The Role of Caspases in Alzheimer’s Disease: Pathophysiology Implications and Pharmacologic Modulation
Abstract
Alzheimer's disease (AD) is the most common neurodegenerative disorder worldwide. Although the main cause of the onset and development of AD is not known yet, neuronal death due to pathologic changes such as amyloid-β (Aβ) deposition, tau aggregation, neuroinflammation, oxidative stress, and calcium dyshomeostasis are considered to be the main cause. At the present, there is no cure for this insidious disorder. However, accurate identification of molecular changes in AD can help provide new therapeutic goals. Caspases are a group of proteases which are known because of their role in cellular apoptosis. In addition, different caspases are involved in other cellular responses to the environment, such as induction of inflammation. Emerging evidence suggest that these proteases play a central role in AD pathophysiology due to their role in the processing of amyloid-β protein precursor, tau cleavage, and neuroinflammation. Therefore, it seems that targeting caspases may be a suitable therapeutic option to slow the progression of AD. This review focuses on the role of caspases in AD pathophysiology and introduce results from studies targeted caspases in different models of AD.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
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?
Alzheimer's disease (AD) is a progressive, multifactorial, unremitting neurodegenerative disease characterized by memory loss, personality changes, and cognitive impairment.
“Alzheimer's disease (AD) is a progressive, multifactorial, and unremitting neurodegenerative disease characterized by memory loss, personality changes, and cognitive impairment.”
From Unlocking the Therapeutic Potential of Medicinal Plants for Alzheimer’s Disease: Preclinical to Clinical Trial Insights (2023) · cites this paper as [27]
Alzheimer's disease is the most prevalent form of dementia worldwide.
“The most prevalent form of dementia worldwide is Alzheimer's disease (AD), a progressive neurological condition with a high social and caregiver cost.”
From Unlocking the Therapeutic Potential of Medicinal Plants for Alzheimer’s Disease: Preclinical to Clinical Trial Insights (2023) · cites this paper as [27]
Alzheimer's disease is an irreversible neurodegenerative disorder marked by occasional unusual behavior, memory loss, and cognitive impairment.
“It is an irreversible neurodegenerative disorder marked by occasional unusual behavior, memory loss, and cognitive impairment.”
From Unlocking the Therapeutic Potential of Medicinal Plants for Alzheimer’s Disease: Preclinical to Clinical Trial Insights (2023) · cites this paper as [27]
Cites
3 retracted
Ahmad, S., Jo, M. H., Ikram, M. A., Khan, A., & Kim, M. O. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179583 · Cited by 106 · see citing works
RetractedCarvedilol protection against endogenous Aβ-induced neurotoxicity in N2a cells
Liu, J., & Wang, M. (2018) · Cell Stress and Chaperones · doi:10.1007/s12192-018-0881-6 · Cited by 26 · see citing works
RetractedSharma, A. K., & Rohrer, B. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.a117.401037 · Cited by 5 · see citing works
RetractedNeuroinflammation in Alzheimer's disease
Heneka, M. T., Carson, M. J., Khoury, J. E., Landreth, G. E., Brosseron, F., Feinstein, D. L., Jacobs, A. H., Wyss-Coray, T., Vitorica, J., Ransohoff, R. M., et al. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(15)70016-5 · Cited by 6,226 · see citing works
A Unique Microglia Type Associated with Restricting Development of Alzheimer’s Disease
Keren-Shaul, H., Spinrad, A., Weiner, A., Matcovitch-Natan, O., Dvir-Szternfeld, R., Ulland, T. K., David, E., Baruch, K., Lara-Astaiso, D., Toth, B., et al. (2017) · Cell · doi:10.1016/j.cell.2017.05.018 · Cited by 5,493 · see citing works
Inflammation and Alzheimer’s disease
Akiyama, H. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00124-x · Cited by 4,514 · see citing works
Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676 · see citing works
Bjørkøy, G., Lamark, T., Brech, A., Outzen, H., Perander, M., Øvervatn, A., Stenmark, H., & Johansen, T. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200507002 · Cited by 3,276 · see citing works
NLRP3 is activated in Alzheimer’s disease and contributes to pathology in APP/PS1 mice
Heneka, M. T., Kummer, M. P., Stutz, A., Delekate, A., Schwartz, S., Vieira-Saecker, A., Griep, A., Axt, D., Remus, A., Tzeng, T.-C., et al. (2013) · Nature · doi:10.1038/nature11729 · Cited by 2,898 · see citing works
Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes
Micheau, O., & Tschopp, J. (2003) · Cell · doi:10.1016/s0092-8674(03)00521-x · Cited by 2,738 · see citing works
Ji, Y. (1993) · Cell · doi:10.1016/0092-8674(93)90485-9 · Cited by 2,497 · see citing works
PI3K/Akt signalling pathway and cancer
Vara, J. Á. F., Casado, E., de Castro, J., Cejas, P., Belda-Iniesta, C., & González-Barón, M. (2003) · Cancer Treatment Reviews · doi:10.1016/j.ctrv.2003.07.007 · Cited by 2,446 · see citing works
Lu, T. X., & Rothenberg, M. E. (2018) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2017.08.034 · Cited by 2,425 · see citing works
Human ICE/CED-3 Protease Nomenclature
Alnemri, E. S., Livingston, D. J., Nicholson, D. W., Salvesen, G. S., Thornberry, N. A., Wong, W. W., & Yuan, J. (1996) · Cell · doi:10.1016/s0092-8674(00)81334-3 · Cited by 2,371 · see citing works
A Combinatorial Approach Defines Specificities of Members of the Caspase Family and Granzyme B
Thornberry, N. A., Rano, T. A., Peterson, E. P., Rasper, D., Timkey, T., Garcia-Calvo, M. M., Houtzager, V. M., Nordstrom, P. A., Roy, S., Vaillancourt, J. P., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.29.17907 · Cited by 2,072 · see citing works
The role of autophagy in neurodegenerative disease
Nixon, R. A. (2013) · Nature Medicine · doi:10.1038/nm.3232 · Cited by 2,059 · see citing works
Neuroinflammation in Alzheimer's disease: current evidence and future directions
Calsolaro, V., & Edison, P. (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.02.010 · Cited by 1,726 · see citing works
Steen, E., Terry, B. M., J. Rivera, E., Cannon, J. L., Neely, T. R., Tavares, R., Xu, X. J., Wands, J. R., & de la Monte, S. M. (2005) · Journal of Alzheimer's Disease · doi:10.3233/jad-2005-7107 · Cited by 1,703 · see citing works
Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study
Nixon, R. A., Wegiel, J., Kumar, A., Yu, W. H., Peterhoff, C., Cataldo, A., & Cuervo, A. M. (2005) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/64.2.113 · Cited by 1,588 · see citing works
NLRP3 inflammasome activation drives tau pathology
Ising, C., Venegas, C., Zhang, S., Scheiblich, H., Schmidt, S. V., Vieira-Saecker, A., Schwartz, S., Albasset, S., McManus, R. M., Tejera, D., et al. (2019) · Nature · doi:10.1038/s41586-019-1769-z · Cited by 1,487 · see citing works
Propagation of Tau Pathology in a Model of Early Alzheimer's Disease
de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427 · see citing works
Plasma membrane translocation of trimerized MLKL protein is required for TNF-induced necroptosis
Cai, Z., Jitkaew, S., Zhao, J., Chiang, H.-C., Choksi, S., Liu, J., Ward, Y., Wu, L.-G., & Liu, Z.-G. (2014) · Nature Cell Biology · doi:10.1038/ncb2883 · Cited by 1,322 · see citing works
Caspases in Cell Death, Inflammation, and Disease
Opdenbosch, N. V., & Lamkanfi, M. (2019) · Immunity · doi:10.1016/j.immuni.2019.05.020 · Cited by 1,230 · see citing works
Clinical Neurology and Epidemiology of the Major Neurodegenerative DiseasesPreprint
Erkkinen, M. G., Kim, M., & Geschwind, M. D. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033118 · Cited by 1,152 · see citing works
A Unified Model for Apical Caspase Activation
Boatright, K. M., Renatus, M., Scott, F. L., Sperandio, S., Shin, H., Pedersen, I. M., Ricci, J., Edris, W. A., Sutherlin, D. P., Green, D. R., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00051-0 · Cited by 963 · see citing works
Mebratu, Y. A., & Tesfaigzi, Y. (2009) · Cell Cycle · doi:10.4161/cc.8.8.8147 · Cited by 959 · see citing works
Du, H., Guo, L., Fang, F., Chen, D., Sosunov, A. A., McKhann, G. M., Yan, Y., Wang, C., Zhang, H., Molkentin, J. D., et al. (2008) · Nature Medicine · doi:10.1038/nm.1868 · Cited by 935 · see citing works
De Felice, F. G., Velasco, P. T., Lambert, M. P., Viola, K., Fernandez, S. J., Ferreira, S. T., & Klein, W. L. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m607483200 · Cited by 882 · see citing works
Molecular Interplay between Mammalian Target of Rapamycin (mTOR), Amyloid-β, and Tau
Caccamo, A., Majumder, S., Richardson, A., Strong, R., & Oddo, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100420 · Cited by 881 · see citing works
Devi, L., Prabhu, B. M., Galati, D. F., Avadhani, N. G., & Anandatheerthavarada, H. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.1469-06.2006 · Cited by 792 · see citing works
The Epidemiology of Alzheimer's Disease Modifiable Risk Factors and Prevention
Zhang, X.-X., Tian, Y., Wang, Z.-T., Ma, Y.-H., Tan, L., & Yu, J.-T. (2021) · The Journal of Prevention of Alzheimer's Disease · doi:10.14283/jpad.2021.15 · Cited by 789 · see citing works
Gervais, F. G., Xu, D., Robertson, G. S., Vaillancourt, J. P., Zhu, Y., Huang, J., LeBlanc, A. C., Smith, D., Rigby, M., Shearman, M. S., et al. (1999) · Cell · doi:10.1016/s0092-8674(00)80748-5 · Cited by 784 · see citing works
Activation of the apoptotic protease CPP32 by cytotoxic T-cell-derived granzyme B
Darmon, A. J., Nicholson, D. W., & Bleackley, R. C. (1995) · Nature · doi:10.1038/377446a0 · Cited by 707 · see citing works
Hansson Petersen, C. A., Alikhani, N., Behbahani, H., Wiehager, B., Pavlov, P. F., Alafuzoff, I., Leinonen, V., Ito, A., Winblad, B., Glaser, E., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0806192105 · Cited by 693 · see citing works
ERK1/2 MAP kinases in cell survival and apoptosis
Lu, Z., & Xu, S. (2006) · IUBMB Life · doi:10.1080/15216540600957438 · Cited by 654 · see citing works
Mitochondrial Dysfunction and Oxidative Stress in Alzheimer’s Disease
Misrani, A., Tabassum, S., & Yang, L. (2021) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2021.617588 · Cited by 654 · see citing works
Caspase signalling controls microglia activation and neurotoxicity
Burguillos, M. A., Deierborg, T., Kavanagh, E., Persson, A., Hajji, N., Garcia-Quintanilla, A., Cano, J., Brundin, P., Englund, E., Venero, J. L., et al. (2011) · Nature · doi:10.1038/nature09788 · Cited by 585 · see citing works
Crystal structure of the cysteine protease interleukin-1β-converting enzyme: A (p20/p10)2 homodimer
Walker, N. P. C., Talanian, R. V., Brady, K. D., Dang, L. C., Bump, N. J., Ferenza, C. R., Franklin, S., Ghayur, T., Hackett, M. C., Hammill, L., et al. (1994) · Cell · doi:10.1016/0092-8674(94)90303-4 · Cited by 576 · see citing works
Caspase-3 triggers early synaptic dysfunction in a mouse model of Alzheimer's disease
D'Amelio, M., Cavallucci, V., Middei, S., Marchetti, C., Pacioni, S., Ferri, A., Diamantini, A., De Zio, D., Carrara, P., Battistini, L., et al. (2011) · Nature Neuroscience · doi:10.1038/nn.2709 · Cited by 572 · see citing works
Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
Rissman, R. A., Poon, W. W., Blurton-Jones, M., Oddo, S., Torp, R., Vitek, M. P., LaFerla, F. M., Rohn, T. T., & Cotman, C. W. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200420640 · Cited by 543 · see citing works
Caspase-2 Induces Apoptosis by Releasing Proapoptotic Proteins from Mitochondria
Guo, Y., Srinivasula, S. M., Druilhe, A., Fernandes‐Alnemri, T., & Alnemri, E. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108029200 · Cited by 521 · see citing works
Deficient brain insulin signalling pathway in Alzheimer's disease and diabetes
Liu, Y. M., Liu, F., Grundke, I., Iqbal, K., & Gong, C. (2011) · The Journal of Pathology · doi:10.1002/path.2912 · Cited by 505 · see citing works
Caspase-9 Can Be Activated without Proteolytic Processing
Stennicke, H. R., Deveraux, Q. L., Humke, E. W., Reed, J. C., Dixit, V. M., & Salvesen, G. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.13.8359 · Cited by 497 · see citing works
A current view on Tau protein phosphorylation in Alzheimer's disease
Wegmann, S., Biernat, J., & Mandelkow�, E. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.03.003 · Cited by 464 · see citing works
Ahmed, Z., Cooper, J., Murray, T. K., Garn, K., McNaughton, E., Clarke, H., Parhizkar, S., Ward, M. A., Cavallini, A., Jackson, S., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1254-6 · Cited by 460 · see citing works
Aβ Secretion and Plaque Formation Depend on Autophagy
Nilsson, P., Loganathan, K., Sekiguchi, M., Matsuba, Y., Hui, K., Tsubuki, S., Tanaka, M., Iwata, N., Saito, T., & Saido, T. C. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.08.042 · Cited by 459 · see citing works
Stadelmann, C., Deckwerth, T., Srinivasan, A., Bancher, C., Brück, W., Jellinger, K. A., & Lassmann, H. (1999) · American Journal of Pathology · doi:10.1016/s0002-9440(10)65460-0 · Cited by 449 · see citing works
Calvo-Rodríguez, M., Hou, S. S., Snyder, A. C., Kharitonova, E. K., Russ, A., Das, S., Fan, Z., Muzikansky, A., Garcı́a-Alloza, M., Serrano‐Pozo, A., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16074-2 · Cited by 432 · see citing works
Targeting the extrinsic apoptosis pathway in cancer
Ashkenazi, A. (2008) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2008.04.001 · Cited by 419 · see citing works
Prevention of Constitutive TNF Receptor 1 Signaling by Silencer of Death Domains
Jiang, Y., Woronicz, J. D., Liu, W., & Goeddel, D. V. (1999) · Science · doi:10.1126/science.283.5401.543 · Cited by 415 · see citing works
Regulation of the Intrinsic Apoptosis Pathway by Reactive Oxygen Species
Wu, C.-C., & Bratton, S. B. (2012) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4905 · Cited by 410 · see citing works
Bratton, S. B., Walker, G., Srinivasula, S. M., Sun, X., Butterworth, M., Alnemri, E. S., & Cohen, G. M. (2001) · The EMBO Journal · doi:10.1093/emboj/20.5.998 · Cited by 406 · see citing works
Targeting apoptotic caspases in cancer
Boice, A., & Bouchier‐Hayes, L. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2020.118688 · Cited by 402 · see citing works
Altered Insulin Signaling in Alzheimer’s Disease Brain – Special Emphasis on PI3K-Akt Pathway
Gabbouj, S., Ryhänen, S., Marttinen, M., Wittrahm, R., Takalo, M., Kemppainen, S., Martiskainen, H., Tanila, H., Haapasalo, A., Hiltunen, M., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00629 · Cited by 401 · see citing works
Young, M. M., Takahashi, Y., Khan, O. A., Park, S., Hori, T., Yun, J. K., Sharma, A. K., Amin, S., Hu, C., Zhang, J., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.309104 · Cited by 372 · see citing works
Dickens, L. S., Boyd, R. S., Jukes-Jones, R., Hughes, M. A., Robinson, G. L., Fairall, L., Schwabe, J. W. R., Cain, K., & MacFarlane, M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.004 · Cited by 349 · see citing works
The role of cell signalling in the crosstalk between autophagy and apoptosis
Booth, L. A., Tavallai, S., Hamed, H. A., Cruickshanks, N. A., & Dent, P. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.11.028 · Cited by 340 · see citing works
FADD and caspase-8 control the outcome of autophagic signaling in proliferating T cells
Bell, B. D., Leverrier, S., Weist, B. M., Newton, R. H., Arechiga, A. F., Luhrs, K. A., Morrissette, N. S., & Walsh, C. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0808597105 · Cited by 290 · see citing works
Insulin signaling pathway and related molecules: Role in neurodegeneration and Alzheimer's disease
Akhtar, A., & Sah, S. P. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104707 · Cited by 290 · see citing works
Flores, J., Noël, A., Foveau, B., Lynham, J., Lecrux, C., & LeBlanc, A. C. (2018) · Nature Communications · doi:10.1038/s41467-018-06449-x · Cited by 288 · see citing works
Hamano, T., Gendron, T. F., Causevic, E., Yen, S., Lin, W., Isidoro, C., DeTure, M., & Ko, L. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06084.x · Cited by 283 · see citing works
Piras, A., Collin, L., Grüninger, F., Graff, C., & Rönnbäck, A. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0292-9 · Cited by 271 · see citing works
Betin, V. M. S., & Lane, J. D. (2009) · Journal of Cell Science · doi:10.1242/jcs.046250 · Cited by 261 · see citing works
Su, J. H., Zhao, M., Anderson, A. J., Srinivasan, A. N., & Cotman, C. W. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02018-2 · Cited by 260 · see citing works
The multifaceted nature of amyloid precursor protein and its proteolytic fragments: friends and foes
Nhan, H. S., Chiang, K., & Koo, E. H. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1347-2 · Cited by 256 · see citing works
WD-40 Repeat Region Regulates Apaf-1 Self-association and Procaspase-9 Activation
Hu, Y., Ding, L., Spencer, D. M., & Núñez, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.50.33489 · Cited by 256 · see citing works
Caspases: A Molecular Switch Node in the Crosstalk between Autophagy and Apoptosis
Wu, H., Che, X., Zheng, Q., Wu, A., Pan, K., Shao, A., Wu, Q., Zhang, J., & Hong, Y. (2014) · International Journal of Biological Sciences · doi:10.7150/ijbs.9719 · Cited by 255 · see citing works
Beclin 1 cleavage by caspase-3 inactivates autophagy and promotes apoptosis
Zhu, Y., Zhao, L., Liu, L., Gao, P., Tian, W., Wang, X., Jin, H., Xu, H., & Chen, Q. (2010) · Protein & Cell · doi:10.1007/s13238-010-0048-4 · Cited by 254 · see citing works
Mitochondria and Calcium in Alzheimer’s Disease: From Cell Signaling to Neuronal Cell Death
Calvo-Rodriguez, M., & Bacskai, B. J. (2021) · Trends in Neurosciences · doi:10.1016/j.tins.2020.10.004 · Cited by 254 · see citing works
Crystal Structure of a Procaspase-7 Zymogen
Chai, J., Wu, Q. Y., Shiozaki, E. N., Srinivasula, S. M., Alnemri, E. S., & Shi, Y. (2001) · Cell · doi:10.1016/s0092-8674(01)00544-x · Cited by 246 · see citing works
Caspase-9 Activation and Caspase Cleavage of tau in the Alzheimer's Disease Brain
Rohn, T. T., Rissman, R. A., Davis, M. C., Kim, Y., Cotman, C. W., & Head, E. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0549 · Cited by 242 · see citing works
Kelly, B. L., & Ferreira, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605081200 · Cited by 240 · see citing works
Caspase-mediated cleavage of ATG6/Beclin-1 links apoptosis to autophagy in HeLa cells
Cho, D., Jo, Y. K., Hwang, J. J., Lee, Y. M., Roh, S. A., & Kim, J. C. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.09.004 · Cited by 230 · see citing works
Structural basis for the activation of human procaspase-7
Riedl, S. J., Fuentes‐Prior, P., Renatus, M., Kairies, N., Krapp, S., Huber, R., Salvesen, G. S., & Bode, W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.221580098 · Cited by 220 · see citing works
Sanz‐Blasco, S., Valero, R. A., Rodríguez‐Crespo, I., Villalobos, C., & Núñez, L. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002718 · Cited by 219 · see citing works
The in vitro cleavage of the hAtg proteins by cell death proteases
Norman, J., Cohen, G., & Bampton, E. (2010) · Autophagy · doi:10.4161/auto.6.8.13337 · Cited by 209 · see citing works
Caspase-3 Is Enriched in Postsynaptic Densities and Increased in Alzheimer's Disease
Louneva, N., Cohen, J. W., Han, L., Talbot, K., Wilson, R. S., Bennett, D. A., Trojanowski, J. Q., & Arnold, S. E. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.080434 · Cited by 207 · see citing works
Recent developments in Alzheimer's disease therapeutics
Rafii, M., & Aisen, P. (2009) · BMC Medicine · doi:10.1186/1741-7015-7-7 · Cited by 204 · see citing works
Molecular Mechanisms and Genetics of Oxidative Stress in Alzheimer’s Disease
Cioffi, F., Adam, R. H. I., & Broersen, K. (2019) · Journal of Alzheimer s Disease · doi:10.3233/jad-190863 · Cited by 204 · see citing works
The biochemical mechanism of caspase-2 activation
Baliga, B. C., Read, S. H., & Kumar, S. (2004) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401492 · Cited by 200 · see citing works
Schleich, K., Warnken, U., Fricker, N., Öztürk, S., Richter, P., Kammerer, K., Schnölzer, M., Krammer, P. H., & Lavrik, I. N. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.006 · Cited by 198 · see citing works
Fu, T.-M., Li, Y., Lu, A., Li, Z., Vajjhala, P. R., Cruz, A. C., Srivastava, D. B., DiMaio, F., Penczek, P. A., Siegel, R. M., et al. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.09.009 · Cited by 196 · see citing works
Beta-amyloid activates NLRP3 inflammasome via TLR4 in mouse microglia
Liu, Y., Dai, Y., Li, Q., Chen, C., Chen, H., Song, Y., Hua, F., & Zhang, Z. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.135279 · Cited by 183 · see citing works
MicroRNA-132 provides neuroprotection for tauopathies via multiple signaling pathways
Fatimy, R. E., Li, S., Chen, Z., Mushannen, T., Gongala, S., Wei, Z., Balu, D. T., Rabinovsky, R., Cantlon, A., Elkhal, A., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1880-5 · Cited by 172 · see citing works
Activation of Caspase-8 in the Alzheimer's Disease Brain
Rohn, T. T., Head, E., Nesse, W. H., Cotman, C. W., & Cribbs, D. H. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2001.0449 · Cited by 171 · see citing works
A primer on caspase mechanisms
Ramirez, M. L. G., & Salvesen, G. S. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.01.002 · Cited by 166 · see citing works
Fu, W., Luo, H., Parthasarathy, S., & Mattson, M. P. (1998) · Neurobiology of Disease · doi:10.1006/nbdi.1998.0192 · Cited by 164 · see citing works
The γ-secretase complex: from structure to function
Zhang, X., Li, Y., Xu, H., & Zhang, Y. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00427 · Cited by 164 · see citing works
Correlation between Caspase Activation and Neurofibrillary Tangle Formation in Alzheimer’s Disease
Rohn, T. T., Head, E., Su, J. H., Anderson, A. J., Bahr, B. A., Cotman, C. W., & Cribbs, D. H. (2001) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63957-0 · Cited by 164 · see citing works
Neuronal Apoptosis and Autophagy Cross Talk in Aging PS/APP Mice, a Model of Alzheimer's Disease
Yang, D., Kumar, A. R., Stavrides, P. H., Peterson, J. N., Peterhoff, C., Pawlik, M., Levy, E., Cataldo, A. M., & Nixon, R. A. (2008) · American Journal Of Pathology · doi:10.2353/ajpath.2008.071176 · Cited by 164 · see citing works
Depletion of Beclin-1 due to proteolytic cleavage by caspases in the Alzheimer's disease brain
Rohn, T. T., Wirawan, E., Brown, R. J., Harris, J. R., Masliah, E., & Vandenabeele, P. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.11.003 · Cited by 160 · see citing works
Zheng, F., Qin, C., Chang, Y. S., & Zhang, J. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.014 · Cited by 156 · see citing works
Genistein ameliorates β-amyloid peptide (25–35)-induced hippocampal neuronal apoptosis
Zeng, H., Chen, Q., & Zhao, B. (2003) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2003.10.018 · Cited by 155 · see citing works
Che, H., Li, Q., Zhang, T., Wang, D., Yang, L., Xu, J., Yanagita, T., Xue, C., Chang, Y., & Wang, Y. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b00988 · Cited by 152 · see citing works
Pagliarini, V., Wirawan, E., Romagnoli, A., Ciccosanti, F., Lisi, G., Lippens, S., Cecconi, F., Fimia, G. M., Vandenabeele, P., Corazzari, M., et al. (2012) · Cell Death and Differentiation · doi:10.1038/cdd.2012.27 · Cited by 149 · see citing works
MacManus, A., Ramsden, M., Murray, M., Henderson, Z., Pearson, H. A., & Campbell, V. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.7.4713 · Cited by 137 · see citing works
Yoshiyama, Y., Kojima, A., Ishikawa, C., & Arai, K. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-100681 · Cited by 132 · see citing works
Liu, Q., & Zhao, B. (2004) · British Journal of Pharmacology · doi:10.1038/sj.bjp.0705653 · Cited by 130 · see citing works
Lai, A. Y., & McLaurin, J. (2010) · International Journal of Alzheimer s Disease · doi:10.4061/2011/548380 · Cited by 130 · see citing works
Inflammasomes: Molecular Regulation and Implications for Metabolic and Cognitive Diseases
Choi, A. J. S., & Ryter, S. W. (2014) · Molecules and Cells · doi:10.14348/molcells.2014.0104 · Cited by 130 · see citing works
Zhong, X., Liu, M., Yao, W., Du, K., He, M., Jin, X., Jiao, L., Ma, G., Wei, B., & Wei, M. (2019) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.201801230 · Cited by 129 · see citing works
NLRP3 inflammasome as a novel therapeutic target for Alzheimer’s disease
Zhang, Y., Dong, Z., & Song, W. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0145-7 · Cited by 128 · see citing works
Minocycline reduces the development of abnormal tau species in models of Alzheimer's disease
Noble, W., Garwood, C., Stephenson, J., Kinsey, A. M., Hanger, D., & Anderton, B. (2009) · The FASEB Journal · doi:10.1096/fj.08-113795 · Cited by 123 · see citing works
Cieri, D., Vicario, M., Vallese, F., D’Orsi, B., Berto, P., Grinzato, A., Catoni, C., Stefani, D. D., Rizzuto, R., Brini, M., et al. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.07.011 · Cited by 122 · see citing works
Eldufani, J., & Blaise, G. A. (2019) · Alzheimer s & Dementia Translational Research & Clinical Interventions · doi:10.1016/j.trci.2019.03.004 · Cited by 121 · see citing works
Lower cerebral blood flow is associated with faster cognitive decline in Alzheimer’s disease
Benedictus, M. R., Leeuwis, A. E., Binnewijzend, M. A. A., Kuijer, J. P. A., Scheltens, P., Barkhof, F., van der Flier, W. M., & Prins, N. D. (2016) · European Radiology · doi:10.1007/s00330-016-4450-z · Cited by 118 · see citing works
Adrain, C., Slee, E. A., Harte, M. T., & Martin, S. J. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.20855 · Cited by 117 · see citing works
Liu, M., Chen, F., Sha, L., Wang, S., Lin, T., Yao, L., He, M., Yao, Z., Liu, H., Zhu, Z., et al. (2013) · Molecular Neurobiology · doi:10.1007/s12035-013-8608-2 · Cited by 117 · see citing works
Glycogen Synthase Kinase 3β Induces Caspase-cleaved Tau Aggregation in Situ
Cho, J., & Johnson, G. V. W. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403364200 · Cited by 116 · see citing works
Huang, W., Li, Z., Zhao, L., & Zhao, W. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.05.060 · Cited by 113 · see citing works
Di, J., Cohen, L. S., Corbo, C. P., Phillips, G. R., Idrissi, A. E., & Alonso, A. D. C. (2016) · Scientific Reports · doi:10.1038/srep20833 · Cited by 112 · see citing works
Caspase cleavage of the amyloid precursor protein modulates amyloid β‐protein toxicity
Lu, D. C.-T., Soriano, S., Bredesen, D. E., & Koo, E. H. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02059.x · Cited by 110 · see citing works
Chiang, M., Nicol, C. J. B., & Cheng, Y. (2017) · Neurochemistry International · doi:10.1016/j.neuint.2017.10.002 · Cited by 109 · see citing works
Crude caffeine reduces memory impairment and amyloid β1–42 levels in an Alzheimer’s mouse model
Chu, Y.-F., Chang, W.-H., Black, R. M., Liu, J.-R., Sompol, P., Chen, Y., Wei, H., Zhao, Q., & Cheng, I. H. (2012) · Food Chemistry · doi:10.1016/j.foodchem.2012.04.148 · Cited by 106 · see citing works
Neuroinflammation in Alzheimer’s Disease: from Pathogenesis to a Therapeutic Target
Pimplikar, S. W. (2014) · Journal of Clinical Immunology · doi:10.1007/s10875-014-0032-5 · Cited by 103 · see citing works
Caspase activation in the limbic cortex of subjects with early Alzheimer's disease
Gastard, M. C., Troncoso, J. C., & Koliatsos, V. E. (2003) · Annals of Neurology · doi:10.1002/ana.10680 · Cited by 101 · see citing works
A Complex between Atg7 and Caspase-9
Han, J., Hou, W., Goldstein, L. A., Stolz, D. B., Watkins, S. C., & Rabinowich, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.536854 · Cited by 101 · see citing works
Tau inhibits mitochondrial calcium efflux and makes neurons vulnerable to calcium-induced cell death
Britti, E., Ros, J., Esteras, N., & Abramov, A. Y. (2019) · Cell Calcium · doi:10.1016/j.ceca.2019.102150 · Cited by 101 · see citing works
Lai, J., Hu, M., Wang, H., Hu, M. Y., Long, Y., Miao, M., Li, J.-C., Wang, X., Kong, L., & Hong, H. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.01.011 · Cited by 98 · see citing works
Mechanism of amyloidogenesis: nucleation-dependent fibrillation versus double-concerted fibrillation
Bhak, G., Choe, Y., & Paik, S.-R. (2009) · BMB Reports · doi:10.5483/bmbrep.2009.42.9.541 · Cited by 95 · see citing works
TREM2 in Alzheimer’s Disease: Microglial Survival and Energy Metabolism
Zheng, H., Cheng, B., Li, Y., Li, X., Chen, X., & Zhang, Y.-W. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00395 · Cited by 94 · see citing works
Melatonin attenuates amyloid beta25–35-induced apoptosis in mouse microglial BV2 cells
Jang, M.-H., Jung, S.-B., Lee, M., Kim, C., Oh, Y.-T., Kang, I., Kim, J., & Kim, E. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.01.003 · Cited by 93 · see citing works
Park, G., Nhan, H. S., Tyan, S.-H., Kawakatsu, Y., Zhang, C., Navarro, M., & Koo, E. H. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107839 · Cited by 92 · see citing works
Khezri, M. R., Yousefi, K., Esmaeili, A., & Ghasemnejad‐Berenji, M. (2022) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-022-01191-x · Cited by 92 · see citing works
Effect of phosphodiesterase-5 inhibition on apoptosis and beta amyloid load in aged mice
Puzzo, D., Loreto, C., Giunta, S., Musumeci, G., Frasca, G., Podda, M. V., Arancio, O., & Palmeri, A. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.09.002 · Cited by 88 · see citing works
Wang, J., Sun, B.-L., Xiang, Y., Tian, D.-Y., Zhu, C., Li, W.-W., Liu, Y.-H., Bu, X.-L., Shen, L.-L., Jin, W.-S., et al. (2020) · Translational Psychiatry · doi:10.1038/s41398-020-00918-y · Cited by 87 · see citing works
Early Stages of Pathogenesis in Memory Impairment during Normal Senescence and Alzheimer's Disease
Daulatzai, M. A. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-1374 · Cited by 82 · see citing works
García–Tsao, G., Fuchs, M. A., Shiffman, M. L., Borg, B. B., Pyrsopoulos, N., Shetty, K., Gallegos-Orozco, J. F., Reddy, K. R., Feyssa, E. L., Chan, J. L., et al. (2018) · Hepatology · doi:10.1002/hep.30199 · Cited by 82 · see citing works
Gu, X., CAI, Z., Cai, M., Liu, K., Liu, D., ZHANG, Q., Tan, J. H., & Ma, Q. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.4805 · Cited by 81 · see citing works
Cacidases: caspases can cleave after aspartate, glutamate and phosphoserine residues
Seaman, J. E., Julien, O., Lee, P. S., Rettenmaier, T. J., Thomsen, N. D., & Wells, J. A. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2016.62 · Cited by 81 · see citing works
Sun, Q., Gao, W., Loughran, P., Shapiro, R., Fan, J., Billiar, T. R., & Scott, M. J. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.426791 · Cited by 80 · see citing works
Mechanisms of action of amyloid-beta and its precursor protein in neuronal cell death
Leong, Y. Q., Ng, K. Y., Chye, S. M., Ling, A. P. K., & Koh, R. Y. (2019) · Metabolic Brain Disease · doi:10.1007/s11011-019-00516-y · Cited by 78 · see citing works
The Role of Aβ-Induced Calcium Dysregulation in the Pathogenesis of Alzheimer's Disease
Small, D. H., Gasperini, R., Vincent, A. J., Hung, A. C., & Foa, L. C. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-0951 · Cited by 75 · see citing works
A nonapoptotic role for CASP2/caspase 2
Tiwari, M., Sharma, L. K., Vanegas, D., Callaway, D. A., Bai, Y., Lechleiter, J. D., & Herman, B. A. (2014) · Autophagy · doi:10.4161/auto.28528 · Cited by 75 · see citing works
Challenges in Neuronal Apoptosis
Jellinger, K. A. (2006) · Current Alzheimer Research · doi:10.2174/156720506778249434 · Cited by 74 · see citing works
You, M., Savaraj, N., Kuo, M. T., Wangpaichitr, M., Varona-Santos, J., Wu, C., Nguyen, D. M., & Feun, L. G. (2012) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-012-1518-1 · Cited by 72 · see citing works
Tiwari, M., Lopez‐Cruzan, M., MORGAN, W. W., & Herman, B. A. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.163824 · Cited by 71 · see citing works
Liu, X., Xu, K., Yan, M., Wang, Y., & Zheng, X. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.07.007 · Cited by 71 · see citing works
Kim, Y., Choi, H., Lee, W., Park, H., Kam, T.-I., Hong, S.-H., Nah, J., Jung, S., Shin, B., Lee, H., et al. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.12.006 · Cited by 71 · see citing works
Babaei, J. F., Baluchnejadmojarad, T., Nikbakht, F., & Roghani, M. (2018) · Metabolic Brain Disease · doi:10.1007/s11011-018-0338-8 · Cited by 71 · see citing works
Oguchi, T., Ono, R., Tsuji, M., Shozawa, H., Somei, M., Inagaki, M., Mori, Y., Yasumoto, T., Ono, K., & Kiuchi, Y. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00337 · Cited by 66 · see citing works
Lieberman, O. J., & Sulzer, D. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.028 · Cited by 65 · see citing works
Apoptosis: A Potential Therapeutic Target for Retinal Degenerations
Doonan, F., & Cotter, T. G. (2004) · Current Neurovascular Research · doi:10.2174/1567202043480215 · Cited by 64 · see citing works
Qin, X., Cheng, Y., & Yu, L. (2010) · Neuroscience Letters · doi:10.1016/j.neulet.2010.05.062 · Cited by 62 · see citing works
He, D., Tan, J., & Zhang, J. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.06.144 · Cited by 61 · see citing works
Bose, K., Pop, C., Feeney, B., & Clark, A. C. (2003) · Biochemistry · doi:10.1021/bi034998x · Cited by 60 · see citing works
Lin, Y., Wu, Y., Sun, G., Ho, C., Wong, T., Lin, C., Chen, H., Yeh, T., Li, C., Tseng, C., et al. (2018) · Journal of Clinical Medicine · doi:10.3390/jcm7100329 · Cited by 60 · see citing works
Arrozi, A. P., Shukri, S. N. S., Ngah, W. Z. W., Yusof, Y. A. M., Damanhuri, H. A., Jaafar, F., & Makpol, S. (2020) · Scientific Reports · doi:10.1038/s41598-020-65570-4 · Cited by 59 · see citing works
Targeting Aggrephagy for the Treatment of Alzheimer’s Disease
Malampati, S., Song, J., Tong, B. C., Nalluri, A., Yang, C., Wang, Z., Sreenivasmurthy, S. G., Zhu, Z., Liu, J., Su, C.-F., et al. (2020) · Cells · doi:10.3390/cells9020311 · Cited by 58 · see citing works
Jiang, S., Zhao, Y., Zhang, T., Lan, J., Yang, J., Yuan, L., Zhang, Q., Pan, K., & Zhang, K. (2018) · Cell Proliferation · doi:10.1111/cpr.12427 · Cited by 54 · see citing works
Effects of resveratrol on learning and memory in rats with vascular dementia
Zhang, Y., Li, Y., Wang, Y., Wang, G., Mao, L., Zhang, D., & Wang, J. (2019) · Molecular Medicine Reports · doi:10.3892/mmr.2019.10723 · Cited by 54 · see citing works
Aluminum-Induced Synaptic Plasticity Impairment via PI3K-Akt-mTOR Signaling Pathway
Li, H., Xue, X., Li, L., Li, Y., Wang, Y., Huang, T., Wang, Y., Meng, H., Pan, B., & Niu, Q. L. (2020) · Neurotoxicity Research · doi:10.1007/s12640-020-00165-5 · Cited by 53 · see citing works
Kong, J., Ren, G., Jia, N., Wang, Y., Zhang, H., Zhang, W., Chen, B., & Cao, Y. (2013) · European Neurology · doi:10.1159/000351247 · Cited by 49 · see citing works
Molecular Mechanism of Vitamin K2 Protection against Amyloid-β-Induced Cytotoxicity
Huang, S.-H., Fang, S.-T., & Chen, Y.-C. (2021) · Biomolecules · doi:10.3390/biom11030423 · Cited by 49 · see citing works
Icariin Prevents Amyloid Beta-Induced Apoptosis via the PI3K/Akt Pathway in PC-12 Cells
Zhang, D., Wang, Z., Sheng, C., Peng, W., Hui, S., Gong, W., & Chen, S. (2015) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2015/235265 · Cited by 48 · see citing works
Tacconi, S., Perri, R., Balestrieri, E., Grelli, S., Bernardini, S., Annichiarico, R., Mastino, A., Caltagirone, C., & Macchi, B. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.07.009 · Cited by 44 · see citing works
Cavieres, V. A., González, A., Muñoz, V. C., Yefi, C. P., Bustamante, H. A., Barraza, R. R., Tapia-Rojas, C., Otth, C., Barrera, M. J., González, C., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0136313 · Cited by 43 · see citing works
Zhang, Q., Zhang, X., & Sun, A. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0491-6 · Cited by 43 · see citing works
Liang, Y., Huang, M., Jiang, X., Liu, Q., Chang, X., & Guo, Y. C. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.06.048 · Cited by 43 · see citing works
Lai, C., Chen, Q., Ding, Y., Liu, H., & Tang, Z. (2020) · Environmental Toxicology · doi:10.1002/tox.22928 · Cited by 43 · see citing works
Chu, Q., Zhu, Y., Cao, T., Zhang, Y., Chang, Z., Lü, J., Lu, J., & Zhang, Y. (2019) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-019-03101-2 · Cited by 42 · see citing works
Hampel, H. J., Lista, S., Vanmechelen, E., Zetterberg, H., Giorgi, F. S., Galgani, A., Blennow, K., Caraci, F., Das, B., Yan, R., et al. (2020) · Alzheimer s Research & Therapy · doi:10.1186/s13195-020-00686-3 · Cited by 42 · see citing works
Khezri, M. R., Yousefi, K., Mahboubi, N., Hodaei, D., & Ghasemnejad‐Berenji, M. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.114945 · Cited by 41 · see citing works
Melatonin ameliorates Aβ1-42-induced Alzheimer's cognitive deficits in mouse model
Gong, Y., Hua, N., Zang, X., Huang, T., & He, L. (2017) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12830 · Cited by 39 · see citing works
Villavicencio-Tejo, F., Olesen, M. A., Aránguiz, A., & Quintanilla, R. A. (2022) · Antioxidants · doi:10.3390/antiox11030515 · Cited by 39 · see citing works
Qin, X., Cheng, Y., Cui, J., Zhang, Y., & Yu, L. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.07.047 · Cited by 38 · see citing works
Gupta, P., Tiwari, S., Singh, A., Pal, A., Mishra, A., & Singh, S. (2021) · Biochemical Journal · doi:10.1042/bcj20200754 · Cited by 38 · see citing works
Galantamine attenuates amyloid-β deposition and astrocyte activation in APP/PS1 transgenic mice
Wu, Z., Zhao, L., Chen, X., Cheng, X., & Zhang, Y. (2015) · Experimental Gerontology · doi:10.1016/j.exger.2015.10.015 · Cited by 36 · see citing works
Genistein Inhibits Aβ25–35 –Induced Neurotoxicity in PC12 Cells via PKC Signaling Pathway
Luo, S., Lan, T., Liao, W., Zhao, M., & Yang, H. (2012) · Neurochemical Research · doi:10.1007/s11064-012-0872-4 · Cited by 36 · see citing works
Ban, J. Y., & Seong, Y. H. (2005) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2005.07.021 · Cited by 36 · see citing works
Critical Molecular and Cellular Contributors to Tau Pathology
Song, L., Wells, E. A., & Robinson, A. S. (2021) · Biomedicines · doi:10.3390/biomedicines9020190 · Cited by 36 · see citing works
Genetic control of programmed cell death and aging in the nematode Caenorhabditis elegans
Hengartner, M. O. (1997) · Experimental Gerontology · doi:10.1016/s0531-5565(96)00167-2 · Cited by 31 · see citing works
Miguel-Hidalgo, J. J., Paul, I. A., Wanzo, V., & Banerjee, P. (2012) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2012.07.032 · Cited by 31 · see citing works
A soluble tau fragment generated by caspase-2 is associated with dementia in Lewy body disease
Smith, B. R., Nelson, K. M., Kemper, L. J., Leinonen-Wright, K., Petersen, A. J., Keene, C. D., & Ashe, K. H. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0765-8 · Cited by 30 · see citing works
Son, Y., Kim, K., & Cho, H.-R. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.04.128 · Cited by 29 · see citing works
Xiao, S., Wu, Q., Yao, X., Zhang, J., Zhong, W., Zhao, J., Liu, Q., & Zhang, M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00617 · Cited by 27 · see citing works
Caspase-Mediated Truncation of Tau Potentiates Aggregation
Lee, S., & Shea, T. B. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/731063 · Cited by 25 · see citing works
Tian, Z., Dong, Q., Wu, T., & Guo, J. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.135542 · Cited by 25 · see citing works
Neuroprotective Effects of Statins in an In Vitro Model of Alzheimer's Disease
Fonseca, A. C. R. G., Proença, T., Resende, R., Oliveira, C. R., & Pereira, C. (2009) · Journal of Alzheimer s Disease · doi:10.3233/jad-2009-1067 · Cited by 24 · see citing works
Övey, İ. S., & Nazıroğlu, M. (2020) · Journal of Receptors and Signal Transduction · doi:10.1080/10799893.2020.1806321 · Cited by 23 · see citing works
Gao, X., Liu, J., Fan, D., Li, X., Fang, Z., Yan, K., & Fan, Y. (2021) · Oncology Reports · doi:10.3892/or.2021.8244 · Cited by 22 · see citing works
MicroRNAs in the pathophysiology of Alzheimer’s disease and Parkinson's disease: an overview
Khezri, M. R., Yousefi, K., Zolbanin, N. M., & Ghasemnejad‐Berenji, M. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02727-4 · Cited by 22 · see citing works
Li, Q., Liu, T., Yang, S., & Zhang, Z. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/2140427 · Cited by 20 · see citing works
Noël, A., Foveau, B., & LeBlanc, A. C. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03506-0 · Cited by 16 · see citing works
The effect of vitamin B12 on synaptic plasticity of hippocampus in Alzheimer’s disease model rats
Jahanshahi, M., Elyasi, L., & Nikmahzar, E. (2021) · International Journal of Neuroscience · doi:10.1080/00207454.2021.1962863 · Cited by 16 · see citing works
Abdel‐Aal, R. A., Hussein, O. A., Elsaady, R. G., & Abdelzaher, L. A. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.174695 · Cited by 16 · see citing works
Abdel-Aal, R., Hussein, O. A., Elsaady, R. G., & Abdelzaher, L. A. (2021) · Journal of medical and life sciences · doi:10.21608/jmals.2021.210630 · Cited by 16 · see citing works
Islam, M. R., Sharoar, M. G., Ryu, E.-K., & Park, I. (2017) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2017.3193 · Cited by 16 · see citing works
Anticancer potential of metformin: focusing on gastrointestinal cancers
Khezri, M. R., Malekinejad, H., Zolbanin, N. M., & Ghasemnejad‐Berenji, M. (2021) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-021-04256-8 · Cited by 12 · see citing works
Flagged first, then by citations
3 of the 192 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Nagori, K., Nakhate, K. T., Yadav, K., Ajazuddin, & Pradhan, M. (2023) · Future Pharmacology · doi:10.3390/futurepharmacol3040053 · Cited by 61 · see citing works
Therapeutic potential of ADAM10 modulation in Alzheimer’s disease: a review of the current evidence
Khezri, M. R., Mohebalizadeh, M., & Ghasemnejad‐Berenji, M. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01072-w · Cited by 41 · see citing works
Bhatia, V., Sharma, V. V., Chandel, A., & Rattan, A. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01715-z · Cited by 21 · see citing works
“Since tau pathology makes caspase activation worse in AD, therapies that focus on tau–caspase interactions may lessen tau aggregation and fragmentation, which would lessen the negative effects of tau-mediated toxicity (Khezri and Ghasemnejad-Berenji 2023).”
The PI3K/AKT Signaling Pathway and Caspase-3 in Alzheimer’s Disease: Which One Is the Beginner?
Khezri, M. R., Ghasemnejad‐Berenji, M., & Moloodsouri, D. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221157 · Cited by 13 · see citing works
Chen, H., Guo, F., Zhao, Y., Liu, W., Chen, B., Wang, C., Huang, L., Jiang, S., Ma, X., Ren, H., et al. (2025) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2025.1572976 · Cited by 8 · see citing works
Singh, A. A., Khan, F., & Song, M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26104707 · Cited by 8 · see citing works
“Caspases, a family of proteases involved in cell death and inflammation, are essential to the pathophysiology of AD [22].”
Banu, Z., & Das, N. R. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04478-9 · Cited by 4 · see citing works
Senkowska, Z., & Węglarz‐Tomczak, E. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103116 · Cited by 2 · see citing works
Yadav, E., Mandal, A. K., Sah, A. K., Poudel, S., Pathak, P., Khalilullah, H., Jaremko, M., Emwas, A.-H. M., Yadav, P. S., & Verma, A. (2024) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273298025240905130205 · Cited by 1 · see citing works
Advances in Developing Small Molecule Drugs for Alzheimer's Disease
Zhang, W., Zhang, L., Lv, M., Fu, Y., Meng, X., Wang, M., & Wang, H. (2024) · Current Alzheimer Research · doi:10.2174/0115672050329828240805074938
Five Key Criteria for Identifying Optimal Therapeutic Targets in Protein‐Mediated Diseases
Al‐Shuhaib, M. B. S., & Al‐Shuhaib, J. M. B. (2025) · ChemistrySelect · doi:10.1002/slct.202403409
Hassan, M., Bhatti, S. G., Yasir, M., Chun, W., & Kloczkowski, A. (2026) · Journal of Chemical Information and Modeling · doi:10.1021/acs.jcim.6c02284
- Authors
- Khezri, M. R., & Ghasemnejad-Berenji, M.
- Affiliations
- Urmia University of Medical Sciences (IR)
- Department of Pharmacology and Toxicology, Faculty of Pharmacy, Urmia University of Medical Sciences, Urmia, Iran
- Corresponding author
- Khezri, Mohammad Rafi
- Venue
- Journal of Alzheimer s Disease
- Publisher
- SAGE Publications
- Published
- 2023-01-03
- Volume
- 91
- Issue
- 1
- Pages
- 71-90
- ISSN
- 1387-2877 (ISSN-L)
- 1875-8908
- OpenAlex
- W4309692331
- Cited by
- 12
- References
- 192
- Citations by year
- 2026: 2 · 2025: 5 · 2024: 2 · 2023: 3
- FWCI
- 0.34
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of Alzheimer s Disease (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- caspases, Alzheimer's disease
- MeSH terms
- Neuroinflammatory Diseases, Alzheimer Disease, Humans, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Caspases
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