Cited by 53Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchCholinesterase and Neurodegenerative Diseases

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Symptomatic and Disease-Modifying Therapy Pipeline for Alzheimer’s Disease: Towards a Personalized Polypharmacology Patient-Centered Approach

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Morató, Xavier, Pytel, Vanesa, Jofresa, Sara, Ruiz, Agustín, Boada, Mercè·2022·International Journal of Molecular Sciences

DOI 10.3390/ijms23169305PMC PMC9409252

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Abstract

Since 1906, when Dr. Alois Alzheimer first described in a patient “a peculiar severe disease process of the cerebral cortex”, people suffering from this pathology have been waiting for a breakthrough therapy. Alzheimer’s disease (AD) is an irreversible, progressive neurodegenerative brain disorder and the most common form of dementia in the elderly with a long presymptomatic phase. Worldwide, approximately 50 million people are living with dementia, with AD comprising 60–70% of cases. Pathologically, AD is characterized by the deposition of amyloid β-peptide (Aβ) in the neuropil (neuritic plaques) and blood vessels (amyloid angiopathy), and by the accumulation of hyperphosphorylated tau in neurons (neurofibrillary tangles) in the brain, with associated loss of synapses and neurons, together with glial activation, and neuroinflammation, resulting in cognitive deficits and eventually dementia. The current competitive landscape in AD consists of symptomatic treatments, of which there are currently six approved medications: three AChEIs (donepezil, rivastigmine, and galantamine), one NMDA-R antagonist (memantine), one combination therapy (memantine/donepezil), and GV-971 (sodium oligomannate, a mixture of oligosaccharides derived from algae) only approved in China. Improvements to the approved therapies, such as easier routes of administration and reduced dosing frequencies, along with the developments of new strategies and combined treatments are expected to occur within the next decade and will positively impact the way the disease is managed. Recently, Aducanumab, the first disease-modifying therapy (DMT) has been approved for AD, and several DMTs are in advanced stages of clinical development or regulatory review. Small molecules, mAbs, or multimodal strategies showing promise in animal studies have not confirmed that promise in the clinic (where small to moderate changes in clinical efficacy have been observed), and therefore, there is a significant unmet need for a better understanding of the AD pathogenesis and the exploration of alternative etiologies and therapeutic effective disease-modifying therapies strategies for AD. Therefore, a critical review of the disease-modifying therapy pipeline for Alzheimer’s disease is needed.

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Bivalent Brain Shuttle Increases Antibody Uptake by Monovalent Binding to the Transferrin Receptor
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A 36-week multicenter, randomized, double-blind, placebo-controlled, parallel-group, phase 3 clinical trial of sodium oligomannate for mild-to-moderate Alzheimer’s dementia
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Aducanumab produced a clinically meaningful benefit in association with amyloid lowering
Cummings, J., Aisen, P., Lemere, C., Atri, A., Sabbagh, M., & Salloway, S. (2021) · Alzheimer's Research & Therapy · doi:10.1186/s13195-021-00838-z · Cited by 224
Evaluating the effects of the novel GLP-1 analogue liraglutide in Alzheimer’s disease: study protocol for a randomised controlled trial (ELAD study)
Femminella, G. D., Frangou, E., Love, S., Busza, G., Holmes, C., Ritchie, C. W., Lawrence, R., McFarlane, B., Tadros, G., Ridha, B. H., et al. (2019) · Trials · doi:10.1186/s13063-019-3259-x · Cited by 220
TREM2, microglia, and Alzheimer’s disease.
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Safety and Efficacy of Semorinemab in Individuals With Prodromal to Mild Alzheimer Disease
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Substrate and Inhibitor Profile of BACE (β-Secretase) and Comparison with Other Mammalian Aspartic Proteases
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Untangling the association of amyloid-β and tau with synaptic and axonal loss in Alzheimer’s disease
Pereira, J. B., Janelidze, S., Ossenkoppele, R., Kvartsberg, H., Brinkmalm, A., Mattsson, N., Stomrud, E., Smith, R. A., Zetterberg, H., Blennow, K., et al. (2020) · Brain · doi:10.1093/brain/awaa395 · Cited by 208
Aducanumab: Appropriate Use Recommendations Update
Cummings, J. L., Rabinovici, G. D., Atri, A., Aisen, P. S. S., Apostolova, L. G., Hendrix, S. B., Sabbagh, M. N., Selkoe, D. J., Weiner, M. W., & Salloway, S. (2022) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2022.34 · Cited by 204
Novel dual GLP-1/GIP receptor agonists show neuroprotective effects in Alzheimer's and Parkinson's disease models
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The role of innate immune genes in Alzheimer's disease
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NSAID Exposure and Risk of Alzheimer's Disease: An Updated Meta-Analysis From Cohort Studies
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Liposomal vaccines with conformation-specific amyloid peptide antigens define immune response and efficacy in APP transgenic mice
Muhs, A., Hickman, D. T., Pihlgren, M., Chuard, N., Giriens, V., Meerschman, C., der Auwera, I. V., LEUVEN, F. V., Sugawara, M., Weingertner, M.-C., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703137104 · Cited by 182
Brain insulin resistance: role in neurodegenerative disease and potential for targeting
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APOE immunotherapy reduces cerebral amyloid angiopathy and amyloid plaques while improving cerebrovascular function
Xiong, M., Jiang, H., Serrano, J. R., Gonzales, E. R., Wang, C., Gratuze, M., Hoyle, R., Bien-Ly, N., Silverman, A. P., Sullivan, P. M., et al. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abd7522 · Cited by 179
BACE1 (β-secretase) knockout mice do not acquire compensatory gene expression changes or develop neural lesions over time
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Soluble oligomeric amyloid-β induces calcium dyshomeostasis that precedes synapse loss in the living mouse brain
Arbel‐Ornath, M., Hudry, E., Boivin, J. R., Hashimoto, T., Takeda, S., Kuchibhotla, K. V., Hou, S. S., Lattarulo, C. R., Belcher, A. M., Shakerdge, N. B., et al. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0169-9 · Cited by 176
AAVrh.10-Mediated APOE2 Central Nervous System Gene Therapy for APOE4-Associated Alzheimer's Disease
Rosenberg, J. B., Kaplitt, M. G., De, B. P., Chen, A., Flagiello, T., Salami, C., Pey, E., Zhao, L., Ricart Arbona, R. J., Monette, S., et al. (2018) · Human Gene Therapy Clinical Development · doi:10.1089/humc.2017.231 · Cited by 176 · cited 3×
“The study assessed the safety and toxicity of intrathecal administration of LX1001 (an adeno-associated virus gene transfer vector expressing the cDNA coding for human ApoE2) [219].”
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Peripheral administration of the soluble TNF inhibitor XPro1595 modifies brain immune cell profiles, decreases beta-amyloid plaque load, and rescues impaired long-term potentiation in 5xFAD mice
MacPherson, K. P., Sompol, P. M., Kannarkat, G. T., Chang, J., Sniffen, L. J., Wildner, M., Norris, C. M., & Tansey, M. G. (2017) · Neurobiology of Disease · doi:10.1016/j.nbd.2017.02.010 · Cited by 166
Extracellular Monomeric Tau Protein Is Sufficient to Initiate the Spread of Tau Protein Pathology
Michel, C. H., Kumar, S., Pinotsi, D., Tunnacliffe, A., St. George-Hyslop, P., Mandelkow, E., Mandelkow, E.-M., Kaminski, C. F., & Kaminski Schierle, G. S. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.515445 · Cited by 165
Memantine, Donepezil, or Combination Therapy—What is the best therapy for Alzheimer’s Disease? A Network Meta‐Analysis
Guo, J., Wang, Z., Liu, R., Huang, Y., Zhang, N., & Zhang, R. (2020) · Brain and Behavior · doi:10.1002/brb3.1831 · Cited by 165
Fifteen Years of the Australian Imaging, Biomarkers and Lifestyle (AIBL) Study: Progress and Observations from 2,359 Older Adults Spanning the Spectrum from Cognitive Normality to Alzheimer’s Disease
Fowler, C., Rainey-Smith, S. R., Bird, S., Bomke, J., Bourgeat, P., Brown, B. M., Burnham, S. C., Bush, A. I., Chadunow, C., Collins, S., et al. (2021) · Journal of Alzheimer's Disease Reports · doi:10.3233/adr-210005 · Cited by 164
Amyloid-Related Imaging Abnormalities With Anti-amyloid Antibodies for the Treatment of Dementia Due to Alzheimer's Disease
Withington, C., & Turner, R. S. (2022) · Frontiers in Neurology · doi:10.3389/fneur.2022.862369 · Cited by 158
A phase 3 trial of IV immunoglobulin for Alzheimer disease
Relkin, N. R., Thomas, R. G., Rissman, R. A., Brewer, J. B., Rafii, M. S., van Dyck, C. H., Jack, C. R., Sano, M., Knopman, D. S., Raman, R., et al. (2017) · Neurology · doi:10.1212/wnl.0000000000003904 · Cited by 157
Preclinical Assessment of Young Blood Plasma for Alzheimer Disease
Middeldorp, J., Lehallier, B., Villeda, S. A., Miedema, S. S. M., Evans, E., Czirr, E., Zhang, H., Luo, J., Stan, T., Mosher, K. I., et al. (2016) · JAMA Neurology · doi:10.1001/jamaneurol.2016.3185 · Cited by 153
UB‐311, a novel UBITh ® amyloid β peptide vaccine for mild Alzheimer's disease
Wang, C. Y., Wang, P., Chiu, M., Finstad, C. L., Lin, F., Lynn, S., Tai, Y., De Fang, X., Zhao, K., Hung, C., et al. (2017) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2017.03.005 · Cited by 150
Plasma Amyloid-β (Aβ 42 ) Correlates with Cerebrospinal Fluid Aβ 42 in Alzheimer’s Disease
Teunissen, C. E., Chiu, M., Yang, C., Yang, S., Scheltens, P., Zetterberg, H., & Blennow, K. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170784 · Cited by 150
Safety and efficacy of tilavonemab in progressive supranuclear palsy: a phase 2, randomised, placebo-controlled trial
Höglinger, G. U., Litvan, I., Mendonça, N., Wang, D., Zheng, H., Rendenbach‐Mueller, B., Lon, H., Jin, Z., Fisseha, N., Budur, K. S., et al. (2021) · The Lancet Neurology · doi:10.1016/s1474-4422(20)30489-0 · Cited by 150
FUNDAMANT: an interventional 72-week phase 1 follow-up study of AADvac1, an active immunotherapy against tau protein pathology in Alzheimer's disease
Novak, P., Schmidt, R., Kontsekova, E., Kovacech, B., Smolek, T., Katina, S., Fialova, L., Prcina, M., Parrak, V., Dal-Bianco, P., et al. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0436-1 · Cited by 147
Active Aβ immunotherapy CAD106 in Alzheimer's disease: A phase 2b study
Vandenberghe, R. R., Riviere, M., Caputo, A., Sóvágó, J., Maguire, R. P., Farlow, M. R., Marotta, G., Sánchez‐Valle, R., Scheltens, P., Ryan, J. M., et al. (2016) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2016.12.003 · Cited by 146
Therapeutic Trem2 activation ameliorates amyloid-beta deposition and improves cognition in the 5XFAD model of amyloid deposition
Price, B. R., Sudduth, T. L., Weekman, E. M., Johnson, S. N., Hawthorne, D., Woolums, A. E., & Wilcock, D. M. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01915-0 · Cited by 146
Recent Advances in Incretin-Based Pharmacotherapies for the Treatment of Obesity and Diabetes
Tan, Q., Akindehin, S. E., Orsso, C. E., Waldner, R. C., DiMarchi, R. D., Müller, T. D., & Haqq, A. M. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.838410 · Cited by 146
CSF evidence of pericyte damage in Alzheimer’s disease is associated with markers of blood-brain barrier dysfunction and disease pathology
Miners, J. S., Kehoe, P. G., Love, S., Zetterberg, H., & Blennow, K. (2019) · Alzheimer s Research & Therapy · doi:10.1186/s13195-019-0534-8 · Cited by 143
A randomized, controlled clinical trial of plasma exchange with albumin replacement for Alzheimer's disease: Primary results of the AMBAR Study
Boada, M., López, O. L., Olazarán, J., Núñez, L., Pfeffer, M., Paricio, M., Lorites, J., Piñol‐Ripoll, G., Gámez, J. E., Anaya, F., et al. (2020) · Alzheimer's & Dementia · doi:10.1002/alz.12137 · Cited by 143
Self-citation
Targeting soluble tumor necrosis factor as a potential intervention to lower risk for late-onset Alzheimer’s disease associated with obesity, metabolic syndrome, and type 2 diabetes
Rodrigues, M. E. D. S., Houser, M. C., Walker, D. I., Jones, D. P., Chang, J., Barnum, C. J., & Tansey, M. G. (2019) · Alzheimer s Research & Therapy · doi:10.1186/s13195-019-0546-4 · Cited by 141
Plasma lipidome is dysregulated in Alzheimer’s disease and is associated with disease risk genes
Liu, Y., Thalamuthu, A., Mather, K. A., Crawford, J. D., Ulanova, M., Wong, M. W. K., Pickford, R., Sachdev, P. S., & Braidy, N. (2021) · Translational Psychiatry · doi:10.1038/s41398-021-01362-2 · Cited by 140
DEFINING DISEASE MODIFYING THERAPY FOR ALZHEIMER’S DISEASE
Cummings, J., & Fox, N. (2017) · The Journal of Prevention of Alzheimer's Disease · doi:10.14283/jpad.2017.12 · Cited by 139
Epitope determines efficacy of therapeutic anti-Tau antibodies in a functional assay with human Alzheimer Tau
Courade, J., Angers, R. C., Mairet‐Coello, G., Pacico, N., Tyson, K. L., Lightwood, D. J., Munro, R., McMillan, D., Griffin, R., BAKER, T. S., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1911-2 · Cited by 137
The amyloid plaque proteome in early onset Alzheimer’s disease and Down syndrome
Drummond, E., Kavanagh, T., Pires, G., Marta-Ariza, M., Kanshin, E., Nayak, S., Faustin, A., Berdah, V., Ueberheide, B., & Wisniewski, T. (2022) · Acta Neuropathologica Communications · doi:10.1186/s40478-022-01356-1 · Cited by 137
The Ca2+-gated channel TMEM16A amplifies capillary pericyte contraction and reduces cerebral blood flow after ischemia
Korte, N., Ilkan, Z., Pearson, C. L., Pfeiffer, T., Singhal, P., Rock, J., Sethi, H., Gill, D., Attwell, D., & Tammaro, P. (2022) · Journal of Clinical Investigation · doi:10.1172/jci154118 · Cited by 135
Clinical Pharmacokinetics and Safety of ALZ-801, a Novel Prodrug of Tramiprosate in Development for the Treatment of Alzheimer’s Disease
Hey, J. A., Yu, Y., Versavel, M., Abushakra, S. R., Kočiš, P., Power, A., Kaplan, P. L., Amedio, J. C., & Tolar, M. (2017) · Clinical Pharmacokinetics · doi:10.1007/s40262-017-0608-3 · Cited by 132
Preclinical and Clinical Development of ABBV-8E12, a Humanized Anti-Tau Antibody, for Treatment of Alzheimer's Disease and Other Tauopathies.
West, T., Hu, Y., Verghese, P. B., Bateman, R. J., Braunstein, J. B., Fogelman, I., Budur, K., Florian, H., Mendonca, N., & Holtzman, D. M. (2017) · PubMed · doi:10.14283/jpad.2017.36 · Cited by 132
Activation of NLRP3 Inflammasome and Onset of Alzheimer’s Disease
Bai, H., & Zhang, Q. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.701282 · Cited by 132
APOE-amyloid interaction: Therapeutic targets
Wisniewski, T., & Drummond, E. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.104784 · Cited by 131
Huperzine A and Its Neuroprotective Molecular Signaling in Alzheimer’s Disease
Friedli, M. J., & Inestrosa, N. C. (2021) · Molecules · doi:10.3390/molecules26216531 · Cited by 131
Safety, tolerability and efficacy of the glutaminyl cyclase inhibitor PQ912 in Alzheimer’s disease: results of a randomized, double-blind, placebo-controlled phase 2a study
Scheltens, P., Hallikainen, M., Grimmer, T., Duning, T., Gouw, A. A., Teunissen, C. E., Wink, A. M., Maruff, P., Harrison, J., van Baal, C. M., et al. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0431-6 · Cited by 129
GLP-1’s role in neuroprotection: a systematic review
Erbil, D., Eren, C. Y., Demirel, Ç., Küçüker, M. U., Solaroğlu, İ., & Eser, H. Y. (2019) · Brain Injury · doi:10.1080/02699052.2019.1587000 · Cited by 129
Amyloid precursor protein transgenic mouse models and Alzheimer's disease: Understanding the paradigms, limitations, and contributions
Kokjohn, T. A., & Roher, A. E. (2009) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2009.03.002 · Cited by 126
CD33 in Alzheimer’s Disease – Biology, Pathogenesis, and Therapeutics: A Mini-Review
Zhao, L. (2018) · Gerontology · doi:10.1159/000492596 · Cited by 126
Counteracting the effects of TNF receptor‐1 has therapeutic potential in Alzheimer's disease
Steeland, S., Gorlé, N., Vandendriessche, C., Balusu, S., Brkić, M., Cauwenberghe, C. V., Imschoot, G. V., Wonterghem, E. V., Rycke, R. M. D., Kremer, A., et al. (2018) · EMBO Molecular Medicine · doi:10.15252/emmm.201708300 · Cited by 125
Characterisation of PDGF-BB:PDGFRβ signalling pathways in human brain pericytes: evidence of disruption in Alzheimer’s disease
Smyth, L. C. D., Highet, B., Jansson, D., Wu, J., Rustenhoven, J., Aalderink, M., Tan, A. Y. S., Li, S., Johnson, R. H., Coppieters, N., et al. (2022) · Communications Biology · doi:10.1038/s42003-022-03180-8 · Cited by 123
Donanemab (LY3002813) Phase 1b Study in Alzheimer's Disease: Rapid and Sustained Reduction of Brain Amyloid Measured by Florbetapir F18 Imaging
Lowe, S. L., Evans, C. D., Shcherbinin, S., Cheng, Y.-J., Willis, B. A., Gueorguieva, I., Lo, A., Fleisher, A., Dage, J. L., Ardayfio, P. A., et al. (2021) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2021.56 · Cited by 121
Ageing and rejuvenation models reveal changes in key microbial communities associated with healthy ageing
Shin, J., Noh, J., Choe, D., Lee, N., Song, Y., Cho, S., Kang, E., Go, M., Ha, S. K., Chang, D., et al. (2021) · Microbiome · doi:10.1186/s40168-021-01189-5 · Cited by 119
Amyloidogenic Processing of Amyloid Precursor Protein: Evidence of a Pivotal Role of Glutaminyl Cyclase in Generation of Pyroglutamate-Modified Amyloid-β
Cynis, H., Scheel, E., Saido, T. C., Schilling, S., & Demuth, H. (2008) · Biochemistry · doi:10.1021/bi800250p · Cited by 117
The Inflammatory Marker YKL-40 Is Elevated in Cerebrospinal Fluid from Patients with Alzheimer’s but Not Parkinson’s Disease or Dementia with Lewy Bodies
Wennström, M., Surova, Y., Hall, S., Nilsson, C., Minthon, L., Hansson, O., & Nielsen, H. M. (2015) · PLoS ONE · doi:10.1371/journal.pone.0135458 · Cited by 116
AADvac1, an Active Immunotherapy for Alzheimer's Disease and Non Alzheimer Tauopathies: An Overview of Preclinical and Clinical Development
Novák, P., Žilka, N., Žilková, M., Kováčech, B., Škrabana, R., Ondrus, M., Fialová, L., Kontseková, E., Otto, M., & Novák, M. (2019) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2018.45 · Cited by 115
Rejuvenation of three germ layers tissues by exchanging old blood plasma with saline-albumin
Mehdipour, M., Skinner, C., Wong, N., Lieb, M., Liu, C., Etienne, J., Kato, C., Kiprov, D., Conboy, M. J., & Conboy, I. M. (2020) · Aging · doi:10.18632/aging.103418 · Cited by 115
Glutaminyl Cyclase in Human Cortex: Correlation with (pGlu)-Amyloid-β Load and Cognitive Decline in Alzheimer's Disease
Morawski, M., Schilling, S., Kreuzberger, M., Waniek, A., Jäger, C., Koch, B. M., Cynis, H., Kehlen, A., Arendt, T., Hartlage‐Rübsamen, M., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131535 · Cited by 114
INTREPAD: A randomized trial of naproxen to slow progress of presymptomatic Alzheimer disease
Meyer, P.-F., Tremblay-Mercier, J., Leoutsakos, J., Madjar, C., Lafaille-Maignan, M.-É., Savard, M., Rosa-Neto, P., Poirier, J., Etienne, P., Breitner, J., et al. (2019) · Neurology · doi:10.1212/wnl.0000000000007232 · Cited by 113
Engagement of TREM2 by a novel monoclonal antibody induces activation of microglia and improves cognitive function in Alzheimer’s disease models
Fassler, M., Rappaport, M., Benaim, C., & George, J. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01980-5 · Cited by 112
Safety, tolerability and immunogenicity of an active anti-Aβ40 vaccine (ABvac40) in patients with Alzheimer’s disease: a randomised, double-blind, placebo-controlled, phase I trial
Lacosta, A.-M., Pascual-Lucas, M., Pesini, P., Casabona, D., Pérez-Grijalba, V., Marcos-Campos, I., Sarasa, L., Canudas, J., Badi, H., Monleón, I., et al. (2018) · Alzheimer's Research & Therapy · doi:10.1186/s13195-018-0340-8 · Cited by 111
Safety, Tolerability, and Feasibility of Young Plasma Infusion in the Plasma for Alzheimer Symptom Amelioration Study: A Randomized Clinical Trial
Sha, S. J., Deutsch, G. K., Tian, L., Richardson, K., Coburn, M., Gaudioso, J. L., Marcal, T., Solomon, E., Boumis, A., Bet, A., et al. (2019) · JAMA Neurology · doi:10.1001/jamaneurol.2018.3288 · Cited by 109
Drug repositioning for Alzheimer’s disease based on systematic “omics” data mining
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The Link Between Tau and Insulin Signaling: Implications for Alzheimer’s Disease and Other Tauopathies
Gonçalves, R. A., Wijesekara, N., Fraser, P. E., & Felice, F. G. D. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00017 · Cited by 108
Intracerebral adeno-associated virus gene delivery of apolipoprotein E2 markedly reduces brain amyloid pathology in Alzheimer's disease mouse models
Zhao, L., Gottesdiener, A. J., Parmar, M., Li, M., Kaminsky, S. M., Chiuchiolo, M. J., Sondhi, D., Sullivan, P. M., Holtzman, D. M., Crystal, R. G., et al. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.04.020 · Cited by 107
Brain Shuttle Antibody for Alzheimer’s Disease with Attenuated Peripheral Effector Function due to an Inverted Binding Mode
Weber, F. C., Bohrmann, B., Niewoehner, J., Fischer, J. A. A., Rueger, P., Tiefenthaler, G., Moelleken, J., Bujotzek, A., Brady, K., Singer, T., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.12.019 · Cited by 107
The Role of Mitochondrial Calcium Homeostasis in Alzheimer’s and Related Diseases
Ryan, K. C., Ashkavand, Z., & Norman, K. R. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21239153 · Cited by 106
Alzheimer's disease: β‐amyloid plaque formation in human brain
Seeman, P. M., & Seeman, N. (2011) · Synapse · doi:10.1002/syn.20957 · Cited by 103
GIP has neuroprotective effects in Alzheimer and Parkinson’s disease models
Zhang, Z., & Hölscher, C. (2019) · Peptides · doi:10.1016/j.peptides.2019.170184 · Cited by 101
Microglial Phenotypic Transition: Signaling Pathways and Influencing Modulators Involved in Regulation in Central Nervous System Diseases
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Cromolyn Reduces Levels of the Alzheimer’s Disease-Associated Amyloid β-Protein by Promoting Microglial Phagocytosis
Zhang, C., Griciuc, A., Hudry, E., Wan, Y., Quinti, L., Ward, J., Forte, A. M., Shen, X., Ran, C., Elmaleh, D. R., et al. (2018) · Scientific Reports · doi:10.1038/s41598-018-19641-2 · Cited by 99
Elevating the Levels of Calcium Ions Exacerbate Alzheimer’s Disease via Inducing the Production and Aggregation of β-Amyloid Protein and Phosphorylated Tau
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Young bone marrow transplantation preserves learning and memory in old mice
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Pyroglutamate and Isoaspartate modified Amyloid-Beta in ageing and Alzheimer’s disease
Moro, M. L., Phillips, A. S., Gaimster, K., Paul, C., Mudher, A. K., Nicoll, J. A. R., & Boche, D. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0505-x · Cited by 97
Molecular basis for mid-region amyloid-β capture by leading Alzheimer's disease immunotherapies
Crespi, G. A. N., Hermans, S. J., Parker, M. W., & Miles, L. A. (2015) · Scientific Reports · doi:10.1038/srep09649 · Cited by 96
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See all 53

Authors: Morató, X., Pytel, V., Jofresa, S., Ruiz, A., & Boada, M.
Affiliations: Universitat Internacional de Catalunya (ES)
Research Center and Memory Clinic, Fundació ACE, Institut Català de Neurociències Aplicades, Universitat Internacional de Catalunya, 08017 Barcelona, Spain
Corresponding author: Morató, Xavier
ORCID: Morató, Xavier
Pytel, Vanesa
Ruiz, Agustín
Venue: International Journal of Molecular Sciences
Publisher: MDPI AG
Published: 2022-08-18
Volume: 23
Issue: 16
Pages: 9305
ISSN: 1422-0067 (ISSN-L)
DOI: 10.3390/ijms23169305
PMC: PMC9409252
OpenAlex: W4292247066
Cited by: 53
References: 249
Citations by year: 2026: 10 · 2025: 16 · 2024: 15 · 2023: 10 · 2022: 2
FWCI: 1.48
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: International Journal of Molecular Sciences (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
Keywords: Alzheimer's disease, disease-modifying therapy, symptomatic treatment, drug development pipeline, polypharmacology, personalized medicine, amyloid-beta, tau hyperphosphorylation, cholinesterase inhibitors, memantine, aducanumab, anti-amyloid monoclonal antibodies, neuroinflammation
MeSH terms: Donepezil, Alzheimer Disease, Animals, Humans, Memantine, Amyloid beta-Peptides, Patient-Centered Care, Polypharmacology

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Symptomatic and Disease-Modifying Therapy Pipeline for Alzheimer’s Disease: Towards a Personalized Polypharmacology Patient-Centered Approach

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