Internalized Tau Oligomers Cause Neurodegeneration by Inducing Accumulation of Pathogenic Tau in Human Neurons Derived from Induced Pluripotent Stem Cells

LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing.

Kabeya, Y., Mizushima, N., Ueno, T., Yamamoto, A., Kirisako, T., Noda, T., Kominami, E., Ohsumi, Y., & Yoshimori, T. (2000) · The EMBO Journal · doi:10.1093/emboj/19.21.5720 · Cited by 6,605 · see citing works

Induction of the Vitamin D Receptor Attenuates Autophagy Dysfunction-Mediated Cell Death Following Traumatic Brain Injury

Cui, C., Cui, J., Jin, F., Cui, Y., Li, R., Jiang, X., Tian, Y., Wang, R. C., Jiang, P., & Gao, J. (2017) · Cellular Physiology and Biochemistry · doi:10.1159/000479571 · Cited by 5,214 · see citing works

Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis

Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · see citing works

Guidelines for the use and interpretation of assays for monitoring autophagy

Klionsky, D. J., Abdalla, F. C., Abeliovich, H., Abraham, R. T., Acevedo-Arozena, A., Adeli, K., Agholme, L., Agnello, M., Agostinis, P., Aguirre-Ghiso, J. A., et al. (2012) · Autophagy · doi:10.4161/auto.19496 · Cited by 3,996 · see citing works

Neurofibrillary tangles but not senile plaques parallel duration and severity of Alzheimer's disease

Arriagada, P. V., Growdon, J. H., Hedley-Whyte, E. T., & Hyman, B. T. (1992) · Neurology · doi:10.1212/wnl.42.3.631 · Cited by 2,668 · see citing works

Staging of alzheimer's disease-related neurofibrillary changes

Braak, H., & Braak, E. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00021-6 · Cited by 2,357 · see citing works

Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model

Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208 · see citing works

Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders

Ballatore, C., Lee, V. M.-Y., & Trojanowski, J. Q. (2007) · Nature Reviews Neuroscience · doi:10.1038/nrn2194 · Cited by 2,174 · 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

Self-propagation of pathogenic protein aggregates in neurodegenerative diseases

Jucker, M., & Walker, L. C. (2013) · Nature · doi:10.1038/nature12481 · Cited by 1,663 · see citing works

Propagation of Tau Pathology in a Model of Early Alzheimer's Disease

de Calignon, A., Polydoro, M., Suárez-Calvet, M., William, C., Adamowicz, D. H., Kopeikina, K. J., Pitstick, R., Sahara, N., Ashe, K. H., Carlson, G. A., et al. (2012) · Neuron · doi:10.1016/j.neuron.2011.11.033 · Cited by 1,427 · see citing works

[18] Quantification of β-sheet amyloid fibril structures with thioflavin T

LeVine, H. (1999) · Methods in Enzymology · doi:10.1016/s0076-6879(99)09020-5 · Cited by 1,365 · cited 3× · see citing works

Propagation of Tau Misfolding from the Outside to the Inside of a Cell

Frost, B., Jacks, R. L., & Diamond, M. I. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808759200 · Cited by 1,252 · see citing works

A microfluidic culture platform for CNS axonal injury, regeneration and transport

Taylor, A. M., Blurton-Jones, M. M., Rhee, S. W., Cribbs, D. H., Cotman, C. W., & Jeon, N. L. (2005) · Nature Methods · doi:10.1038/nmeth777 · Cited by 1,138 · see citing works

Mutation-Specific Functional Impairments in Distinct Tau Isoforms of Hereditary FTDP-17

Hong, M. (1998) · Science · doi:10.1126/science.282.5395.1914 · Cited by 1,003 · see citing works

Exosome-associated tau is secreted in tauopathy models and is selectively phosphorylated in cerebrospinal fluid in early Alzheimer disease

Saman, S., Kim, W., Raya, M., Visnick, Y., Miro, S., Saman, S., Jackson, B., McKee, A. C., Alvarez, V. E., Lee, N. C. Y., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.277061 · Cited by 985 · see citing works

Neuronal calcium mishandling and the pathogenesis of Alzheimer's disease

Bezprozvanny, I., & Mattson, M. P. (2008) · Trends in Neurosciences · doi:10.1016/j.tins.2008.06.005 · Cited by 938 · see citing works

Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds

Holmes, B. B., DeVos, S. L., Kfoury, N., Li, M., Jacks, R., Yanamandra, K., Ouidja, M. O., Brodsky, F. M., Marasa, J., Bagchi, D. P., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1301440110 · Cited by 859 · see citing works

Biochemistry and Cell Biology of Tau Protein in Neurofibrillary DegenerationPreprint

Mandelkow, E., & Mandelkow, E. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006247 · Cited by 839 · 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

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

Rapamycin alleviates toxicity of different aggregate-prone proteins

Berger, Z., Ravikumar, B., Menzies, F. M., Oroz, L. G., Underwood, B. R., Pangalos, M. N., Schmitt, I., Wullner, U., Evert, B. O., O'Kane, C. J., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddi458 · Cited by 657 · see citing works

Physiological release of endogenous tau is stimulated by neuronal activity

Pooler, A. M., Phillips, E. C., Lau, D. H. W., Noble, W., & Hanger, D. P. (2013) · The EMBO Reports · doi:10.1038/embor.2013.15 · Cited by 642 · 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

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

Trans-cellular Propagation of Tau Aggregation by Fibrillar Species

Kfoury, N., Holmes, B. B., Jiang, H., Holtzman, D. M., & Diamond, M. I. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.346072 · Cited by 552 · see citing works

Small Misfolded Tau Species Are Internalized via Bulk Endocytosis and Anterogradely and Retrogradely Transported in Neurons

Wu, J. W., Herman, M., Liu, L., Simoes, S., Acker, C. M., Figueroa, H., Steinberg, J. I., Margittai, M., Kayed, R., Zurzolo, C., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.394528 · Cited by 537 · 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

A Transgenic Alzheimer Rat with Plaques, Tau Pathology, Behavioral Impairment, Oligomeric Aβ, and Frank Neuronal Loss

Cohen, R. M., Rezai-Zadeh, K. P., Weitz, T. M., Rentsendorj, A., Gate, D., Spivak, I. E., Bholat, Y., Vasilevko, V., Glabe, C. G., Breunig, J. J., et al. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.3672-12.2013 · Cited by 522 · 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

The distribution of synapsin I and synaptophysin in hippocampal neurons developing in culture

Fletcher, T., Cameron, P. L., Camilli, P. V. D., & Banker, G. A. (1991) · Journal of Neuroscience · doi:10.1523/jneurosci.11-06-01617.1991 · Cited by 454 · 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

The dysregulation of intracellular calcium in Alzheimer disease

Supnet, C. B., & Борисович, Б. И. (2010) · Cell Calcium · doi:10.1016/j.ceca.2009.12.014 · Cited by 324 · 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

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

Conformation Determines the Seeding Potencies of Native and Recombinant Tau Aggregates

Falcon, B., Cavallini, A., Angers, R. C., Glover, S. J., Murray, T. K., Barnham, L., Jackson, S., O'Neill, M. J., Isaacs, A. M., Hutton, M. L., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589309 · Cited by 252 · see citing works

Constitutive secretion of tau protein by an unconventional mechanism

Chai, X., Dage, J. L., & Citron, M. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.05.021 · Cited by 224 · see citing works

Tau Trimers Are the Minimal Propagation Unit Spontaneously Internalized to Seed Intracellular Aggregation

Mirbaha, H., Holmes, B. B., Sanders, D. W., Bieschke, J., & Diamond, M. I. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.652693 · Cited by 215 · see citing works

The calpains in aging and aging-related diseases

Nixon, R. A. (2003) · Ageing Research Reviews · doi:10.1016/s1568-1637(03)00029-1 · Cited by 211 · see citing works

Fluorescence Polarization (FP) Assays for Monitoring Peptide‐Protein or Nucleic Acid‐Protein Binding

Moerke, N. J. (2009) · Current Protocols in Chemical Biology · doi:10.1002/9780470559277.ch090102 · Cited by 197 · see citing works

Characterization of Two VQIXXK Motifs for Tau Fibrillization in Vitro

Li, W., & Lee, V. M. ‐. (2006) · Biochemistry · doi:10.1021/bi061422+ · Cited by 197 · see citing works

Nonoverlapping but synergetic tau and APP pathologies in sporadic Alzheimer’s disease

Delacourte, A., Sergeant, N., Champain, D., Wattez, A., Maurage, C., Lebert, F., Pasquier, F., & David, J. (2002) · Neurology · doi:10.1212/wnl.59.3.398 · Cited by 168 · see citing works

Autophagy in Protein and Organelle TurnoverPreprint

Mizushima, N. (2011) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2011.76.011023 · Cited by 165 · see citing works

Proteostasis of tau. Tau overexpression results in its secretion via membrane vesicles

Simón, D., García‐García, E., Royo, F., Falcón‐Pérez, J. M., & Ávila, J. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.11.022 · Cited by 156 · see citing works

Paired Helical Filaments from Alzheimer Disease Brain Induce Intracellular Accumulation of Tau Protein in Aggresomes

Santa‐María, I., Varghese, M., Ksiȩżak-Reding, H., Dzhun, A., Wang, J., & Pasinetti, G. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.323279 · Cited by 140 · 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

Transgenic animal models of tauopathies

Lee, V. M. ‐., Kenyon, T. K., & Trojanowski, J. Q. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.014 · Cited by 134 · see citing works

Hippocampal Neurons Predisposed to Neurofibrillary Tangle Formation Are Enriched in Type II Calcium/Calmodulin-Dependent Protein Kinase

McKee, A. C., Kosik, K. S., Kennedy, M. B., & Kowall, N. W. (1990) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/00005072-199001000-00006 · Cited by 116 · see citing works

Neurofibrillary tangle‐like tau pathology induced by synthetic tau fibrils in primary neurons over‐expressing mutant tau

Guo, J., & Lee, V. M. ‐. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.051 · Cited by 113 · see citing works

Prevention of β-amyloid induced toxicity in human iPS cell-derived neurons by inhibition of Cyclin-dependent kinases and associated cell cycle events

Xu, X., Lei, Y., Luo, J., Wang, J., Zhang, S., Yang, X., Sun, M., Nuwaysir, E. F., Fan, G.-H., Zhao, J. Y., et al. (2012) · Stem Cell Research · doi:10.1016/j.scr.2012.11.005 · Cited by 112 · see citing works

Fluorescence Polarization: Past, Present and Future

Jameson, D., & Croney, J. C. (2003) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/138620703106298347 · Cited by 111 · see citing works

Quantification of Protein–Protein Interactions Using Fluorescence Polarization

Jameson, D. M., & Seifried, S. E. (1999) · Methods · doi:10.1006/meth.1999.0853 · Cited by 98 · see citing works

Tau aggregation in the hippocampal formation: an ageing or a pathological process?

Delacourte, A., Sergeant, N., Wattez, A., Maurage, C., Lebert, F., Pasquier, F., & David, J. (2002) · Experimental Gerontology · doi:10.1016/s0531-5565(02)00141-9 · Cited by 98 · see citing works

Promoting Autophagic Clearance: Viable Therapeutic Targets in Alzheimer's Disease

Friedman, L. G., Qureshi, Y. H., & Yu, W. H. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0320-z · Cited by 87 · see citing works

Cellular mechanisms of protein aggregate propagation

Holmes, B. B., & Diamond, M. I. (2012) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32835a3ee0 · Cited by 79 · see citing works

FTDP-17 Tau Mutations Induce Distinct Effects on Aggregation and Microtubule Interactions

Combs, B., & Gamblin, T. C. (2012) · Biochemistry · doi:10.1021/bi3010818 · Cited by 79 · see citing works

Rapamycin Ester Analog CCI-779/Temsirolimus Alleviates Tau Pathology and Improves Motor Deficit in Mutant Tau Transgenic Mice

Frédérick, C., Ando, K., Leroy, K., Héraud, C., Suain, V., Buée, L., & Brion, J. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142097 · Cited by 69 · see citing works

Intercellular transfer of tau aggregates and spreading of tau pathology: Implications for therapeutic strategies

Clavaguera, F., Grueninger, F., & Tolnay, M. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.08.037 · Cited by 60 · see citing works

Immunoassays with Direct Mass Spectrometric Detection

Nazabal, A., Wenzel, R. J., & Zenobi, R. (2006) · Analytical Chemistry · doi:10.1021/ac0519108 · Cited by 59 · see citing works

Characterizing Human Ion Channels in Induced Pluripotent Stem Cell–Derived Neurons

Haythornthwaite, A., Stoelzle, S., Hasler, A., Kiss, A., Mosbacher, J., George, M., Brüggemann, A., & Fertig, N. (2012) · SLAS DISCOVERY · doi:10.1177/1087057112457821 · Cited by 59 · see citing works

Thymoquinone protects cultured hippocampal and human induced pluripotent stem cells-derived neurons against α-synuclein-induced synapse damage

Alhebshi, A., Odawara, A., Gotoh, M., & Suzuki, I. (2013) · Neuroscience Letters · doi:10.1016/j.neulet.2013.09.049 · Cited by 56 · see citing works

Characteristics of the binding of thioflavin S to tau paired helical filaments

Santa‐María, I., Pérez, M., Hernández, F., Ávila, J., & Moreno, F. J. (2006) · Journal of Alzheimer s Disease · doi:10.3233/jad-2006-9307 · Cited by 53 · see citing works

Pharmacological characterisation of ligand- and voltage-gated ion channels expressed in human iPSC-derived forebrain neurons

Dage, J., Colvin, E. M., Fouillet, A., Langron, E., Roell, W., Li, J.-L., Mathur, S., Mogg, A., Schmitt, M. G., Felder, C., et al. (2014) · Psychopharmacology · doi:10.1007/s00213-013-3384-2 · Cited by 52 · see citing works

Reactivity and Applications of New Amine Reactive Cross-Linkers for Mass Spectrometric Detection of Protein−Protein Complexes

Bich, C., Mädler, S., Chiesa, K., Giacomo, F. D., Bogliotti, N., & Zenobi, R. (2009) · Analytical Chemistry · doi:10.1021/ac901651r · Cited by 43 · see citing works

Untitled work

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

NLRP3 inflammasome activation drives tau pathology

Ising, C., Venegas, C., Zhang, S., Scheiblich, H., Schmidt, S. V., Vieira-Saecker, A., Schwartz, S., Albasset, S., McManus, R. M., Tejera, D., et al. (2019) · Nature · doi:10.1038/s41586-019-1769-z · Cited by 1,487 · see citing works

Synergy between amyloid-β and tau in Alzheimer’s disease

Busche, M. A., & Hyman, B. T. (2020) · Nature Neuroscience · doi:10.1038/s41593-020-0687-6 · Cited by 1,242 · see citing works

Tau-targeting therapies for Alzheimer disease

Congdon, E. E., & Sigurdsson, E. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0013-z · Cited by 1,113 · see citing works

Propagation of Tau aggregates and neurodegeneration

Goedert, M., Eisenberg, D. S., & Crowther, R. A. (2017) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-072116-031153 · Cited by 632 · see citing works

Development of Multifunctional Molecules as Potential Therapeutic Candidates for Alzheimer’s Disease, Parkinson’s Disease, and Amyotrophic Lateral Sclerosis in the Last Decade

Savelieff, M. G., Nam, G., Kang, J., Lee, H. J., Lee, M., & Lim, M. H. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00138 · Cited by 603 · see citing works

LRP1 is a master regulator of tau uptake and spread

Rauch, J. N., Luna, G., Guzman, E., Audouard, M., Challis, C., Sibih, Y. E., Leshuk, C., Hernandez, I., Wegmann, S., Hyman, B. T., et al. (2020) · Nature · doi:10.1038/s41586-020-2156-5 · Cited by 541 · see citing works

Synaptic degeneration in Alzheimer disease

Tzioras, M., McGeachan, R. I., Durrant, C. S., & Spires-Jones, T. L. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-022-00749-z · Cited by 504 · see citing works

Tau molecular diversity contributes to clinical heterogeneity in Alzheimer’s disease

Dujardin, S., Commins, C., Lathuiliere, A., Beerepoot, P., Fernandes, A. R., Kamath, T. V., De Los Santos, M. B., Klickstein, N., Corjuc, D. L., Corjuc, B. T., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-0938-9 · Cited by 438 · see citing works

Amyloid-β and tau complexity — towards improved biomarkers and targeted therapies

Polanco, J. C., Li, C., Bodea, L., Martínez‐Mármol, R., Meunier, F. A., & Götz, J. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.162 · Cited by 374 · see citing works

Like prions: the propagation of aggregated tau and α-synuclein in neurodegeneration

Goedert, M., Masuda-Suzukake, M., & Falcon, B. (2017) · Brain · doi:10.1093/brain/aww230 · Cited by 323 · see citing works

A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration

Walsh, D. M., & Selkoe, D. J. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.13 · Cited by 290 · see citing works

Tau-based therapies in neurodegeneration: opportunities and challenges

Li, C., & Götz, J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.155 · Cited by 272 · see citing works

Enhanced tau aggregation in the presence of Amyloid β

Bennett, R. E., DeVos, S. L., Dujardin, S., Corjuc, B., Gor, R., Gonzalez, J., Roe, A. D., Frosch, M. P., Pitstick, R., Carlson, G. A., et al. (2017) · The American Journal of Pathology · doi:10.1016/j.ajpath.2017.03.011 · Cited by 245 · see citing works

Restoring hippocampal glucose metabolism rescues cognition across Alzheimer’s disease pathologies

Minhas, P. S., Jones, J. R., Latif‐Hernandez, A., Sugiura, Y., Durairaj, A. S., Wang, Q., Mhatre, S. D., Uenaka, T., Crapser, J. D., Conley, T. E., et al. (2024) · Science · doi:10.1126/science.abm6131 · Cited by 241 · see citing works

Tau Internalization is Regulated by 6-O Sulfation on Heparan Sulfate Proteoglycans (HSPGs)

Rauch, J. N., Chen, J. J., Sorum, A. W., Miller, G. M., Sharf, T., See, S. K., Hsieh-Wilson, L. C., Kampmann, M., & Kosik, K. S. (2018) · Scientific Reports · doi:10.1038/s41598-018-24904-z · Cited by 211 · see citing works

Four-repeat tauopathies

Rösler, T. W., Marvian, A. T., Brendel, M., Nykänen, N.-P., Höllerhage, M., Schwarz, S. C., Hopfner, F., Koeglsperger, T., Respondek, G., Schweyer, K., et al. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101644 · Cited by 219 · see citing works

Synaptic oligomeric tau in Alzheimer’s disease — A potential culprit in the spread of tau pathology through the brain

Colom‐Cadena, M., Davies, C., Sirisi, S., Lee, J., Simzer, E. M., Tzioras, M., Querol‐Vilaseca, M., Sánchez‐Aced, É., Chang, Y. Y., Holt, K., et al. (2023) · Neuron · doi:10.1016/j.neuron.2023.04.020 · Cited by 203 · see citing works

Three Dimensional Human Neuro-Spheroid Model of Alzheimer’s Disease Based on Differentiated Induced Pluripotent Stem Cells

Lee, H.-K., Velazquez Sanchez, C., Chen, M., Morin, P. J., Wells, J. M., Hanlon, E. B., & Xia, W. (2016) · PLOS ONE · doi:10.1371/journal.pone.0163072 · Cited by 190 · 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

Curcumin Inhibits Tau Aggregation and Disintegrates Preformed Tau Filaments in vitro

Rane, J. S., Bhaumik, P., & Panda, D. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170351 · Cited by 167 · see citing works

PrP is a central player in toxicity mediated by soluble aggregates of neurodegeneration-causing proteins

Corbett, G. T., Wang, Z., Hong, W., Colom‐Cadena, M., Rose, J. L., Liao, M., Asfaw, A., Hall, T. C., Ding, L., DeSousa, A., et al. (2019) · Acta Neuropathologica · doi:10.1007/s00401-019-02114-9 · Cited by 153 · see citing works

Tau-mediated synaptic and neuronal dysfunction in neurodegenerative disease

Tracy, T. E., & Gan, L. (2018) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2018.04.027 · Cited by 147 · see citing works

Linking deregulation of non-coding RNA to the core pathophysiology of Alzheimer’s disease: An integrative review

Millan, M. J. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.03.004 · Cited by 146 · see citing works

Stem cell models of Alzheimer’s disease: progress and challenges

Arber, C., Lovejoy, C., & Wray, S. (2017) · Alzheimer's Research & Therapy · doi:10.1186/s13195-017-0268-4 · Cited by 143 · see citing works

Role of Aβ in Alzheimer’s-related synaptic dysfunction

Zhang, H., Jiang, X., Ma, L., Wei, W., Li, Z., Chang, S., Wen, J., Sun, J., & Li, H. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.964075 · Cited by 144 · see citing works

In vitro prion-like behaviour of TDP-43 in ALS

Smethurst, P., Newcombe, J., Troakes, C., Simone, R., Chen, Y., Patani, R., & Sidle, K. C. L. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.08.007 · Cited by 139 · see citing works

Tau Oligomers Neurotoxicity

Niewiadomska, G., Niewiadomski, W., Steczkowska, M., & Gąsiorowska, A. (2021) · Life · doi:10.3390/life11010028 · Cited by 132 · see citing works

Neuropathogenesis-on-chips for neurodegenerative diseases

Amartumur, S., Nguyen, H. M., Huynh, T., Kim, T. S., Woo, R., Oh, E., Kim, K. K., Lee, L. P., & Heo, C. (2024) · Nature Communications · doi:10.1038/s41467-024-46554-8 · Cited by 120 · see citing works

Synaptic tau: A pathological or physiological phenomenon?

Robbins, M., Clayton, E. L., & Schierle, G. S. K. (2021) · Acta Neuropathologica Communications · doi:10.1186/s40478-021-01246-y · Cited by 117 · see citing works

Internalization mechanisms of brain-derived tau oligomers from patients with Alzheimer’s disease, progressive supranuclear palsy and dementia with Lewy bodies

Puangmalai, N., Bhatt, N. N., Montalbano, M., Sengupta, U., Gaikwad, S., Ventura, F. L., McAllen, S., Ellsworth, A., García, S., & Kayed, R. (2020) · Cell Death and Disease · doi:10.1038/s41419-020-2503-3 · Cited by 110 · see citing works

Galectin-8–mediated selective autophagy protects against seeded tau aggregation

Falcon, B., Noad, J., McMahon, H. T., Randow, F., & Goedert, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.809293 · Cited by 109 · see citing works

Advances in microfluidic in vitro systems for neurological disease modeling

Holloway, P. M., Willaime‐Morawek, S., Siow, R. C. M., Barber, M., Owens, R. M., Sharma, A. D., Rowan, W. C., Hill, E. J., & Zagnoni, M. (2021) · Journal of Neuroscience Research · doi:10.1002/jnr.24794 · Cited by 101 · see citing works

Tau physiology and pathomechanisms in frontotemporal lobar degeneration

Bodea, L., Eckert, A., Ittner, L. M., Piguet, O., & Götz, J. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13600 · Cited by 104 · see citing works

Possible Mechanisms of Tau Spread and Toxicity in Alzheimer’s Disease

Zhang, H., Cao, Y., Ma, L., Wei, Y., & Li, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.707268 · Cited by 104 · see citing works

Pathological Changes of Tau Related to Alzheimer’s Disease

Chu, D., & Liu, F. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00457 · Cited by 103 · see citing works

Tau in neurodegenerative diseases: molecular mechanisms, biomarkers, and therapeutic strategies

Zhang, X., Wang, J., Zhang, Z., & Ye, K. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00429-6 · Cited by 106 · see citing works

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 · see citing works

Research Progress on Alzheimer's Disease and Resveratrol

Yan, Y., Yang, H., Xie, Y., Ding, Y., Kong, D., & Yu, H. (2020) · Neurochemical Research · doi:10.1007/s11064-020-03007-0 · Cited by 91 · see citing works

Calcium dysregulation contributes to neurodegeneration in FTLD patient iPSC-derived neurons

Imamura, K., Sahara, N., Kanaan, N. M., Tsukita, K., Kondo, T., Kutoku, Y., Ohsawa, Y., Sunada, Y., Kawakami, K., Hotta, A., et al. (2016) · Scientific Reports · doi:10.1038/srep34904 · Cited by 84 · see citing works

Neuroprotective astrocyte-derived insulin/insulin-like growth factor 1 stimulates endocytic processing and extracellular release of neuron-bound Aβ oligomers

Pitt, J. E., Wilcox, K. C., Tortelli, V., Diniz, L. P., Oliveira, M. S., Dobbins, C., Yu, X., Nandamuri, S., Gomes, F. C. A., DiNunno, N., et al. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0416 · Cited by 86 · see citing works

Human pluripotent stem cell–derived models and drug screening in CNS precision medicine

Silva, M. C., & Haggarty, S. J. (2019) · Annals of the New York Academy of Sciences · doi:10.1111/nyas.14012 · Cited by 82 · see citing works

Tau prion-like propagation: state of the art and current challenges

Dujardin, S., & Hyman, B. T. (2019) · Advances in Experimental Medicine and Biology · doi:10.1007/978-981-32-9358-8_23 · Cited by 84 · see citing works

Alzheimer’s-like pathology in aging rhesus macaques: Unique opportunity to study the etiology and treatment of Alzheimer’s disease

Arnsten, A. F. T., Datta, D., Leslie, S., Yang, S.-T., Wang, M., & Nairn, A. C. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1903671116 · Cited by 74 · see citing works

Extracellular Tau Oligomers Induce Invasion of Endogenous Tau into the Somatodendritic Compartment and Axonal Transport Dysfunction

Swanson, E., Breckenridge, L., McMahon, L. P., Som, S., McConnell, I., & Bloom, G. S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170168 · Cited by 73 · see citing works

Tau-mediated Neurodegeneration and Potential Implications in Diagnosis and Treatment of Alzheimer's Disease

Wu, X., Piña-Crespo, J., Zhang, Y., Chen, X., & Xu, H. (2017) · Chinese Medical Journal · doi:10.4103/0366-6999.220313 · Cited by 79 · see citing works

Vectored Intracerebral Immunization with the Anti-Tau Monoclonal Antibody PHF1 Markedly Reduces Tau Pathology in Mutant Tau Transgenic Mice

Liu, W., Zhao, L., Blackman, B. A., Parmar, M. S., Wong, M. Y., Woo, T., Yu, F., Chiuchiolo, M. J., Sondhi, D., Kaminsky, S. M., et al. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2016-16.2016 · Cited by 68 · see citing works

The Role of P2X7 Receptor in Alzheimer’s Disease

Francistiová, L., Bianchi, C., Lauro, C. D., Sebastián‐Serrano, Á., de Diego-García, L., Kobolák, J., Dinnyés, A., & Dı́az-Hernández, M. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00094 · Cited by 69 · see citing works

Toxic Tau Oligomers Modulated by Novel Curcumin Derivatives

Cascio, F. L., Puangmalai, N., Ellsworth, A., Bucchieri, F., Pace, A., Piccionello, A. P., & Kayed, R. (2019) · Scientific Reports · doi:10.1038/s41598-019-55419-w · Cited by 71 · see citing works

Lysine 63-linked ubiquitination of tau oligomers contributes to the pathogenesis of Alzheimer’s disease

Puangmalai, N., Sengupta, U., Bhatt, N., Gaikwad, S., Montalbano, M., Bhuyan, A., Garcia, S., McAllen, S., Sonawane, M., Jerez, C., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101766 · Cited by 68 · see citing works

Computational modeling of tau pathology spread reveals patterns of regional vulnerability and the impact of a genetic risk factor

Cornblath, E. J., Li, H. L., Changolkar, L., Zhang, B., Brown, H. J., Gathagan, R. J., Olufemi, M. F., Trojanowski, J. Q., Bassett, D. S., Lee, V. M. Y., et al. (2021) · Science Advances · doi:10.1126/sciadv.abg6677 · Cited by 66 · see citing works

Human cyclophilin 40 unravels neurotoxic amyloids

Baker, J. D., Shelton, L. B., Zheng, D., Favretto, F., Nordhues, B. A., Darling, A. L., Sullivan, L. E., Sun, Z., Solanki, P. K., Martin, M. D., et al. (2017) · PLoS Biology · doi:10.1371/journal.pbio.2001336 · Cited by 63 · see citing works

Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target

Oakley, S. S., Maina, M. B., Marshall, K. E., Al‐Hilaly, Y. K., Harrington, C., Wischik, C. M., & Serpell, L. C. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590754 · Cited by 57 · see citing works

The Amyloid-Beta Clearance: From Molecular Targets to Glial and Neural Cells

Cai, W., Wu, T., & Chen, N. (2023) · Biomolecules · doi:10.3390/biom13020313 · Cited by 65 · 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

Advancing drug discovery for neuropsychiatric disorders using patient-specific stem cell models

Haggarty, S. J., Silva, M. C., Cross, A. J., Brandon, N. J., & Perlis, R. H. (2016) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2016.01.011 · Cited by 56 · see citing works

Modeling neurodegenerative diseases with cerebral organoids and other three-dimensional culture systems: focus on Alzheimer’s disease

Venkataraman, L., Fair, S. R., McElroy, C. A., Hester, M. E., & Fu, H. (2020) · Stem Cell Reviews and Reports · doi:10.1007/s12015-020-10068-9 · Cited by 54 · see citing works

Alzheimer’s disease and related tauopathies: disorders of disrupted neuronal identity

Frost, B. E. (2023) · Trends in Neurosciences · doi:10.1016/j.tins.2023.07.006 · Cited by 56 · see citing works

Extracellular truncated tau causes early presynaptic dysfunction associated with Alzheimer’s disease and other tauopathies

Florenzano, F., Corsetti, V., Ciasca, G., Ciotti, M. T., Pittaluga, A., Olivero, G., Feligioni, M., Iannuzzi, F., Latina, V., Sciacca, M. F. M., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.17371 · Cited by 52 · see citing works

Prospects for strain-specific immunotherapy in Alzheimer’s disease and tauopathies

Bittar, A., Sengupta, U., & Kayed, R. (2018) · npj Vaccines · doi:10.1038/s41541-018-0046-8 · Cited by 50 · see citing works

Inhibition of Death-associated Protein Kinase 1 Attenuates Cis P-tau and Neurodegeneration in Traumatic Brain Injury

Kim, N., Wang, B., Koikawa, K., Nezu, Y., Qiu, C., Lee, T., & Zhou, X.-Z. (2021) · Progress in neurobiology · doi:10.1016/j.pneurobio.2021.102072 · Cited by 43 · see citing works

Induced pluripotent stem cell-based organ-on-a-chip as personalized drug screening tools: A focus on neurodegenerative disorders

Fanizza, F., Campanile, M., Forloni, G., Giordano, C., & Albani, D. (2022) · Journal of Tissue Engineering · doi:10.1177/20417314221095339 · Cited by 51 · see citing works

Stretch Injury of Human Induced Pluripotent Stem Cell Derived Neurons in a 96 Well Format

Sherman, S. A., Phillips, J. K., Costa, J. T., Cho, F. S., Oungoulian, S. R., & Finan, J. D. (2016) · Scientific Reports · doi:10.1038/srep34097 · Cited by 47 · see citing works

Quantitative super-resolution imaging of pathological aggregates reveals distinct toxicity profiles in different synucleinopathies

Morten, M. J., Sirvio, L., Rupawala, H., Hayes, E. M., Franco, A., Radulescu, C. I., Ying, L., Barnes, S. J., Muga, A., & Ye, Y. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2205591119 · Cited by 43 · see citing works

Nasal tau immunotherapy clears intracellular tau pathology and improves cognitive functions in aged tauopathy mice

Gaikwad, S., Puangmalai, N., Sonawane, M., Montalbano, M., Price, R., Iyer, M. S., Ray, A., Moreno, S., & Kayed, R. (2024) · Science Translational Medicine · doi:10.1126/scitranslmed.adj5958 · Cited by 46 · see citing works

Stress-Induced Synaptic Dysfunction and Neurotransmitter Release in Alzheimer’s Disease: Can Neurotransmitters and Neuromodulators be Potential Therapeutic Targets?

Jha, S. K., Jha, N. K., Kumar, D., Sharma, R., Shrivastava, A., Ambasta, R. K., & Kumar, P. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-160623 · Cited by 46 · see citing works

Distribution of tau hyperphosphorylation in canine dementia resembles early Alzheimer’s disease and other tauopathies

Abey, A. S., Davies, D., Goldsbury, C. S., Buckland, M. E., Valenzuela, M., & Duncan, T. (2020) · Brain Pathology · doi:10.1111/bpa.12893 · Cited by 46 · see citing works

Tau internalization: A complex step in tau propagation

Zhao, J., Wu, H., & Tang, X. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101272 · Cited by 46 · see citing works

Tau Oligomer Pathology in Nucleus Basalis Neurons During the Progression of Alzheimer Disease

Tiernan, C. T., Mufson, E. J., Kanaan, N. M., & Counts, S. (2018) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/nlx120 · Cited by 45 · see citing works

The prion-like transmission of tau oligomers via exosomes

Jackson, N. A., Guerrero‐Munoz, M. J., & Castillo‐Carranza, D. L. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.974414 · Cited by 44 · see citing works

Focused ultrasound as a novel strategy for Alzheimer disease therapeutics

Meng, Y., Volpini, M., Black, S. E., Lozano, A. M., Hynynen, K., & Lipsman, N. (2017) · Annals of Neurology · doi:10.1002/ana.24933 · Cited by 44 · see citing works

Astrocytic uptake of neuronal corpses promotes cell‐to‐cell spreading of tau pathology

Mothes, T., Portal, B., Konstantinidis, E., Eltom, K., Libard, S., Streubel-Gallasch, L., Ingelsson, M., Rostami, J., Lindskog, M., & Erlandsson, A. (2023) · Acta Neuropathologica Communications · doi:10.1186/s40478-023-01589-8 · Cited by 43 · see citing works

siRNA drug delivery across the blood–brain barrier in Alzheimer's disease

Sajid, M. I., Sheikh, F. S., Anis, F., Nasim, N., Sumbria, R. K., Nauli, S. M., & Tiwari, R. K. (2023) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2023.114968 · Cited by 45 · see citing works

Understanding the Pathophysiological Actions of Tau Oligomers: A Critical Review of Current Electrophysiological Approaches

Hill, E., Wall, M. J., Moffat, K. G., & Karikari, T. K. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00155 · Cited by 42 · see citing works

Human iPSC application in Alzheimer’s disease and tau-related neurodegenerative diseases

TCW, J. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.01.043 · Cited by 39 · see citing works

Distinct Conformations, Aggregation and Cellular Internalization of Different Tau Strains

Karikari, T. K., Nagel, D. A., Grainger, A. I., Clarke-Bland, C., Crowe, J. A., Hill, E. J., & Moffat, K. G. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00296 · Cited by 39 · see citing works

Single cell transcriptomic profiling of a neuron-astrocyte assembloid tauopathy model

Rickner, H., Jiang, L., Hong, R., O’Neill, N. K., Mojica, C. A., Snyder, B. J., Zhang, L., Shaw, D., Medalla, M., Wolozin, B. L., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-34005-1 · Cited by 41 · see citing works

Harnessing cerebral organoids for Alzheimer's disease research

Bubnys, A., & Tsai, L. (2021) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2021.10.003 · Cited by 39 · see citing works

Near Infrared Light Treatment Reduces Synaptic Levels of Toxic Tau Oligomers in Two Transgenic Mouse Models of Human Tauopathies

Comerota, M. M., Tumurbaatar, B., Krishnan, B., Kayed, R., & Taglialatela, G. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-1248-9 · Cited by 37 · see citing works

Current and future applications of induced pluripotent stem cell-based models to study pathological proteins in neurodegenerative disorders

Jacquet, A. D. R., Denis, H. L., Cicchetti, F., & Alpaugh, M. (2021) · Molecular Psychiatry · doi:10.1038/s41380-020-00999-7 · Cited by 35 · see citing works

Astrocytic expression of the Alzheimer’s disease risk allele, ApoEε4, potentiates neuronal tau pathology in multiple preclinical models

Jablonski, A. M., Warren, L., Usenovic, M., Zhou, H. H., Sugam, J. A., Parmentier‐Batteur, S., & Voleti, B. (2021) · Scientific Reports · doi:10.1038/s41598-021-82901-1 · Cited by 35 · see citing works

In vivo coupling of dendritic complexity with presynaptic density in primary tauopathies

Mak, E., Holland, N., Jones, P. S., Savulich, G., Low, A., Malpetti, M., Kaalund, S. S., Passamonti, L., Rittman, T., Romero-García, R., et al. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.01.016 · Cited by 38 · see citing works

Modeling Neurodegenerative Diseases Using In Vitro Compartmentalized Microfluidic Devices

Miny, L., Maisonneuve, B. G. C., Quadrio, I., & Honegger, T. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.919646 · Cited by 36 · see citing works

Antioxidants reduce neurodegeneration and accumulation of pathologic Tau proteins in the auditory system after blast exposure

Du, X., West, M., Cai, Q., Cheng, W., Ewert, D. L., Li, W., Floyd, R. A., & Kopke, R. D. (2017) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2017.04.343 · Cited by 36 · see citing works

Quantitative propagation of assembled human Tau from Alzheimer's disease brain in microfluidic neuronal cultures

Katsikoudi, A., Ficulle, E., Cavallini, A., Sharman, G. J., Guyot, A., Zagnoni, M., Eastwood, B. J., Hutton, M. L., & Bose, S. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013325 · Cited by 35 · see citing works

Curcumin as Scaffold for Drug Discovery against Neurodegenerative Diseases

Cascio, F. L., Marzullo, P., Kayed, R., & Piccionello, A. P. (2021) · Biomedicines · doi:10.3390/biomedicines9020173 · Cited by 37 · see citing works

Tau proteinopathies and the prion concept

(2020) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2020.08.003 · Cited by 38 · see citing works

Aggregation, Transmission, and Toxicity of the Microtubule-Associated Protein Tau: A Complex Comprehension

Hu, J., Sha, W., Yuan, S., Wu, J., & Huang, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241915023 · Cited by 35 · see citing works

NMR Meets Tau: Insights into Its Function and Pathology

Lippens, G. M., Landrieu, I., Smet‐Nocca, C., Huvent, I., Gandhi, N. S., Gigant, B., Despres, C., Qi, H., & Lopez, J. M. (2016) · Biomolecules · doi:10.3390/biom6020028 · Cited by 34 · see citing works

Microfluidic approaches for probing amyloid assembly and behaviour

Herling, T. W., Levin, A., Saar, K. L., Dobson, C. M., & Knowles, T. P. J. (2018) · Lab on a Chip · doi:10.1039/c7lc01241a · Cited by 33 · see citing works

Uncovering specificity of endogenous TAU aggregation in a human iPSC-neuron TAU seeding model

Manos, J. D., Preiss, C. N., Venkat, N., Tamm, J. A., Reinhardt, P., Kwon, T., Wu, J., Winter, A. D., Jahn, T. R., Yanamandra, K., et al. (2021) · iScience · doi:10.1016/j.isci.2021.103658 · Cited by 33 · see citing works

“Prion-like” seeding and propagation of oligomeric protein assemblies in neurodegenerative disorders

Zampar, S., Gregorio, S. E. D., Grimmer, G., Watts, J. C., & Ingelsson, M. (2024) · Frontiers in Neuroscience · doi:10.3389/fnins.2024.1436262 · Cited by 34 · see citing works

Progressing neurobiological strategies against proteostasis failure: Challenges in neurodegeneration

Amanullah, A., Upadhyay, A., Joshi, V., Mishra, R., Jana, N. R., & Mishra, A. (2017) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2017.08.005 · Cited by 33 · see citing works

Pharmacological Modulators of Tau Aggregation and Spreading

Dominguez‐Meijide, A., Vasili, E., & Outeiro, T. F. (2020) · Brain Sciences · doi:10.3390/brainsci10110858 · Cited by 34 · see citing works

Alzheimer’s Disease (AD) Therapeutics—2: Beyond Amyloid—Re-Defining AD and Its Causality to Discover Effective Therapeutics

Mullane, K., & Williams, M. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.09.027 · Cited by 32 · see citing works

Preparation of stable tau oligomers for cellular and biochemical studies

Karikari, T. K., Nagel, D. A., Grainger, A. I., Clarke-Bland, C., Hill, E. J., & Moffat, K. G. (2018) · Analytical Biochemistry · doi:10.1016/j.ab.2018.10.013 · Cited by 32 · see citing works

Visualization of soluble tau oligomers in TauP301L-BiFC transgenic mice demonstrates the progression of tauopathy

Shin, S., Kim, D., Song, J. Y., Jeong, H., Hyeon, S. J., Kowall, N. W., Ryu, H., Pae, A. N., Lim, S., & Kim, Y. K. (2020) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2020.101782 · Cited by 29 · see citing works

Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease

Abskharon, R. N. N., Seidler, P. M., Sawaya, M. R., Cascio, D., Yang, T. P., Philipp, S., Williams, C. K., Newell, K. L., Ghetti, B. F., Deture, M. A., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013638 · Cited by 31 · see citing works

Compartmentalized Signaling in Aging and Neurodegeneration

Benedetto, G. D., Iannucci, L. F., Surdo, N. C., Zanin, S., Conca, F., Grisan, F., Gerbino, A., & Lefkimmiatis, K. (2021) · Cells · doi:10.3390/cells10020464 · Cited by 29 · see citing works

The Significance of NLRP Inflammasome in Neuropsychiatric Disorders

Shen, Y., Qian, L., Luo, H., Li, X., Ruan, Y., Fan, R., Si, Z., Chen, Y.-P., Li, L., & Liu, Y. (2022) · Brain Sciences · doi:10.3390/brainsci12081057 · Cited by 31 · see citing works

Transcellular Spreading of Tau in Tauopathies

Demaegd, K. C., Schymkowitz, J. W. H., & Rousseau, F. (2018) · ChemBioChem · doi:10.1002/cbic.201800288 · Cited by 30 · see citing works

P3‐006: Models of tau pathology in induced pluripotent stem cell‐derived human neurons

Usenovic, M., Niroomand, S., Schachter, J. B., Zhou, H. H., Renger, J. J., & Parmentier‐Batteur, S. (2015) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2015.06.872

Extracellular Tau Oligomers Induce Disruption of Endogenous Tau Distribution, Invasion of Tau into the Somatodendritic Compartment and Axonal Transport Dysfunction

Swanson, E. C. (2017) · doi:10.18130/v3p643

Extracellular Tau Oligomers Induce Invasion of Endogenous Tau into the Somatodendritic Compartment and Axonal Transport Dysfunction

Swanson, E., Breckenridge, L., McMahon, L. P., Som, S., McConnell, I., & Bloom, G. S. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170168 · Cited by 73 · see citing works

Continuous Monitoring of Tau-Induced Neurotoxicity in Patient-Derived iPSC-Neurons

Oakley, D. H., Klickstein, N., Commins, C., Chung, M., Dujardin, S., Bennett, R. E., Hyman, B. T., & Frosch, M. P. (2021) · The Journal of Neuroscience · doi:10.1523/jneurosci.2590-20.2021 · Cited by 18 · see citing works

Dual Mechanism of Toxicity for Extracellular Injection of Tau Oligomers versus Monomers in Human Tau Mice

Manassero, G., Guglielmotto, M., Monteleone, D., Vasciaveo, V., Butenko, O., Tamagno, E., Arancio, O., & Tabaton, M. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170298 · Cited by 18 · see citing works