Tau phosphorylation in neuronal cell function and dysfunction

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126 · 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

Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17

Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498 · see citing works

A protein factor essential for microtubule assembly

Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089 · see citing works

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492 · see citing works

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

GSK-3: tricks of the trade for a multi-tasking kinase

Doble, B. W., & Woodgett, J. R. (2003) · Journal of Cell Science · doi:10.1242/jcs.00384 · Cited by 2,084 · see citing works

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780 · 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 glamour and gloom of glycogen synthase kinase-3

Jope, R. S., & Johnson, G. V. W. (2004) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2003.12.004 · Cited by 1,522 · see citing works

Mutation in the tau gene in familial multiple system tauopathy with presenile dementia

Spillantini, M. G., Murrell, J. R., Goedert, M., Farlow, M. R., Klug, A., & Ghetti, B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7737 · Cited by 1,474 · see citing works

Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.

Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,462 · see citing works

Tau is a candidate gene for chromosome 17 frontotemporal dementia

Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374 · see citing works

Molecular cloning and expression of glycogen synthase kinase‐3/factor A.

Woodgett, J. R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07419.x · Cited by 1,362 · see citing works

Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells

Stambolic, V., Ruel, L., & Woodgett, J. R. (1996) · Current Biology · doi:10.1016/s0960-9822(02)70790-2 · Cited by 1,321 · see citing works

GSK-3α regulates production of Alzheimer's disease amyloid-β peptides

Phiel, C. J., Wilson, C., Lee, V. M. ‐., & Klein, P. S. (2003) · Nature · doi:10.1038/nature01640 · Cited by 1,200 · see citing works

A decade of CDK5

Dhavan, R., & Tsai, L. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35096019 · Cited by 1,052 · see citing works

Role of tau protein in both physiological and pathological conditions

AVILA, J., LUCAS, J. J., PÉREZ, M., & HERNÁNDEZ, F. (2004) · Physiological Reviews · doi:10.1152/physrev.00024.2003 · Cited by 1,005 · see citing works

Specific tau phosphorylation sites correlate with severity of neuronal cytopathology in Alzheimer's disease

Augustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998 · 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

Decreased nuclear β‐catenin, tau hyperphosphorylation and neurodegeneration in GSK‐3β conditional transgenic mice

Lucas, J. J., Hernández, F., Gómez‐Ramos, P., Morán, M. A., Hen, R., & Avila, J. (2001) · The EMBO Journal · doi:10.1093/emboj/20.1.27 · Cited by 903 · see citing works

Phosphorylation affects the ability of tau protein to promote microtubule assembly.

Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901 · see citing works

Tau blocks traffic of organelles, neurofilaments, and APP vesicles in neurons and enhances oxidative stress

Stamer, K., Vogel, R., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108057 · Cited by 885 · see citing works

Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly

Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90214-5 · Cited by 881 · see citing works

MARK, a Novel Family of Protein Kinases That Phosphorylate Microtubule-Associated Proteins and Trigger Microtubule Disruption

Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80208-1 · Cited by 878 · see citing works

Alzheimer’s disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules

Alonso, A. D. C., Grundke-Iqbal, I., & Iqbal, K. (1996) · Nature Medicine · doi:10.1038/nm0796-783 · Cited by 859 · see citing works

Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease

Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831 · see citing works

Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer’s disease

Ebneth, A., Godemann, R., Stamer, K., Illenberger, S., Trinczek, B., Mandelkow, E.-M., & Mandelkow, E. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.3.777 · Cited by 820 · see citing works

Tau is essential to β-amyloid-induced neurotoxicity

Rapoport, M., Dawson, H. N., Binder, L. I., Vitek, M. P., & Ferreira, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092136199 · Cited by 807 · see citing works

Altered microtubule organization in small-calibre axons of mice lacking tau protein

Harada, A., Oguchi, K., Okabe, S., Kuno, J., Terada, S., Ohshima, T., Sato-Yoshitake, R., Takei, Y., Noda, T., & Hirokawa, N. (1994) · Nature · doi:10.1038/369488a0 · Cited by 806 · see citing works

Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding

Biernat, J., Gustke, N., Drewes, G., Mandelkow, E., & Mandelkow, E. (1993) · Neuron · doi:10.1016/0896-6273(93)90279-z · Cited by 796 · see citing works

Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)

Wood, J. G., Mirra, S. S., Pollock, N. J., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4040 · Cited by 749 · see citing works

DEFECTIVE BRAIN MICROTUBULE ASSEMBLY IN ALZHEIMER'S DISEASE

Iqbal, K., Zaidi, T., Wen, G. Y., Grundke, I., MERZ, P. A., Shaikh, S., Wisniewski, H., Alafuzoff, I. I., & Winblad, B. G. (1986) · The Lancet · doi:10.1016/s0140-6736(86)92134-3 · Cited by 727 · see citing works

Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons

Cáceres, A., & Kosik, K. S. (1990) · Nature · doi:10.1038/343461a0 · Cited by 657 · 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

Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain.

Brandt, R., Léger, J. G., & Lee, G. S. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.5.1327 · Cited by 624 · see citing works

Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles

Cruz, J. C., Tseng, H.-C., Goldman, J. A., Shih, H., & Tsai, L.-H. (2003) · Neuron · doi:10.1016/s0896-6273(03)00627-5 · Cited by 609 · see citing works

Developmentally regulated expression of specific tau sequences

Kosik, K. S., Orecchio, L. D., Bakalis, S., & Neve, R. L. (1989) · Neuron · doi:10.1016/0896-6273(89)90077-9 · Cited by 598 · see citing works

β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding

Busciglio, J., Lorenzo, A., Yeh, J., & Yankner, B. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90232-5 · Cited by 595 · see citing works

Age-Dependent Emergence and Progression of a Tauopathy in Transgenic Mice Overexpressing the Shortest Human Tau Isoform

Ishihara, T., Hong, M., Zhang, B., Nakagawa, Y., Lee, M. K., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Neuron · doi:10.1016/s0896-6273(00)81127-7 · Cited by 564 · see citing works

Phosphorylation that Detaches Tau Protein from Microtubules (Ser262, Ser214) Also Protects It against Aggregation into Alzheimer Paired Helical Filaments

Schneider, A., Biernat, J., von Bergen, M., Mandelkow, E., & Mandelkow, E.-M. (1999) · Biochemistry · doi:10.1021/bi981874p · Cited by 564 · see citing works

Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice

Dawson, H. N., Ferreira, A., Eyster, M. V., Ghoshal, N., Binder, L. I., & Vitek, M. P. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.6.1179 · Cited by 527 · see citing works

Cdk5 Is a Key Factor in Tau Aggregation and Tangle Formation In Vivo

Noble, W. J., Olm, V., Takata, K., Casey, E., Mary, O., Meyerson, J. L., Gaynor, K., LaFrancois, J. J., Wang, L., Kondo, T., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00259-9 · Cited by 511 · see citing works

Lithium and GSK-3: one inhibitor, two inhibitory actions, multiple outcomes

Jope, R. S. (2003) · Trends in Pharmacological Sciences · doi:10.1016/s0165-6147(03)00206-2 · Cited by 501 · see citing works

Lithium Reduces Tau Phosphorylation by Inhibition of Glycogen Synthase Kinase-3

Hong, M., Chen, D. C. R., Klein, P. S., & Lee, V. M. ‐. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.25326 · Cited by 470 · see citing works

Tau phosphorylation: physiological and pathological consequences

Stoothoff, W. H., & Johnson, G. V. W. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.017 · Cited by 439 · see citing works

Clogging of axons by tau, inhibition of axonal traffic and starvation of synapses.

Mandelkow, E., Stamer, K., Vogel, R., Thies, E., & Mandelkow, E. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.04.007 · Cited by 422 · see citing works

Glycogen synthase kinase 3: a drug target for CNS therapies

Bhat, R. V., Haeberlein, S. L. B., & Ávila, J. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02422.x · Cited by 408 · see citing works

Defects in Axonal Elongation and Neuronal Migration in Mice with Disrupted tau and map1b Genes

Takei, Y., Teng, J., Harada, A., & Hirokawa, N. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.150.5.989 · Cited by 408 · see citing works

Prominent axonopathy in the brain and spinal cord of transgenic mice overexpressing four-repeat human tau protein.

Spittaels, K., den Haute, C. V., Dorpe, J. V., Bruynseels, K., Vandezande, K., Laenen, I., Geerts, H., Mercken, M., Sciot, R., Lommel, A. V. V., et al. (1999) · American Journal of Pathology · doi:10.1016/s0002-9440(10)65533-2 · Cited by 405 · see citing works

Glycogen synthase kinase 3β is identical to tau protein kinase I generating several epitopes of paired helical filaments

Ishiguro, K., Shiratsuchi, A., Sato, S., Omori, A., Arioka, M., Kobayashi, S., Uchida, T., & Imahori, K. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)81066-9 · Cited by 402 · see citing works

Microtubule-associated Protein/Microtubule Affinity-regulating Kinase (p110mark)

Meyer, H. E., Mandelkow, E.-M., Drewes, G., Trinczek, B., Illenberger, S., Biernat, J., Schmitt-Ulms, G., & Mandelkow, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7679 · Cited by 388 · see citing works

Calpain-dependent Proteolytic Cleavage of the p35 Cyclin-dependent Kinase 5 Activator to p25

Kusakawa, G.-I., Saito, T., Onuki, R., Ishiguro, K., Kishimoto, T., & Hisanaga, S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m907757199 · Cited by 381 · see citing works

Tau protein kinase I is essential for amyloid beta-protein-induced neurotoxicity.

Takashima, A., Noguchi, K., Sato, K., Hoshino, T., & Imahori, K. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7789 · Cited by 381 · see citing works

Epitope mapping of monoclonal antibodies to the paired helical filaments of Alzheimer's disease: identification of phosphorylation sites in tau protein

Goedert, M., Jakes, R., Crowther, R. A., Cohen, P., Vanmechelen, E., Vandermeeren, M., & Cras, P. (1994) · Biochemical Journal · doi:10.1042/bj3010871 · Cited by 375 · see citing works

Axonopathy and amyotrophy in mice transgenic for human four-repeat tau protein

Probst, A., Götz, J., Wiederhold, K., Tolnay, M., Mistl, C., Jaton, A., Hong, M., Ishihara, T., Lee, V., Trojanowski, J., et al. (2000) · Acta Neuropathologica · doi:10.1007/s004010051148 · Cited by 362 · see citing works

Detection of Phosphorylated Ser262 in Fetal Tau, Adult Tau, and Paired Helical Filament Tau

Seubert, P., Mawal-Dewan, M., Barbour, R., Jakes, R., Goedert, M., Johnson, G. V. W., Litersky, J. M., Schenk, D., Lieberburg, I., Trojanowski, J. Q., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.32.18917 · Cited by 345 · see citing works

Hyperphosphorylated tau and neurofilament and cytoskeletal disruptions in mice overexpressing human p25, an activator of cdk5

Ahlijanian, M. K., Barrezueta, N. X., Williams, R. D., Jakowski, A. B., Kowsz, K. P., McCarthy, S. A., Coskran, T., Carlo, A. A., Seymour, P. A., Burkhardt, J. E., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.040577797 · Cited by 339 · see citing works

C-terminal inhibition of tau assembly in vitro and in Alzheimer’s disease

Abraha, A., Ghoshal, N., Gamblin, T. C., Cryns, V. L., Berry, R. W., Kuret, J., & Binder, L. I. (2000) · Journal of Cell Science · doi:10.1242/jcs.113.21.3737 · Cited by 326 · see citing works

PAR-1 Kinase Plays an Initiator Role in a Temporally Ordered Phosphorylation Process that Confers Tau Toxicity in Drosophila

Nishimura, I., Yang, Y., & Lu, B. (2004) · Cell · doi:10.1016/s0092-8674(04)00170-9 · Cited by 324 · see citing works

Further evidence that the tyrosine phosphorylation of glycogen synthase kinase-3 (GSK3) in mammalian cells is an autophosphorylation event

Cole, A. R., Frame, S., & Cohen, P. (2004) · Biochemical Journal · doi:10.1042/bj20031259 · Cited by 324 · see citing works

Glycogen Synthase Kinase-3β Phosphorylates Protein Tau and Rescues the Axonopathy in the Central Nervous System of Human Four-repeat Tau Transgenic Mice

Spittaels, K., den Haute, C. V., Dorpe, J. V., Geerts, H., Mercken, M. H., Bruynseels, K., Lasrado, R., Vandezande, K., Laenen, I., Boon, T., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006219200 · Cited by 317 · 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

Lithium, a Common Drug for Bipolar Disorder Treatment, Regulates Amyloid-β Precursor Protein Processing

Yuan, S., Ryder, J. W., Li, B., Wu, X., Fox, N. W., Solenberg, P., Brune, K. A., Paul, S. M., Zhou, Y., Liu, F., et al. (2004) · Biochemistry · doi:10.1021/bi035627j · Cited by 295 · see citing works

Microtubule-Associated Protein Tau

Yen, S.-H. C., Nacharaju, P., Ko, L., Kenessey, Á., & Liu, W.-K. (1998) · Elsevier eBooks · doi:10.1016/b978-012734610-6/50012-9 · Cited by 284 · see citing works

Primed phosphorylation of tau at Thr231 by glycogen synthase kinase 3β (GSK3β) plays a critical role in regulating tau's ability to bind and stabilize microtubules

Cho, J., & Johnson, G. V. W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02155.x · Cited by 282 · see citing works

Protein Kinase MARK/PAR-1 Is Required for Neurite Outgrowth and Establishment of Neuronal Polarity

Biernat, J., Wu, Y.-Z., Timm, T., Zheng-Fischhöfer, Q., Mandelkow, E., Meijer, L., & Mandelkow, E.-M. (2002) · Molecular Biology of the Cell · doi:10.1091/mbc.02-03-0046 · Cited by 279 · see citing works

A Spatial Gradient of Tau Protein Phosphorylation in Nascent Axons

Mandell, J. W., & Banker, G. A. (1996) · Journal of Neuroscience · doi:10.1523/jneurosci.16-18-05727.1996 · Cited by 270 · see citing works

A novel CDK5‐dependent pathway for regulating GSK3 activity and kinesin‐driven motility in neurons

Morfini, G. A., Szebenyi, G., Brown, H. J., Pant, H. C., Pigino, G. F., DeBoer, S. R., Beffert, U., & Brady, S. T. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600237 · Cited by 268 · see citing works

Glycogen Synthase Kinase 3β Phosphorylates Tau at Both Primed and Unprimed Sites

Cho, J.-H., & Johnson, G. V. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m206236200 · Cited by 266 · see citing works

Exposure of rat hippocampal neurons to amyloid β peptide (25–35) induces the inactivation of phosphatidyl inositol-3 kinase and the activation of tau protein kinase I/glycogen synthase kinase-3β

Takashima, A., Noguchi, K., Michel, G., Mercken, M., Hoshi, M., Ishiguro, K., & Imahori, K. (1996) · Neuroscience Letters · doi:10.1016/0304-3940(95)12257-5 · Cited by 260 · see citing works

Single-molecule investigation of the interference between kinesin, tau and MAP2c

Seitz, A., Kojima, H., Oiwa, K., Mandelkow, E.-M., Song, Y.-H., & Mandelkow, E. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf503 · Cited by 257 · see citing works

Cellular phosphorylation of tau by GSK-3β influences tau binding to microtubules and microtubule organisation

Wagner, U., Utton, M. A., Gallo, J., & Miller, C. C. J. (1996) · Journal of Cell Science · doi:10.1242/jcs.109.6.1537 · Cited by 255 · see citing works

Inhibition of microtubule assembly by phosphorylation of microtubule-associated proteins

Jameson, J. L., Frey, T., Zeebèrg, B. R., Dalldorf, F., & Caplow, M. (1980) · Biochemistry · doi:10.1021/bi00552a027 · Cited by 246 · see citing works

Caspase-9 Activation and Caspase Cleavage of tau in the Alzheimer's Disease Brain

Rohn, T. T., Rissman, R. A., Davis, M. C., Kim, Y., Cotman, C. W., & Head, E. (2002) · Neurobiology of Disease · doi:10.1006/nbdi.2002.0549 · Cited by 242 · see citing works

Developmental expression and localization of glycogen synthase kinase-3β in rat brain

Leroy, K., & Brion, J. (1999) · Journal of Chemical Neuroanatomy · doi:10.1016/s0891-0618(99)00012-5 · Cited by 241 · see citing works

MARK/PAR1 kinase is a regulator of microtubule-dependent transport in axons

Mandelkow, E.-M., Thies, E., Trinczek, B., Biernat, J., & Mandelkow, E. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200401085 · Cited by 236 · see citing works

Tau-Mediated Cytotoxicity in a Pseudohyperphosphorylation Model of Alzheimer's Disease

Fath, T., Eidenmüller, J., & Brandt, R. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-22-09733.2002 · Cited by 233 · see citing works

τ in Paired Helical Filaments Is Functionally Distinct from Fetal τ: Assembly Incompetence of Paired Helical Filament‐τ

Yoshida, H., & Ihara, Y. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03642.x · Cited by 232 · see citing works

In vivo phosphorylation sites in fetal and adult rat tau

Watanabe, A., Hasegawa, M., Suzuki, M., Takio, K., Morishima-Kawashima, M., Titani, K., Arai, T., Kosik, K. S., & Ihara, Y. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74447-0 · Cited by 231 · see citing works

Phosphorylation of tau by glycogen synthase kinase-3β in intact mammalian cells: The effects on the organization and stability of microtubules

Lovestone, S., Hartley, C. L., Pearce, J., & Anderton, B. H. (1996) · Neuroscience · doi:10.1016/0306-4522(96)00126-1 · Cited by 201 · see citing works

Phosphorylation of recombinant tau by cAMP-dependent protein kinase. Identification of phosphorylation sites and effect on microtubule assembly.

Scott, C. W., Spreen, R. C., Herman, J. L., Chow, F. P., Davison, M. D., Young, J., & Caputo, C. B. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54055-2 · Cited by 200 · see citing works

Involvement of aberrant glycosylation in phosphorylation of tau by cdk5 and GSK‐3β

Liu, F., Iqbal, K., Grundke, I., & Gong, C. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03487-7 · Cited by 197 · see citing works

The effect of tau antisense oligonucleotides on neurite formation of cultured cerebellar macroneurons

Cáceres, A., Potrebic, S., & Kosik, K. S. (1991) · Journal of Neuroscience · doi:10.1523/jneurosci.11-06-01515.1991 · Cited by 193 · see citing works

β-Amyloid Induces Paired Helical Filament-like Tau Filaments in Tissue Culture

Ferrari, A., Hoerndli, F. J., Baechi, T., Nitsch, R. M., & Götz, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308243200 · Cited by 182 · see citing works

Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model

Pérez, M., Hernández, F., Lim, F., Díaz‐Nido, J., & Ávila, J. (2003) · Journal of Alzheimer s Disease · doi:10.3233/jad-2003-5405 · Cited by 180 · see citing works

Functions and malfunctions of the tau proteins

Shahani, N., & Brandt, R. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/pl00012495 · Cited by 171 · see citing works

Pseudophosphorylation of tau protein alters its ability for self‐aggregation

Haase‐Kohn, C., Stieler, J., Arendt, T., & Holzer, M. (2004) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02287.x · Cited by 169 · see citing works

Lithium reduces tau phosphorylation: effects in living cells and in neurons at therapeutic concentrations

Lovestone, S., Davis, D. R., Webster, M.-T., Kaech, S., Brion, J., Matus, A. I., & Anderton, B. H. (1999) · Biological Psychiatry · doi:10.1016/s0006-3223(98)00183-8 · Cited by 157 · see citing works

Characterization of mAb AP422, a novel phosphorylation‐dependent monoclonal antibody against tau protein

Hasegawa, M., Jakes, R., Crowther, R. A., Lee, V. M.-Y., Ihara, Y., & Goedert, M. (1996) · FEBS Letters · doi:10.1016/0014-5793(96)00271-2 · Cited by 156 · see citing works

Tau protein is phosphorylated by cyclic AMP-dependent protein kinase and calcium/calmodulin-dependent protein kinase II within its microtubule-binding domains at Ser-262 and Ser-356

Litersky, J. M., Johnson, G. V. W., Jakes, R., Goedert, M., Lee, M., & Seubert, P. A. (1996) · Biochemical Journal · doi:10.1042/bj3160655 · Cited by 150 · see citing works

Truncation of CDK5 Activator p35 Induces Intensive Phosphorylation of Ser202/Thr205 of Human Tau

Hashiguchi, M., Saito, T., Hisanaga, S., & Hashiguchi, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207426200 · Cited by 149 · see citing works

The Development of Cell Processes Induced by tau Protein Requires Phosphorylation of Serine 262 and 356 in the Repeat Domain and Is Inhibited by Phosphorylation in the Proline-rich Domains

Biernat, J., & Mandelkow, E.-M. (1999) · Molecular Biology of the Cell · doi:10.1091/mbc.10.3.727 · Cited by 149 · see citing works

Protein Phosphatase 1 Is Targeted to Microtubules by the Microtubule-associated Protein Tau

Liao, H., Li, Y., Brautigan, D. L., & Gundersen, G. G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.34.21901 · Cited by 145 · see citing works

Cyclin‐dependent kinase‐5 in neurodegeneration

Shelton, S. B., & Johnson, G. V. W. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2003.02328.x · Cited by 144 · see citing works

Calpain-mediated Cleavage of the Cyclin-dependent Kinase-5 Activator p39 to p29

Patzke, H., & Tsai, L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109645200 · Cited by 143 · see citing works

Distribution of the phosphorylated microtubule-associated protein tau in developing cortical neurons

Brion, J., Octave, J., & Couck, A. M. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90533-9 · Cited by 141 · see citing works

Tau protein I is essential for amyloid β-protein iduced neurotoxicity

Takashima, A. (1993) · Medical Entomology and Zoology · Cited by 125 · see citing works

MAPK recruitment by β‐amyloid in organotypic hippocampal slice cultures depends on physical state and exposure time

Bell, K. A., O’Riordan, K. J., Sweatt, J. D., & Dineley, K. T. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02722.x · Cited by 114 · see citing works

Decreased Cyclin-Dependent Kinase 5 (cdk5) Activity Is Accompanied by Redistribution of cdk5 and Cytoskeletal Proteins and Increased Cytoskeletal Protein Phosphorylation in p35 Null Mice

Hallows, J. L., Chen, K., DePinho, R. A., & Vincent, I. J. (2003) · Journal of Neuroscience · doi:10.1523/jneurosci.23-33-10633.2003 · Cited by 111 · see citing works

Mitotic-like Tau Phosphorylation by p25-Cdk5 Kinase Complex

Hamdane, M., Sambo, A., Delobel, P., Bégard, S., Violleau, A., Delacourte, A., Bertrand, P., Bénavidès, J., & Buée, L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302872200 · Cited by 107 · see citing works

Cdk5 on the brain.

Smith, D. S., Greer, P. L., & Tsai, L. (2001) · PubMed · Cited by 105 · see citing works

Sites of phosphorylation in tau and factors affecting their regulation

Anderton, B. H., Betts, J. C., Blackstock, W. P., Brion, J., Chapman, S., Connell, J. W., Dayanandan, R., Gallo, J., Gibb, G., Hanger, D. P., et al. (2001) · Biochemical Society Symposia · doi:10.1042/bss0670073 · Cited by 99 · see citing works

Functional studies of Alzheimer's disease tau protein

Lu, Q., & Jg, W. (1993) · Journal of Neuroscience · doi:10.1523/jneurosci.13-02-00508.1993 · Cited by 96 · see citing works

Dephosphorylation of microtubule‐associated protein tau by protein phosphatase‐1 and ‐2C and its implication in Alzheimer disease

Gong, C., Grundke, I., Damuni, Z., & Iqbal, K. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80247-5 · Cited by 96 · see citing works

Microtubule-Affinity Regulating Kinase (MARK) Is Tightly Associated with Neurofibrillary Tangles in Alzheimer Brain: A Fluorescence Resonance Energy Transfer Study

Chin, J., Knowles, R. B., Schneider, A., Drewes, G., Mandelkow, E., & Hyman, B. T. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.11.966 · Cited by 95 · see citing works

Role of tau phosphorylation by glycogen synthase kinase-3β in the regulation of organelle transport

Tatebayashi, Y., Haque, N., Tung, Y. C., Iqbal, K., & Grundke, I. (2004) · Journal of Cell Science · doi:10.1242/jcs.01018 · Cited by 92 · see citing works

Phosphorylation of Protein Phosphatase Inhibitor-1 by Cdk5

Bibb, J. A., Nishi, A., O'Callaghan, J. P., Ule, J., Lan, M. J., Snyder, G. L., Horiuchi, A., Saito, T., Hisanaga, S.-I., Czernik, A. J., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007197200 · Cited by 91 · see citing works

Tau Protein in Normal and Alzheimer's Disease Brain

Johnson, G. V., & Jenkins, S. (1999) · Journal of Alzheimer's Disease · doi:10.3233/jad-1999-14-511 · Cited by 83 · see citing works

Coexpression of Human cdk5 and Its Activator p35 with Human Protein Tau in Neurons in Brain of Triple Transgenic Mice

den Haute, C. V., Spittaels, K., Dorpe, J. V., Lasrado, R., Vandezande, K., Laenen, I., Geerts, H., & Leuven, F. V. (2001) · Neurobiology of Disease · doi:10.1006/nbdi.2000.0333 · Cited by 81 · see citing works

Regulation of neuronal cytoskeleton by lysophosphatidic acid: role of GSK-3

Sayas, C. L. (2002) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/s1388-1981(02)00149-x · Cited by 81 · see citing works

Modulation of the phosphorylation state of tau in situ: the roles of calcium and cyclic AMP

Fleming, L. M., & Johnson, G. V. W. (1995) · Biochemical Journal · doi:10.1042/bj3090041 · Cited by 80 · see citing works

The Relationship between Amyloid and Tau

Hardy, J. (2003) · Journal of Molecular Neuroscience · doi:10.1385/jmn:20:2:203 · Cited by 80 · see citing works

Tau, where are we now?

Johnson, G. V. W., & Bailey, C. D. C. (2002) · Journal of Alzheimer s Disease · doi:10.3233/jad-2002-4505 · Cited by 78 · see citing works

Characterization of the in vitro phosphorylation of human tau by tau protein kinase II (cdk5/p20) using mass spectrometry

Lund, E. T., McKenna, R., EVANS, D. B., Sharma, S. K., & Mathews, W. R. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00130.x · Cited by 74 · see citing works

Ser‐262 in human recombinant tau protein is a markedly more favorable site for phosphorylation by CaMKII than PKA or PhK

Sironi, J., Yen, S.-H. C., Gondal, J. A., Wu, Q., Grundke, I., & Iqbal, K. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01185-5 · Cited by 73 · see citing works

Neuronal Cdc2-like Protein Kinase (Cdk5/p25) Is Associated with Protein Phosphatase 1 and Phosphorylates Inhibitor-2

Agarwal-Mawal, A., & Paudel, H. K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010002200 · Cited by 53 · see citing works

Ser 67 -phosphorylated inhibitor 1 is a potent protein phosphatase 1 inhibitor

Huang, K.-X., & Paudel, H. K. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100460897 · Cited by 53 · see citing works

Significance and mechanism of alzheimer neurofibrillary degeneration and therapeutic targets to inhibit this lesion

Iqbal, K., Alonso, A. D. C., El-Akkad, E., Gong, C., Haque, N., Khatoon, S., Pei, J.-J., Tsujio, I., Wang, J., & Grundke, I. (2002) · Journal of Molecular Neuroscience · doi:10.1007/s12031-002-0017-3 · Cited by 49 · see citing works

Cleavage of the cyclin-dependent kinase 5 activator p35 to p25 does not induce tau hyperphosphorylation

Kerokoski, P., Suuronen, T., Salminen, A., Soininen, H. S., & Pirttilä, T. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02543-3 · Cited by 37 · see citing works

Effects of cyclin‐dependent kinase‐5 activity on apoptosis and tau phosphorylation in immortalized mouse brain cortical cells

Shelton, S. B., Krishnamurthy, P., & Johnson, G. V. W. (2004) · Journal of Neuroscience Research · doi:10.1002/jnr.20051 · Cited by 26 · see citing works

Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature

Nelson, P. T., Alafuzoff, I., Bigio, E. H., Bouras, C., Braak, H., Cairns, N. J., Castellani, R. J., Crain, B. J., Davies, P., Tredici, K. D., et al. (2012) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/nen.0b013e31825018f7 · Cited by 2,050 · see citing works

Tau protein liquid–liquid phase separation can initiate tau aggregation

Wegmann, S., Eftekharzadeh, B., Tepper, K., Zoltowska, K. M., Bennett, R. E., Dujardin, S., Laskowski, P. R., MacKenzie, D., Kamath, T., Commins, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201798049 · Cited by 1,102 · see citing works

Microglia in Neurological Diseases: A Road Map to Brain-Disease Dependent-Inflammatory Response

Bachiller, S., Jiménez-Ferrer, I., Paulus, A., Yang, Y., Swanberg, M., Deierborg, T., & Boza‐Serrano, A. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00488 · Cited by 706 · see citing works

Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer’s Disease, Parkinson’s Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis

Nguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Domı́nguez, L., Shea, J., Dokholyan, N. V., Simone, A. D., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 676 · see citing works

Identification of oligomers at early stages of tau aggregation in Alzheimer's disease

Lasagna‐Reeves, C. A., Castillo‐Carranza, D. L., Sengupta, U., Sarmiento, J., Troncoso, J., Jackson, G. R., & Kayed, R. (2012) · The FASEB Journal · doi:10.1096/fj.11-199851 · Cited by 527 · see citing works

Phase separation and neurodegenerative diseases: a disturbance in the force

Zbinden, A., Pérez-Berlanga, M., De Rossi, P., & Polymenidou, M. (2020) · Developmental Cell · doi:10.1016/j.devcel.2020.09.014 · Cited by 500 · see citing works

How does diabetes accelerate Alzheimer disease pathology?

Sims-Robinson, C., Kim, B., Rosko, A., & Feldman, E. L. (2010) · Nature Reviews Neurology · doi:10.1038/nrneurol.2010.130 · Cited by 492 · see citing works

Deciphering the mechanism underlying late-onset Alzheimer disease

Krstic, D., & Knuesel, I. (2013) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.236 · Cited by 457 · see citing works

Untangling tau hyperphosphorylation in drug design for neurodegenerative diseases

Mazanetz, M. P., & Fischer, P. M. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2111 · Cited by 459 · see citing works

Alzheimer’s Disease

de Paula, V. D. J. R., Radanovic, M., Diniz, B. S., & Forlenza, O. V. (2012) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-007-5416-4_14 · Cited by 444 · see citing works

Tau Protein Modifications and Interactions: Their Role in Function and Dysfunction

Mietelska‐Porowska, A., Wasik, U., Goras, M., Filipek, A., & Niewiadomska, G. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15034671 · Cited by 407 · see citing works

Impaired neurogenesis is an early event in the etiology of familial Alzheimer’s disease in transgenic mice

Demars, M., Hu, Y., Gadadhar, A., & Lazarov, O. (2010) · Journal of Neuroscience Research · doi:10.1002/jnr.22387 · Cited by 326 · see citing works

Neurogenesis and Alzheimer's disease: At the crossroads

Lazarov, O., & Marr, R. A. (2009) · Experimental Neurology · doi:10.1016/j.expneurol.2009.08.009 · Cited by 326 · see citing works

Alzheimer Disease-specific Conformation of Hyperphosphorylated Paired Helical Filament-Tau Is Polyubiquitinated through Lys-48, Lys-11, and Lys-6 Ubiquitin Conjugation

Cripps, D., Thomas, S. N., Jeng, Y., Yang, F., Davies, P., & Yang, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512786200 · Cited by 312 · see citing works

The Therapeutic Potential of Metformin in Neurodegenerative Diseases

Rotermund, C., Machetanz, G., & Fitzgerald, J. C. (2018) · Frontiers in Endocrinology · doi:10.3389/fendo.2018.00400 · Cited by 310 · see citing works

Physiological and pathological phosphorylation of tau by Cdk5

Kimura, T., Ishiguro, K., & Hisanaga, S. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00065 · Cited by 297 · see citing works

Amyloid Activates GSK-3β to Aggravate Neuronal Tauopathy in Bigenic Mice

Terwel, D., Muyllaert, D., Dewachter, I., Borghgraef, P., Croes, S., Devijver, H., & Van Leuven, F. (2008) · The American Journal of Pathology · doi:10.2353/ajpath.2008.070904 · Cited by 300 · see citing works

DYRK1A-mediated Hyperphosphorylation of Tau

Ryoo, S., Jeong, H. K., Radnaabazar, C., Yoo, J.-J., Cho, H.-J., Lee, H. W., Kim, I.-S., Cheon, Y. H., Ahn, Y. S., Chung, S., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m707358200 · Cited by 285 · see citing works

Proline-directed Pseudo-phosphorylation at AT8 and PHF1 Epitopes Induces a Compaction of the Paperclip Folding of Tau and Generates a Pathological (MC-1) Conformation

Jeganathan, S., Hascher, A., Chinnathambi, S., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805300200 · Cited by 278 · see citing works

Targeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models

Silva, M. C., Ferguson, F. M., Cai, Q., Donovan, K. A., Nandi, G., Patnaik, D., Zhang, T., Huang, H.-T., Lucente, D. E., Dickerson, B. C., et al. (2019) · eLife · doi:10.7554/elife.45457 · Cited by 283 · see citing works

Role of tau protein in Alzheimer’s disease: The prime pathological player

Muralidar, S., Ambi, S. V., Sekaran, S., Thirumalai, D., & Palaniappan, B. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.327 · Cited by 278 · see citing works

Metformin attenuates Alzheimer’s disease-like neuropathology in obese, leptin-resistant mice

Li, J., Deng, J., Sheng, W., & Zuo, Z. (2012) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2012.03.002 · Cited by 260 · see citing works

Metformin – a Future Therapy for Neurodegenerative Diseases

Markowicz-Piasecka, M., Sikora, J., Szydłowska, A., Skupień, A., Mikiciuk-Olasik, E., & Huttunen, K. (2017) · Pharmaceutical Research · doi:10.1007/s11095-017-2199-y · Cited by 248 · see citing works

Diabetes and Alzheimer’s disease crosstalk

Baglietto‐Vargas, D., Shi, J. J., Yaeger, D. M., Ager, R. R., & LaFerla, F. M. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.03.005 · Cited by 254 · see citing works

Tau protein aggregation in Alzheimer's disease: An attractive target for the development of novel therapeutic agents

Jouanne, M., Rault, S., & Voisin‐Chiret, A. S. (2017) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2017.07.070 · Cited by 252 · see citing works

Tau oligomers and tau toxicity in neurodegenerative disease

Ward, S., Himmelstein, D. S., Lancia, J. K., & Binder, L. I. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120134 · Cited by 244 · see citing works

Tau Protects Microtubules in the Axon from Severing by Katanin

Qiang, L., Yu, W., Andreadis, A., Luo, M., & Baas, P. W. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.5392-05.2006 · Cited by 235 · see citing works

Neurons derived from sporadic Alzheimer’s disease iPSCs reveal elevated TAU hyperphosphorylation, increased amyloid levels, and GSK3B activation

Ochalek, A., Mihalik, B., Avci, H. X., Chandrasekaran, A., Téglási, A., Bock, I., Giudice, M. L., Táncos, Z., Molnár, K., László, L., et al. (2017) · Alzheimer's Research &amp; Therapy · doi:10.1186/s13195-017-0317-z · Cited by 225 · see citing works

Mesenchymal stem cell-derived extracellular vesicles ameliorate Alzheimer's disease-like phenotypes in a preclinical mouse model

Cone, A. S., Yuan, X., Sun, L. J., Duke, L. C., Vreones, M. P., Carrier, A. N., Kenyon, S. M., Carver, S. R., Cushing, S. D., Stimmell, A. C., et al. (2021) · Theranostics · doi:10.7150/thno.62069 · Cited by 224 · see citing works

Repeated Mild Traumatic Brain Injury

Fehily, B., & Fitzgerald, M. (2017) · Cell Transplantation · doi:10.1177/0963689717714092 · Cited by 223 · see citing works

Enzymatic Noncovalent Synthesis

He, H., Tan, W., Guo, J., Yi, M., Shy, A. N., & Xu, B. (2020) · Chemical Reviews · doi:10.1021/acs.chemrev.0c00306 · Cited by 224 · see citing works

MicroRNA: Implications for Alzheimer Disease and other Human CNS Disorders

Maes, O. C., Chertkow, H. M., Wang, E., & Schipper, H. M. (2009) · Current Genomics · doi:10.2174/138920209788185252 · Cited by 217 · see citing works

Death Associated Protein Kinase 1 (DAPK1): A Regulator of Apoptosis and Autophagy

Singh, P., Ravanan, P., & Talwar, P. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00046 · Cited by 215 · see citing works

Calcium dysregulation in Alzheimer's disease

Bojarski, Ł., Herms, J. W., & Kuźnicki, J. (2007) · Neurochemistry International · doi:10.1016/j.neuint.2007.10.002 · Cited by 202 · see citing works

Molecular links between Alzheimer’s disease and diabetes mellitus

Yang, Y., & Song, W. (2013) · Neuroscience · doi:10.1016/j.neuroscience.2013.07.009 · Cited by 201 · see citing works

Tau oligomers and aggregation in Alzheimer’s disease

Meraz‐Ríos, M. A., León, K. I. L.-D., Campos‐Peña, V., Anda-Hernández, M. A. D., & Mena‐López, R. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06511.x · Cited by 193 · see citing works

Fibroblasts in three dimensional matrices: cell migration and matrix remodeling

Rhee, S. (2009) · Experimental & Molecular Medicine · doi:10.3858/emm.2009.41.12.096 · Cited by 185 · see citing works

Oxidative Stress Occurs Prior to Amyloid Aβ Plaque Formation and Tau Phosphorylation in Alzheimer’s Disease: Role of Glutathione and Metal Ions

Roy, R. G., Mandal, P. K., & Maroon, J. C. (2023) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.3c00486 · Cited by 194 · see citing works

Alzheimer’s disease-specific tau phosphorylation is induced by herpes simplex virus type 1

Wozniak, M. A., Frost, A. L., & Itzhaki, R. F. (2009) · Journal of Alzheimer's Disease · doi:10.3233/jad-2009-0963 · Cited by 216 · see citing works

Tau Is Hyperphosphorylated at Multiple Sites in Mouse Brain In Vivo After Streptozotocin-Induced Insulin Deficiency

Clodfelder‐Miller, B., Zmijewska, A. A., Johnson, G. V. W., & Jope, R. S. (2006) · Diabetes · doi:10.2337/db06-0485 · Cited by 185 · see citing works

Local translation and directional steering in axons

Lin, A. C., & Holt, C. E. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601808 · Cited by 184 · see citing works

β-Amyloid Immunotherapy Prevents Synaptic Degeneration in a Mouse Model of Alzheimer's Disease

Buttini, M., Masliah, E., Barbour, R., Grajeda, H., Motter, R., Johnson-Wood, K., Khan, K., Seubert, P., Freedman, S., Schenk, D., et al. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1697-05.2005 · Cited by 176 · see citing works

Tau Mutations in Neurodegenerative Diseases

Wolfe, M. S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800013200 · Cited by 166 · see citing works

Behavioural and psychological symptoms of dementia in mouse models of Alzheimer’s disease-related pathology

Kosel, F., Pelley, J. M. S., & Franklin, T. B. (2020) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2020.02.012 · Cited by 162 · see citing works

Relationship Between Tau Pathology and Neuroinflammation in Alzheimer's Disease

Metcalfe, M., & Figueiredo‐Pereira, M. E. (2010) · Mount Sinai Journal of Medicine A Journal of Translational and Personalized Medicine · doi:10.1002/msj.20163 · Cited by 158 · see citing works

Phosphorylation of Tau Protein as the Link between Oxidative Stress, Mitochondrial Dysfunction, and Connectivity Failure: Implications for Alzheimer’s Disease

Mondragón‐Rodríguez, S., Perry, G. L., Zhu, X., Moreira, P. I., Acevedo, M., & Williams, S. (2013) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2013/940603 · Cited by 155 · see citing works

GSK3 and Alzheimer’s disease: facts and fiction…

Kremer, A. (2011) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2011.00017 · Cited by 155 · see citing works

Neurobiological pathways to Alzheimer's disease: Amyloid-beta, TAU protein or both?

de Paula, V. D. J. R., Guimarães, F. M., Diniz, B. S., & Forlenza, O. V. (2009) · Dementia & Neuropsychologia · doi:10.1590/s1980-57642009dn30300003 · Cited by 155 · see citing works

Methamphetamine-induced neuroinflammation and neuronal dysfunction in the mice hippocampus: preventive effect of indomethacin

Gonçalves, J., Baptista, S., Martins, T., Milhazes, N., Borges, F., Ribeiro, C. F., Malva, J. O., & Silva, A. P. (2010) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.07059.x · Cited by 152 · see citing works

Dynamic association of tau with neuronal membranes is regulated by phosphorylation

Pooler, A. M., Usardi, A., Evans, C. J., Philpott, K. L., Noble, W., & Hanger, D. P. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.01.005 · Cited by 148 · see citing works

Rapid Accumulation of Endogenous Tau Oligomers in a Rat Model of Traumatic Brain Injury

Hawkins, B. E., Krishnamurthy, S., Castillo‐Carranza, D. L., Sengupta, U., Prough, D. S., Jackson, G. R., DeWitt, D. S., & Kayed, R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.472746 · Cited by 148 · see citing works

Impaired adult neurogenesis is an early event in Alzheimer’s disease neurodegeneration, mediated by intracellular Aβ oligomers

Scopa, C., Marrocco, F., Latina, V., Ruggeri, F., Corvaglia, V., Regina, F. L., Ammassari‐Teule, M., Middei, S., Amadoro, G., Meli, G., et al. (2019) · Cell Death and Differentiation · doi:10.1038/s41418-019-0409-3 · 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

The role of tau phosphorylation and cleavage in neuronal cell death

Chun, W. (2006) · Frontiers in bioscience · doi:10.2741/2097 · Cited by 142 · see citing works

Abnormally phosphorylated tau is associated with neuronal and axonal loss in experimental autoimmune encephalomyelitis and multiple sclerosis

Anderson, J. M., Hampton, D. W., Patani, R., Pryce, G., Crowther, R. A., Reynolds, R., Franklin, R. J. M., Giovannoni, G., Compston, D. A. S., Baker, D., et al. (2008) · Brain · doi:10.1093/brain/awn119 · Cited by 141 · see citing works

Metabolic Risk Factors of Sporadic Alzheimer's Disease: Implications in the Pathology, Pathogenesis and Treatment

Chakrabarti, S., Kumar Khemka, V., Banerjee, A., Chatterjee, G., Ganguly, A., & Biswas, A. (2015) · Aging and disease · doi:10.14336/ad.2014.002 · Cited by 134 · see citing works

Tau pathology induces loss of GABAergic interneurons leading to altered synaptic plasticity and behavioral impairments

Levenga, J., Krishnamurthy, P., Rajamohamedsait, H. B., Wong, H., Franke, T. F., Cain, P., Sigurdsson, E. M., & Hoeffer, C. A. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-34 · Cited by 128 · see citing works

Modulation of Phosphoprotein Activity by Phosphorylation Targeting Chimeras (PhosTACs)

Chen, P.-H., Hu, Z., An, E., Okeke, I., Zheng, S., Luo, X., Gong, A., Jaime-Figueroa, S., & Crews, C. M. (2021) · ACS Chemical Biology · doi:10.1021/acschembio.1c00693 · Cited by 130 · see citing works

Glycogen synthase kinase‐3β, or a link between amyloid and tau pathology?

Muyllaert, D., Kremer, A., Jaworski, T., Borghgraef, P., Devijver, H., Croes, S., Dewachter, I., & Leuven, F. V. (2008) · Genes Brain & Behavior · doi:10.1111/j.1601-183x.2007.00376.x · Cited by 130 · see citing works

Chronic neurodegenerative consequences of traumatic brain injury

Chauhan, N. B. (2014) · Restorative Neurology and Neuroscience · doi:10.3233/rnn-130354 · Cited by 126 · see citing works

Direct evidence of phosphorylated neuronal intermediate filament proteins in neurofibrillary tangles (NFTs): phosphoproteomics of Alzheimer's NFTs

Rudrabhatla, P., Jaffe, H., & Pant, H. C. (2011) · The FASEB Journal · doi:10.1096/fj.11-181297 · Cited by 121 · see citing works

The Role of Tau Oligomers in the Onset of Alzheimer's Disease Neuropathology

Cárdenas-Aguayo, M. D. C., Gómez-Virgilio, L., DeRosa, S., & Meraz-Ríos, M. A. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500148z · Cited by 120 · see citing works

Drosophila IKK-related kinase Ik2 and Katanin p60-like 1 regulate dendrite pruning of sensory neuron during metamorphosis

Lee, H., Jan, L. Y., & Jan, Y. N. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902051106 · Cited by 120 · see citing works

Nobiletin, a Citrus Flavonoid, Ameliorates Cognitive Impairment, Oxidative Burden, and Hyperphosphorylation of Tau in Senescence-Accelerated Mouse

Nakajima, A., Aoyama, Y., Nguyen, T.-T. L., Shin, E.-J., Kim, H.-C., Yamada, S., Nakai, T., Nagai, T., Yokosuka, A., Mimaki, Y., et al. (2013) · Behavioural Brain Research · doi:10.1016/j.bbr.2013.05.025 · Cited by 115 · see citing works

The Role of microRNAs in Alzheimer’s Disease and Their Therapeutic Potentials

Shaik, M. M., Tamargo, I. A., Abubakar, M. B., Kamal, M. A., Greig, N. H., & Gan, S. H. (2018) · Genes · doi:10.3390/genes9040174 · Cited by 114 · see citing works

Synaptic tau: A pathological or physiological phenomenon?

Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01246-y · Cited by 117 · see citing works

The Role of Post-Translational Modifications on Prion-Like Aggregation and Liquid-Phase Separation of FUS

Rhoads, S. N., Monahan, Z. T., Yee, D. S., & Shewmaker, F. P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030886 · Cited by 115 · see citing works

Phosphorylation of tau at Ser214 mediates its interaction with 14‐3‐3 protein: implications for the mechanism of tau aggregation

Sadik, G., Tanaka, T., Kato, K., Yamamori, H., Begum, N. N., Morihara, T., & Takeda, M. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05716.x · Cited by 114 · see citing works

Prion-Like Propagation of Post-Translationally Modified Tau in Alzheimer’s Disease: A Hypothesis

Sonawane, S. K., & Chinnathambi, S. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1111-5 · Cited by 113 · see citing works

Mice lacking phosphatase PP2A subunit PR61/B’δ ( <i>Ppp2r5d</i> ) develop spatially restricted tauopathy by deregulation of CDK5 and GSK3β

Louis, J. V., Martens, E., Borghgraef, P., Lambrecht, C., Sents, W., Longin, S., Zwaenepoel, K., Pijnenborg, R., Landrieu, I., Lippens, G., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018777108 · Cited by 112 · see citing works

Alpha‐Synuclein induces hyperphosphorylation of Tau in the MPTP model of Parkinsonism

Duka, T., Rusnak, M., Drolet, R. E., Duka, V., Wersinger, C., Goudreau, J. L., & Sidhu, A. (2006) · The FASEB Journal · doi:10.1096/fj.06-6092com · Cited by 112 · see citing works

Mitochondrial Dynamics: A Key Role in Neurodegeneration and a Potential Target for Neurodegenerative Disease

Yang, D., Ying, J., Wang, X., Zhao, T., Yoon, S., Yang, F., Zheng, Q., Liu, X., Yu, W., & Hua, F. (2021) · Frontiers in Neuroscience · doi:10.3389/fnins.2021.654785 · Cited by 110 · see citing works

Cytoskeleton proteins are modulators of mutant tau-induced neurodegeneration in Drosophila

Blard, O., Feuillette, S., Bou, J., Chaumette, B., Frébourg, T., Campion, D., & Lecourtois, M. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm011 · Cited by 110 · see citing works

Methylation as a key regulator of Tau aggregation and neuronal health in Alzheimer’s disease

Balmik, A. A., & Chinnathambi, S. (2021) · Cell Communication and Signaling · doi:10.1186/s12964-021-00732-z · Cited by 108 · see citing works

Reactive Oxygen Species, Redox Signaling and Neuroinflammation in Alzheimer's Disease: The NF-κB Connection

Kaur, U., Banerjee, P., Bir, A., Sinha, M. S., Biswas, A., & Chakrabarti, S. (2015) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026615666150114160543 · Cited by 107 · see citing works

A novel tau‐based rhesus monkey model of Alzheimer's pathogenesis

Beckman, D., Chakrabarty, P., Ott, S. P., Dao, A., Zhou, E., Janssen, W. G. M., Donis‐Cox, K., Muller, S., Kordower, J. H., & Morrison, J. H. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12318 · Cited by 112 · see citing works

Tau Phosphorylated at Tyrosine 394 is Found in Alzheimer's Disease Tangles and can be a Product of the Abl-Related Kinase, Arg

Tremblay, M. A., Acker, C. M., & Davies, P. (2010) · Journal of Alzheimer s Disease · doi:10.3233/jad-2010-1271 · Cited by 106 · see citing works

Brain Derived Exosomes Are a Double-Edged Sword in Alzheimer’s Disease

Song, Z., Xu, Y., Deng, W., Zhang, L., Zhu, H., Yü, P., Qu, Y., Zhao, W., Han, Y., & Qin, C. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00079 · Cited by 103 · see citing works

Insights into Disease-Associated Tau Impact on Mitochondria

Szabo, L., Eckert, A., & Grimm, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176344 · Cited by 102 · see citing works

Human iPSC-derived neuronal model of Tau-A152T frontotemporal dementia reveals tau-mediated mechanisms of neuronal vulnerability

Silva, M. C., Cheng, C., Mair, W., Almeida, S., Fong, H., Biswas, M. H. U., Zhang, Z., Huang, Y., Temple, S., Coppola, G., et al. (2016) · Stem Cell Reports · doi:10.1016/j.stemcr.2016.08.001 · Cited by 103 · see citing works

Interleukin-18 increases expression of kinases involved in tau phosphorylation in SH-SY5Y neuroblastoma cells

Ojala, J. O., Sutinen, E. M., Salminen, A., & Pirttilä, T. (2008) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2008.09.012 · Cited by 102 · see citing works

Moonlighting chaperone‐like activity of the universal regulatory 14‐3‐3 proteins

Sluchanko, N. N., & Gusev, N. B. (2016) · FEBS Journal · doi:10.1111/febs.13986 · Cited by 103 · see citing works

Possible Mechanisms of Tau Spread and Toxicity in Alzheimer’s Disease

Zhang, H., Cao, Y., Ma, L., Wei, Y., & Li, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.707268 · Cited by 104 · see citing works

Glucocorticoids Trigger Alzheimer disease-like pathobiochemistry in rat neuronal cells expressing human tau

Sotiropoulos, I., Catania, C., Riedemann, T., Fry, J. P., Breen, K. C., Michaelidis, T. M., & Almeida, O. F. X. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05613.x · Cited by 97 · see citing works

The interactions of p53 with tau and Aß as potential therapeutic targets for Alzheimer’s disease

Jembrek, M. J., Slade, N., Hof, P. R., & Šimić, G. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.05.001 · Cited by 99 · see citing works

Wnt/&amp;#946;-Catenin Signaling in Alzheimer’s Disease

Ferrari, G., Avila, M., Medina, M., Perez-Palma, E., Bustos, B., & Alarcon, M. (2014) · CNS &amp; Neurological Disorders - Drug Targets · doi:10.2174/1871527312666131223113900 · Cited by 95 · see citing works

MIRNAS in Astrocyte-Derived Exosomes as Possible Mediators of Neuronal Plasticity

Lafourcade, C., Ramírez, J. P., Luarte, A., Fernández, A., & Wyneken, Ú. (2016) · Journal of Experimental Neuroscience · doi:10.4137/jen.s39916 · Cited by 98 · see citing works

Death-associated protein kinase 1 has a critical role in aberrant tau protein regulation and function

Kim, B. M., You, M.-H., Chen, C.-H., Lee, S., Hong, Y., Hong, Y., Kimchi, A., Zhou, X. Z., & Lee, T. H. (2014) · Cell Death &amp; Disease · doi:10.1038/cddis.2014.216 · Cited by 98 · see citing works

The Role of Tau in Neurodegenerative Diseases and Its Potential as a Therapeutic Target

Wolfe, M. S. (2012) · Scientifica · doi:10.6064/2012/796024 · Cited by 97 · see citing works

Extracellular association of APP and tau fibrils induces intracellular aggregate formation of tau

Takahashi, M., Miyata, H., Kametani, F., Nonaka, T., Akiyama, H., Hisanaga, S., & Hasegawa, M. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1415-2 · Cited by 90 · see citing works

Interaction between NH2-tau fragment and Aβ in Alzheimer's disease mitochondria contributes to the synaptic deterioration

Amadoro, G., Corsetti, V., Atlante, A., Florenzano, F., Capsoni, S., Bussani, R., Mercanti, D., & Calissano, P. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.08.001 · Cited by 94 · see citing works

p73 Regulates Neurodegeneration and Phospho-Tau Accumulation during Aging and Alzheimer's Disease

Wetzel, M. K., Naska, S., Laliberté, C. L., Rymar, V. V., Fujitani, M., Biernaskie, J., Cole, C. J., Lerch, J. P., Spring, S., Wang, S., et al. (2008) · Neuron · doi:10.1016/j.neuron.2008.07.021 · Cited by 92 · see citing works

Intrinsically disordered proteins/regions and insight into their biomolecular interactions

Chakrabarti, P., & Chakravarty, D. (2022) · Biophysical Chemistry · doi:10.1016/j.bpc.2022.106769 · Cited by 90 · see citing works

Long-term exercise pre-training attenuates Alzheimer’s disease–related pathology in a transgenic rat model of Alzheimer’s disease

Yang, L., Wu, C., Li, Y., Dong, Y., Wu, C. Y., Lee, R. H., Brann, D. W., Lin, H. W., & Zhang, Q. (2022) · GeroScience · doi:10.1007/s11357-022-00534-2 · Cited by 93 · see citing works

Alzheimer disease specific phosphoepitopes of Tau interfere with assembly of tubulin but not binding to microtubules

Amniai, L., Barbier, P., Sillen, A., Wieruszeski, J.-M., Peyrot, V., Lippens, G., & Landrieu, I. (2009) · The FASEB Journal · doi:10.1096/fj.08-121590 · Cited by 105 · see citing works

Abnormal pathways in the genu of the corpus callosum in schizophrenia pathogenesis: a proteome study

Sivagnanasundaram, S., Crossett, B., Dedova, I. V., Cordwell, S. J., & Matsumoto, I. (2007) · PROTEOMICS - CLINICAL APPLICATIONS · doi:10.1002/prca.200700230 · Cited by 90 · see citing works

Possible Compensatory Events in Adult Down Syndrome Brain Prior to the Development of Alzheimer Disease Neuropathology: Targets for Nonpharmacological Intervention

Head, E., Lott, I. T., Patterson, D. W., Doran, E. W., & Haier, R. J. (2007) · Journal of Alzheimer s Disease · doi:10.3233/jad-2007-11110 · Cited by 89 · 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

A metabolic and functional overview of brain aging linked to neurological disorders

Baquer, N. Z., Taha, A., Kumar, P., McLean, P., Cowsik, S. M., Kale, R. K., Singh, R., & Sharma, D. (2009) · Biogerontology · doi:10.1007/s10522-009-9226-2 · Cited by 87 · see citing works

Sterile Neuroinflammation and Strategies for Therapeutic Intervention

Banjara, M., & Ghosh, C. (2017) · International Journal of Inflammation · doi:10.1155/2017/8385961 · Cited by 87 · see citing works

Tau phosphorylation: physiological and pathological consequences

Stoothoff, W. H., & Johnson, G. V. W. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.017 · Cited by 439 · see citing works

The Role of Tau Phosphorylation in the Pathogenesis of Alzheimers Disease

Mi, K., & Johnson, G. V. W. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025279 · Cited by 166 · see citing works

Regulated phosphorylation and dephosphorylation of tau protein: effects on microtubule interaction, intracellular trafficking and neurodegeneration.

Billingsley, M., & Kincaid, R. (1997) · Biochemical Journal · doi:10.1042/bj3230577 · Cited by 469 · see citing works

The role of tau kinases in Alzheimer's disease.

Dolan, P. J., & Johnson, G. V. W. (2010) · PubMed · Cited by 174 · see citing works

Tau Protein Phosphorylation as a Therapeutic Target in Alzheimers Disease

Lau, L., Schachter, J. B., Seymour, P. A., & Sanner, M. A. (2002) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026024607526 · Cited by 62 · see citing works