Molecular mechanisms of Alzheimer’s disease: From therapeutic targets to promising drugs
Abstract
Alzheimer's disease (AD) is a neurodegenerative disease characterized by cognitive impairment so widespread that it interferes with a person's ability to complete daily activities. AD is becoming increasingly common, and it is estimated that the number of patients will reach 152 million by 2050. Current treatment options for AD are symptomatic and have modest benefits. Therefore, considering the human, social, and economic burden of the disease, the development of drugs with the potential to alter disease progression has become a global priority. In this review, the molecular mechanisms involved in the pathology of AD were evaluated as therapeutic targets. The main aim of the review is to focus on new knowledge about mitochondrial dysfunction, oxidative stress, and neuronal transmission in AD, as well as a range of cellular signaling mechanisms and associated treatments. Important molecular interactions leading to AD were described in amyloid cascade and in tau protein function, oxidative stress, mitochondrial dysfunction, cholinergic and glutamatergic neurotransmission, cAMP-regulatory element-binding protein (CREB), the silent mating type information regulation 2 homolog 1 (SIRT-1), neuroinflammation (glial cells), and synaptic alterations. This review summarizes recent experimental and clinical research in AD pathology and analyzes the potential of therapeutic applications based on molecular disease mechanisms.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
γ-secretase inhibitors such as tarenflurbil, avagacestat, and semagacestat lower amyloid beta synthesis by preventing gamma secretase enzyme from functioning.
“This includes γ-secretase inhibitors, such as tarenflurbil (7, Figure 5) [155,156], avagacestat (labeled as 6, Figure 5) [157,158], and semagacestat (5, Figure 5) [159,160]. Their purpose is to lower the synthesis of amyloid beta by preventing the gamma secretase enzyme from functioning.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [159]
Cites
1 retracted
Dementia prevention, intervention, and care: 2020 report of the Lancet Commission
Livingston, G., Huntley, J., Sommerlad, A., Ames, D., Ballard, C., Banerjee, S., Brayne, C., Burns, A., Cohen-Mansfield, J., Cooper, C., et al. (2020) · The Lancet · doi:10.1016/s0140-6736(20)30367-6 · Cited by 10,430 · cited 1× · see citing works
“The estimated global cost of the disease is estimated about US$ 1 trillion annually.(1) There are many hypotheses such as Aβ protein accumulation, tau hyperphosphorylation, oxidative stress, cholinergic neuron damage, and neuroinflammation in AD.”
BackgroundRetractedThe M1 and M2 paradigm of macrophage activation: Time for reassessment
Martinez, F. O., & Gordon, S. (2014) · F1000Prime Reports · doi:10.12703/p6-13 · Cited by 4,689 · see citing works
Apolipoprotein E and Alzheimer disease: risk, mechanisms and therapy
Liu, C.-C., Kanekiyo, T., Xu, H., & Bu, G. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.263 · Cited by 3,459 · see citing works
Oxidative Stress: A Key Modulator in Neurodegenerative Diseases
Singh, A., Kukreti, R., Saso, L., & Kukreti, S. (2019) · Molecules · doi:10.3390/molecules24081583 · Cited by 2,305 · see citing works
Apolipoprotein E and Alzheimer disease: pathobiology and targeting strategies
Yamazaki, Y., Zhao, N., Caulfield, T. R., Liu, C.-C., & Bu, G. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-019-0228-7 · Cited by 1,425 · see citing works
The role of oxidative stress in neurodegenerative diseases
Kim, G. H., Kim, J. E., Rhie, S. J., & Yoon, S. (2015) · Experimental Neurobiology · doi:10.5607/en.2015.24.4.325 · Cited by 1,355 · see citing works
ABAD Directly Links Aß to Mitochondrial Toxicity in Alzheimer's Disease
Lustbader, J. W., Cirilli, M., Lin, C., Xu, H. W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., et al. (2004) · Science · doi:10.1126/science.1091230 · Cited by 1,303 · see citing works
ApoE-Directed Therapeutics Rapidly Clear β-Amyloid and Reverse Deficits in AD Mouse Models
Cramer, P. E., Cirrito, J. R., Wesson, D. W., Lee, C. Y. D., Karlo, J. C., Zinn, A. E., Casali, B. T., Restivo, J. L., Goebel, W. D., James, M. J., et al. (2012) · Science · doi:10.1126/science.1217697 · Cited by 1,050 · see citing works
Role of Glutamate and NMDA Receptors in Alzheimer’s Disease
Wang, R., & Reddy, P. H. (2017) · Journal of Alzheimer’s Disease · doi:10.3233/jad-160763 · Cited by 1,009 · see citing works
Alzheimer’s Disease Risk Gene CD33 Inhibits Microglial Uptake of Amyloid Beta
Griciuc, A., Serrano-Pozo, A., Parrado, A. R., Lesinski, A. N., Asselin, C. N., Mullin, K., Hooli, B., Choi, S. H., Hyman, B. T., & Tanzi, R. E. (2013) · Neuron · doi:10.1016/j.neuron.2013.04.014 · Cited by 1,004 · see citing works
Current and Future Treatments in Alzheimer Disease: An Update
Yiannopoulou, K. G., & Papageorgiou, S. G. (2020) · Journal of Central Nervous System Disease · doi:10.1177/1179573520907397 · Cited by 966 · cited 1× · see citing works
“These drugs partially treat the symptoms of the disease but do not prevent the loss of neurons, brain atrophy, and deterioration of cognition, that is, the progression of the disease.(4,5) In order to evaluate the treatment options in AD, it is very important to learn the molecular mechanisms in the pathophysiology of…”
BackgroundThe Amyloid Beta Peptide: A Chemist’s Perspective. Role in Alzheimer’s and Fibrillization
Hamley, I. W. (2012) · Chemical Reviews · doi:10.1021/cr3000994 · Cited by 881 · see citing works
Mitochondria and Mitochondrial Cascades in Alzheimer’s disease
Swerdlow, R. H. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170585 · Cited by 850 · see citing works
Takahashi, R. H., Milner, T. A., Li, F., Nam, E. E., Edgar, M. A., Yamaguchi, H., Beal, M. F., Xu, H., Greengard, P., & Gouras, G. K. (2002) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64463-x · Cited by 706 · see citing works
The β-Secretase BACE1 in Alzheimer’s Disease
Hampel, H., Vassar, R., De Strooper, B., Hardy, J., Willem, M., Singh, N., Zhou, J., Yan, R., Vanmechelen, E., De Vos, A., et al. (2021) · Biological Psychiatry · doi:10.1016/j.biopsych.2020.02.001 · Cited by 694 · see citing works
Amyloid β oligomers constrict human capillaries in Alzheimer's disease via signaling to pericytes
Nortley, R., Korte, N., Izquierdo, P., Hirunpattarasilp, C., Mishra, A., Jaunmuktane, Z., Kyrargyri, V., Pfeiffer, T., Khennouf, L., Madry, C., et al. (2019) · Science · doi:10.1126/science.aav9518 · Cited by 682 · see citing works
Cholinesterase inhibitors as Alzheimer's therapeutics (Review)
Sharma, K. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.10374 · Cited by 611 · see citing works
Alzheimer’s disease hypothesis and related therapies
Du, X., Wang, X., & Geng, M. (2018) · Translational Neurodegeneration · doi:10.1186/s40035-018-0107-y · Cited by 609 · see citing works
Dempsey, C., Rubio Araiz, A., Bryson, K. J., Finucane, O., Larkin, C., Mills, E. L., Robertson, A. A. B., Cooper, M. A., O'Neill, L. A. J., & Lynch, M. A. (2017) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2016.12.014 · Cited by 571 · see citing works
Vitolo, O. V., Sant'Angelo, A., Costanzo, V., Battaglia, F., Arancio, O., & Shelanski, M. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.172504199 · Cited by 534 · see citing works
Is CREB a key to neuronal survival?
Walton, M. R., & Dragunow, M. (2000) · Trends in Neurosciences · doi:10.1016/s0166-2236(99)01500-3 · Cited by 520 · see citing works
Amyloid Beta and Phosphorylated Tau-Induced Defective Autophagy and Mitophagy in Alzheimer’s Disease
Reddy, P. H., & Oliver, D. M. (2019) · Cells · doi:10.3390/cells8050488 · Cited by 496 · cited 1× · see citing works
“Reducing dynamin-like protein 1, Aβ, and phosphorylated tau levels and increasing PINK1/parkin levels were recommended to treat autophagy and mitophagy disorders in AD.(136) Investigation of treatments related to autophagy and mitophagy, which play roles in the accumulation of protein aggregates and the degradation of…”
BackgroundMicroglia and Astrocytes in Alzheimer's Disease: Implications for Therapy
Fakhoury, M. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666170720095240 · Cited by 482 · see citing works
Ali, T., Kim, T. H., Rehman, S. U., Khan, M. S., Amin, F. U., Khan, M., Ikram, M. A., & Kim, M. O. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0798-6 · Cited by 477 · see citing works
The role of CREB and BDNF in neurobiology and treatment of Alzheimer's disease
Amidfar, M., de Oliveira, J., Kucharska, E., Budni, J., & Kim, Y. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118020 · Cited by 413 · see citing works
Stabilization of a β-hairpin in monomeric Alzheimer's amyloid-β peptide inhibits amyloid formation
Hoyer, W., Grönwall, C., Jonsson, A., Ståhl, S., & Härd, T. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711731105 · Cited by 411 · see citing works
Antioxidant Therapies for Alzheimer's Disease
Feng, Y., & Wang, X. (2012) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2012/472932 · Cited by 382 · see citing works
The innate immunity protein IFITM3 modulates γ-secretase in Alzheimer’s disease
Hur, J.-Y., Frost, G. R., Wu, X., Crump, C., Pan, S. J., Wong, E., Barros, M., Li, T., Nie, P., Zhai, Y., et al. (2020) · Nature · doi:10.1038/s41586-020-2681-2 · Cited by 382 · see citing works
TREM2 Acts Downstream of CD33 in Modulating Microglial Pathology in Alzheimer's Disease
Griciuc, A., Patel, S., Federico, A. N., Choi, S. H., Innes, B. J., Oram, M. K., Cereghetti, G., McGinty, D., Anselmo, A., Sadreyev, R. I., et al. (2019) · Neuron · doi:10.1016/j.neuron.2019.06.010 · Cited by 378 · see citing works
The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases
Lackie, R. E., Maciejewski, A., Ostapchenko, V. G., Marques-Lopes, J., Choy, W., Duennwald, M. L., Prado, V. F., & Prado, M. A. M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00254 · Cited by 375 · see citing works
Somatostatin regulates brain amyloid β peptide Aβ42 through modulation of proteolytic degradation
Saito, T., Iwata, N., Tsubuki, S., Takaki, Y., Takano, J., Huang, S.-M., Suemoto, T., Higuchi, M., & Saido, T. C. (2005) · Nature Medicine · doi:10.1038/nm1206 · Cited by 361 · see citing works
Synaptic basis of Alzheimer’s disease: Focus on synaptic amyloid beta, P-tau and mitochondria
John, A., & Reddy, P. H. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101208 · Cited by 359 · see citing works
APOE and Alzheimer’s Disease: From Lipid Transport to Physiopathology and Therapeutics
Husain, M. A., Laurent, B., & Plourde, M. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.630502 · Cited by 353 · see citing works
Manczak, M., & Reddy, P. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds360 · Cited by 348 · see citing works
Inhibition of Stat3‐mediated astrogliosis ameliorates pathology in an Alzheimer's disease model
Reichenbach, N., Delekate, A., Plescher, M., Schmitt, F., Krauss, S., Blank, N., Halle, A., & Petzold, G. C. (2019) · EMBO Molecular Medicine · doi:10.15252/emmm.201809665 · Cited by 343 · see citing works
A review of butyrylcholinesterase as a therapeutic target in the treatment of Alzheimer’s disease
Nordberg, A., Ballard, C., Bullock, R., Darreh-Shori, T., & Somogyi, M. (2013) · The Primary Care Companion For CNS Disorders · doi:10.4088/pcc.12r01412 · Cited by 323 · see citing works
Astrogliosis: An integral player in the pathogenesis of Alzheimer's disease
Osborn, L. M., Kamphuis, W., Wadman, W. J., & Hol, E. M. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.01.001 · Cited by 312 · see citing works
Zhang, Z., Song, M., Liu, X., Kang, S. S., Duong, D. M., Seyfried, N. T., Cao, X., Cheng, L., Sun, Y. E., Yu, S. P., et al. (2015) · Nature Communications · doi:10.1038/ncomms9762 · Cited by 289 · see citing works
Flores, J., Noël, A., Foveau, B., Lynham, J., Lecrux, C., & LeBlanc, A. C. (2018) · Nature Communications · doi:10.1038/s41467-018-06449-x · Cited by 288 · see citing works
VDAC1, mitochondrial dysfunction, and Alzheimer’s disease
Shoshan-Barmatz, V., Nahon-Crystal, E., Shteinfer-Kuzmine, A., & Gupta, R. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.03.010 · Cited by 286 · see citing works
Oxidative stress in alzheimer’s disease: A review on emergent natural polyphenolic therapeutics
Cassidy, L., Fernandez, F., Johnson, J. B., Naiker, M., Owoola, A. G., & Broszczak, D. A. (2019) · Complementary Therapies in Medicine · doi:10.1016/j.ctim.2019.102294 · Cited by 283 · see citing works
Dysfunction of NMDA receptors in Alzheimer’s disease
Zhang, Y., Li, P., Feng, J., & Wu, M. (2016) · Neurological Sciences · doi:10.1007/s10072-016-2546-5 · Cited by 282 · cited 4× · see citing works
“Overexpression of human tau protein in primary neuronal cultures induced cell death by stimulation of extrasynaptic NMDA receptors containing the GluN2B subunit, which was inhibited by administration of GluN2B selective antagonist.(175) A close link between α7-nicotinic acetylcholine receptors and glutamatergic transm…”
BackgroundInfluentialRole of tau protein in Alzheimer’s disease: The prime pathological player
Muralidar, S., Ambi, S. V., Sekaran, S., Thirumalai, D., & Palaniappan, B. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.327 · Cited by 278 · see citing works
Mechanism for the α‐helix to β‐hairpin transition
Ding, F., Borreguero, J. M., Buldyrey, S. V., Stanley, E., & Dokholyan, N. V. (2003) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.10468 · Cited by 272 · see citing works
Mitochondria and Calcium in Alzheimer’s Disease: From Cell Signaling to Neuronal Cell Death
Calvo-Rodriguez, M., & Bacskai, B. J. (2021) · Trends in Neurosciences · doi:10.1016/j.tins.2020.10.004 · Cited by 254 · see citing works
NLRP3 Inflammasome Inhibitor Ameliorates Amyloid Pathology in a Mouse Model of Alzheimer’s Disease
Yin, J., Zhao, F., Chojnacki, J. E., Fulp, J., Klein, W. L., Zhang, S., & Zhu, X. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0467-9 · Cited by 240 · see citing works
Immune hyperreactivity of Aβ plaque-associated microglia in Alzheimer's disease
Yin, Z., Raj, D., Saiepour, N., Van Dam, D., Brouwer, N., Holtman, I. R., Eggen, B. J. L., Möller, T., Tamm, J. A., Abdourahman, A., et al. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.03.021 · Cited by 238 · see citing works
Pratt, W. B., Gestwicki, J. E., Osawa, Y., & Lieberman, A. P. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124332 · Cited by 237 · see citing works
Den, H., Dong, X., Chen, M., & Zou, Z. (2020) · Aging · doi:10.18632/aging.102810 · Cited by 230 · see citing works
Heat-shock proteins: chaperoning DNA repair
Dubrez, L., Causse, S., Borges Bonan, N., Dumétier, B., & Garrido, C. (2020) · Oncogene · doi:10.1038/s41388-019-1016-y · Cited by 224 · see citing works
Neuronal Sigma-1 Receptors: Signaling Functions and Protective Roles in Neurodegenerative Diseases
Ryskamp, D. A., Korban, S. A., Zhemkov, V., Kraskovskaya, N., & Борисович, Б. И. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00862 · Cited by 221 · see citing works
TREM2, microglia, and Alzheimer’s disease.
Qin, Q., Teng, Z., Liu, C., Li, Q., Yin, Y., & Tang, Y. (2021) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2021.111438 · Cited by 219 · see citing works
Combination Drug Therapy for the Management of Alzheimer’s Disease
Kabir, M. T., Uddin, M. S., Mamun, A. A., Jeandet, P., Aleya, L., Mansouri, R. A., Ashraf, G. M., Mathew, B., Bin-Jumah, M. N., & Abdel-Daim, M. M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21093272 · Cited by 217 · see citing works
Seeger, T., Fedorova, I. D., Zheng, F., Miyakawa, T., Koustova, E., Gomeza, J., Basile, A. S., Alzheimer, C., & Wess, J. (2004) · Journal of Neuroscience · doi:10.1523/jneurosci.3581-04.2004 · Cited by 214 · see citing works
Molecular mechanisms of astrocyte-induced synaptogenesis
Baldwin, K. T., & Eroğlu, Ç. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.05.006 · Cited by 214 · see citing works
The mitochondrial complex I inhibitor rotenone triggers a cerebral tauopathy
Höglinger, G. U., Lannuzel, A., Escobar-Khondiker, M., Michel, P. P., Duyckaerts, C. J., Féger, J., Champy, P., Prigent, A., Medja, F., Lombès, A., et al. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03493.x · Cited by 203 · see citing works
The neurobiology of sirtuins and their role in neurodegeneration
Dönmez, G. (2012) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2012.05.007 · Cited by 195 · see citing works
Karpova, A., Mikhaylova, M., Bera, S., Bär, J., Reddy, P. P., Behnisch, T., Rankovic, V., Spilker, C., Bethge, P., Şahin, J., et al. (2013) · Cell · doi:10.1016/j.cell.2013.02.002 · Cited by 194 · see citing works
Cerebral amyloid-β proteostasis is regulated by the membrane transport protein ABCC1 in mice
Krohn, M., Lange, C., Hofrichter, J., Scheffler, K., Stenzel, J., Steffen, J., Schumacher, T., Brüning, T., Plath, A.-S., Alfen, F., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci57867 · Cited by 190 · see citing works
Di Benedetto, G., Burgaletto, C., Bellanca, C. M., Munafò, A., Bernardini, R., & Cantarella, G. (2022) · Cells · doi:10.3390/cells11172728 · Cited by 189 · see citing works
Plascencia‐Villa, G., & Perry, G. L. (2020) · Antioxidants and Redox Signaling · doi:10.1089/ars.2020.8134 · Cited by 188 · see citing works
Role of Kynurenine Pathway in Oxidative Stress during Neurodegenerative Disorders
Mor, A., Tankiewicz‐Kwedlo, A., Krupa, A., & Pawlak, D. (2021) · Cells · doi:10.3390/cells10071603 · Cited by 188 · see citing works
Formation and function of apolipoprotein E-containing lipoproteins in the nervous system.
Vance, J., & Hayashi, H. (2010) · Biochimica et Biophysica Acta · doi:10.1016/j.bbalip.2010.02.007 · Cited by 185 · see citing works
Kandimalla, R. J. L., Mańczak, M., Fry, D., Yeguvapalli, S., Sesaki, H., & Reddy, P. H. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw312 · Cited by 180 · see citing works
Targeting of nonlipidated, aggregated apoE with antibodies inhibits amyloid accumulation
Liao, F., Li, A., Xiong, M., Bien-Ly, N., Jiang, H., Zhang, Y., Finn, M. B., Hoyle, R., Keyser, J., Lefton, K. B., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci96429 · Cited by 178 · see citing works
Astrocytes in Alzheimer's disease: pathological significance and molecular pathways
Preman, P., Alfonso-Triguero, M., Alberdi, E., Verkhratsky, A., & Arranz, A. M. (2021) · Cells · doi:10.3390/cells10030540 · Cited by 176 · see citing works
Heat Shock Proteins in Alzheimer’s Disease: Role and Targeting
Campanella, C., Pace, A., Bavisotto, C. C., Marzullo, P., Marino, A., Buscemi, S., & Piccionello, A. P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092603 · Cited by 175 · see citing works
Targeting amyloid clearance in Alzheimer's disease as a therapeutic strategy
Nalivaeva, N. N., & Turner, A. J. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14593 · Cited by 172 · see citing works
Inhibition of p25/Cdk5 Attenuates Tauopathy in Mouse and iPSC Models of Frontotemporal Dementia
Seo, J., Kritskiy, O., Watson, L. A., Barker, S. J., Dey, D. C., Raja, W. K., Lin, Y.-T., Ko, T., Cho, S., Penney, J., et al. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.0621-17.2017 · Cited by 165 · see citing works
Balducci, C., Frasca, A., Zotti, M., La Vitola, P., Mhillaj, E., Grigoli, E., Iacobellis, M., Grandi, F., Messa, M., Colombo, L., et al. (2017) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2016.10.012 · Cited by 164 · cited 1× · see citing works
“In another study, cyanobacterial product (CyP) was injected into the intracerebroventricular region and reduced memory impairment by causing TLR4 receptor blockage in mice.(234) Activation of TLRs could be beneficial or detrimental for AD.”
BackgroundHe, Y., Wei, M., Wu, Y., Qin, H., Li, W., Ma, X., Cheng, J., Ren, J., Shen, Y., Chen, Z., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09114-z · Cited by 156 · see citing works
Du, Q., Zhu, X., & Si, J. (2019) · Experimental Biology and Medicine · doi:10.1177/1535370219894558 · Cited by 153 · see citing works
Synaptic Therapy in Alzheimer's Disease: A CREB-centric Approach
Teich, A. F., Nicholls, R. E., Puzzo, D., Fiorito, J., Purgatorio, R., Fà, M., & Arancio, O. (2015) · Neurotherapeutics · doi:10.1007/s13311-014-0327-5 · Cited by 147 · see citing works
Beneficial Effects of Walnuts on Cognition and Brain Health
Chauhan, A., & Chauhan, V. P. S. (2020) · Nutrients · doi:10.3390/nu12020550 · Cited by 147 · see citing works
Alpha 7 nicotinic acetylcholine receptor and its effects on Alzheimer's disease
Ma, K., & Qian, Y. (2018) · Neuropeptides · doi:10.1016/j.npep.2018.12.003 · Cited by 143 · see citing works
Fisher, A. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07507.x · Cited by 140 · see citing works
Reconsideration of Anticholinesterase Therapeutic Strategies against Alzheimer’s Disease
Wang, H., & Zhang, H. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00391 · Cited by 140 · see citing works
Rangasamy, S. B., Jana, M., Roy, A., Corbett, G. T., Kundu, M., Chandra, S., Mondal, S., Dasarathi, S., Mufson, E. J., Mishra, R. K., et al. (2018) · Journal of Clinical Investigation · doi:10.1172/jci96209 · Cited by 139 · see citing works
Mitochondrial Dysfunction in Alzheimer’s Disease: A Biomarker of the Future?
Bell, S., Barnes, K., Marco, M. D., Shaw, P. J., Ferraiuolo, L., Blackburn, D. J., Venneri, A., & Mortiboys, H. (2021) · Biomedicines · doi:10.3390/biomedicines9010063 · Cited by 136 · see citing works
Hu, Y.-S., Long, N., Pigino, G. F., Brady, S. T., & Lazarov, O. (2013) · PLoS ONE · doi:10.1371/journal.pone.0064460 · Cited by 134 · see citing works
The Role of Sigma-1 Receptor, an Intracellular Chaperone in Neurodegenerative Diseases
Penke, B., Fülöp, L., Szűcs, M., & Frecska, E. (2017) · Current Neuropharmacology · doi:10.2174/1570159x15666170529104323 · Cited by 132 · see citing works
Tabassum, R., & Jeong, N. Y. (2019) · International Journal of Medical Sciences · doi:10.7150/ijms.36516 · Cited by 129 · see citing works
Eckert, A., Nisbet, R. M., Grimm, A., & Götz, J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.08.013 · Cited by 127 · see citing works
Ma, X., Sun, Z., Han, X., Li, S., Jiang, X., Chen, D., Zhang, J., & Lu, H. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.01400 · Cited by 126 · see citing works
Nicotinic Acetylcholine Receptor Agonists for the Treatment of Alzheimer’s Dementia: An Update
Hoskin, J. L., Al-Hasan, Y. M., & Sabbagh, M. N. (2018) · Nicotine & Tobacco Research · doi:10.1093/ntr/nty116 · Cited by 123 · see citing works
Blair, L. J., Baker, J. D., Sabbagh, J. J., & Dickey, C. A. (2015) · Journal of Neurochemistry · doi:10.1111/jnc.13033 · Cited by 120 · see citing works
The Many Faces of Astrocytes in Alzheimer's Disease
Monterey, M. D., Wei, H., Wu, X., & Wu, J. Q. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.619626 · Cited by 117 · see citing works
Pierzynowska, K., Podlacha, M., Gaffke, L., Majkutewicz, I., Mantej, J., Węgrzyn, A., Osiadły, M., Myślińska, D., & Węgrzyn, G. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.01.030 · Cited by 116 · see citing works
Therapeutic Potential of Secreted Amyloid Precursor Protein APPsα
Mockett, B. G., Richter, M., Abraham, W. C., & Müller, U. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00030 · Cited by 115 · see citing works
Phospho-Tau Bar Code: Analysis of Phosphoisotypes of Tau and Its Application to Tauopathy
Kimura, T., Sharma, G., Ishiguro, K., & Hisanaga, S. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00044 · Cited by 112 · see citing works
Tau Protein Squired by Molecular Chaperones During Alzheimer’s Disease
Gorantla, N. V., & Chinnathambi, S. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1174-3 · Cited by 112 · see citing works
Amyloid-<i>β</i>-Induced Dysregulation of AMPA Receptor Trafficking
Guntupalli, S., Widagdo, J., & Anggono, V. (2016) · Neural Plasticity · doi:10.1155/2016/3204519 · Cited by 110 · see citing works
Verma, S., Kumar, A., Tripathi, T., & Kumar, A. (2018) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12919 · Cited by 110 · see citing works
Involvement of calpain in the neuropathogenesis of Alzheimer’s disease
Mahaman, Y. A. R., Huang, F., Afewerky, H. K., Salissou, M. T. M., Bishwajit, G., & Wang, X. (2018) · Medicinal Research Reviews · doi:10.1002/med.21534 · Cited by 107 · see citing works
Wilcock, D. M., & Colton, C. A. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-15404 · Cited by 106 · see citing works
Viayna, E., Coquelle, N., Cieslikiewicz-Bouet, M., Cisternas, P., Oliva, C. A., Sánchez-López, E., Ettcheto, M., Bartolini, M., De Simone, A., Ricchini, M., et al. (2021) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c01775 · Cited by 106 · see citing works
Vascular Hypothesis of Alzheimer Disease
Scheffer, S., Hermkens, D. M. A., van der Weerd, L., de Vries, H. E., & Daemen, M. J. A. P. (2021) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.120.311911 · Cited by 103 · see citing works
Iraji, A., Khoshneviszadeh, M., Firuzi, O., Khoshneviszadeh, M., & Edraki, N. (2020) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2020.103649 · Cited by 102 · see citing works
Sang, Z., Wang, K., Shi, J., Cheng, X., Zhu, G., Wei, R., Ma, Q., Yu, L., Zhao, Y., Tan, Z., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111958 · Cited by 101 · see citing works
Tau inhibits mitochondrial calcium efflux and makes neurons vulnerable to calcium-induced cell death
Britti, E., Ros, J., Esteras, N., & Abramov, A. Y. (2019) · Cell Calcium · doi:10.1016/j.ceca.2019.102150 · Cited by 101 · see citing works
Gulisano, W., Melone, M., Ripoli, C., Tropea, M. R., Li Puma, D. D., Giunta, S., Cocco, S., Marcotulli, D., Origlia, N., Palmeri, A., et al. (2019) · The Journal of Neuroscience · doi:10.1523/jneurosci.0163-19.2019 · Cited by 100 · see citing works
Molecular and Therapeutic Targets of Genistein in Alzheimer’s Disease
Devi, K. P., Shanmuganathan, B., Manayi, A., Nabavi, S. F., & Nabavi, S. M. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0215-6 · Cited by 96 · see citing works
Development of novel phosphodiesterase 5 inhibitors for the therapy of Alzheimer’s disease
Zuccarello, E., Acquarone, E., Calcagno, E., Argyrousi, E. K., Deng, S., Landry, D. W., Arancio, O., & Fiorito, J. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113818 · Cited by 93 · see citing works
Labban, S., Alghamdi, B. S., Alshehri, F. S., & Kurdi, M. (2021) · Behavioural Brain Research · doi:10.1016/j.bbr.2020.113100 · Cited by 92 · see citing works
Rivastigmine modifies the α-secretase pathway and potentially early Alzheimer’s disease
Ray, B., Maloney, B., Sambamurti, K., Karnati, H. K., Nelson, P. T., Greig, N. H., & Lahiri, D. K. (2020) · Translational Psychiatry · doi:10.1038/s41398-020-0709-x · Cited by 91 · see citing works
Zhao, X., Li, S., Gaur, U., & Zheng, W. (2020) · Aging and Disease · doi:10.14336/ad.2019.0813 · Cited by 91 · see citing works
Calderwood, S. K., & Murshid, A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00192 · Cited by 87 · see citing works
Cirillo, C., Capoccia, E., Iuvone, T., Cuomo, R., Sarnelli, G., Steardo, L., & Esposito, G. (2015) · BioMed Research International · doi:10.1155/2015/508342 · Cited by 86 · see citing works
Manzine, P. R., Ettcheto, M., Cano, A. C., Busquets, O., Marcello, E. E., Pelucchi, S., Luca, M. D., Endres, K., Olloquequi, J., Camins, A., et al. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.108661 · Cited by 83 · see citing works
Bojarski, Ł., Pomorski, P., Szybińska, A., Drab, M., Skibinska-Kijek, A., Gruszczynska‐Biegala, J., & Kuźnicki, J. (2008) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2008.11.008 · Cited by 82 · see citing works
Allnutt, A., Waters, A. K., Kesari, S., & Yenugonda, V. M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00096 · Cited by 82 · see citing works
Small Molecule Binding to Alzheimer Risk Factor CD33 Promotes Aβ Phagocytosis
Miles, L. A., Hermans, S. J., Crespi, G. A. N., Gooi, J. H., Doughty, L., Nero, T. L., Markulić, J., Ebneth, A., Wroblowski, B., Oehlrich, D., et al. (2019) · iScience · doi:10.1016/j.isci.2019.07.023 · Cited by 81 · see citing works
Fracassi, A., Marcatti, M., Zolochevska, O., Tabor, N., Woltjer, R., Moreno, S., & Taglialatela, G. (2021) · The Journal of Neuroscience · doi:10.1523/jneurosci.0295-20.2020 · Cited by 81 · see citing works
Mori, T., Koyama, N., Yokoo, T., Segawa, T., Maeda, M., Sawmiller, D. R., Tan, J., & Town, T. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.012330 · Cited by 78 · see citing works
α-Linolenic acid inhibits Tau aggregation and modulates Tau conformation
Desale, S. E., Dubey, T., & Chinnathambi, S. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.10.226 · Cited by 77 · see citing works
Niikura, T., Sidahmed, E., Hirata‐Fukae, C., Aisen, P. S. S., & Matsuoka, Y. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016259 · Cited by 76 · see citing works
Rho-kinase ROCK inhibitors reduce oligomeric tau protein
Hamano, T., Shirafuji, N., Yen, S.-H., Yoshida, H., Kanaan, N. M., Hayashi, K., Ikawa, M., Yamamura, O., Fujita, Y., Kuriyama, M., et al. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.12.009 · Cited by 76 · see citing works
Sildenafil for the Treatment of Alzheimer’s Disease: A Systematic Review
Sanders, O. D. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-200166 · Cited by 76 · see citing works
Mitochondrial dysfunction, mitophagy, and role of dynamin‐related protein 1 in Alzheimer's disease
Medala, V. K., Gollapelli, B., Dewanjee, S., Ogunmokun, G., Kandimalla, R. J. L., & Vallamkondu, J. (2021) · Journal of Neuroscience Research · doi:10.1002/jnr.24781 · Cited by 76 · see citing works
Duan, A. R., Jonasson, E. M., Alberico, E. O., Li, C., Scripture, J. P., Miller, R. A., Alber, M., & Goodson, H. V. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.03.018 · Cited by 74 · see citing works
New evolutions in the BACE1 inhibitor field from 2014 to 2018
Hsiao, C., Rombouts, F. J. R., & Gijsen, H. J. M. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.12.049 · Cited by 74 · see citing works
Ettcheto, M., Cano, A., Manzine, P. R., Busquets, O., Verdaguer, E., Castro-Torres, R. D., García, M. L., Beas-Zarate, C., Olloquequi, J., Auladell, C., et al. (2020) · Molecular Neurobiology · doi:10.1007/s12035-019-01849-6 · Cited by 73 · see citing works
Higuchi, M., Iwata, N., & Saido, T. C. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2005.02.013 · Cited by 72 · see citing works
Gong, L., Zhang, X., Ge, K., Yin, Y., Machuki, J. O., Yang, Y. Q., Shi, H., Geng, D., & Gao, F. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2020.120483 · Cited by 72 · see citing works
Toll-like receptors in Alzheimer's disease
Momtazmanesh, S., Perry, G. L., & Rezaei, N. (2020) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2020.577362 · Cited by 71 · see citing works
Spencer, B. J., Marr, R. A., Gindi, R., Potkar, R., Michael, S. A., Adame, A., Rockenstein, E. M., Verma, I. M., & Masliah, E. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016575 · Cited by 69 · see citing works
Xhima, K., Markham-Coultes, K., Nedev, H., Heinen, S., Saragovi, H. U., Hynynen, K., & Aubert, I. (2020) · Science Advances · doi:10.1126/sciadv.aax6646 · Cited by 69 · see citing works
The Role of P2X7 Receptor in Alzheimer’s Disease
Francistiová, L., Bianchi, C., Lauro, C. D., Sebastián‐Serrano, Á., de Diego-García, L., Kobolák, J., Dinnyés, A., & Dı́az-Hernández, M. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00094 · Cited by 69 · see citing works
Pourbadie, H. G., Sayyah, M., Khoshkholgh-Sima, B., Choopani, S., Nategh, M., Motamedi, F., & Shokrgozar, M. A. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.06.020 · Cited by 68 · see citing works
TDMQ20, a Specific Copper Chelator, Reduces Memory Impairments in Alzheimer’s Disease Mouse Models
Zhao, J. J., Shi, Q., Tian, H., Li, Y., Liu, Y., Xu, Z., Robert, A., Liu, Q., & Meunier, B. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00621 · Cited by 66 · see citing works
Linking APOE-ε4, blood-brain barrier dysfunction, and inflammation to Alzheimer's pathology
Riphagen, J. M., Ramakers, I. H. G. B., Freeze, W. M., Pagen, L. H. G., Hanseeuw, B. J., Verbeek, M. M., Verhey, F. R. J., & Jacobs, H. I. L. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.09.020 · Cited by 65 · see citing works
Ding, Y. J., Zhao, J., Zhang, X., Wang, S., Viola, K. L., Chow, F. E., Zhang, Y., Lippa, C. F., Klein, W. L., & Gong, Y. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.01140 · Cited by 65 · see citing works
Guo, J., Yang, G., He, Y., Xu, H., Fan, H., An, J., Zhang, L., Zhang, R., Cao, G., Hao, D., et al. (2020) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-01009-8 · Cited by 65 · see citing works
A Novel NMDA Receptor Antagonist Protects against Cognitive Decline Presented by Senescent Mice
Companys‐Alemany, J., Turcu, A. L., Bellver‐Sanchís, A., Loza, M. I., Brea, J. M., Canudas, A. M., Leiva, R., Vázquez, S., Pallàs, M., & Griñán‐Ferré, C. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12030284 · Cited by 64 · see citing works
Metformin Ameliorates Synaptic Defects in a Mouse Model of AD by Inhibiting Cdk5 Activity
Wang, Y., Zhao, J., Guo, F., Gao, X., Xie, X., Liu, S., Yang, X., Xinfeng, Y., Zhang, L., Ye, Y., et al. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00170 · Cited by 62 · see citing works
Calpain Dysregulation in Alzheimer’s Disease
Ferreira, A. (2012) · ISRN Biochemistry · doi:10.5402/2012/728571 · Cited by 61 · see citing works
An evaluation of memantine ER + donepezil for the treatment of Alzheimer’s disease
Calhoun, A. J., King, C., Khoury, R., & Grossberg, G. T. (2018) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2018.1519022 · Cited by 61 · see citing works
Stavudine Reduces NLRP3 Inflammasome Activation and Modulates Amyloid-β Autophagy
Rosa, F. L., Saresella, M., Marventano, I., Piancone, F., Ripamonti, E., Al‐Daghri, N. M., Bazzini, C., Zoia, C., Conti, E., Ferrarese, C., et al. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-181259 · Cited by 61 · see citing works
Roberts, J. P., Stokoe, S. A., Sathler, M. F., Nichols, R. A., & Kim, S. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100402 · Cited by 61 · see citing works
Rosini, M., Simoni, E., Caporaso, R., Basagni, F., Catanzaro, M., Abu, I. F., Fagiani, F., Fusco, F., Masuzzo, S., Albani, D., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.07.011 · Cited by 59 · see citing works
Telmisartan Protects Against Aluminum-Induced Alzheimer-like Pathological Changes in Rats
Khalifa, M., Safar, M. M., Abdelsalam, R. M., & Zaki, H. F. (2019) · Neurotoxicity Research · doi:10.1007/s12640-019-00085-z · Cited by 59 · see citing works
Stazi, M., & Wirths, O. (2021) · Molecular Neurobiology · doi:10.1007/s12035-020-02120-z · Cited by 59 · see citing works
Molecular Modulation of Human α7 Nicotinic Receptor by Amyloid-β Peptides
Lasala, M., Fabiani, C., Corradi, J., Antollini, S. S., & Bouzat, C. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00037 · Cited by 58 · see citing works
Maurice, T., Volle, J., Strehaïano, M., Crouzier, L., Pereira, C., Kaloyanov, N., Virieux, D., & Pirat, J. (2019) · Pharmacological Research · doi:10.1016/j.phrs.2019.04.026 · Cited by 56 · see citing works
Scarpa, M., Hesse, S., & Bradley, S. J. (2020) · Advances in pharmacology · doi:10.1016/bs.apha.2019.12.003 · Cited by 54 · see citing works
N -Methyl-D-Aspartate (NMDA) receptor modulators: a patent review (2015-present)
Ahmed, H., Haider, A., & Ametamey, S. M. (2020) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2020.1811234 · Cited by 54 · see citing works
Wang, X., Deng, Y., Gao, Y.-M., Dong, Y., Wang, F., Guan, Z.-Z., Hong, W., & Qi, X. (2020) · Aging · doi:10.18632/aging.102640 · Cited by 53 · see citing works
Impairment of muscarinic transmission in transgenic APPswe/PS1dE9 mice
Machová, E., Jakubík, J., Michal, P., Oksman, M., Iivonen, H., Tanila, H., & Doležal, V. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2006.10.029 · Cited by 50 · see citing works
Recent developments of small molecule γ-secretase modulators for Alzheimer's disease
Mekala, S., Nelson, G. L., & Li, Y. (2020) · RSC Medicinal Chemistry · doi:10.1039/d0md00196a · Cited by 50 · see citing works
Mao, L., Tang, Q., & Wang, J. Q. (2007) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2007.01.009 · Cited by 48 · see citing works
The role of mitochondrial defects and oxidative stress in Alzheimer’s disease
Islam, B. U., Jabir, N. R., & Tabrez, S. S. M. (2019) · Journal of drug targeting · doi:10.1080/1061186x.2019.1584808 · Cited by 48 · see citing works
Brain Shuttle Neprilysin reduces central Amyloid-β levels
Campos, C. R., Kemble, A. M., Niewoehner, J., Freskgård, P., & Urich, E. (2020) · PLoS ONE · doi:10.1371/journal.pone.0229850 · Cited by 48 · see citing works
Peng, Y., Lee, D. Y. W., Jiang, L., Ma, Z., Schachter, S. C., & Lemere, C. A. (2007) · Neuroscience · doi:10.1016/j.neuroscience.2007.09.022 · Cited by 47 · see citing works
Chen, P., Chen, Z.-T., Hou, W., Yu, L., & Chen, R. P. ‐. (2016) · Scientific Reports · doi:10.1038/srep29760 · Cited by 47 · see citing works
Dong, Y., Cao, K., Tan, L.-C., Wang, X., Qi, X., Xiao, Y. C., & Guan, Z.-Z. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-171020 · Cited by 47 · see citing works
Biased M1-muscarinic-receptor-mutant mice inform the design of next-generation drugs
Bradley, S. J., Molloy, C., Valuskova, P., Dwomoh, L., Scarpa, M., Rossi, M., Finlayson, L., Svensson, K. A., Chernet, E., Barth, V., et al. (2020) · Nature Chemical Biology · doi:10.1038/s41589-019-0453-9 · Cited by 47 · see citing works
FKBP immunophilins and Alzheimer’s disease: A chaperoned affair
Cao, W., & Konsolaki, M. (2011) · Journal of Biosciences · doi:10.1007/s12038-011-9080-7 · Cited by 46 · see citing works
Youn, K., Park, J.-H., Lee, S., Lee, S., Lee, J., Yun, E.-Y., Jeong, W.-S., & Jun, M. (2018) · Journal of Medicinal Food · doi:10.1089/jmf.2017.4068 · Cited by 46 · see citing works
Ketamine inhibits LPS‐mediated BV2 microglial inflammation via NMDA receptor blockage
Lu, Y., Ding, X., Wu, X., & Huang, S. (2019) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12508 · Cited by 46 · see citing works
Wang, J., Liu, B., Xu, Y. X., Yang, M., Wang, C., Song, M., Liu, J., Wang, W., You, J., Sun, F., et al. (2021) · Aging Cell · doi:10.1111/acel.13333 · Cited by 46 · see citing works
Klein, C., Roussel, G., Brun, S., Rusu, C., Patte‐Mensah, C., Maître, M., & Mensah‐Nyagan, A. G. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0640-z · Cited by 44 · see citing works
Gong, Y., Chen, J., Jin, Y., Wang, C., Zheng, M., & He, L. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107899 · Cited by 44 · see citing works
Successive cleavage of β-amyloid precursor protein by γ-secretase
Funamoto, S., Tagami, S., Okochi, M., & Morishima‐Kawashima, M. (2020) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2020.04.002 · Cited by 44 · see citing works
Cyclin dependent kinase 5: A novel avenue for Alzheimer’s disease
Bhounsule, A. S., Bhatt, L. K., Prabhavalkar, K. S., & Oza, M. J. (2017) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2017.05.006 · Cited by 43 · see citing works
Ren, J.-M., Zhang, S.-L., Wang, X., Guan, Z., & Qi, X. (2020) · Molecular Medicine Reports · doi:10.3892/mmr.2020.11253 · Cited by 43 · see citing works
Dysfunctional γ-Secretase in Familial Alzheimer’s Disease
Wolfe, M. S. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2511-1 · Cited by 42 · see citing works
M1 muscarinic acetylcholine receptor dysfunction in moderate Alzheimer’s disease pathology
Yi, J. H., Whitcomb, D. J., Park, S. J., Martinez-Perez, C., Barbati, S. A., Mitchell, S. J., & Cho, K. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa058 · Cited by 41 · see citing works
Mitochondria as a promising target for developing novel agents for treating Alzheimer's disease
Shevtsova, E. F., Maltsev, A. V., Vinogradova, D. V., Shevtsov, P. N., & Бачурин, С. О. (2020) · Medicinal Research Reviews · doi:10.1002/med.21715 · Cited by 41 · see citing works
Riluzole attenuates glutamatergic tone and cognitive decline in AβPP/PS1 mice
Hascup, K. N., Findley, C. A., Britz, J., Esperant‐Hilaire, N., Broderick, S. O., Delfino, K. R., Tischkau, S. A., Bartke, A., & Hascup, E. R. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15224 · Cited by 41 · see citing works
Rofo, F., Yılmaz, C. U., Metzendorf, N. G., Gustavsson, T., Beretta, C., Erlandsson, A., Sehlin, D., Syvänen, S., Nilsson, P., & Hultqvist, G. (2020) · Theranostics · doi:10.7150/thno.50263 · Cited by 41 · see citing works
Passive Immunotherapies Targeting Amyloid Beta and Tau Oligomers in Alzheimer’s Disease
Zanden, C. M. V., & Chi, E. Y. (2019) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2019.10.024 · Cited by 40 · see citing works
PKR kinase directly regulates tau expression and Alzheimer's disease‐related tau phosphorylation
Reimer, L., Betzer, C., Kofoed, R. H., Volbracht, C., Fog, K., Kurhade, C., Nilsson, E., Överby, A. K., & Jensen, P. H. (2020) · Brain Pathology · doi:10.1111/bpa.12883 · Cited by 39 · see citing works
Thompson, K. J., & Tobin, A. B. (2020) · Cellular Signalling · doi:10.1016/j.cellsig.2020.109545 · Cited by 38 · see citing works
Casticin ameliorates scopolamine-induced cognitive dysfunction in mice
Kim, J., Seo, Y. H., Kim, J., Goo, N., Jeong, Y., Bae, H. J., Jung, S. Y., Lee, J. H., & Ryu, J. H. (2020) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2020.112843 · Cited by 38 · see citing works
Enhancement of neutral endopeptidase activity in SK-N-SH cells by green tea extract
Melzig, M. F., & Janka, M. (2003) · Phytomedicine · doi:10.1078/094471103322331449 · Cited by 36 · see citing works
Serwach, K., & Gruszczynska‐Biegala, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092289 · Cited by 36 · see citing works
Role of Cdk5 in Amyloid-beta Pathology of Alzheimer’s Disease
Lu, T.-T., Wan, C., Yang, W., & Cai, Z. (2019) · Current Alzheimer Research · doi:10.2174/1567205016666191210094435 · Cited by 36 · see citing works
Zhou, L., Flores, J., Noël, A., Beauchet, O., Sjöström, P. J., & LeBlanc, A. C. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0856-6 · Cited by 36 · see citing works
Mohamed, T. M., Youssef, M. A. M., Bakry, A. A., & El-Keiy, M. M. (2020) · Metabolic Brain Disease · doi:10.1007/s11011-020-00639-7 · Cited by 36 · see citing works
Uncoupling of M1 muscarinic receptor/G-protein interaction by amyloid β1–42
Janíčková, H., Rudajev, V., Zimčík, P., Jakubík, J., Tanila, H., El‐Fakahany, E. E., & Doležal, V. (2012) · Neuropharmacology · doi:10.1016/j.neuropharm.2012.11.014 · Cited by 35 · see citing works
Kiss, A. K., Kowalski, J., & Melzig, M. (2006) · PubMed · Cited by 35 · see citing works
Sun, J. L., Stokoe, S. A., Roberts, J. P., Sathler, M. F., Nip, K., Shou, J., Ko, K. H., Tsunoda, S., & Kim, S. (2019) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2019.09.005 · Cited by 35 · see citing works
Liu, Z., Qiu, X., Mak, S., Guo, B., Hu, S., Wang, J., Luo, F., Xu, D., Sun, Y., Zhang, G., et al. (2020) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2020.109020 · Cited by 35 · see citing works
Dong, Y., Cao, K., Xiang, J., Shan, L., & Guan, Z.-Z. (2020) · American Journal Of Pathology · doi:10.1016/j.ajpath.2020.03.015 · Cited by 34 · see citing works
Extracellular Vesicles as a Neprilysin Delivery System Memory Improvement in Alzheimer's Disease.
Izadpanah, M., Dargahi, L., Ai, J., Taei, A. A., Barough, S. E., Mowla, S. J., Tavoosidana, G., & Farahmandfar, M. (2020) · PubMed Central · doi:10.22037/ijpr.2020.112062.13508 · Cited by 34 · see citing works
CD33‐Targeted Therapies: Beating the Disease or Beaten to Death?
Maakaron, J. E., Rogosheske, J., Long, M., Bachanová, V., & Mims, A. S. (2020) · The Journal of Clinical Pharmacology · doi:10.1002/jcph.1730 · Cited by 32 · see citing works
Potasiewicz, A., Krawczyk, M., Gzieło, K., Popik, P., & Nikiforuk, A. (2020) · Behavioural Brain Research · doi:10.1016/j.bbr.2020.112547 · Cited by 31 · see citing works
Sinha, N., Karche, N. P., Verma, M. K., Walunj, S. S., Nigade, P. B., Jana, G., Kurhade, S. P., Hajare, A. K., Tilekar, A. R., Jadhav, G. R., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01569 · Cited by 30 · see citing works
Losartan Improves Memory, Neurogenesis and Cell Motility in Transgenic Alzheimer’s Mice
Drews, H. J., Klein, R., Lourhmati, A., Buadze, M., Schaeffeler, E., Lang, T., Seferyan, T., Hanson, L. R., Frey, W. H., de Vries, T. C. G. M., et al. (2021) · Pharmaceuticals · doi:10.3390/ph14020166 · Cited by 30 · see citing works
Yuede, C. M., Wallace, C. E., Davis, T. A., Gardiner, W. D., Hettinger, J. C., Edwards, H. M., Hendrix, R. D., Doherty, B. M., Yuede, K. M., Burstein, E. S., et al. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15260 · Cited by 29 · see citing works
Yan, T., Liu, B., Wang, N., Liao, Z., Wu, B., He, B., & Jia, Y. (2021) · Experimental Gerontology · doi:10.1016/j.exger.2021.111263 · Cited by 29 · see citing works
Mitochondrial Complex 1 Inhibition Increases 4-Repeat Isoform Tau by SRSF2 Upregulation
Bruch, J., Xu, H. W., Andrade, A. D., & Höglinger, G. U. (2014) · PLoS ONE · doi:10.1371/journal.pone.0113070 · Cited by 28 · see citing works
Neprilysin gene transfer: A promising therapeutic approach for A lzheimer's disease
Li, Y., Wang, J., Zhang, S., & Liu, Z. (2015) · Journal of Neuroscience Research · doi:10.1002/jnr.23564 · Cited by 27 · see citing works
Lv, S., Wu, N., Wang, Q., & Yang, L. (2020) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12543 · Cited by 27 · see citing works
The age-related microglial transformation in Alzheimer's disease pathogenesis
Yuan, C., Aierken, A., Xie, Z., Li, N., Zhao, J., & Qing, H. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.03.024 · Cited by 27 · see citing works
Evaluation of the neuroprotective effect of donepezil in type 2 diabetic rats
Gomaa, A. A., Makboul, R. M., El‐Mokhtar, M. A., Abdel‐Rahman, E. A., Ahmed, E. A., & Nicola, M. A. (2020) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12585 · Cited by 27 · see citing works
An update on the therapeutic potential of calpain inhibitors: a patent review
Donkor, I. O. (2020) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2020.1797678 · Cited by 27 · see citing works
Tiwari, V., Mishra, A., Singh, S., Mishra, S. K., Sahu, K. K., Parul, P., Kulkarni, M. J., Shukla, R., & Shukla, S. (2021) · Brain Research · doi:10.1016/j.brainres.2020.147261 · Cited by 27 · see citing works
Fu, H., Dou, J., Li, W., Cui, W., Mak, S., Hu, Q., Luo, J., Lam, C. S. C., Pang, Y., Youdim, M. B. H., et al. (2009) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2009.09.013 · Cited by 26 · see citing works
Lin, M., Chen, Y., Yang, H.-B., Lin, C., & Hung, S. (2019) · Neurotherapeutics · doi:10.1007/s13311-019-00803-7 · Cited by 26 · see citing works
Flagged first, then by citations
1 of the 240 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease
Thawabteh, A. M., Ghanem, A. W., AbuMadi, S., Thaher, D., Jaghama, W., Karaman, D., & Karaman, R. (2024) · Molecules · doi:10.3390/molecules29215131 · Cited by 56 · see citing works
“This includes γ -secretase inhibitors, such as tarenflurbil ( 7 , Figure 5) [155,156], avagacestat (labeled as 6 , Figure 5) [157,158], and semagacestat ( 5 , Figure 5) [159,160].”
BackgroundAsghar, S., Mushtaq, N., Ahmed, A., Anwar, L., Munawar, R., & Akhtar, S. (2024) · Molecules · doi:10.3390/molecules29020490 · Cited by 48 · see citing works
The double-edged nature of nicotine: toxicities and therapeutic potentials
Cao, Y., Sun, J., Wang, X., Zhang, X., Tian, H., Huang, L., Huang, Z. H., Zhang, Y., Zhang, J., Li, L., et al. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1427314 · Cited by 24 · see citing works
Khan, Y., Naeem, M., Arooj, K., Naseem, M., Adnan, R., & Azmatullah (2025) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2025.108789 · Cited by 10 · see citing works
Metamodulation of presynaptic NMDA receptors: New perspectives for pharmacological interventions
Olivero, G., Grilli, M., Marchi, M., & Pittaluga, A. (2023) · Neuropharmacology · doi:10.1016/j.neuropharm.2023.109570 · Cited by 10 · see citing works
Aging and Alzheimer’s: the critical role of mitochondrial dysfunction and synaptic alterations
Pinky, Wali, Z., Neha, Tiwari, P., El‐Tanani, M., Rabbani, S. A., & Parvez, S. (2026) · Frontiers in Synaptic Neuroscience · doi:10.3389/fnsyn.2025.1676317 · Cited by 10 · see citing works
Godinez, J., Lee, C. Y., & Schwans, J. P. (2023) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2023.129392 · Cited by 9 · see citing works
Manuel, M. T. A., & Tayo, L. L. (2023) · Brain Sciences · doi:10.3390/brainsci13111564 · Cited by 7 · see citing works
Mohamadi, M. H., Bavafa, A., Salehi, S., Abedi, M., Shahabi, F., Jafarlou, S., Kolivand, P., & Negah, S. S. (2025) · Current Therapeutic Research · doi:10.1016/j.curtheres.2025.100798 · Cited by 7 · see citing works
Molecular Mechanisms Underlying Alzheimer’s Disease Pathogenesis: Comprehensive Overview
Vecchio, F. L., la Torre, A., Gravina, C., D’Onofrio, G., & Greco, A. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27104651 · Cited by 4 · see citing works
Zyuz’kov, G. N., Miroshnichenko, L. A., Polyakova, T. Y., Simanina, E. V., & Chaikovskii, A. V. (2024) · Central Nervous System Agents in Medicinal Chemistry · doi:10.2174/0118715249302264240715060630 · Cited by 4 · see citing works
Design, Synthesis, and In Silico Analyses of Nitroimidazole Derivatives Targeting Cholinesterases
Biyik, B., Tarikogullari, A. H., Alagöz, M. A., Demir, Y., Gülçın, İ., Burmaoğlu, S., & Algül, Ö. (2025) · ChemistrySelect · doi:10.1002/slct.202502275 · Cited by 3 · see citing works
Sayar, G., Parlar, S., Tarikogullari, A. H., Erdoğan, M. A., Armağan, G., & Alptüzün, V. (2026) · Chemical Biology & Drug Design · doi:10.1111/cbdd.70285 · Cited by 3 · see citing works
Sani, A., Liu, C., Azam, J., & Khan, S. (2026) · Research Square · doi:10.21203/rs.3.rs-8572610/v1 · Cited by 1 · see citing works
Mazza, L., Crosta, F., Caragnulo, R., Ceci, M., de Lucia, C., Dini, S., & Palleschi, L. (2025) · Geriatric Care · doi:10.4081/gc.2025.13734
Khan, S. A., Ahmad, I., Faruk, M. O., Hariharasudhan, D., Баратова, Ш. Н., Djamolidinovna, D. S., Mim, T. J., O’gli, S. X. N., Mulik, R., Murad, A. B., et al. (2026) · Pharmacological Research - Natural Products · doi:10.1016/j.prenap.2026.100883
- Authors
- Alan, E., Kerry, Z., & Sevin, G.
- Affiliations
- Ege University (TR)
- Department of Pharmacology, Faculty of Pharmacy Ege University Izmir Turkey
- Venue
- Fundamental & Clinical Pharmacology
- Publisher
- Wiley
- Published
- 2023-01-13
- Volume
- 37
- Issue
- 3
- Pages
- 397-427
- ISSN
- 0767-3981 (ISSN-L)
- 1472-8206
- OpenAlex
- W4313225649
- Cited by
- 17
- References
- 240
- Citations by year
- 2026: 5 · 2025: 4 · 2024: 5 · 2023: 3
- FWCI
- 0.41
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Fundamental and Clinical Pharmacology (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, molecular mechanisms, therapeutic target, mitochondrial dysfunction, oxidative stress, neural transmission, amyloid hypothesis, tau protein, cholinergic neurotransmission, glutamatergic neurotransmission, CREB, SIRT1, neuroinflammation, glial cells, synaptic changes, disease-modifying drugs
- MeSH terms
- Alzheimer Disease, Humans, Amyloid beta-Peptides, Oxidative Stress, Neurodegenerative Diseases
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review