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

Role of miRNAs in Alzheimer’s Disease and Possible Fields of Application

Silvestro, S., Bramanti, P., & Mazzon, E. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20163979 · Cited by 113

Proteotoxic stress and the ubiquitin proteasome system

Kandel, R., Jung, J., & Neal, S. E. (2023) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2023.08.002 · Cited by 124

Alzheimer disease therapeutics: Focus on the disease and not just plaques and tangles

Iqbal, K., Liu, F., & Gong, C. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.002 · Cited by 114

Regional conformational change involving phosphorylation of tau protein at the Thr231, precedes the structural change detected by Alz-50 antibody in Alzheimer's disease

Luna‐Muñoz, J., García‐Sierra, F., Falcón, V., Menéndez, I., Chávez-Macías, L., & Mena, R. (2005) · Journal of Alzheimer s Disease · doi:10.3233/jad-2005-8104 · Cited by 113

A68 proteins in Alzheimer's disease are composed of several tau isoforms in a phosphorylated state which affects their electrophoretic mobilities

Brion, J., Hanger, D. P., Couck, A. M., & Anderton, B. H. (1991) · Biochemical Journal · doi:10.1042/bj2790831 · Cited by 109

The effect of insomnia on development of Alzheimer’s disease

Sadeghmousavi, S., Eskian, M., Rahmani, F., & Rezaei, N. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01960-9 · Cited by 122

Ubiquitination and abnormal phosphorylation of paired helical filaments in Alzheimer's disease

Iqbal, K., & Grundke, I. (1991) · Molecular Neurobiology · doi:10.1007/bf02935561 · Cited by 108

Immunochemical evidence that fragments of phosphorylated MAP5 (MAP1B) are bound to neurofibrillary tangles in Alzheimer's disease

Hasegawa, M., Arai, T., & Ihara, Y. (1990) · Neuron · doi:10.1016/0896-6273(90)90144-5 · Cited by 107

Role of Microglial Cells in Alzheimer’s Disease Tau Propagation

Španić, E., Horvat, L. L., Hof, P. R., & Šimić, G. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00271 · Cited by 112

Dynamic Regulation of Expression and Phosphorylation of Tau by Fibroblast Growth Factor-2 In Neural Progenitor Cells from Adult Rat Hippocampus

Tatebayashi, Y., Iqbal, K., & Grundke, I. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-13-05245.1999 · Cited by 106

Microheterogeneity of Micro tubule‐Associated τ Proteins Is Due to Differences in Phosphorylation

Butler, M., & Shelanski, M. L. (1986) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1986.tb00788.x · Cited by 106

Amyloid β-Exposed Human Astrocytes Overproduce Phospho-Tau and Overrelease It within Exosomes, Effects Suppressed by Calcilytic NPS 2143—Further Implications for Alzheimer's Therapy

Chiarini, A., Armato, U., Gardenal, E., Gui, L., & Prà, I. D. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00217 · Cited by 109

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

Inhibition of PP‐2A upregulates CaMKII in rat forebrain and induces hyperphosphorylation of tau at Ser 262/356

Bennecib, M., Gong, C., Grundke, I., & Iqbal, K. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02127-5 · Cited by 109

The cell cycle in Alzheimer disease: A unique target for neuropharmacology

Webber, K. M., Raina, A. K., Marlatt, M. W., Zhu, X., Prat, M. I., Morelli, L., Casadesús, G., Perry, G. L., & Smith, M. A. (2005) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2005.03.024 · Cited by 104

Alzheimer’s Disease: Mechanism and Approach to Cell Therapy

Amemori, T., Jendelová, P., Růžička, J., Urdzíková, L. M., & Syková, E. (2015) · International Journal of Molecular Sciences · doi:10.3390/ijms161125961 · Cited by 110

Prion-like Spreading in Tauopathies

Ayers, J. I., Giasson, B. I., & Borchelt, D. (2017) · Biological Psychiatry · doi:10.1016/j.biopsych.2017.04.003 · Cited by 106

Microbial Infections Are a Risk Factor for Neurodegenerative Diseases

Lotz, S. K., Blackhurst, B. M., Reagin, K. L., & Funk, K. E. (2021) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2021.691136 · Cited by 100

Respective roles of neurofilaments, microtubules, MAP1B, and tau in neurite outgrowth and stabilization.

Shea, T. B., & Beermann, M. L. (1994) · Molecular Biology of the Cell · doi:10.1091/mbc.5.8.863 · Cited by 101

PIN1 promoter polymorphisms are associated with Alzheimer's disease

Segat, L., Pontillo, A., Annoni, G., Trabattoni, D., Vergani, C., Clerici, M., Arosio, B., & Crovella, S. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.11.009 · Cited by 100

Binding of pp170 to microtubules is regulated by phosphorylation.

Rickard, J. E., & Kreis, T. E. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47414-0 · Cited by 100

Microtubule stabilization by assembly‐promoting microtubule‐associated proteins: A repeat performance

Chapin, S. J., & Bulinski, J. C. (1992) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.970230403 · Cited by 100

Tau phosphorylation in transgenic mice expressing glycogen synthase kinase-3β transgenes

Brownlees, J., Irving, N. G., Brion, J., Gibb, B. J. M., Wagner, U., Woodgett, J. R., & Miller, C. C. J. (1997) · Neuroreport · doi:10.1097/00001756-199710200-00013 · Cited by 99

Tau as a Therapeutic Target for Alzheimers Disease

Boutajangout, A., Sigurdsson, E. M., & Krishnamurthy, P. K. (2011) · Current Alzheimer Research · doi:10.2174/156720511796717195 · Cited by 102

Aging with alcohol-related brain damage: Critical brain circuits associated with cognitive dysfunction

Nunes, P. T., Kipp, B. T., Reitz, N. L., & Savage, L. M. (2019) · International review of neurobiology · doi:10.1016/bs.irn.2019.09.002 · Cited by 103

Tau gene expression in rat sensory neurons during development and regeneration

Oblinger, M., Argasinski, A., Wong, J., & Kosik, K. S. (1991) · Journal of Neuroscience · doi:10.1523/jneurosci.11-08-02453.1991 · Cited by 98

Short and Long Term Behavioral and Pathological Changes in a Novel Rodent Model of Repetitive Mild Traumatic Brain Injury

McAteer, K. M., Corrigan, F., Thornton, E., Turner, R. J., & Vink, R. (2016) · PLoS ONE · doi:10.1371/journal.pone.0160220 · Cited by 100

Microtubule-binding proteins from carrot

Cyr, R. J., & Palevitz, B. A. (1989) · Planta · doi:10.1007/bf00392813 · Cited by 97

Anesthesia and tau pathology

Whittington, R. A., Bretteville, A., Dickler, M., & Planel, E. (2013) · Progress in Neuro-Psychopharmacology and Biological Psychiatry · doi:10.1016/j.pnpbp.2013.03.004 · Cited by 101

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

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

PHF‐tau from Alzheimer's brain comprises four species on SDS‐PAGE which can be mimicked by in vitro phosphorylation of human brain tau by glycogen synthase kinase‐3β

Mulot, S., Hughes, K., Woodgett, J. R., Anderton, B. H., & Hanger, D. P. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00702-0 · Cited by 96

Alz-50 recognizes a phosphorylated epitope of tau protein

Ueda, K., Masliah, E., Saitoh, T., Bakalis, S., Scoble, H. A., & Kosik, K. S. (1990) · Journal of Neuroscience · doi:10.1523/jneurosci.10-10-03295.1990 · Cited by 96

Hypothesis: microtubules, a key to Alzheimer disease

Matsuyama, S. S., & Jarvik, L. F. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.20.8152 · Cited by 95

Does neuroinflammation drive the relationship between tau hyperphosphorylation and dementia development following traumatic brain injury?

Collins-Praino, L. E., & Corrigan, F. (2017) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2016.09.027 · Cited by 95

Regional expression of the MAPT gene is associated with loss of hubs in brain networks and cognitive impairment in Parkinson disease and progressive supranuclear palsy

Rittman, T., Rubinov, M., Vértes, P. E., Patel, A. X., Ginestet, C. E., Ghosh, B. C. P., Barker, R. A., Spillantini, M. G., Bullmore, E. T., & Rowe, J. B. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.09.001 · Cited by 94

Coupling of Mammalian Target of Rapamycin with Phosphoinositide 3-Kinase Signaling Pathway Regulates Protein Phosphatase 2A- and Glycogen Synthase Kinase-3β-dependent Phosphorylation of Tau

Meske, V., Albert, F., & Ohm, T. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704292200 · Cited by 95

The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer’s Disease

Sulistio, Y. A., & Heese, K. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-9063-4 · Cited by 93

Tau downregulates BDNF expression in animal and cellular models of Alzheimer's disease

Rosa, E., Mahendram, S., Ke, Y. D., Ittner, L. M., Ginsberg, S. D., & Fahnestock, M. L. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.08.020 · Cited by 92

Hirano bodies contain tau protein

Galloway, P. G., Perry, G. L., Kosik, K. S., & Gambetti, P. L. (1987) · Brain Research · doi:10.1016/0006-8993(87)90071-0 · Cited by 93

Evidence of Tau Hyperphosphorylation and Dystrophic Microglia in the Common Marmoset

Rodríguez-Callejas, J. D., Fuchs, E., & Perez‐Cruz, C. (2016) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2016.00315 · Cited by 94

Immunochemical and biochemical characterization of tau proteins in normal and Alzheimer's disease brains with Alz 50 and Tau-1.

Ksiȩżak-Reding, H., Binder, L. I., & Yen, S. H. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68426-1 · Cited by 92

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 104

Small molecule therapeutics for tauopathy in Alzheimer’s disease: Walking on the path of most resistance

Wang, L., Bharti, Kumar, R., Pavlov, P. F., & Winblad, B. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112915 · Cited by 92

Association of Tau Protein with Microtubules in Living Cells

Drubin, D. G., KOBAYASHI, S., & Kirschner, M. W. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38398.x · Cited by 91

The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics

Pritchard, S. M., Dolan, P. J., Vitkus, A., & Johnson, G. V. W. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01273.x · Cited by 89

The cytoskeleton as a target for organophosphorus ester-induced delayed neurotoxicity (OPIDN)

Abou-Donia, M. B. (1993) · Chemico-Biological Interactions · doi:10.1016/0009-2797(93)90066-8 · Cited by 89

Targeting Tau Protein in Alzheimerʼs Disease

Gong, C., Grundke, I., & Iqbal, K. (2010) · Drugs & Aging · doi:10.2165/11536110-000000000-00000 · Cited by 90

New insights into the molecular mechanisms of axon guidance receptor regulation and signaling

Zang, Y., Chaudhari, K., & Bashaw, G. J. (2021) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2020.11.008 · Cited by 88

MAPping the Eukaryotic Tree of Life: Structure, Function, and Evolution of the MAP215⧸Dis1 Family of Microtubule-Associated Proteins

Gard, D. L., Becker, B. E., & Romney, S. J. (2004) · International review of cytology · doi:10.1016/s0074-7696(04)39004-2 · Cited by 94

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

Phosphorylation of Tau, Aβ-Formation, and Apoptosis After In Vivo Inhibition of PP-1 and PP-2A

Arendt, T., Holzer, M., Fruth, R., Brückner, M. K., & Gärtner, U. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00003-7 · Cited by 88

Separation of the different microtubule-associated tau protein species from bovine brain and their mode II phosphorylation by Ca2+/phospholipid-dependent protein kinase C.

Baudier, J., Lee, S., & Cole, R. D. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45421-x · Cited by 88

Antidiabetic Drugs for the Risk of Alzheimer Disease in Patients With Type 2 DM Using FAERS

Akimoto, H., Negishi, A., Oshima, S., Wakiyama, H., Okita, M., Horii, N., Inoue, N., Ohshima, S., & Kobayashi, D. (2020) · American Journal of Alzheimer's Disease & Other Dementias® · doi:10.1177/1533317519899546 · Cited by 89

Invited review: Animal models of tauopathies and their implications for research/translation into the clinic

Dujardin, S., Colin, M., & Buée, L. (2014) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12200 · Cited by 101

Alzheimer's Disease and Related Conditions.

Calne, D. B. (1971) · Annals of Internal Medicine · doi:10.7326/0003-4819-75-5-826_1 · Cited by 87

Tau Phosphorylation by Cyclin-dependent Kinase 5/p39 during Brain Development Reduces Its Affinity for Microtubules

Takahashi, S., Saito, T., Hisanaga, S.-I., Pant, H. C., & Kulkarni, A. B. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211964200 · Cited by 86

The Gonadotropin Connection in Alzheimer's Disease

Meethal, S. V., Smith, M. A., Bowen, R. L., & Atwood, C. (2005) · Endocrine · doi:10.1385/endo:26:3:317 · Cited by 85

Ascorbic acid reduction of microtubule protein disulfides and its relevance to protein S-nitrosylation assays

Landino, L. M., Koumas, M. T., Mason, C. E., & Alston, J. A. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.12.013 · Cited by 88

Casein kinase II preferentially phosphorylates human tau isoforms containing an amino-terminal insert. Identification of threonine 39 as the primary phosphate acceptor.

Greenwood, J. A., Scott, C. W., Spreen, R. C., Caputo, C. B., & Johnson, G. V. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)41790-x · Cited by 86

The distribution and phosphorylation of the microtubule-associated protein MAP 1B in growth cones

Mansfield, S. G., Díaz‐Nido, J., Gordon‐Weeks, P. R., & Ávila, J. (1991) · Journal of Neurocytology · doi:10.1007/bf01187918 · Cited by 86

Role of GSK‐3β in Alzheimer's disease pathology

Planel, E., Sun, X., & Takashima, A. (2002) · Drug Development Research · doi:10.1002/ddr.10100 · Cited by 87

τ Protein Kinase II Is Involved in the Regulation of the Normal Phosphorylation State of τ Protein

Arioka, M., Tsukamoto, M., Ishiguro, K., Kato, R., Sato, K., Imahori, K., & Uchida, T. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03173.x · Cited by 85

Lithium ion inhibits nerve growth factor-induced neurite outgrowth and phosphorylation of nerve growth factor-modulated microtubule-associated proteins.

Burstein, D. E., Seeley, P. J., & Greene, L. A. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.3.862 · Cited by 85

Abnormally phosphorylated tau protein in Alzheimer's disease: Heterogeneity of individual regional distribution and relationship to clinical severity

Holzer, M., Holzapfel, H.-P., Zedlick, D., Brückner, M. K., & Arendt, T. (1994) · Neuroscience · doi:10.1016/0306-4522(94)90546-0 · Cited by 83

An Insight into Cellular and Molecular Mechanisms Underlying the Pathogenesis of Neurodegeneration in Alzheimer’s Disease

Ratan, Y., Rajput, A., Maleysm, S., Pareek, A., Jain, V. K., Pareek, A., Kaur, R., & Singh, G. (2023) · Biomedicines · doi:10.3390/biomedicines11051398 · Cited by 89

SUMO and Its Role in Human Diseases

Sarge, K. D., & Park-Sarge, O.-K. (2011) · International review of cytology · doi:10.1016/b978-0-12-386041-5.00004-2 · Cited by 82

Sequential phosphorylation of tau protein by cAMP‐dependent protein kinase and SAPK4/p38δ or JNK2 in the presence of heparin generates the AT100 epitope

Yoshida, H., & Goedert, M. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04052.x · Cited by 87

Cdk5 and MAPK are associated with complexes of cytoskeletal proteins in rat brain

Veeranna, G. J., Shetty, K. T., Takahashi, M., Grant, P. G., & Pant, H. C. (2000) · Molecular Brain Research · doi:10.1016/s0169-328x(00)00003-6 · Cited by 83

Neurite Aggregation and Calcium Dysfunction in iPSC-Derived Sensory Neurons with Parkinson’s Disease-Related LRRK2 G2019S Mutation

Schwab, A. J., & Ebert, A. D. (2015) · Stem Cell Reports · doi:10.1016/j.stemcr.2015.11.004 · Cited by 87

Evidence for the progression through S-phase in the ectopic cell cycle re-entry of neurons in Alzheimer disease

Bonda, D., Evans, T. A., Santocanale, C., Llosá, J. C., Viña, J., Bajić, V., Castellani, R. J., Siedlak, S. L., Perry, G. L., Smith, M. A., et al. (2009) · Aging · doi:10.18632/aging.100044 · Cited by 82

Association of S100B with intermediate filaments and microtubules in glial cells

Sorci, G., Agneletti, A. L., Bianchi, R., & Donato, R. (1998) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/s0167-4889(98)00134-7 · Cited by 83

Quantitative Analysis of the Brain Ubiquitylome in Alzheimer's Disease

Abreha, M. H., Dammer, E. B., Ping, L., Zhang, T., Duong, D. M., Gearing, M., Lah, J. J., Levey, A. I., & Seyfried, N. T. (2018) · PROTEOMICS · doi:10.1002/pmic.201800108 · Cited by 82

Site-specific Dephosphorylation of Tau Protein at Ser202/Thr205 in Response to Microtubule Depolymerization in Cultured Human Neurons Involves Protein Phosphatase 2A

Merrick, S. E., Demoise, D. C., & Lee, V. M. ‐. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5589 · Cited by 81

Phosphorylation by CDK1 regulates XMAP215 function in vitro

Vasquez, R., Gard, D. L., & Cassimeris, L. (1999) · Cell Motility and the Cytoskeleton · doi:10.1002/(sici)1097-0169(1999)43:4 · Cited by 83

Generation of microtubule stability subclasses by microtubule-associated proteins: implications for the microtubule "dynamic instability" model.

Job, D., Pabion, M., & Margolis, R. L. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.101.5.1680 · Cited by 80

Current Understanding of Neurodegenerative Diseases Associated With the Protein Tau

Josephs, K. A. (2017) · Mayo Clinic Proceedings · doi:10.1016/j.mayocp.2017.04.016 · Cited by 87

Involvement of 14‐3‐3 in tubulin instability and impaired axon development is mediated by Tau

Joo, Y., Schumacher, B., Landrieu, I., Bartel, M., Smet‐Nocca, C., Jang, A., Choi, H. S., Jeon, N. L., Chang, K., Kim, H., et al. (2015) · The FASEB Journal · doi:10.1096/fj.14-265009 · Cited by 81

Microtubule dynamics and the neurodegenerative triad of Alzheimer's disease: The hidden connection

Brandt, R., & Bakota, L. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.14011 · Cited by 83

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

Current directions in tau research: Highlights from Tau 2020

Sexton, C. E., Snyder, H. M., Beher, D., Boxer, A. L., Brannelly, P., Brion, J., Buée, L., Cacace, A. M., Chételat, G., Citron, M., et al. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12452 · Cited by 89

Cytosolic Abnormally Hyperphosphorylated Tau But Not Paired Helical Filaments Sequester Normal MAPs and Inhibit Microtubule Assembly

Iqbal, K., Alonso, A. D. C., & Grundke, I. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14402 · Cited by 77

Regulation of neuronal microtubule dynamics by tau: Implications for tauopathies

Venkatramani, A., & Panda, D. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.04.120 · Cited by 84

Differences in microtubule binding and self-association abilities of bovine brain tau isoforms.

de Ancos, J. G., Correas, I., & Ávila, J. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53053-2 · Cited by 79

Expression of protein phosphatases (PP-1, PP-2A, PP-2B and PTP-1B) and protein kinases (MAP kinase and P34cdc2) in the hippocampus of patients with Alzheimer disease and normal aged individuals.

Pei, J.-J., Sersen, E., Iqbal, K., & Grundke-Iqbal, I. (1994) · Brain Research · doi:10.1016/0006-8993(94)91598-9 · Cited by 89

Dysregulation of Protein Phosphorylation/Dephosphorylation in Alzheimer′s Disease: A Therapeutic Target

Gong, C., Liu, F., Grundke, I., & Iqbal, K. (2006) · BioMed Research International · doi:10.1155/jbb/2006/31825 · Cited by 81

Tau complexes with phospholipase C-γ in situ

Jenkins, S. M., & Johnson, G. V. W. (1998) · Neuroreport · doi:10.1097/00001756-199801050-00014 · Cited by 81

Tau isoform expression and phosphorylation state during differentiation of cultured neuronal cells

Smith, C. J., Anderton, B. H., Davis, D. R., & Gallo, J. (1995) · FEBS Letters · doi:10.1016/0014-5793(95)01221-y · Cited by 78

Microtubule associated protein tau binds to double-stranded but not single-stranded DNA

Hua, Q., He, R.-Q., Haque, N., Qu, M., Alonso, A. D. C., Grundke, I., & Iqbal, K. (2003) · Cellular and Molecular Life Sciences · doi:10.1007/s000180300034 · Cited by 77

Nerve growth factor enhances the synthesis, phosphorylation, and metabolic stability of neurofilament proteins in PC12 cells.

Lindenbaum, M. H., Carbonetto, S., & Mushynski, W. E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75826-8 · Cited by 77

Phosphorylation of microtubule‐associated protein tau by stress‐activated protein kinases in intact cells

Buée‐Scherrer, V., & Goedert, M. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)02460-2 · Cited by 76

The phosphorylation state of the microtubule-associated protein tau as affected by glutamate, colchicine and β-amyloid in primary rat cortical neuronal cultures

Davis, D. R., Brion, J., Couck, A. M., Gallo, J., Hanger, D. P., Ladhani, K., Lewis, C., Miller, C. C. J., Rupniak, T., Smith, C. E., et al. (1995) · Biochemical Journal · doi:10.1042/bj3090941 · Cited by 76

When Good Kinases Go Rogue: GSK3, p38 MAPK and CDKs as Therapeutic Targets for Alzheimer’s and Huntington’s Disease

D’Mello, S. R. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22115911 · Cited by 80

The emerging link between O-GlcNAcylation and neurological disorders

Ma, X., Li, H., He, Y., & Hao, J. (2017) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-017-2542-9 · Cited by 75

A critical appraisal of tau‐targeting therapies for primary and secondary tauopathies

Imbimbo, B. P., Ippati, S., Watling, M., & Balducci, C. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12453 · Cited by 76

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 75

Impaired retrograde transport by the Dynein/Dynactin complex contributes to Tau-induced toxicity

Butzlaff, M., Hannan, S. B., Karsten, P., Lenz, S., Ng, J., Voßfeldt, H., Prüßing, K., Pflanz, R., Schulz, J. B., Rasse, T. M., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv107 · Cited by 74

Biomarkers in Alzheimer's Disease: Past, Present and Future

Gustaw‐Rothenberg, K., Lerner, A. J., Bonda, D., Lee, H., Zhu, X., Perry, G. L., & Smith, M. A. (2010) · Biomarkers in Medicine · doi:10.2217/bmm.09.86 · Cited by 71

Mechanism of neurofibrillary degeneration in Alzheimer's disease

Iqbal, K., Alonso, A. D. C., Gong, C., Khatoon, S., Singh, T. J., & Grundke, I. (1994) · Molecular Neurobiology · doi:10.1007/bf02816111 · Cited by 72

Brain lesions comprised of aluminum-rich cells that lack microtubules may be associated with the cognitive deficit of Alzheimer's disease

Walton, J. R. (2009) · NeuroToxicology · doi:10.1016/j.neuro.2009.06.010 · Cited by 71

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