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

Morató, Xavier; Pytel, Vanesa; Jofresa, Sara; Ruiz, Agustín; Boada, Mercè

doi:10.3390/ijms23169305

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

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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DMTs are intended to delay progression of long-term conditions such as AD and ultimately improve patient's quality of life.
“DMTs are intended to delay the progression of long-term conditions such as AD and ultimately improve the patient’s quality of life [60].”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [60]
DMTs are treatments that postpone, moderate, or even reverse the evolution of an illness by addressing its underlying cause.
“DMTs are treatments that postpone, moderate, or even reverse the evolution of an illness by addressing its underlying cause.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [60]

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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
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NSAID Exposure and Risk of Alzheimer's Disease: An Updated Meta-Analysis From Cohort Studies
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Soluble oligomeric amyloid-β induces calcium dyshomeostasis that precedes synapse loss in the living mouse brain
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Extracellular Monomeric Tau Protein Is Sufficient to Initiate the Spread of Tau Protein Pathology
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Memantine, Donepezil, or Combination Therapy—What is the best therapy for Alzheimer’s Disease? A Network Meta‐Analysis
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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 · see citing works
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 158 · see citing works
A phase 3 trial of IV immunoglobulin for Alzheimer disease
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Preclinical Assessment of Young Blood Plasma for Alzheimer Disease
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Amyloid-Related Imaging Abnormalities With Anti-amyloid Antibodies for the Treatment of Dementia Due to Alzheimer's Disease
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UB‐311, a novel UBITh <sup>®</sup> amyloid β peptide vaccine for mild Alzheimer's disease
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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 · see citing works
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 146 · see citing works
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 146 · see citing works
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 · see citing works
A randomized, controlled clinical trial of plasma exchange with albumin replacement for Alzheimer's disease: Primary results of the AMBAR Study
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Therapeutic Trem2 activation ameliorates amyloid-beta deposition and improves cognition in the 5XFAD model of amyloid deposition
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Active Aβ immunotherapy CAD106 in Alzheimer's disease: A phase 2b study
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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
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DEFINING DISEASE MODIFYING THERAPY FOR ALZHEIMER’S DISEASE
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CSF evidence of pericyte damage in Alzheimer’s disease is associated with markers of blood-brain barrier dysfunction and disease pathology
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The amyloid plaque proteome in early onset Alzheimer’s disease and Down syndrome
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Plasma lipidome is dysregulated in Alzheimer’s disease and is associated with disease risk genes
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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 · see citing works
The Ca2+-gated channel TMEM16A amplifies capillary pericyte contraction and reduces cerebral blood flow after ischemia
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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 131 · see citing works
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 130 · see citing works
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 · see citing works
Activation of NLRP3 Inflammasome and Onset of Alzheimer’s Disease
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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 128 · see citing works
APOE-amyloid interaction: Therapeutic targets
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Huperzine A and Its Neuroprotective Molecular Signaling in Alzheimer’s Disease
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CD33 in Alzheimer’s Disease – Biology, Pathogenesis, and Therapeutics: A Mini-Review
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Amyloid precursor protein transgenic mouse models and Alzheimer's disease: Understanding the paradigms, limitations, and contributions
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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 119 · see citing works
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 119 · see citing works
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 118 · see citing works
Amyloidogenic Processing of Amyloid Precursor Protein: Evidence of a Pivotal Role of Glutaminyl Cyclase in Generation of Pyroglutamate-Modified Amyloid-β
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Ageing and rejuvenation models reveal changes in key microbial communities associated with healthy ageing
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AADvac1, an Active Immunotherapy for Alzheimer's Disease and Non Alzheimer Tauopathies: An Overview of Preclinical and Clinical Development
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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 · see citing works
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
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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 · see citing works
Rejuvenation of three germ layers tissues by exchanging old blood plasma with saline-albumin
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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 · see citing works
A phase 1 clinical trial of the sigma‐2 receptor complex allosteric antagonist CT1812, a novel therapeutic candidate for Alzheimer's disease
Grundman, M., Morgan, R. E., Lickliter, J. D., Schneider, L. S., DeKosky, S. T., Izzo, N. J., Guttendorf, R. J., Higgin, M., Pribyl, J., Mozzoni, K., et al. (2018) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2018.11.001 · Cited by 111 · see citing works
Engagement of TREM2 by a novel monoclonal antibody induces activation of microglia and improves cognitive function in Alzheimer’s disease models
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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 · see citing works
Drug repositioning for Alzheimer’s disease based on systematic “omics” data mining
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Intracerebral adeno-associated virus gene delivery of apolipoprotein E2 markedly reduces brain amyloid pathology in Alzheimer's disease mouse models
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The Link Between Tau and Insulin Signaling: Implications for Alzheimer’s Disease and Other Tauopathies
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The Role of Mitochondrial Calcium Homeostasis in Alzheimer’s and Related Diseases
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Brain Shuttle Antibody for Alzheimer’s Disease with Attenuated Peripheral Effector Function due to an Inverted Binding Mode
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Preclinical and clinical biomarker studies of CT1812: A novel approach to Alzheimer's disease modification
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Cromolyn Reduces Levels of the Alzheimer’s Disease-Associated Amyloid β-Protein by Promoting Microglial Phagocytosis
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Young bone marrow transplantation preserves learning and memory in old mice
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Molecular basis for mid-region amyloid-β capture by leading Alzheimer's disease immunotherapies
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Pyroglutamate and Isoaspartate modified Amyloid-Beta in ageing and Alzheimer’s disease
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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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Efficacy and Safety of Plasma Exchange with 5% Albumin to Modify Cerebrospinal Fluid and Plasma Amyloid-β Concentrations and Cognition Outcomes in Alzheimer’s Disease Patients: A Multicenter, Randomized, Controlled Clinical Trial
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Neuroinflammation as a Potential Therapeutic Target in Alzheimer’s Disease
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Vaccination of Alzheimer's model mice with Aβ derivative in alum adjuvant reduces Aβ burden without microhemorrhages
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Target engagement in an Alzheimer trial: crenezumab lowers amyloid β oligomers in cerebrospinal fluid
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Microglial Phenotypic Transition: Signaling Pathways and Influencing Modulators Involved in Regulation in Central Nervous System Diseases
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Neurotransmitter Imbalance in the Brain and Alzheimer’s Disease Pathology
Snowden, S. G., Ebshiana, A. A., Hye, A., Pletniková, O., O’Brien, R., An, Y., Troncoso, J. C., Legido‐Quigley, C., & Thambisetty, M. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190577 · Cited by 89 · see citing works
Deletion of Alzheimer's disease‐associated CD33 results in an inflammatory human microglia phenotype
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TREM2/DAP12 Complex Regulates Inflammatory Responses in Microglia via the JNK Signaling Pathway
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Is Brain Amyloid Production a Cause or a Result of Dementia of The Alzheimer's Type?
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Association of β-Amyloid Level, Clinical Progression, and Longitudinal Cognitive Change in Normal Older Individuals
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Lessons from a BACE1 inhibitor trial: Off‐site but not off base
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The Neurotoxic Role of Extracellular Tau Protein
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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
Neuronal Calcium Signaling and Alzheimer’s Disease
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A Review on Tramiprosate (Homotaurine) in Alzheimer's Disease and Other Neurocognitive Disorders
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A Food and Drug Administration-approved Asthma Therapeutic Agent Impacts Amyloid β in the Brain in a Transgenic Model of Alzheimer Disease
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“Cromolyn sodium, a small molecule approved for the treatment of asthma (with structural similarity to fisetin, an anti-Aβ aggregation molecule) [148] reduced Aβ levels in transgenic AD mouse brains and showed increased Aβ42 uptake in microglial cell-based assays [149,150].”
Background
Presenilin transgenic mice as models of Alzheimer’s disease
Elder, G. A., Sosa, M. A. G., Gasperi, R. D., Dickstein, D. L., & Hof, P. R. (2009) · Brain Structure and Function · doi:10.1007/s00429-009-0227-3 · Cited by 76 · see citing works
The Alzheimer's disease–protective CD33 splice variant mediates adaptive loss of function via diversion to an intracellular pool
Siddiqui, S. S., Springer, S. A., Verhagen, A., Sundaramurthy, V., Alisson‐Silva, F., Jiang, W., Ghosh, P., & Varki, A. P. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.799346 · Cited by 76 · see citing works
Galantamine-Memantine combination in the treatment of Alzheimer's disease and beyond
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Dynamic changes of CSF sPDGFRβ during ageing and AD progression and associations with CSF ATN biomarkers
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Atorvastatin‐induced activation of Alzheimer's α secretase is resistant to standard inhibitors of protein phosphorylation‐regulated ectodomain shedding
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Potential of the Antibody Against cis–Phosphorylated Tau in the Early Diagnosis, Treatment, and Prevention of Alzheimer Disease and Brain Injury
Lu, K. P., Kondo, A., Albayram, Ö., Herbert, M. K., Liu, H., & Zhou, X. Z. (2016) · JAMA Neurology · doi:10.1001/jamaneurol.2016.2027 · Cited by 74 · see citing works
Innate immune activation in Alzheimer’s disease
Wang, M., Miao, D., Cao, X., Tan, L., & Tan, L. (2018) · Annals of Translational Medicine · doi:10.21037/atm.2018.04.20 · Cited by 74 · see citing works
Discovery and Identification of an Endogenous Metabolite of Tramiprosate and Its Prodrug ALZ-801 that Inhibits Beta Amyloid Oligomer Formation in the Human Brain
Hey, J. A., Kočiš, P., Hort, J., Abushakra, S. R., Power, A., Vyhnálek, M., Yu, Y., & Tolar, M. (2018) · CNS Drugs · doi:10.1007/s40263-018-0554-0 · Cited by 73 · see citing works
Symptomatic amyloid‐related imaging abnormalities in an APOE ε4/ε4 patient treated with aducanumab
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Interaction between cerebrovascular disease and Alzheimer pathology
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Amyloid-β Oligomers Relate to Cognitive Decline in Alzheimer's Disease
Jongbloed, W., Bruggink, K. A., Kester, M. I., Visser, P.-J., Scheltens, P., Blankenstein, M. A., Verbeek, M. M., Teunissen, C. E., & Veerhuis, R. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-142136 · Cited by 68 · see citing works
IVIG treatment of mild cognitive impairment due to Alzheimer's disease: a randomised double-blinded exploratory study of the effect on brain atrophy, cognition and conversion to dementia
Kile, S. J., Au, W. J., Parise, C. A., Rose, K., Donnel, T., Hankins, A. I., Chan, M., & Ghassemi, A. (2015) · Journal of Neurology Neurosurgery & Psychiatry · doi:10.1136/jnnp-2015-311486 · Cited by 67 · see citing works
Amyloid-β Peptide Impact on Synaptic Function and Neuroepigenetic Gene Control Reveal New Therapeutic Strategies for Alzheimer’s Disease
Karisetty, B. C., Bhatnagar, A., Armour, E. M., Beaver, M., Zhang, H., & Elefant, F. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.577622 · Cited by 67 · see citing works
Glutaminyl cyclase contributes to the formation of focal and diffuse pyroglutamate (pGlu)-Aβ deposits in hippocampus via distinct cellular mechanisms
Hartlage‐Rübsamen, M., Morawski, M., Waniek, A., Jäger, C., Zeitschel, U., Koch, B. C. P., Cynis, H., Schilling, S., Schliebs, R., Demuth, H., et al. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0806-2 · Cited by 66 · see citing works
Deciphering Brain Insulin Receptor and Insulin‐Like Growth Factor 1 Receptor Signalling
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Long-term extensions of randomized vaccination trials of ACC-001 and QS-21 in mild to moderate Alzheimer’s disease
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Characterization of tau binding by gosuranemab
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The Role of GIP in the Regulation of GLP-1 Satiety and Nausea
Hayes, M. R., Borner, T., & Jonghe, B. C. D. (2021) · Diabetes · doi:10.2337/dbi21-0004 · Cited by 64 · see citing works
Aducanumab: The first targeted Alzheimer's therapy
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Treatment Guidelines for Alzheimer's Disease
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Establishing In-House Cutoffs of CSF Alzheimer’s Disease Biomarkers for the AT(N) Stratification of the Alzheimer Center Barcelona Cohort
Orellana, A., García‐González, P., Valero, S., Montrreal, L., de Rojas, I., Hernández, I., Rosende‐Roca, M., Vargas, L., Tartari, J. P., Antonio, E. E., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23136891 · Cited by 57 · see citing works
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How plausible is an Alzheimer’s disease vaccine?
Cacabelos, R. (2020) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2019.1667329 · Cited by 54 · cited 1× · see citing works
“Active vaccination is defined as introducing an exogenous substance to stimulate the immune system to mount a response (Figure 1) [88].”
Background
Immunotherapy for Alzheimer's Disease: Rational Basis in Ongoing Clinical Trials
Menéndez‐González, M., Pérez‐Piñera, P., Martínez-Rivera, M., Muñíz, A. L., & Vega, J. A. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211795164112 · Cited by 52 · see citing works
Cost-Effectiveness and Value-Based Pricing of Aducanumab for Patients With Early Alzheimer Disease
Whittington, M. D., Campbell, J. D., Rind, D. M., Fluetsch, N., Lin, G. A., & Pearson, S. D. (2022) · Neurology · doi:10.1212/wnl.0000000000013314 · Cited by 52 · see citing works
Brain Endothelial Cells Regulate Glucagon-Like Peptide 1 Entry Into the Brain via a Receptor-Mediated Process
Fu, Z., Gong, L., Liu, J., Wu, J., Barrett, E. J., Aylor, K. W., & Liu, Z. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00555 · Cited by 51 · see citing works
Lessons Learnt from the Second Generation of Anti-Amyloid Monoclonal Antibodies Clinical Trials
Kwan, A. T. H., Arfaie, S., Therriault, J., Rosa-Neto, P., & Gauthier, S. (2020) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000511506 · Cited by 51 · see citing works
APOE: The New Frontier in the Development of a Therapeutic Target towards Precision Medicine in Late-Onset Alzheimer’s
Yang, A., Kantor, B., & Chiba‐Falek, O. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22031244 · Cited by 50 · see citing works
Pharmacokinetics and pharmacodynamic effect of crenezumab on plasma and cerebrospinal fluid beta-amyloid in patients with mild-to-moderate Alzheimer’s disease
Yoshida, K. J., Moein, A., Bittner, T., Ostrowitzki, S., Lin, H. H., Honigberg, L. A., Jin, J. Y., & Quartino, A. L. (2020) · Alzheimer s Research & Therapy · doi:10.1186/s13195-020-0580-2 · Cited by 48 · see citing works
Cromolyn inhibits the secretion of inflammatory cytokines by human microglia (HMC3)
Wang, Y.-J., Monteagudo, A., Downey, M. A., Ashton‐Rickardt, P. G., & Elmaleh, D. R. (2021) · Scientific Reports · doi:10.1038/s41598-021-85702-8 · Cited by 47 · see citing works
Glucagon-like Peptide-1 (GLP-1) and Protective Effects in Cardiovascular Disease: A New Therapeutic Approach for Myocardial Protection
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Pericytes in Cerebrovascular Diseases: An Emerging Therapeutic Target
Su, X., Huang, L., Qu, Y., Xiao, D., & Mu, D. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00519 · Cited by 44 · see citing works
Pericytes: Problems and Promises for CNS Repair
Laredo, F., Plebanski, J., & Tedeschi, A. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00546 · Cited by 44 · cited 1× · see citing works
“In these disorders, pericyte malfunction often leads to BBB disruption and/or a decrease of CBF, thus causing secondary neurological damage [180].”
Background
Identification of Novel Alzheimer’s Disease Loci Using Sex-Specific Family-Based Association Analysis of Whole-Genome Sequence Data
Prokopenko, D., Hecker, J., Kirchner, R. D., Chapman, B., Hofmann, O., Mullin, K., Hide, W., Bertram, L., Laird, N. M., DeMeo, D. L., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-61883-6 · Cited by 43 · see citing works
The structure and phase of tau: from monomer to amyloid filament
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[155]Renee M. Elmore P. Najafi A.R. Koike M.A. Nazih N. Spangenberg E.E. Rice R.A. Kitazawa M. Nguyen H. West B.L. CSF1 receptor signaling is necessary for microglia viability, which unmasks a cell that rapidly repopulates the microglia-depleted adult brain Neuron 2015 82 380 397 10.1016/j.neuron.2014.02.040.CSF1 PMC4161285 24742461 · DOI

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Recent advances in Alzheimer's disease: Mechanisms, clinical trials and new drug development strategies.
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Basic information about memantine and its treatment of Alzheimer's disease and other clinical applications
Tang, B., Wang, Y., & Ren, J. (2023) · Ibrain · doi:10.1002/ibra.12098 · Cited by 114 · see citing works
Proteostasis and neurodegeneration: a closer look at autophagy in Alzheimer's disease
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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
“DMTs are intended to delay the progression of long-term conditions such as AD and ultimately improve the patient’s quality of life [60].”
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Harnessing microalgae as sustainable cellular factories for biopharmaceutical production
Goshtasbi, H., Okolodkov, Y. B., Movafeghi, A., Awale, S., Safary, A., Barar, J., & Omidi, Y. (2023) · Algal Research · doi:10.1016/j.algal.2023.103237 · Cited by 44 · see citing works
Therapeutics of Alzheimer’s Disease: Recent Developments
Burns, S., Selman, A., Sehar, U., Rawat, P., Reddy, A. P., & Reddy, P. H. (2022) · Antioxidants · doi:10.3390/antiox11122402 · Cited by 31 · see citing works
Ellagic Acid: A Green Multi-Target Weapon That Reduces Oxidative Stress and Inflammation to Prevent and Improve the Condition of Alzheimer’s Disease
Alfei, S., & Zuccari, G. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26020844 · Cited by 28 · see citing works
Calcium (Ca2+) hemostasis, mitochondria, autophagy, and mitophagy contribute to Alzheimer's disease as early moderators
Hadi, F., Mortaja, M., & Hadi, Z. (2024) · Cell Biochemistry and Function · doi:10.1002/cbf.4085 · Cited by 23 · see citing works
Pharmacodynamic and Clinical Effects of Ginkgo Biloba Extract EGb 761 and Its Phytochemical Components in Alzheimer’s Disease
Morató, X., Tartari, J. P., Pytel, V., & Boada, M. (2024) · Journal of Alzheimer s Disease · doi:10.3233/jad-231372 · Cited by 23 · see citing works
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Alzheimer's Disease and Frontotemporal Dementia: A Review of Pathophysiology and Therapeutic Approaches
Kelliny, S., Zhou, X., & Bobrovskaya, L. (2025) · Journal of Neuroscience Research · doi:10.1002/jnr.70046 · Cited by 25 · see citing works
The role of probiotics, prebiotics, and postbiotics: cellular and molecular pathways activated on glial cells in Alzheimer’s disease
Patricio-Martínez, A., Patricio, F., Macuil-Chapuli, E., Martínez-Juárez, E. Á., Flores-Díaz, S., Cedillo-Ramirez, M. L., & Limón, I. D. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1598011 · Cited by 22 · see citing works
Bibliometric analysis of research on Alzheimer’s disease and non-coding RNAs: Opportunities and challenges
Fei, X., Wang, S., Li, J., Zeng, Q., Gao, Y., & Hu, Y. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1037068 · Cited by 16 · see citing works
Surface-functionalized nanoparticles for targeted drug delivery across the blood-brain barrier: advances and challenges in neurodegenerative disease therapy
Pramoda, G., Verma, R. K., Kesharwani, P., & Shukla, R. (2025) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2025.127938 · Cited by 15 · see citing works
Role of mitogen-activated protein kinase inhibitors in Alzheimer's disease: Rouge of brain kinases
Almasoudi, S. H., Al-Kuraishy, H. M., Al-Gareeb, A. I., Eliwa, D., Alexiou, A. T., Papadakis, M., & Batiha, G. E. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111296 · Cited by 14 · see citing works
A meta-analysis update evaluating the treatment effects of donepezil alone versus donepezil combined with memantine for Alzheimer's disease
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Human serum albumin-3-amino-1-propanesulfonic acid conjugate inhibits amyloid-β aggregation and mitigates cognitive decline in Alzheimer's disease
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A Model Predicting Healthcare Capacity Gaps For Alzheimer’s Disease-Modifying Treatment in Canada
Black, S. E., Budd, N., Nygaard, H. B., Verret, L., Virdi, S., Watts, L. T., & Wilson, M. (2023) · Canadian Journal of Neurological Sciences / Journal Canadien des Sciences Neurologiques · doi:10.1017/cjn.2023.270 · Cited by 11 · see citing works
Advances in Understanding and Managing Alzheimer's Disease: From Pathophysiology to Innovative Therapeutic Strategies
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Toward a new nosology of neurodegenerative diseases
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Advancing Early Detection of Alzheimer Disease in the Primary Care Setting in the United States
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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: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Health Sciences › Medicine › Pharmacology › 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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