Amyloidosis in Alzheimer’s Disease: Pathogeny, Etiology, and Related Therapeutic Directions

Ma, Chen; Hong, Fenfang; Yang, Shulong

doi:10.3390/molecules27041210

Cited by 243Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

Amyloidosis in Alzheimer’s Disease: Pathogeny, Etiology, and Related Therapeutic Directions

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Ma, Chen, Hong, Fenfang, Yang, Shulong·2022·Molecules

DOI 10.3390/molecules27041210PMC PMC8876037

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Abstract

The amyloid hypothesis of Alzheimer’s disease has long been the predominant theory, suggesting that Alzheimer’s disease is caused by the accumulation of amyloid beta protein (Aβ) in the brain, leading to neuronal toxicity in the central nervous system (CNS). Because of breakthroughs in molecular medicine, the amyloid pathway is thought to be central to the pathophysiology of Alzheimer’s disease (AD). Currently, it is believed that altered biochemistry of the Aβ cycle remains a central biological feature of AD and is a promising target for treatment. This review provides an overview of the process of amyloid formation, explaining the transition from amyloid precursor protein to amyloid beta protein. Moreover, we also reveal the relationship between autophagy, cerebral blood flow, ACHE, expression of LRP1, and amyloidosis. In addition, we discuss the detailed pathogenesis of amyloidosis, including oxidative damage, tau protein, NFTs, and neuronal damage. Finally, we list some ways to treat AD in terms of decreasing the accumulation of Aβ in the brain.

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The amyloid hypothesis emphasizes that accumulation of Aβ plaques in the brain is a central event in the pathogenesis of AD, leading to neurodegeneration and cognitive decline.
“The amyloid hypothesis emphasizes that the accumulation of Aβ plaques in the brain is a central event in the pathogenesis of AD, leading to neurodegeneration and cognitive decline.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [11]
The hydrophobic C-terminus of Aβ42 facilitates its aggregation and formation of senile plaques.
“The hydrophobic C-terminus of Aβ42 facilitates its aggregation and the formation of senile plaques.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [11]
Aβ originates from processing of APP through sequential cleavage by β-secretase and γ-secretase, resulting in various lengths of Aβ fragments, with Aβ40 and Aβ42 predominant.
“Aβ originates from the processing of the amyloid precursor protein (APP) through sequential cleavage by β-secretase and γ-secretase, resulting in various lengths of Aβ fragments, with Aβ40 and Aβ42 being predominant.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [11]
The relationship between FAD mutations and Aβ levels is complex, and plaque formation in sporadic AD is influenced by a dynamic imbalance between Aβ production and clearance mechanisms.
“However, the relationship between FAD mutations and Aβ levels is complex, and the plaque formation in sporadic AD is influenced by a dynamic imbalance between Aβ production and clearance mechanisms [11,12].”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [11]
Mutations in PS1 can promote Aβ accumulation through increased production and impaired autophagy functions.
“Mutations in presenilin-1 (PS1) can promote Aβ accumulation through increased production and impaired autophagy functions.”
From Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease (2024) · cites this paper as [11]

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Dangerous Liaisons between Beta-Amyloid and Cholinergic Neurotransmission
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The effects of Danggui-Shaoyao-San on neuronal degeneration and amyloidosis in mouse and its molecular mechanism for the treatment of Alzheimer’s disease
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Activation of Neuronal Defense Mechanisms in Response to Pathogenic Factors Triggering Induction of Amyloidosis in Alzheimer's Disease
Maltsev, A. V., Santockyte, R., Bystryak, S. M., & Galzitskaya, O. V. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-131562 · Cited by 14 · see citing works

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The role of probiotics and prebiotics in modulating of the gut-brain axis
Ansari, F., Neshat, M., Pourjafar, H., Jafari, S. M., Samakkhah, S. A., & Mirzakhani, E. (2023) · Frontiers in Nutrition · doi:10.3389/fnut.2023.1173660 · Cited by 219 · see citing works
Neuroinflammation in Neurodegenerative Disorders: Current Knowledge and Therapeutic Implications
Giri, P. M., Banerjee, A., Ghosal, A., & Layek, B. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25073995 · Cited by 123 · see citing works
BACE1 Inhibitors for Alzheimer’s Disease: The Past, Present and Any Future?
Bazzari, F. H., & Bazzari, A. H. (2022) · Molecules · doi:10.3390/molecules27248823 · Cited by 115 · see citing works
Nanotechnology-based drug delivery for the treatment of CNS disorders
Mittal, K. R., Pharasi, N., Sarna, B., Singh, M., Rachana, R., Haider, S., Singh, S. K., Dua, K., Jha, S. K., Dey, A., et al. (2022) · Translational Neuroscience · doi:10.1515/tnsci-2022-0258 · Cited by 112 · see citing works
Alzheimer’s Disease and Inflammaging
Kosyreva, A., Sentyabreva, A., Tsvetkov, I., & Makarova, O. (2022) · Brain Sciences · doi:10.3390/brainsci12091237 · Cited by 98 · see citing works
Copper homeostasis and cuproptosis in health and disease
Yang, Y., Wu, J., Wang, L., Ji, G., & Dang, Y. (2024) · MedComm · doi:10.1002/mco2.724 · Cited by 91 · see citing works
Akt signaling pathway: a potential therapy for Alzheimer’s disease through glycogen synthase kinase 3 beta inhibition
Limantoro, J., de Liyis, B. G., & Sutedja, J. C. (2023) · The Egyptian Journal of Neurology Psychiatry and Neurosurgery · doi:10.1186/s41983-023-00751-2 · Cited by 59 · see citing works
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
“However, the relationship between FAD mutations and A β levels is complex, and the plaque formation in sporadic AD is influenced by a dynamic imbalance between A β production and clearance mechanisms [11,12].”
Background
Alzheimer's disease: The role of proteins in formation, mechanisms, and new therapeutic approaches
Gholami, A. (2023) · Neuroscience Letters · doi:10.1016/j.neulet.2023.137532 · Cited by 51 · see citing works
A new andrographolide derivative ADA targeting SIRT3-FOXO3a signaling mitigates cognitive impairment by activating mitophagy and inhibiting neuroinflammation in Apoe4 mice
Zhou, Y., Zhao, Q., Zhang, Y., Di, L., Feng, X., Xu, W., Gao, W.-P., Guo, Y., He, Y., Kou, J., et al. (2023) · Phytomedicine · doi:10.1016/j.phymed.2023.155298 · Cited by 46 · see citing works
Rg1 improves Alzheimer's disease by regulating mitochondrial dynamics mediated by the AMPK/Drp1 signaling pathway
Zhang, Y., Liu, S., Cao, D., Zhao, M., Lu, H., & Wang, P. (2024) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2024.119285 · Cited by 46 · see citing works
Dendrimers in Alzheimer’s Disease: Recent Approaches in Multi-Targeting Strategies
Arbez‐Gindre, C., Steele, B. R., & Micha‐Screttas, M. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15030898 · Cited by 43 · see citing works
The microbiota–gut–brain axis in mental and neurodegenerative disorders: opportunities for prevention and intervention
Yassin, L. K., Skrabulyte-Barbulescu, J., Alshamsi, S. H., Saeed, S., Alkuwaiti, S. H., Almazrouei, S., Alnuaimi, A., BaniYas, S., Aldhaheri, D., Alderei, M., et al. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1667448 · Cited by 46 · see citing works
Molecular mechanism and therapeutic strategy of bile acids in Alzheimer’s disease from the emerging perspective of the microbiota–gut–brain axis
Wu, M., Cheng, Y., Zhang, R., Han, W., Jiang, H., Bi, C., Zhang, Z., Ye, M., Lin, X., & Liu, Z. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117228 · Cited by 38 · see citing works
Artificial Intelligence in Alzheimer’s Disease Diagnosis and Prognosis Using PET-MRI: A Narrative Review of High-Impact Literature Post-Tauvid Approval
Christodoulou, R. C., Woodward, A. L., Pitsillos, R., Ibrahim, R., & Georgiou, M. F. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14165913 · Cited by 37 · see citing works
Neuroimmune mechanisms underlying Alzheimer’s disease: Insights into central and peripheral immune cell crosstalk
Liu, Y., Tan, Y., Zhang, Z., Li, H., Yi, M., Zhang, Z., Hui, S., & Peng, W. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101831 · Cited by 33 · see citing works
CircLPAR1 Promotes Neuroinflammation and Oxidative Stress in APP/PS1 Mice by Inhibiting SIRT1/Nrf-2/HO-1 Axis Through Destabilizing GDF-15 mRNA
Xiong, W., Li, D., Feng, Y., Jia, C., Zhang, X., & Liu, Z. (2023) · Molecular Neurobiology · doi:10.1007/s12035-022-03177-8 · Cited by 33 · see citing works
Neuroprotective effects of riluzole in Alzheimer's disease: A comprehensive review
Golmohammadi, M., Mahmoudian, M., Hasan, E. K., Alshahrani, S. H., Romero‐Parra, R. M., Malviya, J., Hjazi, A. M., Najm, M. A. A., Almulla, A. F., Zamanian, M. Y., et al. (2023) · Fundamental and Clinical Pharmacology · doi:10.1111/fcp.12955 · Cited by 32 · see citing works
Aβ1-42 promotes microglial activation and apoptosis in the progression of AD by binding to TLR4
Dou, R.-X., Zhang, Y., Hu, X., Gao, F.-L., Zhang, L., Liang, Y.-H., Zhang, Y.-Y., Yao, Y.-P., Li, Y., Zhang, Y., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103428 · Cited by 29 · see citing works
Investigating the effects of Ginkgo biloba leaf extract on cognitive function in Alzheimer's disease
Zhu, C., Liu, J., Lin, J., Xu, J., & Yu, E. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14914 · Cited by 28 · see citing works
Neuroprotective effects of resistance physical exercise on the APP/PS1 mouse model of Alzheimer’s disease
Campos, H. C., Ribeiro, D. E., Hashiguchi, D., Glaser, T., Milanis, M. D. S., Gimenes, C., Suchecki, D., Arida, R. M., Ulrich, H., & Longo, B. M. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1132825 · Cited by 28 · see citing works
Multidimensional autophagy nano-regulator boosts Alzheimer's disease treatment by improving both extra/intraneuronal homeostasis
Li, Y., Yang, P., Meng, R., Xu, S., Zhou, L., Qian, K., Wang, P., Cheng, Y., Sheng, D., Xu, M., et al. (2023) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2023.10.009 · Cited by 26 · see citing works
Exploring the Role of GLP-1 Receptor Agonists in Alzheimer’s Disease: A Review of Preclinical and Clinical Evidence
Teixeira, L. C. R., Luizon, M. R., & Gomes, K. B. (2025) · Receptors · doi:10.3390/receptors4010002 · Cited by 24 · see citing works
miR ‐107‐5p ameliorates neurological damage, oxidative stress, and immune responses in mice with Alzheimer's disease by suppressing the Toll‐like receptor 4 (TLR4)/nuclear factor‐kappaB(NF‐κB) pathway
Hu, G., Jiang, X., Du, S., Zhang, K., & Chen, Z. (2024) · The Kaohsiung Journal of Medical Sciences · doi:10.1002/kjm2.12797 · Cited by 22 · see citing works
Edaravone Dexborneol ameliorates the cognitive deficits of APP/PS1 mice by inhibiting TLR4/MAPK signaling pathway via upregulating TREM2
Wang, J., Du, L., Zhang, T., Chu, Y., Wang, Y., Wang, Y. T., Ji, X., Kang, Y., Cui, R., Zhang, G., et al. (2024) · Neuropharmacology · doi:10.1016/j.neuropharm.2024.110006 · Cited by 22 · see citing works
Tetrameric Transthyretin as a Protective Factor Against Alzheimer’s Disease
Corino, C., Aimo, A., Luigetti, M., Ciccone, L., Chen, Y. F. F., Panichella, G., Musetti, V., Castiglione, V., Vergaro, G., Emdin, M., et al. (2024) · Molecular Neurobiology · doi:10.1007/s12035-024-04442-8 · Cited by 21 · see citing works
Efficacy and molecular mechanisms of hesperidin in mitigating Alzheimer's disease: A systematic review
Han, X., Zhang, Y., Zhang, L., Zhang, L., & Wang, Y. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.117144 · Cited by 22 · see citing works
Is blood pTau a reliable indicator of the CSF status? A narrative review
Antonioni, A., Raho, E. M., & Lorenzo, F. D. (2023) · Neurological Sciences · doi:10.1007/s10072-023-07258-x · Cited by 20 · see citing works
Pathogenesis, Animal Models, and Drug Discovery of Alzheimer’s Disease
Xia, Z.-D., Ma, R.-X., Wen, J.-F., Zhai, Y.-F., Wang, Y.-Q., Wang, F.-Y., Liu, D., Zhao, X.-L., Sun, B., Jia, P., et al. (2023) · Journal of Alzheimer's Disease · doi:10.3233/jad-230326 · Cited by 19 · see citing works
The Role of Dietary Antioxidants and Their Potential Mechanisms in Alzheimer’s Disease Treatment
Knight, E., Geetha, T., Broderick, T. L., & Babu, J. R. (2023) · Metabolites · doi:10.3390/metabo13030438 · Cited by 19 · see citing works
Tau proteins and senescent Cells: Targeting aging pathways in Alzheimer’s disease
Singh, M., Ali, H., Jyothi, S. R., Kaur, I., Kumar, S., Sharma, N., Prasad, G. V. S., Pramanik, A., Almalki, W. H., & Imran, M. (2024) · Brain Research · doi:10.1016/j.brainres.2024.149165 · Cited by 18 · see citing works
Neurodegenerative diseases early detection and monitoring system for point-of-care applications
Thakur, R. R., Saini, A. K., Taliyan, R., & Chaturvedi, N. (2024) · Microchemical Journal · doi:10.1016/j.microc.2024.112280 · Cited by 18 · see citing works
Cerebroprotein hydrolysate-I ameliorates cognitive dysfunction in APP/PS1 mice by inhibiting ferroptosis via the p53/SAT1/ALOX15 signalling pathway
Ren, X., Wen, Y., Yuan, M., Li, C., Zhang, J., Li, S., Zhang, X., Wang, L., & Wang, S. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176820 · Cited by 17 · see citing works
β-Amyloid peptide modulates peripheral immune responses and neuroinflammation in rats
Adhikary, K., Mohanty, S., Bandyopadhyay, B., Maiti, R., Bhattacharya, K., & Karak, P. (2024) · Biomolecular Concepts · doi:10.1515/bmc-2022-0042 · Cited by 13 · see citing works
Targeting Amyloid Beta Aggregation and Neuroinflammation in Alzheimer’s Disease: Advances and Future Directions
Dagla, I., Gkikas, F., Gikas, E. E., & Tsarbopoulos, A. (2026) · Cells · doi:10.3390/cells15030295 · Cited by 15 · see citing works
Plasma Exchange Reduces Aβ Levels in Plasma and Decreases Amyloid Plaques in the Brain in a Mouse Model of Alzheimer’s Disease
Ramírez, S., Koerich, S., Astudillo, N., Gregorio, N. D., Al‐Lahham, R., Allison, T., Rocha, N. P., Wang, F., & Soto, C. A. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242317087 · Cited by 14 · see citing works
GLP-1/GIP Agonist as an Intriguing and Ultimate Remedy for Combating Alzheimer’s Disease through its Supporting DPP4 Inhibitors: A Review
Abubakar, M., Nama, L., Ansari, M. M., Ansari, M. M., Bhardwaj, S., Daksh, R., Syamala, K. L. V., Jamadade, M. S., Chhabra, V., Kumar, D., et al. (2024) · Current Topics in Medicinal Chemistry · doi:10.2174/0115680266293416240515075450 · Cited by 14 · see citing works
Predicting Amyloid Positivity from Fdg Pet Images Using Radiomics: A Parsimonious Model
Rasi, R., & Güveniş, A. (2023) · Computer Methods and Programs in Biomedicine · doi:10.1016/j.cmpb.2024.108098 · Cited by 13 · see citing works
Modifying Alzheimer’s disease pathophysiology with photobiomodulation: model, evidence, and future with EEG-guided intervention
Lim, L. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2024.1407785 · Cited by 14 · see citing works
Stem cell therapy in Alzheimer’s disease: current status and perspectives
Ou, C.-M., Xue, W.-W., Liu, D., Ma, L., Xie, H.-T., & Ning, K. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1440334 · Cited by 16 · see citing works
Protective Effects of Bifidobacterium Breve MCC1274 as a Novel Therapy for Alzheimer’s Disease
Abdelhamid, M., Counts, S., Zhou, C., Hida, H., Kim, J., Michikawa, M., & Jung, C. (2025) · Nutrients · doi:10.3390/nu17030558 · Cited by 16 · see citing works
Design, Synthesis, and In Vitro, In Silico and In Cellulo Evaluation of New Pyrimidine and Pyridine Amide and Carbamate Derivatives as Multi-Functional Cholinesterase Inhibitors
Bortolami, M., Pandolfi, F., Tudino, V., Messore, A., Madia, V. N., Vita, D. D., Santo, R. D., Costi, R., Romeo, I., Alcaro, S., et al. (2022) · Pharmaceuticals · doi:10.3390/ph15060673 · Cited by 12 · see citing works
Passive Anti-Amyloid Beta Immunotherapies in Alzheimer’s Disease: From Mechanisms to Therapeutic Impact
Schreiner, T. G., Croitoru, C. G., Hodorog, D. N., & Cuciureanu, D. I. (2024) · Biomedicines · doi:10.3390/biomedicines12051096 · Cited by 12 · see citing works
Unraveling the Potential Underlying Mechanisms of Mild Behavioral Impairment: Focusing on Amyloid and Tau Pathology
Angelopoulou, E., Bougea, A. M., Hatzimanolis, A., Scarmeas, N., & Papageorgiou, S. G. (2024) · Cells · doi:10.3390/cells13131164 · Cited by 14 · see citing works
Behavioral and pathological characteristics of 5xFAD female mice in the early stage
Zhu, C., & Liu, X. (2025) · Scientific Reports · doi:10.1038/s41598-025-90335-2 · Cited by 12 · see citing works
PR-957 Suppresses Th1 and Th17 Cell Differentiation via Inactivating PI3K/AKT Pathway in Alzheimer’s Disease
Li, Y., Fan, H., Han, X., Sun, J., Ni, M., Zhang, L., Fang, F., Zhang, W., & Ma, P. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.10.021 · Cited by 12 · see citing works
Visual Function in Alzheimer’s Disease: Current Understanding and Potential Mechanisms Behind Visual Impairment
Alvite‐Piñeiro, T., López‐López, M., Regueiro, U., Peleteiro, J. M. P., Sobrino, T., & Lema, I. (2025) · Journal of Clinical Medicine · doi:10.3390/jcm14175963 · Cited by 11 · see citing works
Innovations in Alzheimer’s disease diagnostic technologies: clinical prospects of novel biomarkers, multimodal integration, and non-invasive detection
Wang, R., Peng, S., Zhu, J., Xu, Y., Wang, M., Zhang, L., Qiu, Y., Hou, D., Wang, Q., & Liu, R. (2025) · Frontiers in Neurology · doi:10.3389/fneur.2025.1651708 · Cited by 11 · see citing works
Network Pharmacology and Mechanism Studies of the Protective Effect of Ginseng against Alzheimerʼs Disease Based on Aβ Pathogenesis
Liu, J., Yu, W., Ma, C., Li, T., Liang, Y., Su, S., Zhong, G., Xie, Z., Wu, Q., Chen, J., et al. (2023) · Planta Medica · doi:10.1055/a-2014-6061 · Cited by 11 · see citing works
Self-citation
Recent Progress in the Treatment Strategies for Alzheimer’s Disease
Kumar, V., & Roy, K. (2023) · Neuromethods · doi:10.1007/978-1-0716-3311-3_1 · Cited by 11 · see citing works
Exploring the potential mechanism of ginsenoside Rg1 to regulate ferroptosis in Alzheimer's disease based on network pharmacology
Deng, X., Qiu, Z., Chen, X., Liu, J., Wang, X., Li, J., Zhang, J., Cui, X., Fu, Y., & Jiang, M. (2024) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2024.176859 · Cited by 11 · see citing works
Potential links between platelets and amyloid-β in the pathogenesis of Alzheimer's disease: Evidence from in vitro, in vivo, and clinical studies
Yubolphan, R., Pratchayasakul, W., Koonrungsesomboon, N., Chattipakorn, N., & Chattipakorn, S. C. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114683 · Cited by 11 · see citing works
The total withanolides from the leaves of Datura stramonium L. Improves Alzheimer’s disease pathology by restraining neuroinflammation through NLRP3/IL-1β/IL1R1/TOM 1 pathway
Li, X., Pan, J., Liu, X., Li, M., Zhuang, L., Jiang, P., Wang, S., Guan, W., Xue, S., Chen, Q., et al. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113893 · Cited by 10 · see citing works
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 · see citing works
Machine learning model for predicting Amyloid-β positivity and cognitive status using early-phase 18F-Florbetaben PET and clinical features
Choi, D. H., Ahn, S. H., Chung, Y., Kim, J. S., Jeong, J. H., & Yoon, H. (2025) · Scientific Reports · doi:10.1038/s41598-025-00743-7 · Cited by 10 · see citing works
Korean Red Pine (<i>Pinus densiflora</i>) Bark Extract Attenuates Aβ-Induced Cognitive Impairment by Regulating Cholinergic Dysfunction and Neuroinflammation
Go, M. J., Kim, J. M., Kang, J. Y., Park, S. K., Lee, C. J., Kim, M. J., Lee, H. R., Kim, T. Y., Joo, S. G., Kim, D.-O., et al. (2022) · Journal of Microbiology and Biotechnology · doi:10.4014/jmb.2207.07015 · Cited by 9 · see citing works
Naringin and Naringenin: Potential Multi-Target Agents for Alzheimer’s Disease
Lu, J., Chen, J., Li, S., Pan, G.-J., Ou, Y., Yuan, L.-F., Jiang, J., Zeng, L., & Zhao, J. J. (2024) · Current Medical Science · doi:10.1007/s11596-024-2921-z · Cited by 9 · see citing works
Exposure to nano-polystyrene during pregnancy leads to Alzheimer's disease-related pathological changes in adult offspring
Wang, F., Wang, J., Luo, N., Luo, Y., Gao, Z., Ye, C., Jiang, M., Shen, Z., Xiao, J., Xue, P., et al. (2025) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2025.117736 · Cited by 9 · see citing works
Expression and potential regulatory mechanism of cellular senescence-related genes in Alzheimer’s disease based on single-cell and bulk RNA datasets
Sha, D., Zhang, J., Xu, F., Wang, X., He, X., & Shu, X. (2025) · Frontiers in Neuroscience · doi:10.3389/fnins.2025.1595847 · Cited by 9 · see citing works
From copper homeostasis to cuproptosis: a new perspective on CNS immune regulation and neurodegenerative diseases
Li, L., Lv, L., Wang, Z., Liu, X., Wang, Q., Zhu, H., Jiang, B., Han, Y., Pan, X., Zhou, X., et al. (2025) · Frontiers in Neurology · doi:10.3389/fneur.2025.1581045 · Cited by 9 · see citing works
Dissolution of Lysozyme Amyloid Fibrils Using Magnetic Nanoparticles in an Alternating Magnetic Field: Design of an Effective Treatment for Cutaneous Amyloidosis
Andrýsková, N., Vrbovská, H., Babincová, M., Babinec, P., & Šimaljaková, M. (2023) · Magnetochemistry · doi:10.3390/magnetochemistry9030084 · Cited by 8 · see citing works
Identifying pathogenic variants associated with Alzeimer by integrating genomic databases and bioinformatics approaches
Amukti, D., Wazni, A. R., Irham, L., Sulistyani, N., Ma'ruf, M., Adikusuma, W., Sarasmita, M. A., Khairi, S., Purwanto, B., Suyatmi, S., et al. (2024) · E3S Web of Conferences · doi:10.1051/e3sconf/202450101021 · Cited by 6 · see citing works
A Positive Allosteric Modulator of the SERCA Pump Rescues Hippocampal Neuronal Circuits Dysfunction and Cognitive Defects in a Mouse Model of Alzheimer's Disease
Gerasimov, E., Rakovskaya, A., Pchitskaya, E. I., Власова, О. Л., Dahl, R. S., & Борисович, Б. И. (2025) · Journal of Neuroscience · doi:10.1523/jneurosci.2337-24.2025 · Cited by 8 · see citing works
Therapeutic Applications of Oxysterols and Derivatives in Age-Related Diseases, Infectious and Inflammatory Diseases, and Cancers
Ksila, M., Ghzaiel, I., Sassi, K., Zarrouk, A., Leoni, V., Poli, G., Rezig, L., Pires, V., Meziane, S., Atanasov, A. G., et al. (2023) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-43883-7_19 · Cited by 8 · see citing works
ECSIT: Biological function and involvement in diseases
Zhang, T., Fan, J., Wen, X., & Duan, X. (2024) · International Immunopharmacology · doi:10.1016/j.intimp.2024.113524 · Cited by 8 · see citing works
Mitochondrial Calcium Uniporter knockdown improves the viability of HT22 hippocampal neurons in Alzheimer's disease
Cai, H.-Y., Hou, F., Wang, Y., Wu, L.-H., Wang, Z.-J., Wu, M., Wang, X., & Hölscher, C. (2025) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2025.177347 · Cited by 7 · see citing works
Codelivery of fibronectin and rapamycin via bioactive phosphorus dendrimers to ameliorate Alzheimer’s disease through macrophage autophagy, oxidative stress alleviation and polarization modulation
Zhan, M., Dai, W., Sun, H., Gao, Y., Zou, Y., Laurent, R., Sun, X., Mignani, S. M., Majoral, J., Shen, M., et al. (2025) · Nano Today · doi:10.1016/j.nantod.2025.102664 · Cited by 7 · see citing works
Therapeutic potential of dual HDAC6/SIRT2 inhibition in Alzheimer's disease
Wang, X., Li, C., Chen, L., He, B., & Li, Y. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117733 · Cited by 8 · see citing works
Genetics and Epigenetics of Alzheimer’s Disease: Understanding Pathogenesis and Exploring Therapeutic Potential
Tiwari, P., Dwivedi, R., Kaushik, M., Tripathi, M., & Dada, R. (2025) · Journal of Molecular Neuroscience · doi:10.1007/s12031-025-02363-2 · Cited by 7 · see citing works
LCN2 of cerebrospinal fluid: A potential biomarker for diagnosis and disease progression in Alzheimer's disease
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Authors: Ma, C., Hong, F., & Yang, S.
Affiliations: Nanchang University (CN)
Experimental Center of Pathogen Biology, Nanchang University, Nanchang 330006, China
Department of Physiology, College of Medicine, Nanchang University, Nanchang 330006, China
ORCID: Ma, Chen
Venue: Molecules
Publisher: MDPI AG
Published: 2022-02-11
Volume: 27
Issue: 4
Pages: 1210
ISSN: 1420-3049 (ISSN-L)
DOI: 10.3390/molecules27041210
PMC: PMC8876037
OpenAlex: W4212889165
Cited by: 243
References: 83
Citations by year: 2026: 51 · 2025: 80 · 2024: 65 · 2023: 36 · 2022: 11
FWCI: 6.60
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Molecules (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: the National Natural Science Foundation of China (82060661,81660151 and 81660751)
Topics: Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: Alzheimer's disease, amyloidosis, amyloid hypothesis, amyloid-beta, amyloid precursor protein, amyloid fibril formation, autophagy, cerebral blood flow, acetylcholinesterase, LRP1, oxidative damage, tau protein, neurofibrillary tangles, neuronal injury, Alzheimer's disease treatment
MeSH terms: Alzheimer Disease, Amyloid, Amyloidosis, Animals, Autophagy, Brain, Disease Susceptibility, Gene Expression Regulation, Humans, Risk Factors, Biomarkers, Amyloid beta-Peptides, Disease Management, Plaque, Amyloid

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Amyloidosis in Alzheimer’s Disease: Pathogeny, Etiology, and Related Therapeutic Directions

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