RNA stimulates aggregation of microtubule-associated protein tau into Alzheimer-like paired helical filaments

Cloning and sequencing of the cDNA encoding an isoform of microtubule‐associated protein tau containing four tandem repeats: differential expression of tau protein mRNAs in human brain.

Goedert, M., Spillantini, M. G., Potier, M. C., Ulrich, J., & Crowther, R. A. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb03390.x · Cited by 1,037 · 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

Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease.

Wischik, C. M., Novak, M., Thøgersen, H. C., Edwards, P. C., Runswick, M. J., Jakes, R., Walker, J. E., Milstein, C., Roth, M., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.12.4506 · Cited by 939 · see citing works

A sequence of cytoskeleton changes related to the formation of neurofibrillary tangles and neuropil threads

Braak, F., Braak, H., & Mandelkow, E. (1994) · Acta Neuropathologica · doi:10.1007/bf00293315 · Cited by 769 · see citing works

Domains of tau Protein and Interactions with Microtubules

Gustke, N., Trinczek, B., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1994) · Biochemistry · doi:10.1021/bi00198a017 · Cited by 655 · 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

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

Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament

Novak, M., Kabat, J., & Wischik, C. M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05665.x · Cited by 398 · see citing works

Oxidation of cysteine-322 in the repeat domain of microtubule-associated protein tau controls the in vitro assembly of paired helical filaments.

Schweers, O., Mandelkow, E., Biernat, J., & Mandelkow, E. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.18.8463 · Cited by 379 · 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

Straight and paired helical filaments in Alzheimer disease have a common structural unit.

Crowther, R. A. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.6.2288 · Cited by 354 · see citing works

Tau domains, phosphorylation, and interactions with microtubules

Mandelkow, E.-M., Biernat, J., Drewes, G., Gustke, N., Trinczek, B., & Mandelkow, E. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00025-a · Cited by 308 · see citing works

Subunit structure of paired helical filaments in Alzheimer's disease.

Wischik, C. M., Crowther, R. A., Stewart, M. D., & Roth, M. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.6.1905 · Cited by 230 · see citing works

Tubulin domains probed by limited proteolysis and subunit-specific antibodies

Mandelkow, E., Herrmann, M. E., & Rühl, U. (1985) · Journal of Molecular Biology · doi:10.1016/0022-2836(85)90406-1 · Cited by 219 · see citing works

Common and distinct tubulin binding sites for microtubule-associated proteins.

Littauer, U. Z., Giveon, D., Thierauf, M., Ginzburg, I., & Ponstingl, H. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.19.7162 · Cited by 217 · see citing works

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 198 · see citing works

Phosphorylation-dependent epitopes of neurofilament antibodies on tau protein and relationship with Alzheimer tau.

Lichtenberg-Kraag, B., Mandelkow�, E., Biernat, J., Steiner, B., Schröter, C., Gustke, N., Meyer, H. E., & Mandelkow�, E. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.12.5384 · Cited by 157 · see citing works

Assembly of Alzheimer‐like filaments from full‐length tau protein

Crowther, R. A., Olesen, O. F., Smith, M. J., Jakes, R., & Goedert, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)80260-2 · Cited by 154 · see citing works

Identification of 3‐ and 4‐repeat tau isoforms within the PHF in Alzheimer's disease.

Jakes, R., Novák, M., Davison, M., & Wischik, C. M. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07820.x · Cited by 149 · see citing works

Inhibition of tubulin assembly by RNA and other polyanions: evidence for a required protein.

Bryan, J., Nagle, B. W., & Doenges, K. H. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.9.3570 · Cited by 134 · see citing works

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 132 · see citing works

Polycation-induced assembly of purified tubulin.

Erickson, H., & Voter, W. A. (1976) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.73.8.2813 · Cited by 129 · see citing works

Tau as a nucleolar protein in human nonneural cells in vitro and in vivo

Thurston, V. C., Zinkowski, R. P., & Binder, L. I. (1996) · Chromosoma · doi:10.1007/bf02510035 · Cited by 100 · 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

Polymerization of Microtubule-associated Protein Tau under Near-physiological Conditions

Wilson, D. M., & Binder, L. I. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.41.24306 · Cited by 79 · see citing works

Domain structure and antiparallel dimers of microtubule-associated protein 2 (MAP2)

Wille, H., Mandelkow�, E., Dingus, J., Vallee, R. B., Binder, L. I., & Mandelkow�, E. (1992) · Journal of Structural Biology · doi:10.1016/1047-8477(92)90006-v · Cited by 46 · see citing works

Short- and long-term mechanisms of tau regulation in PC12 cells

Sadot, E., Barg, J., Rasouly, D., Lazarovici, P., & Ginzburg, I. (1995) · Journal of Cell Science · doi:10.1242/jcs.108.8.2857 · Cited by 25 · see citing works

Isoforms of tau protein from mammalian brain and avian erythrocytes: Structure, self-assembly, and elasticity

Lichtenberg-Kraag, B., & Mandelkow�, E. (1990) · Journal of Structural Biology · doi:10.1016/1047-8477(90)90097-v · Cited by 21 · see citing works

The molecular pathology of Alzheimer's disease

Selkoe, D. J. (1991) · Neuron · doi:10.1016/0896-6273(91)90052-2 · Cited by 2,708 · see citing works

Neurodegenerative Tauopathies

Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q. (2001) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.24.1.1121 · Cited by 2,480 · see citing works

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

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

Tau protein liquid–liquid phase separation can initiate tau aggregation

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

Tau pathology and neurodegeneration

Spillantini, M. G., & Goedert, M. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(13)70090-5 · Cited by 1,133 · 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

Tau pathology in Alzheimer disease and other tauopathies

Iqbal, K., del C. Alonso, A., Chen, S., Chohan, M. O., El-Akkad, E., Gong, C.-X., Khatoon, S., Li, B., Liu, F., Rahman, A., et al. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.09.008 · Cited by 1,037 · see citing works

The many faces of tau

Morris, M., Maeda, S., Vossel, K., & Mucke, L. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.009 · Cited by 899 · see citing works

Liquid–liquid phase separation of the microtubule-binding repeats of the Alzheimer-related protein Tau

Ambadipudi, S., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-00480-0 · Cited by 782 · see citing works

Axonal transport deficits and neurodegenerative diseases

Millecamps, S., & Julien, J.-P. (2013) · Nature Reviews Neuroscience · doi:10.1038/nrn3380 · Cited by 755 · see citing works

Tau PTM Profiles Identify Patient Heterogeneity and Stages of Alzheimer’s Disease

Wesseling, H., Mair, W., Kumar, M., Schlaffner, C. N., Tang, S., Beerepoot, P., Fatou, B., Guise, A. J., Cheng, L., Takeda, S., et al. (2020) · Cell · doi:10.1016/j.cell.2020.10.029 · Cited by 688 · see citing works

Tau and tauopathies

Arendt, T., Stieler, J. T., & Holzer, M. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.08.018 · Cited by 609 · see citing works

Seeding of Normal Tau by Pathological Tau Conformers Drives Pathogenesis of Alzheimer-like Tangles

Guo, J. L., & Lee, V. M.-Y. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.209296 · Cited by 636 · see citing works

Mechanisms of tau-induced neurodegeneration

Iqbal, K., Liu, F., Gong, C.-X., Alonso, A. D. C., & Grundke-Iqbal, I. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0486-3 · Cited by 628 · see citing works

The importance of tau phosphorylation for neurodegenerative diseases

Noble, W., Hanger, D. P., Miller, C. C. J., & Lovestone, S. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00083 · Cited by 475 · see citing works

Tau Protein Disrupts Nucleocytoplasmic Transport in Alzheimer’s Disease

Eftekharzadeh, B., Daigle, J. G., Kapinos, L. E., Coyne, A., Schiantarelli, J., Carlomagno, Y., Cook, C., Miller, S. J., Dujardin, S., Amaral, A. S., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.07.039 · Cited by 460 · see citing works

Unique pathological tau conformers from Alzheimer’s brains transmit tau pathology in nontransgenic mice

Guo, J. L., Narasimhan, S., Changolkar, L., He, Z., Stieber, A., Zhang, B., Gathagan, R. J., Iba, M., McBride, J. D., Trojanowski, J. Q., et al. (2016) · Journal of Experimental Medicine · doi:10.1084/jem.20160833 · Cited by 440 · see citing works

What is the evidence that tau pathology spreads through prion-like propagation?

Mudher, A., Colin, M., Dujardin, S., Medina, M., Dewachter, I., Alavi Naini, S. M., Mandelkow, E.-M., Mandelkow, E., Buée, L., Goedert, M., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0488-7 · Cited by 384 · see citing works

Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation

Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367 · see citing works

Toward a unified scheme for the aggregation of tau into Alzheimer paired helical filaments

Barghorn, S., & Mandelkow, E. (2002) · Biochemistry · doi:10.1021/bi026469j · Cited by 341 · see citing works

Sites of Tau Important for Aggregation Populate β-Structure and Bind to Microtubules and Polyanions

Mukrasch, M. D., Biernat, J., von Bergen, M., Griesinger, C., Mandelkow, E., & Zweckstetter, M. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501565200 · Cited by 324 · see citing works

Mechanisms of secretion and spreading of pathological tau protein

Brunello, C. A., Merezhko, M., Uronen, R.-L., & Huttunen, H. J. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03349-1 · Cited by 304 · see citing works

Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic Tau mutant

Sydow, A., Van der Jeugd, A., Zheng, F., Ahmed, T., Balschun, D., Petrova, O., Drexler, D., Zhou, L., Rune, G., Mandelkow, E., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.5245-10.2011 · Cited by 302 · see citing works

Amyloid-β oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin

Zempel, H., Luedtke, J., Kumar, Y., Biernat, J., Dawson, H., Mandelkow, E., & Mandelkow, E. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.207 · Cited by 283 · see citing works

Tau Mutations Cause Frontotemporal Dementias

Goedert, M., Crowther, R. A., & Spillantini, M. G. (1998) · Neuron · doi:10.1016/s0896-6273(00)80615-7 · Cited by 268 · see citing works

A major role for Tau in neuronal DNA and RNA protection in vivo under physiological and hyperthermic conditions

Violet, M., Delattre, L., Tardivel, M., Sultan, A., Chauderlier, A., Caillierez, R., Talahari, S., Nesslany, F., Lefebvre, B., Bonnefoy, E., et al. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00084 · Cited by 251 · see citing works

Structural Principles of Tau and the Paired Helical Filaments of Alzheimer's Disease

Mandelkow, E., Von Bergen, M., Biernat, J., & Mandelkow, E. (2007) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00053.x · Cited by 243 · see citing works

Tau Protein Interaction Partners and Their Roles in Alzheimer’s Disease and Other Tauopathies

Sinsky, J., Pichlerova, K., & Hanes, J. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22179207 · Cited by 220 · see citing works

Nuclear Tau and Its Potential Role in Alzheimer’s Disease

Bukar Maina, M., Al-Hilaly, Y., & Serpell, L. (2016) · Biomolecules · doi:10.3390/biom6010009 · Cited by 161 · see citing works

Cofactors are essential constituents of stable and seeding-active tau fibrils

Fichou, Y., Lin, Y., Rauch, J. N., Vigers, M., Zeng, Z., Srivastava, M., Keller, T. J., Freed, J. H., Kosik, K. S., & Han, S. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1810058115 · Cited by 128 · see citing works

Different distribution of phosphorylated tau protein isoforms in Alzheimer's and Pick's diseases

Sergeant, N., David, J.-P., Lefranc, D., Vermersch, P., Wattez, A., & Delacourte, A. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00859-4 · Cited by 117 · see citing works

Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation

Ambegaokar, S. S., & Jackson, G. R. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr432 · Cited by 113 · see citing works

Glycan Determinants of Heparin-Tau Interaction

Zhao, J., Huvent, I., Lippens, G., Eliezer, D., Zhang, A., Li, Q., Tessier, P., Linhardt, R. J., Zhang, F., & Wang, C. (2017) · Biophysical Journal · doi:10.1016/j.bpj.2017.01.024 · Cited by 87 · see citing works

Aggregates of Small Nuclear Ribonucleic Acids ( <scp>snRNAs</scp> ) in <scp>A</scp> lzheimer's Disease

Hales, C. M., Dammer, E. B., Diner, I., Yi, H., Seyfried, N. T., Gearing, M., Glass, J. D., Montine, T. J., Levey, A. I., & Lah, J. J. (2014) · Brain Pathology · doi:10.1111/bpa.12133 · Cited by 89 · see citing works

Pathological tau drives ectopic nuclear speckle scaffold protein SRRM2 accumulation in neuron cytoplasm in Alzheimer’s disease

McMillan, P. J., Strovas, T. J., Baum, M., Mitchell, B. K., Eck, R. J., Hendricks, N., Wheeler, J. M., Latimer, C. S., Keene, C. D., & Kraemer, B. C. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01219-1 · Cited by 64 · see citing works

Role of the Lipid Membrane and Membrane Proteins in Tau Pathology

Bok, E., Leem, E., Lee, B.-R., Lee, J. M., Yoo, C. J., Lee, E. M., & Kim, J. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.653815 · Cited by 61 · see citing works

Liquid-liquid phase separation of protein tau: An emerging process in Alzheimer's disease pathogenesis

Ainani, H., Bouchmaa, N., Ben Mrid, R., & El Fatimy, R. (2023) · Neurobiology of Disease · doi:10.1016/j.nbd.2023.106011 · Cited by 54 · see citing works

Further understanding of tau phosphorylation: implications for therapy

Medina, M., & Avila, J. (2015) · Expert Review of Neurotherapeutics · doi:10.1586/14737175.2015.1000864 · Cited by 41 · see citing works

Cellular and molecular modifier pathways in tauopathies: the big picture from screening invertebrate models

Hannan, S. B., Dräger, N. M., Rasse, T. M., Voigt, A., & Jahn, T. R. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13532 · Cited by 38 · see citing works

N368-Tau fragments generated by legumain are detected only in trace amount in the insoluble Tau aggregates isolated from AD brain

Schlegel, K., Awwad, K., Heym, R. G., Holzinger, D., Doell, A., Barghorn, S., Jahn, T. R., Klein, C., Mordashova, Y., Schulz, M., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0831-2 · Cited by 30 · see citing works

Tau liquid–liquid phase separation: At the crossroads of tau physiology and tauopathy

Islam, M., Shen, F., Regmi, D., Petersen, K., Karim, M. R. U., & Du, D. (2024) · Journal of Cellular Physiology · doi:10.1002/jcp.30853 · Cited by 28 · see citing works

Tau Oligomers

Maeda, S., & Takashima, A. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-32-9358-8_27 · Cited by 22 · see citing works

Physiological Role of Na,K‐ATPase Isoforms

Lingrel, J. B., Neumann, J. C., Dostanic, I., et al. (2004) · doi:10.1002/3527606122.ch16

Classification of FABP isoforms and tissues based on quantitative evaluation of transcript levels of these isoforms in various rat tissues

Yamamoto, T., Yamamoto, A., Watanabe, M., Matsuo, T., Yamazaki, N., Kataoka, M., Terada, H., & Shinohara, Y. (2009) · Biotechnology Letters · doi:10.1007/s10529-009-0065-7 · Cited by 39 · see citing works

Functional Roles of the α Isoforms of the Na,K‐ATPase

Lingrel, J. B., Moseley, A. E., Dostanic, I., et al. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb07214.x · Cited by 100 · see citing works

Collagen fibril ultrastructure alters after glycanolytic digestion

Quacci, D. E., Dell’Orbo, C., & Diaz, G. (1992) · Annals of Anatomy - Anatomischer Anzeiger · doi:10.1016/s0940-9602(11)80324-9 · Cited by 6 · see citing works

Brain tau isoform mRNA and protein correlation in PSP brain

Luk, C. Y., Vandrovcová, J., Malzer, E., Lees, A. J., & de Silva, R. (2010) · Translational Neuroscience · doi:10.2478/v10134-010-0009-8 · Cited by 9 · see citing works