Cited by 588Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchCholinesterase and Neurodegenerative Diseases

The DOI matches its Crossref record; 365 of the 371 references it cites were found in a registry or an index.

Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease

Barage, Sagar H., Sonawane, Kailas D.·2015·Neuropeptides

DOI 10.1016/j.npep.2015.06.008

Open this paper in CoChat — free account

Abstract

Alzheimer's disease is an irreversible, progressive neurodegenerative disorder. Various therapeutic approaches are being used to improve the cholinergic neurotransmission, but their role in AD pathogenesis is still unknown. Although, an increase in tau protein concentration in CSF has been described in AD, but several issues remains unclear. Extensive and accurate analysis of CSF could be helpful to define presence of tau proteins in physiological conditions, or released during the progression of neurodegenerative disease. The amyloid cascade hypothesis postulates that the neurodegeneration in AD caused by abnormal accumulation of amyloid beta (Aβ) plaques in various areas of the brain. The amyloid hypothesis has continued to gain support over the last two decades, particularly from genetic studies. Therefore, current research progress in several areas of therapies shall provide an effective treatment to cure this devastating disease. This review critically evaluates general biochemical and physiological functions of Aβ directed therapeutics and their relevance.

Integrity signals

Registry

Crossref · 10.1016/j.npep.2015.06.008

Cites

365 of 365 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

A novel potent vasoconstrictor peptide produced by vascular endothelial cells
Yanagisawa, M., Kurihara, H., Kimura, S., Tomobe, Y. I., Kobayashi, M., Mitsui, Y., Yazaki, Y., Goto, K., & Masaki, T. (1988) · Nature · doi:10.1038/332411a0 · Cited by 10,716
Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families
Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429
Mild Cognitive Impairment: Clinical Characterization and Outcome
Petersen, R. C., Smith, G. E., Waring, S. C., Ivnik, R. J., Tangalos, E. G., & Kokmen, E. (1999) · Archives of Neurology · doi:10.1001/archneur.56.3.303 · Cited by 8,980
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484
The cholinergic hypothesis of geriatric memory dysfunction
Bartus, R. T., Dean, R. L., Beer, B., & Lippa, A. S. (1982) · Science · doi:10.1126/science.7046051 · Cited by 5,545
2016 Alzheimer's disease facts and figures
Alzheimer's Association (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.03.001 · Cited by 5,069
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
Goate, A., Chartier-Harlin, M.-C., Mullan, M., Brown, J., Crawford, F., Fidani, L., Giuffra, L., Haynes, A., Irving, N., James, L., et al. (1991) · Nature · doi:10.1038/349704a0 · Cited by 4,659
The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
Kang, J., Lemaire, H.-G., Unterbeck, A., Salbaum, J. M., Masters, C. L., Grzeschik, K.-H., Multhaup, G., Beyreuther, K., & Müller-Hill, B. (1987) · Nature · doi:10.1038/325733a0 · Cited by 4,619
Alzheimer’s disease
Querfurth, H. W., & LaFerla, F. M. (2010) · New England Journal of Medicine · doi:10.1056/nejmra0909142 · Cited by 4,569

Show all 371 references

Research works printed but not linked: 1

Kehoe, 2009, 1, 3

Sorted by citations

Recent Advancements in Pathogenesis, Diagnostics and Treatment of Alzheimer’s Disease
Khan, S., Barve, K. H., & Kumar, M. S. (2020) · Current Neuropharmacology · doi:10.2174/1570159x18666200528142429 · Cited by 820
“The Aβ plaque comprises of Aβ peptides obtained from amyloid precursor protein (APP) by the enzymatic cleavage via secretases (α, β and γ) [2].”
Background
Pathophysiologic relationship between Alzheimer's disease, cerebrovascular disease, and cardiovascular risk: A review and synthesis
Santos, C. Y., Snyder, P. J., Wu, W., Zhang, M., Echeverria, A., & Alber, J. (2017) · Alzheimer's & Dementia: Diagnosis, Assessment & Disease Monitoring · doi:10.1016/j.dadm.2017.01.005 · Cited by 431
Early long-term administration of the CSF1R inhibitor PLX3397 ablates microglia and reduces accumulation of intraneuronal amyloid, neuritic plaque deposition and pre-fibrillar oligomers in 5XFAD mouse model of Alzheimer’s disease
Sosna, J., Philipp, S., Albay, R., Reyes-Ruiz, J. M., Baglietto-Vargas, D., LaFerla, F. M., & Glabe, C. G. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0244-x · Cited by 406
Shaping the Nrf2-ARE-related pathways in Alzheimer’s and Parkinson’s diseases
Fão, L., Mota, S. I., & Rego, A. C. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100942 · Cited by 281
Plasma neuronal exosomes serve as biomarkers of cognitive impairment in HIV infection and Alzheimer’s disease
Pulliam, L., Sun, B., Mustapić, M., Chawla, S., & Kapogiannis, D. (2019) · Journal of NeuroVirology · doi:10.1007/s13365-018-0695-4 · Cited by 246
Therapies for Prevention and Treatment of Alzheimer’s Disease
Mendiola-Precoma, J., Berumen, L. C., Padilla, K., & García‐Alcocer, G. (2016) · BioMed Research International · doi:10.1155/2016/2589276 · Cited by 262
MAP/ERK Signaling in Developing Cognitive and Emotional Function and Its Effect on Pathological and Neurodegenerative Processes
Albert‐Gascó, H., Ros‐Bernal, F., Castillo-Gómez, E., & Olucha-Bordonau, F. E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21124471 · Cited by 248
Natural Compounds for Alzheimer’s Disease Therapy: A Systematic Review of Preclinical and Clinical Studies
Andrade, S., Ramalho, M. J., Loureiro, J. A., & Pereira, M. D. C. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092313 · Cited by 240
Insulin Resistance in Alzheimer's Disease
Ferreira, L. S. S., Fernandes, C., Vieira, M. N. N., & Felice, F. G. D. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00830 · Cited by 238
RETRACTED ARTICLE: Neuroprotective Effect of Fisetin Against Amyloid-Beta-Induced Cognitive/Synaptic Dysfunction, Neuroinflammation, and Neurodegeneration in Adult Mice
Ahmad, A., Ali, T., Park, H. Y., Badshah, H., Rehman, S. U., & Kim, M. O. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-9795-4 · Cited by 216
Retracted
Deficits in cholinergic neurotransmission and their clinical correlates in Parkinson’s disease
Perez‐Lloret, S., & Barrantes, F. J. (2016) · npj Parkinson s Disease · doi:10.1038/npjparkd.2016.1 · Cited by 216
GABAergic Inhibitory Interneuron Deficits in Alzheimer’s Disease: Implications for Treatment
Xu, Y., Zhao, M., Han, Y., & Zhang, H. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.00660 · Cited by 203
Hesperetin Confers Neuroprotection by Regulating Nrf2/TLR4/NF-κB Signaling in an Aβ Mouse Model
Ikram, M. A., Muhammad, T., Rehman, S. U., Khan, A., Jo, M. G., Ali, T., & Kim, M. O. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1512-7 · Cited by 195
Alzheimer’s Disease: The Link Between Amyloid-β and Neurovascular Dysfunction
Solis, E., Hascup, K. N., & Hascup, E. R. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200473 · Cited by 192
The Role of ADAM10 in Alzheimer’s Disease
Yuan, X., Sun, S., Tan, C., Yu, J., & Tan, L. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170061 · Cited by 160
Amyloid β-42 induces neuronal apoptosis by targeting mitochondria
Han, X., Hu, Y., Yang, Z., Jiang, L., Shi, S.-L., Li, Y.-R., Guo, M., Wu, H., & Wan, Y. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7203 · Cited by 146
Pathophysiology and management of alzheimer’s disease: an overview
Thakur, A. K., Kamboj, P., Goswami, K., & Ahuja, K. (2018) · Journal of Analytical & Pharmaceutical Research · doi:10.15406/japlr.2018.07.00230 · Cited by 144
Drug development for alzheimer’s disease: Microglia induced neuroinflammation as a target
Dong, Y., Li, X., Cheng, J., & Hou, L. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030558 · Cited by 136
FFPM, a PDE4 inhibitor, reverses learning and memory deficits in APP/PS1 transgenic mice via cAMP/PKA/CREB signaling and anti-inflammatory effects
Guo, H., Cheng, Y., Wang, C., Wu, J., Zou, Z., Niu, B., Yu, H. M., Wang, H., & Xu, J. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.01.004 · Cited by 134
Neurotransmitters in Prevention and Treatment of Alzheimer’s Disease
Yang, Z., Zou, Y., & Wang, L. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24043841 · Cited by 138
Future Therapeutic Perspectives into the Alzheimer’s Disease Targeting the Oxidative Stress Hypothesis
Teixeira, J. P., de Castro, A. A., Soares, F. V., da Cunha, E. F. F., & Ramalho, T. C. (2019) · Molecules · doi:10.3390/molecules24234410 · Cited by 124
The Many Faces of Astrocytes in Alzheimer's Disease
Monterey, M. D., Wei, H., Wu, X., & Wu, J. Q. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2021.619626 · Cited by 117
Nose-to-brain drug delivery: from bench to bedside
Drath, I., Richter, F., & Feja, M. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00481-w · Cited by 132
Novel tacrine-tryptophan hybrids: Multi-target directed ligands as potential treatment for Alzheimer's disease
Chalupova, K., Korabecny, J., Bartolini, M., Monti, B., Lamba, D., Caliandro, R., Pesaresi, A., Brazzolotto, X., Gastellier, A.-J., Nachon, F., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.02.021 · Cited by 118
Tackling neuroinflammation and cholinergic deficit in Alzheimer's disease: Multi-target inhibitors of cholinesterases, cyclooxygenase-2 and 15-lipoxygenase
AlFadly, E. D., Elzahhar, P. A., Tramarin, A., Elkazaz, S., Shaltout, H. A., Abu-Serie, M. M., Janočková, J., Soukup, O., Ghareeb, D. A., EL‐Yazbi, A. F., et al. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.02.012 · Cited by 110
Application of Iron Oxide Nanoparticles in the Diagnosis and Treatment of Neurodegenerative Diseases With Emphasis on Alzheimer’s Disease
Luo, S., Ma, C., Zhu, M., Ju, W.-N., Yu, Y., & Wang, X. (2020) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2020.00021 · Cited by 114
Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane
Fatafta, H., Khaled, M., Owen, M. C., Sayyed–Ahmad, A., & Strodel, B. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2106210118 · Cited by 107
Natural Phytochemicals in the Treatment and Prevention of Dementia: An Overview
Libro, R., Giacoppo, S., Soundara Rajan, T., Bramanti, P., & Mazzon, E. (2016) · Molecules · doi:10.3390/molecules21040518 · Cited by 107
T Lymphocytes and Inflammatory Mediators in the Interplay between Brain and Blood in Alzheimer’s Disease: Potential Pools of New Biomarkers
Mietelska‐Porowska, A., & Wojda, U. (2017) · Journal of Immunology Research · doi:10.1155/2017/4626540 · Cited by 111
Advances in developing therapeutic strategies for Alzheimer's disease
Nguyen, T. T., Nguyen, T. T. D., Nguyen, T. K. O., Vo, T. K., & Giau, V. V. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.111623 · Cited by 108
Role of Amyloid Precursor Protein (APP) and Its Derivatives in the Biology and Cell Fate Specification of Neural Stem Cells
Coronel, R., Bernabeu-Zornoza, A., Palmer, C., Moreno, M. D. M. M., Zambrano, A., Cano, E., & Liste, I. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0914-2 · Cited by 112
Brain‐Penetration and Neuron‐Targeting DNA Nanoflowers Co‐Delivering miR‐124 and Rutin for Synergistic Therapy of Alzheimer's Disease
Ouyang, Q., Liu, K., Zhu, Q., Deng, H., Le, Y., Ouyang, W., Yan, X., Zhou, W., & Tong, J. (2022) · Small · doi:10.1002/smll.202107534 · Cited by 94
Early pathologic amyloid induces hypersynchrony of BOLD resting‐state networks in transgenic mice and provides an early therapeutic window before amyloid plaque deposition
Shah, D., Praet, J., Latif‐Hernandez, A., Höfling, C., Anckaerts, C., Bard, F., Morawski, M., Detrez, J. R., Prinsen, E., Villa, A. M., et al. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.03.010 · Cited by 102
Design, synthesis and biological evaluation of new phthalimide and saccharin derivatives with alicyclic amines targeting cholinesterases, beta-secretase and amyloid beta aggregation
Panek, D., Więckowska, A., Wichur, T., Bajda, M., Godyń, J., Jończyk, J., Mika, K., Janočková, J., Soukup, O., Knez, D., et al. (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.09.078 · Cited by 98
Oligodendrocyte progenitor cells in Alzheimer's disease: from physiology to pathology
Zou, P., Wu, C., Liu, T. C.-Y., Duan, R., & Yang, L. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00385-7 · Cited by 97
Pharmacotherapy Evolution in Alzheimer’s Disease: Current Framework and Relevant Directions
Miculas, D. C., Negru, P. A., Bungau, S. G., Behl, T., Hassan, S. S. U., & Tit, D. M. (2022) · Cells · doi:10.3390/cells12010131 · Cited by 96
Harnessing endophenotypes and network medicine for Alzheimer's drug repurposing
Fang, J., Pieper, A. A., Nussinov, R., Lee, G., Bekris, L. M., Leverenz, J. B., Cummings, J. L., & Cheng, F. (2020) · Medicinal Research Reviews · doi:10.1002/med.21709 · Cited by 96
Current Progress on Peroxisome Proliferator-activated Receptor Gamma Agonist as an Emerging Therapeutic Approach for the Treatment of Alzheimer's Disease: An Update
Khan, M. A., Alam, Q., Haque, A., Ashafaq, M., Khan, M. J., Ashraf, G. M., & Ahmad, M. (2018) · Current Neuropharmacology · doi:10.2174/1570159x16666180828100002 · Cited by 92
Long-term exercise pre-training attenuates Alzheimer’s disease–related pathology in a transgenic rat model of Alzheimer’s disease
Yang, L., Wu, C., Li, Y., Dong, Y., Wu, C. Y., Lee, R. H., Brann, D. W., Lin, H. W., & Zhang, Q. (2022) · GeroScience · doi:10.1007/s11357-022-00534-2 · Cited by 100
Fenugreek Seed Powder Attenuated Aluminum Chloride-Induced Tau Pathology, Oxidative Stress, and Inflammation in a Rat Model of Alzheimer’s Disease1
Prema, A., Justin Thenmozhi, A., Manivasagam, T., Mohamed Essa, M., & Guillemin, G. J. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161103 · Cited by 90
Microbiota-gut-brain axis and toll-like receptors in Alzheimer’s disease
Lin, C., Zhao, S., Zhu, Y., Fan, Z., Wang, J., Zhang, B., & Chen, Y. (2019) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2019.09.008 · Cited by 94
Essential Oils as Treatment Strategy for Alzheimerʼs Disease: Current and Future Perspectives
Benny, A., & Thomas, J. (2018) · Planta Medica · doi:10.1055/a-0758-0188 · Cited by 89
Ginsenoside Re Inhibits ROS/ASK-1 Dependent Mitochondrial Apoptosis Pathway and Activation of Nrf2-Antioxidant Response in Beta-Amyloid-Challenged SH-SY5Y Cells
Liu, M., Bai, X., Yu, S., Zhao, W., Qiao, J., Liu, Y., Zhao, D., Wang, J., & Wang, S. (2019) · Molecules · doi:10.3390/molecules24152687 · Cited by 89
Potential application of endocannabinoid system agents in neuropsychiatric and neurodegenerative diseases—focusing on FAAH/MAGL inhibitors
Ren, S., Wang, Z., Zhang, Y., & Chen, N. (2020) · Acta Pharmacologica Sinica · doi:10.1038/s41401-020-0385-7 · Cited by 88
Design, Synthesis, and Evaluation of Novel Ferulic Acid Derivatives as Multi-Target-Directed Ligands for the Treatment of Alzheimer’s Disease
Sang, Z., Wang, K., Han, X., Cao, M., Tan, Z., & Liu, W. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00530 · Cited by 87
Antidiabetic Drugs for the Risk of Alzheimer Disease in Patients With Type 2 DM Using FAERS
Akimoto, H., Negishi, A., Oshima, S., Wakiyama, H., Okita, M., Horii, N., Inoue, N., Ohshima, S., & Kobayashi, D. (2020) · American Journal of Alzheimer's Disease & Other Dementias® · doi:10.1177/1533317519899546 · Cited by 89
Near-Infrared Fluorescent Probes as Imaging and Theranostic Modalities for Amyloid-Beta and Tau Aggregates in Alzheimer’s Disease
Rai, H., Gupta, S., Kumar, S., Yang, J., Singh, S. K., Ran, C., & Modi, G. P. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01619 · Cited by 87
Wnt signaling loss accelerates the appearance of neuropathological hallmarks of Alzheimer's disease in J20‐ APP transgenic and wild‐type mice
Tapia‐Rojas, C., & Inestrosa, N. C. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14278 · Cited by 87
Sirtuin 1 and Alzheimer's disease: An up-to-date review
Rizzi, L., & Roriz‐Cruz, M. (2018) · Neuropeptides · doi:10.1016/j.npep.2018.07.001 · Cited by 84
Nanomaterials toward the treatment of Alzheimer’s disease: Recent advances and future trends
Zeng, H., Qi, Y., Zhang, Z., Liu, C., Peng, W., & Zhang, Y. (2021) · Chinese Chemical Letters · doi:10.1016/j.cclet.2021.01.014 · Cited by 83
Alzheimer’s Disease: Pathogenesis and Therapeutic Interventions
Ogbodo, J. O., Agbo, C. P., Njoku, U. O., Ogugofor, M. O., Egba, S. I., Ihim, S. A., Echezona, A. C., Brendan, K. C., Upaganlawar, A. B., & Upasani, C. D. (2021) · Current Aging Science · doi:10.2174/1874609814666210302085232 · Cited by 86
Natural Therapeutics in Aid of Treating Alzheimer’s Disease: A Green Gateway Toward Ending Quest for Treating Neurological Disorders
Bhat, B. A., Almilaibary, A., Mir, R. A., Aljarallah, B. M., Mir, W. R., Ahmad, F., & Mir, M. A. (2022) · Frontiers in Neuroscience · doi:10.3389/fnins.2022.884345 · Cited by 85
Mitochondrial Bioenergetics Is Altered in Fibroblasts from Patients with Sporadic Alzheimer's Disease
Maria Jose Perez, J., Ponce, D. P., Osorio‐Fuentealba, C., Behrens, M. I., & Quintanilla, R. A. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00553 · Cited by 81
Protective Effects of Pioglitazone on Cognitive Impairment and the Underlying Mechanisms: A Review of Literature
Alhowail, A. H., Alsikhan, R. S., Alsaud, M. M., Aldubayan, M. A., & Rabbani, S. I. (2022) · Drug Design Development and Therapy · doi:10.2147/dddt.s367229 · Cited by 84
Longitudinal Assessment of Tau Pathology in Patients with Alzheimer’s Disease Using [18F]THK-5117 Positron Emission Tomography
Ishiki, A., Okamura, N., Furukawa, K., Furumoto, S., Harada, R., Tomita, N., Hiraoka, K., Watanuki, S., Ishikawa, Y., Tago, T., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0140311 · Cited by 77
Bioactive Food Abates Metabolic and Synaptic Alterations by Modulation of Gut Microbiota in a Mouse Model of Alzheimer’s Disease
Syeda, T., Sánchez‐Tapia, M., Pinedo‐Vargas, L., Granados, O., Cuervo-Zanatta, D., Rojas-Santiago, E., Díaz-Cintra, S. Y., Torres, N., & Perez‐Cruz, C. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-180556 · Cited by 80
AMPK activation does not enhance autophagy in neurons in contrast to MTORC1 inhibition: different impact on β-amyloid clearance
Benito‐Cuesta, I., Ordóñez‐Gutiérrez, L., & Wandosell, F. G. (2020) · Autophagy · doi:10.1080/15548627.2020.1728095 · Cited by 80
When Good Kinases Go Rogue: GSK3, p38 MAPK and CDKs as Therapeutic Targets for Alzheimer’s and Huntington’s Disease
D’Mello, S. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115911 · Cited by 80
Synaptic Mitochondria: An Early Target of Amyloid-β and Tau in Alzheimer’s Disease
Torres, A. K., Jara, C., Park-Kang, H. S., Polanco, C. M., Tapia, D., Alarcón, F., de la Peña, A., Llanquinao, J., Vargas-Mardones, G., Álvarez‐Indo, J., et al. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215139 · Cited by 80
Pyrazoline Containing Compounds as Therapeutic Targets for Neurodegenerative Disorders
Ahsan, M. J., Ali, A., Ali, A., Thiriveedhi, A., Bakht, M. A., Yusuf, M., Salahuddin, S., Afzal, O., & Altamimi, A. S. A. (2022) · ACS Omega · doi:10.1021/acsomega.2c05339 · Cited by 78
Discovery and validation of plasma proteomic biomarkers relating to brain amyloid burden by SOMAscan assay
Shi, L., Westwood, S., Baird, A. L., Winchester, L. M., Dobričić, V., Kilpert, F., Hong, S., Franke, A., Hye, A., Ashton, N. J., et al. (2019) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2019.06.4951 · Cited by 70
Nanocarrier mediated drug delivery as an impeccable therapeutic approach against Alzheimer’s disease
Taliyan, R., Kakoty, V., Sarathlal, K. C., Kharavtekar, S. S., Karennanavar, C. R., Choudhary, Y. K., Singhvi, G., Riadi, Y., Dubey, S. K., & Kesharwani, P. (2022) · Journal of Controlled Release · doi:10.1016/j.jconrel.2022.01.044 · Cited by 79
Signaling Mechanisms of Selective PPARγ Modulators in Alzheimer’s Disease
Govindarajulu, M., Pinky, P. D., Bloemer, J., Ghanei, N., Suppiramaniam, V. D., & Amin, R. (2018) · PPAR Research · doi:10.1155/2018/2010675 · Cited by 77
Commonalities between Copper Neurotoxicity and Alzheimer’s Disease
Patel, R., & Aschner, M. (2021) · Toxics · doi:10.3390/toxics9010004 · Cited by 73
Neurotransmission systems in Parkinson’s disease
Moghaddam, H. S., Zare-Shahabadi, A., Rahmani, F., & Rezaei, N. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2016-0068 · Cited by 78
Environment-Sensitive Near-Infrared Probe for Fluorescent Discrimination of Aβ and Tau Fibrils in AD Brain
Zhou, K., Yuan, C., Dai, B., Wang, K., Chen, Y., Ma, D., Dai, J., Liang, Y., Tan, H., & Cui, M. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b00672 · Cited by 73
Roflumilast ameliorates cognitive impairment in APP/PS1 mice via cAMP/CREB/BDNF signaling and anti-neuroinflammatory effects
Feng, H., Wang, C., He, W., Wu, X.-J., Li, S., Zeng, Z., Wei, M., & He, B. (2019) · Metabolic Brain Disease · doi:10.1007/s11011-018-0374-4 · Cited by 72
Therapeutic Actions of the Thiazolidinediones in Alzheimer’s Disease
Maria Jose Perez, J., & Quintanilla, R. A. (2015) · PPAR Research · doi:10.1155/2015/957248 · Cited by 75
Profiling donepezil template into multipotent hybrids with antioxidant properties
Mezeiová, E., Špilovská, K., Nepovimová, E., Górecki, L., Soukup, O., Doležal, R., Maliňák, D., Janočková, J., Jun, D., Kuča, K., et al. (2018) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.1080/14756366.2018.1443326 · Cited by 74
MicroRNA in Alzheimer’s disease revisited: implications for major neuropathological mechanisms
Dehghani, R., Rahmani, F., & Rezaei, N. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0042 · Cited by 72
Functionalised Carbon Nanotubes Enhance Brain Delivery of Amyloid-Targeting Pittsburgh Compound B (PiB)-Derived Ligands
Costa, P. M., Wang, J. T.-W., Morfin, J., Khanum, T., To, W., Sosabowski, J. K., Tóth, É., & Al‐Jamal, K. T. (2018) · Nanotheranostics · doi:10.7150/ntno.23125 · Cited by 72
Metal-involved theranostics: An emerging strategy for fighting Alzheimer’s disease
Wang, X., Wang, X., & Guo, Z. (2018) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2018.03.010 · Cited by 72
Mitochondrial Abnormalities and Synaptic Loss Underlie Memory Deficits Seen in Mouse Models of Obesity and Alzheimer’s Disease
Martins, I. V. A., Rivers‐Auty, J., Allan, S. M., & Lawrence, C. B. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160640 · Cited by 70
Low Phytanic Acid-Concentrated DHA Prevents Cognitive Deficit and Regulates Alzheimer Disease Mediators in an ApoE−/− Mice Experimental Model
Ruiz-Roso, M. B., Echeverry‐Alzate, V., Ruiz‐Roso, B., Quintela, J. C., Ballesteros, S., Lahera, V., Heras, N. D. L., López‐Moreno, J. A., & Martín‐Fernández, B. (2018) · Nutrients · doi:10.3390/nu11010011 · Cited by 70
Microbial BMAA elicits mitochondrial dysfunction, innate immunity activation, and Alzheimer’s disease features in cortical neurons
Silva, D. F., Candeias, E., Esteves, A. R., Magalhães, J. D., Ferreira, I. L., Nunes‐Costa, D., Rego, A. C., Empadinhas, N., & Cardoso, S. M. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-02004-y · Cited by 73
Dietary Polyphenols as Therapeutic Intervention for Alzheimer’s Disease: A Mechanistic Insight
Bukhari, S. N. A. (2022) · Antioxidants · doi:10.3390/antiox11030554 · Cited by 71
Caffeic acid loaded into engineered lipid nanoparticles for Alzheimer's disease therapy
Andrade, S., Pereira, M. D. C., & Loureiro, J. A. (2023) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2023.113270 · Cited by 71
Role of Fluid Biomarkers and PET Imaging in Early Diagnosis and its Clinical Implication in the Management of Alzheimer’s Disease
Hameed, S., Fuh, J., Senanarong, V., Ebenezer, E. G. M., Looi, I., Dominguez, J. C., Park, K. W., Karanam, A. K., & Simon, O. (2020) · Journal of Alzheimer s Disease Reports · doi:10.3233/adr-190143 · Cited by 69
Amyloid β-Targeted Metal Complexes for Potential Applications in Alzheimer's Disease
Liu, H., Qu, Y., & Wang, X. (2018) · Future Medicinal Chemistry · doi:10.4155/fmc-2017-0248 · Cited by 70
A Primer on the Evolution of Aducanumab: The First Antibody Approved for Treatment of Alzheimer’s Disease
Mukhopadhyay, S., & Banerjee, D. (2021) · Journal of Alzheimer s Disease · doi:10.3233/jad-215065 · Cited by 66
Synthesis and metabolism of methylglyoxal, S-D-lactoylglutathione and D-lactate in cancer and Alzheimer’s disease. Exploring the crossroad of eternal youth and premature aging
Lidia de, B. A. R. I., Atlante, A., Armeni, T., & Kalapos, M. P. (2019) · Ageing Research Reviews · doi:10.1016/j.arr.2019.100915 · Cited by 68
Thermodynamics and kinetics of the amyloid-β peptide revealed by Markov state models based on MD data in agreement with experiment
Paul, A., Samantray, S., Anteghini, M., Khaled, M., & Strodel, B. (2021) · Chemical Science · doi:10.1039/d0sc04657d · Cited by 67
Neuroprotective Effects of Metformin Through the Modulation of Neuroinflammation and Oxidative Stress
Reed, S., Taka, E., Darling‐Reed, S., & Soliman, K. F. A. (2025) · Cells · doi:10.3390/cells14141064 · Cited by 76
Amyloid β production is regulated by β2-adrenergic signaling-mediated post-translational modifications of the ryanodine receptor
Bussiere, R., Lacampagne, A., Reiken, S., Liu, X.-P., Scheuerman, V., Zalk, R., Martin, C., Checler, F., Marks, A., & Chami, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.743070 · Cited by 57
Deep Brain Stimulation for Alzheimer's Disease: Stimulation Parameters and Potential Mechanisms of Action
Luo, Y., Sun, Y., Tian, X., Zheng, X., Wang, X., Li, W., Wu, X., Shu, B., & Hou, W. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.619543 · Cited by 69
Differential Phenotypes of Myeloid-Derived Suppressor and T Regulatory Cells and Cytokine Levels in Amnestic Mild Cognitive Impairment Subjects Compared to Mild Alzheimer Diseased Patients
Page, A. Y. L., Garneau, H., Dupuis, G., Frost, E. H., Larbi, A., Witkowski, J. M., Pawelec, G., & Fülöp, T. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00783 · Cited by 67
Newly Developed Drugs for Alzheimer’s Disease in Relation to Energy Metabolism, Cholinergic and Monoaminergic Neurotransmission
Korábečný, J., Nepovimová, E., Cikánková, T., Špilovská, K., Vašková, L., Mezeiová, E., Kuča, K., & Hroudová, J. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2017.06.034 · Cited by 64
Curcumin improves memory deficits by inhibiting HMGB1‐RAGE/TLR4‐NF‐κB signalling pathway in APPswe/PS1dE9 transgenic mice hippocampus
Han, Y., Chen, R., Lin, Q., Liu, Y., Ge, W., Cao, H., & Li, J. (2021) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.16855 · Cited by 64
Synthesis and evaluation of frentizole-based indolyl thiourea analogues as MAO/ABAD inhibitors for Alzheimer’s disease treatment
Hroch, L., Guest, P. N., Benek, O., Soukup, O., Janočková, J., Doležal, R., Kuča, K., Aitken, L., Smith, T., Gunn‐Moore, F. J., et al. (2016) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2016.12.029 · Cited by 62
Early functional connectivity deficits and progressive microstructural alterations in the TgF344-AD rat model of Alzheimer’s Disease: A longitudinal MRI study
Anckaerts, C., Blockx, I., Summer, P., Michael, J., Hamaide, J., Kreutzer, C., Boutin, H., Couillard‐Després, S., Verhoye, M., & der Linden, A. V. (2018) · Neurobiology of Disease · doi:10.1016/j.nbd.2018.11.010 · Cited by 61
GSK-3β as a target for apigenin-induced neuroprotection against Aβ 25–35 in a rat model of Alzheimer's disease
Alireza, M. S., Nikbakht, F., Nia, H. H., Golab, F., Khadem, Y., Barati, M., & Vazifekhah, S. (2021) · Neuropeptides · doi:10.1016/j.npep.2021.102200 · Cited by 61
Aromatherapy and Aromatic Plants for the Treatment of Behavioural and Psychological Symptoms of Dementia in Patients with Alzheimer’s Disease: Clinical Evidence and Possible Mechanisms
Scuteri, D., Morrone, L. A., Rombolà, L., Avato, P., Bilia, A. R., Corasaniti, M. T., Sakurada, S., Sakurada, T., & Bagetta, G. (2017) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2017/9416305 · Cited by 63
Design, Synthesis, and Biological Evaluation of 1-Benzylamino-2-hydroxyalkyl Derivatives as New Potential Disease-Modifying Multifunctional Anti-Alzheimer’s Agents
Panek, D., Więckowska, A., Jończyk, J., Godyń, J., Bajda, M., Wichur, T., Pasieka, A., Knez, D., Pišlar, A. H., Korábečný, J., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00461 · Cited by 58
Role of Specialized Pro-resolving Mediators in Reducing Neuroinflammation in Neurodegenerative Disorders
Ponce, J., Ulu, A., Hanson, C., Cameron‐Smith, E., Bertoni, J. M., Wuebker, J., Fisher, A. L., Siu, K., Marmelat, V., Adamec, J., et al. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.780811 · Cited by 59
Glycogen Synthase Kinase 3β Involvement in Neuroinflammation and Neurodegenerative Diseases
Gianferrara, T., Cescon, E., Grieco, I., Spalluto, G., & Federico, S. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220216113517 · Cited by 58
The role of Cdk5‐mediated Drp1 phosphorylation in Aβ1‐42 induced mitochondrial fission and neuronal apoptosis
Guo, M., Shang, L., Hu, Y., Jiang, L., Wan, Y., Zhou, Q., Zhang, K., Liao, H., Yi, J., & Han, X. (2018) · Journal of Cellular Biochemistry · doi:10.1002/jcb.26680 · Cited by 56
Peptide‐Functionalized Prussian Blue Nanomaterial for Antioxidant Stress and NIR Photothermal Therapy against Alzheimer's Disease
Song, X., Ding, Q., Wei, W., Zhang, J., Sun, R., Yin, L., Liu, S., & Pu, Y. (2023) · Small · doi:10.1002/smll.202206959 · Cited by 54
Alzheimer’s disease in people with Down’s syndrome: the prospects for and the challenges of developing preventative treatments
Castro, P., Zaman, S. H., & Holland, A. J. (2016) · Journal of Neurology · doi:10.1007/s00415-016-8308-8 · Cited by 59
Molecular Insights into Destabilization of Alzheimer’s Aβ Protofibril by Arginine Containing Short Peptides: A Molecular Modeling Approach
Barale, S. S., Parulekar, R. S., Fandilolu, P. M., Dhanavade, M. J., & Sonawane, K. D. (2019) · ACS Omega · doi:10.1021/acsomega.8b02672 · Cited by 55
Self-citation
Synthesis and evaluation of novel GSK-3β inhibitors as multifunctional agents against Alzheimer's disease
Shi, X., Wu, J., Liu, P., & Liu, Z. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.02.001 · Cited by 55

Authors: Barage, S. H., & Sonawane, K. D.
Affiliations: Shivaji University (IN)
Corresponding author: Sonawane, Kailas D.
ORCID: Barage, Sagar H.
Sonawane, Kailas D.
Venue: Neuropeptides
Publisher: Elsevier BV
Published: 2015-08
Volume: 52
Pages: 1-18
ISSN: 0143-4179 (ISSN-L)
DOI: 10.1016/j.npep.2015.06.008
OpenAlex: W2099751992
Cited by: 579
References: 371
Citations by year: 2026: 22 · 2025: 57 · 2024: 75 · 2023: 69 · 2022: 58 · 2021: 67 · 2020: 59 · 2019: 58 · 2018: 51 · 2017: 33 · 2016: 24 · 2015: 5
FWCI: 4.66
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Neuropeptides (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Health Sciences › Medicine › Pharmacology (medical) › Cholinesterase and Neurodegenerative Diseases
Keywords: Alzheimer's disease, amyloid hypothesis, amyloid-beta, amyloid plaques, tau protein, cerebrospinal fluid biomarkers, cholinergic neurotransmission, neurodegeneration, Alzheimer's disease therapeutics, genetic risk factors
MeSH terms: Acetylcholine, Alzheimer Disease, Animals, Brain, Humans, Signal Transduction, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Neurofibrillary Tangles, tau Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Amyloid cascade hypothesis: Pathogenesis and therapeutic strategies in Alzheimer's disease

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks