Tau Oligomers

Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function

SantaCruz, K., Lewis, J., Spires, T., Paulson, J., Kotilinek, L., Ingelsson, M., Guimaraes, A., DeTure, M., Ramsden, M., McGowan, E., et al. (2005) · Science · doi:10.1126/science.1113694 · Cited by 2,014 · see citing works

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979 · 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

Neuronal loss correlates with but exceeds neurofibrillary tangles in Alzheimer's disease

Gómez‐Isla, T., Hollister, R., West, H., Mui, S., Growdon, J. H., Petersen, R. C., Parisi, J. E., & Hyman, B. T. (1997) · Annals of Neurology · doi:10.1002/ana.410410106 · Cited by 1,489 · 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

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

Hyperphosphorylation induces self-assembly of τ into tangles of paired helical filaments/straight filaments

Alonso, A. D. C., Zaidi, T., Novák, M., Grundke, I., & Iqbal, K. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.121119298 · Cited by 968 · see citing works

Tauopathy in <i>Drosophila</i> : Neurodegeneration Without Neurofibrillary Tangles

Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939 · 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

Tau oligomers impair memory and induce synaptic and mitochondrial dysfunction in wild-type mice

Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Clos, A. L., Jackson, G. R., & Kayed, R. (2011) · Molecular Neurodegeneration · doi:10.1186/1750-1326-6-39 · Cited by 633 · see citing works

Mutations of Tau Protein in Frontotemporal Dementia Promote Aggregation of Paired Helical Filaments by Enhancing Local β-Structure

von Bergen�, M., Barghorn, S., Li, L., Marx, A., Biernat, J., Mandelkow, E., & Mandelkow�, E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105196200 · Cited by 590 · see citing works

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

Kampers, T., Friedhoff, P., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (1996) · FEBS Letters · doi:10.1016/s0014-5793(96)01386-5 · Cited by 548 · see citing works

Identification of oligomers at early stages of tau aggregation in Alzheimer's disease

Lasagna‐Reeves, C. A., Castillo‐Carranza, D. L., Sengupta, U., Sarmiento, J., Troncoso, J., Jackson, G. R., & Kayed, R. (2012) · The FASEB Journal · doi:10.1096/fj.11-199851 · Cited by 527 · see citing works

Alzheimer brain-derived tau oligomers propagate pathology from endogenous tau

Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Sengupta, U., Guerrero-Munoz, M. J., Kiritoshi, T., Neugebauer, V., Jackson, G. R., & Kayed, R. (2012) · Scientific Reports · doi:10.1038/srep00700 · Cited by 502 · see citing works

Accumulation of Pathological Tau Species and Memory Loss in a Conditional Model of Tauopathy

Berger, Z., Roder, H. M., Hanna, A., Carlson, A. M., Rangachari, V., Yue, M., Wszołek, Z. K., Ashe, K. H., Knight, J. A., Dickson, D. W., et al. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0587-07.2007 · Cited by 485 · 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

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

Preparation and Characterization of Neurotoxic Tau Oligomers

Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Jackson, G. R., & Kayed, R. (2010) · Biochemistry · doi:10.1021/bi1016233 · Cited by 359 · 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

Characterization of Prefibrillar Tau Oligomers in Vitro and in Alzheimer Disease

Patterson, K. R., Remmers, C. L., Fu, Y., Brooker, S. M., Kanaan, N. M., Vana, L., Ward, S., Reyes, J. F., Philibert, K., Glucksman, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237974 · Cited by 354 · see citing works

Tau Oligomers: Cytotoxicity, Propagation, and Mitochondrial Damage

Shafiei, S. S., Guerrero-Muñoz, M. J., & Castillo-Carranza, D. L. (2017) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2017.00083 · Cited by 314 · see citing works

Conformational change as one of the earliest alterations of tau in Alzheimer's disease

Weaver, C. (2000) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00157-3 · Cited by 310 · 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

Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimer's disease

Maeda, S., Sahara, N., Saito, Y., Murayama, S., Ikai, A., & Takashima, A. (2006) · Neuroscience Research · doi:10.1016/j.neures.2005.11.009 · Cited by 301 · see citing works

Accelerated filament formation from tau protein with specific FTDP‐17 missense mutations

Nacharaju, P., Lewis, J. M., Easson, C., Yen, S. H., Hackett, J., Hutton, M., & Yen, S.-H. C. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00294-x · Cited by 283 · see citing works

Proline-directed Pseudo-phosphorylation at AT8 and PHF1 Epitopes Induces a Compaction of the Paperclip Folding of Tau and Generates a Pathological (MC-1) Conformation

Jeganathan, S., Hascher, A., Chinnathambi, S., Biernat, J., Mandelkow, E.-M., & Mandelkow, E. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805300200 · Cited by 278 · see citing works

Passive Immunization with Tau Oligomer Monoclonal Antibody Reverses Tauopathy Phenotypes without Affecting Hyperphosphorylated Neurofibrillary Tangles

Castillo-Carranza, D. L., Sengupta, U., Guerrero-Muñoz, M. J., Lasagna-Reeves, C. A., Gerson, J. E., Singh, G., Estes, D. M., Barrett, A. D. T., Dineley, K. T., Jackson, G. R., et al. (2014) · The Journal of Neuroscience · doi:10.1523/jneurosci.3192-13.2014 · Cited by 278 · see citing works

Pathogenic Forms of Tau Inhibit Kinesin-Dependent Axonal Transport through a Mechanism Involving Activation of Axonal Phosphotransferases

Kanaan, N. M., Morfini, G. A., LaPointe, N. E., Pigino, G. F., Patterson, K. R., Song, Y., Andreadis, A., Fu, Y., Brady, S. T., & Binder, L. I. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0560-11.2011 · Cited by 273 · see citing works

Anionic Micelles and Vesicles Induce Tau Fibrillization in Vitro

Chirita, C. N., Necula, M., & Kuret, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301663200 · Cited by 244 · see citing works

The amino terminus of tau inhibits kinesin‐dependent axonal transport: Implications for filament toxicity

LaPointe, N. E., Morfini, G. A., Pigino, G. F., Gaisina, I. N., Kozikowski, A. P., Binder, L. I., & Brady, S. T. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21850 · Cited by 240 · see citing works

Targeting Hsp90/Hsp70-Based Protein Quality Control for Treatment of Adult Onset Neurodegenerative Diseases

Pratt, W. B., Gestwicki, J. E., Osawa, Y., & Lieberman, A. P. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124332 · Cited by 237 · see citing works

Extracellular tau promotes intracellular calcium increase through M1 and M3 muscarinic receptors in neuronal cells

Gómez‐Ramos, A., Dı́az-Hernández, M., Rubio, A., Miras‐Portugal, M. T., & Ávila, J. (2008) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2007.12.010 · Cited by 233 · see citing works

Neurofibrillary tangle-bearing neurons are functionally integrated in cortical circuits in vivo

Kuchibhotla, K. V., Wegmann, S., Kopeikina, K. J., Hawkes, J., Rudinskiy, N., Andermann, M. L., Spires-Jones, T. L., Bacskai, B. J., & Hyman, B. T. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1318807111 · Cited by 193 · see citing works

Assembly of two distinct dimers and higher‐order oligomers from full‐length tau

Sahara, N., Maeda, S., Murayama, M., Suzuki, T., Dohmae, N., Yen, S.-H. C., & Takashima, A. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05555.x · Cited by 192 · see citing works

Specific Targeting of Tau Oligomers in Htau Mice Prevents Cognitive Impairment and Tau Toxicity Following Injection with Brain-Derived Tau Oligomeric Seeds

Castillo‐Carranza, D. L., Gerson, J. E., Sengupta, U., Guerrero‐Munoz, M. J., Lasagna‐Reeves, C. A., & Kayed, R. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-132477 · Cited by 180 · see citing works

Tauopathy-like Abnormalities and Neurologic Deficits in Mice Immunized With Neuronal Tau Protein

Rosenmann, H., Grigoriadis, N., Karussis, D., Boimel, M., Touloumi, O., Ovadia, H., & Abramsky, O. (2006) · Archives of Neurology · doi:10.1001/archneur.63.10.1459 · Cited by 178 · see citing works

Oligomer Formation of Tau Protein Hyperphosphorylated in Cells

Tepper, K., Biernat, J., Kumar, S., Wegmann, S., Timm, T., Hübschmann, S., Redecke, L., Mandelkow, E., Müller, D. J., & Mandelkow�, E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.611368 · Cited by 151 · see citing works

Formation and Propagation of Tau Oligomeric Seeds

Gerson, J. E., & Kayed, R. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00093 · Cited by 137 · 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

Allosteric Heat Shock Protein 70 Inhibitors Rapidly Rescue Synaptic Plasticity Deficits by Reducing Aberrant Tau

Abisambra, J. F., Jinwal, U. K., Miyata, Y., Rogers, J. T., Blair, L. J., Li, X., Seguin, S. P., Wang, L., Jin, Y. L., Bacon, J. A., et al. (2013) · Biological Psychiatry · doi:10.1016/j.biopsych.2013.02.027 · Cited by 109 · see citing works

Extracellular low‐n oligomers of tau cause selective synaptotoxicity without affecting cell viability

Kaniyappan, S., Chandupatla, R., Mandelkow, E., & Mandelkow, E. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.04.002 · Cited by 95 · see citing works

Assembly of paired helical filaments from mouse tau: implications for the neurofibrillary pathology in transgenic mouse models for Alzheimer's disease

Kampers, T., Pangalos, M. N., Geerts, H., Wiech, H., & Mandelkow, E. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)00522-0 · Cited by 85 · see citing works

A Soluble Oligomer of Tau Associated with Fiber Formation Analyzed by NMR

Peterson, D. W., Zhou, H., Dahlquist, F. W., & Lew, J. (2008) · Biochemistry · doi:10.1021/bi702466a · Cited by 76 · see citing works

Analysis of Isoform-specific Tau Aggregates Suggests a Common Toxic Mechanism Involving Similar Pathological Conformations and Axonal Transport Inhibition

Cox, K. K., Combs, B., Abdelmesih, B., Morfini, G., Brady, S., & Kanaan, N. (2016) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2016.07.015 · Cited by 54 · see citing works

The active Hsc70/tau complex can be exploited to enhance tau turnover without damaging microtubule dynamics

Fontaine, S. N., Martin, M. D., Akoury, E., Assimon, V. A., Borysov, S. I., Nordhues, B. A., Sabbagh, J. J., Cockman, M., Gestwicki, J. E., Zweckstetter, M., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv135 · Cited by 38 · see citing works

Frontotemporal dementia with Parkinsonism linked to chromosome-17 mutations enhance tau oligomer formation

Maeda, S., Sato, Y., & Takashima, A. (2018) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2018.04.014 · Cited by 33 · see citing works

PHF and PHF-like fibrils –cause or consequence?

Ihara, Y. (2001) · Neurobiology of Aging · doi:10.1016/s0197-4580(00)00200-1 · Cited by 28 · see citing works

In Vivo Tau Imaging for a Diagnostic Platform of Tauopathy Using the rTg4510 Mouse Line

Sahara, N., Shimojo, M., Ono, M., Takuwa, H., Febo, M., Higuchi, M., & Suhara, T. (2017) · Frontiers in Neurology · doi:10.3389/fneur.2017.00663 · Cited by 11 · see citing works

Untitled work

(1997) · doi:10.1002/(sici)1097-4547(19970415)48:2

Senescence, brain inflammation, and oligomeric tau drive cognitive decline in Alzheimer's disease: Evidence from clinical and preclinical studies

Gaikwad, S., Senapati, S., Haque, M. A., & Kayed, R. (2024) · Alzheimer's &amp; Dementia · doi:10.1002/alz.13490 · Cited by 117 · see citing works

Novel Strategy for the Prevention of Recurrent Hypersensitivity Reactions to Radiocontrast Media Based on Skin Testing

Kwon, O. Y., Lee, J., Park, S., et al. (2019) · The Journal of Allergy and Clinical Immunology In Practice · doi:10.1016/j.jaip.2019.04.036 · Cited by 45 · see citing works

CULPRIT VERSUS CULPRIT AND NON- CULPRIT PRIMARY CORONARY REVASCULARIZATION

Saad, A. M. A., Hassanien, M., Farag, E.-S. M., et al. (2014) · Zagazig University Medical Journal · doi:10.21608/zumj.2014.4429

Case study on the evolution of hetero-oligomer interfaces based on the differences in paralogous proteins

Aoto, S., & Yura, K. (2015) · Biophysics and Physicobiology · doi:10.2142/biophysico.12.0_103 · Cited by 2 · see citing works

Solution Structure of Apoptotic BAX Oligomer: Oligomerization Likely Precedes Membrane Insertion

Sung, T.-C., Li, C.-Y., Lai, Y., et al. (2015) · Structure · doi:10.1016/j.str.2015.07.013 · Cited by 50 · see citing works

Ultrasound-assessed non-culprit and culprit coronary vessels differ by age and gender

Schoenenberger, A. W. (2013) · World Journal of Cardiology · doi:10.4330/wjc.v5.i3.42 · Cited by 16 · see citing works