Acetylated tau exacerbates learning and memory impairment by disturbing with mitochondrial homeostasis

Apoptosis: A Review of Programmed Cell Death

Elmore, S. (2007) · Toxicologic Pathology · doi:10.1080/01926230701320337 · Cited by 13,853 · see citing works

Mitochondrial Dysfunction and Oxidative Stress in Neurodegenerative Diseases

Lin, M. T., & Beal, M. F. (2006) · Nature · doi:10.1038/nature05292 · Cited by 6,455 · see citing works

Sample size determination and power analysis using the G*Power software

Kang, H. (2021) · Journal of Educational Evaluation for Health Professions · doi:10.3352/jeehp.2021.18.17 · Cited by 2,572 · see citing works

The cell biology of mitochondrial membrane dynamics

Giacomello, M., Pyakurel, A., Glytsou, C., & Scorrano, L. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0210-7 · Cited by 1,550 · 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

Mitochondrial dynamics: overview of molecular mechanisms

Tilokani, L., Nagashima, S., Paupe, V., & Prudent, J. (2018) · Essays in Biochemistry · doi:10.1042/ebc20170104 · Cited by 1,397 · see citing works

Mitochondria dysfunction in the pathogenesis of Alzheimer’s disease: Recent advances.

Wang, W., Zhao, F., Ma, X., Perry, G., & Zhu, X. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00376-6 · Cited by 1,274 · see citing works

Mitochondrial dynamics and apoptosis

Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270 · see citing works

Mitochondrial cristae shape determines respiratory chain supercomplexes assembly and respiratory efficiency

Cogliati, S., Frezza, C., Soriano, M. E., Varanita, T., Quintana-Cabrera, R., Corrado, M., Cipolat, S., Costa, V., Casarin, A., Gomes, L. C., et al. (2013) · Cell · doi:10.1016/j.cell.2013.08.032 · Cited by 1,265 · see citing works

Targeting Antioxidants to Mitochondria by Conjugation to Lipophilic Cations

Murphy, M. P., & Smith, R. A. J. (2007) · Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev.pharmtox.47.120505.105110 · Cited by 1,173 · see citing works

Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer’s disease

Giannakopoulos, P., Herrmann, F. R., Bussière, T., Bouras, C., Kövari, E., Perl, D. P., Morrison, J. H., Gold, G., & Hof, P. R. (2003) · Neurology · doi:10.1212/01.wnl.0000063311.58879.01 · Cited by 1,118 · see citing works

Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949 · see citing works

Mitochondrial bioenergetic deficit precedes Alzheimer's pathology in female mouse model of Alzheimer's disease

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

Mitophagy and Alzheimer’s Disease: Cellular and Molecular Mechanisms

Kerr, J. S., Adriaanse, B. A., Greig, N. H., Mattson, M. P., Cader, M. Z., Bohr, V. A., & Fang, E. F. (2017) · Trends in Neurosciences · doi:10.1016/j.tins.2017.01.002 · Cited by 870 · see citing works

Tau pathology and neurodegeneration contribute to cognitive impairment in Alzheimer’s disease

Bejanin, A., Schonhaut, D. R., La Joie, R., Kramer, J. H., Baker, S. L., Sosa, N., Ayakta, N., Cantwell, A., Janabi, M., Lauriola, M., et al. (2017) · Brain · doi:10.1093/brain/awx243 · Cited by 778 · see citing works

The acetylation of tau inhibits its function and promotes pathological tau aggregation

Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., & Lee, V. M. Y. (2011) · Nature Communications · doi:10.1038/ncomms1255 · Cited by 724 · see citing works

Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease

Wesseling, H., Mair, W., Kumar, M., Schlaffner, C. N., Tang, S., Beerepoot, P., Fatou, B., Guise, A. J., Cheng, L., Takeda, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.029 · Cited by 688 · see citing works

NOX4 promotes ferroptosis of astrocytes by oxidative stress-induced lipid peroxidation via the impairment of mitochondrial metabolism in Alzheimer’s diseases

Park, M. W., Cha, H. W., Kim, J., Kim, J. H., Yang, H., Yoon, S., Boonpraman, N., Yi, S. S., Yoo, I. D., & Moon, J.-S. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101947 · Cited by 683 · see citing works

Acetylation of the C Terminus of Ku70 by CBP and PCAF Controls Bax-Mediated Apoptosis

Cohen, H. Y., Lavu, S., Bitterman, K. J., Hekking, B., Imahiyerobo, T. A., Miller, C. M., Frye, R. A., Ploegh, H. L., Kessler, B. M., & Sinclair, D. A. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00094-2 · Cited by 574 · see citing works

HSP72 protects against obesity-induced insulin resistance

Chung, J., Nguyen, A.-K., Henstridge, D. C., Holmes, A. G., Chan, M. H. S., Mesa, J. L., Lancaster, G. I., Southgate, R. J., Bruce, C. R., Duffy, S. J., et al. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0705799105 · Cited by 553 · see citing works

Mitochondrial Dysfunction and Biogenesis in Neurodegenerative diseases: Pathogenesis and Treatment

Golpich, M., Amini, E., Mohamed, Z., Raymond, A. A., Ibrahim, N. M., & Ahmadiani, A. (2016) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.12655 · Cited by 540 · see citing works

Impaired Mitochondrial Biogenesis Contributes to Mitochondrial Dysfunction in Alzheimer's Disease

Sheng, B., Wang, X.-L., Su, B., Lee, H.-G., Casadesus, G., Perry, G., & Zhu, X.-W. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07581.x · Cited by 538 · see citing works

Abnormal Hyperphosphorylation of Tau: Sites, Regulation, and Molecular Mechanism of Neurofibrillary Degeneration

Wang, J., Xia, Y., Grundke, I., & Iqbal, K. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129031 · Cited by 530 · see citing works

Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits

Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3951 · Cited by 516 · see citing works

Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease

Zhang, Z., Song, M., Liu, X., Kang, S. S., Kwon, I.-S., Duong, D. M., Seyfried, N. T., Hu, W. T., Liu, Z., Wang, J.-Z., et al. (2014) · Nature Medicine · doi:10.1038/nm.3700 · Cited by 494 · see citing works

Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice

Morris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472 · see citing works

Mitochondrial biogenesis and dynamics in the developing and diseased heart

Dorn, G. W., Vega, R. B., & Kelly, D. P. (2015) · Genes & Development · doi:10.1101/gad.269894.115 · Cited by 470 · see citing works

Abnormal interaction between the mitochondrial fission protein Drp1 and hyperphosphorylated tau in Alzheimer's disease neurons: implications for mitochondrial dysfunction and neuronal damage

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

Glycosylation of microtubule–associated protein tau: An abnormal posttranslational modification in Alzheimer's disease

Wang, J.-Z., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0896-871 · Cited by 360 · see citing works

Mitochondrial and apoptotic neuronal death signaling pathways in cerebral ischemia

Niizuma, K., Yoshioka, H., Chen, H., Kim, G. S., Jung, J. E., Katsu, M., Okami, N., & Chan, P. H. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.002 · Cited by 360 · see citing works

Nicotinamide riboside restores cognition through an upregulation of proliferator-activated receptor-γ coactivator 1α regulated β-secretase 1 degradation and mitochondrial gene expression in Alzheimer's mouse models

Gong, B., Pan, Y., Vempati, P., Zhao, W., Knable, L., Ho, L., Wang, J., Sastre, M., Ono, K., Sauve, A. A., et al. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.12.005 · Cited by 345 · see citing works

A neurological perspective on mitochondrial disease

McFarland, R., Taylor, R. W., & Turnbull, D. M. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(10)70116-2 · Cited by 315 · see citing works

Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies

Irwin, D. J., Cohen, T. J., Grossman, M., Arnold, S. E., Xie, S. X., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Brain · doi:10.1093/brain/aws013 · Cited by 281 · see citing works

Acetylated Tau Obstructs KIBRA-Mediated Signaling in Synaptic Plasticity and Promotes Tauopathy-Related Memory Loss

Tracy, T. E., Sohn, P. D., Minami, S. S., Wang, C., Min, S.-W., Li, Y., Zhou, Y., Le, D., Lo, I., Ponnusamy, R., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.005 · Cited by 277 · see citing works

Mitochondrial dysfunction in oocytes of obese mothers: transmission to offspring and reversal by pharmacological endoplasmic reticulum stress inhibitors

Wu, L., Russell, D. L., Wong, S. L., Chen, M., Tsai, T., John, J. C. S., Norman, R. J., Febbraio, M. A., Carroll, J., & Robker, R. L. (2015) · Development · doi:10.1242/dev.114850 · Cited by 276 · see citing works

Glycogen synthase kinase-3 beta (GSK-3β) signaling: Implications for Parkinson's disease

Golpich, M., Amini, E., Hemmati, F., Ibrahim, N. M., Rahmani, B., Mohamed, Z., Raymond, A. A., Dargahi, L., Ghasemi, R., & Ahmadiani, A. (2015) · Pharmacological Research · doi:10.1016/j.phrs.2015.03.010 · Cited by 276 · see citing works

Hsp72 preserves muscle function and slows progression of severe muscular dystrophy

Gehrig, S. M., van der Poel, C., Sayer, T. A., Schertzer, J. D., Henstridge, D. C., Church, J. E., Lamon, S., Russell, A. P., Davies, K. E., Febbraio, M. A., et al. (2012) · Nature · doi:10.1038/nature10980 · Cited by 274 · see citing works

Mitochondrial Biogenesis: A Therapeutic Target for Neurodevelopmental Disorders and Neurodegenerative Diseases

Uittenbogaard, M. N., & Chiaramello, A. (2014) · Current Pharmaceutical Design · doi:10.2174/1381612820666140305224906 · Cited by 240 · see citing works

SUMOylation at K340 inhibits tau degradation through deregulating its phosphorylation and ubiquitination

Luo, H.-B., Xia, Y.-Y., Shu, X.-J., Liu, Z.-C., Feng, Y., Liu, X.-H., Yu, G., Yin, G., Xiong, Y.-S., Zeng, K., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1417548111 · Cited by 236 · see citing works

Reducing acetylated tau is neuroprotective in brain injury

Shin, M.-K., Vázquez-Rosa, E., Koh, Y., Dhar, M., Chaubey, K., Cintrón-Pérez, C. J., Barker, S., Miller, E., Franke, K., Noterman, M. F., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.032 · Cited by 226 · see citing works

Phosphorylation of tau antagonizes apoptosis by stabilizing β-catenin, a mechanism involved in Alzheimer's neurodegeneration

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

MAPT/Tau accumulation represses autophagy flux by disrupting IST1-regulated ESCRT-III complex formation: a vicious cycle in Alzheimer neurodegeneration

Feng, Q., Luo, Y., Zhang, X., Yang, X., Hong, X.-Y., Sun, D., Li, X., Hu, Y., Li, X., Zhang, J., et al. (2019) · Autophagy · doi:10.1080/15548627.2019.1633862 · Cited by 211 · see citing works

Activating HSP72 in Rodent Skeletal Muscle Increases Mitochondrial Number and Oxidative Capacity and Decreases Insulin Resistance

Henstridge, D. C., Bruce, C. R., Drew, B. G., Tory, K., Kolonics, A., Estevez, E., Chung, J., Watson, N., Gardner, T., Lee-Young, R. S., et al. (2014) · Diabetes · doi:10.2337/db13-0967 · Cited by 201 · see citing works

Altered brain energetics induces mitochondrial fission arrest in Alzheimer’s Disease

Zhang, L., Trushin, S., Christensen, T. A., Bachmeier, B. V., Gateno, B., Schroeder, A., Yao, J., Itoh, K., Sesaki, H., Poon, W. W., et al. (2016) · Scientific Reports · doi:10.1038/srep18725 · Cited by 198 · see citing works

The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass

Romanello, V., & Sandri, M. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03662-0 · Cited by 197 · see citing works

Regulation of neuron mitochondrial biogenesis and relevance to brain health

Onyango, I. G., Lu, J., Rodova, M., Lezi, E., Crafter, A. B., & Swerdlow, R. H. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.07.014 · Cited by 188 · see citing works

Tau accumulation induces synaptic impairment and memory deficit by calcineurin-mediated inactivation of nuclear CaMKIV/CREB signaling

Yin, Y., Gao, D., Wang, Y., Wang, Z.-H., Wang, X., Ye, J., Wu, D., Fang, L., Pi, G., Yang, Y., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1604519113 · Cited by 174 · see citing works

Caspase-cleaved Tau Expression Induces Mitochondrial Dysfunction in Immortalized Cortical Neurons

Quintanilla, R. A., Matthews-Roberson, T. A., Dolan, P. J., & Johnson, G. V. W. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808908200 · Cited by 170 · see citing works

Why size matters – balancing mitochondrial dynamics in Alzheimer's disease

DuBoff, B., Feany, M. Β., & Götz, J. (2013) · Trends in Neurosciences · doi:10.1016/j.tins.2013.03.002 · Cited by 164 · see citing works

Human wild-type full-length tau accumulation disrupts mitochondrial dynamics and the functions via increasing mitofusins

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

Coenzyme Q10 Decreases Amyloid Pathology and Improves Behavior in a Transgenic Mouse Model of Alzheimer's Disease

Dumont, M., Kipiani, K., Yu, F., Wille, E. J., Katz, M., Calingasan, N. Y., Gouras, G. K., Lin, M. T. S., & Beal, M. F. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-110209 · Cited by 161 · see citing works

Medication‐induced mitochondrial damage and disease

Neustadt, J. O., & Pieczenik, S. R. (2008) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200700075 · Cited by 158 · see citing works

Interneuron Accumulation of Phosphorylated tau Impairs Adult Hippocampal Neurogenesis by Suppressing GABAergic Transmission

Zheng, J., Li, H., Tian, N., Liu, F., Wang, L., Yin, Y., Yue, L., Ma, L., Wan, Y., & Wang, J. (2020) · Cell stem cell · doi:10.1016/j.stem.2019.12.015 · Cited by 155 · see citing works

Mitoguardin regulates mitochondrial fusion through MitoPLD and is required for neuronal homeostasis.

Zhang, Y., Liu, X., Bai, J., Tian, X., Zhao, X., Liu, W., Duan, X., Shang, W., Fan, H.-Y., & Tong, C. (2016) · Molecular Cell · doi:10.1016/j.molcel.2015.11.017 · Cited by 145 · see citing works

FLEXITau: Quantifying Post-translational Modifications of Tau Protein in Vitro and in Human Disease

Mair, W., Muntel, J., Tepper, K., Tang, S., Biernat, J., Seeley, W. W., Kosik, K. S., Mandelkow�, E., Steen, H., & Steen, J. A. J. (2016) · Analytical Chemistry · doi:10.1021/acs.analchem.5b04509 · Cited by 144 · see citing works

Effect of Poly(ADP-Ribose) Polymerase Inhibitors on the Ischemia-Reperfusion-Induced Oxidative Cell Damage and Mitochondrial Metabolism in Langendorff Heart Perfusion System

Halmosi, R., Berente, Z., Ősz, E., Tóth, K., Literati-Nagy, P., & Sümegi, B. (2001) · Molecular Pharmacology · doi:10.1124/mol.59.6.1497 · Cited by 140 · see citing works

Tau: From research to clinical development

Holtzman, D. M., Carrillo, M. C., Hendrix, J. A., Bain, L. J., Catafau, A. M., Gault, L. M., Goedert, M., Mandelkow, E., Mandelkow, E., Miller, D. S., et al. (2016) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2016.03.018 · Cited by 139 · see citing works

The dentate gyrus neurogenesis: a therapeutic target for Alzheimer's disease

Tatebayashi, Y., Lee, M. H., Li, L., Iqbal, K., & Grundke, I. (2003) · Acta Neuropathologica · doi:10.1007/s00401-002-0636-3 · Cited by 126 · see citing works

Exercise induces mitochondrial biogenesis after brain ischemia in rats

Zhang, Q., Wu, Y., Zhang, P., Sha, H., Jia, J., Hu, Y., & Zhu, J. (2012) · Neuroscience · doi:10.1016/j.neuroscience.2011.12.053 · Cited by 121 · see citing works

Restoring mitochondrial DNA copy number preserves mitochondrial function and delays vascular aging in mice

Foote, K., Reinhold, J., Yu, E., Figg, N. L., Finigan, A. J., Murphy, M. P., & Bennett, M. R. (2018) · Aging Cell · doi:10.1111/acel.12773 · Cited by 120 · see citing works

Improvement of Insulin Sensitivity by a Novel Drug, BGP-15, in Insulin-resistant Patients: A Proof of Concept Randomized Double-blind Clinical Trial

Literáti-Nagy, B., Kulcsár, E., Literáti-Nagy, Z., Buday, B., Péterfai, E., Horváth, T., Tory, K., Kolonics, A., Fleming, A., Mandl, J., et al. (2009) · Hormone and Metabolic Research · doi:10.1055/s-0028-1128142 · Cited by 113 · see citing works

O‐GlcNAcylation: A regulator of tau pathology and neurodegeneration

Gong, C., Liu, F., & Iqbal, K. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.02.011 · Cited by 111 · see citing works

Opposite monosynaptic scaling of BLP–vCA1 inputs governs hopefulness- and helplessness-modulated spatial learning and memory

Yang, Y., Wang, Z.-H., Jin, S., Gao, D., Liu, N., Chen, S., Zhang, S., Liu, Q., Liu, E., Wang, X., et al. (2016) · Nature Communications · doi:10.1038/ncomms11935 · Cited by 111 · see citing works

The small-molecule BGP-15 protects against heart failure and atrial fibrillation in mice

Sapra, G., Tham, Y. K., Cemerlang, N., Matsumoto, A., Kiriazis, H., Bernardo, B. C., Henstridge, D. C., Ooi, J. Y. Y., Pretorius, L., Boey, E. J. H., et al. (2014) · Nature Communications · doi:10.1038/ncomms6705 · Cited by 107 · see citing works

BGP-15—a novel poly(ADP-ribose) polymerase inhibitor—protects against nephrotoxicity of cisplatin without compromising its antitumor activity

Rácz, I., Tory, K., Gallyas, F., Berente, Z., Ősz, E., Jaszlits, L., Bernath, S., Sümegi, B., Rabloczky, G., & Literati-Nagy, P. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(01)00935-2 · Cited by 97 · see citing works

Activation of mitochondrial fusion provides a new treatment for mitochondria-related diseases

Szabó, A., Sümegi, K., Fekete, K., Hocsák, E., Debreceni, B., Sétáló, G., Kovács, K., Deres, L., Kengyel, A. M., Kovács, D., et al. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.01.038 · Cited by 92 · see citing works

BGP-15, a nicotinic amidoxime derivate protecting heart from ischemia reperfusion injury through modulation of poly(ADP-ribose) polymerase

Szabados, E., Literati-Nagy, P., Farkas, B., & Sümegi, B. (2000) · Biochemical Pharmacology · doi:10.1016/s0006-2952(99)00418-9 · Cited by 84 · see citing works

Tau accumulation triggers STAT1‐dependent memory deficits by suppressing NMDA receptor expression

Li, X., Hong, X., Wang, Y., Zhang, S., Zhang, J., Li, X., Liu, Y., Sun, D., Feng, Q., Ye, J., et al. (2019) · The EMBO Reports · doi:10.15252/embr.201847202 · Cited by 81 · see citing works

A novel dephosphorylation targeting chimera selectively promoting tau removal in tauopathies

Zheng, J., Tian, N., Liu, F., Zhang, Y., Su, J., Gao, Y., Deng, M., Wei, L., Ye, J., Li, H., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00669-2 · Cited by 78 · see citing works

Preclinical Alzheimer's disease: A systematic review of the cohorts underlying the concept

Epelbaum, S., Genthon, R., Cavedo, E., Habert, M. O., Lamari, F., Gagliardi, G. P., Lista, S., Teichmann, M., Bakardjian, H., Hampel, H. J., et al. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.12.003 · Cited by 77 · see citing works

The chaperone co-inducer BGP-15 alleviates ventilation-induced diaphragm dysfunction

Salah, H. A., Li, M., Cacciani, N., Gastaldello, S., Ogilvie, H., Akkad, H., Namuduri, A. V., Morbidoni, V., Artemenko, K. A., Balogh, G. E., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf7099 · Cited by 76 · see citing works

Tau hyperphosphorylation induces apoptotic escape and triggers neurodegeneration in Alzheimer’s disease

Wang, J., Wang, Z.-H., & Tian, Q. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1415-y · Cited by 74 · see citing works

Disease-modified glycogen synthase kinase-3β intervention by melatonin arrests the pathology and memory deficits in an Alzheimer's animal model

Peng, C., Hu, J., Liu, D., Hong, X., Wu, Y., Zhu, L., & Wang, J. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2012.12.010 · Cited by 74 · see citing works

Phosphorylated tau potentiates Aβ-induced mitochondrial damage in mature neurons

Quintanilla, R. A., Rommy von Bernhardi, M., Godoy, J. A., Inestrosa, N. C., & Johnson, G. V. W. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.016 · Cited by 72 · see citing works

Acetylated tau in Alzheimer's disease: An instigator of synaptic dysfunction underlying memory loss

Tracy, T. E., & Gan, L. (2017) · BioEssays · doi:10.1002/bies.201600224 · Cited by 72 · see citing works

BGP-15 inhibits caspase-independent programmed cell death in acetaminophen-induced liver injury

Nagy, G., Szarka, A., Lotz, G., Dóczi, J., Wunderlich, L., Kiss, A., Jemnitz, K., Veres, Z., Bánhegyi, G., Schaff, Z., et al. (2009) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2009.11.017 · Cited by 63 · see citing works

Assessment of newly synthesized mitochondrial DNA using BrdU labeling in primary neurons from Alzheimer's disease mice: Implications for impaired mitochondrial biogenesis and synaptic damage

Calkins, M. J., & Reddy, P. H. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.04.006 · Cited by 62 · see citing works

BGP-15 prevents the death of neurons in a mouse model of familial dysautonomia

Ohlen, S. B., Russell, M. L., Brownstein, M., & Lefcort, F. B. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1620212114 · Cited by 59 · see citing works

Posttranslational Modifications Mediate the Structural Diversity of Tauopathy Strains

Arakhamia, T., Lee, C. E., Carlomagno, Y., Kumar, M., Duong, D. M., Wesseling, H., Kundinger, S. R., Wang, K., Williams, D., Deture, M. A., et al. (2021) · Cell · doi:10.1016/j.cell.2021.11.029 · Cited by 57 · see citing works

BGP-15, a PARP-inhibitor, prevents imatinib-induced cardiotoxicity by activating Akt and suppressing JNK and p38 MAP kinases

Sárszegi, Z., Bognar, E., Gaszner, B., Kónyi, A., Gallyas, F., Sümegi, B., & Berente, Z. (2012) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-012-1252-8 · Cited by 55 · see citing works

BGP-15, a hydroximic acid derivative, protects against cisplatin- or taxol-induced peripheral neuropathy in rats

Bárdos, G. (2003) · Toxicology and Applied Pharmacology · doi:10.1016/s0041-008x(03)00155-8 · Cited by 50 · see citing works

A possible overestimation of the effect of acetylation on lysine residues in KQ mutant analysis

Fujimoto, H., Higuchi, M., Koike, M., Ode, H., Pinák, M., Bunta, J. K., Nemoto, T., Sakudoh, T., Honda, N., Maekawa, H., et al. (2011) · Journal of Computational Chemistry · doi:10.1002/jcc.21956 · Cited by 46 · see citing works

Mitochondrial transcription factor A (TFAM) polymorphisms and risk of late-onset Alzheimer's disease in Han Chinese

Zhang, Q., Yu, J., Wang, P., Chen, W., Wu, Z., Jiang, H. F., & Tan, L. (2010) · Brain Research · doi:10.1016/j.brainres.2010.10.074 · Cited by 37 · see citing works

BGP-15 Improves Aspects of the Dystrophic Pathology in mdx and dko Mice with Differing Efficacies in Heart and Skeletal Muscle

Kennedy, T. L., Swiderski, K., Murphy, K. T., Gehrig, S. M., Curl, C. L., Chandramouli, C., Febbraio, M. A., Delbridge, L. M. D., Koopman, R., & Lynch, G. S. (2016) · American Journal Of Pathology · doi:10.1016/j.ajpath.2016.08.008 · Cited by 36 · see citing works

Pseudo-acetylation of multiple sites on human Tau proteins alters Tau phosphorylation and microtubule binding, and ameliorates amyloid beta toxicity

Gorsky, M. K., Burnouf, S., Sofola-Adesakin, O., Dols, J., Augustin, H., Weigelt, C. M., Grönke, S., & Partridge, L. (2017) · Scientific Reports · doi:10.1038/s41598-017-10225-0 · Cited by 36 · see citing works

The Mitochondrial Dynamics of Alzheimers Disease and Parkinsons Disease Offer Important Opportunities for Therapeutic Intervention

Bonda, D., Smith, M. A., Perry, G. L., Lee, H., Wang, X., & Zhu, X. (2011) · Current Pharmaceutical Design · doi:10.2174/138161211798072562 · Cited by 34 · see citing works

Preconditioning as a Potential Strategy for the Prevention of Parkinson’s Disease

Golpich, M., Rahmani, B., Ibrahim, N. M., Dargahi, L., Mohamed, Z., Raymond, A. A., & Ahmadiani, A. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8689-6 · Cited by 26 · see citing works

BGP‐15 Protects against Heart Failure by Enhanced Mitochondrial Biogenesis and Decreased Fibrotic Remodelling in Spontaneously Hypertensive Rats

Horváth, O., Ördög, K., Bruszt, K., Deres, L., Gallyas, F., Sümegi, B., Tóth, K., & Halmosi, R. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/1250858 · Cited by 25 · see citing works

Rifaximin protects against circadian rhythm disruption–induced cognitive impairment through preventing gut barrier damage and neuroinflammation

Meng, D., Yang, M., Hu, L., Liu, T., Zhang, H., Sun, X., Wang, X., Chen, Y., Jin, Y. T., & Liu, R. (2022) · Journal of Neurochemistry · doi:10.1111/jnc.15701 · Cited by 25 · see citing works

PINK1 Alleviates Cognitive Impairments via Attenuating Pathological Tau Aggregation in a Mouse Model of Tauopathy

Jiang, X. J., Wu, Y. Q., Ma, R., Chang, Y. M., Li, L. L., Zhu, J. H., Liu, G. P., & Li, G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.736267 · Cited by 22 · see citing works

REACHING TO A REWARDED VISUAL STIMULUS: INTERHEMISPHERIC CONFLICT AND HAND USE IN MONKEYS WITH FOREBRAIN COMMISSUROTOMY

Eacott, M. J., & Gaffan, D. (1989) · Brain · doi:10.1093/brain/112.5.1215 · Cited by 10 · see citing works

Targeting Mitochondrial Dysfunction and Reactive Oxygen Species for Neurodegenerative Disease Treatment

Choi, E.-H., Kim, M.-H., & Park, S.-J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25147952 · Cited by 109 · see citing works

Role of Tau Protein in Neurodegenerative Diseases and Development of Its Targeted Drugs: A Literature Review

Yang, J., Zhi, W., & Wang, L. (2024) · Molecules · doi:10.3390/molecules29122812 · Cited by 63 · see citing works

A positive feedback inhibition of isocitrate dehydrogenase 3β on paired-box gene 6 promotes Alzheimer-like pathology

Wang, X., Liu, Q., Yu, H., Xie, J., Zhao, J., Fang, Z.-T., Qu, M., Zhang, Y., Yang, Y., & Wang, J. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01812-5 · Cited by 60 · see citing works

BGP-15 alleviates LPS-induced depression-like behavior by promoting mitophagy

Liu, Q. R., Zhao, J., Fang, Z., Wang, X., Zhang, B., He, Y., Liu, R., Chen, J., & Liu, G. (2024) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2024.04.036 · Cited by 59 · see citing works

Mitochondrial dysfunction as a therapeutic strategy for neurodegenerative diseases: Current insights and future directions

Gu, Y., Zhao, X., Zhang, N., Yang, Y., Yi, Y., Shao, Q.-H., Liu, M.-X., & Zhang, X.-L. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102577 · Cited by 58 · see citing works

The Role and Pathogenesis of Tau Protein in Alzheimer’s Disease

Hong, X.-Y., Huang, L., Lei, F., Li, T., Luo, Y., Zeng, M., & Wang, Z. (2025) · Biomolecules · doi:10.3390/biom15060824 · Cited by 52 · see citing works

Cerebral neurotoxicity of amino-modified polystyrene nanoplastics in mice and the protective effects of functional food Camellia pollen

Bai, H., Wu, Y., Li, H., Zhu, Y., Che, R., Wang, F., & Zhang, C. (2023) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2023.169511 · Cited by 48 · see citing works

4-Octyl itaconate alleviates endothelial cell inflammation and barrier dysfunction in LPS-induced sepsis via modulating TLR4/MAPK/NF-κB signaling

Li, R., Ma, Y., Wu, H., Zhang, X., Ding, N., Li, Z., Hu, X., Rao, J., Zhou, Y., Wang, L., et al. (2025) · Molecular Medicine · doi:10.1186/s10020-025-01160-2 · Cited by 33 · see citing works

Complicated Role of Post-translational Modification and Protease-Cleaved Fragments of Tau in Alzheimer’s Disease and Other Tauopathies

Yang, J., Shen, N., Shen, J., Yang, Y., & Li, H.-L. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03867-x · Cited by 32 · see citing works

Bioenergetic failure and oxidative stress: mitochondrial contributions to Alzheimer’s disease

Wasim, R. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01916-6 · Cited by 30 · see citing works

Synaptic sabotage: How Tau and α-Synuclein undermine synaptic health

Uytterhoeven, V., Verstreken, P., & Nachman, E. (2024) · The Journal of Cell Biology · doi:10.1083/jcb.202409104 · Cited by 28 · see citing works

Low-dose BPA-induced neuronal energy metabolism dysfunction and apoptosis mediated by PINK1/parkin mitophagy pathway in juvenile rats

Meng, L., Ouyang, Z., Chen, Y., Huang, C., Yu, Y., & Fan, R. (2024) · The Science of The Total Environment · doi:10.1016/j.scitotenv.2024.172655 · Cited by 25 · see citing works

Interplay Between Aging and Tau Pathology in Alzheimer’s Disease: Mechanisms and Translational Perspectives

Alrouji, M., Alshammari, M. S., Syed, T., & Shamsi, A. (2025) · Antioxidants · doi:10.3390/antiox14070774 · Cited by 21 · see citing works

Upregulation of ISG15 induced by MAPT/tau accumulation represses autophagic flux by inhibiting HDAC6 activity: a vicious cycle in Alzheimer disease

Liu, Q. R., Wang, X., Fang, Z., Zhao, J.-N., RUI, X., Zhang, B., He, Y., Liu, R., Chen, J., Chai, G., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2431472 · Cited by 20 · see citing works

Kaixinsan regulates neuronal mitochondrial homeostasis to improve the cognitive function of Alzheimer's disease by activating CaMKKβ-AMPK-PGC-1α signaling axis

Ren, J., Xiang, B., Song, L., René, D. J., Luo, Y., Wen, G., Gu, H., Yang, Z., & Zhang, Y. (2024) · Phytomedicine · doi:10.1016/j.phymed.2024.156170 · Cited by 19 · see citing works

Tau association with synaptic mitochondria coincides with energetic dysfunction and excitatory synapse loss in the P301S tauopathy mouse model

Estrella, L. D., Trease, A. J., Sheldon, L., Roland, N. J., Fox, H. S., & Stauch, K. L. (2024) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2024.12.006 · Cited by 18 · see citing works

Selenoprotein W modulates tau homeostasis in an Alzheimer’s disease mouse model

Ren, B., Situ, J., Huang, X., Tan, Q., Xiao, S., Li, N., Tian, J., Du, X., Ni, J., & Liu, Q. (2024) · Communications Biology · doi:10.1038/s42003-024-06572-0 · Cited by 17 · see citing works

From powerhouse to regulator: The role of mitoepigenetics in mitochondrion-related cellular functions and human diseases

Donato, L., Mordà, D., Scimone, C., Alibrandi, S., D’Angelo, R., & Sidoti, A. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.03.025 · Cited by 13 · see citing works

Sleep restriction exacerbates cardiac dysfunction in diabetic mice by causing cardiomyocyte death and fibrosis through mitochondrial damage

Zhang, J., Zhao, X., Tang, J. P., Liu, C., Zhang, Y., Cai, C., & Du, Q. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-02214-w · Cited by 13 · see citing works

The tolerable upper intake level of manganese alleviates Parkinson-like motor performance and neuronal loss by activating mitophagy

Han, X., Zhang, B., Gong, Q., Liu, T., Wang, C., Sun, Y., Jia, H., pu, Y., Hou, Q., & Yang, X. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.10.281 · Cited by 12 · see citing works

Acetylated tau exacerbates apoptosis by disturbing mitochondrial dynamics in HEK293 cells

Zhang, J., Fang, Z., Zhao, J., Liu, G., Shen, X., Jiang, G., & Liu, Q. R. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16053 · Cited by 11 · see citing works

Glutaminolysis regulates endometrial fibrosis in intrauterine adhesion via modulating mitochondrial function

Chen, P., Ye, C., Huang, Y., Xu, B., Wu, T., Dong, Y., Jin, Y., Zhao, L., Hu, C., Mao, J., et al. (2024) · Biological Research · doi:10.1186/s40659-024-00492-3 · Cited by 13 · see citing works

The Deficits of Insulin Signal in Alzheimer’s Disease and the Mechanisms of Vanadium Compounds in Curing AD

Yao, J., He, Z., You, G., Liu, Q., & Li, N. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45080402 · Cited by 9 · see citing works

Mitochondrial dynamics in neurodegenerative diseases: Research hotspots and trends from 2005 to 2025

Hu, S., Yang, Z., Bao, K., Hou, W., Qin, Y., Wu, C., Wang, Q., Luo, X., & Luo, L. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102987 · Cited by 9 · see citing works

Modulation of the cognitive impairment associated with Alzheimer’s disease by valproic acid: possible drug repurposing

Sorial, M. E. S., Abdelghany, R. M., & Sayed, N. S. E. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01695-0 · Cited by 8 · see citing works

Decoding tau acetylation in Alzheimer’s disease and tauopathies: from site-specific mechanisms to therapeutic horizons

Oh, Y. R., & Shin, M. (2025) · BMB Reports · doi:10.5483/bmbrep.2025-0077 · Cited by 9 · see citing works

Development and characterization of novel anti-acetylated tau monoclonal antibodies to probe pathogenic tau species in Alzheimer’s disease

Bryan, M. R., Tian, X., Tseng, J., Evangelista, B., Ragusa, J. V., Bryan, A. F., Trotman, W., Irwin, D. J., & Cohen, T. J. (2024) · Acta Neuropathologica Communications · doi:10.1186/s40478-024-01865-1 · Cited by 8 · see citing works

Comprehensive review on Alzheimer's disease: From the posttranslational modifications of Tau to corresponding treatments

Li, X., Ba, Z., Huang, J., Chen, J., Jiang, J., Huang, N., & Luo, Y. (2024) · Ibrain · doi:10.1002/ibra.12176 · Cited by 7 · see citing works

Tau post-translational modifications in Alzheimer's disease: Insights into pathogenesis, therapeutic strategies, and diagnostic advances

Lei, H., Chen, X., Ruan, L., Liu, X., Ye, F., Li, K., Cheng, W., Yu, B., Di, C., & Di, C. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102927 · Cited by 7 · see citing works

Multiple Mechanisms and Therapeutic Strategies for the Involvement of AMPK in the Development of Alzheimer’s Disease

Yu, L., Yang, X., Lei, H.-P., Hu, Y., Wu, L., Zhou, S., & Jin, F. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05162-3 · Cited by 6 · see citing works

Carvacrol acetate activated Nrf2 modulates mitophagy for the treatment of neurocyte oxidative stress induced by chlorpyrifos

Zhou, H.-L., Wang, B., Fan, X.-L., Zhang, X.-M., & Song, Y. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.117484 · Cited by 6 · see citing works

BMP1 inhibitor UK383367 improves MI-induced cardiac remodeling and fibrosis in mice via ameliorating macrophage polarization and mitochondrial dysfunction

Guo, C., Wang, Q., Li, J., Ji, W., Chen, L., Chang, M., Ma, L., Liu, X., & Ni, M. (2025) · Acta Pharmacologica Sinica · doi:10.1038/s41401-025-01655-y · Cited by 5 · see citing works

Advances in Alzheimer’s disease: mechanistic insights and therapeutic targets

Jia, Y.-J., Ge, Y., Li, B., Yang, Y., Chen, H., Liu, J., Guo, J., Yu, J., Ye, K., Wang, J., et al. (2026) · Science China Life Sciences · doi:10.1007/s11427-025-2991-7 · Cited by 5 · see citing works

Making tau amyloid models in vitro: a crucial and underestimated challenge

Broc, J., Piersson, C., & Fichou, Y. (2025) · FEBS Letters · doi:10.1002/1873-3468.70022 · Cited by 5 · see citing works

Novel insights from comprehensive analysis: The role of cuproptosis and peripheral immune infiltration in Alzheimer’s disease

Wang, J., Yu, Z.-W., Liu, Q., Wu, J., Zhang, Y.-D., Wan, H., Bi, M., Xiao, N., Zheng, K.-M., & Jiang, B. (2025) · PLoS ONE · doi:10.1371/journal.pone.0325799 · Cited by 4 · see citing works

Therapeutic importance of hydrogen sulfide in cognitive impairment diseases

Wei, H., Tan, H., Cao, J.-P., He, J., Zhang, Q., Jiang, L., Zhou, G., & Xiao, F. (2025) · Brain Research · doi:10.1016/j.brainres.2025.149547 · Cited by 3 · see citing works

The Role and Mechanism of the cGAS–STING/NLRP3 Signaling Axis-Regulated p38 MAPK/NF–κB Pathway in Manganese-Induced Tau Aggregation-Mediated Neurotoxicity

Zhong, S., Zhou, Q., Yang, J., Zhang, Z., Chai, X., Luo, J., Zhang, X., Liu, J., Yixi, Y., Shi, L., et al. (2026) · Environment & Health · doi:10.1021/envhealth.5c00504 · Cited by 3 · see citing works

Histone lactylation leads to perioperative neurocognitive disorders by promoting the expression of Ralbp1 and inducing excessive mitochondrial fission in hippocampal neurons

Meng, F., Cao, S., Wu, W.-F., Zhang, M., Jing, Q., Xie, Z., Sun, X., Song, J., Fei, M., QIAN Cunyuan, C. G., et al. (2026) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-026-06095-3 · Cited by 3 · see citing works

Protein lysine acetylation regulates beef color stability during storage

Shu, Y., Lv, J., Lou, A., Quan, W., & Shen, Q. W. (2025) · LWT · doi:10.1016/j.lwt.2025.117468 · Cited by 3 · see citing works

Mitochondrial Dysfunction in Neurodegenerative Diseases

Chen, C., Zhao, Y., Wang, J., Pan, D., Wang, X., Xu, Y., Yan, J., Wang, L., Yang, X., Lu, M., et al. (2025) · MedComm · doi:10.1002/mco2.70326 · Cited by 3 · see citing works

Nicotine Improves Memory Impairment in Aged Rats Through Enhanced Mitochondrial Homeostasis

Ni, Z., Li, Y., Wang, G., Wang, S., Chen, H., Hou, H., & Hu, Q. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-05342-1 · Cited by 2 · see citing works

Bioenergetic impairment-induced Tau acetylation: Converging pathways in Alzheimer’s disease

C, B. K., & G., P. P. C. (2026) · International review of neurobiology · doi:10.1016/bs.irn.2026.05.020 · Cited by 2 · see citing works

The potential of mulberry (Morus alba L.) leaf extract against pro-aggregant tau-mediated inflammation and mitochondrial dysfunction

Lin, T., Tseng, P.-H., Chen, I., Lin, C., Lee, M.-C., Chang, K., Lee‐Chen, G., & Chen, C. (2025) · Neurochemistry International · doi:10.1016/j.neuint.2025.106042 · Cited by 1 · see citing works

The therapeutic effect of nicotinamide riboside chloride on ameliorating alcohol-induced neuronal damage with a focus on mitochondrial unfolded protein response and mitophagy

Wang, J., Wang, J., Xie, W., Shen, Q., Wang, C., Li, R., & Deng, S. (2025) · Genes & Diseases · doi:10.1016/j.gendis.2025.101886 · Cited by 1 · see citing works

Neuronal gene profiling of tau oligomer-bearing cholinergic nucleus basalis neurons during the onset of Alzheimer’s disease

Kara, B., Beck, J. S., Fu, Z., Hickey, S. L., Kanaan, N. M., Mufson, E. J., Ginsberg, S. D., & Counts, S. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02080-2 · Cited by 1 · see citing works

Understanding the impact of cytoskeleton disruption on synaptic plasticity in Alzheimer’s disease

Basavaraju, K. C., & Priyadarshini, P. (2025) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2025.10.020 · Cited by 1 · see citing works

Three alternative promoters govern PGC-1α expression in chicken and are directly repressed by PPARγ

Huang, J., Mu, F., Lou, M., Gao, F., Ning, B., Luo, H., Yan, X., Jing, Y., & Wang, N. (2026) · Poultry Science · doi:10.1016/j.psj.2026.106481 · Cited by 1 · see citing works

ScFv T1 Protects Against Mitochondrial Damage of SH-SY5Y Cells Caused by Extracellular Tau Aggregates

Wang, Z., Jiang, X., Lin, J., An, R., He, Y., & Li, S. (2026) · Antioxidants · doi:10.3390/antiox15040515 · Cited by 1 · see citing works

Toward common treatment strategies: convergent proteinopathies and mitochondrial dysfunction in Alzheimer’s and Parkinson’s diseases

Offerdahl, J. E. V., & Mor, D. E. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1846384 · Cited by 1 · see citing works

Emerging diagnostic biomarkers and therapeutic targets in Alzheimer's disease

Dineshbhai, T. K., Rafaliya, D., Singh, A., Maheshwari, S., Lalan, M. S., & Chakraborthy, G. S. (2026) · Inflammopharmacology · doi:10.1007/s10787-026-02341-z · Cited by 1 · see citing works

Mitochondrial ecosystem restoration in Alzheimer’s disease: from mechanisms to multi-target therapeutic strategies

Song, D. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1886145 · Cited by 1 · see citing works

Response to comment on: BGP-15 alleviates LPS-induced depression-like behavior by promoting mitophagy

Liu, Q., & Liu, G. (2024) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2024.06.029 · Cited by 1 · see citing works

Transcriptomic analysis reveals the critical role and mechanisms of Shenxian zhou in preventing age-related cognitive impairment

Jia, X., Liu, M. Y., Liang, Y., Zhang, Y., Li, S., Bai, M., & Yongqiang, D. U. A. N. (2026) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2026.121584

BGP ‐15 Mitigates Oxidative Stress and Mitochondrial Dysfunction in In Vitro Matured Oocytes From Type 1 Diabetic Mice

Wang, L., Yin, L., Li, Y., Guo, F., Li, Q., Li, Y., mi, J., Huang, H., & Xu, J. (2026) · The FASEB Journal · doi:10.1096/fj.202505013rr

CAPNS1 restoration partially alleviates mitochondrial dysfunction and synaptic deficits in Alzheimer’s disease through the Ca2+-CaMKIIβ-MAPK-PGC-1α axis

Han, J., Wu, S., Cui, X., Zhou, X., Yu, Q., Cheng, Q., Lu, Z., & Zong, S. (2026) · Neuroscience · doi:10.1016/j.neuroscience.2026.07.021

MFN2-mediated remodelling of ER-mitochondria communication alleviates ochratoxin A-induced hepatocyte ferroptosis by enhancing mitophagy

Hu, Z.-Y., Liu, R., Ouyang, Y.-X., Chen, M., Wang, J.-X., Lou, M., Huang, Y.-F., Si, H.-L., Jiang, F., Liu, Z.-Y., et al. (2026) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2026.143458

Targeting microglial glutaminase 1 protects against ferroptosis-driven cognitive impairment in perioperative neurocognitive disorders

Sun, Y., Li, Y., Zhang, F., Wan, Z., Zhang, X., Xu, P., Wang, Y., Li, C., Zuo, Y., Liu, J., et al. (2026) · Cell Death and Differentiation · doi:10.1038/s41418-026-01833-3

Targeting tau acetylation in Alzheimer's disease: Molecular mechanisms, pathological consequences, and therapeutic opportunities of dietary phytochemicals

Basavaraju, K. C., & G., P. P. C. (2026) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2026.154717

Acetylated tau exacerbates apoptosis by disturbing mitochondrial dynamics in HEK293 cells

Zhang, J., Fang, Z., Zhao, J., Liu, G., Shen, X., Jiang, G., & Liu, Q. R. (2024) · Journal of Neurochemistry · doi:10.1111/jnc.16053 · Cited by 11 · see citing works

Acetylated Tau Obstructs KIBRA-Mediated Signaling in Synaptic Plasticity and Promotes Tauopathy-Related Memory Loss

Tracy, T. E., Sohn, P. D., Minami, S. S., Wang, C., Min, S.-W., Li, Y., Zhou, Y., Le, D., Lo, I., Ponnusamy, R., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.005 · Cited by 277 · see citing works

The role of tau in Alzheimer’s Disease: Effects of Lys-280 and Lys-281 acetylation on tau function and structure

Constance, B. H. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/jk28-gv66

Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits

Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3951 · Cited by 516 · see citing works

Comprehensive analysis of nerve activity in the brain under neuropathic pain using functional magnetic resonance imaging

Yanase, M., Yamashita, A., Horiuchi, H., & Narita, M. (2011) · Neuroscience Research · doi:10.1016/j.neures.2011.07.1579