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 accessAbstract
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.
Overview
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
Verification
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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“Beyond neurodegenerative and neurodevelopmental disorders, tau ablation has also been shown to improve outcomes in models of neurological injury and vascular stress, such TBI and high-salt diet-induced vascular dysfunction, with associated improvements in cognitive performance [72, 86, 87].”
From Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease (2026) · cites this paper as [72]
Experimental — accuracy not yet measuredIn the citing paper
“In addition, the acetylation of tau is an early pathological feature of neurodegeneration. Acetylated tau inhibits its degradation, promotes pathological aggregation and propagation, and contributes to tauopathy [46–51].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [51]
In the citing paper
“Inhibiting p300 with salsalate, a non-steroidal anti-inflammatory drug, could induce tau deacetylation, preserve tau axonal localization, and protect mice from neurodegeneration [51].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [51]
In the citing paper
“Abnormal acetylation of tau on lysine residues spans the microtubule-binding repeat region (MTBR), and this modification alone is sufficient to induce tau pathology and neurodegeneration [51].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [51]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
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
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
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-citationS-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
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
Cited by
Sorted by citations
Items 101–200 of 229
Nicotinamide Adenine Dinucleotide (NAD + )-Dependent Signaling in Neurological Disorders
Bresque, M., Esteve, D., Pehar, M., & Vargas, M. R. (2023) · Antioxidants and Redox Signaling · doi:10.1089/ars.2023.0241 · Cited by 13
Traumatic Brian Injury (TBI) unraveled: molecular disruptions and therapeutic avenues
Kumari, N., Bagri, K., Kumari, S., & Deshmukh, R. R. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01870-3 · Cited by 11
Li, H., Liu, Y., Wang, X., Xu, C., Zhang, X., Zhang, J., Lin, L., & Niu, Q. L. (2024) · Ecotoxicology and Environmental Safety · doi:10.1016/j.ecoenv.2024.115966 · Cited by 12
Wei, F., Hughes, M., Omer, M., Ngo, C., Pugazhendhi, A. S., Kolanthai, E., Aceto, M., Ghattas, Y. S., Razavi, M., Kean, T. J., et al. (2024) · Advanced Science · doi:10.1002/advs.202308698 · Cited by 11
Zhou, Y., Qiao, S., Zhang, L., Liu, M., Ji, Q., Zhang, B., Gao, H., Zhou, S., & Liu, D. (2025) · Journal of Controlled Release · doi:10.1016/j.jconrel.2025.113795 · Cited by 11
Antiepileptic Drugs as Potential Dementia Prophylactics Following Traumatic Brain Injury
Locskai, L. F., Alyenbaawi, H., & Allison, W. T. (2023) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-051921-013930 · Cited by 11
Zegarra-Valdivia, J. A., Pignatelli, J., Núñez, Á., & Torres‐Alemán, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms242216440 · Cited by 11
Targeting tau in traumatic brain injury
Crunkhorn, S. (2021) · Nature Reviews Drug Discovery · doi:10.1038/d41573-021-00070-2 · Cited by 10
Yang, Y., Li, C., Yang, S., Zhang, Z., Bai, X. H., Tang, H., & Huang, J. (2024) · Aging · doi:10.18632/aging.205678 · Cited by 10
Bahuguna, D., Amulya, E., Arya, S., Loharkar, S., Vambhurkar, G. B., Bhattacharjee, S., Chandanapalli, D. K., Madan, J., & Srivastava, S. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01923-7 · Cited by 11
Longitudinal in vivo monitoring of axonal degeneration after brain injury
Chornyy, S., Borovicka, J. A., Patel, D., Shin, M., Vázquez‐Rosa, E., Miller, E., Wilson, B. M., Pieper, A. A., & Dana, H. (2023) · Cell Reports Methods · doi:10.1016/j.crmeth.2023.100481 · Cited by 11
Self-citationNishiguchi, T., Yamanishi, K., Patel, S. S., Malicoat, J. R., Phuong, N. J., Seki, T., Ishii, T., Aoyama, B., Shimura, A., Gorantla, N., et al. (2024) · Translational Psychiatry · doi:10.1038/s41398-024-03130-4 · Cited by 9
Self-citationStress-induced nuclear GAPDH: Scientific update and clinical application
Vedula, P., Ishizuka, K., Hayashida, A., Sueo, K., & Sawa, A. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2025.e00725 · Cited by 9
Protein acylation in inflammatory diseases: from mechanisms to therapeutic strategies
Ding, J., Wang, H., Yang, Z., Wang, X., & Cao, Z. (2025) · Cell Communication and Signaling · doi:10.1186/s12964-025-02484-6 · Cited by 11
Targeting tau in Alzheimer’s Disease: rationale, approach and challenges
Aslanyan, A., Foiani, M. S., Giovannucci, T. A., McDade, E., Duff, K., Mummery, C. J., Schöll, M., Wildsmith, K. R., & Paterson, R. W. (2026) · Molecular Neurodegeneration · doi:10.1186/s13024-026-00925-5 · Cited by 10
Acetylated Tau Protein: A New Piece in the Puzzle between Brain Ischemia and Alzheimer’s Disease
Pluta, R. M., Januszewski, S., & Jabłoński, M. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23169174 · Cited by 8
Shareena, G., & Kumar, D. (2023) · Springer eBooks · doi:10.1007/978-981-99-2657-2_14 · Cited by 8
Yu, J., Zhao, Y., Gong, X., Liang, Z., Zhao, Y., Li, X., Chen, Y., Yang, Y., Wu, M., Wang, X., et al. (2023) · Current Medical Science · doi:10.1007/s11596-023-2792-8 · Cited by 8
Lin, C., Zhao, P., Sun, G., Liu, N., & Ji, J. (2024) · The FASEB Journal · doi:10.1096/fj.202401117r · Cited by 8
Transferrin and Borneol-Enhanced Liposomes for Targeted Rapamycin Delivery in TBI
Cai, S., Yuan, Z., Chen, Y., Gong, M., Lai, J., Yan, P., & Mei, Z. (2025) · International Journal of Nanomedicine · doi:10.2147/ijn.s489165 · Cited by 8
Role of sirtuins in cerebral ischemia-reperfusion injury: Mechanisms and therapeutic potential
Li, Z., & Xing, J. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143591 · Cited by 8
Oh, Y. R., & Shin, M. (2025) · BMB Reports · doi:10.5483/bmbrep.2025-0077 · Cited by 9
Self-citationRecent advances in Alzheimer’s disease: From molecular mechanisms to therapeutic strategies
Rudman, M. D., Ulrich, J. D., & Holtzman, D. M. (2026) · Cell · doi:10.1016/j.cell.2026.06.006 · Cited by 12
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 10
He, X. J., Cao, Z., Chen, X., Hu, J., Li, J., Jia, X., Wu, J., & Xuechun, L. (2025) · Brain and Behavior · doi:10.1002/brb3.70413 · Cited by 9
Zempel, H. (2023) · Cytoskeleton · doi:10.1002/cm.21793 · Cited by 7
Role of saturated fatty acid metabolism in posttranslational modifications of the Tau protein
García-Cruz, V. M., Coria, R., & Arias, C. (2025) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-025-05275-2 · Cited by 7
Neuschmid, S., Schallerer, C., Ehrlich, B. E., & McGuone, D. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26189245 · Cited by 8
Advances of therapeutic strategies for Alzheimer’s disease
Guo, X., Yue, R.-Z., Cui, Z., Wang, S., Jia, T., Li, W., Zhang, W., Shan, L., & Li, C. (2025) · Journal of Neurology · doi:10.1007/s00415-025-13456-8 · Cited by 9
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
Liu, Z., Li, X., Wang, Q., Liu, K., Zeng, W., Li, D., Zhao, K., Ma, Y., Long, H., Zhang, S., et al. (2026) · Journal of the American Chemical Society · doi:10.1021/jacs.5c22156 · Cited by 7
Self-citationHistone Deacetylation in Alzheimer’s Diseases (AD); Hope or Hype
Ateya, N. H., Al-Taie, S. F., Jasim, S. A., Uthirapathy, S., Chaudhary, K., Rani, P., Kundlas, M., Naidu, K. S., Amer, N. A., & Ahmed, J. K. (2025) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-025-01670-0 · Cited by 7
Wu, Y., Hu, Q., Wu, X., Cai, Y., Zhang, Y.-Z., Wu, Y., Zhu, G., Luo, J., Cheng, H.-B., Yu, J., et al. (2023) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2023/7857760 · Cited by 7
Wu, M., Song, W., Teng, L., Li, J., Liu, J., Ma, H., Zhang, G., Zhang, J., & Chen, Q. (2024) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2024.1405782 · Cited by 6
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 7
Smith, E. D., Torrellas, J., McKenna, R., Vo, Q., Mietzsch, M., Borchelt, D., Prokop, S., & Chakrabarty, P. (2025) · Journal of Neurochemistry · doi:10.1111/jnc.70221 · Cited by 6
Roles and therapeutic potential of PARP-1 in neurodegenerative diseases
Liu, C., Lai, F., Zhang, T., Mao, K., Wan, H., & He, Y. T. (2025) · Biochemical Pharmacology · doi:10.1016/j.bcp.2025.117373 · Cited by 7
Yue, C.-B., Luan, W.-W., Qiu, D., Ding, X., Gu, H.-W., Liu, P.-M., Hashimoto, K., Yang, J.-J., & Wang, X.-M. (2025) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2025.111702 · Cited by 6
Qiu, F., Liu, Y., & Liu, Z. (2024) · Aging and Disease · doi:10.14336/ad.2024.0099 · Cited by 6
Luan, W.-W., Gu, H., Qiu, D., Ding, X., Liu, P., Hashimoto, K., Yang, J., & Wang, X. (2025) · Neurochemistry International · doi:10.1016/j.neuint.2025.105961 · Cited by 6
Kane, E. I., Waters, K. L., & Spratt, D. E. (2021) · Cells · doi:10.3390/cells10082121 · Cited by 6
Ji, Y., Chen, Z., Cen, Z., Ye, Y., Li, S., Lu, X., Shao, Q., Wang, D., Ji, J., & Ji, Q. (2022) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2022.980815 · Cited by 7
DUB’ling down uncovers an X-linked vulnerability in Alzheimer’s disease
Paul, B. D. (2022) · Cell · doi:10.1016/j.cell.2022.09.029 · Cited by 6
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 6
Acetylation and deacetylation dynamics in stress response to cancer and infections
Li, L., Zeng, Y., Cheng, G., & Yang, H. (2025) · Seminars in Immunology · doi:10.1016/j.smim.2025.101957 · Cited by 5
Self-citationSu, W.-S., Wu, M.-T., Cheng, I. H.-J., & Yang, F. (2025) · Experimental Neurology · doi:10.1016/j.expneurol.2025.115420 · Cited by 5
Acetylated tau: A missing link between head injury and dementia
Zhao, Z., & Zloković, B. V. (2021) · Med · doi:10.1016/j.medj.2021.05.005 · Cited by 5
Molecular Mechanism of Tau Misfolding and Aggregation: Insights from Molecular Dynamics Simulation
Zhong, H., Liu, H., & Liu, H. (2023) · Current Medicinal Chemistry · doi:10.2174/0929867330666230409145247 · Cited by 5
The role of snapin in regulation of brain homeostasis
Li, J., Huang, X., An, Y., Chen, X., Chen, Y., Xu, M., Shan, H., & Zhang, M. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.389364 · Cited by 5
GFAP degradation in TBI: linking novel modified products to astrocyte pathology and patient outcome
Wanner, I. B., Halford, J., Lopez, J., Shen, S., Chen, Y., Zhao, H., Salas, C., Loo, R. R. O., Robicsek, S. A., Ellingson, B. M., et al. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02240-y · Cited by 5
Pathophysiology of Alzheimer’s Disease: Focus on H3 Receptor Modulators and Their Implications
Bandaru, N., Bukke, S. P. N., Pedapati, V. M. D., Sowjanaya, G., Suggu, V. S., Nalla, S., Dudhe, P. B., Ezeonwumelu, J. O. C., Alagbonsi, A. I., & Onohuean, H. (2025) · Drugs and Drug Candidates · doi:10.3390/ddc4020022 · Cited by 4
Kumar, M., Chaudhary, J., & Jain, A. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01823-w · Cited by 4
Deng, H., Zhang, S., Wang, H., Liu, X., Zhong, K., Huang, K., Li, Y., Deng, Z., Tong, A., & Zhou, L. (2026) · Experimental Neurology · doi:10.1016/j.expneurol.2026.115644 · Cited by 4
Artificial Intelligence to Guide Repurposing of Drugs
Fu, Z., Yang, Y., Chung, M. K., & Cheng, F. (2026) · Annual Review of Medicine · doi:10.1146/annurev-med-050224-122802 · Cited by 17
Self-citationChen, M., Gu, C., Lai, Y., Lin, Y., Xu, Y., Li, X., & Chen, X. (2026) · International Journal of Nanomedicine · doi:10.2147/ijn.s580440 · Cited by 4
Lv, X., Ye, T., Yang, W., Zhu, Z., Xiang, K., Lü, Z., Sun, J., & Liu, J. (2025) · Neurochemical Research · doi:10.1007/s11064-025-04423-w · Cited by 4
Giarratana, A. O. (2025) · Frontiers in Neurology · doi:10.3389/fneur.2025.1637243 · Cited by 4
Comprehensive bibliometric analysis of sirtuins: Focus on sirt1 and kidney disease
Liu, T., Mu, S., Yang, L., Mao, H., Ma, F., Wang, Y., & Zhan, Y. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.966786 · Cited by 4
Multifunctional Proteins and their Role in the Vital Activity of Cells
Korshunov, D. A., Sereda, E. E., & Кондакова, И. В. (2023) · Russian Journal of Bioorganic Chemistry · doi:10.1134/s1068162023030147 · Cited by 4
Lin, Y.-W., Jin, J., Han, Q., Hang, D., Chen, Z., Ye, S., Guo, Q., Huang, X.-Y., Li, J.-N., Zhang, H., et al. (2025) · Chemical Engineering Journal · doi:10.1016/j.cej.2025.166618 · Cited by 3
Long-term gabapentin treatment impairs cognitive function in aged mice via tau hyperphosphorylation
Xia, S., You, Z., Wu, X., Yang, J., Wang, S., Li, N., Dai, J., Dong, Y., Chen, L. L., Yan, M., et al. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1616775 · Cited by 3
Liang, Y., Zhao, D., Wu, P., Liang, Y., Zhang, X. Y., Xing, J., Sun, X., An, M., Shi, J., Gao, Q., et al. (2025) · Journal of the American Heart Association · doi:10.1161/jaha.125.043416 · Cited by 3
Ge, S., Chen, W., Huang, C., Shan, H., Ye, J., Li, J., & Gui, Y. (2024) · Journal of Cancer · doi:10.7150/jca.90439 · Cited by 3
SIRT1: potential target in glucocorticoid-resistant diseases
Xie, J., Che, S., Liu, J., & Long, X. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1514745 · Cited by 3
Liu, B., Zhao, Q., Shi, Q., Xu, W., Shi, F.-X., Yang, R., & Zhou, X. (2025) · Neurocritical Care · doi:10.1007/s12028-025-02293-2 · Cited by 4
Sun, F., & Huang, W. (2025) · Investigación Clínica · doi:10.54817/ic.v66n2a06 · Cited by 3
Xu, S., Zhu, J., Wen, J., Wang, C., Chen, X., Liao, W., Lu, Z., Wang, Z., & Gong, P. (2025) · Neurotherapeutics · doi:10.1016/j.neurot.2025.e00709 · Cited by 3
Self-citationPriemer, D. S., & Perl, D. P. (2022) · Free Neuropathology · doi:10.17879/freeneuropathology-2022-4495 · Cited by 3
Mignot, E. J.-M., Guen, Y. L., Luo, G., Ambati, A., Damotte, V., Jansen, I. E., Yu, E., Nicolas, A., de Rojas, I., Leal, T. P., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1285855/v1 · Cited by 3
Rogers, E. A., Diorio, T. C., Beauclair, T., Martinez, J., Mufti, S. J., Kim, D., Krishnan, N., Rayz, V. L., & Shi, R. (2025) · Lab on a Chip · doi:10.1039/d5lc00067j · Cited by 2
Vázquez‐Rosa, E., Shin, M., Chaubey, K., Barker, S., Corella, S. G., Chakraborty, S., Tripathi, S. J., Yu, Y., Hyung, J., Dashora, H. R., et al. (2026) · Redox Biology · doi:10.1016/j.redox.2026.104052 · Cited by 2
Self-citationBykova, M., Karavani, E., Danziger, M. M., Tonegawa‐Kuji, R., Martin, W., Sha, Z., Pieper, A. A., Rosen‐Zvi, M., & Cheng, F. (2026) · Neurotherapeutics · doi:10.1016/j.neurot.2026.e00836 · Cited by 2
Self-citationSex-specific effects of acetylation on tauopathy in aging htau mice
Sabir, U., Csubak, B. A., Ilchenko, S., ANSARI, M. Y. K., Kanaan, N. M., Tsai, T., Srinivasan, D., Dengler-Crish, C. M., & Kasumov, T. (2026) · Scientific Reports · doi:10.1038/s41598-026-41691-0 · Cited by 2
Molecular and environmental drivers of tau post-translational modifications and tau pathology
Price, T. M., Tucker, A. E., & Funk, K. E. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103223 · Cited by 2
Gao, T.-X., Liang, Y., Li, J., Zhao, D., Dong, B.-J., Xu, C., Zhao, W., Li, X., & Zhao, C. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114983 · Cited by 2
A prolyl oligopeptidase ligand blocks memory deficit in a repeated mild traumatic brain injury model
Uhari-Väänänen, J. K., Eteläinen, T. S., Zuo, C., Lorenzo, F. D., Kilpeläinen, T. P., & Myöhänen, T. T. (2025) · Experimental Neurology · doi:10.1016/j.expneurol.2025.115454 · Cited by 2
The role of protein phosphatase 2A tau axis in traumatic brain injury therapy
Salissou, M. T. M., Mahaman, Y. A. R., Wang, X., & Magaji, R. A. (2022) · Beni-Suef University Journal of Basic and Applied Sciences · doi:10.1186/s43088-022-00223-1 · Cited by 2
Age-related hearing loss: possible associations with Alzheimer’s disease
Ma, Y., Yang, Y., Zhou, Y.-F., Le, W., & Chai, R. (2024) · Ageing and Neurodegenerative Diseases · doi:10.20517/and.2024.24 · Cited by 1
Lin, J., Ma, J., Wang, Z., Xu, C., Sun, Y., Miao, Z., Chen, Z., Sun, Z., Zhang, X., & Wu, Y. (2025) · Life Sciences · doi:10.1016/j.lfs.2025.123689 · Cited by 1
Impact of Lysine Acetylation Mutations on the Structure of Full-Length Tau Fibrils
Dregni, A. J., & Hong, M. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00149 · Cited by 1
Study on the pathogenesis of vascular dementia by gene expression regulatory network
Bai, H. (2025) · Gene · doi:10.1016/j.gene.2025.149749 · Cited by 1
Garrahy, J. P. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251404970 · Cited by 1
Chen, W., Wu, Z., Lin, L., Huang, S., Jiang, Q., Huang, H., Xie, Y.-C., Huang, L.-X., Li, G., Fu, Q.-L., et al. (2026) · International Immunopharmacology · doi:10.1016/j.intimp.2026.116415 · Cited by 2
Hao, W., Sun, N., Xue, R., Chang, J., Pang, X., Zhou, Y., & Gao, C. (2026) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6c01290 · Cited by 1
Tan, C., Chen, L.-C., Guan, X., Huang, W., Feng, Y., Li, Z., Wu, L., Huang, X., Ouyang, Q., Liu, S., et al. (2024) · Journal of Translational Medicine · doi:10.1186/s12967-024-05068-z · Cited by 1
Bailey, C., Soden, D., Maroon, J. C., Selman, W. R., Tangen, C., Gunstad, J., Briskin, S. M., Miskovsky, S. N., Miller, E., & Pieper, A. A. (2024) · Neurotrauma Reports · doi:10.1089/neur.2023.0132 · Cited by 1
Self-citationBrieck, K., Brieck, Z. J., Ashby, J. A., Phelps, O. C., & Černak, I. (2025) · Cureus · doi:10.7759/cureus.77625 · Cited by 1
Kumar, M., Chaudhary, J., Kamboj, S., & Jain, A. (2025) · Inflammopharmacology · doi:10.1007/s10787-025-01845-4 · Cited by 1
Hsp multichaperone complex buffers pathologically modified TauPreprint
Moll, A., Ramirez, L. M., Ninov, M., Schwarz, J., Urlaub, H., & Zweckstetter, M. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.03.18.484853 · Cited by 1
DRD1 signaling enhances recovery after traumatic brain injury via an autophagy dependent pathway.Preprint
Lin, C., Chang, H., Bao, Z., Luo, H., Xu, L., Wu, W., Liu, N., & Ji, J. (2022) · Research Square · doi:10.21203/rs.3.rs-1598118/v1 · Cited by 1
S-Nitrosation-Based Target Discovery and Drug Development: Toward a Nitric Oxide Drug 2.0 Paradigm
Ye, H., Zhang, C., Zhang, Y., Wu, J., & Huang, Z. (2026) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6c00247 · Cited by 1
Tau Ablation Rewires Brain Cell Programs in Health and Restores Function in Disease
Chimal-Juárez, E., Patel, H., Jury-Garfe, N., Dabin, L. C., Vidal, R., Kim, J., & Lasagna-Reeves, C. A. (2026) · bioRxiv · doi:10.64898/2026.05.12.724684
Yates, D. M. (2021) · Nature reviews. Neuroscience · doi:10.1038/s41583-021-00471-7
Tau acetylation reduces its autophagic degradation and is a targetable pathway for human tauopathies
Johnson, N. R. (2022) · BioEssays · doi:10.1002/bies.202200062
Longitudinal in vivo monitoring of axonal integrity after brain injuryPreprint
Chornyy, S., Borovicka, J. A., Patel, D., Shin, M., Vázquez‐Rosa, E., Miller, E., Wilson, B. M., Pieper, A. A., & Dana, H. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.07.22.501178
Self-citationGherman, A.-M., Strilciuc, A., & Muresanu, D. F. (2022) · Journal of Medicine and Life · doi:10.25122/jml-2022-1012
Zhou, X., He, J., Yue, A., Song, H., Liu, X., Han, W., & Li, Q. (2023) · Research Square · doi:10.21203/rs.3.rs-2612464/v1
Chaubey, K., Alam, S. I., Waghmare, C. K., & Bhattacharya, B. K. (2023) · Toxicology Research · doi:10.1093/toxres/tfad013
Self-citationMultifunctional Proteins and Their Role in the Vital Activity of Cells
Korshunov, D. A., Sereda, E. E., & Кондакова, И. В. (2023) · Биоорганическая химия · doi:10.31857/s0132342323030144
Metadata
- 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)
- 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
- 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
