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

Is tau ready for admission to the prion club?

Hall, G. F., & Patuto, B. A. (2012) · Prion · doi:10.4161/pri.19912 · Cited by 43

Kinase–Kinase Interaction and Modulation of Tau Phosphorylation

Hashiguchi, M., & Hashiguchi, T. (2012) · International review of cytology · doi:10.1016/b978-0-12-405210-9.00004-7 · Cited by 44

Developing pharmacological therapies for Alzheimer disease

Iqbal, K., & Grundke, I. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7221-9 · Cited by 42

Pathological glial tau accumulations in neurodegenerative disease: review and case report

Berry, R. W., Quinn, B., Johnson, N., Cochran, E. J., Ghoshal, N., & Binder, L. I. (2001) · Neurochemistry International · doi:10.1016/s0197-0186(01)00054-7 · Cited by 43

An Analysis of an Axonal Gradient of Phosphorylated MAP 1B in Cultured Rat Sensory Neurons

Bush, M. S., Goold, R., Moya, F., & Gordon‐Weeks, P. R. (1996) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.1996.tb01208.x · Cited by 42

Pseudohyperphosphorylation Has Differential Effects on Polymerization and Function of Tau Isoforms

Combs, B., Voss, K., & Gamblin, T. C. (2011) · Biochemistry · doi:10.1021/bi2010569 · Cited by 41

Chaperone-dependent Neurodegeneration: A Molecular Perspective on Therapeutic Intervention

Kishinevsky, A. C. S., & Lou, J. K. I. W. (2013) · Journal of Alzheimer’s Disease & Parkinsonism · doi:10.4172/2161-0460.s10-007 · Cited by 42

Phosphoproteome profiling of substantia nigra and cortex regions of Alzheimer’s disease patients

Zahid, S., Oellerich, M., Asif, A. R., & Ahmed, N. (2012) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2012.07737.x · Cited by 41

Regulation of Phosphorylation of tau by Protein Kinases in Rat Brain

Sengupta, A., Grundke, I., & Iqbal, K. (2006) · Neurochemical Research · doi:10.1007/s11064-006-9205-9 · Cited by 41

Diabetes synergistically exacerbates poststroke dementia and tau abnormality in brain

Zhang, T., Pan, B., Sun, G., Sun, X., & Sun, F. (2010) · Neurochemistry International · doi:10.1016/j.neuint.2010.04.003 · Cited by 41

The Microtubule Binding of Tau and High Molecular Weight Tau in Apoptotic PC12 Cells Is Impaired because of Altered Phosphorylation

Davis, P. K., & Johnson, G. V. W. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35686 · Cited by 41

Microtubules in Tip Growth Systems

Derksen, J. J. L., & Emons, A. M. C. (1990) · Elsevier eBooks · doi:10.1016/b978-0-12-335845-5.50009-4 · Cited by 41

Ferroptosis promotes microtubule-associated protein tau aggregation via GSK-3β activation and proteasome inhibition

Wang, S., Jiang, Y. X., Liu, Y., Liu, Q., Sun, H., Mei, M., & Liao, X. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02731-8 · Cited by 40

Dephosphorylation of tau during transient forebrain ischemia in the rat

Shackelford, D. A., & Yeh, R. Y. (1998) · Molecular and Chemical Neuropathology · doi:10.1007/bf02815073 · Cited by 40

Exploring the interplay between fibrillization and amorphous aggregation channels on the energy landscapes of tau repeat isoforms

Chen, X., Chen, M., Schafer, N. P., & Wolynes, P. G. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1921702117 · Cited by 40

Adenosine receptor signalling in Alzheimer’s disease

Trinh, P. N. H., Baltos, J., Hellyer, S. D., May, L. T., & Gregory, K. J. (2022) · Purinergic Signalling · doi:10.1007/s11302-022-09883-1 · Cited by 43

Effects of progesterone and its reduced metabolites, dihydroprogesterone and tetrahydroprogesterone, on the expression and phosphorylation of glycogen synthase kinase‐3 and the microtubule‐associated protein Tau in the rat cerebellum

Guerra‐Araiza, C., Amorim, M. A. R., Camacho‐Arroyo, I., & García‐Segura, L. M. (2007) · Developmental Neurobiology · doi:10.1002/dneu.20383 · Cited by 40

Modulation of PHF-like tau phosphorylation in cultured neurones and transfected cells

Anderton, B. H., Brion, J., Couck, A. M., Davis, D. R., Gallo, J., Hanger, D. P., Ladhani, K., Latimer, D. A., Lewis, C., Lovestone, S., et al. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(94)00160-3 · Cited by 41

Regional distribution and biochemical characteristics of high molecular weight tau in the nervous system

Taleghany, N., & Oblinger, M. (1992) · Journal of Neuroscience Research · doi:10.1002/jnr.490330209 · Cited by 40

Co-ordinate regulation of the cytoskeleton in 3T3 cells overexpressing thymosin-β4

Golla, R., Philp, N. J., Safer, D., Chintapalli, J., Hoffman, R. K., Collins, L., & Nachmias, V. T. (1997) · Cell Motility and the Cytoskeleton · doi:10.1002/(sici)1097-0169(1997)38:2 · Cited by 46

PKR kinase directly regulates tau expression and Alzheimer's disease‐related tau phosphorylation

Reimer, L., Betzer, C., Kofoed, R. H., Volbracht, C., Fog, K., Kurhade, C., Nilsson, E., Överby, A. K., & Jensen, P. H. (2020) · Brain Pathology · doi:10.1111/bpa.12883 · Cited by 39

Compression Alters Kinase and Phosphatase Activity and Tau and MAP2 Phosphorylation Transiently while Inducing the Fast Adaptive Dendritic Remodeling of Underlying Cortical Neurons

Chen, L.-J., Wang, Y., & Tseng, G. (2010) · Journal of Neurotrauma · doi:10.1089/neu.2010.1308 · Cited by 39

CELL MOTILITY IN THE RETINA

Burnside, B., & Dearry, A. (1986) · Elsevier eBooks · doi:10.1016/b978-0-12-044275-1.50011-9 · Cited by 39

Expression of Alzheimer-like pathological human tau induces a behavioral motor and olfactory learning deficit in Drosophila melanogaster

Beharry, C., Alaniz, M. E., & Alonso, A. D. C. (2013) · Journal of Alzheimer's Disease · doi:10.3233/jad-130617 · Cited by 39

Tau phosphorylation at threonine‐175 leads to fibril formation and enhanced cell death: implications for amyotrophic lateral sclerosis with cognitive impairment

Gohar, M., Yang, W., Strong, W., Volkening, K., Leystra‐Lantz, C., & Strong, M. J. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05791.x · Cited by 38

Tau phosphorylation and assembly

Gómez‐Ramos, A., Smith, M. A., Perry, G. L., & Ávila, J. (2004) · Acta Neurobiologiae Experimentalis · doi:10.55782/ane-2004-1489 · Cited by 38

Molecular Mechanism of Alzheimer's Neurofibrillary Degeneration and Therapeutic Interventiona

Iqbal, K., & Grundke, I. (1996) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1996.tb34411.x · Cited by 38

Microtubule destruction induces tau liberation and its subsequent phosphorylation

Miyasaka, T., Sato, S., Tatebayashi, Y., & Takashima, A. (2010) · FEBS Letters · doi:10.1016/j.febslet.2010.06.014 · Cited by 41

GSK-3 dependent phosphoepitopes recognized by PHF-1 and AT-8 antibodies are present in different tau isoforms

HERNANDEZ, F. (2003) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2003.04.002 · Cited by 41

Neuroprotective signaling by hydrogen sulfide and its dysregulation in Alzheimer's disease

Paul, B. D., & Pieper, A. A. (2024) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2024.102511 · Cited by 38

Post-translational modifications in neurodegeneration

Didonna, A., & Benetti, F. (2015) · AIMS Biophysics · doi:10.3934/biophy.2016.1.27 · Cited by 36

Neurophysiological assessment of neural network plasticity and connectivity: Progress towards early functional biomarkers for disease interception therapies in Alzheimer’s disease

Walsh, C., Drinkenburg, W. H. I. M., & Ahnaou, A. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.12.020 · Cited by 37

Frontrunner in Translation: Progressive Supranuclear Palsy

Shoeibi, A., Olfati, N., & Litvan, I. (2019) · Frontiers in Neurology · doi:10.3389/fneur.2019.01125 · Cited by 39

Dendritic/Post-synaptic Tau and Early Pathology of Alzheimer’s Disease

Yin, X., Zhao, C., Qiu, Y., Zhou, Z., Bao, J., & Qian, W. (2021) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2021.671779 · Cited by 41

Is Tau Aggregation Toxic or Protective: A Sensible Question in the Absence of Sensitive Methods?

Götz, J., Ittner, L. M., Fändrich, M., & Schönrock, N. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14410 · Cited by 37

Co-localization of hyperphosphorylated tau and caspases in the brainstem of Alzheimer’s disease patients

Wai, M. S. M., Liang, Y., Shi, C., Cho, E. Y. P., Kung, H., & Yew, D. T. W. (2008) · Biogerontology · doi:10.1007/s10522-008-9189-8 · Cited by 37

A brief history of tau: the evolving view of the microtubule-associated protein tau in neurodegenerative diseases

Lace, G., Wharton, S. B., & Ince, P. G. (2007) · Clinical Neuropathology · doi:10.5414/npp26043 · Cited by 37

Regulation of the phosphoinositide‐3 kinase and mitogen‐activated protein kinase signaling pathways by progesterone and its reduced metabolites in the rat brain

Guerra‐Araiza, C., Amorim, M. A. R., Pinto‐Almazán, R., González‐Arenas, A., Campos, M. G., & García‐Segura, L. M. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21848 · Cited by 37

Hyperphosphorylation at serine 199/202 of tau factor in the gerbil hippocampus after transient forebrain ischemia

Morioka, M., Kawano, T., Yano, S., Kai, Y., Tsuiki, H., Yoshinaga, Y., Matsumoto, J., Maeda, T., Hamada, J.-I., Yamamoto, H., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.06.096 · Cited by 37

Characterization of a PC12 cell sub-clone (PC12-c41) with enhanced neurite outgrowth capacity: implications for a modulatory role of high molecular weight tau in neuritogenesis

Teng, K. K., Georgieff, I. S., Aletta, J. M., Nunez, J., Shelanski, M. L., & Greene, L. A. (1993) · Journal of Cell Science · doi:10.1242/jcs.106.2.611 · Cited by 37

A modified form of microtubule-associated tau protein is the main component of paired helical filaments

Nieto, A., Correas, I., de Garcini, E. M., & Ávila, J. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(88)90190-8 · Cited by 37

Role of Microglia in Regulating Cholesterol and Tau Pathology in Alzheimer’s Disease

Nanjundaiah, S., Chidambaram, H., Chandrashekar, M., & Chinnathambi, S. (2021) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-020-00883-6 · Cited by 36

Cellular and molecular mechanisms of pathological tau phosphorylation in traumatic brain injury: implications for chronic traumatic encephalopathy

Donison, N. S., Palik, J., Volkening, K., & Strong, M. J. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00842-z · Cited by 42

Pseudo-acetylation of multiple sites on human Tau proteins alters Tau phosphorylation and microtubule binding, and ameliorates amyloid beta toxicity

Gorsky, M. K., Burnouf, S., Sofola-Adesakin, O., Dols, J., Augustin, H., Weigelt, C. M., Grönke, S., & Partridge, L. (2017) · Scientific Reports · doi:10.1038/s41598-017-10225-0 · Cited by 36

Aducanumab and Its Effects on Tau Pathology: Is This the Turning Point of Amyloid Hypothesis?

Silvestro, S., Valeri, A., & Mazzon, E. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23042011 · Cited by 37

Schisantherin B ameliorates Aβ 1–42 -induced cognitive decline via restoration of GLT-1 in a mouse model of Alzheimer's disease

Xu, M., Dong, Y., Wan, S., Yan, T., Cao, J., Wu, L., Bi, K., & Jia, Y. (2016) · Physiology & Behavior · doi:10.1016/j.physbeh.2016.09.018 · Cited by 36

Tau phosphorylation during apoptosis of human SH-SY5Y neuroblastoma cells

Mookherjee, P., & Johnson, G. V. W. (2001) · Brain Research · doi:10.1016/s0006-8993(01)03074-8 · Cited by 36

Characterization of a 100‐kDa heat‐stable microtubule‐associated protein from higher plants

Vantard, M., PETER, C., Fellous, A., Schellenbaum, P., & Lambert, A. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18687.x · Cited by 36

Phosphorylation characteristics of the A68 protein in Alzheimer's disease

Vincent, I. J., & Davies, P. (1990) · Brain Research · doi:10.1016/0006-8993(90)90765-4 · Cited by 36

Expression of a developmentally regulated, phosphorylated isoform of microtubule-associated protein 1B in regenerating axons of the sciatic nerve

Bush, M. S., Tonge, D., Woolf, C. J., & Gordon‐Weeks, P. R. (1996) · Neuroscience · doi:10.1016/0306-4522(96)00078-4 · Cited by 36

The expression of phosphorylated and non-phosphorylated forms of MAP5 in the amphibian CNS

Viereck, C., & Matus, A. I. (1990) · Brain Research · doi:10.1016/0006-8993(90)90404-y · Cited by 36

Why should stationary plant cells have such dynamic microtubules?

Lloyd, C. W. (1994) · Molecular Biology of the Cell · doi:10.1091/mbc.5.12.1277 · Cited by 36

Stem Cell Therapy: A Prospective Treatment for Alzheimer's Disease

Lee, J. H., Oh, I., & Lim, H. K. (2016) · Psychiatry Investigation · doi:10.4306/pi.2016.13.6.583 · Cited by 35

Inhibition of 14-3-3/Tau by Hybrid Small-Molecule Peptides Operating via Two Different Binding Modes

Andrei, S. A., Meijer, F. A., Neves, J. F., Brunsveld, L., Landrieu, I., Ottmann, C., & Milroy, L. ‐. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00118 · Cited by 35

Pathological Alterations of Tau in Alzheimer’s Disease and 3xTg-AD Mouse Brains

Li, L., Jiang, Y., Hu, W. H., Tung, Y. C., Dai, C., Chu, D., Gong, C., Iqbal, K., & Liu, F. (2019) · Molecular Neurobiology · doi:10.1007/s12035-019-1507-4 · Cited by 36

Usnic acid derivatives as tau-aggregation and neuroinflammation inhibitors

Shi, C., Peng, W., Zhao, J., Yang, H., Qu, L., Wang, C., Kong, L., & Wang, X. (2019) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2019.111961 · Cited by 36

How it all Started: Tau and Protein Phosphatase 2A

Liu, C., & Götz, J. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130503 · Cited by 38

Serotonin‐induced activation of the network for locomotion in adult spinal rats

Feraboli‐Lohnherr, D., Barthe, J., & Orsal, D. (1999) · Journal of Neuroscience Research · doi:10.1002/(sici)1097-4547(19990101)55:1 · Cited by 106

Neural crest specification by noncanonical Wnt signaling and PAR-1

Ossipova, O., & Sokol, S. Y. (2011) · Development · doi:10.1242/dev.067280 · Cited by 36

Heterogeneity of tau proteins during mouse brain development and differentiation of cultured neurons

Larcher, J. C., Boucher, D., Ginzburg, I., Gros, F., & Denoulet, P. (1992) · Developmental Biology · doi:10.1016/0012-1606(92)90059-p · Cited by 35

Deciphering Alzheimer's disease: the pace quickens

Selkoe, D. J. (1987) · Trends in Neurosciences · doi:10.1016/0166-2236(87)90140-8 · Cited by 35

Expression and phosphorylation of a three-repeat isoform of tau in transfected non-neuronal cells

Gallo, J., Hanger, D. P., Twist, E. C., Kosik, K. S., & Anderton, B. H. (1992) · Biochemical Journal · doi:10.1042/bj2860399 · Cited by 35

TBK1 interacts with tau and enhances neurodegeneration in tauopathy

Abreha, M. H., Ojelade, S. A., Dammer, E. B., McEachin, Z. T., Duong, D. M., Gearing, M., Bassell, G. J., Lah, J. J., Levey, A. I., Shulman, J. M., et al. (2021) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2021.100760 · Cited by 33

Axonal plasticity in response to active forces generated through magnetic nano-pulling

Falconieri, A., Vincentiis, S. D., Cappello, V., Convertino, D., Das, R., Ghignoli, S., Figoli, S., Luin, S., Català-Castro, F., Marchetti, L., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111912 · Cited by 35

The new indirubin derivative inhibitors of glycogen synthase kinase‐3, 6‐BIDECO and 6‐BIMYEO, prevent tau phosphorylation and apoptosis induced by the inhibition of protein phosphatase‐2A by okadaic acid in cultured neurons

Martin, L., Magnaudeix, A., Wilson, C. M., Yardin, C., & Terro, F. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22723 · Cited by 34

Sustained high levels of neuroprotective, high molecular weight, phosphorylated tau in the longest-lived rodent

Orr, M. E., Garbarino, V. R., Salinas, A., & Buffenstein, R. (2014) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2014.12.004 · Cited by 34

Alteration in neurofilament axonal transport in the sciatic nerve of the diisopropyl phosphorofluoridate (DFP)-treated hen

Gupta, R. P., Abdel-Rahman, A. A., Wilmarth, K. W., & Abou-Donia, M. B. (1997) · Biochemical Pharmacology · doi:10.1016/s0006-2952(97)00002-6 · Cited by 34

Site-specific regulation of Alzheimer-like tau phosphorylation in living neurons

Burack, M. A., & Halpain, S. (1996) · Neuroscience · doi:10.1016/0306-4522(95)00546-3 · Cited by 36

The Amyloid Peptide and Its Precursor in Alzheimer's Disease

Octave, J. N. (1995) · Reviews in the Neurosciences · doi:10.1515/revneuro.1995.6.4.287 · Cited by 34

Ablation of C/EBP homologous protein attenuates renal fibrosis after ureteral obstruction by reducing autophagy and microtubule disruption

Noh, M. R., Woo, C.-H., Park, M.-J., In Kim, J., & Park, K. M. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.02.001 · Cited by 33

MicroRNAs and MAPKs: Evidence of These Molecular Interactions in Alzheimer’s Disease

Raffaele, I., Silvestro, S., & Mazzon, E. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054736 · Cited by 33

GSK-3β phosphorylation of functionally distinct tau isoforms has differential, but mild effects

Voss, K., & Gamblin, T. C. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-18 · Cited by 33

Modification of the Drosophila model of in vivo Tau toxicity reveals protective phosphorylation by GSK3β

Povellato, G., Tuxworth, R. I., Hanger, D. P., & Tear, G. (2013) · Biology Open · doi:10.1242/bio.20136692 · Cited by 35

Fluorescence Lifetime Imaging of p-tau Protein in Single Neuron with a Highly Selective Fluorescent Probe

Ge, L., & Tian, Y. (2019) · Analytical Chemistry · doi:10.1021/acs.analchem.8b03992 · Cited by 34

Acetyl‐ L ‐Carnitine ameliorates spatial memory deficits induced by inhibition of phosphoinositol‐3 kinase and protein kinase C

Jiang, X., Tian, Q., Wang, Y., Zhou, X., Xie, J., Wang, J., & Zhu, L. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07355.x · Cited by 33

Tau and S100B Proteins as Biochemical Markers of Bilirubin-Induced Neurotoxicity in Term Neonates

Okumuş, N., Türkyılmaz, C., Önal, E. E., Atalay, Y., Serdaroğlu, A., Elbeğ, Ş., Koç, E., Deda, G., Cansu, A., & Gündüz, B. (2008) · Pediatric Neurology · doi:10.1016/j.pediatrneurol.2008.07.004 · Cited by 33

Effect of chronic administration of estradiol, progesterone, and tibolone on the expression and phosphorylation of glycogen synthase kinase‐3β and the microtubule‐associated protein tau in the hippocampus and cerebellum of female rat

Pinto‐Almazán, R., Calzada‐Mendoza, C. C., Campos-Lara, M. G., & Guerra‐Araiza, C. (2011) · Journal of Neuroscience Research · doi:10.1002/jnr.22808 · Cited by 35

Possible role of enhanced microtubule phosphorylation in dichlorvos induced delayed neurotoxicity in rat

Choudhary, S., Joshi, K., & Gill, K. D. (2001) · Brain Research · doi:10.1016/s0006-8993(00)03222-4 · Cited by 33

Examination of phosphorylated tau protein as a PHF-precursor at early stage alzheimer's disease

Lai, R. Y. K., Gertz, H. N.-J., Wischik, D., Xuereb, J. H., Mukaetova-Ladinska, E. B., Harrington, C. R., Edwards, P. C., Mena, R., Paykel, E. S., Brayne, C., et al. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00041-c · Cited by 33

Differential distribution of tau proteins in developing cat cerebellum

Riederer, B. M., & Binder, L. I. (1994) · Brain Research Bulletin · doi:10.1016/0361-9230(94)90245-3 · Cited by 33

The link between periodontitis and Alzheimer's disease – emerging clinical evidence

Wu, D. T. S., Cho, Y. W., Spalti, M. D., Bishara, M., & Nguyen, T. T. H. (2022) · Dentistry Review · doi:10.1016/j.dentre.2022.100062 · Cited by 38

In vivo and in vitro effects of diisopropyl phosphorofluoridate (DFP) on the rate of hen brain tubulin polymerization

Gupta, R. P., & Abou-Donia, M. B. (1994) · Neurochemical Research · doi:10.1007/bf00967321 · Cited by 32

Abortive oncogeny and cell cycle-mediated events in Alzheimer disease

Raina, A. K., Zhu, X., Monteiro, M. J., Takeda, A., & Smith, M. A. (2000) · Springer eBooks · doi:10.1007/978-1-4615-4253-7_20 · Cited by 32

Alzheimer neurofibrillary tangles contain 2.1 nm filaments structurally identical to the microtubule-associated protein τ: a high-resolution transmission electron microscope study of tangles and senile plaque core amyloid

Ruben, G. C., Iqbal, K., Wisniewski, H. M., Johnson, J. E., & Grundke, I. (1992) · Brain Research · doi:10.1016/0006-8993(92)91092-s · Cited by 32

Pathological Tau proteins of Alzheimer's disease as a biochemical marker of neurofibrillary degeneration

Delacourte, A. (1994) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(94)90174-0 · Cited by 33

Aristolactam BIII, a naturally derived DYRK1A inhibitor, rescues Down syndrome-related phenotypes

Choi, M., Kim, A., Ham, Y., Lee, J., Kim, D., Yang, A., Jo, M. J., Yoon, E., Heo, J., Han, S., et al. (2021) · Phytomedicine · doi:10.1016/j.phymed.2021.153695 · Cited by 34

Disruption of tubulin-alpha4a polyglutamylation prevents aggregation of hyper-phosphorylated tau and microglia activation in mice

Hausrat, T. J., Janiesch, P. C., Breiden, P., Lutz, D., Hoffmeister‐Ullerich, S., Hermans‐Borgmeyer, I., Failla, A. V., & Kneussel, M. (2022) · Nature Communications · doi:10.1038/s41467-022-31776-5 · Cited by 29

Human fetal tau protein isoform: Possibilities for Alzheimer's disease treatment

Milošević, N. J., Petrović, D., Sedmak, G., Vukšić, M., Hof, P. R., & Šimić, G. (2012) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2012.05.001 · Cited by 34

A Tangled Web – Tau and Sporadic Parkinson's Disease

Wray, S., & Lewis, P. A. (2010) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2010.00150 · Cited by 31

Differential phosphorylation of some proteins of the neuronal cytoskeleton during brain development

Riederer, B. M. (1992) · The Histochemical Journal · doi:10.1007/bf01046350 · Cited by 31

Book Review: Is Alzheimer’s Disease a Mitochondrial Disorder?

Cash, A., Perry, G. L., Ogawa, O., Raina, A. K., Zhu, X., & Smith, M. A. (2002) · The Neuroscientist · doi:10.1177/107385802236968 · Cited by 32

LRRK2 Facilitates tau Phosphorylation through Strong Interaction with tau and cdk5

Shanley, M. R., Hawley, D., Leung, S., Zaidi, N. F., Dave, R., Schlosser, K. A., Bandopadhyay, R., Gerber, S. A., & Liu, M. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00326 · Cited by 31

Specific ion channels contribute to key elements of pathology during secondary degeneration following neurotrauma

Doig, R. O., Chiha, W., Giacci, M. K., Yates, N. J., Bartlett, C. A., Smith, N. M., Hodgetts, S. I., Harvey, A. R., & Fitzgerald, M. (2017) · BMC Neuroscience · doi:10.1186/s12868-017-0380-1 · Cited by 30

Investigation of therapeutic potential of cerium oxide nanoparticles in Alzheimer’s disease using transgenic Drosophila

Sundararajan, V., Venkatasubbu, G. D., & Mohideen, S. S. (2021) · 3 Biotech · doi:10.1007/s13205-021-02706-x · Cited by 30

Use of Magnetization Transfer Contrast MRI to Detect Early Molecular Pathology in Alzheimer's Disease

Pérez‐Torres, C. J., Reynolds, J. O., & Pautler, R. G. (2013) · Magnetic Resonance in Medicine · doi:10.1002/mrm.24665 · Cited by 30

GSK3β polymorphisms, MAPT H1 haplotype and Parkinson's disease in a Greek cohort

Kalinderi, K., Fidani, L., Katsarou, Z., Clarimón, J., Bostantjopoulou, S., & Kotsis, A. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.05.007 · Cited by 30

A putative role for cell cycle‐related proteins in microtubule‐based neuroplasticity

Schmetsdorf, S., Arnold, E., Holzer, M., Arendt, T., & Gärtner, U. (2009) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2009.06661.x · Cited by 30

The HSP40 family chaperone isoform DNAJB6b prevents neuronal cells from tau aggregation

Chang, Y.-L., Yang, C.-C., Huang, Y.-Y., Chen, Y., Yang, C., Liao, C.-Y., Li, H., Wu, C.-S. P., Lin, C., & Teng, S. (2023) · BMC Biology · doi:10.1186/s12915-023-01798-6 · Cited by 28

Nutraceutical based SIRT3 activators as therapeutic targets in Alzheimer's disease

Govindarajulu, M., Ramesh, S., Neel, L. T., Fabbrini, M., Buabeid, M. A., Fujihashi, A., Dwyer, D., Lynd, T. O., Shah, K., Mohanakumar, K. P., et al. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.104958 · Cited by 31

Overexpression of tau protein in COS-1 cells results in the stabilization of centrosome-independent microtubules and extension of cytoplasmic processes

de Garcini, E. M., de la Luna, S., Domínguez, J. E., & Ávila, J. (1994) · Molecular and Cellular Biochemistry · doi:10.1007/bf01457399 · Cited by 29

P4‐268: ROLE OF TAU PHOSPHORYLATION ON MICROTUBULE POLYMERIZATION

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

A pathological phosphorylation pattern enhances tau cooperativity on microtubules and facilitates tau filament assembly

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