Reactivating Kinase/p38 Phosphorylates τ Protein In Vitro

Bip Enhanced the Association of GSK-3β with Tau During ER Stress Both in vivo and in vitro

Liu, Z.-C., Fu, Z., Song, J., Zhang, J. Y., Wei, Y., Chu, J., Han, L., Qu, N., Wang, J., & Tian, Q. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-111898 · Cited by 36

Feasibility of β-Sheet Breaker Peptide-H102 Treatment for Alzheimer's Disease Based on β-Amyloid Hypothesis

Lin, L., Xiangyu, B. O., Tan, Y., Sun, F.-X., Song, M., Zhao, J., Zhihong, M., Li, M., ZHENG, K., & Xu, S. (2014) · PLoS ONE · doi:10.1371/journal.pone.0112052 · Cited by 35

Asiaticoside ameliorates β-amyloid-induced learning and memory deficits in rats by inhibiting mitochondrial apoptosis and reducing inflammatory factors

Zhang, Z., Li, X., Li, D., Luo, M., Li, Y., Li, S., & Jiang, X. (2016) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2016.4004 · Cited by 35

Alzheimer risk gene product Pyk2 suppresses tau phosphorylation and phenotypic effects of tauopathy

Brody, A. H., Nies, S. H., Guan, F., Smith, L. M., Mukherjee, B., Salazar, S. A., Lee, S., Lam, T. K. T., & Strittmatter, S. M. (2022) · Molecular Neurodegeneration · doi:10.1186/s13024-022-00526-y · Cited by 36

Effect of Gender on Mitochondrial Toxicity of Alzheimer's A β Peptide

Viña, J., Lloret, A., Vallés, S. L., Borrás, C., Badía, M.-C., Pallardó, F. V., Sastre, J., & Alonso, M.-D. (2007) · Antioxidants and Redox Signaling · doi:10.1089/ars.2007.1773 · Cited by 33

The p38 pathway is activated in Pick disease and progressive supranuclear palsy: a mechanistic link between mitogenic pathways, oxidative stress, and tau

HARTZLER, A., ZHU, X., SIEDLAK, S., CASTELLANI, R., AVILA, J., PERRY, G., & SMITH, M. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(02)00029-5 · Cited by 43

Implication of JNK pathway on tau pathology and cognitive decline in a senescence-accelerated mouse model

Orejana, L., Barros-Miñones, L., Aguirre, N., & Puerta, E. (2013) · Experimental Gerontology · doi:10.1016/j.exger.2013.03.001 · Cited by 32

Glycogen synthase kinase 3 (GSK3) inhibition: a potential therapeutic strategy for Alzheimer’s disease

Karati, D., Meur, S., Roy, S., Mukherjee, S., Debnath, B., Jha, S. K., Sarkar, B. K., Naskar, S., & Ghosh, P. (2024) · Naunyn-Schmiedeberg s Archives of Pharmacology · doi:10.1007/s00210-024-03500-1 · Cited by 31

Argyrophilic grain disease: An update on a frequent cause of dementia

Grinberg, L. T., & Heinsen, H. (2009) · Dementia & Neuropsychologia · doi:10.1590/s1980-57642009dn30100002 · Cited by 31

p38 Mitogen Activated Protein Kinase as a Therapeutic Target for Alzheimer's Disease

Dalrymple, S. A. (2002) · Journal of Molecular Neuroscience · doi:10.1385/jmn:19:3:295 · Cited by 30

Trophic Factor Modulation of c-Jun Expression in Supraspinal Neurons after Chronic Spinal Cord Injury

Houlé, J. D., Schramm, P., & Herdegen, T. (1998) · Experimental Neurology · doi:10.1006/exnr.1998.6954 · Cited by 29

Active stress kinase p38 enhances and perpetuates abnormal tau phosphorylation and deposition in Pick?s disease

Puig, B., Vinals, F., & Ferrer, I. (2004) · Acta Neuropathologica · doi:10.1007/s00401-003-0793-z · Cited by 27

Free PKC catalytic subunits (PKM) phosphorylate tau via a pathway distinct from that utilized by intact PKC

Ekinci, F. J., & SHEA, T. B. (1999) · Brain Research · doi:10.1016/s0006-8993(99)02146-0 · Cited by 26

Alterations of tau and VASP during microcystin‐LR‐induced cytoskeletal reorganization in a human liver cell line

Sun, Y., Liu, J., Huang, P., Guo, Z., & Xu, L. (2013) · Environmental Toxicology · doi:10.1002/tox.21898 · Cited by 25

p38 mitogen‐activated protein kinase: Functions and targeted therapy in diseases

Zheng, Q., Li, S., Wang, A., Zhe, M., Yang, P., Wu, Y., Zhao, M., Zhu, Y., Luo, Y., Wang, G., et al. (2023) · MedComm – Oncology · doi:10.1002/mog2.53 · Cited by 24

p38 Inhibition Decreases Tau Toxicity in Microglia and Improves Their Phagocytic Function

Perea, J. R., Bolós, M., Cuadros, R., García, E., García‐Escudero, V., Hernández, F., McManus, R. M., Heneka, M. T., & Ávila, J. (2022) · Molecular Neurobiology · doi:10.1007/s12035-021-02715-0 · Cited by 24

Phosphorylation state of tau in the hippocampus of apolipoprotein E4 and E3 knock-in mice

Kobayashi, M., Ishiguro, K., Fukui, Y., Yokoyama, M., & Fujita, S. C. (2003) · Neuroreport · doi:10.1097/00001756-200304150-00008 · Cited by 23

Activation Mechanism of c-Jun Amino-terminal Kinase in the Course of Neural Differentiation of P19 Embryonic Carcinoma Cells

Akiyama, S., Yonezawa, T., Kudo, T., Li, M. G., Wang, H., Ito, M., Yoshioka, K., Ninomiya‐Tsuji, J., Matsumoto, K., Kanamaru, R., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406610200 · Cited by 20

p38 activation occurs mainly in microglia in the P301S Tauopathy mouse model

Perea, J. R., García, E., Vallés‐Saiz, L., Cuadros, R., Hernández, F., Bolós, M., & Ávila, J. (2022) · Scientific Reports · doi:10.1038/s41598-022-05980-8 · Cited by 16

Atypical role of proximal caspase-8 in truncated Tau-induced neurite regression and neuronal cell death.

Chung, C., Hong, Y.-M., Song, S.-M., Woo, H.-N., Choi, Y.-H., Rohn, T., & Jung, Y.-K. (2003) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.08.017 · Cited by 18

Road to Alzheimer’s Disease: The Pathomechanism Underlying

Anand, R., Kaushal, A., Wani, W. Y., & Gill, K. D. (2011) · Pathobiology · doi:10.1159/000332218 · Cited by 16

Arsenic and Tau Phosphorylation: A Mechanistic Review

Ariafar, S., Makhdoomi, S., & Mohammadi, M. (2023) · Biological Trace Element Research · doi:10.1007/s12011-023-03634-y · Cited by 13

Drosophila Toll-9 is induced by aging and neurodegeneration to modulate stress signaling and its deficiency exacerbates tau-mediated neurodegeneration

Sakakibara, Y., Yamashiro, R., Chikamatsu, S., Hirota, Y., Tsubokawa, Y., Nishijima, R., Takei, K., Sekiya, M., & Iijima, K. (2023) · iScience · doi:10.1016/j.isci.2023.105968 · Cited by 14

Tau Loss of Function, by Deletion or Aggregation, Contributes to Peripheral Insulin Resistance

Al‐Lahham, R., & Méndez, N. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-230392 · Cited by 13

Gene-environment interplay in neurogenesis and neurodegeneration

Palomo, T., Archer, T., Beninger, R. J., & Kostrzewa, R. M. (2004) · Neurotoxicity Research · doi:10.1007/bf03033279 · Cited by 11

Tau Phosphorylation

Buée, L., & Delacourte, A. (2001) · Elsevier eBooks · doi:10.1016/b978-012351830-9/50023-8 · Cited by 8

STAU1 exhibits a dual function by promoting amyloidogenesis and tau phosphorylation in cultured cells

Li, C., Zhou, G., Xie, X., Wang, L., Chen, X., Pan, Q., Pu, Y., Yang, J., Li, S., & Chen, G. (2024) · Experimental Neurology · doi:10.1016/j.expneurol.2024.114805 · Cited by 9

Anesthesia promotes acute expression of genes related to Alzheimer’s disease and latent tau aggregation in transgenic mouse models of tauopathy

Eun, J. D., Jimenez, H. T., Adrien, L. R., Wolin, A., Marambaud, P., Davies, P., & Koppel, J. L. (2022) · Molecular Medicine · doi:10.1186/s10020-022-00506-4 · Cited by 7

MPC-n (IgG) improves long-term cognitive impairment in the mouse model of repetitive mild traumatic brain injury

Zhang, C., Wei, C., Huang, X., Hou, C., Liu, C., Zhang, S., Zhao, Z., Liu, Y., Zhang, R., Zhou, L., et al. (2023) · BMC Medicine · doi:10.1186/s12916-023-02895-7 · Cited by 7

Do aluminium and/or glutamate induce Alzheimer PHF-like formation? An electron microscopic study

Jones, K. R., Black, M. J., & Oorschot, D. E. (1998) · Journal of Neurocytology · doi:10.1023/a:1006939020525 · Cited by 5

Differential Expression of Neurodegeneration-Related Genes in SH-SY5Y Neuroblastoma Cells Under the Influence of Cyclophilin A: Could the Enzyme be a Likely Trigger and Therapeutic Target for Alzheimer’s Disease?

Pashaei, S., Shabani, S., Mohammadi, S., Morozova‐Roche, L. A., Salari, N., Rahimi, Z., & Khodarahmi‬, R. (2024) · Neurochemical Research · doi:10.1007/s11064-024-04253-2 · Cited by 4

Disease phenotypic screening in neuron-glia cocultures identifies blockers of inflammatory neurodegeneration

Birkle, T. J. Y., Willems, H. M. G., Skidmore, J., & Brown, G. C. (2024) · iScience · doi:10.1016/j.isci.2024.109454 · Cited by 4

Tau Phosphorylation Both In Vitro and in Cells

Reynolds, C. H., Gibb, G., & Lovestone, S. (2003) · Humana Press eBooks · doi:10.1385/1-59259-195-7:375 · Cited by 4

Immediate Early Genes, Inducible Transcription Factors and Stress Kinases in Alzheimer’s Disease

Ferrer, I., Santpere, G., & Puig, B. (2006) · Springer eBooks · doi:10.1007/978-0-387-33604-6_13 · Cited by 2

CD2AP in Alzheimer's disease: Key mechanisms and therapeutic potential

Wang, Y., & Zhang, Y.-W. (2025) · Brain medicine : · doi:10.61373/bm025i.0026 · Cited by 2

Single-nucleus and spatial transcriptomic analysis identified molecular features of neuronal heterogeneity and distinct glial responses in Parkinson’s diseasePreprint

Yoo, S., Lee, K., Seo, J., Choi, H. K., Kim, S., Chang, J., Shim, Y., Kim, J., Won, J., & Park, S. (2024) · Research Square · doi:10.1101/2024.07.28.605055 · Cited by 2

Oxidative Stress and Alzheimer Disease: Mechanisms and Therapeutic Opportunities

Mondragón‐Rodríguez, S., García‐Sierra, F., Casadesús, G., Lee, H., Petersen, R. B., Perry, G. L., Zhu, X., & Smith, M. A. (2010) · Advances in neurobiology · doi:10.1007/978-1-4419-7104-3_18 · Cited by 1

Chemokines in the Central Nervous System and Alzheimer's Disease

Xia, M. Q., & Hyman, B. T. (2002) · Elsevier eBooks · doi:10.1016/b978-044451002-0/50026-9 · Cited by 1

Distinct Tau Gene Mutations Induce Specific Dysfunctions/Toxic Properties in Tau Proteins Associated With Specific FTDP-17 Phenotypes

Lee, V. M. Y., & Trojanowski, J. Q. (2000) · Research and perspectives in Alzheimer's disease · doi:10.1007/978-3-662-04056-0_7 · Cited by 1

Metabolic Abnormalities in Alzheimer Disease

Gebhardt, F. M., & Dodd, P. R. (2008) · Springer eBooks · doi:10.1007/978-0-387-79112-8_22 · Cited by 1

Cooperative calcium and zinc signaling underlies oxidantinduced neuronal injury

McCord, M. C. (2013) · D-Scholarship@Pitt (University of Pittsburgh)

Factors patogènics convergents en taupaties

Santpere, G. (2009) · LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas)

Preclinical characterization of the myxobacterial compound pretubulysin as novel vascular disrupting agent

Kretzschmann, V. K. (2013) · Electronic Theses of LMU Munich (Ludwig-Maximilians-Universität München) · doi:10.5282/edoc.16431

Modulation of growth factor-induced ERK signaling by the microtubule associated protein tau

Leugers, C. J. (2010) · doi:10.17077/etd.44cmdeo5

Modulation of Alzheimer's Disease Pathology and Neuroplasticity by Environmental Factors

Hu, Y. (2012) · Figshare

The Functional Role of the Microtubule/Microfilament Cytoskeleton in the Regulation of Pulmonary Vascula rEndothelial Barrier

Gouget, C. L. M. (2013) · CRC Press eBooks · doi:10.1201/b15421-7

Alzheimer Disease

Obrenovich, M. E., Raina, A. K., Ogawa, O., Atwood, C., Morelli, L., & Smith, M. A. (2007) · Springer eBooks · doi:10.1007/0-387-29390-6_6

Additional file 5 of MPC-n (IgG) improves long-term cognitive impairment in the mouse model of repetitive mild traumatic brain injury

Zhang, C., Wei, C., Huang, X., Hou, C., Liu, C., Zhang, S., Zhao, Z., Liu, Y., Zhang, R., Zhou, L., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23265018

Additional file 4 of MPC-n (IgG) improves long-term cognitive impairment in the mouse model of repetitive mild traumatic brain injury

Zhang, C., Wei, C., Huang, X., Hou, C., Liu, C., Zhang, S., Zhao, Z., Liu, Y., Zhang, R., Zhou, L., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23265015

Additional file 9 of MPC-n (IgG) improves long-term cognitive impairment in the mouse model of repetitive mild traumatic brain injury

Zhang, C., Wei, C., Huang, X., Hou, C., Liu, C., Zhang, S., Zhao, Z., Liu, Y., Zhang, R., Zhou, L., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23265030

Additional file 1 of Alzheimer risk gene product Pyk2 suppresses tau phosphorylation and phenotypic effects of tauopathy

Brody, A. H., Nies, S. H., Guan, F., Smith, L. M., Mukherjee, B., Salazar, S. A., Lee, S., Lam, T. K. T., & Strittmatter, S. M. (2022) · Figshare · doi:10.6084/m9.figshare.19695711

Additional file 7 of MPC-n (IgG) improves long-term cognitive impairment in the mouse model of repetitive mild traumatic brain injury

Zhang, C., Wei, C., Huang, X., Hou, C., Liu, C., Zhang, S., Zhao, Z., Liu, Y., Zhang, R., Zhou, L., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23265024

Additional file 1 of MPC-n (IgG) improves long-term cognitive impairment in the mouse model of repetitive mild traumatic brain injury

Zhang, C., Wei, C., Huang, X., Hou, C., Liu, C., Zhang, S., Zhao, Z., Liu, Y., Zhang, R., Zhou, L., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23265006

Additional file 2 of MPC-n (IgG) improves long-term cognitive impairment in the mouse model of repetitive mild traumatic brain injury

Zhang, C., Wei, C., Huang, X., Hou, C., Liu, C., Zhang, S., Zhao, Z., Liu, Y., Zhang, R., Zhou, L., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23265009

Additional file 3 of MPC-n (IgG) improves long-term cognitive impairment in the mouse model of repetitive mild traumatic brain injury

Zhang, C., Wei, C., Huang, X., Hou, C., Liu, C., Zhang, S., Zhao, Z., Liu, Y., Zhang, R., Zhou, L., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23265012

Additional file 6 of MPC-n (IgG) improves long-term cognitive impairment in the mouse model of repetitive mild traumatic brain injury

Zhang, C., Wei, C., Huang, X., Hou, C., Liu, C., Zhang, S., Zhao, Z., Liu, Y., Zhang, R., Zhou, L., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23265021

Additional file 1 of Anesthesia promotes acute expression of genes related to Alzheimer’s disease and latent tau aggregation in transgenic mouse models of tauopathy

Eun, J. D., Jimenez, H. T., Adrien, L. R., Wolin, A., Marambaud, P., Davies, P., & Koppel, J. L. (2022) · Figshare · doi:10.6084/m9.figshare.20347460

Additional file 8 of MPC-n (IgG) improves long-term cognitive impairment in the mouse model of repetitive mild traumatic brain injury

Zhang, C., Wei, C., Huang, X., Hou, C., Liu, C., Zhang, S., Zhao, Z., Liu, Y., Zhang, R., Zhou, L., et al. (2023) · Figshare · doi:10.6084/m9.figshare.23265027

Repeated mild spinal cord contusions exacerbate tauopathy development in PS19 mice

Halloin, N., Debortoli, N., Lopez‐Gutierrez, L., COLLIGNON, H., Marlier, Z., Ando, K., Suain, V., Conrard, L., Mignolet, M., Sprimont, L., et al. (2026) · Acta Neuropathologica Communications · doi:10.1186/s40478-026-02378-9

Functional Study of the Threonine Phosphorylation and the Transcriptional Coactivator Role of P68 RNA Helicase

Dey, H. T. (2012) · Digital Archive @ GSU · doi:10.57709/3489823

Role of the microtubulin-associated molecule tau in inflammatory-mediated axonal damage

Gorlovoy, P. (2008) · doi:10.53846/goediss-3390

Topographic organization of connections between the hypothalamus and prefrontal cortex in the rhesus monkey

Rempel-Clower, N. L., & Barbas, H. (1998) · The Journal of Comparative Neurology · doi:10.1002/(sici)1096-9861(19980831)398:3

Stress‐Activated Protein Kinase/c‐Jun N‐Terminal Kinase Phosphorylates τ Protein

Reynolds, C. H., Utton, M. A., Gibb, G., Yates, A., & Anderton, B. H. (1997) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1997.68041736.x · Cited by 214

Phosphorylation of microtubule‐associated protein tau by stress‐activated protein kinases

Goedert, M., Hasegawa, M., Jakes, R., Lawler, S., Cuenda, A., & Cohen, P. R. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00483-3 · Cited by 308

P2‐149: The role of protein kinase A in coordinating tau phosphorylation state relevant to Alzheimer's disease

Seereeram, A., Siemann, M., Anderton, B. H., & Hanger, D. P. (2008) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2008.05.1222

P3‐024: An unbiased approach to identifying tau kinases that phosphorylate tau at sites associated with early Alzheimer's disease

Bose, S., Cavallini, A., Brewerton, S. C., Bell, A., Sargent, S., Glover, S. J., Hardy, C., Moore, R., Calley, J. N., Ramachandran, D., et al. (2012) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2012.05.1242

Phosphorylation Sites on Tau Identified by Nanoelectrospray Mass Spectrometry

Reynolds, C. H., Betts, J. C., Blackstock, W. P., Nebreda, Á. R., & Anderton, B. H. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741587.x · Cited by 372