Stress‐induced hyperphosphorylation of tau in the mouse brain

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676 · see citing works

STRESS AND HIPPOCAMPAL PLASTICITY

McEwen, B. S. (1999) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.22.1.105 · Cited by 2,087 · see citing works

Conversion of p35 to p25 deregulates Cdk5 activity and promotes neurodegeneration

Patrick, G. N., Zukerberg, L. R., Nikolić, M., de la Monte, S. M., Dikkes, P., & Tsai, L. (1999) · Nature · doi:10.1038/45159 · Cited by 1,541 · see citing works

The neuronal MAP kinase cascade: a biochemical signal integration system subserving synaptic plasticity and memory

Sweatt, J. D. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00054.x · Cited by 1,131 · see citing works

Inactivation of glycogen synthase kinase-3 <i>β</i> by phosphorylation: new kinase connections in insulin and growth-factor signalling

Sutherland, C., Leighton, I. A., & Cohen, P. (1993) · Biochemical Journal · doi:10.1042/bj2960015 · Cited by 903 · see citing works

The biochemical pathway of neurofibrillary degeneration in aging and Alzheimer's disease.

Delacourte, A., David, J. P., Sergeant, N., Buée, L., Wattez, A., Vermersch, P., Ghozali, F., Fallet-Bianco, C., Pasquier, F., Lebert, F., et al. (1999) · Neurology · doi:10.1212/wnl.52.6.1158 · Cited by 828 · see citing works

Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase

Hanger, D. P., Hughes, K., Woodgett, J. R., Brion, J.-P., & Anderton, B. H. (1992) · Neuroscience Letters · doi:10.1016/0304-3940(92)90774-2 · Cited by 737 · see citing works

Tau protein and the neurofibrillary pathology of Alzheimer's disease

Goedert, M. (1993) · Trends in Neurosciences · doi:10.1016/0166-2236(93)90078-z · Cited by 718 · see citing works

Tau protein pathology in neurodegenerative diseases

Spillantini, M. G., & Goedert, M. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01337-x · Cited by 683 · see citing works

Modulation of the glycogen synthase kinase‐3 family by tyrosine phosphorylation.

Hughes, K., Nikolakaki, E., Plyte, S. E., Totty, N. F., & Woodgett, J. R. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05715.x · Cited by 630 · see citing works

A brain-specific activator of cyclin-dependent kinase 5

Lew, J., Huang, Q.-Q., Qi, R. Z., Winkfein, R. J., Aebersold, R. H., Hunt, T., & Wang, J. H.-C. (1994) · Nature · doi:10.1038/371423a0 · Cited by 580 · see citing works

Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer‐like state.

Drewes, G., Lichtenberg‐Kraag, B., Döring, F., Mandelkow, E. M., Biernat, J., Goris, J., Dorée, M., & Mandelkow, E. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05272.x · Cited by 565 · see citing works

Proline-directed and non-proline-directed phosphorylation of PHF-tau

Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Yoshida, H., Titani, K., & Ihara, Y. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.823 · Cited by 557 · see citing works

The microtubule binding domain of tau protein

Lee, G., Neve, R. L., & Kosik, K. S. (1989) · Neuron · doi:10.1016/0896-6273(89)90050-0 · Cited by 500 · see citing works

Alzheimer's disease-like phosphorylation of the microtubule-associated protein tau by glycogen synthase kinase-3 in transfected mammalian cells

Lovestone, S., Reynolds, C. H., Latimer, D. A., Davis, D. R., Anderton, B. H., Gallo, J., Hanger, D. P., Mulot, S., Marquardt, B., Stabel, S., et al. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00246-3 · Cited by 470 · see citing works

Distribution of Active Glycogen Synthase Kinase 3β (GSK-3β) in Brains Staged for Alzheimer Disease Neurofibrillary Changes

Pei, J.-J., Braak, E., Braak, H., Grundke-Iqbal, I., Iqbal, K., Winblad, B., & Cowburn, R. F. (1999) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/00005072-199909000-00011 · Cited by 459 · see citing works

New Phosphorylation Sites Identified in Hyperphosphorylated Tau (Paired Helical Filament‐Tau) from Alzheimer's Disease Brain Using Nanoelectrospray Mass Spectrometry

Hanger, D. P., Betts, J. C., Loviny, T. L. F., Blackstock, W. P., & Anderton, B. H. (1998) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1998.71062465.x · Cited by 378 · 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

p35, the Neuronal-specific Activator of Cyclin-dependent Kinase 5 (Cdk5) Is Degraded by the Ubiquitin-Proteasome Pathway

Patrick, G. N., Zhou, P., Kwon, Y. T., Howley, P. M., & Tsai, L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.37.24057 · Cited by 311 · see citing works

Presymptomatic cognitive deficits in individuals at risk of familial Alzheimer's disease. A longitudinal prospective study

Fox, N. C. (1998) · Brain · doi:10.1093/brain/121.9.1631 · Cited by 263 · see citing works

Preferential labeling of Alzheimer neurofibrillary tangles with antisera for tau protein kinase (TPK) I/glycogen synthase kinase-3β and cyclin-dependent kinase 5, a component of TPK II

Yamaguchi, H., Ishiguro, K., Uchida, T., Takashima, A., Lemere, C. A., & Imahori, K. (1996) · Acta Neuropathologica · doi:10.1007/s004010050513 · Cited by 253 · see citing works

Tau protein kinase I converts normal tau protein into A68-like component of paired helical filaments.

Ishiguro, K., Takamatsu, M., Tomizawa, K., OMORI, A., Takahashi, M., Arioka, M., Uchida, T., & Imahori, K. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50102-8 · Cited by 249 · see citing works

Physiology and pathology of tau protein kinases in relation to Alzheimer's disease.

Imahori, K., & Uchida, T. (1997) · PubMed · Cited by 236 · see citing works

A cdc2‐related kinase PSSALRE/cdk5 is homologous with the 30 kDa subunit of tau protein kinase II, a proline‐directed protein kinase associated with microtubule

Kobayashi, S., Ishiguro, K., Omori, A., Takamatsu, M., Arioka, M., Imahori, K., & Uchida, T. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80723-8 · Cited by 234 · see citing works

Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration

Pei, J.-J., Grundke-Iqbal, I., Iqbal, K., Bogdanovic, N., Winblad, B., & Cowburn, R. F. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00296-0 · Cited by 226 · see citing works

The Alzheimer‐like phosphorylation of tau protein reduces microtubule binding and involves Ser‐Pro and Thr‐Pro motifs

Gustke, N., Steiner, B., Mandelkow, E., Biernat, J., Meyer, H. E., Goedert, M., & Mandelkow, E. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)80767-b · Cited by 219 · see citing works

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 · see citing works

The limbic system in Alzheimer's disease. A neuropathologic investigation.

Hopper, M., & Vogel, F. S. (1976) · PubMed Central · Cited by 208 · see citing works

Alternative splicing isoform of tau protein kinase I/glycogen synthase kinase 3β

Mukai, F., Ishiguro, K., Sano, Y., & Fujita, S. C. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.00918.x · Cited by 204 · see citing works

Inhibition of Protein Phosphatase 2A Overrides Tau Protein Kinase I/Glycogen Synthase Kinase 3β and Cyclin-dependent Kinase 5 Inhibition and Results in Tau Hyperphosphorylation in the Hippocampus of Starved Mouse

Planel, E., Yasutake, K., Fujita, S. C., & Ishiguro, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102780200 · Cited by 197 · see citing works

Phosphorylated tau in human cerebrospinal fluid is a diagnostic marker for Alzheimer's disease

Ishiguro, K., Ohno, H., Arai, H., Yamaguchi, H., Urakami, K., Park, J., Sato, K., Kohno, H., & Imahori, K. (1999) · Neuroscience Letters · doi:10.1016/s0304-3940(99)00476-0 · Cited by 175 · see citing works

Phosphorylation sites on tau by tau protein kinase I, a bovine derived kinase generating an epitope of paired helical filaments

Ishiguro, K., Omori, A., Takamatsu, M., Sato, K., Arioka, M., Uchida, T., & Imahori, K. (1992) · Neuroscience Letters · doi:10.1016/0304-3940(92)90839-y · Cited by 151 · 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

Dynamic regulation of c-Jun N-terminal kinase activity in mouse brain by environmental stimuli

Xu, X., Raber, J., Yang, D., Su, B., & Mucke, L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.23.12655 · Cited by 109 · see citing works

A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope.

Ishiguro, K., Omori, A., Sato, K., Tomizawa, K., Imahori, K., & Uchida, T. (1991) · Neuroscience Letters · doi:10.1016/0304-3940(91)90259-v · Cited by 106 · see citing works

Aβ amyloidosis induces the initial stage of tau accumulation in APPSw mice

Tomidokoro, Y., Ishiguro, K., Harigaya, Y., Matsubara, E., Ikeda, M., Park, J., Yasutake, K., Kawarabayashi, T., Okamoto, K., & Shoji, M. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01767-5 · Cited by 92 · see citing works

Characterization of tau phosphorylation in glycogen synthase kinase-3beta and cyclin dependent kinase-5 activator (p23) transfected cells.

Michel, G., Mercken, M., Murayama, M., Noguchi, K., Ishiguro, K., Imahori, K., & Takashima, A. (1998) · Biochimica et Biophysica Acta · doi:10.1016/s0304-4165(97)00139-6 · Cited by 89 · see citing works

The heat shock-induced hyperphosphorylation of τ is estrogen-independent and prevented by androgens: Implications for Alzheimer disease

Papasozomenos, S. C. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.13.6612 · Cited by 89 · see citing works

Phosphorylation of tau by glycogen synthase kinase 3β affects the ability of tau to promote microtubule self-assembly

Utton, M. A., Vandecandelaere, A., Wagner, U., Reynolds, C. H., Gibb, G., Miller, C. C. J., Bayley, P. M., & Anderton, B. H. (1997) · Biochemical Journal · doi:10.1042/bj3230741 · Cited by 86 · see citing works

Analysis of phosphorylation of tau with antibodies specific for phosphorylation sites

Ishiguro, K., Sato, K., Takamatsu, M., Park, J., Uchida, T., & Imahori, K. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)12206-0 · Cited by 84 · see citing works

Precursor of cdk5 activator, the 23 kDa subunit of tau protein kinase II: Its sequence and developmental change in brain

Uchida, T., Ishiguro, K., Ohnuma, J., Takamatsu, M., Yonekura, S., & Imahori, K. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)01163-x · Cited by 72 · see citing works

Glucocorticoids, stress and exacerbation of excitotoxic neuron death

Sapolsky, R. M. (1994) · Seminars in Neuroscience · doi:10.1006/smns.1994.1041 · Cited by 72 · see citing works

Immunocytochemistry of tau phosphoserine 413 and tau protein kinase I in Alzheimer pathology.

Shiurba, R., Ishiguro, K., Takahashi, M., Sato, K., Spooner, E. T., Mercken, M., Yoshida, R., Wheelock, T. R., Yanagawa, H., Imahori, K., et al. (1996) · Brain Research · doi:10.1016/0006-8993(96)00717-2 · Cited by 69 · see citing works

Altered phosphorylation of tau protein in heat-shocked rats and patients with Alzheimer disease.

Papasozomenos, S. C., & Su, Y. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.10.4543 · Cited by 68 · see citing works

Microtubule-Stimulated Phosphorylation of tau at Ser202 and Thr205 by cdk5 Decreases Its Microtubule Nucleation Activity

Wada, Y., Ishiguro, K., Itoh, T. J., Uchida, T., Hotani, H., Saito, T., Kishimoto, T., & Hisanaga, S.-I. (1998) · Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a022174 · Cited by 58 · see citing works

Rapid reversible phosphorylation of rat brain tau proteins in response to cold water stress

Korneyev, A., Binder, L. I., & Bernardis, J. (1995) · Neuroscience Letters · doi:10.1016/0304-3940(95)11546-3 · Cited by 57 · see citing works

Heat Shock Induces Rapid Dephosphorylation of τ in Both Female and Male Rats Followed by Hyperphosphorylation Only in Female Rats: Implications for Alzheimer's Disease

Papasozomenos, S. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.66031140.x · Cited by 44 · see citing works

Okadaic Acid-Stimulated Degradation of p35, an Activator of CDK5, by Proteasome in Cultured Neurons

Saito, T., Ishiguro, K., Onuki, R., Nagai, Y., Kishimoto, T., & Hisanaga, S. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1998.9739 · Cited by 39 · see citing works

Stress-Induced Tau Phosphorylation in Mouse Strains with Different Brain Erk 1 + 2 Immunoreactivity

Korneyev, A. (1998) · Neurochemical Research · doi:10.1023/a:1020980004539 · Cited by 28 · see citing works

Stress weakens prefrontal networks: molecular insults to higher cognition

Arnsten, A. F. T. (2015) · Nature Neuroscience · doi:10.1038/nn.4087 · Cited by 752 · see citing works

The Neuropathology of Chronic Traumatic Encephalopathy

McKee, A. C., Stein, T. D., Kiernan, P. T., & Alvarez, V. E. (2015) · Brain Pathology · doi:10.1111/bpa.12248 · Cited by 585 · see citing works

The neuropathology of sport

McKee, A. C., Daneshvar, D. H., Alvarez, V. E., & Stein, T. D. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1230-6 · Cited by 422 · see citing works

Neurological consequences of traumatic brain injuries in sports

Ling, H., Hardy, J., & Zetterberg, H. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2015.03.012 · Cited by 197 · see citing works

Aberrant Wnt signaling pathway in medial temporal lobe structures of Alzheimer’s disease

Riise, J., Plath, N., Pakkenberg, B., & Parachikova, A. (2015) · Journal of Neural Transmission · doi:10.1007/s00702-015-1375-7 · Cited by 66 · see citing works

Do infectious agents play a role in dementia?

Dobson, C. B., Wozniak, M. A., & Itzhaki, R. F. (2003) · Trends in Microbiology · doi:10.1016/s0966-842x(03)00146-x · Cited by 56 · see citing works

GSK3B wt Allele

National Cancer Institute (2020) · Definitions · doi:10.32388/jn7r58

In Vivo Evidence in the Brain for Lithium Inhibition of Glycogen Synthase Kinase-3

Gould, T. D., Chen, G. J., & Manji, H. K. (2003) · Neuropsychopharmacology · doi:10.1038/sj.npp.1300283 · Cited by 217 · see citing works

[The role of glycogen synthase kinase-3 beta in the pathogenesis of liver ischemia reperfusion injury].

Ren, F., Zhang, H., Piao, Z.-F., et al. (2011) · PubMed · doi:10.3760/cma.j.issn.1007-3418.2011.07.018

GSK‐3 inhibition by adenoviral FRAT1 overexpression is neuroprotective and induces Tau dephosphorylation and β‐catenin stabilisation without elevation of glycogen synthase activity

Culbert, A. A., Brown, M. J. B., Frame, S., Hagen, T., Cross, D. A. E., Bax, B. D., & Reith, A. D. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02990-8 · Cited by 85 · see citing works

Clinical and biological significance of GSK-3β inactivation in breast cancer—an immunohistochemical study

Armanious, H., Deschênes, J., Gélébart, P., Ghosh, S., Mackey, J. R., & Lai, R. L. (2010) · Human Pathology · doi:10.1016/j.humpath.2010.04.015 · Cited by 25 · see citing works