The Association of Tau With Mitochondrial Dysfunction in Alzheimer’s Disease
Open accessAbstract
Increasing evidence suggests that abnormally hyperphosphorylated tau plays a vital role in the pathogenesis of Alzheimer's disease (AD). Mitochondrial dysfunction also has a recognized role in the pathophysiology of AD. In recent years, mitochondrial dysfunction has been strongly associated with tau pathology in AD. Overexpression of hyperphosphorylated and aggregated tau appears to damage the axonal transport, leading to abnormal mitochondrial distribution. In addition, pathological tau impairs mitochondrial dynamics by regulating mitochondrial fission/fusion proteins, and further causes mitochondrial dysfunction and neuronal damage. Moreover, mitochondrial dysfunction is also involved in promoting tau pathology in AD. In this article, we evaluate the relationship between phosphorylated tau and mitochondrial dysfunction in AD.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
Decrease in Δψm has been observed in several in vitro and in vivo AD models.
“A decrease in Δψm (or mitochondrial depolarization) has been observed in several in vitro and in vivo AD models [65,66]”
From Apoe4 and Alzheimer’s Disease Pathogenesis—Mitochondrial Deregulation and Targeted Therapeutic Strategies (2023) · cites this paper as [66]
The ‘Tau pathology and mitochondrial dysfunction in AD’ section reports depolarized mitochondrial membrane potential in a triple-transgenic AD mouse model and impaired membrane potential associated with truncated tau. It also discusses cell-culture studies, but does not clearly establish decreased membrane potential across several in vitro and in vivo AD models. No page number is available in our copy. (LLM, conf=0.84)
Experimental — accuracy not yet measuredAberrant tau phosphorylation and aggregation promote neuronal and synaptic damage, leading to cognitive decline in AD, through alterations in mitochondrial localization, imbalance in fusion/fission, ATP synthesis, ROS production and mitochondrial depolarization.
“Through alterations in mitochondrial localization in neurons, imbalance in fusion and fission processes and in ATP synthesis, ROS production and mitochondrial depolarization, aberrant tau phosphorylation and aggregation promote neuronal and synaptic damage, leading to cognitive decline in AD [66].”
From Apoe4 and Alzheimer’s Disease Pathogenesis—Mitochondrial Deregulation and Targeted Therapeutic Strategies (2023) · cites this paper as [66]
Tau hyperphosphorylation and aggregation have been related to impairment of mitochondrial dynamics, namely axonal transport and bioenergetics.
“Tau hyperphosphorylation and aggregation have been related to the impairment of mitochondrial dynamics, namely axonal transport and bioenergetics.”
From Apoe4 and Alzheimer’s Disease Pathogenesis—Mitochondrial Deregulation and Targeted Therapeutic Strategies (2023) · cites this paper as [66]
Although Alzheimer's disease has complex multifactorial effects, oxidative stress is key to the initiation of the pathophysiological process in cholinergic neurons.
“Although AD has complex multifactorial, effects OS is key to the initiation of the pathophysiological process in cholinergic neurons [107,108,109].”
From Multi-Target Mechanisms of Phytochemicals in Alzheimer’s Disease: Effects on Oxidative Stress, Neuroinflammation and Protein Aggregation (2022) · cites this paper as [109]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864 · see citing works
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · see citing works
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484 · 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
Mitochondrial Fission, Fusion, and Stress
Youle, R. J., & van der Bliek, A. M. (2012) · Science · doi:10.1126/science.1219855 · Cited by 3,674 · see citing works
Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders
Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174 · see citing works
Guo, J., Huang, F., Liu, J., Chen, Y., Wang, W., Cao, B., Zou, Z., Liu, S., Pan, J., Bao, C., et al. (2016) · Scientific Reports · doi:10.1038/srep21230 · Cited by 2,148 · see citing works
Mitochondria: Dynamic Organelles in Disease, Aging, and Development
Chan, D. C. (2006) · Cell · doi:10.1016/j.cell.2006.06.010 · Cited by 1,987 · see citing works
Oxidative Stress, Synaptic Dysfunction, and Alzheimer’s Disease
Tönnies, E., & Trushina, E. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161088 · Cited by 1,750 · see citing works
The distribution of tau in the mammalian central nervous system.
Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588 · see citing works
Mitochondrial dynamics-fusion, fission, movement, and mitophagy-in neurodegenerative diseases
Chen, H., & Chan, D. C. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp326 · Cited by 1,455 · see citing works
Oxidative stress and mitochondrial dysfunction in Alzheimer’s disease
Wang, X., Wang, W., Li, L., Perry, G., Lee, H.-G., & Zhu, X. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.10.015 · Cited by 1,357 · see citing works
Amyloid-β and tau — a toxic pas de deux in Alzheimer's disease
Ittner, L. M., & Götz, J. (2010) · Nature reviews. Neuroscience · doi:10.1038/nrn2967 · Cited by 1,357 · see citing works
OPA1 requires mitofusin 1 to promote mitochondrial fusion
Cipolat, S., de Brito, O. M., Dal Zilio, B., & Scorrano, L. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0407043101 · Cited by 1,300 · see citing works
Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1357-09.2009 · Cited by 1,224 · see citing works
Yao, J., Irwin, R. W., Zhao, L., Nilsen, J., Hamilton, R. T., & Brinton, R. D. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0903563106 · Cited by 940 · see citing works
Mitochondrial fusion protects against neurodegeneration in the cerebellum
Chen, H., McCaffery, J. M., & Chan, D. C. (2007) · Cell · doi:10.1016/j.cell.2007.06.026 · Cited by 924 · see citing works
Ebneth, A., Godemann, R., Stamer, K., Illenberger, S., Trinczek, B., Mandelkow, E.-M., & Mandelkow, E. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.3.777 · Cited by 820 · see citing works
Oxidative stress in Alzheimer’s disease
Chen, Z., & Zhong, C. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1423-y · Cited by 797 · see citing works
O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease
Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775 · see citing works
Mitochondrial dysfunction is a trigger of Alzheimer's disease pathophysiology
Moreira, P. I., Carvalho, C., Zhu, X., Smith, M. A., & Perry, G. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.10.006 · Cited by 734 · see citing works
Bioenergetic role of mitochondrial fusion and fission
Westermann, B. (2012) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2012.02.033 · Cited by 687 · see citing works
Rhein, V., Song, X., Wiesner, A., Ittner, L. M., Baysang, G., Meier, F., Ozmen, L., Bluethmann, H., Dröse, S., Brandt, U., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905529106 · Cited by 655 · see citing works
The microtubule binding domain of tau protein
Lee, G., Neve, R. L., & Kosik, K. S. (1989) · Neuron · doi:10.1016/0896-6273(89)90050-0 · Cited by 500 · see citing works
Tau Reduction Prevents Aβ-Induced Defects in Axonal Transport
Vossel, K. A., Zhang, K., Brodbeck, J., Daub, A. C., Sharma, P., Finkbeiner, S., Cui, B., & Mucke, L. (2010) · Science · doi:10.1126/science.1194653 · Cited by 486 · see citing works
Mitochondrial filaments and clusters as intracellular power-transmitting cables
Skulachev, V. P. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01735-7 · Cited by 477 · see citing works
Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases
Mazanetz, M. P., & Fischer, P. M. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2111 · Cited by 459 · see citing works
Mańczak, M., & Reddy, P. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds072 · Cited by 453 · see citing works
Proteomic and functional analyses reveal a mitochondrial dysfunction in P301L tau transgenic mice
David, D. C., Hauptmann, S., Scherping, I., Schuessel, K., Keil, U., Rizzu, P., Ravid, R., Dröse, S., Brandt, U., Müller, W. E., et al. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m500356200 · Cited by 447 · see citing works
Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses.
Mandelkow, E., Stamer, K., Vogel, R., Thies, E., & Mandelkow, E. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.04.007 · Cited by 422 · see citing works
Mitochondrial Oxidative Stress Causes Hyperphosphorylation of Tau
Melov, S., Adlard, P. A., Morten, K., Johnson, F., Golden, T. R., Hinerfeld, D., Schilling, B., Mavros, C., Masters, C. L., Volitakis, I., et al. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000536 · Cited by 363 · see citing works
The Microtubule-associated Protein Tau Is Extensively Modified with O-linked N-acetylglucosamine
Arnold, C. S., Johnson, G. W., Cole, R. N., Dong, D. L.-Y., Lee, M., & Hart, G. W. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.46.28741 · Cited by 361 · see citing works
Manczak, M., & Reddy, P. H. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds360 · Cited by 348 · see citing works
One of the Antigenic Determinants of Paired Helical Filaments Is Related to Tau Protein1
Nukina, N., & Ihara, Y. (1986) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135625 · Cited by 338 · see citing works
Mitochondrial morphology transitions and functions: implications for retrograde signaling?
Picard, M. A., Shirihai, O. S., Gentil, B. J., & Burelle, Y. (2013) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00584.2012 · Cited by 320 · see citing works
Abnormal mitochondrial dynamics and neurodegenerative diseases
Su, B., Wang, X., Zheng, L., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.013 · Cited by 289 · see citing works
Kopeikina, K. J., Carlson, G. A., Pitstick, R., Ludvigson, A. E., Peters, A., Luebke, J. I., Koffie, R. M., Frosch, M. P., Hyman, B. T., & Spires‐Jones, T. L. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.07.004 · Cited by 276 · see citing works
Mitochondrial Aspects of Synaptic Dysfunction in Alzheimer’s Disease
Cai, Q., & Tammineni, P. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160726 · Cited by 274 · see citing works
Kanaan, N. M., Morfini, G. A., LaPointe, N. E., Pigino, G. F., Patterson, K. R., Song, Y., Andreadis, A., Fu, Y., Brady, S. T., & Binder, L. I. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0560-11.2011 · Cited by 273 · see citing works
GSK-3β inhibition reverses axonal transport defects and behavioural phenotypes in Drosophila
Mudher, A., Shepherd, D., Newman, T. A., Mildren, P., Jukes, J. P., Squire, A., Mears, A., Berg, S., MacKay, D., Asuni, A. A., et al. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001483 · Cited by 265 · see citing works
Molecular Machinery of Mitochondrial Fusion and Fission
Westermann, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800011200 · Cited by 251 · see citing works
Abnormalities of Mitochondrial Dynamics in Neurodegenerative Diseases
Gao, J., Wang, L., Liu, J., Xie, F., Su, B., & Wang, X. (2017) · Antioxidants · doi:10.3390/antiox6020025 · Cited by 250 · see citing works
Soluble forms of tau are toxic in Alzheimer's disease
Kopeikina, K., Hyman, B., & Spires-Jones, T. (2012) · Translational Neuroscience · doi:10.2478/s13380-012-0032-y · Cited by 232 · see citing works
Li, H.-L., Wang, H.-H., Liu, S.-J., Deng, Y.-Q., Zhang, Y.-J., Tian, Q., Wang, X.-C., Chen, X., Yang, Y., Zhang, J.-Y., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0609303104 · Cited by 225 · see citing works
Annonacin, a Natural Mitochondrial Complex I Inhibitor, Causes Tau Pathology in Cultured Neurons
Escobar-Khondiker, M., Höllerhage, M., Muriel, M., Champy, P., Bach, A., Depienne, C., Respondek, G., Yamada, E. S., Lannuzel, A., Yagi, T., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.1644-07.2007 · Cited by 212 · see citing works
Mitochondrial Dysfunction and Synaptic Transmission Failure in Alzheimer’s Disease
Guo, L., Tian, J., & Du, H. (2017) · Journal of Alzheimer’s Disease · doi:10.3233/jad-160702 · Cited by 211 · see citing works
Lovell, M., Xiong, S., Xie, C.-S., Davies, P., & Markesbery, W. (2005) · Journal of Alzheimer's Disease · doi:10.3233/jad-2004-6610 · Cited by 207 · see citing works
Shahpasand, K., Uemura, I., Saito, T., Asano, T., Hata, K., Shibata, K., Toyoshima, Y., Hasegawa, M., & Hisanaga, S.-I. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.5927-11.2012 · Cited by 206 · see citing works
Mitochondrial dynamics and Ca2+ signaling
Szabadkai, G., Simoni, A. M., Bianchi, K., Stefani, D. D., Leo, S., Wieckowski, M. R., & Rizzuto, R. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.04.002 · Cited by 204 · see citing works
Tau phosphorylation affects its axonal transport and degradation
Rodríguez-Martín, T., Cuchillo‐Ibáñez, I., Noble, W. J., Nyenya, F., Anderton, B. H., & Hanger, D. P. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.03.015 · Cited by 200 · see citing works
Microtubule structure and its stabilisation
Amos, L. (2004) · Organic & Biomolecular Chemistry · doi:10.1039/b403634d · Cited by 193 · see citing works
Kandimalla, R. J. L., Mańczak, M., Fry, D., Yeguvapalli, S., Sesaki, H., & Reddy, P. H. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw312 · Cited by 180 · see citing works
Chronic oxidative stress causes increased tau phosphorylation in M17 neuroblastoma cells
Su, B., Wang, X., Lee, H., Tabaton, M., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.010 · Cited by 178 · see citing works
Eckert, A., Schmitt, K., & Götz, J. (2011) · Alzheimer's Research & Therapy · doi:10.1186/alzrt74 · Cited by 177 · see citing works
Li, X., Hu, Y., Wang, Z.-H., Luo, Y., Zhang, Y., Liu, X., Feng, Q., Wang, Q., Ye, K., Liu, G., et al. (2016) · Scientific Reports · doi:10.1038/srep24756 · Cited by 164 · see citing works
Santos, R. X., Correia, S., Wang, X.-L., Perry, G., Smith, M. A., Moreira, P., & Zhu, X.-W. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-100666 · Cited by 157 · see citing works
Ittner, L. M., Ke, Y. D., & Götz, J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.014472 · Cited by 156 · see citing works
Mondragón‐Rodríguez, S., Perry, G. L., Zhu, X., Moreira, P. I., Acevedo, M., & Williams, S. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/940603 · Cited by 155 · see citing works
Mitochondrial Dysfunction Contributes to the Pathogenesis of Alzheimer’s Disease
Cabezas-Opazo, F., Vergara-Pulgar, K., Maria Jose Perez, J., Jara, C., Osorio‐Fuentealba, C., & Quintanilla, R. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/509654 · Cited by 148 · see citing works
Iijima-Ando, K., Sekiya, M., Maruko-Otake, A., Ohtake, Y., Suzuki, E., Lu, B., & Iijima, K. M. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002918 · Cited by 142 · see citing works
Patil, S. P., & Chan, C. (2005) · Neuroscience Letters · doi:10.1016/j.neulet.2005.05.003 · Cited by 138 · see citing works
Eckert, A., Nisbet, R. M., Grimm, A., & Götz, J. (2013) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2013.08.013 · Cited by 127 · see citing works
Evaluating triggers and enhancers of tau fibrillization
Kuret, J., Congdon, E. E., Li, G., Yin, H., Yu, X., & Zhong, Q. (2005) · Microscopy Research and Technique · doi:10.1002/jemt.20187 · Cited by 110 · see citing works
Mitochondrial Dynamics in Alzheimerʼs Disease
Bonda, D., Wang, X., Perry, G. L., Smith, M. A., & Zhu, X. (2010) · Drugs & Aging · doi:10.2165/11532140-000000000-00000 · Cited by 106 · see citing works
Atlante, A., Amadoro, G., Bobba, A., Lidia de, B. A. R. I., Corsetti, V., Pappalardo, G., Marra, E., Calissano, P., & Passarella, S. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.07.004 · Cited by 93 · see citing works
Axonal Transport Defects in Alzheimer’s Disease
Wang, Z., Tan, L., & Yu, J. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8810-x · Cited by 86 · see citing works
Caspase-Cleaved Tau Impairs Mitochondrial Dynamics in Alzheimer’s Disease
Pérez, M. J., Vergara-Pulgar, K., Jara, C., Cabezas-Opazo, F., & Quintanilla, R. A. (2018) · Molecular Neurobiology · doi:10.1007/s12035-017-0385-x · Cited by 81 · see citing works
Wang, J., Wang, Z.-H., & Tian, Q. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1415-y · Cited by 74 · see citing works
DREAM-Dependent Activation of Astrocytes in Amyotrophic Lateral Sclerosis
Larrodé, P., Calvo, A. C., Moreno‐Martínez, L., de la Torre, M., Moreno‐García, L., Molina, N., Castiella, T., Íñiguez, C., Pascual, L. F., Mena, F. J. M., et al. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0713-1 · Cited by 51 · see citing works
Morel, M., Authelet, M., Dedecker, R., & Brion, J. P. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.02.077 · Cited by 46 · see citing works
Oxidative Stress Modifies the Levels and Phosphorylation State of Tau Protein in Human Fibroblasts
Ibáñez-Salazar, A., Bañuelos-Hernández, B., Rodríguez‐Leyva, I., Chi-Ahumada, É., Monreal‐Escalante, E., Jiménez-Capdeville, M. E., & Rosales‐Mendoza, S. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00495 · Cited by 43 · see citing works
Wang, X., Yin, J., Zhang, Y., et al. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1351 · Cited by 38 · see citing works
Improving Yeast for Biofuel Production
(2010) · Science · doi:10.1126/science.330.6000.10-c · Cited by 3 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease
Guo, T., Zhang, D., Zeng, Y., Huang, T. Y., Xu, H., & Zhao, Y. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00391-7 · Cited by 994 · see citing works
Amyloid Beta and Phosphorylated Tau-Induced Defective Autophagy and Mitophagy in Alzheimer’s Disease
Reddy, P. H., & Oliver, D. M. (2019) · Cells · doi:10.3390/cells8050488 · Cited by 496 · see citing works
Monzio Compagnoni, G., Di Fonzo, A., Corti, S., Comi, G. P., Bresolin, N., & Masliah, E. (2020) · Molecular Neurobiology · doi:10.1007/s12035-020-01926-1 · Cited by 378 · see citing works
Tau-targeting therapies for Alzheimer disease: Current status and future directions
Congdon, E. E., Ji, C., Tetlow, A. M., Jiang, Y., & Sigurdsson, E. M. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00883-2 · Cited by 371 · see citing works
Exercise benefits on Alzheimer’s disease: State-of-the-science
Valenzuela, P. L., Castillo-García, A., Morales, J. S., de la Villa, P., Hampel, H., Emanuele, E., Lista, S., & Lucia, A. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101108 · Cited by 337 · see citing works
Jamwal, S., Blackburn, J. K., & Elsworth, J. D. (2021) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107705 · Cited by 236 · see citing works
Pires, M., & Rego, A. C. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24010778 · Cited by 157 · see citing works
Role of natural products for the treatment of Alzheimer’s disease
Noori, T., Dehpour, A. R., Sureda, A., Sobarzo-Sanchez, E., & Shirooie, S. (2021) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2021.173974 · Cited by 141 · see citing works
Sharifi-Rad, J., Rapposelli, S., Sestito, S., Herrera-Bravo, J., Arancibia-Diaz, A., Salazar, L. A., Yeskaliyeva, B., Beyatli, A., Leyva-Gómez, G., González-Contreras, C., et al. (2022) · Journal of Personalized Medicine · doi:10.3390/jpm12091515 · Cited by 125 · see citing works
Li, H., Liu, C.-C., Zheng, H., & Huang, T. Y. (2018) · Translational Neurodegeneration · doi:10.1186/s40035-018-0139-3 · Cited by 103 · see citing works
Association of Aβ with ceramide-enriched astrosomes mediates Aβ neurotoxicity
Elsherbini, A., Kirov, A. S., Dinkins, M. B., Wang, G., Qin, H., Zhu, Z., Tripathi, P., Crivelli, S. M., & Bieberich, E. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00931-8 · Cited by 72 · see citing works
Vijayan, M., Alvir, R. V., Alvir, R. V., Bunquin, L. E., Pradeepkiran, J. A., & Reddy, P. H. (2022) · Aging Cell · doi:10.1111/acel.13663 · Cited by 40 · see citing works
Recent trends of natural based therapeutics for mitochondria targeting in Alzheimer’s disease
Dhiman, A., Handa, M., Ruwali, M., Singh, D. P., Kesharwani, P., & Shukla, R. (2022) · Mitochondrion · doi:10.1016/j.mito.2022.03.006 · Cited by 21 · see citing works
- Authors
- Cheng, Y., & Bai, F.
- Affiliations
- Zhongda Hospital Southeast University (CN)
- Nanjing Drum Tower Hospital (CN)
- Corresponding author
- Bai, Feng
- ORCID
- Venue
- Frontiers in Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2018-03-22
- Volume
- 12
- Pages
- 163-163
- ISSN
- 1662-453X (ISSN-L)
- PMC
- PMC5874499
- OpenAlex
- W2790161245
- Cited by
- 239
- References
- 73
- Citations by year
- 2026: 22 · 2025: 32 · 2024: 25 · 2023: 26 · 2022: 41 · 2021: 30 · 2020: 37 · 2019: 17 · 2018: 9
- FWCI
- 3.05
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Frontiers in Neuroscience (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Natural Science Foundation of China (81671665)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- tau hyperphosphorylation, mitochondrial dysfunction, Alzheimer's disease, axonal transport, mitochondrial distribution, mitochondrial dynamics, neuronal injury, tau pathology
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
