Alzheimer’s Disease: The Challenge of the Second Century

The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics

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A default mode of brain function

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Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359

The Clinical Dementia Rating (CDR): Current version and scoring rules

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Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families

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Finding the missing heritability of complex diseases

Manolio, T. A., Collins, F. S., Cox, N. J., Goldstein, D. B., Hindorff, L. A., Hunter, D. J., McCarthy, M. I., Ramos, E. M., Cardon, L. R., Chakravarti, A., et al. (2009) · Nature · doi:10.1038/nature08494 · Cited by 8,336

Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein

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Hypothetical model of dynamic biomarkers of the Alzheimer's pathological cascade

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Molecular Links Between Alzheimer's Disease and Gastrointestinal Microbiota: Emphasis on Helicobacter pylori Infection Involvement

Katsinelos, P., Doulberis, M., Pοlyzos, S. A., Papaefthymiou, A., Katsinelos, P., & Kountouras, J. (2019) · Current Molecular Medicine · doi:10.2174/1566524019666190917125917 · Cited by 13

Orexin-A aggravates cytotoxicity and mitochondrial impairment in SH-SY5Y cells transfected with APPswe via p38 MAPK pathway

Li, M., Meng, Y., Chu, B., Shen, Y., Liu, X., Ding, M., Song, C., Cao, X., Wang, P., Xu, L., et al. (2020) · Annals of Translational Medicine · doi:10.21037/atm.2019.11.68 · Cited by 13

Structural and functional characterization of H2 haplotype MAPT promoter: Unique neurospecific domains and a hypoxia-inducible element would enhance rationally targeted tauopathy research for Alzheimer's disease

Maloney, B., & Lahiri, D. K. (2012) · Gene · doi:10.1016/j.gene.2012.01.049 · Cited by 13

Increased Insoluble Amyloid-β Induces Negligible Cognitive Deficits in Old AppNL/NL Knock-In Mice

Salas, I. H., Callaerts-Vegh, Z., D’Hooge, R., Saido, T. C., Dotti, C. G., & De Strooper, B. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-180410 · Cited by 12

The Role of RIN3 Gene in Alzheimer’s Disease Pathogenesis: a Comprehensive Review

Meshref, M. M., Ghaith, H. S., Hammad, M. A., Shalaby, M. M. M., Ayasra, F., Monib, F. A., Attia, M. S., Ebada, M. A., Elsayed, H., Shalash, A., et al. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03802-0 · Cited by 12

Rationally Designed Cu(I) Ligand to Prevent CuAβ-Generated ROS Production in the Alzheimer’s Disease Context

Rulmont, C., Stigliani, J., Hureau, C., & Esmieu, C. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.3c02693 · Cited by 12

Validation of an Ultra-Sensitive Method for Quantitation of Phospho-Tau 217 (pTau217) in Human Plasma, Serum, and CSF using the ALZpath pTau217 Assay on the Quanterix HD-X Platform

Zhang, H., Liu, J., Zhang, N., Jeromin, A., & Lin, Z. J. (2024) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2024.155 · Cited by 12

Will PET Amyloid Imaging Lead to Overdiagnosis of Alzheimer Dementia?

Dubroff, J. G., & Nasrallah, I. M. (2015) · Academic Radiology · doi:10.1016/j.acra.2015.02.005 · Cited by 12

Inhibition of mTORC1 improves STZ-induced AD-like impairments in mice

Cao, Y., Liu, B., Xu, W., Wang, L., Shi, F.-X., Li, N., Lei, Y., Wang, J., Tian, Q., & Zhou, X. (2020) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2020.06.002 · Cited by 12

Determination of plasma β-amyloids by rolling circle amplification chemiluminescent immunoassay for noninvasive diagnosis of Alzheimer’s disease

Wang, D., Dai, Y., Wang, X., Pan, Y., Qu, S., Liu, Z., Cao, Y., Zhang, L., Ying, P., Liu, W., et al. (2021) · Microchimica Acta · doi:10.1007/s00604-020-04650-8 · Cited by 12

Undetected Neurodegenerative Disease Biases Estimates of Cognitive Change in Older Adults

Harrington, K., Aschenbrenner, A. J., Maruff, P. T., Masters, C. L., Fagan, A. M., Benzinger, T. L. S., Gordon, B. A., Cruchaga, C., Morris, J. C., & Hassenstab, J. J. (2021) · Psychological Science · doi:10.1177/0956797620985518 · Cited by 12

Effects of Acute Sepsis on Cellular Dynamics and Amyloid Formation in a Mouse Model of Alzheimer’s Disease

Rotaru-Zăvăleanu, A. D., Neacșu, A. I., Neacsu, A., Pirici, D. N., Osiac, E., Cătălin, B., & Gheonea, D. I. (2022) · Current Issues in Molecular Biology · doi:10.3390/cimb44090262 · Cited by 12

Exploring the Genetic Predisposition to Epigenetic Changes in Alzheimer’s Disease

Bryzgalov, L. O., Korbolina, E. E., & Merkulova, T. I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24097955 · Cited by 12

Uncovering neuroinflammation-related modules and potential repurposing drugs for Alzheimer's disease through multi-omics data integrative analysis

Li, S., Lu, C., Zhao, Z., Lu, D., & Zheng, G. (2023) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2023.1161405 · Cited by 12

The role of N-methyl-D-aspartate receptor in Alzheimer's disease

Zhang, J., Li, Y., Xu, J., & Zhou, Y. (2014) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2014.01.041 · Cited by 12

APOE ε4genotype predicts memory for everyday activities

Bailey, H. R., Sargent, J. Q., Flores, S. E., Nowotny, P., Goate, A., & Zacks, J. M. (2015) · Aging Neuropsychology and Cognition · doi:10.1080/13825585.2015.1020916 · Cited by 12

Copper ligation to soluble oligomers of the English mutant of the amyloid-β peptide yields a linear Cu(i) site that is resistant to O2 oxidation

Peck, K. L., Clewett, H. S., Schmitt, J. C., & Shearer, J. (2013) · Chemical Communications · doi:10.1039/c3cc40326b · Cited by 12

Neuroinflammation and Alzheimer’s disease: lessons learned from 5-lipoxygenase

Joshi, Y. B., & Praticò, D. (2014) · Translational Neuroscience · doi:10.2478/s13380-014-0225-7 · Cited by 12

Allosteric Modulators of Potential Targets Related to Alzheimer's Disease: a Review

Silva, G. M., Barcelos, M. P., Poiani, J. G. C., Hage-Melim, L. I. D. S., & da Silva, C. H. T. D. P. (2019) · ChemMedChem · doi:10.1002/cmdc.201900299 · Cited by 12

Phenothiazine-based theranostic compounds for in vivo near-infared fluorescence imaging of β-amyloid plaques and inhibition of Aβ aggregation

Li, Y., Cai, J., Yan, L., Zhang, W., Li, L., Du, Z., Fang, Y., Dong, C., Meunier, B., & Chen, H. (2019) · Dyes and Pigments · doi:10.1016/j.dyepig.2019.107744 · Cited by 12

The combined risk effect among BIN1, CLU, and APOE genes in Alzheimer’s disease

dos Santos, L. R., Almeida, J. F. F., Pimassoni, L. H. S., Morelato, R. L., & Paula, F. (2019) · Genetics and Molecular Biology · doi:10.1590/1678-4685-gmb-2018-0320 · Cited by 12

Exploration of the Potential Role for Aβ in Delivery of Extracellular Copper to Ctr1

Stefaniak, E., Pushie, M. J., Vaerewyck, C., Corcelli, D., Griggs, C., Lewis, W. C., Kelley, E., Maloney, N., Sendzik, M. R., Bal, W., et al. (2020) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.0c02100 · Cited by 12

Interventions to Improve the Oral Hygiene of Individuals with Alzheimer’s Disease: A Systematic Review

Hernández‐Vásquez, A., Barrenechea-Pulache, A., Aguirre-Ipenza, R., Comandé, D., & Azañedo, D. (2022) · Dentistry Journal · doi:10.3390/dj10050092 · Cited by 12

S100B chaperone multimers suppress the formation of oligomers during Aβ42 aggregation

Figueira, A. J., Saavedra, J., Cardoso, I., & Gomes, C. M. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1162741 · Cited by 12

Recent Developments in Diffusion Tensor Imaging of Brain

Parekh, M. B., Gurjarpadhye, A. A., Manoukian, M. A. C., Dubņika, A., Rajadas, J., & Inayathullah, M. (2016) · Radiology - Open Journal · doi:10.17140/roj-1-101 · Cited by 12

Pyrazinyl ureas revisited: 1-(3-(Benzyloxy)pyrazin-2-yl)-3-(3,4-dichlorophenyl)urea, a new blocker of Aβ-induced mPTP opening for Alzheimer's disease

Elkamhawy, A., Park, J.-E., Hassan, A. H. E., Pae, A. N., Lee, J., Paik, S., Park, B.-G., & Roh, E. J. (2018) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2018.07.068 · Cited by 12

Fighting the Cause of Alzheimer’s and GNE Myopathy

Devi, S., Yadav, R., Chanana, P., & Arya, R. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00669 · Cited by 12

Aβ, tau, α-synuclein, huntingtin, TDP-43, PrP and AA are members of the innate immune system: a unifying hypothesis on the etiology of AD, PD, HD, ALS, CJD and RSA as innate immunity disordersPreprint

BANDEA, C. I. (2013) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/000604 · Cited by 12

Unraveling the mystery of citrate transporters in Alzheimer’s disease: An updated review

Mukherjee, A. G., Mishra, S., Gopalakrishnan, A. V., Kannampuzha, S., Murali, R., Wanjari, U. R., Stany, B. K., Vellingiri, B., Madhyastha, H., Deepankumar, K., et al. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102726 · Cited by 11

A Novel Aβ B-cell epitope Vaccine, Aβ1-10 with carrier protein OVA and KLH reduce Aβ-induced neuroinflammation mediated neuropathology in mouse model of Alzheimer’s disease

Park, J. S., Choe, K., Ahmad, R., Park, H. Y., Kang, M. H., Park, T. J., & Kim, M. O. (2025) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2025.06.001 · Cited by 11

15 years of longitudinal genetic, clinical, cognitive, imaging, and biochemical measures in DIAN

Daniels, A. J., McDade, E., Llibre‐Guerra, J. J., Xiong, C., Perrin, R. J., Ibáñez, L., Supnet‐Bell, C., Cruchaga, C., Goate, A., Renton, A. E., et al. (2026) · npj Dementia · doi:10.1038/s44400-025-00047-7 · Cited by 11

Aldosterone exerts anti-inflammatory effects on LPS stimulated microglia

Bast, B.-O., Rickert, U., Schneppenheim, J., Cossais, F., Wilms, H., Arnold, P., & Lucius, R. (2018) · Heliyon · doi:10.1016/j.heliyon.2018.e00826 · Cited by 11

Clinicopathological correlations and cholinesterase expression in early-onset familial Alzheimer's disease with the presenilin 1 mutation, Leu235Pro

Cash, M. K., Rockwood, K. J., Fisk, J. D., & Darvesh, S. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.02.025 · Cited by 11

Understanding familial Alzheimer's disease: The fit‐stay‐trim mechanism of γ‐secretase

Mehra, R., & Kepp, K. P. (2021) · Wiley Interdisciplinary Reviews Computational Molecular Science · doi:10.1002/wcms.1556 · Cited by 11

Two-Photon Fluorescent Probes for Amyloid-β Plaques Imaging In Vivo

Chen, Y. (2023) · Molecules · doi:10.3390/molecules28176184 · Cited by 11

Biomarkers and Risk Assessment of Alzheimer’s Disease in Low- and Middle-Income Countries

Adewale, B. A., Coker, M. M., Ogunniyi, A. O., Kalaria, R. N., & Akinyemi, R. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221030 · Cited by 11

Five similar anthocyanidin molecules display distinct disruptive effects and mechanisms of action on Aβ1–42 protofibril: A molecular dynamic simulation study

Chen, Y., Zhan, C., Li, X., Pan, T., Yao, Y., Tan, Y., & Wei, G. (2023) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2023.128467 · Cited by 11

Bioactive peptides as multipotent molecules bespoke and designed for Alzheimer's disease

Mesias, A., Borges, S., Pintado, M., & Baptista-Silva, S. (2025) · Neuropeptides · doi:10.1016/j.npep.2025.102515 · Cited by 11

Research progress in animal models and stem cell therapy for Alzheimer’s disease

Han, F., Wang, W., & Chen, C. (2014) · Journal of Neurorestoratology · doi:10.2147/jn.s74160 · Cited by 11

Current Versus Lifetime Depression, APOE Variation, and Their Interaction on Cognitive Performance in Younger and Older Adults

Luciano, M., Fernandez-Pujals, A. M., Marioni, R. E., Campbell, A., Hayward, C., MacIntyre, D. J., Porteous, D. J., McIntosh, A. M., & Deary, I. J. (2015) · Psychosomatic Medicine · doi:10.1097/psy.0000000000000190 · Cited by 11

Amylin and pramlintide modulate γ-secretase level and APP processing in lipid rafts

Mousa, Y. M., Abdallah, I. M., Hwang, M., Martin, D. R., & Kaddoumi, A. (2020) · Scientific Reports · doi:10.1038/s41598-020-60664-5 · Cited by 11

Cognitive improvements in a rat model with polyunsaturated fatty acids EPA and DHA through α7-nicotinic acetylcholine receptors

Carlos, D.-H., Roselly, C.-R. B., Angel, U. L., Laura, M. A., Karina, S. R. K., Manuel, C.-B. J., Alejandra, C. S., Gabriela, C. C. E., Ochoa-Ruiz, E., & Serrano‐Medina, A. (2020) · Nutritional Neuroscience · doi:10.1080/1028415x.2020.1809878 · Cited by 11

Computational prediction and molecular mechanism of γ-secretase modulators

Mehra, R., & Kepp, K. P. (2020) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2020.105626 · Cited by 11

Genetics of Alzheimer Disease

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Alzheimer's disease research progress in Australia: The Alzheimer's Association International Conference Satellite Symposium in Sydney

Sexton, C. E., Anstey, K. J., Baldacci, F., Barnum, C. J., Barron, A. M., Blennow, K., Brodaty, H., Burnham, S. C., Elahi, F. M., Götz, J., et al. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12380 · Cited by 11

Distinguishing Amyloid β-Protein in a Mouse Model of Alzheimer’s Disease by Label-Free Vibrational Imaging

Li, S., Luo, Z., Zhang, R., Xu, H., Zhou, T., Liu, L., & Qu, J. (2021) · Biosensors · doi:10.3390/bios11100365 · Cited by 11

Study of altered functional connectivity in individuals at risk for Alzheimer’s Disease

Zhang, Y., Liu, X., Zhao, K., Li, L., & Ding, Y. (2018) · Technology and Health Care · doi:10.3233/thc-174235 · Cited by 11

Relationship between F-18 florbetapir uptake in occipital lobe and neurocognitive performance in Alzheimer’s disease

Thientunyakit, T., Thongpraparn, T., Sethanandha, C., Yamada, T., Kimura, Y., Muangpaisan, W., & Ishii, K. (2021) · Japanese Journal of Radiology · doi:10.1007/s11604-021-01132-6 · Cited by 11

Structure–Activity Relationships of Radioiodinated 6,5,6-Tricyclic Compounds for the Development of Tau Imaging Probes

Watanabe, H., Tatsumi, H., Kaide, S., Shimizu, Y., Iikuni, S., & Ono, M. (2020) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.9b00456 · Cited by 11

Alzheimer's Disease

Dalvi, A. (2012) · Disease-a-Month · doi:10.1016/j.disamonth.2012.08.008 · Cited by 11

Predicting Alzheimer’s disease progression trajectory and clinical subtypes using machine learningPreprint

Satone, V. K., Kaur, R., Dadu, A., Leonard, H. L., Iwaki, H., Makarious, M. B., Sargent, L. J., Initiative, A. D. N., Daneshmand, A., Scholz, S. W., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/792432 · Cited by 11

An mTOR-independent Macroautophagy Activator Ameliorates Tauopathy and Prionopathy Neurodegeneration PhenotypesPreprint

Yoon, L., Botham, R. C., Verhelle, A., Wu, Y., Cole, C. M., Tan, E. P., Massey, L. A., Sanz-Martinez, P., Chou, C., Xu, J., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.09.29.509997 · Cited by 11

The role of AMPKα subunit in Alzheimer's disease: In-depth analysis and future prospects

Xia, L., Chen, J., Huang, J., Lin, X., Jiang, J., Liu, T., Huang, N., & Luo, Y. (2024) · Heliyon · doi:10.1016/j.heliyon.2024.e34254 · Cited by 10

A criterion characterizing accumulated neurotoxicity of Aβ oligomers in Alzheimer's disease

Kuznetsov, A. V. (2025) · Proceedings of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rspa.2024.0652 · Cited by 10

Updates on Tau-Related Drug Targets and Potential Disease-Modifying Therapies for Alzheimer Disease

Djurovic-Topalovic, A., Horgan, N. G., & Fortin, J. S. (2025) · American Journal Of Pathology · doi:10.1016/j.ajpath.2025.05.020 · Cited by 10

Long-term caloric restriction in mice may prevent age-related learning impairment via suppression of apoptosis

Ma, L., Wang, R., Dong, W., Li, Y., Xu, B., Zhang, J., & Zhao, Z. (2016) · Behavioural Brain Research · doi:10.1016/j.bbr.2016.07.036 · Cited by 10

The role of amyloid β in the pathological mechanism of GNE myopathy

Zhang, T., Shang, R., & Miao, J. (2022) · Neurological Sciences · doi:10.1007/s10072-022-06301-7 · Cited by 10

Effects of multi-mode physical stimulation on APP/PS1 Alzheimer's disease model mice

Liu, S., Li, S., Xia, Y., Zhang, H., Tian, J., Shan, C., Pang, F., Wang, Y., Shang, Y., & Chen, N. (2022) · Heliyon · doi:10.1016/j.heliyon.2022.e12366 · Cited by 10

Synthesis, structural characterization and study of antioxidant and anti-PrPSc properties of flavonoids and their rhenium(I)–tricarbonyl complexes

Glykofridi, P., Tziouri, V.-E., Xanthopoulos, K., Vlachou, M.-E., Correia, S., Fischer, A.-L., Thüne, K., Hatzidimitriou, A. G., Zerr, I., Schmitz, M., et al. (2023) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-022-01986-9 · Cited by 10

PARP16-Mediated Stabilization of Amyloid Precursor Protein mRNA Exacerbates Alzheimer’s Disease Pathogenesis

Wang, J., Cheng, Q., Zhang, Y., Hong, C., Liu, J., Liu, X., & Chang, J. (2023) · Aging and Disease · doi:10.14336/ad.2023.0119 · Cited by 10

Deciphering mechanisms of action of ACE inhibitors in neurodegeneration using Drosophila models of Alzheimer’s disease

Ghalayini, J., & Boulianne, G. L. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1166973 · Cited by 10

sc2MeNetDrug: A computational tool to uncover inter-cell signaling targets and identify relevant drugs based on single cell RNA-seq data

Feng, J., Goedegebuure, S. P., Zeng, A., Bi, Y., Wang, T., Payne, P., Ding, L., DeNardo, D. G., Hawkins, W. G., Fields, R. C., et al. (2024) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1011785 · Cited by 10

Subtype-specific neurons from patient iPSCs display distinct neuropathological features of Alzheimer’s disease

Tao, R. N., Yue, C., Guo, Z., Guo, W., Yao, Y., Yang, X., Shao, Z., Gao, C., Ding, J., Shen, L. H., et al. (2024) · Cell Regeneration · doi:10.1186/s13619-024-00204-y · Cited by 10

Advancing Alzheimer's Therapy: Computational strategies and treatment innovations

Paul, J. K., Malik, A., Azmal, M., Gulzar, T., Afghan, M. T. R., Talukder, O. F., Shahzadi, S., & Ghosh, A. (2025) · IBRO Neuroscience Reports · doi:10.1016/j.ibneur.2025.02.002 · Cited by 10

Stepping back to move forward: a current review of iPSCs in the fight against Alzheimer's disease.

Devineni, A., Tohme, S., Mt, K., Cowley, R. A., & Harris, B. T. (2016) · Europe PMC (PubMed Central) · Cited by 10

Tranexamic Acid Improves Memory and Learning Abilities in Aging Mice

Hiramoto, K., Yamate, Y., Matsuda, K., Sugiyama, D., & Iizuka, Y. (2020) · Journal of Experimental Pharmacology · doi:10.2147/jep.s284532 · Cited by 10

Cerebral Aβ deposition in an Aβ-precursor protein-transgenic rhesus monkey

Chan, A. W. S., Cho, I. K., Li, C., Zhang, X., Patel, S., Rusnak, R., Raper, J., Bachevalier, J., Moran, S. P., Chi, T., et al. (2022) · Aging Brain · doi:10.1016/j.nbas.2022.100044 · Cited by 10

Mechanistic Role of Jak3 in Obesity-Associated Cognitive Impairments

Kumar, P., Mishra, J., & Kumar, N. (2022) · Nutrients · doi:10.3390/nu14183715 · Cited by 10

Pathology steered stratification network for subtype identification in Alzheimer's disease

Xu, E., Zhang, J., Li, J., Song, Q., Yang, D., Guorong Wu, A., & Chen, M. (2023) · Medical Physics · doi:10.1002/mp.16655 · Cited by 10

Combination of Aβ clearance and neurotrophic factors as a potential treatment for Alzheimer’s disease

Lin, L.-F., Liao, M., Xue, X., Zhang, W., Yan, L., Cai, L., Zhou, X., Zhou, X., & Luo, H. (2012) · Neuroscience Bulletin · doi:10.1007/s12264-012-1287-6 · Cited by 10

Recent Advances from the Bench Toward the Bedside in Alzheimer's Disease

Macauley, S. L., & Holtzman, D. M. (2015) · EBioMedicine · doi:10.1016/j.ebiom.2015.01.002 · Cited by 10

Chronic Lithium Treatment in a Rat Model of Basal Forebrain Cholinergic Depletion: Effects on Memory Impairment and Neurodegeneration

Gelfo, F., Cutuli, D., Nobili, A., Bartolo, P. D., D’Amelio, M., Petrosini, L., & Caltagirone, C. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-160892 · Cited by 10

Transcriptome Profile of Nicotinic Receptor-Linked Sensitization of Beta Amyloid Neurotoxicity

Arora, K., Belcaid, M., Lantz, M. J., Taketa, R., & Nichols, R. A. (2020) · Scientific Reports · doi:10.1038/s41598-020-62726-0 · Cited by 10

Development of AD-Like Pathology in Skeletal Muscle

Chen, X., Miller, N. M., Afghah, Z., & Geiger, J. D. (2019) · Journal of Parkinson’s Disease and Alzheimer’s Disease · doi:10.13188/2376-922x.1000028 · Cited by 10

Impaired glymphatic clearance is an important cause of Alzheimer’s disease

Hazzard, I., Batiste, M., Luo, T., Cheung, C., & Lui, F. (2024) · Exploration of Neuroprotective Therapy · doi:10.37349/ent.2024.00091 · Cited by 9

Benfotiamine Ameliorates Streptozotocin-Induced Alzheimer’s Disease in Rats by Modulating Neuroinflammation, Oxidative Stress, and Microglia

Cardinali, C. A. E. F., Martins, Y. A., de Moraes, R. C. M., Costa, A. P., & Torrão, A. D. S. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04811-x · Cited by 9

Evaluating computational and experimental approaches in early-stage Alzheimer’s drug discovery: a systematic review

Azmal, M., Paul, J. K., Shohan, M. N. H., Haque, A. N. M. S. N. B., Mrinmoy, M., Talukder, O. F., & Ghosh, A. (2025) · Journal of Computer-Aided Molecular Design · doi:10.1007/s10822-025-00610-7 · Cited by 9

Alzheimer’s disease polygenic risk’s association with all-cause dementia through the plasma metabolome in the UK Biobank study

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Single-nucleus multi-omics identifies shared and distinct pathways in Pick’s and Alzheimer’s disease

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