alzheimer's disease","volume":"370","author":"Salloway","year":"2014","journal-title":"N. Engl. J. Med."},{"issue":"21","key":"10.1016\/j.bioorg.2021.105562_b0755","doi-asserted-by":"crossref","first-page":"e1889","DOI":"10.1212\/WNL.0000000000005550","article-title":"ABBY: A phase 2 randomized trial of crenezumab in mild to moderate Alzheimer disease","volume":"90","author":"Cummings","year":"2018","journal-title":"Neurology"},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0760","first-page":"255","article-title":"Clinical development of aducanumab, an anti-A\u03b2 human monoclonal antibody being investigated for the treatment of early Alzheimer's disease","volume":"4","author":"Budd","year":"2017","journal-title":"J. Prevent. Alzheimer's Dis."},{"key":"10.1016\/j.bioorg.2021.105562_b0765","series-title":"The Alzheimer Disease Market","author":"Qian","year":"2015"},{"key":"10.1016\/j.bioorg.2021.105562_b0770","doi-asserted-by":"crossref","first-page":"S95","DOI":"10.1016\/j.jalz.2005.06.330","article-title":"[O2-01-05]: A placebo-controlled, double-blind trial of the selective AB-42 lowering agent, flurizan (MPC-7869,(R)-flurbiprofen) in patients with mild to moderate Alzheimer's disease","volume":"1","author":"Wilcock","year":"2005","journal-title":"Alzheimer's Dementia"},{"issue":"9","key":"10.1016\/j.bioorg.2021.105562_b0775","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pmed.1002660","article-title":"Nilvadipine in mild to moderate Alzheimer disease: a randomised controlled trial","volume":"15","author":"Lawlor","year":"2018","journal-title":"PLoS Med."},{"key":"10.1016\/j.bioorg.2021.105562_b0780","article-title":"Donepezil for dementia due to Alzheimer's disease","volume":"6","author":"Birks","year":"2018","journal-title":"Cochrane Database Syst. Rev."},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0785","doi-asserted-by":"crossref","first-page":"307","DOI":"10.2165\/00023210-199912040-00005","article-title":"Selectivity of cholinesterase inhibition","volume":"12","author":"Weinstock","year":"1999","journal-title":"CNS Drugs"},{"key":"10.1016\/j.bioorg.2021.105562_b0790","doi-asserted-by":"crossref","DOI":"10.1002\/14651858.CD001747","article-title":"Galantamine for Alzheimer's disease","volume":"3","author":"Olin","year":"2002","journal-title":"Cochrane Database Syst. Rev."},{"issue":"2","key":"10.1016\/j.bioorg.2021.105562_b0795","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1177\/153331750502000206","article-title":"Memantine: targeting glutamate excitotoxicity in Alzheimer's disease and other dementias","volume":"20","author":"Molinuevo","year":"2005","journal-title":"Am. J. Alzheimer's Dis. Other Dementias\u00ae"},{"key":"10.1016\/j.bioorg.2021.105562_b0800","doi-asserted-by":"crossref","first-page":"177","DOI":"10.3389\/fnins.2016.00177","article-title":"One for all? Hitting multiple Alzheimer's disease targets with one drug","volume":"10","author":"Hughes","year":"2016","journal-title":"Front. Neurosci."},{"issue":"5","key":"10.1016\/j.bioorg.2021.105562_b0805","doi-asserted-by":"crossref","first-page":"377","DOI":"10.1021\/cn500016p","article-title":"Acetylcholinesterase inhibitors with photoswitchable inhibition of \u03b2-amyloid aggregation","volume":"5","author":"Chen","year":"2014","journal-title":"ACS Chem. Neurosci."},{"issue":"4","key":"10.1016\/j.bioorg.2021.105562_b0810","doi-asserted-by":"crossref","first-page":"1445","DOI":"10.3233\/JAD-160813","article-title":"Protein expression of BACE1 is downregulated by donepezil in Alzheimer\u2019s disease platelets","volume":"55","author":"Sarno","year":"2017","journal-title":"J. Alzheimers Dis."},{"issue":"22","key":"10.1016\/j.bioorg.2021.105562_b0815","doi-asserted-by":"crossref","first-page":"9708","DOI":"10.1021\/jm3009458","article-title":"Combining galantamine and memantine in multitargeted, new chemical entities potentially useful in Alzheimer\u2019s disease","volume":"55","author":"Simoni","year":"2012","journal-title":"J. Med. Chem."}],"container-title":["Bioorganic Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206821009408?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0045206821009408?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,23]],"date-time":"2025-09-23T08:27:31Z","timestamp":1758616051000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0045206821009408"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2022,2]]},"references-count":163,"alternative-id":["S0045206821009408"],"URL":"https:\/\/doi.org\/10.1016\/j.bioorg.2021.105562","relation":{},"ISSN":["0045-2068"],"issn-type":[{"value":"0045-2068","type":"print"}],"subject":[],"published":{"date-parts":[[2022,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The molecular mechanism, targets, and novel molecules in the treatment of Alzheimer\u2019s disease","name":"articletitle","label":"Article Title"},{"value":"Bioorganic Chemistry","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.bioorg.2021.105562","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2021 Elsevier Inc. All rights reserved.","name":"copyright","label":"Copyright"}],"article-number":"105562"}}