Multi-Target-Directed Ligands and other Therapeutic Strategies in the Search of a Real Solution for Alzheimer’s Disease

Novel Class of Quinone-Bearing Polyamines as Multi-Target-Directed Ligands To Combat Alzheimer's Disease

Bolognesi, M. L., Banzi, R., Bartolini, M., Cavalli, A., Tarozzi, A., Andrisano, V., Minarini, A., Rosini, M., Tumiatti, V., Bergamini, C., et al. (2007) · Journal of Medicinal Chemistry · doi:10.1021/jm070559a · Cited by 134

Alzheimer's disease: new approaches to drug discovery

Bolognesi, M. L., Matera, R., Minarini, A., Rosini, M., & Melchiorre, C. (2009) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2009.04.619 · Cited by 132

Effect of phenserine treatment on brain functional activity and amyloid in Alzheimer's disease

Kadir, A., Andreasen, N., Almkvist, O., Wall, A. E., Forsberg, A., Engler, H., Hagman, G., Lärksäter, M., Winblad, B. G., Zetterberg, H., et al. (2008) · Annals of Neurology · doi:10.1002/ana.21345 · Cited by 132

Small-Molecule Structure Correctors Target Abnormal Protein Structure and Function: Structure Corrector Rescue of Apolipoprotein E4–Associated Neuropathology: Miniperspective

Mahley, R. W., & Huang, Y. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm3008618 · Cited by 132

Alzheimer's disease; taking the edge off with cannabinoids?

Campbell, V. A., & Gowran, A. (2007) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0707446 · Cited by 132

Treatment Strategies Targeting Amyloid -ProteinPreprint

Schenk, D., Basi, G. S., & Pangalos, M. N. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006387 · Cited by 131

Anandamide and 2-arachidonoylglycerol: Pharmacological Properties, Functional Features, and Emerging Specificities of the Two Major Endocannabinoids

Luchicchi, A., & Pistis, M. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8299-0 · Cited by 130

Therapeutic targets and potential of the novel brain‐ permeable multifunctional iron chelator–monoamine oxidase inhibitor drug, M‐30, for the treatment of Alzheimer's disease1

Avramovich‐Tirosh, Y., Amit, T., Bar‐Am, O., Zheng, H., Fridkin, M., & Youdim, M. B. H. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04258.x · Cited by 130

NSAIDs: small molecules for prevention of Alzheimer's disease or precursors for future drug development?

Weggen, S., Rogers, M. V., & Eriksen, J. L. (2007) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2007.09.004 · Cited by 127

Dementia care costs and outcomes: a systematic review

Knapp, M., Iemmi, V., & Romeo, R. (2013) · International Journal of Geriatric Psychiatry · doi:10.1002/gps.3864 · Cited by 126

Nuclear receptors as therapeutic targets for Alzheimer's disease

Mandrekar-Colucci, S., & Landreth, G. E. (2011) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2011.594043 · Cited by 126

Memantine in patients with Alzheimer's disease receiving donepezil: new analyses of efficacy and safety for combination therapy

Atri, A., Molinuevo, J. L., Lemming, O., Wirth, Y., Pulte, I., & Wilkinson, D. (2013) · Alzheimer's Research & Therapy · doi:10.1186/alzrt160 · Cited by 126

3D Structure of Torpedo californica Acetylcholinesterase Complexed with Huprine X at 2.1 Å Resolution: Kinetic and Molecular Dynamic Correlates,

Dvir, H., Wong, D. M., Harel, M., Barril, X., Orozco, M., Luque, F. J., Muñoz‐Torrero, D., Camps, P., Rosenberry, T. L., Silman, I., et al. (2002) · Biochemistry · doi:10.1021/bi011652i · Cited by 125

The “LEARn” (Latent Early-life Associated Regulation) model integrates environmental risk factors and the developmental basis of Alzheimer’s disease, and proposes remedial steps

Lahiri, D. K., & Maloney, B. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.01.001 · Cited by 124

Current therapeutic targets for the treatment of Alzheimer’s disease

Grill, J. D., & Cummings, J. L. (2010) · Expert Review of Neurotherapeutics · doi:10.1586/ern.10.29 · Cited by 123

An Overview of Phenserine Tartrate, A Novel Acetylcholinesterase Inhibitor for the Treatment of Alzheimers Disease

Greig, N. H., Sambamurti, K., Yu, Q.-S., Brossi, A. R., Bruinsma, G., & Lahiri, D. K. (2005) · Current Alzheimer Research · doi:10.2174/1567205054367829 · Cited by 122

TV3326, a novel neuroprotective drug with cholinesterase and monoamine oxidase inhibitory activities for the treatment of Alzheimer’s disease

Weinstock, M., Bejar, C., Wang, R.-H., Poltyrev, T., Gross, A., Finberg, J. P. M., & Youdim, M. B. H. (2000) · Springer eBooks · doi:10.1007/978-3-7091-6301-6_10 · Cited by 120

Minocycline corrects early, pre-plaque neuroinflammation and inhibits BACE-1 in a transgenic model of Alzheimer's disease-like amyloid pathology

Ferretti, M. T., Allard, S., Partridge, V., Ducatenzeiler, A., & Cuello, A. C. (2012) · Journal of Neuroinflammation · doi:10.1186/1742-2094-9-62 · Cited by 120

nNOS Expressing Neurons in the Entorhinal Cortex and Hippocampus Are Affected in Patients with Alzheimer's Disease

Thorns, V., Hansen, L., & Masliah, E. (1998) · Experimental Neurology · doi:10.1006/exnr.1997.6751 · Cited by 119

Terminal dUTP nick end labeling (TUNEL) positive cells in the different regions of the brain in normal aging and alzheimer patients

Li, W. P., Chan, W. Y., Lai, H. W. L., & Yew, D. T. (1997) · Journal of Molecular Neuroscience · doi:10.1007/bf02736774 · Cited by 118

Altered synaptic function in Alzheimer's disease

Bell, K. F. S., & Cuello, A. C. (2006) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2006.06.045 · Cited by 117

Activation of the CB1 cannabinoid receptor protects cultured mouse spinal neurons against excitotoxicity

Abood, M. E., Rizvi, G., Sallapudi, N., & McAllister, S. D. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(01)02065-1 · Cited by 116

Structure-dependent Impairment of Intracellular Apolipoprotein E4 Trafficking and Its Detrimental Effects Are Rescued by Small-molecule Structure Correctors

Brodbeck, J., McGuire, J., Liu, Z., Meyer-Franke, A., Balestra, M. E., Jeong, D.-E., Pleiss, M., McComas, C., Hess, F., Witter, D., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.217380 · Cited by 113

Combating Alzheimer's Disease With Multifunctional Molecules Designed for Metal Passivation

Schugar, H. J., Green, D. E., Bowen, M. L., Scott, L. E., Storr, T., Böhmerle, K., Thomas, F. C., Allen, D. D., Lockman, P. R., Merkel, M., et al. (2007) · Angewandte Chemie International Edition · doi:10.1002/anie.200603866 · Cited by 112

Timosaponin AIII, a saponin isolated from Anemarrhena asphodeloides, ameliorates learning and memory deficits in mice

Lee, B., Jung, K., & Kim, D. (2009) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2009.04.021 · Cited by 111

Multi Target Neuroprotective and Neurorestorative Anti-Parkinson and Anti-Alzheimer Drugs Ladostigil and M30 Derived from Rasagiline

Youdim, M. B. H. (2013) · Experimental Neurobiology · doi:10.5607/en.2013.22.1.1 · Cited by 111

A Review on the Monoacylglycerol Lipase: At the Interface Between Fat and Endocannabinoid Signalling

Labar, G., Wouters, J., & Lambert, D. M. (2010) · Current Medicinal Chemistry · doi:10.2174/092986710791859414 · Cited by 111

Multifunctional Neuroprotective Derivatives of Rasagiline as Anti-Alzheimer's Disease Drugs

Weinreb, O., Mandel, S. A., Bar‐Am, O., Yogev‐Falach, M., Avramovich‐Tirosh, Y., Amit, T., & Youdim, M. B. H. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.10.030 · Cited by 110

Apoptosis of astrocytes with enhanced lysosomal activity and oligodendrocytes in white matter lesions in Alzheimer's disease

Kobayashi, K., Hayashi, M., Nakano, H., Fukutani, Y., Sasaki, K., Shimazaki, M., & Koshino, Y. (2002) · Neuropathology and Applied Neurobiology · doi:10.1046/j.1365-2990.2002.00390.x · Cited by 110

The Multiplicity of Action of Cannabinoids: Implications for Treating Neurodegeneration

Gowran, A., Noonan, J., & Campbell, V. A. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00195.x · Cited by 109

Cannabinoids and Neuroprotection

Beltramo, M., Grundy, R. I., & Rabuffetti, M. (2001) · Molecular Neurobiology · doi:10.1385/mn:24:1-3:029 · Cited by 109

Neuroprotective and Cholinergic Properties of Multifunctional Glutamic Acid Derivatives for the Treatment of Alzheimer’s Disease

Arce, M. P., Rodrı́guez-Franco, M. I., González-Muñoz, G. C., Pérez, C., López, B., Villarroya, M., López, M. G., Garcı́a, A. G., & Conde, S. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900628z · Cited by 109

Inhibition of monoamine oxidase B by selective adenosine A2A receptor antagonists

Petzer, J. P., Steyn, S., Castagnoli, K., Chen, J., Schwarzschild, M. A., der Schyf, C. J. V., & Castagnoli, N. (2003) · Bioorganic & Medicinal Chemistry · doi:10.1016/s0968-0896(02)00648-x · Cited by 108

Acetylcholinesterase enzyme inhibitory potential of standardized extract of Trigonella foenum graecum L and its constituents

Satheeshkumar, N., Mukherjee, P. K., Bhadra, S., & Saha, B. P. (2009) · Phytomedicine · doi:10.1016/j.phymed.2009.06.006 · Cited by 107

Protective Effects of Ferulic Acid in Amyloid Precursor Protein Plus Presenilin-1 Transgenic Mouse Model of Alzheimer Disease

Yan, J.-J., Jung, J., Kim, T.-K., Hasan, M. A., Hong, C.-W., Nam, J., & Song, D. (2012) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.b12-00798 · Cited by 107

Huperzine A protects isolated rat brain mitochondria against β-amyloid peptide

Gao, X., Zheng, C. Y., Yang, L., Tang, X. C., & Zhang, H. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.02.028 · Cited by 103

Design, synthesis and biological evaluation of novel dual inhibitors of acetylcholinesterase and β-secretase

Zhu, Y., Xiao, K., Ma, L., Xiong, B., Fu, Y., Yu, H., Wang, W., Wang, X., Hu, D., Peng, H., et al. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.12.067 · Cited by 102

Targeting Synaptic Dysfunction in Alzheimer’s Disease Therapy

Nisticò, R., Pignatelli, M., Piccinin, S., Mercuri, N. B., & Collingridge, G. L. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8324-3 · Cited by 102

Do NSAIDs prevent Alzheimer's disease? And, if so, why? The epidemiological evidence

Zandi, P. P. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00297-4 · Cited by 101

What the halted phase III γ‐secretase inhibitor trial may (or may not) be telling us

Schor, N. F. (2011) · Annals of Neurology · doi:10.1002/ana.22365 · Cited by 101

Molecular Insights into Human Monoamine Oxidase B Inhibition by the Glitazone Antidiabetes Drugs

Binda, C., Aldeco, M., Geldenhuys, W. J., Tortorici, M., Mattevi, A., & Edmondson, D. E. (2011) · ACS Medicinal Chemistry Letters · doi:10.1021/ml200196p · Cited by 100

Novel Dimeric Acetylcholinesterase Inhibitor Bis(7)-tacrine, but Not Donepezil, Prevents Glutamate-induced Neuronal Apoptosis by Blocking N-Methyl-d-aspartate Receptors

Li, W., Pi, R., Chan, H. H. N., Fu, H., Lee, N. T. K., Tsang, H. W., Pu, Y., Chang, D. C., Li, Z., Luo, J., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m411085200 · Cited by 100

Memantine hydrochloride

Witt, A. S., MacDonald, N. C., & Kirkpatrick, P. N. (2004) · Nature Reviews Drug Discovery · doi:10.1038/nrd1311 · Cited by 100

Structure-Function Implications in Alzheimers Disease: Effect of Aβ Oligomers at Central Synapses

Cerpa, W. F., Dinamarca, M. C., & Inestrosa, N. C. (2008) · Current Alzheimer Research · doi:10.2174/156720508784533321 · Cited by 99

Asiatic acid protects primary neurons against C2-ceramide-induced apoptosis

Zhang, X., Wu, J., Dou, Y., Xia, B., Rong, W., Rimbach, G., & Lou, Y. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.01.006 · Cited by 99

Targeting Alzheimer’s disease: Novel indanone hybrids bearing a pharmacophoric fragment of AP2238

Rizzo, S., Bartolini, M., Ceccarini, L., Piazzi, L., Gobbi, S., Cavalli, A., Recanatini, M., Andrisano, V., & Rampa, A. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.01.071 · Cited by 99

Cholinergic and glutamatergic alterations beginning at the early stages of Alzheimer disease: participation of the phospholipase A2 enzyme

Schaeffer, E. L., & Gattaz, W. F. (2008) · Psychopharmacology · doi:10.1007/s00213-008-1092-0 · Cited by 98

Is RAGE Still A Therapeutic Target For Alzheimer’s Disease?

Deane, R. J. (2012) · Future Medicinal Chemistry · doi:10.4155/fmc.12.51 · Cited by 97

Activated mTOR and PKR Kinases in Lymphocytes Correlate with Memory and Cognitive Decline in Alzheimer’s Disease

Paccalin, M., Pain-Barc, S., Pluchon, C., Paul, C., Besson, M.-N., Carret-Rebillat, A.-S., Rioux-Bilan, A., Gil, R., & Hugon, J. (2006) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000095562 · Cited by 96

Bioactive Iridoid Glucosides from the Fruit of Gardenia jasminoides

Yu, Y., Xie, Z., Gao, H., Ma, W., Dai, Y., Wang, Y., Zhong, Y., & Yao, X. (2009) · Journal of Natural Products · doi:10.1021/np900176q · Cited by 95

Latrepirdine (Dimebon®), a potential Alzheimer therapeutic, regulates autophagy and neuropathology in an Alzheimer mouse model

Steele, J., & Gandy, S. (2013) · Autophagy · doi:10.4161/auto.23487 · Cited by 95

Withanolide A and Asiatic Acid Modulate Multiple Targets Associated with Amyloid-β Precursor Protein Processing and Amyloid-β Protein Clearance

Patil, S. P., Maki, S., Khedkar, S. A., Rigby, A. C., & Chan, C. (2010) · Journal of Natural Products · doi:10.1021/np900633j · Cited by 92

Huprine-tacrine heterodimers as anti-amyloidogenic compounds of potential interest against Alzheimer's and prion diseases.

Galdeano, C., Viayna, E., Sola, I., Formosa, X., Camps, P., Badía, A., Clos, M. V., Relat, J., Ratia, M., Bartolini, M., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm200840c · Cited by 91

An update on amine oxidase inhibitors: Multifaceted drugs

Song, M.-S., Matveychuk, D., MacKenzie, E. M., Duchcherer, M., Mousseau, D. D., & Baker, G. B. (2013) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2013.02.001 · Cited by 90

Fructus Gardenia ( Gardenia jasminoides J. Ellis) phytochemistry, pharmacology of cardiovascular, and safety with the perspective of new drugs development

Liu, H., Chen, Y., Li, F., & Zhang, H. (2012) · Journal of Asian Natural Products Research · doi:10.1080/10286020.2012.723203 · Cited by 90

The Role of Autophagy in Age-Related Neurodegeneration

McCray, B. A., & Taylor, J. P. (2007) · Neurosignals · doi:10.1159/000109761 · Cited by 90

Synthesis, biological evaluation of 9-N-substituted berberine derivatives as multi-functional agents of antioxidant, inhibitors of acetylcholinesterase, butyrylcholinesterase and amyloid-β aggregation

Shan, W., Huang, L., Zhou, Q., Meng, F.-C., & Li, X. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.09.051 · Cited by 89

Okadaic acid-induced Tau phosphorylation in rat brain: Role of NMDA receptor

Kamat, P., Rai, S., Swarnkar, S., Shukla, R., Ali, S., Najmi, A. K., & Nath, C. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.01.075 · Cited by 89

2,3‐Dihydro‐1‐Benzofuran Derivatives as a Series of Potent Selective Cannabinoid Receptor 2 Agonists: Design, Synthesis, and Binding Mode Prediction through Ligand‐Steered Modeling

Diaz, P., Phatak, S. S., Xu, J. J., Fronczek, F. R., Astruc‐Diaz, F., Thompson, C. M., Cavasotto, C. N., & Naguib, M. (2009) · ChemMedChem · doi:10.1002/cmdc.200900226 · Cited by 88

Benzenediol-berberine hybrids: Multifunctional agents for Alzheimer’s disease

Jiang, H., Wang, X., Huang, L., Luo, Z., Su, T., Ding, K., & Li, X. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.09.040 · Cited by 88

Regulation of alpha-secretase ADAM10 expression and activity

Endres, K., & Fahrenholz, F. (2011) · Experimental Brain Research · doi:10.1007/s00221-011-2885-7 · Cited by 87

TDP-43 in central nervous system development and function: clues to TDP-43-associated neurodegeneration

Sephton, C. F., Cenik, B., Cenik, B. K., Herz, J., & Yu, G. (2012) · bchm · doi:10.1515/hsz-2012-0115 · Cited by 86

Design, synthesis, and evaluation of indanone derivatives as acetylcholinesterase inhibitors and metal-chelating agents

Meng, F.-C., Mao, F., Shan, W., Qin, F., Huang, L., & Li, X. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.04.029 · Cited by 86

CB1 Cannabinoid Receptor Activation Rescues Amyloid ß-Induced Alterations in Behaviour and Intrinsic Electrophysiological Properties of Rat Hippocampal CA1 Pyramidal Neurones

Haghani, M., Shabani, M., Javan, M., Motamedi, F., & Janahmadi, M. (2012) · Cellular Physiology and Biochemistry · doi:10.1159/000338494 · Cited by 86

Three distinct neuroprotective functions of myricetin against glutamate‐induced neuronal cell death: Involvement of direct inhibition of caspase‐3

Shimmyo, Y., Kihara, T., Akaike, A., Niidome, T., & Sugimoto, H. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21629 · Cited by 85

Muscarinic agonists reduce tau phosphorylation in non-neuronal cells via GSK-3β inhibition and in neurons

Forlenza, O. V., Spink, J. M., Dayanandan, R., Anderton, B. H., Olesen, O. F., & Lovestone, S. (2000) · Journal of Neural Transmission · doi:10.1007/s007020070034 · Cited by 85

Cystamine-tacrine dimer: A new multi-target-directed ligand as potential therapeutic agent for Alzheimer’s disease treatment

Minarini, A., Milelli, A., Tumiatti, V., Rosini, M., Simoni, E., Bolognesi, M. L., Andrisano, V., Bartolini, M., Motori, E., Angeloni, C., et al. (2011) · Neuropharmacology · doi:10.1016/j.neuropharm.2011.10.007 · Cited by 85

The Role of the Endocannabinoid System in Alzheimers Disease: Facts and Hypotheses

Bisogno, T., & Marzo, V. D. (2008) · Current Pharmaceutical Design · doi:10.2174/138161208785740027 · Cited by 84

The Path from Anti Parkinson Drug Selegiline and Rasagiline to Multifunctional Neuroprotective Anti Alzheimer Drugs Ladostigil and M30

Youdim, M. B. H. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025288 · Cited by 84

In vitro protective effects of Withania somnifera (L.) dunal root extract against hydrogen peroxide and β‐amyloid(1–42)‐induced cytotoxicity in differentiated PC12 cells

Kumar, S., Seal, C. J., Howes, M. R., Kite, G. C., & Okello, E. J. (2010) · Phytotherapy Research · doi:10.1002/ptr.3261 · Cited by 84

Latrepirdine stimulates autophagy and reduces accumulation of α-synuclein in cells and in mouse brain

Steele, J., Ju, S., Lachenmayer, M. L., Liken, J., Stock, A., Kim, S. Y., Delgado, L. M., Alfaro, I. E., Bernales, S., Verdile, G., et al. (2012) · Molecular Psychiatry · doi:10.1038/mp.2012.115 · Cited by 82

Drugs: A tangled web of targets

Gravitz, L. (2011) · Nature · doi:10.1038/475s9a · Cited by 81

Design, synthesis and evaluation of novel tacrine-multialkoxybenzene hybrids as dual inhibitors for cholinesterases and amyloid beta aggregation

Luo, W., Li, Y., He, Y., Huang, S., Tan, J., Ou, T., Li, D., Gu, L., & Huang, Z. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.12.022 · Cited by 81

β-secretase (BACE1)-inhibiting stilbenoids from Smilax Rhizoma

Jeon, S. Y., Kwon, S.-H., Seong, Y. H., Bae, K., Hur, J.-M., Lee, Y.-Y., Suh, D., & Song, K. S. (2006) · Phytomedicine · doi:10.1016/j.phymed.2006.09.003 · Cited by 81

Acetylcholinesterase Noncovalent Inhibitors Based on a Polyamine Backbone for Potential Use against Alzheimer's Disease

Melchiorre, C., Andrisano, V., Bolognesi, M. L., Budriesi, R., Cavalli, A., Cavrini, V., Rosini, M., Tumiatti, V., & Recanatini, M. (1998) · Journal of Medicinal Chemistry · doi:10.1021/jm9810452 · Cited by 81

Sirtuins in cognitive ageing and Alzheimer's disease

Braidy, N., Jayasena, T., Poljak, A., & Sachdev, P. S. (2012) · Current Opinion in Psychiatry · doi:10.1097/yco.0b013e32835112c1 · Cited by 81

Epigenetic programming of neurodegenerative diseases by an adverse environment

Babenko, O., Kovalchuk, I., & Metz, G. A. S. (2012) · Brain Research · doi:10.1016/j.brainres.2012.01.038 · Cited by 80

Cellular Source of Apolipoprotein E4 Determines Neuronal Susceptibility to Excitotoxic Injury in Transgenic Mice

Buttini, M., Masliah, E., Yu, G.-Q., Palop, J. J., Chang, S., Bernardo, A., Lin, C., Wyss-Coray, T., Huang, Y., & Mucke, L. (2010) · The American Journal of Pathology · doi:10.2353/ajpath.2010.090973 · Cited by 80

Bis-(−)-nor-meptazinols as Novel Nanomolar Cholinesterase Inhibitors with High Inhibitory Potency on Amyloid-β Aggregation

Xie, Q., Wang, H., Xia, Z., Lu, M., Zhang, W., Wang, X., Fu, W., Tang, Y., Sheng, W., Li, W., et al. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm070154q · Cited by 80

Synergistic neuroprotective effect of combined low concentrations of galantamine and melatonin against oxidative stress in SH‐SY5Y neuroblastoma cells

Romero, A., Egea, J., Garcı́a, A. G., & López, M. G. (2010) · Journal of Pineal Research · doi:10.1111/j.1600-079x.2010.00778.x · Cited by 79

Curcuminoids and resveratrol as anti-Alzheimer agents

Villaflores, O. B., Chen, Y., Chen, C., Yeh, J., & Wu, T. (2012) · Taiwanese Journal of Obstetrics and Gynecology · doi:10.1016/j.tjog.2012.09.005 · Cited by 79

Pharmacological Characterization of Memoquin, a Multi-Target Compound for the Treatment of Alzheimer's Disease

Capurro, V., Busquet, P., Lopes, J. P., Bertorelli, R., Tarozzo, G., Bolognesi, M. L., Piomelli, D., Reggiani, A. M., & Cavalli, A. (2013) · PLoS ONE · doi:10.1371/journal.pone.0056870 · Cited by 79

Opioid System and Alzheimer’s Disease

Cai, Z., & Ratka, A. (2012) · NeuroMolecular Medicine · doi:10.1007/s12017-012-8180-3 · Cited by 79

A non-cholinergic, trophic action of acetylcholinesterase on hippocampal neurones in vitro: molecular mechanisms

Day, T., & Greenfield, S. A. (2002) · Neuroscience · doi:10.1016/s0306-4522(02)00031-3 · Cited by 79

Alzheimer's Disease: Recent Advances and Future Perspectives

Ubhi, K. K., & Masliah, E. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129028 · Cited by 78

Alzheimer's Disease and Co-Morbidity: Increased Prevalence and Possible Risk Factors of Excess Mortality in a Naturalistic 7-Year Follow-Up

Heun, R., Schoepf, D., Potluri, R., & Natalwala, A. (2011) · European Psychiatry · doi:10.1016/j.eurpsy.2011.06.001 · Cited by 78

Dietary Regulation of Histone Acetylases and Deacetylases for the Prevention of Metabolic Diseases

Pham, T. X., & Lee, J. (2012) · Nutrients · doi:10.3390/nu4121868 · Cited by 78

Dual inhibition of monoamine oxidase B and antagonism of the adenosine A2A receptor by (E,E)-8-(4-phenylbutadien-1-yl)caffeine analogues

Pretorius, J., Malan, S. F., Castagnoli, N., Bergh, J. J., & Petzer, J. P. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.07.088 · Cited by 77

Synthesis, biological evaluation and molecular modeling of oxoisoaporphine and oxoaporphine derivatives as new dual inhibitors of acetylcholinesterase/butyrylcholinesterase

Tang, H., Wei, Y., Zhang, C., Ning, F.-X., Qiao, W., Huang, S., Ma, L., Huang, Z., & Gu, L. (2009) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2009.01.021 · Cited by 75

First and Second Generation γ-Secretase Modulators (GSMs) Modulate Amyloid-β (Aβ) Peptide Production through Different Mechanisms

Borgegård, T., Juréus, A., Olsson, F., Rosqvist, S., Sabirsh, A., Rotticci, D., Paulsen, K., Klintenberg, R., Yan, H., Waldman, M., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.305227 · Cited by 75

Role of the endocannabinoid system in Alzheimer's disease: New perspectives

Pazos, M. R., Núñez, E., Benito, C., Tolón, R. M., & Romero, J. (2004) · Life Sciences · doi:10.1016/j.lfs.2004.03.026 · Cited by 75

Searching for the Multi-Target-Directed Ligands against Alzheimer’s disease: Discovery of quinoxaline-based hybrid compounds with AChE, H3R and BACE 1 inhibitory activities

Huang, W., Tang, L., Shi, Y., Huang, S., Xu, L., Sheng, R., Wu, P., Li, J. X., Zhou, N., & Hu, Y. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.09.061 · Cited by 75

Ubiquitin receptors and protein quality control

Wang, X., & Terpstra, E. J. M. (2012) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2012.09.012 · Cited by 75

New tacrine-dihydropyridine hybrids that inhibit acetylcholinesterase, calcium entry, and exhibit neuroprotection properties

Leon, R. M., Rı́os, C. D. L., Marco, J. L., Huertas, Ó., Barril, X., Luque, F. J., López, M. G., Garcı́a, A. G., & Villarroya, M. (2008) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2008.07.005 · Cited by 74

Focusing on New Monoamine Oxidase Inhibitors: Differently Substituted Coumarins As An Interesting Scaffold

Matos, M. J., Viña, D., Vázquez-Rodríguez, S., Uriarte, E., & Santana, L. (2012) · Current Topics in Medicinal Chemistry · doi:10.2174/156802612805220002 · Cited by 74

In vitro biological activities of niloticane, a new bioactive cassane diterpene from the bark of Acacia nilotica subsp. kraussiana

Eldeen, I. M. S., van Heerden, F. R., & Staden, J. V. (2010) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2010.01.057 · Cited by 73

The immunopathogenic role of reactive oxygen species in Alzheimer disease.

Mohsenzadegan, M., & Mirshafiey, A. (2012) · PubMed · Cited by 73

[+]-Huperzine A treatment protects against N-methyl-d-aspartate-induced seizure/status epilepticus in rats

Coleman, B. R., Ratcliffe, R. H., Oguntayo, S., Shi, X., Doctor, B. P., Gordon, R. K., & Nambiar, M. P. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.05.023 · Cited by 72

Novel NMDA receptor modulators: an update

Santangelo, R., Acker, T. M., Zimmerman, S. S., Katzman, B. M., Strong, K. L., Traynelis, S. F., & Liotta, D. C. (2012) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.2012.728587 · Cited by 72

Binding of Curcumin to Senile Plaques and Cerebral Amyloid Angiopathy in the Aged Brain of Various Animals and to Neurofibrillary Tangles in Alzheimer's Brain

Mutsuga, M., CHAMBERS, J. K., Uchida, K., Tei, M., MAKIBUCHI, T., 溝呂木達也, Takashima, A., & Nakayama, H. (2011) · Journal of Veterinary Medical Science · doi:10.1292/jvms.11-0307 · Cited by 72

Inhibition of monoamine oxidase B by selected benzimidazole and caffeine analogues

van den Berg, D., Zoellner, K. R., Ogunrombi, M. O., Malan, S. F., Terre’Blanche, G., Castagnoli, N. J., Bergh, J. J., & Petzer, J. P. (2007) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.03.046 · Cited by 72

Phospholipase A2 activation as a therapeutic approach for cognitive enhancement in early-stage Alzheimer disease

Schaeffer, E. L., Forlenza, O. V., & Gattaz, W. F. (2009) · Psychopharmacology · doi:10.1007/s00213-008-1351-0 · Cited by 71

Co-morbidity and drug treatment in Alzheimer's disease. A cross sectional study of participants in the Dementia Study in Northern Norway

Andersen, F., Viitanen, M. H., Halvorsen, D. S., Straume, B., & Engstad, T. A. (2011) · BMC Geriatrics · doi:10.1186/1471-2318-11-58 · Cited by 71

2-Arylbenzofuran-based molecules as multipotent Alzheimer's disease modifying agents

Rizzo, S., Tarozzi, A., Bartolini, M., Costa, G. D., Bisi, A., Gobbi, S., Belluti, F., Ligresti, A., Allarà, M., Monti, J., et al. (2012) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2012.10.045 · Cited by 70

PDE 7 Inhibitors: New Potential Drugs for the Therapy of Spinal Cord Injury

Paterniti, I., Mazzon, E., Gil, C., Impellizzeri, D., Palomo, V., Redondo, M., Pérez, D. I., Esposito, E., Martı́nez, A., & Cuzzocrea, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0015937 · Cited by 70

Designed Multiple Ligands: Basic Research vs Clinical Outcomes

Costantino, L., & Barlocco, D. (2012) · Current Medicinal Chemistry · doi:10.2174/092986712801215883 · Cited by 69

LMN diet, rich in polyphenols and polyunsaturated fatty acids, improves mouse cognitive decline associated with aging and Alzheimer's disease

Fernández-Fernández, L., Comes, G., Bolea, I., Valente, T., Ruiz, J., Murtra, P., Ramírez, B., Anglès, N., Reguant, J., Morelló, J. R., et al. (2011) · Behavioural Brain Research · doi:10.1016/j.bbr.2011.11.014 · Cited by 68

HU-211, a nonpsychotropic cannabinoid, rescues cortical neurones from excitatory amino acid toxicity in culture

Eshhar, N., Striem, S., & Biegon, A. R. (1993) · Neuroreport · doi:10.1097/00001756-199312000-00013 · Cited by 68

Hybrids of oxoisoaporphine-tacrine congeners: Novel acetylcholinesterase and acetylcholinesterase-induced β-amyloid aggregation inhibitors

Tang, H., Zhao, L.-Z., Zhao, H., Huang, S., Zhong, S., Qin, J., Chen, Z., Huang, Z., & Liang, H. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.08.002 · Cited by 68

The memory ameliorating effects of INM-176, an ethanolic extract of Angelica gigas, against scopolamine- or Aβ1–42-induced cognitive dysfunction in mice

Park, S. J., Jung, J. M., Lee, H. E., Lee, Y. W., Kim, D. H., Kim, J. M., Hong, J. G., Lee, C. H., Jung, I. H., Cho, Y.-B., et al. (2012) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2012.07.019 · Cited by 67

Multitargeted drugs discovery: Balancing anti-amyloid and anticholinesterase capacity in a single chemical entity

Bolognesi, M. L., Bartolini, M., Tarozzi, A., Morroni, F., Lizzi, F., Milelli, A., Minarini, A., Rosini, M., Hrelia, P., Andrisano, V., et al. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.12.093 · Cited by 67

Acetylcholinesterase induces neuronal cell loss, astrocyte hypertrophy and behavioral deficits in mammalian hippocampus

Chacón, M. A., Reyes, A. E., & Inestrosa, N. C. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01985.x · Cited by 66

Methylene Blue as a Cerebral Metabolic and Hemodynamic Enhancer

Lin, A., Poteet, E. C., Du, F., Choudhury, G. R., Liu, R., Wen, Y., Bresnen, A., Huang, S., Fox, P. T., Yang, S.-H., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046585 · Cited by 66

Autophagy Modulation for Alzheimer’s Disease Therapy

Zhu, X., Yu, J., Jiang, T., & Tan, L. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8457-z · Cited by 66

In-vivo histamine H3 receptor antagonism activates cellular signaling suggestive of symptomatic and disease modifying efficacy in Alzheimer’s disease

Bitner, R. S., Markosyan, S., Nikkel, A. L., & Brioni, J. D. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.10.026 · Cited by 65

The Bad, the Good, and the Ugly about Oxidative Stress

Jiménez-Del-Río, M., & Velez‐Pardo, C. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/163913 · Cited by 65

Synthesis, in vitro assay, and molecular modeling of new piperidine derivatives having dual inhibitory potency against acetylcholinesterase and Aβ1–42 aggregation for Alzheimer’s disease therapeutics

Kwon, Y. E., Park, J. Y., No, K. T., Shin, J. H., Lee, S. K., Eun, J. S., Yang, J. H., Shin, T. Y., Kim, D. K., Chae, B. S., et al. (2007) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2007.07.003 · Cited by 64

The Cholinergic Neuronal Phenotype in Alzheimer's Disease

Blusztajn, J. K., & Berse, B. (2000) · Metabolic Brain Disease · doi:10.1007/bf02680013 · Cited by 64

The proteins BACE1 and BACE2 and β-secretase activity in normal and Alzheimer's disease brain

Stockley, J. H., & O’Neill, C. (2007) · Biochemical Society Transactions · doi:10.1042/bst0350574 · Cited by 64

L-3-n-butylphthalide Reduces Tau Phosphorylation and Improves Cognitive Deficits in AβPP/PS1-Alzheimer's Transgenic Mice

Peng, Y., Hu, Y., Xu, S., Li, P., Jiang, L., Lu, L., Yang, H., Feng, N., Wang, L., & Wang, X. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-111577 · Cited by 63

Novel Huprine Derivatives with Inhibitory Activity toward β‐Amyloid Aggregation and Formation as Disease‐Modifying Anti‐Alzheimer Drug Candidates

Viayna, E., Gómez, T., Galdeano, C., Ramírez, L., Ratia, M., Badı́a, A., Clos, M. V., Verdaguer, E., Junyent, F., Camins, A., et al. (2010) · ChemMedChem · doi:10.1002/cmdc.201000322 · Cited by 63

A global view of Hsp90 functions

Chiosis, G., Dickey, C. A., & Johnson, J. L. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2481 · Cited by 63

Ensaculin (KA‐672. HCl): A Multitransmitter Approach to Dementia Treatment

Hoerr, R., & Noeldner, M. (2002) · CNS Drug Reviews · doi:10.1111/j.1527-3458.2002.tb00220.x · Cited by 63

From Anti-Parkinson's Drug Rasagiline to Novel Multitarget Iron Chelators with Acetylcholinesterase and Monoamine Oxidase Inhibitory and Neuroprotective Properties for Alzheimer's Disease

Zheng, H., Amit, T., Bar‐Am, O., Fridkin, M., Youdim, M. B. H., & Mandel, S. A. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-120013 · Cited by 62

Further Studies on the Interaction of the 5-Hydroxytryptamine3(5-HT3) Receptor with Arylpiperazine Ligands. Development of a New 5-HT3Receptor Ligand Showing Potent Acetylcholinesterase Inhibitory Properties

Cappelli, A., Gallelli, A., Manini, M., Anzini, M., Mennuni, L., Makovec, F., Menziani, M. C., Alcaro, S., Ortuso, F., & Vomero, S. (2005) · Journal of Medicinal Chemistry · doi:10.1021/jm0493461 · Cited by 62

Synthesis, biological evaluation and molecular modeling of novel triazole-containing berberine derivatives as acetylcholinesterase and β-amyloid aggregation inhibitors

Shi, A., Huang, L., Lu, C., He, F., & Li, X. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.02.025 · Cited by 62

Hybrid-Based Multi-Target Ligands for the Treatment of Alzheimer's Disease

Rampa, A., Belluti, F., Gobbi, S., & Bisi, A. (2011) · Current Topics in Medicinal Chemistry · doi:10.2174/156802611798184409 · Cited by 62

Megalin interacts with APP and the intracellular adapter protein FE65 in neurons

Alvira, X., Pérez‐González, R., Spuch, C., Vargas, T., Antequera, D., Garzón, M., Bermejo‐Pareja, F., & Carro, E. (2010) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2010.07.005 · Cited by 61

Design, Synthesis, Biological Properties, and Molecular Modeling Investigations of Novel Tacrine Derivatives with a Combination of Acetylcholinesterase Inhibition and Cannabinoid CB1Receptor Antagonism

Lange, J. H. M., Coolen, H. K. A. C., van der Neut, M. A. W., Borst, A. J. M., Stork, B., Verveer, P. C., & Kruse, C. G. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901614b · Cited by 61

Rethinking Alzheimer's Disease Therapy: Are Mitochondria the Key?

Ankarcrona, M., Mangialasche, F., & Winblad, B. G. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100327 · Cited by 60

Physiological functions of the amyloid precursor protein secretases ADAM10, BACE1, and Presenilin

Prox, J., Rittger, A., & Säftig, P. (2011) · Experimental Brain Research · doi:10.1007/s00221-011-2952-0 · Cited by 60

Vicious Cycles Within the Neuropathophysiologic Mechanisms of Alzheimers Disease

Standridge, J. B. (2006) · Current Alzheimer Research · doi:10.2174/156720506776383068 · Cited by 60

Computational Evidence to Inhibition of Human Acetyl Cholinesterase by Withanolide A for Alzheimer Treatment

Grover, A., Shandilya, A., Agrawal, V., Bisaria, V. S., & Sundar, D. (2012) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2012.10507408 · Cited by 60

“Clicked” Bivalent Ligands Containing Curcumin and Cholesterol As Multifunctional Aβ Oligomerization Inhibitors: Design, Synthesis, and Biological Characterization

Lenhart, J. A., Ling Zhi, X. I. A. O., Gandhi, R., Guo, T. L., Gerk, P. M., Brunzell, D. H., & Zhang, S. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm100601q · Cited by 60

Luteolin Reduces Zinc-Induced Tau Phosphorylation at Ser262/356 in an ROS-Dependent Manner in SH-SY5Y Cells

Zhou, F., Chen, S., Xiong, J., Li, Y., & Qu, L. (2012) · Biological Trace Element Research · doi:10.1007/s12011-012-9411-z · Cited by 60

Acetylcholine: Future research and perspectives

van der Zee, E. A., Platt, B., & Riedel, G. (2011) · Behavioural Brain Research · doi:10.1016/j.bbr.2011.01.050 · Cited by 59

Anti-apoptotic and anti-oxidative mechanisms of minocycline against sphingomyelinase/ceramide neurotoxicity: implication in Alzheimer's disease and cerebral ischemia

Chen, S., Yin, J., Hwang, C., Tang, C.-M., & Yang, D. (2012) · Free Radical Research · doi:10.3109/10715762.2012.674640 · Cited by 59

Designing drugs with multi-target activity: the next step in the treatment of neurodegenerative disorders

Geldenhuys, W. J., & der Schyf, C. J. V. (2012) · Expert Opinion on Drug Discovery · doi:10.1517/17460441.2013.744746 · Cited by 59

Toxicity mediated by soluble oligomers of β‐amyloid(1–42) on cholinergic SN56.B5.G4 cells

Heinitz, K., Beck, M., Schliebs, R., & Perez-Polo, J. R. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04015.x · Cited by 58

Synthesis, biological assessment and molecular modeling of new dihydroquinoline-3-carboxamides and dihydroquinoline-3-carbohydrazide derivatives as cholinesterase inhibitors, and Ca channel antagonists

Tomassoli, I., Ismaïli, L., Pudlo, M., Rı́os, C. D. L., Soriano, E., Colmena, I., Gandı́a, L., Rivas, L., Samadi, A., Marco, J. L., et al. (2010) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2010.08.054 · Cited by 58

Dual-target-directed 1,3-diphenylurea derivatives: BACE 1 inhibitor and metal chelator against Alzheimer’s disease

Huang, W., Lv, D., Yu, H., Sheng, R., Kim, S. C., Wu, P., Luo, K., Li, J. X., & Hu, Y. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.06.042 · Cited by 58

Coexpression of striatal dopamine receptor subtypes and excitatory amino acid subunits

Ariano, M. A., Larson, E. R., Noblett, K. L., Sibley, D. R., & Levine, M. S. (1997) · Synapse · doi:10.1002/(sici)1098-2396(199708)26:4 · Cited by 57

Neurotrophic and Neuroprotective Actions of (−)- and (+)-Phenserine, Candidate Drugs for Alzheimer’s Disease

Lilja, A. M., Luo, Y., Yu, Q., Röjdner, J., Li, Y., Marini, A. M., Marutle, A., Nordberg, A. K., & Greig, N. H. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054887 · Cited by 57

Novel Anti-Alzheimer's Dimer Bis(7)-Cognitin: Cellular and Molecular Mechanisms of Neuroprotection Through Multiple Targets

Li, W., Mak, S., Jiang, H., Wang, Q., Pang, Y., Chen, K., & Han, Y. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.10.040 · Cited by 57

The mitochondria permeability transition pore complex in the brain with interacting proteins – promising targets for protection in neurodegenerative diseases

Azarashvili, T., Stricker, R., & Reiser, G. (2010) · Biological Chemistry · doi:10.1515/bc.2010.070 · Cited by 57

Pharmacotherapy of Alzheimer Disease

Seow, D. C. C., & Gauthier, S. G. (2007) · The Canadian Journal of Psychiatry · doi:10.1177/070674370705201003 · Cited by 56

A new strategy to combat Alzheimer’s disease. Combining radical-scavenging potential with metal-protein-attenuating ability in one molecule

Ji, H., & Zhang, H. (2004) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2004.10.047 · Cited by 54

Multiwell fluorometric and colorimetric microassays for the evaluation of beta-secretase (BACE-1) inhibitors

Mancini, F., Naldi, M., Cavrini, V., & Andrisano, V. (2007) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-007-1356-2 · Cited by 54

SLV330, a cannabinoid CB1 receptor antagonist, ameliorates deficits in the T-maze, object recognition and Social Recognition Tasks in rodents

de Bruin, N. M. W. J., Prickaerts, J., Lange, J. H. M., Akkerman, S., Andriambeloson, E., de Haan, M., Wijnen, J., Drimmelen, M. V., Hissink, E., Heijink, L., et al. (2010) · Neurobiology of Learning and Memory · doi:10.1016/j.nlm.2010.01.010 · Cited by 54

N-Acylaminophenothiazines: Neuroprotective agents displaying multifunctional activities for a potential treatment of Alzheimer’s disease

González-Muñoz, G. C., Arce, M. P., López, B., Pérez, C., Romero, A., del Barrio, L., Martin‐de‐Saavedra, M. D., Egea, J., Leon, R. M., Villarroya, M., et al. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.03.003 · Cited by 54

Search for dual function inhibitors for Alzheimer’s disease: Synthesis and biological activity of acetylcholinesterase inhibitors of pyridinium-type and their Aβ fibril formation inhibition capacity

Kapková, P., Alptüzün, V., Frey, P., Erciyas, E., & Holzgrabe, U. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.08.034 · Cited by 54

Novel oxoisoaporphine-based inhibitors of acetyl- and butyrylcholinesterase and acetylcholinesterase-induced beta-amyloid aggregation

Tang, H., Zhao, H.-T., Zhong, S., Wang, Z., Chen, Z., & Liang, H. (2012) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2012.01.090 · Cited by 53

Molecular and cellular mechanisms of apolipoprotein E4 neurotoxicity and potential therapeutic strategies.

Huang, Y. (2006) · PubMed · Cited by 53

Synthesis and biological evaluation of novel γ-carboline analogues of Dimebon as potent 5-HT6 receptor antagonists

Ivachtchenko, A. V., Frolov, E. B., Mitkin, O. D., Kysil, V. M., Khvat, A. V., Okun, I. M., & Tkachenko, S. E. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.04.128 · Cited by 52

Design, synthesis and structure–activity relationship (SAR) studies of 2,4-disubstituted pyrimidine derivatives: Dual activity as cholinesterase and Aβ-aggregation inhibitors

Mohamed, T., Zhao, X., Habib, L. K., Yang, J., & Rao, P. P. N. (2011) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2011.02.030 · Cited by 52

Physostigmine and Galanthamine Bind in the Presence of Agonist at the Canonical and Noncanonical Subunit Interfaces of a Nicotinic Acetylcholine Receptor

Hamouda, A. K., Kimm, T., & Cohen, J. B. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3483-12.2013 · Cited by 52

Design, synthesis and evaluation of isaindigotone derivatives as dual inhibitors for acetylcholinesterase and amyloid beta aggregation

Yan, J., Li, Y., Ye, W.-J., Chen, S.-B., Hou, J., Tan, J., Ou, T., Li, D., Gu, L., & Huang, Z. (2012) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2012.02.061 · Cited by 52

In Vitro BACE-1 Inhibitory Activity of Resveratrol Oligomers from the Seed Extract of Paeonia lactiflora

Choi, C., Choi, Y., Cha, M.-R., Kim, Y., Yon, G., Hong, K., Park, W.-K., Kim, Y., & Ryu, S. (2011) · Planta Medica · doi:10.1055/s-0030-1250370 · Cited by 52

The Potential Use of Hormone-Based Therapeutics for the Treatment of Alzheimers Disease

Carroll, J. C., & Rosario, E. R. (2012) · Current Alzheimer Research · doi:10.2174/156720512799015109 · Cited by 52

Targeting NADPH Oxidase and Phospholipases A2 in Alzheimer’s Disease

Simonyi, Á., He, Y., Sheng, W., Sun, A. Y., Wood, W. G., Weisman, G. A., & Sun, G. Y. (2010) · Molecular Neurobiology · doi:10.1007/s12035-010-8107-7 · Cited by 51

The therapeutic potential of the endocannabinoid system for Alzheimer's disease

Karl, T., Cheng, D., Garner, B., & Arnold, J. C. (2012) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.2012.671812 · Cited by 51

Iron-chelating backbone coupled with monoamine oxidase inhibitory moiety as novel pluripotential therapeutic agents for Alzheimer’s disease: a tribute to Moussa Youdim

Weinreb, O., Mandel, S. A., Bar‐Am, O., & Amit, T. (2011) · Journal of Neural Transmission · doi:10.1007/s00702-011-0597-6 · Cited by 51

Old phenothiazine and dibenzothiadiazepine derivatives for tomorrow’s neuroprotective therapies against neurodegenerative diseases

González-Muñoz, G. C., Arce, M. P., López, B., Pérez, C., Villarroya, M., López, M. G., Garcı́a, A. G., Conde, S., & Rodrı́guez-Franco, M. I. (2010) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2010.09.039 · Cited by 51

Acetylcholinesterase inhibitors from the toadstool Cortinarius infractus

Geissler, T., Brandt, W., Porzel, A., Schlenzig, D., Kehlen, A., Wessjohann, L. A., & Arnold, N. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.01.074 · Cited by 50

Design and synthesis of N-benzylpiperidine–purine derivatives as new dual inhibitors of acetyl- and butyrylcholinesterase

Rodrı́guez-Franco, M. I., Fernández‐Bachiller, M. I., Pérez, C., Castro, A., & Martı́nez, A. (2005) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2005.07.019 · Cited by 50

A Step Further Towards Multitarget Drugs for Alzheimer and Neuronal Vascular Diseases: Targeting the Cholinergic System, Amyloid-β Aggregation and Ca2++ Dyshomeostasis

Leon, R. M., & Marco-Contelles, J. L. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711794480186 · Cited by 49

Hybrid Compounds

Müller‐Schiffmann, A., Sticht, H., & Korth, C. (2011) · BioDrugs · doi:10.2165/11597630-000000000-00000 · Cited by 49

From BACE1 Inhibitor to Multifunctionality of Tryptoline and Tryptamine Triazole Derivatives for Alzheimer’s Disease

Jiaranaikulwanitch, J., Govitrapong, P., Fokin, V. V., & Vajragupta, O. (2012) · Molecules · doi:10.3390/molecules17078312 · Cited by 49

Emerging adenosine receptor agonists – an update

Gao, Z., & Jacobson, K. A. (2011) · Expert Opinion on Emerging Drugs · doi:10.1517/14728214.2011.644786 · Cited by 49

Amyloid β peptide levels and its effects on hippocampal acetylcholine release in aged, cognitively-impaired and -unimpaired rats

Vaucher, E., Aumont, N., Pearson, D., Rowe, W. B., Poirier, J., & Kar, S. (2001) · Journal of Chemical Neuroanatomy · doi:10.1016/s0891-0618(01)00120-x · Cited by 49

Allosteric modulators of the α4β2 subtype of neuronal nicotinic acetylcholine receptors

Pandya, A. A., & Yakel, J. L. (2011) · Biochemical Pharmacology · doi:10.1016/j.bcp.2011.04.020 · Cited by 48

Inhibitory effect of asiatic acid on acetylcholinesterase, excitatory post synapticpotential and locomotor activity

Nasir, M. N., Abdullah, J. M., Habsah, M., Ghani, R. I., & Rammes, G. (2011) · Phytomedicine · doi:10.1016/j.phymed.2011.10.004 · Cited by 48

Identification of novel monoamine oxidase B inhibitors by structure-based virtual screening

Geldenhuys, W. J., Darvesh, A. S., Funk, M. O., der Schyf, C. J. V., & Carroll, R. T. (2010) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2010.06.128 · Cited by 47

Benzophenone-based derivatives: A novel series of potent and selective dual inhibitors of acetylcholinesterase and acetylcholinesterase-induced beta-amyloid aggregation

Belluti, F., Bartolini, M., Bottegoni, G., Bisi, A., Cavalli, A., Andrisano, V., & Rampa, A. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.02.019 · Cited by 46

Potent β-Amyloid Modulators

García‐Palomero, E., Muñoz, P., Usán, P., Garcia, P., Delgado, E., de Austria, C., Valenzuela, R., Rubio, L., Medina, M., & Martı́nez, A. (2008) · Neurodegenerative Diseases · doi:10.1159/000113688 · Cited by 45

Structure–activity relationships of pentacycloundecylamines at the N-methyl-d-aspartate receptor

Geldenhuys, W. J., Malan, S. F., Bloomquist, J. R., & der Schyf, C. J. V. (2006) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2006.09.060 · Cited by 44

Interaction of (benzylidene-hydrazono)-1,4-dihydropyridines with β-amyloid, acetylcholine, and butyrylcholine esterases

Alptüzün, V., Prinz, M., Hörr, V., Scheiber, J., Radacki, K., Fallarero, A., Vuorela, P. M., Engels, B., Braunschweig, H., Erciyas, E., et al. (2010) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2010.01.002 · Cited by 44

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Lerner, A. J., Gustaw‐Rothenberg, K., Smyth, S., & Casadesus, G. (2012) · BioFactors · doi:10.1002/biof.196 · Cited by 44

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Sun, G. Y., He, Y., Chuang, D. Y., Lee, J. C., Gu, Z., Simonyi, Á., & Sun, A. Y. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8261-1 · Cited by 44

Selegiline treatment after transient global ischemia in gerbils enhances the survival of CA1 pyramidal cells in the hippocampus

Lahtinen, H., Koıstınaho, J., Kauppinen, R. A., Haapalinna, A., Keinänen, R., & Sivenius, J. (1997) · Brain Research · doi:10.1016/s0006-8993(97)00227-8 · Cited by 43

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Development of an Efficient Therapeutic Agent for Alzheimer's Disease: Design and Synthesis of Dual Inhibitors of Acetylcholinesterase and Serotonin Transporter

Toda, N., Kaneko, T., & Kogen, H. (2010) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.58.273 · Cited by 43

Bis(7)‐tacrine Derivatives as Multitarget‐Directed Ligands: Focus on Anticholinesterase and Antiamyloid Activities

Bolognesi, M. L., Bartolini, M., Mancini, F., Chiriano, G., Ceccarini, L., Rosini, M., Milelli, A., Tumiatti, V., Andrisano, V., & Melchiorre, C. (2010) · ChemMedChem · doi:10.1002/cmdc.201000086 · Cited by 42

Intracellular Degradation of Misfolded Tau Protein Induced by Geldanamycin is Associated with Activation of Proteasome

Opattová, A., Filipčík, P., Cente, M., & Novák, M. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121072 · Cited by 41

Inhibition of phospholipase A2 reduces neurite outgrowth and neuronal viability

Forlenza, O. V., Mendes, C. T., Marie, S. K. N., & Gattaz, W. F. (2006) · Prostaglandins Leukotrienes and Essential Fatty Acids · doi:10.1016/j.plefa.2006.10.002 · Cited by 41

Multi-target, Neuroprotective and Neurorestorative M30 Improves Cognitive Impairment and Reduces Alzheimer's-Like Neuropathology and Age-Related Alterations in Mice

Kupershmidt, L., Amit, T., Bar‐Am, O., Weinreb, O., & Youdim, M. B. H. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8304-7 · Cited by 41

Activation of α-secretase by curcumin-aminoacid conjugates

Narasingapa, R. B., Jargaval, M. R., Srinivas, P., Htoo, H. H., Rao, K. S. J., Hernandez, J., Govitrapong, P., & Vincent, B. (2012) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2012.07.010 · Cited by 41

The generic amyloid formation inhibition effect of a designed small aromatic β-breaking peptide

Frydman‐Marom, A., Shaltiel‐Karyo, R., Moshe, S., & Gazit, E. (2011) · Amyloid · doi:10.3109/13506129.2011.582902 · Cited by 40

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Rizzo, S., Bisi, A., Bartolini, M., Mancini, F., Belluti, F., Gobbi, S., Andrisano, V., & Rampa, A. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.07.004 · Cited by 39

Possibility of a New Anti-Alzheimerʼs Disease Pharmaceutical Composition Combining Memantine and Vitamin D

Annweiler, C., & Beauchet, O. (2012) · Drugs & Aging · doi:10.2165/11597550-000000000-00000 · Cited by 39

Curcumin protects against cigarette smoke-induced cognitive impairment and increased acetylcholinesterase activity in rats

Jaques, J. A. D. S., Rezer, J. F. P., Carvalho, F. B., da Rosa, M. M., Gutierres, J. M., Gonçalves, J. F., Schmatz, R., de Bairros, A. V., Mazzanti, C. M. D. A., Rubin, M. A., et al. (2012) · Physiology & Behavior · doi:10.1016/j.physbeh.2012.05.001 · Cited by 39

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Choi, S. J., Jeong, C.-H., Choi, S.-G., Chun, J.-Y., Kim, Y. J., Lee, J., Shin, D.-H., & Heo, H. J. (2009) · Journal of Medicinal Food · doi:10.1089/jmf.2007.0678 · Cited by 39

Axonal Transport and Mitochondrial Dysfunction in Alzheimer's Disease

Riemer, J., & Kins, S. (2012) · Neurodegenerative Diseases · doi:10.1159/000342020 · Cited by 39

Introduction to Theme “Chromatin, Epigenetics, and Transcription”

Conaway, J. W. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-090711-093103 · Cited by 39

Phenolic Bis-styrylbenzenes as β-Amyloid Binding Ligands and Free Radical Scavengers

Flaherty, D. P., Kiyota, T., Dong, Y., Ikezu, T., & Vennerstrom, J. L. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm1006929 · Cited by 38

New potent human acetylcholinesterase inhibitors in the tetracyclic triterpene series with inhibitory potency on amyloid β aggregation

Rouleau, J., Iorga, B. I., & Guillou, C. (2011) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2011.02.073 · Cited by 38

Inhibitory effect of zeatin, isolated from Fiatoua villosa, on acetylcholinesterase activity from PC12 cells

Heo, H.-J., Hong, S.-C., Cho, H.-Y., Hong, B., Kim, H.-K., Kim, E.-K., & Shin, D.-H. (2002) · Molecules and Cells · doi:10.1016/s1016-8478(23)15011-4 · Cited by 38

Efficacy of Cholinesterase Inhibitors in the Treatment of Neuropsychiatric Symptoms and Functional Impairment in Alzheimer Disease: A Meta-analysis

Trinh, N.-H., Hoblyn, J., Mohanty, S., & Yaffe, K. (2003) · JAMA · doi:10.1001/jama.289.2.210 · Cited by 37

The neuroprotective effect of ladostigil against hydrogen peroxide-mediated cytotoxicity

Weinreb, O., Bar‐Am, O., Amit, T., Driguès, N., Sagi, Y., & Youdim, M. B. H. (2008) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2008.05.038 · Cited by 37

3,5-Disubstituted-4-hydroxyphenyls Linked to 3-Hydroxy-2-methyl- 4(1H)-pyridinone: Potent Inhibitors of Lipid Peroxidation and Cell Toxicity

Bebbington, D., Monck, N. J. T., Gaur, S., Palmer, A. M., Benwell, K. R., Harvey, V. L., Malcolm, C. S., & Porter, R. H. P. (2000) · Journal of Medicinal Chemistry · doi:10.1021/jm990945v · Cited by 37

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Ivasiv, V., Albertini, C., Gonçalves, A. E., Rossi, M., & Bolognesi, M. L. (2019) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026619666190619115735 · Cited by 396

Potential Impact of the Multi-Target Drug Approach in the Treatment of Some Complex Diseases

Makhoba, X. H., Viegas, C., Mosa, R. A., Viegas, F. P. D., & Pooe, O. J. (2020) · Drug Design Development and Therapy · doi:10.2147/dddt.s257494 · Cited by 337

Recent development of multifunctional agents as potential drug candidates for the treatment of Alzheimer’s disease

Guzior, N., Wi.eckowska, A., Panek, D., & Malawska, B. (2014) · Current Medicinal Chemistry · doi:10.2174/0929867321666141106122628 · Cited by 323

Tau protein aggregation in Alzheimer's disease: An attractive target for the development of novel therapeutic agents

Jouanne, M., Rault, S., & Voisin‐Chiret, A. S. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.07.070 · Cited by 279

Antibacterial and antioxidant activities for natural and synthetic dual-active compounds

Martelli, G., & Giacomini, D. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.09.009 · Cited by 232

Multi-target-directed ligands and other therapeutic strategies in the search of a real solution for Alzheimer’s disease. Curr. Neuropharmacol. 12, 2–36. doi: 10.2174/1570159X113116660047 Alzheimer’s Association

Agis-torres, A., Söllhuber, M. M., Fern, M., & Sanchez-montero, J. M. (2014)

Multi-Target-Directed Ligands in Alzheimer’s Disease Therapy

Nepovimová, E., & Kuča, K. (2020) · IntechOpen eBooks · doi:10.5772/intechopen.93269 · Cited by 5

Multi-Target-Directed Ligands in Alzheimer’s Disease Therapy

Kuca, K. (2018) · BiblioBoard Library Catalog (Open Research Library)

Multi Target Directed Ligand for Alzheimer’s Disease: A Review of Therapeutic Strategies and Advances

Kumar, S., Sharma, V., Happy, & Verma, D. K. K. (2026) · Current Pharmaceutical Research · doi:10.63785/cpr.2026.2.2.292310

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Kumar, R., Kumar, V., Kumar, B., Thakur, A., & Dwivedi, A. R. (2021) · Current Medicinal Chemistry · doi:10.2174/0929867328666210512005508 · Cited by 55