Tau Structures

Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy

Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359 · 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

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

A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation

Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927 · 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

Tau in physiology and pathology

Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251 · see citing works

Paclitaxel (Taxol)

Rowinsky, E. K., & Donehower, R. C. (1995) · New England Journal of Medicine · doi:10.1056/nejm199504133321507 · Cited by 1,924 · see citing works

Dendritic Function of Tau Mediates Amyloid-β Toxicity in Alzheimer's Disease Mouse Models

Ittner, L. M., Ke, Y. D., Delerue, F., Bi, M., Gladbach, A., van Eersel, J., Wölfing, H., Chieng, B. C., Christie, M. J., Napier, I. A., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.036 · Cited by 1,821 · see citing works

Transmission and spreading of tauopathy in transgenic mouse brain

Clavaguera, F., Bolmont, T., Crowther, R. A., Abramowski, D., Frank, S., Probst, A., Fraser, G., Stalder, A. K., Beibel, M., Staufenbiel, M., et al. (2009) · Nature Cell Biology · doi:10.1038/ncb1901 · Cited by 1,803 · 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

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

Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans

Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996) · Nature · doi:10.1038/383550a0 · Cited by 1,036 · see citing works

Assembly of τ protein into Alzheimer paired helical filaments depends on a local sequence motif ( ³⁰⁶ VQIVYK ³¹¹ ) forming β structure

von Bergen, M., Friedhoff, P., Biernat, J., Heberle, J., Mandelkow, E.-M., & Mandelkow, E. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.10.5129 · Cited by 1,021 · 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

Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies

Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986 · see citing works

Tau phosphorylation: the therapeutic challenge for neurodegenerative disease

Hanger, D. P., Anderton, B. H., & Noble, W. (2009) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2009.01.003 · Cited by 965 · 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

Accumulation of abnormally phosphorylated τ precedes the formation of neurofibrillary tangles in Alzheimer's disease

Bancher, C., Brunner, C., Lassmann, H., Budka, H., Jellinger, K., Wiche, G., Seitelberger, F., Grundke-Iqbal, I., Iqbal, K., & Wisniewski, H. M. (1989) · Brain Research · doi:10.1016/0006-8993(89)91396-6 · Cited by 818 · see citing works

Tau and neurodegenerative disease: the story so far

Iqbal, K., Liu, F., & Gong, C.-X. (2016) · Nature Reviews Neurology · doi:10.1038/nrneurol.2015.225 · Cited by 806 · see citing works

Brain homogenates from human tauopathies induce tau inclusions in mouse brain

Clavaguera, F., Akatsu, H., Fraser, G. M., Crowther, R. A., Frank, S., Hench, J., Probst, A., Winkler, D. T., Reichwald, J., Staufenbiel, M., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301175110 · Cited by 750 · see citing works

Tau protein function in living cells.

Drubin, D. G., & Kirschner, M. W. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.6.2739 · Cited by 745 · see citing works

The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721 · see citing works

Synthetic Tau Fibrils Mediate Transmission of Neurofibrillary Tangles in a Transgenic Mouse Model of Alzheimer's-Like Tauopathy

Iba, M., Guo, J. L., McBride, J. D., Zhang, B., Trojanowski, J. Q., & Lee, V. M.-Y. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.2642-12.2013 · Cited by 664 · 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

Structural Polymorphism of 441-Residue Tau at Single Residue Resolution

Mukrasch, M. D., Bibow, S., Korukottu, J., Jeganathan, S., Biernat, J., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2009) · PLoS Biology · doi:10.1371/journal.pbio.1000034 · Cited by 652 · see citing works

Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing

Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617 · see citing works

Microtubule-Associated Proteins: Their Potential Role in Determining Neuronal Morphology

Matus, A. I. (1988) · Annual Review of Neuroscience · doi:10.1146/annurev.ne.11.030188.000333 · Cited by 606 · see citing works

Structural studies of tau protein and Alzheimer paired helical filaments show no evidence for beta-structure.

Schweers, O., Schönbrunn, E., Marx, A., & Mandelkow�, E. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)51080-8 · Cited by 569 · see citing works

Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2

Neve, R. L., Harris, P. K. W., Kosik, K. S., Kurnit, D. M., & Donlon, T. A. (1986) · Molecular Brain Research · doi:10.1016/0169-328x(86)90033-1 · Cited by 565 · 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

X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation.

Kirschner, D. A., Abraham, C., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.83.2.503 · Cited by 517 · see citing works

Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits

Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3951 · Cited by 516 · see citing works

Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease

Zhang, Z., Song, M., Liu, X., Kang, S. S., Kwon, I.-S., Duong, D. M., Seyfried, N. T., Hu, W. T., Liu, Z., Wang, J.-Z., et al. (2014) · Nature Medicine · doi:10.1038/nm.3700 · Cited by 494 · see citing works

The switch of tau protein to an Alzheimer‐like state includes the phosphorylation of two serine‐proline motifs upstream of the microtubule binding region.

Biernat, J., Mandelkow, E. M., Schröter, C., Lichtenberg‐Kraag, B., Steiner, B., Berling, B., Meyer, H., Mercken, M., Vandermeeren, A., & Goedert, M. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05204.x · Cited by 484 · see citing works

Alzheimer-like paired helical filaments and antiparallel dimers formed from microtubule-associated protein tau in vitro.

Wille, H., Drewes, G., Biernat, J., Mandelkow�, E., & Mandelkow�, E. (1992) · The Journal of Cell Biology · doi:10.1083/jcb.118.3.573 · Cited by 477 · see citing works

Tau post-translational modifications in wild-type and human amyloid precursor protein transgenic mice

Morris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472 · see citing works

Mutations causing neurodegenerative tauopathies

Goedert, M., & Jakes, R. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.007 · Cited by 438 · see citing works

Global Hairpin Folding of Tau in Solution

Jeganathan, S., von Bergen, M., Brutlach, H., Steinhoff, H.-J., & Mandelkow, E. (2006) · Biochemistry · doi:10.1021/bi0521543 · Cited by 432 · see citing works

The Structural Basis of Monoclonal Antibody Alz50's Selectivity for Alzheimer's Disease Pathology

Carmel, G., Mager, E. M., Binder, L. I., & Kuret, J. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.51.32789 · Cited by 402 · see citing works

Tau proteins: the molecular structure and mode of binding on microtubules.

Hirokawa, N., Shiomura, Y., & Okabe, S. (1988) · The Journal of Cell Biology · doi:10.1083/jcb.107.4.1449 · Cited by 389 · see citing works

Polymerization of τ into Filaments in the Presence of Heparin: The Minimal Sequence Required for τ ‐ τ Interaction

Pérez, M., Valpuesta, J., Medina, M., de Garcini, E. M., & Ávila, J. (1996) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1996.67031183.x · Cited by 355 · see citing works

Interaction of tau with the RNA-Binding Protein TIA1 Regulates tau Pathophysiology and Toxicity

Vanderweyde, T. E., Apicco, D. J., Youmans-Kidder, K., Ash, P. E. A., Cook, C. N., da Rocha, E. L., Jansen‐West, K. R., Frame, A. A., Citro, A., Leszyk, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.045 · Cited by 346 · see citing works

One of the Antigenic Determinants of Paired Helical Filaments Is Related to Tau Protein1

Nukina, N., & Ihara, Y. (1986) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135625 · Cited by 338 · see citing works

Phase Separation: Linking Cellular Compartmentalization to Disease

Aguzzi, A., & Altmeyer, M. (2016) · Trends in Cell Biology · doi:10.1016/j.tcb.2016.03.004 · Cited by 333 · see citing works

Granular Tau Oligomers as Intermediates of Tau Filaments

Maeda, S., Sahara, N., Saito, Y., Murayama, M., Yoshiike, Y., Kim, H., Miyasaka, T., Murayama, S., Ikai, A., & Takashima, A. (2007) · Biochemistry · doi:10.1021/bi061359o · Cited by 309 · see citing works

The Endogenous and Cell Cycle-dependent Phosphorylation of tau Protein in Living Cells: Implications for Alzheimer’s Disease

Illenberger, S., Zheng‐Fischhöfer, Q., Preuß, U., Stamer, K., Baumann, K., Trinczek, B., Biernat, J., Godemann, R., Mandelkow, E., & Mandelkow�, E. (1998) · Molecular Biology of the Cell · doi:10.1091/mbc.9.6.1495 · Cited by 300 · see citing works

Tau phosphorylation and aggregation in Alzheimer's disease pathology

Ávila, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.02.067 · Cited by 283 · see citing works

Advances in Medicine and Biology

Berhardt, L. V. (2017) · International Linear Collider · Cited by 281 · see citing works

Acetylated Tau Obstructs KIBRA-Mediated Signaling in Synaptic Plasticity and Promotes Tauopathy-Related Memory Loss

Tracy, T. E., Sohn, P. D., Minami, S. S., Wang, C., Min, S.-W., Li, Y., Zhou, Y., Le, D., Lo, I., Ponnusamy, R., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.03.005 · Cited by 277 · see citing works

Proline Isomer-Specific Antibodies Reveal the Early Pathogenic Tau Conformation in Alzheimer's Disease

Nakamura, K., Greenwood, A., Binder, L. I., Bigio, E. H., Denial, S., Nicholson, L. K., Zhou, X. Z., & Lu, K. P. (2012) · Cell · doi:10.1016/j.cell.2012.02.016 · Cited by 255 · see citing works

Cloning of a big tau microtubule-associated protein characteristic of the peripheral nervous system.

Goedert, M., Spillantini, M. G., & Crowther, R. A. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.5.1983 · Cited by 255 · see citing works

Beyond Oil and Water—Phase Transitions in Cells

Hyman, A. A., & Simons, K. (2012) · Science · doi:10.1126/science.1223728 · Cited by 248 · see citing works

Specific Knockdown of Endogenous Tau Protein by Peptide-Directed Ubiquitin-Proteasome Degradation

Chu, T.-T., Gao, N., Li, Q.-Q., Chen, P.-G., Yang, X.-F., Chen, Y.-X., Zhao, Y.-F., & Li, Y.-M. (2016) · Cell Chemical Biology · doi:10.1016/j.chembiol.2016.02.016 · Cited by 247 · see citing works

Are tau aggregates toxic or protective in tauopathies?

Cowan, C. M., & Mudher, A. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00114 · Cited by 215 · see citing works

Intracerebral injection of preformed synthetic tau fibrils initiates widespread tauopathy and neuronal loss in the brains of tau transgenic mice

Peeraer, E., Bottelbergs, A., Van Kolen, K., Stancu, I.-C., Vasconcelos, B., Mahieu, M., Duytschaever, H., Ver Donck, L., Torremans, A., Sluydts, E., et al. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.08.032 · Cited by 214 · 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

Microtubule structure and its stabilisation

Amos, L. (2004) · Organic & Biomolecular Chemistry · doi:10.1039/b403634d · Cited by 193 · see citing works

Activation of Phospholipase C-γ by the Concerted Action of Tau Proteins and Arachidonic Acid

Hwang, S. C., Jhon, D.-Y., Bae, Y. S., Kim, J. H., & Rhee, S. G. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18342 · Cited by 172 · see citing works

Tau Biology and Tau-Directed Therapies for Alzheimer’s Disease

Bakota, L., & Brandt, R. (2016) · Drugs · doi:10.1007/s40265-015-0529-0 · Cited by 170 · see citing works

Acetylated tau destabilizes the cytoskeleton in the axon initial segment and is mislocalized to the somatodendritic compartment

Sohn, P. D., Tracy, T. E., Son, H.-I., Zhou, Y., Leite, R. E. P., Miller, B. L., Seeley, W. W., Grinberg, L. T., & Gan, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0109-0 · Cited by 160 · see citing works

Co-immunoprecipitation with Tau Isoform-specific Antibodies Reveals Distinct Protein Interactions and Highlights a Putative Role for 2N Tau in Disease

Liu, C., Song, X., Nisbet, R. M., & Götz, J. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.641902 · Cited by 145 · see citing works

The tubulin-binding sequence of brain microtubule-associated proteins, tau and MAP-2, is also involved in actin binding

Correas, I., Padilla, R., & Avila, J. (1990) · Biochemical Journal · doi:10.1042/bj2690061 · Cited by 144 · see citing works

Structural stability of paired helical filaments requires microtubule-binding domains of Tau: A model for self-association

Ksiȩżak-Reding, H., & Yen, S.-H. C. (1991) · Neuron · doi:10.1016/0896-6273(91)90169-z · Cited by 136 · see citing works

Hyperphosphorylation determines both the spread and the morphology of tau pathology

Hu, W. H., Zhang, X., Tung, Y. C., Xie, S.-T., Liu, F., & Iqbal, K. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.01.014 · Cited by 131 · see citing works

Expression of A152T human tau causes age‐dependent neuronal dysfunction and loss in transgenic mice

Maeda, S., Djukic, B., Taneja, P., Yu, G.-Q., Lo, I., Davis, A., Craft, R., Guo, W., Wang, X., Kim, D., et al. (2016) · EMBO Reports · doi:10.15252/embr.201541438 · Cited by 130 · see citing works

Toxic tau oligomer formation blocked by capping of cysteine residues with 1,2-dihydroxybenzene groups

Soeda, Y., Yoshikawa, M., Almeida, O. F. X., Sumioka, A., Maeda, S., Osada, H., Kondoh, Y., Saito, A., Miyasaka, T., Kimura, T., et al. (2015) · Nature Communications · doi:10.1038/ncomms10216 · Cited by 126 · see citing works

Identification of Tau and MAP2 as novel substrates of Rho-kinase and myosin phosphatase

Amano, M., Kaneko, T., Maeda, A., Nakayama, M., Ito, M., Yamauchi, T., Goto, H., Fukata, Y., Oshiro, N., Shinohara, A., et al. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.02054.x · Cited by 118 · see citing works

α-Helix Structure in Alzheimer's Disease Aggregates of Tau-Protein

Sadqi, M., Hernández, F., Pan, U., Pérez, M., Schaeberle, M. D., Ávila, J., & Muñoz, V. (2002) · Biochemistry · doi:10.1021/bi025777e · Cited by 117 · see citing works

The Tau/A152T mutation, a risk factor for frontotemporal‐spectrum disorders, leads to NR2B receptor‐mediated excitotoxicity

Decker, J., Krüger, L., Sydow, A., Dennissen, F. J., Šišková, Z., Mandelkow, E., & Mandelkow, E. (2016) · EMBO Reports · doi:10.15252/embr.201541439 · Cited by 115 · see citing works

Self assembly of microtubule associated protein tau into filaments resembling those found in alzheimer disease

de Garcini, E. M., Serrano, L. G., & Ávila, J. (1986) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(86)80242-x · Cited by 110 · see citing works

Understanding tubulin–Taxol interactions: Mutations that impart Taxol binding to yeast tubulin

Gupta, M. L., Bode, C. J., Georg, G. I., & Himes, R. H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1131967100 · Cited by 107 · see citing works

Residual Structure in the Repeat Domain of Tau: Echoes of Microtubule Binding and Paired Helical Filament Formation

Eliezer, D., Barré, P., Kobašlija, M., Chan, D. K., Li, X., & Heend, L. (2004) · Biochemistry · doi:10.1021/bi048953n · Cited by 106 · see citing works

Truncation of Tau Protein and its Pathological Significance in Alzheimer's Disease

García‐Sierra, F., Mondragón‐Rodríguez, S., & Basurto‐Islas, G. (2008) · Journal of Alzheimer s Disease · doi:10.3233/jad-2008-14407 · Cited by 101 · see citing works

Amyloid Precursor Protein (APP) Metabolites APP Intracellular Fragment (AICD), Aβ42, and Tau in Nuclear Roles

Multhaup, G., Huber, O., Buée, L., & Galas, M. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.r115.677211 · Cited by 101 · see citing works

Structural Impact of Proline-Directed Pseudophosphorylation at AT8, AT100, and PHF1 Epitopes on 441-Residue Tau

Bibow, S., Ozenne, V., Biernat, J., Blackledge, M. J., Mandelkow�, E., & Zweckstetter, M. (2011) · Journal of the American Chemical Society · doi:10.1021/ja205836j · Cited by 97 · see citing works

The Presence of Select Tau Species in Human Peripheral Tissues and Their Relation to Alzheimer’s Disease

Dugger, B. N., Whiteside, C. M., Maarouf, C. L., Walker, D. G., Beach, T. G., Sue, L. I., Garcia, A., Dunckley, T. L., Meechoovet, B., Reiman, E. M., et al. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-150859 · Cited by 93 · see citing works

Acetylation mimic of lysine 280 exacerbates human Tau neurotoxicity in vivo

Gorsky, M. K., Burnouf, S., Dols, J., Mandelkow�, E., & Partridge, L. (2016) · Scientific Reports · doi:10.1038/srep22685 · Cited by 93 · see citing works

Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline‐rich region of the disordered Tau protein

Sibille, N., Huvent, I., Fauquant, C., Verdegem, D., Amniai, L., Leroy, A., Wieruszeski, J., Lippens, G. M., & Landrieu, I. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.23210 · Cited by 92 · see citing works

Critical residues involved in tau binding to fyn: implications for tau phosphorylation in Alzheimer’s disease

Lau, D. H. W., Hogseth, M., Phillips, E. C., O’Neill, M. J., Pooler, A. M., Noble, W. J., & Hanger, D. P. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0317-4 · Cited by 91 · see citing works

Trimeric Tau Is Toxic to Human Neuronal Cells at Low Nanomolar Concentrations

Tian, H., Davidowitz, E., Lopez, P., Emadi, S., Moe, J., & Sierks, M. (2013) · International Journal of Cell Biology · doi:10.1155/2013/260787 · Cited by 90 · see citing works

Rho Kinase Inhibition as a Therapeutic for Progressive Supranuclear Palsy and Corticobasal Degeneration

Gentry, E. G., Henderson, B. W., Arrant, A. E., Gearing, M., Feng, Y., Riddle, N. C., & Herskowitz, J. H. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.2336-15.2016 · Cited by 90 · see citing works

α-Synuclein Fibrils Exhibit Gain of Toxic Function, Promoting Tau Aggregation and Inhibiting Microtubule Assembly

Oikawa, T., Nonaka, T., Terada, M., Tamaoka, A., Hisanaga, S., & Hasegawa, M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.736355 · Cited by 87 · see citing works

Nuclear Magnetic Resonance Spectroscopy Characterization of Interaction of Tau with DNA and Its Regulation by Phosphorylation

Qi, H., Cantrelle, F., Benhelli‐Mokrani, H., Smet‐Nocca, C., Buée, L., Lippens, G. M., Bonnefoy, E., Galas, M., & Landrieu, I. (2015) · Biochemistry · doi:10.1021/bi5014613 · Cited by 83 · see citing works

Tauopathies and Tau Oligomers

Takashima, A. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130653 · Cited by 80 · see citing works

The Dynamics and Turnover of Tau Aggregates in Cultured Cells

Guo, J., Buist, A., Soares, A. C., Callaerts, K., Calafate, S., Stevenaert, F., Daniels, J. P., Zoll, B. E., Crowe, A., Brunden, K. R., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.712083 · Cited by 80 · see citing works

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 · see citing works

Rapid treadmilling of brain microtubules free of microtubule-associated proteins in vitro and its suppression by tau

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An evolutionary roadmap to the microtubule-associated protein MAP Tau

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Tauopathy

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