Reactivating Kinase/p38 Phosphorylates τ Protein In Vitro

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480 · see citing works

Activation and signaling of the p38 MAP kinase pathway

Zarubin, T., & Han, J. (2005) · Cell Research · doi:10.1038/sj.cr.7290257 · Cited by 1,711 · see citing works

Tau phosphorylation: the therapeutic challenge for neurodegenerative disease

Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965 · see citing works

MAP Kinases

Chen, Z., Gibson, T. B., Robinson, F. L., Silvestro, L., Pearson, G. W., Xu, B.-E., Wright, A., Vanderbilt, C. A., & Cobb, M. H. (2001) · Chemical Reviews · doi:10.1021/cr000241p · Cited by 789 · see citing works

Tau protein kinases: Involvement in Alzheimer's disease

Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631 · see citing works

JNK and p38 stresskinases — degenerative effectors of signal-transduction-cascades in the nervous system

Mielke, K., & Herdegen, T. (2000) · Progress in Neurobiology · doi:10.1016/s0301-0082(99)00042-8 · Cited by 489 · see citing works

Novel phosphorylation sites in tau from Alzheimer brain support a role for casein kinase 1 in disease pathogenesis

Hanger, D. P., Byers, H. L., Wray, S., Leung, K.-Y., Saxton, M. J., Seereeram, A., Reynolds, C. H., Ward, M. A., & Anderton, B. H. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m703269200 · Cited by 455 · see citing works

Why Women Have More Alzheimer's Disease Than Men: Gender and Mitochondrial Toxicity of Amyloid-β Peptide

Viña, J., & Lloret, A. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-100501 · Cited by 447 · see citing works

The complexity of mitogen-activated protein kinases (MAPKs) made simple

Krishna, M., & Narang, H. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8170-7 · Cited by 432 · see citing works

The Role of Mitogen-Activated Protein Kinase Pathways in Alzheimer’s Disease

Zhu, X., Lee, H., Raina, A. K., Perry, G. L., & Smith, M. A. (2002) · Neurosignals · doi:10.1159/000067426 · Cited by 392 · see citing works

Activation of p38 Kinase Links Tau Phosphorylation, Oxidative Stress, and Cell Cycle-Related Events in Alzheimer Disease

Zhu, X., Rottkamp, C. A., Boux, H., Takeda, A., Perry, G., & Smith, M. A. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.10.880 · Cited by 378 · see citing works

p38 Kinase Is Activated in the Alzheimer's Disease Brain

Hensley, K., Floyd, R. A., Zheng, N., Nael, R., Robinson, K. A., Nguyen, X., Pye, Q. N., Stewart, C. A., Geddes, J., Markesbery, W. R., et al. (1999) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1999.0722053.x · Cited by 373 · see citing works

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 365 · see citing works

MAP kinase pathways activated by stress: The p38 MAPK pathway

Obata, T., Brown, G. E., & Yaffe, M. B. (2000) · Critical Care Medicine · doi:10.1097/00003246-200004001-00008 · Cited by 355 · see citing works

Inflammation and neurodegenerative diseases

Griffin, W. S. T. (2006) · The American Journal of Clinical Nutrition · doi:10.1093/ajcn/83.2.470s · Cited by 351 · see citing works

Oxidative Stress Signaling in Alzheimers Disease

Su, B., Wang, X., Nunomura, A., Moreira, P., Lee, H.-G., Perry, G., Smith, M., & Zhu, X. (2008) · Current Alzheimer Research · doi:10.2174/156720508786898451 · Cited by 344 · see citing works

Dietary Docosahexaenoic Acid and Docosapentaenoic Acid Ameliorate Amyloid-β and Tau Pathology via a Mechanism Involving Presenilin 1 Levels

Green, K. N., Martínez‐Coria, H., Khashwji, H., Hall, E. B., Yurko‐Mauro, K., Ellis, L., & LaFerla, F. M. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0055-07.2007 · Cited by 326 · see citing works

Differential activation of neuronal ERK, JNK/SAPK and p38 in Alzheimer disease: the ‘two hit’ hypothesis

Zhu, X., Castellani, R. J., Takeda, A., Nunomura, A., Atwood, C., Perry, G. L., & Smith, M. A. (2001) · Mechanisms of Ageing and Development · doi:10.1016/s0047-6374(01)00342-6 · Cited by 309 · see citing works

Current Advances on Different Kinases Involved in Tau Phosphorylation, and Implications in Alzheimers Disease and Tauopathies

Ferrer, I., Gómez‐Isla, T., Puig, B., Freixes, M., Ribé, E. M., Dalfó, E., & Ávila, J. (2005) · Current Alzheimer Research · doi:10.2174/1567205052772713 · Cited by 302 · see citing works

Argyrophilic grain disease

Ferrer, I., Santpere, G., & van Leeuwen, F. W. (2008) · Brain · doi:10.1093/brain/awm305 · Cited by 256 · see citing works

Phosphorylated Map Kinase (ERK1, ERK2) Expression is Associated with Early Tau Deposition in Neurones and Glial Cells, but not with Increased Nuclear DNA Vulnerability and Cell Death, in Alzheimer Disease, Pick's Disease, Progressive Supranuclear Palsy and Corticobasal Degeneration

Ferrer, I., Blanco, R., Carmona, M., Ribera, R., Goutan, E., Puig, B., Rey, M. J., Cardozo, A., Viñals, F., & Ribalta, T. (2001) · Brain Pathology · doi:10.1111/j.1750-3639.2001.tb00387.x · Cited by 239 · see citing works

Desmosome Signaling

Berkowitz, P., Hu, P., Liu, Z., Diaz, L. A., Enghild, J. J., Chua, M., & Rubenstein, D. S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501365200 · Cited by 237 · see citing works

P38 MAP kinase is activated at early stages in Alzheimer's disease brain

Sun, A. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00180-8 · Cited by 219 · see citing works

Dissection of tumor-necrosis factor-α inhibition of long-term potentiation (LTP) reveals a p38 mitogen-activated protein kinase-dependent mechanism which maps to early—but not late—phase LTP

Butler, M. P., O'Connor, J. J., & Moynagh, P. N. (2004) · Neuroscience · doi:10.1016/j.neuroscience.2003.11.040 · Cited by 218 · see citing works

β-Amyloid-Induced Inflammation and Cholinergic Hypofunction in the Rat Brain in Vivo: Involvement of the p38MAPK Pathway

Giovannini, M. G., Scali, C., Prosperi, C., Bellucci, A., Vannucchi, M. G., Rosi, S., Pepeu, G., & Casamenti, F. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0538 · Cited by 214 · see citing works

Proapoptotic Effects of Tau Cleavage Product Generated by Caspase-3

Chung, C.-W., Song, Y.-H., Kim, I.-K., Yoon, W. J., Ryu, B. R., Jo, D., Woo, H., Kwon, Y.-K., Kim, H., Gwag, B.-J., et al. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0335 · Cited by 211 · see citing works

α7 Nicotinic Acetylcholine Receptors Mediate β-Amyloid Peptide-induced Tau Protein Phosphorylation

Wang, H.-Y., Li, W., Benedetti, N. J., & Lee, D. H. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212532200 · Cited by 185 · see citing works

Chronic oxidative stress causes increased tau phosphorylation in M17 neuroblastoma cells

Su, B., Wang, X., Lee, H., Tabaton, M., Perry, G. L., Smith, M. A., & Zhu, X. (2009) · Neuroscience Letters · doi:10.1016/j.neulet.2009.11.010 · Cited by 178 · see citing works

Active, phosphorylation-dependent mitogen-activated protein kinase (MAPK/ERK), stress-activated protein kinase/c-Jun N-terminal kinase (SAPK/JNK), and p38 kinase expression in Parkinson's disease and Dementia with Lewy bodies

Ferrer, I., Blanco, R. E., Carmona, M., Puig, B., Barrachina, M., Gómez, C., & Ambrosio, S. (2001) · Journal of Neural Transmission · doi:10.1007/s007020100015 · Cited by 172 · see citing works

Pseudophosphorylation of tau at serine 422 inhibits caspase cleavage: in vitro evidence and implications for tangle formation in vivo

Guillozet-Bongaarts, A. L., Cahill, M. E., Cryns, V. L., Reynolds, M. R., Berry, R. W., & Binder, L. I. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03784.x · Cited by 169 · see citing works

Localization of active forms of C-jun kinase (JNK) and p38 kinase in Alzheimer's disease brains at different stages of neurofibrillary degeneration

Pei, J.-J., Braak, E., Braak, H., Grundke-Iqbal, I., Iqbal, K., Winblad, B., & Cowburn, R. F. (2001) · Journal of Alzheimer's Disease · doi:10.3233/jad-2001-3107 · Cited by 165 · see citing works

Activation of MKK6, an upstream activator of p38, in Alzheimer's disease

Zhu, X.-W., Rottkamp, C., Hartzler, A., Sun, Z., Takeda, A., Boux, H., Shimohama, S., Perry, G., & Smith, M. A. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00597.x · Cited by 151 · see citing works

An overview of mammalian p38 mitogen-activated protein kinases, central regulators of cell stress and receptor signaling

Han, J., Wu, J., & Silke, J. (2020) · F1000Research · doi:10.12688/f1000research.22092.1 · Cited by 159 · see citing works

Jun NH2-terminal Kinase (JNK) Interacting Protein 1 (JIP1) Binds the Cytoplasmic Domain of the Alzheimer's β-Amyloid Precursor Protein (APP)

Scheinfeld, M. H., Roncarati, R., Vito, P., Lopez, P., Abdallah, M., & D'adamio, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108357200 · Cited by 158 · see citing works

Deficiency of Neuronal p38α MAPK Attenuates Amyloid Pathology in Alzheimer Disease Mouse and Cell Models through Facilitating Lysosomal Degradation of BACE1*

Schnöder, L., Hao, W., Qin, Y.-D., Liu, S.-R., Tomic, I., Liu, X., Fassbender, K., & Liu, Y. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.695916 · Cited by 126 · see citing works

Roles of Glycogen Synthase Kinase 3 in Alzheimer’s Disease

Cai, Z., Zhao, Y. C., & Zhao, B. (2012) · Current Alzheimer Research · doi:10.2174/156720512802455386 · Cited by 146 · see citing works

JNK Plays a Key Role in Tau Hyperphosphorylation in Alzheimer's Disease Models

Ploia, C., Antoniou, X., Sclip, A., Grande, V., Cardinetti, D., Colombo, A., Canu, N., Benussi, L., Ghidoni, R., Forloni, G., et al. (2011) · Journal of Alzheimer's Disease · doi:10.3233/jad-2011-110320 · Cited by 145 · see citing works

Effect of the lipid peroxidation product acrolein on tau phosphorylation in neural cells

Gómez‐Ramos, A., Díaz‐Nido, J., Smith, M. A., Perry, G. L., & Ávila, J. (2002) · Journal of Neuroscience Research · doi:10.1002/jnr.10525 · Cited by 143 · see citing works

Interleukin-1 promotion of MAPK-p38 overexpression in experimental animals and in Alzheimer's disease: potential significance for tau protein phosphorylation

Sheng, J. G., Jones, R. A., Zhou, X. Q., McGinness, J. M., Van Eldik, L. J., Mrak, R. E., & Griffin, W. S. T. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(01)00041-9 · Cited by 176 · see citing works

The role of intracellular zinc release in aging, oxidative stress, and Alzheimer’s disease

McCord, M. C., & Aizenman, E. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00077 · Cited by 137 · see citing works

Molecular mechanisms linking amyloid β toxicity and Tau hyperphosphorylation in Alzheimer׳s disease

Lloret, A., Fuchsberger, T., Giraldo, E., & Viña, J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.02.028 · Cited by 135 · see citing works

Tyrosine Phosphorylation of the β-Amyloid Precursor Protein Cytoplasmic Tail Promotes Interaction with Shc

TARR, P. E., Roncarati, R., Pelicci, G., Pelicci, P. G., & D'adamio, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110286200 · Cited by 133 · see citing works

Evidence that phosphorylation of the microtubule-associated protein Tau by SAPK4/p38δ at Thr50 promotes microtubule assembly

Feijoo, C., Campbell, D. G., Jakes, R., Goedert, M., & Cuenda, A. (2005) · Journal of Cell Science · doi:10.1242/jcs.01655 · Cited by 133 · see citing works

The p38 mitogen-activated protein kinase inhibitor SB203580 antagonizes the inhibitory effects of interleukin-1β on long-term potentiation in the rat dentate gyrus in vitro

Coogan, A. N., O'Neill, L. A. J., & O'Connor, J. J. (1999) · Neuroscience · doi:10.1016/s0306-4522(99)00100-1 · Cited by 129 · see citing works

Starvation induces tau hyperphosphorylation in mouse brain: implications for Alzheimer's disease

Yanagisawa, M., Planel, E., Ishiguro, K., & Fujita, S. C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01480-5 · Cited by 123 · see citing works

Cytoskeletal mechanisms regulating vascular endothelial barrier function in response to acute lung injury

Kása, A., Csoŕtos, C., & Verin, A. D. (2014) · Tissue Barriers · doi:10.4161/21688370.2014.974448 · Cited by 119 · see citing works

Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation

Ambegaokar, S. S., & Jackson, G. R. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr432 · Cited by 113 · see citing works

p38α stress-activated protein kinase phosphorylates neurofilaments and is associated with neurofilament pathology in amyotrophic lateral sclerosis

Ackerley, S., Grierson, A. J., Banner, S. J., Perkinton, M. S., Brownlees, J., Byers, H. L., Ward, M. A., Thornhill, P., Hussain, K., Waby, J. S., et al. (2004) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2004.02.009 · Cited by 112 · see citing works

Dendritic changes in Alzheimer's disease and factors that may underlie these changes

Anderton, B. H., Callahan, L. M., Coleman, P. D., Davies, P., Flood, D. G., Jicha, G. A., Ohm, T. G., & Weaver, C. L. (1998) · Progress in Neurobiology · doi:10.1016/s0301-0082(98)00022-7 · Cited by 111 · see citing works

The p38 MAP kinase signaling pathway in Alzheimer's disease

Johnson, G. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(03)00268-1 · Cited by 106 · see citing works

Activated p38MAPK Is a Novel Component of the Intracellular Inclusions Found in Human Amyotrophic Lateral Sclerosis and Mutant SOD1 Transgenic Mice

Bendotti, C., Atzori, C., Piva, R., Tortarolo, M., Strong, M. J., Debiasi, S., & Migheli, A. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.2.113 · Cited by 103 · see citing works

Rapid Tau Aggregation and Delayed Hippocampal Neuronal Death Induced by Persistent Thrombin Signaling

Suo, Z., Wu, M., Citron, B. A., Palazzo, R. E., & Festoff, B. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301406200 · Cited by 99 · see citing works

Activation of oncogenic pathways in degenerating neurons in Alzheimer disease

Zhu, X., Raina, A. K., Boux, H. A., Simmons, Z. L., Takeda, A., & Smith, M. A. (2000) · International Journal of Developmental Neuroscience · doi:10.1016/s0736-5748(00)00010-1 · Cited by 97 · see citing works

Nerve Growth Factor Pathobiology During the Progression of Alzheimer’s Disease

Mufson, E. J., Counts, S., Ginsberg, S. D., Mahady, L. J., Perez, S. E., Massa, S. M., Longo, F. M., & Ikonomović, M. D. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00533 · Cited by 92 · see citing works

Aberrant phosphorylation in the pathogenesis of Alzheimer's disease

Chung, S. (2009) · BMB Reports · doi:10.5483/bmbrep.2009.42.8.467 · Cited by 89 · see citing works

Heparin-induced Conformational Change in Microtubule-associated Protein Tau as Detected by Chemical Cross-linking and Phosphopeptide Mapping

Paudel, H. K., & Li, W. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.12.8029 · Cited by 89 · see citing works

Peroxynitrite induces Alzheimer‐like tau modifications and accumulation in rat brain and its underlying mechanisms

Zhang, Y., Xu, Y., Liu, Y., Yin, J., Li, H., Wang, Q., & Wang, J. (2006) · The FASEB Journal · doi:10.1096/fj.05-5223com · Cited by 86 · see citing works

Expression of stress‐activated kinases c‐Jun N‐terminal kinase (SAPK/JNK‐P) and p38 kinase (p38‐P), and tau hyperphosphorylation in neurites surrounding βA plaques in APP Tg2576 mice

Puig, B., Gómez‐Isla, T., Ribé, E. M., Cuadrado‐Tejedor, M., Torrejón-Escribano, B., Dalfó, E., & Ferrer, I. (2004) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2004.00569.x · Cited by 85 · see citing works

The role of tau in Alzheimer's disease

Trojanowski, J. Q., & Lee, V. M.-Y. (2002) · Medical Clinics of North America · doi:10.1016/s0025-7125(02)00002-0 · Cited by 85 · see citing works

Microcystin-LR induces cytoskeleton system reorganization through hyperphosphorylation of tau and HSP27 via PP2A inhibition and subsequent activation of the p38 MAPK signaling pathway in neuroendocrine (PC12) cells

Meng, G., Sun, Y., Fu, W., Guo, Z., & Xu, L. (2011) · Toxicology · doi:10.1016/j.tox.2011.09.085 · Cited by 84 · see citing works

MAP kinases in lung endothelial permeability induced by microtubule disassembly

Birukova, A. A., Birukov, K. G., Gorshkov, B. A., Liu, F., Garcia, J. G. N., & Verin, A. D. (2005) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00447.2004 · Cited by 84 · see citing works

Secreted β-amyloid precursor protein activates microglia via JNK and p38-MAPK

Bodles, A. M., & Barger, S. W. (2004) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2004.02.022 · Cited by 82 · see citing works

Animal models reveal role for tau phosphorylation in human disease

Götz, J., Gladbach, A., Pennanen, L., van Eersel, J., Schild, A., David, D. C., & Ittner, L. M. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2009.09.008 · Cited by 79 · see citing works

Kinase activities increase during the development of tauopathy in htau mice

Kelleher, I., Garwood, C., Hanger, D. P., Anderton, B. H., & Noble, W. (2007) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2007.04930.x · Cited by 78 · see citing works

Role of protein phosphatase 2A in the regulation of endothelial cell cytoskeleton structure

Tar, K., Csoŕtos, C., Czikora, I., Oláh, G., Ma, S., Wadgaonkar, R., Gergely, P., Garcia, J. G. N., & Verin, A. D. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20829 · Cited by 76 · see citing works

Cdk5 is a major regulator of p38 cascade: relevance to neurotoxicity in Alzheimer’s disease

Chang, K., de Pablo, Y., Lee, H., Lee, H., Smith, M. A., & Shah, K. (2010) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2010.06687.x · Cited by 74 · see citing works

Interleukin-10 deficiency exacerbates inflammation-induced tau pathology

Weston, L. L., Jiang, S., Chisholm, D., Jantzie, L. L., & Bhaskar, K. (2021) · Journal of Neuroinflammation · doi:10.1186/s12974-021-02211-1 · Cited by 69 · see citing works

Tau-tubulin kinase

Ikezu, S., & Ikezu, T. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00033 · Cited by 67 · see citing works

Modulation of Tau Phosphorylation by the Kinase PKR: Implications in Alzheimer's Disease

Bose, A., Mouton‐Liger, F., Paquet, C., Mazot, P., Vigny, M., Gray, F., & Hugon, J. (2010) · Brain Pathology · doi:10.1111/j.1750-3639.2010.00437.x · Cited by 68 · see citing works

Characterization of Neuronal Tau Protein as a Target of Extracellular Signal-regulated Kinase

Qi, H., Prabakaran, S., Cantrelle, F., Chambraud, B., Gunawardena, J., Lippens, G. M., & Landrieu, I. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.700914 · Cited by 67 · see citing works

The Environmental Toxin Arsenite Induces Tau Hyperphosphorylation

Giasson, B. I., Sampathu, D. M., Wilson, C., Vogelsberg-Ragaglia, V., Mushynski, W. E., & Lee, V. M. ‐. (2002) · Biochemistry · doi:10.1021/bi026813c · Cited by 66 · see citing works

Assessments of the accumulation severities of amyloid β-protein and hyperphosphorylated tau in the medial temporal cortex of control and Alzheimer's brains

Zhou, X., Li, X., Björkdahl, C., Sjögren, M. J. C., Alafuzoff, I. I., Soininen, H. S., Grundke, I., Iqbal, K., Winblad, B. G., & Pei, J.-J. (2006) · Neurobiology of Disease · doi:10.1016/j.nbd.2006.01.006 · Cited by 65 · see citing works

Oxidative Stress and Neuronal Adaptation in Alzheimer Disease: The Role of SAPK Pathways

Zhu, X., Raina, A. K., Lee, H., Chao, M. P., Nunomura, A., Tabaton, M., Petersen, R. B., Perry, G. L., & Smith, M. A. (2003) · Antioxidants and Redox Signaling · doi:10.1089/152308603770310220 · Cited by 67 · see citing works

The interrelationship between selective tau phosphorylation and microtubule association

Xie, H., Litersky, J. M., Hartigan, J. A., Jope, R. S., & Johnson, G. V. W. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00407-7 · Cited by 65 · see citing works

N-cadherin Regulates p38 MAPK Signaling via Association with JNK-associated Leucine Zipper Protein

Ando, K., Uemura, K., Kuzuya, A., Maesako, M., Asada-Utsugi, M., Kubota, M., Aoyagi, N., Yoshioka, K., Okawa, K., Inoue, H., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.158477 · Cited by 66 · see citing works

LiCl Attenuates Thapsigargin-Induced Tau Hyperphosphorylation by Inhibiting GSK-3β In Vivo and In Vitro

Fu, Z., Yang, Y., Song, J., Jiang, Q., Liu, Z.-C., Wang, Q., Zhu, L., Wang, J., & Tian, Q. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-100687 · Cited by 64 · see citing works

Modulation of tau phosphorylation and intracellular localization by cellular stress

Jenkins, S. M., ZINNERMAN, M., Garner, C. C., & Johnson, G. V. W. (2000) · Biochemical Journal · doi:10.1042/bj3450263 · Cited by 63 · see citing works

Phosphorylated Protein Kinases Associated with Neuronal and Glial <i>Tau</i> Deposits in Argyrophilic Grain Disease

Ferrer, I., Barrachina, M., Tolnay, M., Rey, M. J., Vidal, N., Carmona, M., Blanco, R., & Puig, B. (2003) · Brain Pathology · doi:10.1111/j.1750-3639.2003.tb00007.x · Cited by 60 · see citing works

Neuronal COX-2 expression and phosphorylation of pRb precede p38 MAPK activation and neurofibrillary changes in AD temporal cortex

Hoozemans, J. J. M., Veerhuis, R., Rozemüller, A. J. M., Arendt, T., & Eikelenboom, P. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2003.11.028 · Cited by 60 · see citing works

The last neuronal division: a unifying hypothesis for the pathogenesis of Alzheimer's disease

Nagy, Z. (2005) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2005.tb00485.x · Cited by 56 · see citing works

Molecular Mechanisms for Neuronal Cell Death by Alzheimer’s Amyloid Precursor Protein-Relevant Insults

Kawasumi, M., Hashimoto, Y., Chiba, T., Kanekura, K., Yamagishi, Y., Ishizaka, M., Tajima, H., Niikura, T., & Nishimoto, I. (2002) · Neurosignals · doi:10.1159/000067424 · Cited by 53 · see citing works

Tau Potentiates Nerve Growth Factor-induced Mitogen-activated Protein Kinase Signaling and Neurite Initiation without a Requirement for Microtubule Binding

Leugers, C. J., & Lee, G. S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.105387 · Cited by 51 · see citing works

Metabolic stress in PC12 cells induces the formation of the endogenous dopaminergic neurotoxin, 3,4-dihydroxyphenylacetaldehyde

Lamensdorf, I., Eisenhofer, G., Harvey-White, J. D., Hayakawa, Y., Kirk, K., & Kopin, I. J. (2000) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(20000515)60:4 · Cited by 90 · see citing works

Stress kinases involved inTau phosphorylation in alzheimer’s disease, tauopathies and APP transgenic mice

Ferrer, I. (2004) · Neurotoxicity Research · doi:10.1007/bf03033283 · Cited by 53 · see citing works

Tau‐Tubulin Kinase 1 Expression, Phosphorylation and Co‐Localization with Phospho‐ S er422 Tau in the A lzheimer's Disease Brain

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Environmental factors in the development and progression of late-onset Alzheimer’s disease

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