Cited by 229Alzheimer's disease research and treatmentsTraumatic Brain Injury ResearchTraumatic Brain Injury and Neurovascular Disturbances

The DOI matches its Crossref record; 64 of the 64 references it cites were found in a registry or an index.

Reducing acetylated tau is neuroprotective in brain injury

Open access

Shin, Min-Kyoo, Vázquez-Rosa, Edwin, Koh, Yeojung, Dhar, Matasha, Chaubey, Kalyani, Cintrón-Pérez, Coral J., Barker, Sarah, Miller, Emiko, Franke, Kathryn, Noterman, Maria F., Seth, Divya, Allen, Rachael S., Motz, Cara T., Rao, Sriganesh Ramachandra, Skelton, Lara A., Pardue, Machelle T., Fliesler, Steven J., Wang, Chao, Tracy, Tara E., Gan, Li, Liebl, Daniel J., Savarraj, Jude P.J., Torres, Glenda L., Ahnstedt, Hilda, McCullough, Louise D., Kitagawa, Ryan S., Choi, H. Alex, Zhang, Pengyue, Hou, Yuan, Chiang, Chien-Wei, Li, Lang, Ortiz, Francisco, Kilgore, Jessica A., Williams, Noelle S., Whitehair, Victoria C., Gefen, Tamar, Flanagan, Margaret E., Stamler, Jonathan S., Jain, Mukesh K., Kraus, Allison, Cheng, Feixiong, Reynolds, James D., Pieper, Andrew A.·2021·Cell

DOI 10.1016/j.cell.2021.03.032PMC PMC8491234

Open this paper in CoChat — free account Open PDF

Abstract

Traumatic brain injury (TBI) is the largest non-genetic, non-aging related risk factor for Alzheimer's disease (AD). We report here that TBI induces tau acetylation (ac-tau) at sites acetylated also in human AD brain. This is mediated by S-nitrosylated-GAPDH, which simultaneously inactivates Sirtuin1 deacetylase and activates p300/CBP acetyltransferase, increasing neuronal ac-tau. Subsequent tau mislocalization causes neurodegeneration and neurobehavioral impairment, and ac-tau accumulates in the blood. Blocking GAPDH S-nitrosylation, inhibiting p300/CBP, or stimulating Sirtuin1 all protect mice from neurodegeneration, neurobehavioral impairment, and blood and brain accumulation of ac-tau after TBI. Ac-tau is thus a therapeutic target and potential blood biomarker of TBI that may represent pathologic convergence between TBI and AD. Increased ac-tau in human AD brain is further augmented in AD patients with history of TBI, and patients receiving the p300/CBP inhibitors salsalate or diflunisal exhibit decreased incidence of AD and clinically diagnosed TBI.

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

Crossref · 10.1016/j.cell.2021.03.032

Cites

64 of 64 references verified0 citation errors · 0 not checkable

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Analyzing real-time PCR data by the comparative CT method
Schmittgen, T. D., & Livak, K. J. (2008) · Nature Protocols · doi:10.1038/nprot.2008.73 · Cited by 26,190
National Institute on Aging–Alzheimer's Association guidelines for the neuropathologic assessment of Alzheimer's disease
Hyman, B. T., Phelps, C. H., Beach, T. G., Bigio, E. H., Cairns, N. J., Carrillo, M. C., Dickson, D. W., Duyckaerts, C., Frosch, M. P., Masliah, E., et al. (2012) · Alzheimer's & Dementia · doi:10.1016/j.jalz.2011.10.007 · Cited by 3,092
National Institute on Aging–Alzheimer’s Association guidelines for the neuropathologic assessment of Alzheimer’s disease: a practical approach
Montine, T. J., Phelps, C. H., Beach, T. G., Bigio, E. H., Cairns, N. J., Dickson, D. W., Duyckaerts, C., Frosch, M. P., Masliah, E., Mirra, S. S., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-011-0910-3 · Cited by 2,894
Quantification of histochemical staining by color deconvolution.
Ruifrok, A. C. C., & Johnston, D. A. (2001) · PubMed · Cited by 2,029
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
Self-citation
S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
Uehara, T., Nakamura, T., Yao, D., Shi, Z., Gu, Z., Ma, Y., Masliah, E., Nomura, Y., & Lipton, S. A. (2006) · Nature · doi:10.1038/nature04782 · Cited by 905
Incidence, Prevalence, Costs, and Impact on Disability of Common Conditions Requiring Rehabilitation in the United States: Stroke, Spinal Cord Injury, Traumatic Brain Injury, Multiple Sclerosis, Osteoarthritis, Rheumatoid Arthritis, Limb Loss, and Back Pain
Ma, V. Y., Chan, L. E., & Carruthers, K. J. (2014) · Archives of Physical Medicine and Rehabilitation · doi:10.1016/j.apmr.2013.10.032 · Cited by 890
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
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
Neuron-Specific Enolase as a Biomarker: Biochemical and Clinical Aspects
Isgrò, M. A., Bottoni, P., & Scatena, R. (2015) · Advances in experimental medicine and biology · doi:10.1007/978-94-017-7215-0_9 · Cited by 600

Flagged first, then by citations

Show all 64 references

Sorted by citations

Modulation of cellular processes by histone and non-histone protein acetylation
Shvedunova, M., & Akhtar, A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00441-y · Cited by 1,007
Neuroinflammation in Alzheimer disease
Heneka, M. T., van der Flier, W. M., Jessen, F., Hoozemanns, J., Thal, D. R., Boche, D., Brosseron, F., Teunissen, C., Zetterberg, H., Jacobs, A. H., et al. (2025) · Nature Reviews Immunology · doi:10.1038/s41577-024-01104-7 · Cited by 638
Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation
Chen, Y., & Yu, Y. (2023) · Journal of Neuroinflammation · doi:10.1186/s12974-023-02853-3 · Cited by 516
Protein posttranslational modifications in health and diseases: Functions, regulatory mechanisms, and therapeutic implications
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
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
Cellular and pathological functions of tau
Bravo, C. P., Naguib, S. A., & Gan, L. (2024) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-024-00753-9 · Cited by 271
Self-citation
X-linked ubiquitin-specific peptidase 11 increases tauopathy vulnerability in women
Yan, Y., Wang, X., Chaput, D., Shin, M.-K., Koh, Y., Gan, L., Pieper, A. A., Woo, J.-A. A., & Kang, D. E. (2022) · Cell · doi:10.1016/j.cell.2022.09.002 · Cited by 144
Self-citation
Neurodegenerative Disease Tauopathies
Creekmore, B. C., Watanabe, R., & Lee, E. B. (2023) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-051222-120750 · Cited by 155
Semaglutide ameliorates cognition and glucose metabolism dysfunction in the 3xTg mouse model of Alzheimer's disease via the GLP-1R/SIRT1/GLUT4 pathway
Wang, Z.-J., Li, X.-R., Chai, S.-F., Li, W.-R., Li, S., Hou, M., Li, J.-L., Ye, Y.-C., Cai, H.-Y., Hölscher, C., et al. (2023) · Neuropharmacology · doi:10.1016/j.neuropharm.2023.109716 · Cited by 125
Alzheimer’s Disease: Novel Targets and Investigational Drugs for Disease Modification
Cummings, J. L., Osse, A. M. L., & Kinney, J. W. (2023) · Drugs · doi:10.1007/s40265-023-01938-w · Cited by 125
Small Molecule Hydrogels Loading Small Molecule Drugs from Chinese Medicine for the Enhanced Treatment of Traumatic Brain Injury
Luo, W., Yang, Z., Zheng, J., Cai, Z., Li, X., Liu, J., Guo, X., Luo, M., Fan, X., Cheng, M., et al. (2024) · ACS Nano · doi:10.1021/acsnano.4c09097 · Cited by 106
Tau in neurodegenerative diseases: molecular mechanisms, biomarkers, and therapeutic strategies
Zhang, X., Wang, J., Zhang, Z., & Ye, K. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00429-6 · Cited by 119
Targeting pyroptosis with nanoparticles to alleviate neuroinflammatory for preventing secondary damage following traumatic brain injury
Zhang, X., Huang, X., Hang, D., Jin, J., Li, S., Zhu, Y., & Liu, H. (2024) · Science Advances · doi:10.1126/sciadv.adj4260 · Cited by 95
Protein S-nitrosylation and oxidation contribute to protein misfolding in neurodegeneration
Nakamura, T., Oh, C.-K., Zhang, X., & Lipton, S. A. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.07.002 · Cited by 84
The Role of Post-Translational Modifications on the Structure and Function of Tau Protein
Ye, H., Han, Y., Li, P., Su, Z., & Huang, Y. (2022) · Journal of Molecular Neuroscience · doi:10.1007/s12031-022-02002-0 · Cited by 76
Membraneless organelles in health and disease: exploring the molecular basis, physiological roles and pathological implications
Li, Y., Liu, Y., Yu, X., Xu, Y., Pan, X., Sun, Y. E., Wang, Y., Song, Y.-H., & Shen, Z. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02013-w · Cited by 72
The m6A methyltransferase METTL3 drives neuroinflammation and neurotoxicity through stabilizing BATF mRNA in microglia
Wu, X., Liu, H., Wang, J., Zhang, S., Hu, Q., Wang, T., Cui, W., Shi, Y., Bai, H., Zhou, J., et al. (2024) · Cell Death and Differentiation · doi:10.1038/s41418-024-01329-y · Cited by 68
Self-citation
Targeting tau in Alzheimer's disease: from mechanisms to clinical therapy
Ye, J., Wan, H., Chen, S., & Liu, G. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.385847 · Cited by 74
Artificial intelligence and open science in discovery of disease-modifying medicines for Alzheimer’s disease
Cheng, F., Wang, F., Tang, J., Zhou, Y., Fu, Z., Zhang, P., Haines, J. L., Leverenz, J. B., Gan, L., Hu, J., et al. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2023.101379 · Cited by 63
Self-citation
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
“The decrease in the acetylated form of tau is neuroprotective [76].”
Background
Tau-targeting therapy in Alzheimer’s disease: Critical advances and future opportunities
Guo, Y., Li, S., Zeng, L.-H., & Tan, J. (2022) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2022.16 · Cited by 61
Drug repurposing for Alzheimer’s disease and other neurodegenerative disorders
Cummings, J. L., Zhou, Y., Stone, A. V., Cammann, D., Tonegawa‐Kuji, R., Cacho, J. R. F., & Cheng, F. (2025) · Nature Communications · doi:10.1038/s41467-025-56690-4 · Cited by 80
Self-citation
Multiancestry analysis of the HLA locus in Alzheimer’s and Parkinson’s diseases uncovers a shared adaptive immune response mediated by HLA-DRB1*04 subtypes
Guen, Y. L., Luo, G., Ambati, A., Damotte, V., Jansen, I. E., Yu, E., Nicolas, A., de Rojas, I., Leal, T. P., Miyashita, A., et al. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2302720120 · Cited by 63
Acetylated tau exacerbates learning and memory impairment by disturbing with mitochondrial homeostasis
Liu, Q., Wang, X., Hu, Y., Zhao, J.-N., Huang, C.-H., Li, T., Zhang, B.-G., He, Y., Wu, Y.-Q., Zhang, Z.-J., et al. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102697 · Cited by 58
Hsp multichaperone complex buffers pathologically modified Tau
Moll, A., Ramirez, L. M., Ninov, M., Schwarz, J., Urlaub, H., & Zweckstetter, M. (2022) · Nature Communications · doi:10.1038/s41467-022-31396-z · Cited by 60
The Role and Pathogenesis of Tau Protein in Alzheimer’s Disease
Hong, X., Huang, L., Lei, F., Tian, L., Luo, Y., Zeng, M., & Wang, Z. (2025) · Biomolecules · doi:10.3390/biom15060824 · Cited by 67
Rescuing mitochondria in traumatic brain injury and intracerebral hemorrhages - A potential therapeutic approach
Ahluwalia, M., Kumar, M., Ahluwalia, P. K., Rahimi, S. Y., Vender, J. R., Raju, R. P., Hess, D. C., Baban, B., Vale, F. Ĺ., Dhandapani, K. M., et al. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105192 · Cited by 55
Increased Risk of Aging-Related Neurodegenerative Disease after Traumatic Brain Injury
Barker, S., Paul, B., & Pieper, A. (2023) · Biomedicines · doi:10.3390/biomedicines11041154 · Cited by 55
Self-citation
Redox signaling and metabolism in Alzheimer's disease
Holubiec, M. I., Gellert, M., & Hanschmann, E.-M. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.1003721 · Cited by 52
A review on traditional Chinese medicine natural products and acupuncture intervention for Alzheimer’s disease based on the neuroinflammatory
Chen, Z., Wang, X., Du, S., Liu, Q., Xu, Z., Guo, Y., & Lin, X. (2024) · Chinese Medicine · doi:10.1186/s13020-024-00900-6 · Cited by 59
TDP-43 drives synaptic and cognitive deterioration following traumatic brain injury
Gao, F., Hu, M., Zhang, J., Hashem, J., & Chen, C. (2022) · Acta Neuropathologica · doi:10.1007/s00401-022-02449-w · Cited by 49
Protein S-Nitrosation: Biochemistry, Identification, Molecular Mechanisms, and Therapeutic Applications
Ye, H., Wu, J., Liang, Z., Zhang, Y., & Huang, Z. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c02194 · Cited by 50
Acetylation discriminates disease-specific tau deposition
Chakraborty, P., Rivière, G., Hebestreit, A., de Opakua, A. I., Vorberg, I. M., Andreas, L. B., & Zweckstetter, M. (2023) · Nature Communications · doi:10.1038/s41467-023-41672-1 · Cited by 52
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 52
Rethinking the initial changes in subarachnoid haemorrhage: Focusing on real-time metabolism during early brain injury
Chen, Y., Galea, I., Macdonald, R. L., Wong, G. K. C., & Zhang, J. H. (2022) · EBioMedicine · doi:10.1016/j.ebiom.2022.104223 · Cited by 45
Genetic forms of tauopathies: inherited causes and implications of Alzheimer’s disease-like TAU pathology in primary and secondary tauopathies
Langerscheidt, F., Wied, T., Kabbani, M. A. A., van Eimeren, T., Wunderlich, G., & Zempel, H. (2024) · Journal of Neurology · doi:10.1007/s00415-024-12314-3 · Cited by 52
Acutely blocking excessive mitochondrial fission prevents chronic neurodegeneration after traumatic brain injury
Sridharan, P. S., Koh, Y., Miller, E., Hu, D., Chakraborty, S., Tripathi, S. J., Kee, T. R., Chaubey, K., Vázquez‐Rosa, E., Barker, S., et al. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101715 · Cited by 44
Self-citation
Systematic characterization of multi-omics landscape between gut microbial metabolites and GPCRome in Alzheimer’s disease
Qiu, Y., Hou, Y., Gohel, D., Zhou, Y., Xu, J., Bykova, M., Yang, Y., Leverenz, J. B., Pieper, A. A., Nussinov, R., et al. (2024) · Cell Reports · doi:10.1016/j.celrep.2024.114128 · Cited by 40
Self-citation
Disrupting pathologic phase transitions in neurodegeneration
Hurtle, B. T., Xie, L., & Donnelly, C. J. (2023) · Journal of Clinical Investigation · doi:10.1172/jci168549 · Cited by 40
The effects of nitric oxide in Alzheimer’s disease
Wang, L., Lu, D., Wang, X., Wang, Z., Li, W., & Chen, G. (2023) · Medical Gas Research · doi:10.4103/2045-9912.385939 · Cited by 37
Blood–brain barrier disruption: a pervasive driver and mechanistic link between traumatic brain injury and Alzheimer's disease
Sun, B., Li, L., Harris, O. A., & Luo, J. (2025) · Translational Neurodegeneration · doi:10.1186/s40035-025-00478-5 · Cited by 44
Self-citation
Cellular and molecular mechanisms of pathological tau phosphorylation in traumatic brain injury: implications for chronic traumatic encephalopathy
Donison, N. S., Palik, J., Volkening, K., & Strong, M. J. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00842-z · Cited by 42
White matter hyperintensities in former American football players
Alosco, M. L., Tripodis, Y., Baucom, Z., Adler, C. H., Balcer, L. J., Bernick, C. B., Mariani, M. L., Au, R., Banks, S. J., Barr, W., et al. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12779 · Cited by 35
Acetylation in pathogenesis: Revealing emerging mechanisms and therapeutic prospects
Jiang, N., Li, W., Jiang, S., Xie, M., & Liu, R. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115519 · Cited by 38
Tau K321/K353 pseudoacetylation within KXGS motifs regulates tau–microtubule interactions and inhibits aggregation
Xia, Y., Bell, B. M., & Giasson, B. I. (2021) · Scientific Reports · doi:10.1038/s41598-021-96627-7 · Cited by 34
The Beneficial Role of Sirtuin 1 in Preventive or Therapeutic Options of Neurodegenerative Diseases
Liu, H., Xu, S., Wang, C., Deng, Y. L., Xu, B., Yang, T., Sun, J., & Liu, W. (2022) · Neuroscience · doi:10.1016/j.neuroscience.2022.09.021 · Cited by 30
Self-citation
Viscoelastic cues to induce stem cell migration and neuronal differentiation in cell-free hydrogel-assisted TBI recovery
Liu, X., Wu, C., Zhang, Y., Li, G., Chen, S., Chen, Z., Liu, P., Wu, K., Wu, X., Zhou, T., et al. (2024) · Chemical Engineering Journal · doi:10.1016/j.cej.2024.152401 · Cited by 32
Multi-omics and artificial intelligence for precision drug discovery and potential clinical applications
Liu, Y., Zhu, K., Peng, W., Liu, Z., & Mao, X. (2026) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-026-02631-6 · Cited by 36
Proteomics of Multiple Sclerosis: Inherent Issues in Defining the Pathoetiology and Identifying (Early) Biomarkers
Sen, M. K., Almuslehi, M. S. M., Shortland, P. J., Mahns, D. A., & Coorssen, J. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147377 · Cited by 32
Interaction between resveratrol and SIRT1: role in neurodegenerative diseases
Zhu, L., Yang, M., Fan, L., Yan, Q., Zhang, L., Mu, P., & Lu, F. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03319-w · Cited by 31
Resveratrol activates the SIRT1/PGC-1 pathway in mice to improve synaptic-related cognitive impairment after TBI
Yu, D., Zhao, X.-Y., Meng, Q.-P., Teng, D., Deng, K., & Lin, N. (2022) · Brain Research · doi:10.1016/j.brainres.2022.148109 · Cited by 29
Brain injury biomarkers and applications in neurological diseases
Zhang, H., Wang, J., Qu, Y., Yang, Y., & Guo, Z. (2024) · Chinese Medical Journal · doi:10.1097/cm9.0000000000003061 · Cited by 29
Patchouli alcohol ameliorates the learning and memory impairments in an animal model of Alzheimer's disease via modulating SIRT1
Xu, Q., Su, Z., Hu, Z. J., Yang, W., Xian, Y., & Lin, Z. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154441 · Cited by 30
Alzheimer's Disease: A Review of Pathology, Current Treatments, and the Potential Therapeutic Effect of Decreasing Oxidative Stress by Combined Vitamin D and l -Cysteine Supplementation
Jain, S. K., Stevens, C. M., Margret, J. J., & Levine, S. N. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0245 · Cited by 33
Traumatic Brain Injury and Secondary Neurodegenerative Disease
Dodd, W., Panther, E. J., Pierre, K., Hernandez, J., Patel, D., & Lucke-Wold, B. P. (2022) · Trauma Care · doi:10.3390/traumacare2040042 · Cited by 27
Effect of Exercise and Oral Niacinamide Mononucleotide on Improving Mitochondrial Autophagy in Alzheimer’s Disease
Wu, W., Yuan, S., Tang, Y., Meng, X., Peng, M., Hu, Z., & Liu, W. (2023) · Nutrients · doi:10.3390/nu15132851 · Cited by 33
Neuronal BAG3 attenuates tau hyperphosphorylation, synaptic dysfunction, and cognitive deficits induced by traumatic brain injury via the regulation of autophagy-lysosome pathway
Sweeney, N., Kim, T. Y., Morrison, C. T., Li, L., Acosta, D. M., Liang, J., Datla, N. V., Fitzgerald, J. A., Huang, H., Liu, X., et al. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02810-1 · Cited by 28
Self-citation
Anti-acetylated-tau immunotherapy is neuroprotective in tauopathy and brain injury
Bravo, C., Krukowski, K., Barker, S., Wang, C., Li, Y., Fan, L., Vázquez‐Rosa, E., Shin, M., Wong, M. Y., McCullough, L. D., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00733-9 · Cited by 26
Self-citation
Disease-associated patterns of acetylation stabilize tau fibril formation
Li, L., Nguyen, B. A., Mullapudi, V., Li, Y., Saelices, L., & Joachimiak, L. A. (2023) · Structure · doi:10.1016/j.str.2023.05.020 · Cited by 25
Self-citation
Mitochondrial transport in neurons and evidence for its involvement in acute neurological disorders
Lu, D., Feng, Y., Liu, G., Yang, Y., Ren, Y., Chen, Z., Sun, X., Guan, Y.-X., & Wang, Z. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1268883 · Cited by 29
Potential use of bioactive nanofibrous dural substitutes with controlled release of IGF-1 for neuroprotection after traumatic brain injury
Wang, Y., Guo, Q., Wang, W., Wang, Y., Fang, K., Wan, Q., Li, H., & Wu, T. S. (2022) · Nanoscale · doi:10.1039/d2nr06081g · Cited by 25
Astrocytic NLRP3 cKO mitigates depression-like behaviors induced by mild TBI in mice.
Miao, H., Wang, J., Shao, J.-J., Song, R., Li, W., Sun, J.-K., Jia, S.-Y., Zhang, D., Li, X., Zhao, J., et al. (2025) · Neurobiology of Disease · doi:10.1016/j.nbd.2024.106785 · Cited by 23
Cathepsin B S-nitrosylation promotes ADAR1-mediated editing of its own mRNA transcript via an ADD1/MATR3 regulatory axis
Lin, Z., Zhao, S., Li, X., Miao, Z., Cao, J., Chen, Y., Shi, Z., Zhang, J., Wang, D., Chen, S., et al. (2023) · Cell Research · doi:10.1038/s41422-023-00812-4 · Cited by 25
The role of the gut–microbiota–brain axis via the subdiaphragmatic vagus nerve in chronic inflammatory pain and comorbid spatial working memory impairment in complete Freund's adjuvant mice
Yue, C., Luan, W.-W., Gu, H., Qiu, D., Ding, X., Liu, P., Wang, X., Hashimoto, K., & Yang, J. (2023) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2023.09.003 · Cited by 22
Neuroprotection strategies in traumatic brain injury: Studying the effectiveness of different clinical approaches
Buccilli, B., Alan, A., Aljeradat, B., Shahzad, A., Almealawy, Y. F., Chisvo, N. S., Ennabe, M., & Weinand, M. E. (2024) · Surgical Neurology International · doi:10.25259/sni_773_2023 · Cited by 22
Neuroprotective Roles of the Biliverdin Reductase-A/Bilirubin Axis in the Brain
Paul, B. D., & Pieper, A. A. (2024) · Biomolecules · doi:10.3390/biom14020155 · Cited by 21
Self-citation
Dibenzo[b,f]oxepine Molecules Used in Biological Systems and Medicine
Krawczyk, H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241512066 · Cited by 20
Application of P7C3 Compounds to Investigating and Treating Acute and Chronic Traumatic Brain Injury
Sridharan, P. S., Miller, E., & Pieper, A. (2023) · Neurotherapeutics · doi:10.1007/s13311-023-01427-8 · Cited by 16
Self-citation
Nanocarrier-mediated siRNA delivery: a new approach for the treatment of traumatic brain injury–related Alzheimer’s disease
Jin, J., Zhang, H., Lu, Q., Tian, L., Yao, S., Lai, F., Liang, Y., Liu, C., Lu, Y., Tian, S., et al. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00303 · Cited by 20
Perioperative neurocognitive disorders: Advances in molecular mechanisms and bioactive molecules
Mao, L., Wang, L., Huang, Z., Switzer, J. A., Hess, D. C., & Zhang, Q. (2025) · Ageing Research Reviews · doi:10.1016/j.arr.2025.102885 · Cited by 24
Unraveling the Influence of K280 Acetylation on the Conformational Features of Tau Core Fragment: A Molecular Dynamics Simulation Study
Zou, Y. F., & Guan, L. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.801577 · Cited by 19
Pharmacological modulation of the PI3K/AKT/GSK3β axis: a new frontier in Alzheimer’s disease treatment
Alqahtani, S. M., Al-Kuraishy, H. M., Al-Gareeb, A. I., Albuhadily, A. K., Shokr, M. M., Alexiou, A. T., Papadakis, M., & Batiha, G. E. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-02000-9 · Cited by 21
Pharmacologic reversal of advanced Alzheimer’s disease in mice and identification of potential therapeutic nodes in human brain
Chaubey, K., Vázquez‐Rosa, E., Tripathi, S. J., Shin, M., Yu, Y., Dhar, M., Chakraborty, S., Yamakawa, M., Wang, X., Sridharan, P. S., et al. (2025) · Cell Reports Medicine · doi:10.1016/j.xcrm.2025.102535 · Cited by 21
Self-citation
Interpretable artificial intelligence and exascale molecular dynamics simulations to reveal kinetics: Applications to Alzheimer's disease
Martin, W., Sheynkman, G., Lightstone, F. C., Nussinov, R., & Cheng, F. (2021) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2021.09.001 · Cited by 20
Self-citation
Structural basis for binding diversity of acetyltransferase p300 to the nucleosome
Hatazawa, S., Liu, J., Takizawa, Y., Zandian, M., Negishi, L., Kutateladze, T. G., & Kurumizaka, H. (2022) · iScience · doi:10.1016/j.isci.2022.104563 · Cited by 18
The regulatory role of Pin1 in neuronal death
Xiong, K., Wang, S., & Hu, X. (2022) · Neural Regeneration Research · doi:10.4103/1673-5374.341043 · Cited by 19
Inhibiting 15-PGDH blocks blood–brain barrier deterioration and protects mice from Alzheimer’s disease and traumatic brain injury
Koh, Y., Vázquez‐Rosa, E., Gao, F., Li, H., Chakraborty, S., Tripathi, S. J., Barker, S., Bud, Z., Bangalore, A., Kandjoze, U. P., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2417224122 · Cited by 17
Self-citation
Reduced ULK1 links impaired autophagy and mitophagy to Alzheimer’s disease pathology
Pan, J., Wang, P.-J., Zhang, J., Knapskog, A., Watne, L. O., Wang, H.-L., Lagartos-Donate, M. J., Lautrup, S., Mao, L.-P., Wang, Q., et al. (2026) · Nature Aging · doi:10.1038/s43587-026-01108-z · Cited by 20
Self-citation
Anti-inflammatory Therapy Protects Spiral Ganglion Neurons After Aminoglycoside Antibiotic-Induced Hair Cell Loss
Rahman, M. T., Bailey, E. M., Gansemer, B. M., Pieper, A. A., Manak, J. R., & Green, S. H. (2023) · Neurotherapeutics · doi:10.1007/s13311-022-01336-2 · Cited by 17
Self-citation
Traumatic brain injury derived pathological tau polymorphs induce the distinct propagation pattern and neuroinflammatory response in wild type mice
Puangmalai, N., Bhatt, N. N., Bittar, A., Jerez, C., Shchankin, N., & Kayed, R. (2023) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2023.102562 · Cited by 17
Inhibition of TREM-1 alleviates neuroinflammation by modulating microglial polarization via SYK/p38MAPK signaling pathway after traumatic brain injury
Zhao, T., Zhou, Y., Zhang, D., Han, D., Ma, J., Li, S., Li, T., Hu, S., & Li, Z. (2024) · Brain Research · doi:10.1016/j.brainres.2024.148907 · Cited by 18
Enhanced Fyn-tau and NR2B-PSD95 interactions in epileptic foci in experimental models and human epilepsy
Putra, M. R. E., Rao, N. S., Gardner, C., Liu, G., Trommater, J., Bunney, M., Gage, M., Bassuk, A. G., Hefti, M. M., Lee, G. S., et al. (2024) · Brain Communications · doi:10.1093/braincomms/fcae327 · Cited by 17
Single‐microglia transcriptomic transition network‐based prediction and real‐world patient data validation identifies ketorolac as a repurposable drug for Alzheimer's disease
Xu, J., Song, W., Xu, Z., Danziger, M. M., Karavani, E., Zang, C., Chen, X., Li, Y., Paz, I. R., Gohel, D., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14373 · Cited by 17
Self-citation
Leukemia inhibitory factor receptor homodimerization mediated by acetylation of extracellular lysine promotes prostate cancer progression through the PDPK1/AKT/GCN5 axis
Ding, Y., Chi, H., Shao, J., Shi, T., Yu, H. T., Wang, X., & Wang, X. (2022) · Clinical and Translational Medicine · doi:10.1002/ctm2.676 · Cited by 17
Accumulation of pTau231 at the Postsynaptic Density in Early Alzheimer’s Disease
Lilek, J. N., Ajroud, K., Feldman, A. Z., Krishnamachari, S., Ghourchian, S., Gefen, T. D., Spencer, C., Kawles, A., Mao, Q., Tranovich, J. F., et al. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-220848 · Cited by 16
Self-citation
Herbacetin alleviates ferroptosis via Hif-1α/SLC7A11/GPX4 axis in traumatic brain injury
Qian, W., Chen, X., Gu, L., Lin, X., Chen, J., Xu, D., Wang, H., Long, F., Zhuge, Q., Zhang, P., et al. (2025) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2025.06.030 · Cited by 15
Self-citation
Integrative Diagnostic and Prognostic Paradigms in Diffuse Axonal Injury: Insights from Clinical, Histopathological, Biomolecular, Radiological, and AI-Based Perspectives
Santurro, A., Simone, M. D., Choucha, A., Morena, D., Consalvo, F., Romano, D. G., Terrasi, P., Corrivetti, F., Scrofani, R., Narciso, N., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26167808 · Cited by 15
Cytokines and related signaling pathways in traumatic brain injury
Zhu, L., Huang, S., Chen, W., Li, K., & Sheng, J. (2026) · Frontiers in Immunology · doi:10.3389/fimmu.2026.1738589 · Cited by 18
Modifiable risk factors of dementia linked to excitation-inhibition imbalance
Hafizi, S., & Rajji, T. K. (2022) · Ageing Research Reviews · doi:10.1016/j.arr.2022.101804 · Cited by 16
DNALI1 Promotes Neurodegeneration after Traumatic Brain Injury via Inhibition of Autophagosome‐Lysosome Fusion
Ding, X., Cao, S., Wang, Q., Du, B., Lu, K., Qi, S., Cheng, Y., Tuo, Q., Liang, W., & Lei, P. (2024) · Advanced Science · doi:10.1002/advs.202306399 · Cited by 14
Ferroptosis: A new strategy for targeting Alzheimer’s disease
Qiang, R. R., Xiang, Y., Zhang, L., Bai, X. Y., Zhang, D., Li, Y. J., Yang, Y. L., & Liu, X. L. (2024) · Neurochemistry International · doi:10.1016/j.neuint.2024.105773 · Cited by 15
The importance of behavioral interventions in traumatic brain injury
Buccilli, B., Alan, A., Aljeradat, B., Shahzad, A., Almealawy, Y. F., Chisvo, N. S., Ennabe, M., & Weinand, M. E. (2024) · Surgical Neurology International · doi:10.25259/sni_776_2023 · Cited by 14
Glutathionylation of a glycolytic enzyme promotes cell death and vigor loss during aging of elm seeds
Li, Y., Wang, Y., He, Y., Ye, T.-T., Huang, X., Wu, H., Ma, T.-X., Pritchard, H. W., Wang, X., & Xue, H. (2024) · PLANT PHYSIOLOGY · doi:10.1093/plphys/kiae197 · Cited by 14
The evolution of S-nitrosylation detection methodology and the role of protein S-nitrosylation in various cancers
Liang, F., Wang, M., Li, J., & Guo, J. (2024) · Cancer Cell International · doi:10.1186/s12935-024-03568-y · Cited by 14
Insulin-incubated palladium clusters promote recovery after brain injury
Fu, S., Zhao, S. Y., Chen, H., Yang, W., Xia, X., Xu, X., Liang, Z., Feng, X., Wang, Z., Ai, P., et al. (2022) · Journal of Nanobiotechnology · doi:10.1186/s12951-022-01495-6 · Cited by 14
Treatment and Rehabilitation for Traumatic Brain Injury: Current Update
Min, J. H., & Shin, Y. (2022) · Brain & Neurorehabilitation · doi:10.12786/bn.2022.15.e14 · Cited by 16
Trans- and Cis-Phosphorylated Tau Protein: New Pieces of the Puzzle in the Development of Neurofibrillary Tangles in Post-Ischemic Brain Neurodegeneration of the Alzheimer’s Disease-like Type
Pluta, R. M., & Czuczwar, S. J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063091 · Cited by 13
Characterisation of Severe Traumatic Brain Injury Severity from Fresh Cerebral Biopsy of Living Patients: An Immunohistochemical Study
Yip, P. K., Hasan, S., Liu, Z., & Uff, C. E. G. (2022) · Biomedicines · doi:10.3390/biomedicines10030518 · Cited by 13
Unknown roles of tau pathology in neurological disorders. Challenges and new perspectives
Olesen, M. A., Villavicencio-Tejo, F., Cuevas-Espinoza, V., & Quintanilla, R. A. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102594 · Cited by 12
Direct Quantification of Neuroprotective Effect of Single‐Atom Catalyst on Neurochemical Transmission by Multi‐Spatiotemporal Electrochemistry
Ma, W., Zhao, G., Liu, R., Li, K., Wu, W., Liu, J., He, X., Hou, L., Yu, P., & Mao, L. (2025) · Angewandte Chemie International Edition · doi:10.1002/anie.202502163 · Cited by 12

Authors: 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., Seth, D., Allen, R. S., Motz, C. T., Rao, S. R., Skelton, L. A., Pardue, M. T., Fliesler, S. J., Wang, C., Tracy, T. E., Gan, L., Liebl, D. J., Savarraj, J. P. J., Torres, G. L., Ahnstedt, H., McCullough, L. D., Kitagawa, R. S., Choi, H. A., Zhang, P., Hou, Y., Chiang, C.-W., Li, L., Ortiz, F., Kilgore, J. A., Williams, N. S., Whitehair, V. C., Gefen, T., Flanagan, M. E., Stamler, J. S., Jain, M. K., Kraus, A., Cheng, F., Reynolds, J. D., & Pieper, A. A.
Affiliations: University Hospitals of Cleveland (US)
University of Iowa (US)
Georgia Institute of Technology (US)
Buffalo VA Medical Center (US)
Gladstone Institutes (US)
Buck Institute for Research on Aging (US)
Weill Cornell Medicine (US)
University of Miami (US)
The University of Texas Health Science Center at Houston (US)
The Ohio State University (US)
Cleveland Clinic (US)
The University of Texas Southwestern Medical Center (US)
MetroHealth (US)
Northwestern University (US)
Case Western Reserve University (US)
Cornell University (US)
Corresponding author: Pieper, Andrew A.
ORCID: Shin, Min-Kyoo
Koh, Yeojung
Dhar, Matasha
Chaubey, Kalyani
Cintrón-Pérez, Coral J.
Barker, Sarah
Miller, Emiko
Franke, Kathryn
Noterman, Maria F.
Seth, Divya
Allen, Rachael S.
Motz, Cara T.
Rao, Sriganesh Ramachandra
Skelton, Lara A.
Pardue, Machelle T.
Fliesler, Steven J.
Wang, Chao
Tracy, Tara E.
Gan, Li
Liebl, Daniel J.
Savarraj, Jude P.J.
Ahnstedt, Hilda
McCullough, Louise D.
Choi, H. Alex
Zhang, Pengyue
Chiang, Chien-Wei
Li, Lang
Kilgore, Jessica A.
Williams, Noelle S.
Whitehair, Victoria C.
Gefen, Tamar
Flanagan, Margaret E.
Stamler, Jonathan S.
Jain, Mukesh K.
Kraus, Allison
Cheng, Feixiong
Reynolds, James D.
Pieper, Andrew A.
Venue: Cell
Publisher: Elsevier BV
Published: 2021-05
Volume: 184
Issue: 10
Pages: 2715-2732.e23
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/j.cell.2021.03.032
PMC: PMC8491234
OpenAlex: W3152963650
Cited by: 226
References: 64
Citations by year: 2026: 36 · 2025: 60 · 2024: 45 · 2023: 40 · 2022: 34 · 2021: 11
FWCI: 20.89
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 377 d)
Locations: Cell (publishedVersion)
PubMed (publishedVersion)
Europe PMC (PubMed Central) (acceptedVersion)
PubMed Central (acceptedVersion)
Funders: U.S. Department of Veterans Affairs (I01 BX002439, IK2 RX002928)
National Institutes of Health (5p30ag062428-02, UL1TR001412)
National Institute on Aging (P30-AG062428, F32AG043301, R01AG066707, K01AG057862, R01AG062566, P30AG013854, K08AG065463)
National Cancer Institute (P01CA217797, T32CA078586)
National Institute of General Medical Sciences (T32GM007250)
National Institute of Neurological Disorders and Stroke (R01NS098740)
National Center for Advancing Translational Sciences
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Clinical Neurology › Traumatic Brain Injury Research
Health Sciences › Medicine › Clinical Neurology › Traumatic Brain Injury and Neurovascular Disturbances
Keywords: tau acetylation, traumatic brain injury, Alzheimer's disease, SIRT1, neurodegeneration, neurobehavioral impairment, blood biomarkers, salsalate, diflunisal, neuroprotection
MeSH terms: Neuroprotection, Brain Injuries, Traumatic, p300-CBP-Associated Factor, Acetylation, Alzheimer Disease, Animals, Anti-Inflammatory Agents, Non-Steroidal, Cell Line, Diflunisal, Female, Humans, Male, Mice, Inbred C57BL, Neurons, Salicylates, Biomarkers, tau Proteins, Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating), p300-CBP Transcription Factors, Mice, Sirtuin 1

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

Reducing acetylated tau is neuroprotective in brain injury

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks