The Amyloid Cascade Hypothesis in Alzheimer’s Disease: It’s Time to Change Our Mind

Neuropathological stageing of Alzheimer-related changes.

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Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

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Alzheimer's disease: the amyloid cascade hypothesis

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Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

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Diffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins

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The antibody aducanumab reduces Aβ plaques in Alzheimer’s disease

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Neurotrophic and Neurotoxic Effects of Amyloid β Protein: Reversal by Tachykinin Neuropeptides

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Recent Progress of Nanomedicine in the Treatment of Central Nervous System Diseases

Feng, L., Wang, H., & Xue, X. (2020) · Advanced Therapeutics · doi:10.1002/adtp.201900159 · Cited by 33

TRA2A-induced upregulation of LINC00662 regulates blood-brain barrier permeability by affecting ELK4 mRNA stability in Alzheimer’s microenvironment

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Plasma Amyloid-β in Relation to Cardiac Function and Risk of Heart Failure in General Population

Zhu, F., Wolters, F. J., Yaqub, A., Leening, M. J. G., Ghanbari, M., Boersma, E. H., Ikram, M. A., & Kavousi, M. (2022) · JACC Heart Failure · doi:10.1016/j.jchf.2022.09.006 · Cited by 33

Mitochondrial Complex I and β-Amyloid Peptide Interplay in Alzheimer’s Disease: A Critical Review of New and Old Little Regarded Findings

Atlante, A., & Valenti, D. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242115951 · Cited by 33

Periodontitis and systemic markers of neurodegeneration: A case–control study

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Mining on Alzheimer’s diseases related knowledge graph to identity potential AD-related semantic triples for drug repurposing

Nian, Y., Hu, X., Zhang, R., Feng, J., Du, J., Li, F., Bu, L., Zhang, Y., Chen, Y., & Tao, C. (2022) · BMC Bioinformatics · doi:10.1186/s12859-022-04934-1 · Cited by 36

Emerging Approaches to Investigate the Influence of Transition Metals in the Proteinopathies

Lermyte, F., Everett, J. L., Brooks, J., Bellingeri, F., Billimoria, K., Sadler, P. J., O’Connor, P. B., Telling, N. D., & Collingwood, J. F. (2019) · Cells · doi:10.3390/cells8101231 · Cited by 31

Enzyme-digested Colla Corii Asini (E’jiao) prevents hydrogen peroxide-induced cell death and accelerates amyloid beta clearance in neuronal-like PC12 cells

Xiao, L., Liao, F., Ide, R., Horie, T., Fan, Y., Saiki, C., & Miwa, N. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.285000 · Cited by 31

G protein‐coupled receptor kinases are associated with Alzheimer's disease pathology

Guimarães, T. R., Swanson, E., Kofler, J., & Thathiah, A. (2021) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12742 · Cited by 31

A potential biomarker of preclinical Alzheimer’s disease: The olfactory dysfunction and its pathogenesis-based neural circuitry impairments

Yan, Y., Aierken, A., Wang, C., Song, D. F., Ni, J., Wang, Z., Quan, Z., & Qing, H. (2021) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2021.11.009 · Cited by 32

Disrupting Neurons and Glial Cells Oneness in the Brain—The Possible Causal Role of Herpes Simplex Virus Type 1 (HSV-1) in Alzheimer’s Disease

Mielcarska, M. B., Skowrońska, K., Wyżewski, Z., & Toka, F. N. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms23010242 · Cited by 32

Deciphering the Link Between Hyperhomocysteinemia and Ceramide Metabolism in Alzheimer-Type Neurodegeneration

Stunff, H. L., Véret, J., Kassis, N., Denom, J., Meneyrol, K., Paul, J., Cruciani‐Guglielmacci, C., Magnan, C., & Janel, N. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.00807 · Cited by 31

The Multifaceted Role of Neuroprotective Plants in Alzheimer’s Disease Treatment

Zieneldien, T., Kim, J., & Cao, C. (2022) · Geriatrics · doi:10.3390/geriatrics7020024 · Cited by 29

Autophagy Modulation in Aggresome Formation: Emerging Implications and Treatments of Alzheimer’s Disease

Rahman, M. A., Rahman, M. H., Mamun-Or-Rashid, A. N. M., Hwang, H., Chung, S., Kim, B., & Rhim, H. (2022) · Biomedicines · doi:10.3390/biomedicines10051027 · Cited by 31

The Interplay between cGMP and Calcium Signaling in Alzheimer’s Disease

Jehle, A., & Garaschuk, O. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23137048 · Cited by 31

Alzheimer disease: Amyloid peptide controversies and challenges of anti-Aβ immunotherapy

Almohmadi, N. H., Al-Kuraishy, H. M., Albuhadily, A. K., Al-Gareeb, A. I., Abdelaziz, A. M., Alexiou, A. T., Papadakis, M., & Batiha, G. E. (2025) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1016/j.jpet.2025.103639 · Cited by 29

Computational Modeling of Catecholamines Dysfunction in Alzheimer’s Disease at Pre-Plaque Stage

Caligiore, D., Silvetti, M., D’Amelio, M., Puglisi‐Allegra, S., & Baldassarre, G. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200276 · Cited by 30

Amyloid, tau and risk of Alzheimer’s disease: a Mendelian randomization study

Yeung, C. H. C., Lau, K. W. D., Yeung, S. L. A., & Schooling, C. M. (2020) · European Journal of Epidemiology · doi:10.1007/s10654-020-00683-8 · Cited by 28

Dysregulated Ca2+ Homeostasis as a Central Theme in Neurodegeneration: Lessons from Alzheimer’s Disease and Wolfram Syndrome

Callens, M., Loncke, J., & Bultynck, G. (2022) · Cells · doi:10.3390/cells11121963 · Cited by 30

A proteomics analysis of 5xFAD mouse brain regions reveals the lysosome-associated protein Arl8b as a candidate biomarker for Alzheimer’s disease

Boeddrich, A., Haenig, C., Neuendorf, N., Blanc, E., Ivanov, A., Kirchner, M., Schleumann, P., Bayraktaroğlu, I., Richter, M., Molenda, C., et al. (2023) · Genome Medicine · doi:10.1186/s13073-023-01206-2 · Cited by 30

Exogenous 3-Iodothyronamine Rescues the Entorhinal Cortex from β-Amyloid Toxicity

Accorroni, A., Rutigliano, G., Sabatini, M., Frascarelli, S., Borsò, M., Novelli, E., Bandini, L., Ghelardoni, S., Saba, A., Zucchi, R., et al. (2019) · Thyroid · doi:10.1089/thy.2019.0255 · Cited by 28

Targeting Impaired Antimicrobial Immunity in the Brain for the Treatment of Alzheimer’s Disease

Fülöp, T., Tripathi, S., Rodrigues, S., Desroches, M., Bunt, T., Eiser, A. R., Bernier, F., Beauregard, P. B., Barron, A. E., Khalil, A., et al. (2021) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s264910 · Cited by 27

An insight into prodrug strategy for the treatment of Alzheimer’s disease

Bhilare, N. V., Marulkar, V. S., Kumar, D., Chatap, V. K., Patil, K. S., & Shirote, P. J. (2022) · Medicinal Chemistry Research · doi:10.1007/s00044-022-02859-1 · Cited by 27

All roads lead to heterogeneity: The complex involvement of astrocytes and microglia in the pathogenesis of Alzheimer’s disease

St‐Pierre, M., VanderZwaag, J., Loewen, S. M., & Tremblay, M. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.932572 · Cited by 27

Single-cell and spatial transcriptomics reveals that PTPRG activates the m6A methyltransferase VIRMA to block mitophagy-mediated neuronal death in Alzheimer’s disease

Zou, D., Huang, X., Lan, Y., Pan, M., Xie, J., Huang, Q., Zeng, J., Zou, C., Pei, Z., Zou, C., et al. (2024) · Pharmacological Research · doi:10.1016/j.phrs.2024.107098 · Cited by 28

Emerging Developments in Targeting Proteotoxicity in Neurodegenerative Diseases

McAlary, L., Plotkin, S. S., & Cashman, N. R. (2019) · CNS Drugs · doi:10.1007/s40263-019-00657-9 · Cited by 26

Neuropathology of Aging in Cats and its Similarities to Human Alzheimer’s Disease

Sordo, L., Martini, A. C., Houston, E. F., Head, E., & Gunn-Moore, D. A. (2021) · Frontiers in Aging · doi:10.3389/fragi.2021.684607 · Cited by 26

Emerging therapeutics agents and recent advances in drug repurposing for Alzheimer’s disease

Neha, N., & Parvez, S. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101815 · Cited by 28

Naphthalene-triazolopyrimidine hybrid compounds as potential multifunctional anti-Alzheimer’s agents

Umar, T., Gusain, S., Raza, M. K., Shalini, S., Kumar, J., Tiwari, M., & Hoda, N. (2019) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2019.06.004 · Cited by 26

Multifunctional indanone–chalcone hybrid compounds with anti-β-amyloid (Aβ) aggregation, monoamine oxidase B (MAO-B) inhibition and neuroprotective properties against Alzheimer’s disease

Wang, K., Yu, L., Shi, J., Liu, W., & Sang, Z. (2019) · Medicinal Chemistry Research · doi:10.1007/s00044-019-02423-4 · Cited by 26

Silk fibroin safety in the eye: a review that highlights a concern

Madden, P. W., Klyubin, I. V., & Ahearne, M. (2020) · BMJ Open Ophthalmology · doi:10.1136/bmjophth-2020-000510 · Cited by 27

Challenges of Integrative Disease Modeling in Alzheimer's Disease

Khatami, S. G., Robinson, C., Birkenbihl, C., Domingo‐Fernándéz, D., Hoyt, C. T., & Hofmann‐Apitius, M. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2019.00158 · Cited by 28

Neurogenesis Makes a Crucial Contribution to the Neuropathology of Alzheimer’s Disease

Young, J. K. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-200218 · Cited by 28

Association of CD2AP neuronal deposits with Braak neurofibrillary stage in Alzheimer’s disease

Camacho, J., Rábano, A., Marazuela, P., Bonaterra‐Pastra, A., Serna, G., Moliné, T., y Cajal, S. R., Martínez-Sáez, E. A., & Hernández‐Guillamón, M. (2021) · Brain Pathology · doi:10.1111/bpa.13016 · Cited by 25

A literature review of MRI techniques used to detect amyloid-beta plaques in Alzheimer’s disease patients

Yu, B., Shan, Y., & Ding, J. (2021) · Annals of Palliative Medicine · doi:10.21037/apm-21-825 · Cited by 26

Microfluidic Platforms to Unravel Mysteries of Alzheimer’s Disease: How Far Have We Come?

Prasanna, P., Rathee, S., Rahul, V., Mandal, D., Goud, M. S. C., Yadav, P., Hawthorne, S. J., Sharma, A., Gupta, P. K., Ojha, S. K., et al. (2021) · Life · doi:10.3390/life11101022 · Cited by 25

Amyloid and Tau in Alzheimer’s Disease: Biomarkers or Molecular Targets for Therapy? Are We Shooting the Messenger?

Kumar, A., Nemeroff, C. B., Cooper, J. J., Widge, A. S., Rodríguez, C. I., Carpenter, L. L., & McDonald, W. M. (2021) · American Journal of Psychiatry · doi:10.1176/appi.ajp.2021.19080873 · Cited by 25

History in Perspective: The prime pathological players and role of phytochemicals in Alzheimer’s disease

Sajad, M., Kumar, R., & Thakur, S. C. (2022) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2022.04.009 · Cited by 25

The separation distress hypothesis of depression – an update and systematic review

Watt, D. F. (2023) · Neuropsychoanalysis · doi:10.1080/15294145.2023.2240340 · Cited by 25

The Neuroprotective Effects of SIRT1 in Mice Carrying the APP/PS1 Double-Transgenic Mutation and in SH-SY5Y Cells Over-Expressing Human APP670/671 May Involve Elevated Levels of α7 Nicotinic Acetylcholine Receptors

Cao, K., Dong, Y., Xiang, J., Xu, Y., Li, Y., Song, H., Yu, W., Qi, X., & Guan, Z.-Z. (2019) · Aging · doi:10.18632/aging.102713 · Cited by 26

Mini Review: Opposing Pathologies in Cancer and Alzheimer's Disease: Does the PI3K/Akt Pathway Provide Clues?

Barker, R. M., Holly, J. M. P., Biernacka, K. M., Allen, S. J., & Perks, C. M. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.00403 · Cited by 25

Alzheimer’s Disease, and Breast and Prostate Cancer Research: Translational Failures and the Importance to Monitor Outputs and Impact of Funded Research

Pistollato, F., Bernasconi, C., McCarthy, J., Campia, I., Desaintes, C., Wittwehr, C., Deceuninck, P., & Whelan, M. (2020) · Animals · doi:10.3390/ani10071194 · Cited by 25

Molecular Signatures of Neurodegenerative Diseases Identified by Proteomic and Phosphoproteomic Analyses in Aging Mouse Brain

Mohallem, R., Schaser, A. J., & Aryal, U. K. (2024) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2024.100819 · Cited by 23

Non-canonical pathways associated to Amyloid beta and tau protein dyshomeostasis in Alzheimer’s disease: A narrative review

Maggiore, A., Latina, V., D’Erme, M., Amadoro, G., & Coccurello, R. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102578 · Cited by 25

Dysmetabolism and Neurodegeneration: Trick or Treat?

Capucho, A. M., Chegão, A., Martins, F. O., Miranda, H. V., & Conde, S. V. (2022) · Nutrients · doi:10.3390/nu14071425 · Cited by 26

Therapeutic nanotechnologies for Alzheimer’s disease: A critical analysis of recent trends and findings

Delbreil, P., Rabanel, J., Banquy, X., & Brambilla, D. (2022) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2022.114397 · Cited by 25

Fluorescence Phenomena in Amyloid and Amyloidogenic Bionanostructures

Apter, B., Lapshina, N., Barhum, H., Fainberg, B. D., Handelman, A., Accardo, A., Diaferia, C., Ginzburg, P., Morelli, G., & Rosenman, G. I. (2020) · Crystals · doi:10.3390/cryst10080668 · Cited by 24

EEG and ERP biosignatures of mild cognitive impairment for longitudinal monitoring of early cognitive decline in Alzheimer’s disease

Meghdadi, A. H., Salat, D. H., Hamilton, J. M., Hong, Y., Boeve, B. F., Louis, E. K. S., Verma, A. K., & Berka, C. (2024) · PLoS ONE · doi:10.1371/journal.pone.0308137 · Cited by 23

A Perspective on Roles Played by Immunosenescence in the Pathobiology of Alzheimer's Disease

Zhao, Y. G., Zhan, J., & Liu, Y. (2020) · Aging and Disease · doi:10.14336/ad.2020.0205 · Cited by 23

Recent trends in artificial intelligence-driven identification and development of anti-neurodegenerative therapeutic agents

Kashyap, K., & Siddiqi, M. I. (2021) · Molecular Diversity · doi:10.1007/s11030-021-10274-8 · Cited by 24

Knowledge graph embeddings in the biomedical domain: are they useful? A look at link prediction, rule learning, and downstream polypharmacy tasks

Gema, A. P., Grabarczyk, D., Wulf, W. D., Borole, P., Alfaro, J. A., Minervini, P., Vergari, A., & Rajan, A. (2024) · Bioinformatics Advances · doi:10.1093/bioadv/vbae097 · Cited by 31

An insight into the concept of neuroinflammation and neurodegeneration in Alzheimer’s disease: targeting molecular approach Nrf2, NF-κB, and CREB

Bhardwaj, S., Grewal, A. K., Singh, S., Dhankar, V., & Jindal, A. (2024) · Inflammopharmacology · doi:10.1007/s10787-024-01502-2 · Cited by 25

BACE-1 Inhibitors Targeting Alzheimer's Disease

Monteiro, K. L. C., Alcântara, M. G. D. S., Freire, N. M. L., Brandão, E. M., do Nascimento, V. L., Viana, L. M. D. S., de Aquino, T. M., & da Silva‐Júnior, E. F. (2023) · Current Alzheimer Research · doi:10.2174/1567205020666230612155953 · Cited by 23

Cerebrospinal fluid microRNAs as potential biomarkers in Alzheimer’s disease

Eddin, A. N., Hamsho, K., Adi, G., Al-Rimawi, M., Alfuwais, M., Rab, S. A., AlKattan, K. M., & Yaqinuddin, A. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1210191 · Cited by 26

The role of A$$\beta $$ and Tau proteins in Alzheimer’s disease: a mathematical model on graphs

Bertsch, M., Franchi, B., Tesi, M. C., & Tora, V. (2023) · Journal of Mathematical Biology · doi:10.1007/s00285-023-01985-7 · Cited by 25

Serotonin Receptors as a Potential Target in the Treatment of Alzheimer’s Disease

Eremin, D. V., Kondaurova, E. M., Rodnyy, A. Y., Molobekova, C. A., Kudlay, D. A., & Naumenko, V. S. (2023) · Biochemistry (Moscow) · doi:10.1134/s0006297923120064 · Cited by 23

Mechanisms, functions and therapeutic targeting of protein tyrosine phosphatases

Tiganis, T., & Tonks, N. K. (2025) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-025-00882-9 · Cited by 25

Cyanobiphenyls: Novel H3 receptor ligands with cholinesterase and MAO B inhibitory activity as multitarget compounds for potential treatment of Alzheimer’s disease

Godyń, J., Zaręba, P., Łażewska, D., Stary, D., Reiner‐Link, D., Frank, A., Latacz, G., Mogilski, S., Kaleta, M., Doroż-Płonka, A., et al. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.105129 · Cited by 21

Mechanistic Insights into the Neuroprotective Potential of Sacred Ficus Trees

Shim, K. H., Sharma, N., & An, S. S. A. (2022) · Nutrients · doi:10.3390/nu14224731 · Cited by 26

Linking cognition to age and amyloid-β burden in the brain of a nonhuman primate (Microcebus murinus)

Schmidtke, D., Zimmermann, E., Trouche, S. G., Fontès, P., Verdier, J., & Mestre‐Francés, N. (2020) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2020.03.025 · Cited by 21

Acute and chronic excitotoxicity in ischemic stroke and late-onset Alzheimer’s disease

Yu, S. P., Choi, E., Jiang, M. Q., & Wei, L. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00398 · Cited by 21

Prostaglandins in the Inflamed Central Nervous System: Potential Therapeutic Targets

Noakes, P., Sheremeta, C.-L., Yarlagadda, S., & Smythe, M. L. (2024) · Current Drug Targets · doi:10.2174/0113894501323980240815113851 · Cited by 20

Inhibition of Astrocytic Histamine N-Methyltransferase as a Possible Target for the Treatment of Alzheimer’s Disease

Flores‐Clemente, C., Nicolás‐Vázquez, M. I., Jiménez, E. M., & Rodríguez, M. H. (2021) · Biomolecules · doi:10.3390/biom11101408 · Cited by 21

Amyloid-β: A potential mediator of aging-related vascular pathologies

Khan, F., & Qiu, H. (2023) · Vascular Pharmacology · doi:10.1016/j.vph.2023.107213 · Cited by 22

Implication of the cooking oil-peroxidation product “hydroxynonenal” for Alzheimer’s disease

Yamashima, T., Seike, T., Mochly‐Rosen, D., Chen, C., Kikuchi, M., & Mizukoshi, E. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1211141 · Cited by 20

Disease-directed engineering for physiology-driven treatment interventions in neurological disorders

Wood, T. R., & Nance, E. A. (2019) · APL Bioengineering · doi:10.1063/1.5117299 · Cited by 21

Fluorinated Molecules and Nanotechnology: Future ‘Avengers’ against the Alzheimer’s Disease?

Dabur, M., Loureiro, J. A., & Pereira, M. D. C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21082989 · Cited by 20

Diagnostic journey and management of patients with mild cognitive impairment and Alzheimer's disease dementia: A multinational, real-world survey

Vasileva-Metodiev, S. Z., Spargo, D. J., Klein, E., Quevenco, F., Cotton, S. E., Sánchez‐Juan, P., Niimi, Y., & Fowler, N. R. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251322978 · Cited by 20

Hypertension & dementia: Pathophysiology & potential utility of antihypertensives in reducing disease burden

Lyon, M., Fullerton, J. L., Kennedy, S., & Work, L. M. (2023) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2023.108575 · Cited by 22

Inflammasome links traumatic brain injury, chronic traumatic encephalopathy, and Alzheimer’s disease

Seplovich, G., Bouchi, Y., Vaccari, J. P. D. R., Pareja, J. C. M., Reisner, A., Blackwell, L. S., Mechref, Y. S., Wang, K., Tyndall, J. A., Tharakan, B., et al. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00107 · Cited by 21

Icariin improves learning and memory function in Aβ1-42-induced AD mice through regulation of the BDNF-TrκB signaling pathway

Wan, M., Sun, S., Di, X., Zhao, M., Lu, F., Zhang, Z., & Li, Y. (2023) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2023.117029 · Cited by 18

An inorganic overview of natural Aβ fragments: Copper(II) and zinc(II)-mediated pathways

Lanza, V., Bellia, F., & Rizzarelli, E. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.04.004 · Cited by 18

Lessons on Differential Neuronal-Death-Vulnerability from Familial Cases of Parkinson’s and Alzheimer’s Diseases

Franco, R., Navarro, G., & Martínez‐Pinilla, E. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20133297 · Cited by 17

Physiological and Pathological Functions of Beta-Amyloid in the Brain and Alzheimer'S Disease

Volicer, L. (2020) · The Chinese Journal of Physiology · doi:10.4103/cjp.cjp_10_20 · Cited by 18

Time-Dependent Lipid Dynamics, Organization and Peptide-Lipid Interaction in Phospholipid Bilayers with Incorporated β‑Amyloid Oligomers

Qiang, W., Doherty, K. E., Klees, L. M., & Tobin-Miyaji, Y. J. (2020) · The Journal of Physical Chemistry Letters · doi:10.1021/acs.jpclett.0c01967 · Cited by 18

Catalytic Cross Talk between Key Peptide Fragments That Couple Alzheimer’s Disease with Amyotrophic Lateral Sclerosis

Laos, V., Bishop, D., Ganguly, P., Schonfeld, G. E., Trapp, E., Cantrell, K. L., Buratto, S. K., Shea, J., & Bowers, M. T. (2021) · Journal of the American Chemical Society · doi:10.1021/jacs.0c12729 · Cited by 19

Toxic SOD1 trimers are off-pathway in the formation of amyloid-like fibrils in ALS

Hnath, B., & Dokholyan, N. V. (2022) · Biophysical Journal · doi:10.1016/j.bpj.2022.04.037 · Cited by 18

Prostaglandin EP2 receptor antagonist ameliorates neuroinflammation in a two-hit mouse model of Alzheimer’s disease

Banik, A., Amaradhi, R., Lee, D. D., Sau, M., Wang, W., Dingledine, R. J., & Ganesh, T. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02297-7 · Cited by 18

Pyridazinones containing the (4-methoxyphenyl)piperazine moiety as AChE/BChE inhibitors: design, synthesis, in silico and biological evaluation

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From Hybrids to New Scaffolds: The Latest Medicinal Chemistry Goals in Multi-target Directed Ligands for Alzheimers Disease

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