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

PROTEIN MEASUREMENT WITH THE FOLIN PHENOL REAGENT

Lowry, O. H., Rosebrough, N., Farr, A. L., & Randall, R. (1951) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)52451-6 · Cited by 316,394

Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

LAEMMLI, U. K. (1970) · Nature · doi:10.1038/227680a0 · Cited by 249,961

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

Microtubule Assembly in the Absence of Added Nucleotides

Shelanski, M. L., Gaskin, F., & Cantor, C. R. (1973) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.70.3.765 · Cited by 2,053

Purification of tau, a microtubule-associated protein that induces assembly of microtubules from purified tubulin

Cleveland, D. W., Hwo, S.-Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90213-3 · Cited by 915

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

A taxol-dependent procedure for the isolation of microtubules and microtubule-associated proteins (MAPs).

Vallee, R. B. (1982) · The Journal of cell biology · doi:10.1083/jcb.92.2.435 · Cited by 551

Cyclic AMP-dependent endogenous phosphorylation of a microtubule-associated protein.

Sloboda, R. D., Rudolph, S. A., Rosenbaum, J. L., & Greengard, P. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.1.177 · Cited by 547

Molecular characterization of the cAMP-dependent protein kinase bound to microtubule-associated protein 2.

Theurkauf, W. E., & Vallee, R. B. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)81107-9 · Cited by 333

Nucleated Assembly of Microtubules in Porcine Brain Extracts

Borisy, G. G., & Olmsted, J. B. (1972) · Science · doi:10.1126/science.177.4055.1196 · Cited by 322

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

Alzheimer Disease

Smith, M. A. (1998) · International review of neurobiology · doi:10.1016/s0074-7742(08)60607-8 · Cited by 206

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 202

τ is phosphorylated by GSK‐3 at several sites found in Alzheimer disease and its biological activity markedly inhibited only after it is prephosphorylated by A‐kinase

Wang, J.-Z., Wu, Q., Smith, A., Grundke, I., & Iqbal, K. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)01090-4 · Cited by 199

The cell biology of primary cell walls during salt stress

Colin, L., Ruhnow, F., Zhu, J., Zhao, C., Zhao, Y., & Persson, S. (2022) · The Plant Cell · doi:10.1093/plcell/koac292 · Cited by 198

Phosphorylation of Microtubule-associated Proteins MAP2 and MAP4 by the Protein Kinase p110mark

Illenberger, S., Drewes, G., Trinczek, B., Biernat, J., Meyer, H. E., Olmsted, J. B., Mandelkow, E., & Mandelkow�, E. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.18.10834 · Cited by 203

Recognition of Alzheimer paired helical filaments by monoclonal neurofilament antibodies is due to crossreaction with tau protein.

Nukina, N., Kosik, K. S., & Selkoe, D. J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.10.3415 · Cited by 199

It’s all about tau

Tapia‐Rojas, C., Cabezas-Opazo, F., Deaton, C. A., Vergara, E. H., Johnson, G. V. W., & Quintanilla, R. A. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.005 · Cited by 207

Transgenic Expression of the Shortest Human Tau Affects Its Compartmentalization and Its Phosphorylation as in the Pretangle Stage of Alzheimer's Disease

Brion, J., Tremp, G. L., & Octave, J. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65272-8 · Cited by 203

Microtubule bundling by tau proteins in vivo: analysis of functional domains

Kanai, Y., Chen, J., & Hirokawa, N. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05489.x · Cited by 194

Tau protein, the paired helical filament and Alzheimer's disease

Goedert, M., Klug, A., & Crowther, R. A. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9s323 · Cited by 205

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

The purification of tau protein and the occurrence of two phosphorylation states of tau in brain.

Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)71345-1 · Cited by 191

Interactions between the microtubule-associated tau proteins and S100b regulate tau phosphorylation by the Ca2+/calmodulin-dependent protein kinase II.

Baudier, J., & Cole, R. D. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60647-7 · Cited by 190

Implication of brain cdc2 and MAP2 kinases in the phosphorylation of tau protein in Alzheimer's disease

Ledesma, M. D., Correas, I., Ávila, J., & Díaz‐Nido, J. (1992) · FEBS Letters · doi:10.1016/0014-5793(92)81278-t · Cited by 190

Tau protein becomes long and stiff upon phosphorylation: correlation between paracrystalline structure and degree of phosphorylation.

Hagestedt, T., Lichtenberg-Kraag, B., Wille, H., Mandelkow�, E., & Mandelkow�, E. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.4.1643 · Cited by 188

Fluorescent BODIPY-Based Zn(II) Complex as a Molecular Probe for Selective Detection of Neurofibrillary Tangles in the Brains of Alzheimer’s Disease Patients

Ojida, A., Sakamoto, T., Inoue, M.-A., Fujishima, S., Lippens, G. M., & Hamachi, I. (2009) · Journal of the American Chemical Society · doi:10.1021/ja9008369 · Cited by 186

Tau Becomes a More Favorable Substrate for GSK-3 When It Is Prephosphorylated by PKA in Rat Brain

Liu, S. J., Zhang, J. Y., Li, H. L., Fang, Z., Wang, Q., Deng, H. M., Gong, C. X., Grundke, I., Iqbal, K., & Wang, J. Z. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m406109200 · Cited by 186

Phosphorylation of microtubule‐associated protein tau by isoforms of c‐Jun N‐terminal kinase (JNK)

Yoshida, H., Hastie, C. J., McLauchlan, H., Cohen, P., & Goedert, M. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02479.x · Cited by 185

Role of protein phosphatase-2A and -1 in the regulation of GSK-3, cdk5 and cdc2 and the phosphorylation of tau in rat forebrain

Bennecib, M., Gong, C.-X., Grundke-Iqbal, I., & Iqbal, K. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02203-1 · Cited by 184

An aluminum-based rat model for Alzheimer’s disease exhibits oxidative damage, inhibition of PP2A activity, hyperphosphorylated tau, and granulovacuolar degeneration

Walton, J. R. (2007) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2007.06.001 · Cited by 183

Plasma tau/amyloid-β1–42 ratio predicts brain tau deposition and neurodegeneration in Alzheimer’s disease

Park, J., Han, S.-H., Yi, D., Byun, M. S., Lee, J. H., Jang, S. S., Ko, K., Jeon, S. Y., Lee, Y., Kim, Y. K., et al. (2018) · Brain · doi:10.1093/brain/awy347 · Cited by 181

Developmental regulation of tau phosphorylation, tau kinases, and tau phosphatases

Yu, Y., Run, X., Liang, Z., Li, Y., Liu, F., Liu, Y. M., Iqbal, K., Grundke, I., & Gong, C. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05882.x · Cited by 186

Microtubule-associated protein tau is phosphorylated by protein kinase C on its tubulin binding domain.

Correas, I., Díaz‐Nido, J., & Ávila, J. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49595-1 · Cited by 176

Identification and preliminary characterization of a 65 kDa higher-plant microtubule-associated protein

Jiang, C., & Sonobe, S. (1993) · Journal of Cell Science · doi:10.1242/jcs.105.4.891 · Cited by 176

The adult rat olfactory system expresses microtubule-associated proteins found in the developing brain

Viereck, C., Tucker, R., & Matus, A. I. (1989) · Journal of Neuroscience · doi:10.1523/jneurosci.09-10-03547.1989 · Cited by 175

Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress

Poppek, D., Keck, S., Ermak, G., Jung, T., Stolzing, A., Ullrich, O., Davies, K. J. A., & Grune, T. (2006) · Biochemical Journal · doi:10.1042/bj20060463 · Cited by 174

Disruption of microtubule network by Alzheimer abnormally hyperphosphorylated tau

Li, B., Chohan, M. O., Grundke, I., & Iqbal, K. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0207-8 · Cited by 173

The role of tau kinases in Alzheimer's disease.

Dolan, P. J., & Johnson, G. V. W. (2010) · PubMed · Cited by 178

Functions and malfunctions of the tau proteins

Shahani, N., & Brandt, R. (2002) · Cellular and Molecular Life Sciences · doi:10.1007/pl00012495 · Cited by 178

It's complicated: The relationship between sleep and Alzheimer's disease in humans

Lucey, B. P. (2020) · Neurobiology of Disease · doi:10.1016/j.nbd.2020.105031 · Cited by 172

Levels of normal and abnormally phosphorylated tau in different cellular and regional compartments of Alzheimer disease and control brains

Khatoon, S., Grundke, I., & Iqbal, K. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00829-9 · Cited by 167

Molecular Structure and Function of Microtubule-Associated Proteins

Wiche, G., Oberkanins, C., & Himmler, A. (1991) · International review of cytology · doi:10.1016/s0074-7696(08)61528-4 · Cited by 165

Tau and Tauopathies

Lee, G. S., & Leugers, C. J. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00004-7 · Cited by 173

Structure of tau protein and assembly into paired helical filaments

Friedhoff, P., von Bergen�, M., Mandelkow, E., & Mandelkow, E. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00038-7 · Cited by 172

Neuronal microtubule‐associated proteins in the embryonic avian spinal cord

Tucker, R. P., Binder, L. I., & Matus, A. I. (1988) · The Journal of Comparative Neurology · doi:10.1002/cne.902710106 · Cited by 166

Interaction of Kinesin Motor Domains with α- and β-Tubulin Subunits at a Tau-independent Binding Site

Larcher, J.-C., Boucher, D., Lazereg, S., Gros, F., & Denoulet, P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.36.22117 · Cited by 163

Amyloidogenesis of Tau protein

Niżyński, B., Dzwolak, W., & Nieznański, K. (2017) · Protein Science · doi:10.1002/pro.3275 · Cited by 166

Type 2 Diabetes Mellitus and Alzheimer’s Disease: Shared Molecular Mechanisms and Potential Common Therapeutic Targets

Hamzé, R., Delangre, E., Tolu, S., Moreau, M., Janel, N., Bailbé, D., & Movassat, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315287 · Cited by 171

Proteolysis of tau by calpain

Johnson, G. V. W., Jope, R. S., & Binder, L. I. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)91150-9 · Cited by 161

Tipping the Scales: Peptide-Dependent Dysregulation of Neural Circuit Dynamics in Alzheimer’s Disease

Harris, S. S., Wolf, F., De Strooper, B., & Busche, M. A. (2020) · Neuron · doi:10.1016/j.neuron.2020.06.005 · Cited by 161

Interaction of Tau Isoforms with Alzheimer's Disease Abnormally Hyperphosphorylated Tau and in VitroPhosphorylation into the Disease-like Protein

Alonso, A. D. C., Zaidi, T., Novák, M., Barra, H. S., Grundke, I., & Iqbal, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105365200 · Cited by 160

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

Isoforms changes of tau protein during development in various species

Takuma, H., Arawaka, S., & Mori, H. (2003) · Developmental Brain Research · doi:10.1016/s0165-3806(03)00056-7 · Cited by 157

Neuropathology of synuclein aggregates

Duda, J. E., Lee, V. M. ‐., & Trojanowski, J. Q. (2000) · Journal of Neuroscience Research · doi:10.1002/1097-4547(20000715)61:2 · Cited by 263

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 162

Restoration of biological activity of Alzheimer abnormally phosphorylated τ by dephosphorylation with protein phosphatase-2A, −2B and −1

Wang, J., Grundke, I., & Iqbal, K. (1996) · Molecular Brain Research · doi:10.1016/0169-328x(95)00316-k · Cited by 154

Metabolic, Metallic, and Mitotic Sources of Oxidative Stress in Alzheimer Disease

Smith, M. A., Nunomura, A., Zhu, X., Takeda, A., & Perry, G. L. (2000) · Antioxidants and Redox Signaling · doi:10.1089/15230860050192198 · Cited by 151

Memantine inhibits and reverses the Alzheimer type abnormal hyperphosphorylation of tau and associated neurodegeneration

Li, L., Sengupta, A., Haque, N., Grundke, I., & Iqbal, K. (2004) · FEBS Letters · doi:10.1016/j.febslet.2004.04.047 · Cited by 154

Alzheimer paired helical filaments Restoration of the biological activity by dephosphorylation

Iqbal, K., Zaidi, T., Bancher, C., & Grundke, I. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00650-4 · Cited by 150

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

Sumoylation and human disease pathogenesis

Sarge, K. D., & Park-Sarge, O.-K. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.01.004 · Cited by 148

Selective Destruction of Stable Microtubules and Axons by Inhibitors of Protein Serine/Threonine Phosphatases in Cultured Human Neurons (NT2N Cells)

Merrick, S. E., Trojanowski, J. Q., & Lee, V. M.-Y. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-15-05726.1997 · Cited by 143

Synapsin I is a microtubule-bundling protein

Baines, A. J., & Bennett, V. (1986) · Nature · doi:10.1038/319145a0 · Cited by 142

Transient increases in intracellular calcium result in prolonged site-selective increases in tau phosphorylation through a glycogen synthase kinase 3β-dependent pathway

Hartigan, J. A., & Johnson, G. V. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.30.21395 · Cited by 141

Microglial activation states and their implications for Alzheimer's Disease

Valiukas, Z., Tangalakis, K., Apostolopoulos, V., & Feehan, J. (2025) · The Journal of Prevention of Alzheimer s Disease · doi:10.1016/j.tjpad.2024.100013 · Cited by 167

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 143

Regulation of Microtubule Dynamics by Extracellular Signals: cAMP-dependent Protein Kinase Switches Off the Activity of Oncoprotein 18 in Intact Cells

Gradin, H. M., Larsson, N., Marklund, U., & Gullberg, M. H. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.140.1.131 · Cited by 141

Mechanisms of neurofibrillary degeneration and the formation of neurofibrillary tangles

Iqbal, K., Alonso, A. D. C., Gong, C., Khatoon, S., Pei, J. ‐., Wang, J. Z., & Grundke, I. (1998) · Journal of neural transmission. Supplementum · doi:10.1007/978-3-7091-6467-9_15 · Cited by 143

The pool of map kinase associated with microtubules is small but constitutively active.

Morishima‐Kawashima, M., & Kosik, K. S. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.6.893 · Cited by 141

Normal and Pathological Tau Proteins as Factors for Microtubule Assembly

Delacourte, A., & Buée, L. (1997) · International review of cytology · doi:10.1016/s0074-7696(08)62588-7 · Cited by 145

Glucose deprivation elicits neurofibrillary tangle-like antigenic changes in hippocampal neurons: Prevention by NGF and bFGF

Cheng, B., & Mattson, M. P. (1992) · Experimental Neurology · doi:10.1016/0014-4886(92)90120-f · Cited by 137

Glycogen Synthase Kinase-3 Plays a Crucial Role in Tau Exon 10 Splicing and Intranuclear Distribution of SC35

Hernández, F., Pérez, M., Lucas, J. J., Mata, A. M., Bhat, R. V., & Ávila, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311512200 · Cited by 139

Cholesterol‐dependent modulation of tau phosphorylation in cultured neurons

Fan, Q., Yu, W., Senda, T., Yanagisawa, K., & Michikawa, M. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.00063.x · Cited by 136

A New Molecular Link between the Fibrillar and Granulovacuolar Lesions of Alzheimer's Disease

Ghoshal, N., Smiley, J. F., DeMaggio, A. J., Hoekstra, M. F., Cochran, E. J., Binder, L. I., & Kuret, J. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65219-4 · Cited by 137

Cross talk between PI3K-AKT-GSK-3β and PP2A pathways determines tau hyperphosphorylation

Wang, Y., Yang, R., Gu, J., Yin, X., Jin, N., Xie, S., Wang, Y., Chang, H., Qian, W., Shi, J., et al. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.07.035 · Cited by 134

Tau and Axonopathy in Neurodegenerative Disorders

Higuchi, M., Lee, V. M.-Y., & Trojanowski, J. Q. (2002) · NeuroMolecular Medicine · doi:10.1385/nmm:2:2:131 · Cited by 134

A Role for Calcineurin in Alzheimers Disease

Reese, L. C., & Taglialatela, G. (2011) · Current Neuropharmacology · doi:10.2174/157015911798376316 · Cited by 132

Microtubular Proteolysis in Focal Cerebral Ischemia

Pettigrew, L. C., Holtz, M. L., Craddock, S. D., Minger, S. L., Hall, N. C., & Geddes, J. W. (1996) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-199611000-00013 · Cited by 132

Two novel kinases phosphorylate tau and the KSP site of heavy neurofilament subunits in high stoichiometric ratios

Roder, H. M., & Ingram, V. M. (1991) · Journal of Neuroscience · doi:10.1523/jneurosci.11-11-03325.1991 · Cited by 133

A novel tau transcript in cultured human neuroblastoma cells expressing nuclear tau.

Wang, Y., Loomis, P. A., Zinkowski, R. P., & Binder, L. I. (1993) · The Journal of Cell Biology · doi:10.1083/jcb.121.2.257 · Cited by 142

Cell cycle re-entry mediated neurodegeneration and its treatment role in the pathogenesis of Alzheimer's disease

Lee, H., Casadesús, G., Zhu, X., Castellani, R. J., McShea, A., Perry, G. L., Petersen, R. B., Bajić, V., & Smith, M. A. (2008) · Neurochemistry International · doi:10.1016/j.neuint.2008.10.013 · Cited by 136

Conversion of Serine to Aspartate Imitates Phosphorylation-induced Changes in the Structure and Function of Microtubule-associated Protein Tau

Léger, J. G., Kempf, M., Lee, G. S., & Brandt, R. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.13.8441 · Cited by 131

Mapping O-GlcNAc modification sites on tau and generation of a site-specific O-GlcNAc tau antibody

Yuzwa, S. A., Yadav, A. K., Skorobogatko, Y., Clark, T., Vosseller, K., & Vocadlo, D. J. (2011) · Amino Acids · doi:10.1007/s00726-010-0705-1 · Cited by 130

Pathological Tau From Alzheimer’s Brain Induces Site-Specific Hyperphosphorylation and SDS- and Reducing Agent-Resistant Aggregation of Tau in vivo

Miao, J., Shi, R., Li, L., Chen, F., Zhou, Y., Tung, Y. C., Hu, W. H., Gong, C., Iqbal, K., & Liu, F. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00034 · Cited by 125

Alzheimer-specific epitopes of tau represent lipid peroxidation-induced conformations

Liu, Q., Smith, M. A., Ávila, J., DeBernardis, J. F., Kansal, M. M., Takeda, A., Zhu, X., Nunomura, A., Honda, K., Moreira, P. I., et al. (2004) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2004.11.005 · Cited by 129

Traditional Chinese Medicine: Role in Reducing β-Amyloid, Apoptosis, Autophagy, Neuroinflammation, Oxidative Stress, and Mitochondrial Dysfunction of Alzheimer’s Disease

Chen, S.-Y., Gao, Y., Sun, J., Meng, X., Yang, D., Fan, L., Li, X., & Wang, P. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00497 · Cited by 131

The role of amyloid oligomers in neurodegenerative pathologies

Wells, C., Brennan, S. E., Keon, M., & Ooi, L. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.03.113 · Cited by 131

Large-scale Identification of Tubulin-binding Proteins Provides Insight on Subcellular Trafficking, Metabolic Channeling, and Signaling in Plant Cells

Chuong, S. D. X., Good, A. G., Taylor, G. J., Freeman, M. C., Moorhead, G. B. G., & Muench, D. G. (2004) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m400053-mcp200 · Cited by 125

Diverse Distribution and Function of Fibrous Microtubule-Associated Proteins in the Nervous System

Schoenfeld, T. A., & Obar, R. A. (1994) · International review of cytology · doi:10.1016/s0074-7696(08)62631-5 · Cited by 128

Development of disease-modifying drugs for frontotemporal dementia spectrum disorders

Panza, F., Lozupone, M., Seripa, D., Daniele, A., Watling, M., Giannelli, G., & Imbimbo, B. P. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0330-x · Cited by 122

Increased expression and subcellular translocation of the mitogen activated protein kinase kinase and mitogen-activated protein kinase in Alzheimer's disease

Arendt, T., Holzer, M., Grossmann, A., Zedlick, D., & Brückner, M. K. (1995) · Neuroscience · doi:10.1016/0306-4522(95)00146-a · Cited by 123

A novel DYRK1A (Dual specificity tyrosine phosphorylation‐regulated kinase 1A) inhibitor for the treatment of Alzheimer's disease: effect on Tau and amyloid pathologies in vitro

Coutadeur, S., Benyamine, H., Delalonde, L., de Oliveira, C., Leblond, B., Foucourt, A., Besson, T., Casagrande, A.-S., Taverne, T., Girard, A., et al. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.13018 · Cited by 121

NMR Investigation of the Interaction between the Neuronal Protein Tau and the Microtubules

Sillen, A., Barbier, P., Landrieu, I., Lefebvre, S., Wieruszeski, J., Leroy, A., Peyrot, V., & Lippens, G. M. (2007) · Biochemistry · doi:10.1021/bi061920i · Cited by 121

Parkin Phosphorylation and Modulation of Its E3 Ubiquitin Ligase Activity

Yamamoto, A., Friedlein, A., Imai, Y., Takahashi, R., Kahle, P. J., & Haass, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m407724200 · Cited by 121

Functional Implications of Glycogen Synthase Kinase‐3‐Mediated Tau Phosphorylation

Hanger, D. P., & Noble, W. J. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/352805 · Cited by 124

Effects of elevated intracellular calcium levels on the cytoskeleton and tau in cultured human cortical neurons

Mattson, M. P., Engle, M. G., & Rychlik, B. (1991) · Molecular and Chemical Neuropathology · doi:10.1007/bf03159951 · Cited by 118

Therapeutic Approaches to Alzheimer’s Disease Through Modulation of NRF2

Bahn, G., & Jo, D. (2019) · NeuroMolecular Medicine · doi:10.1007/s12017-018-08523-5 · Cited by 118

Tau Ser208 phosphorylation promotes aggregation and reveals neuropathologic diversity in Alzheimer’s disease and other tauopathies

Xia, Y., Prokop, S., Gorion, K.-M. M., Kim, J. D., Sorrentino, Z. A., Bell, B. M., Manaois, A. N., Chakrabarty, P., Davies, P., & Giasson, B. I. (2020) · Acta Neuropathologica Communications · doi:10.1186/s40478-020-00967-w · Cited by 118

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 128

Tau Dephosphorylation at Tau-1 Site Correlates with its Association to Cell Membrane

Arrasate, M., Pérez, M., & Ávila, J. (2000) · Neurochemical Research · doi:10.1023/a:1007583214722 · Cited by 130

Biological activity and pathological implications of misfolded proteins

Bellotti, V., Mangione, P. P., & Stoppini, M. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050348 · Cited by 116

Phospho-Tau Bar Code: Analysis of Phosphoisotypes of Tau and Its Application to Tauopathy

Kimura, T., Sharma, G., Ishiguro, K., & Hisanaga, S. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00044 · Cited by 116

Nicotinamide loaded functionalized solid lipid nanoparticles improves cognition in Alzheimer’s disease animal model by reducing Tau hyperphosphorylation

Vakilinezhad, M. A., Amini, A., Javar, H. A., Zarandi, B. F. B. B., Montaseri, H., & Dinarvand, R. (2018) · DARU Journal of Pharmaceutical Sciences · doi:10.1007/s40199-018-0221-5 · Cited by 115

The regulation of phosphorylation of τ in SY5Y neuroblastoma cells: the role of protein phosphatases

Tanaka, T., Zhong, J., Iqbal, K., Trenkner, E., & Grundke, I. (1998) · FEBS Letters · doi:10.1016/s0014-5793(98)00346-9 · Cited by 113

A Role for Glial Cells in Activity-Dependent Development of the Vertebrate Nervous System

Fields, R. D., & Nelson, P. G. (1992) · International review of neurobiology · doi:10.1016/s0074-7742(08)60098-7 · Cited by 113

Alzheimer disease proteins (A68) share epitopes with tau but show distinct biochemical properties

Ksiezak‐Reding, H., Binder, L. I., & Yen, S.-H. C. (1990) · Journal of Neuroscience Research · doi:10.1002/jnr.490250320 · Cited by 113

Tau biology, tauopathy, traumatic brain injury, and diagnostic challenges

Castellani, R. J., & Perry, G. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-180721 · Cited by 110

Calcineurin is associated with the cytoskeleton of cultured neurons and has a role in the acquisition of polarity.

Ferreira, A., Kincaid, R., & Kosik, K. S. (1993) · Molecular Biology of the Cell · doi:10.1091/mbc.4.12.1225 · Cited by 110

Spreading of tau pathology in A lzheimer's disease by cell‐to‐cell transmission

Mohamed, N., Herrou, T., Plouffe, V., Piperno, N., & Leclerc, N. M. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12229 · Cited by 116

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Anwar, S., Ziu, I., & Martić, S. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.07.090

Differential effect of phosphorylation and substrate modulation on tau's ability to promote microtubule growth and nucleation.

Brandt, R., Lee, G. S., Teplow, D. B., Shalloway, D. I., & Abdel-Ghany, M. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)32639-x · Cited by 90

Growth factor stimulation triggers apoptotic cell death in mature oligodendrocytes

Muir, D., & Compston, D. A. S. (1996) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19960401)44:1 · Cited by 68

Influence of Phosphorylation on the Pathological Conformation of Human Microtubule Associated Protein Tau

Chinnathambi, S. (2012) · DZNE Pub

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Fan, X., Truong, J. B., Okada, K., Lin, H., Ori-McKenney, K. M., & McKenney, R. J. (2026) · Communications Biology · doi:10.1038/s42003-026-10797-6 · Cited by 10