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

Triple-Transgenic Model of Alzheimer’s Disease with Plaques and Tangles

Oddo, S., Caccamo, A., Shepherd, J. D., Murphy, M. P., Golde, T. E., Kayed, R., Metherate, R., Mattson, M. P., Akbari, Y., & LaFerla, F. M. (2003) · Neuron · doi:10.1016/s0896-6273(03)00434-3 · Cited by 4,126

Protein aggregation and neurodegenerative disease

Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454

The blood-brain barrier: Bottleneck in brain drug development

Pardridge, W. M. (2005) · NeuroRX · doi:10.1602/neurorx.2.1.3 · Cited by 2,798

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

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

Tau protein isoforms, phosphorylation and role in neurodegenerative disorders11These authors contributed equally to this work.

Buée, L., Bussière, T., Buée‐Scherrer, V., Delacourte, A., & Hof, P. R. (2000) · Brain Research Reviews · doi:10.1016/s0165-0173(00)00019-9 · Cited by 2,142

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

Reducing Endogenous Tau Ameliorates Amyloid ß-Induced Deficits in an Alzheimer's Disease Mouse Model

Roberson, E. D., Scearce-Levie, K., Palop, J. J., Yan, F., Cheng, I. H., Wu, T., Gerstein, H., Yu, G.-Q., & Mucke, L. (2007) · Science · doi:10.1126/science.1141736 · Cited by 1,892

Oxidative stress in neurodegeneration: Cause or consequence?

Andersen, J. K. (2004) · Nature Medicine · doi:10.1038/nrn1434 · Cited by 1,869

The distribution of tau in the mammalian central nervous system.

Binder, L. I., Frankfurter, A., & Rebhun, L. I. (1985) · The Journal of cell biology · doi:10.1083/jcb.101.4.1371 · Cited by 1,588

Developing therapeutic approaches to tau, selected kinases, and related neuronal protein targets

Lee, V. M.-Y., Brunden, K. R., Hutton, M., & Trojanowski, J. Q. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006437 · Cited by 122

AZD 1080, a novel GSK 3 inhibitor, rescues synaptic plasticity deficits in rodent brain and exhibits peripheral target engagement in humans

Georgievska, B., Sandin, J., Doherty, J., Mörtberg, A., Neelissen, J. A. M., Andersson, A., Gruber, S. H. M., Nilsson, Y., Schött, P. A., Arvidsson, P. I., et al. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12203 · Cited by 124

Inflammation and Anti-Inflammatory Strategies for Alzheimer’s Disease – A Mini-Review

McNaull, B., Todd, S., McGuinness, B., & Passmore, A. (2009) · Gerontology · doi:10.1159/000237873 · Cited by 120

A novel DYRK1A (Dual specificity tyrosine phosphorylation‐regulated kinase 1A) inhibitor for the treatment of Alzheimer's disease: effect on Tau and amyloid pathologies in vitro

Coutadeur, S., Benyamine, H., Delalonde, L., de Oliveira, C., Leblond, B., Foucourt, A., Besson, T., Casagrande, A.-S., Taverne, T., Girard, A., et al. (2014) · Journal of Neurochemistry · doi:10.1111/jnc.13018 · Cited by 121

Toxicity mechanisms of arsenic that are shared with neurodegenerative diseases and cognitive impairment: Role of oxidative stress and inflammatory responses

Escudero‐Lourdes, C. (2016) · NeuroToxicology · doi:10.1016/j.neuro.2016.02.002 · Cited by 124

The Role of Microglia in the Spread of Tau: Relevance for Tauopathies

Perea, J. R., Llorens-Martín, M., Ávila, J., & Bolós, M. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00172 · Cited by 129

Human Tau Isoforms Assemble into Ribbon-like Fibrils That Display Polymorphic Structure and Stability

Wegmann, S., Jung, Y. J., Chinnathambi, S., Mandelkow, E., Mandelkow�, E., & Müller, D. J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145318 · Cited by 129

The Role of Tau Oligomers in the Onset of Alzheimer's Disease Neuropathology

Cárdenas-Aguayo, M. D. C., Gómez-Virgilio, L., DeRosa, S., & Meraz-Ríos, M. A. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500148z · Cited by 120

Zinc promotes liquid–liquid phase separation of tau protein

Singh, V. P., Xu, L., Boyko, S., Surewicz, K. A., & Surewicz, W. K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ac120.013166 · Cited by 122

TOR on the brain

Garelick, M. G., & Kennedy, B. K. (2010) · Experimental Gerontology · doi:10.1016/j.exger.2010.08.030 · Cited by 120

The Human Tau Interactome: Binding to the Ribonucleoproteome, and Impaired Binding of the Proline-to-Leucine Mutant at Position 301 (P301L) to Chaperones and the Proteasome

Gunawardana, C. G., Mehrabian, M., Wang, X., Mueller, I., Lubambo, I., Jonkman, J. E. N., Wang, H., & Schmitt‐Ulms, G. (2015) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m115.050724 · Cited by 127

The Microtubule-Associated Protein Tau Mediates the Organization of Microtubules and Their Dynamic Exploration of Actin-Rich Lamellipodia and Filopodia of Cortical Growth Cones

Biswas, S., & Kalil, K. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.2281-17.2017 · Cited by 133

Temsirolimus attenuates tauopathy in vitro and in vivo by targeting tau hyperphosphorylation and autophagic clearance

Jiang, T., Yu, J., Zhu, X., Zhang, Q.-Q., Cao, L., Wang, H.-F., Tan, M., Gao, Q., Qin, H., Zhang, Y., et al. (2014) · Neuropharmacology · doi:10.1016/j.neuropharm.2014.05.032 · Cited by 118

Functional Implications of Glycogen Synthase Kinase‐3‐Mediated Tau Phosphorylation

Hanger, D. P., & Noble, W. J. (2011) · International Journal of Alzheimer s Disease · doi:10.4061/2011/352805 · Cited by 124

Tau directs intracellular trafficking by regulating the forces exerted by kinesin and dynein teams

Chaudhary, A. R., Berger, F., Berger, C. L., & Hendricks, A. G. (2018) · Traffic · doi:10.1111/tra.12537 · Cited by 118

LRP-1 and LRP-2 receptors function in the membrane neuron. Trafficking mechanisms and proteolytic processing in Alzheimer's disease

Spuch, C., Ortolano, S., & Navarro, C. (2012) · Frontiers in Physiology · doi:10.3389/fphys.2012.00269 · Cited by 107

Cerebrospinal fluid lactate levels and brain [18F]FDG PET hypometabolism within the default mode network in Alzheimer’s disease

Liguori, C., Chiaravalloti, A., Sancesario, G., Stefani, A., Sancesario, G. M., Mercuri, N. B., Schillaci, O., & Pierantozzi, M. (2016) · European Journal of Nuclear Medicine and Molecular Imaging · doi:10.1007/s00259-016-3417-2 · Cited by 117

Mitochondrial hyperpolarization in iPSC-derived neurons from patients of FTDP-17 with 10+16 MAPT mutation leads to oxidative stress and neurodegeneration

Esteras, N., Rohrer, J. D., Hardy, J., Wray, S., & Abramov, A. Y. (2017) · Redox Biology · doi:10.1016/j.redox.2017.03.008 · Cited by 120

Silent Allosteric Modulation of mGluR5 Maintains Glutamate Signaling while Rescuing Alzheimer’s Mouse Phenotypes

Haas, L. T., Salazar, S. V., Smith, L. M., Zhao, H. R., Cox, T. O., Herber, C. S., Degnan, A. P., Balakrishnan, A. S., Macor, J. E., Albright, C. F., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.06.023 · Cited by 121

Association between chronic stress and Alzheimer’s disease: Therapeutic effects of Saffron

Saeedi, M., & Rashidy‐Pour, A. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110995 · Cited by 123

Histone Acetylation Modifiers in the Pathogenesis of Alzheimer’s Disease

Lu, X., Wang, L., Yu, C., Yu, D., & Yu, G. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00226 · Cited by 124

Increased Tau Phosphorylation and Impaired Brain Insulin/IGF Signaling in Mice Fed a High Fat/High Cholesterol Diet

Bhat, N. R., & Thirumangalakudi, L. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121030 · Cited by 119

Recent therapeutic strategies targeting beta amyloid and tauopathies in Alzheimer's disease

Madav, Y., Wairkar, S., & Prabhakar, B. R. (2019) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2019.01.004 · Cited by 122

Curcumin activates Wnt/β-catenin signaling pathway through inhibiting the activity of GSK-3β in APPswe transfected SY5Y cells

Zhang, X., Yin, W., Shi, X.-D., & Li, Y. (2011) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2011.02.009 · Cited by 116

Contribution of astrocytes to neuropathology of neurodegenerative diseases

Acıoğlu, Ç., Li, L., & Elkabes, S. (2021) · Brain Research · doi:10.1016/j.brainres.2021.147291 · Cited by 119

Extracellular Monomeric Tau Is Internalized by Astrocytes

Perea, J. R., López, E., Díez-Ballesteros, J. C., Ávila, J., Hernández, F., & Bolós, M. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00442 · Cited by 114

Brain site-specific proteome changes in aging-related dementia

Manavalan, A., Mishra, M., Feng, L., Sze, S. K., Akatsu, H., & Heese, K. (2013) · Experimental & Molecular Medicine · doi:10.1038/emm.2013.76 · Cited by 115

Hesperidin Alleviates Cognitive Impairment, Mitochondrial Dysfunction and Oxidative Stress in a Mouse Model of Alzheimer’s Disease

Wang, D., Liu, L., Zhu, X., Wu, W., & Wang, Y. (2014) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-014-0098-x · Cited by 114

The neuritic plaque facilitates pathological conversion of tau in an Alzheimer’s disease mouse model

Li, T., Braunstein, K. E., Zhang, J., Lau, A., Sibener, L., Deeble, C., & Wong, P. C. (2016) · Nature Communications · doi:10.1038/ncomms12082 · Cited by 114

Selenium, selenoprotein P, and Alzheimer's disease: is there a link?

Solovyev, N. D., Drobyshev, E. J., Bjørklund, G., Dubrovskii, Y. A., Lysiuk, R., & Rayman, M. P. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.02.030 · Cited by 117

Design, synthesis and structure–activity relationships of 1,3,4-oxadiazole derivatives as novel inhibitors of glycogen synthase kinase-3β

Saitoh, M., Kunitomo, J., Kimura, E., Hayase, Y., Kobayashi, H., Uchiyama, N., Kawamoto, T., Tanaka, T., Mol, C. D., Dougan, D. R., et al. (2009) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2009.01.019 · Cited by 115

Imaging transcriptomics of brain disorders

Arnatkeviciute, A., Fulcher, B. D., Bellgrove, M. A., & Fornito, A. (2022) · Biological Psychiatry Global Open Science · doi:10.1016/j.bpsgos.2021.10.002 · Cited by 113

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 117

Amyloid β and APP as biomarkers for Alzheimer’s disease

Zetterberg, H., Blennow, K., & Hanse, E. (2009) · Experimental Gerontology · doi:10.1016/j.exger.2009.08.002 · Cited by 118

Fisetin stimulates autophagic degradation of phosphorylated tau via the activation of TFEB and Nrf2 transcription factors

Kim, S., Choi, K. J., Cho, S., Yun, S., Jeon, J., Koh, Y. H., Song, J., Johnson, G. V. W., & Jo, C. (2016) · Scientific Reports · doi:10.1038/srep24933 · Cited by 116

ACAT1/SOAT1 as a Therapeutic Target for Alzheimer's Disease

Shibuya, Y., Chang, C. C., & Chang, T.-Y. (2015) · Future Medicinal Chemistry · doi:10.4155/fmc.15.161 · Cited by 113

Re-emphasizing early Alzheimer’s disease pathology starting in select entorhinal neurons, with a special focus on mitophagy

Kobro-Flatmoen, A., Lagartos-Donate, M. J., Aman, Y., Edison, P., Witter, M. P., & Fang, E. F. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101307 · Cited by 119

Therapeutic strategies for the treatment of tauopathies: Hopes and challenges

Khanna, M. R., Kovalevich, J., Lee, V. M. ‐., Trojanowski, J. Q., & Brunden, K. R. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.06.006 · Cited by 116

Precision pharmacology for Alzheimer’s disease

Hampel, H. J., Vergallo, A., Aguilar, L. F., Benda, N., Broich, K., Cuello, A. C., Cummings, J. L., Dubois, B., Federoff, H. J., Fiandaca, M. S., et al. (2018) · Pharmacological Research · doi:10.1016/j.phrs.2018.02.014 · Cited by 114

Phospho-Tau Bar Code: Analysis of Phosphoisotypes of Tau and Its Application to Tauopathy

Kimura, T., Sharma, G., Ishiguro, K., & Hisanaga, S. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00044 · Cited by 116

Tau-Centric Multitarget Approach for Alzheimer’s Disease: Development of First-in-Class Dual Glycogen Synthase Kinase 3β and Tau-Aggregation Inhibitors

Gandini, A., Bartolini, M., Tedesco, D., Martínez‐González, L., Roca, C., Campillo, N. E., Zaldívar-Díez, J., Pérez, C., Zuccheri, G., Miti, A., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00610 · Cited by 115

Crowded Cell-like Environment Accelerates the Nucleation Step of Amyloidogenic Protein Misfolding

Zhou, Z., Fan, J.-B., Zhu, H., Shewmaker, F. P., Yan, X., Chen, X., Chen, J., Xiao, G., Guo, L., & Liang, Y. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.002832 · Cited by 114

Silencing of TREM2 exacerbates tau pathology, neurodegenerative changes, and spatial learning deficits in P301S tau transgenic mice

Jiang, T., Tan, L., Zhu, X.-C., Zhou, J.-S., Cao, L., Tan, M.-S., Wang, H.-F., Chen, Q., Zhang, Y.-D., & Yu, J.-T. (2015) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2015.08.019 · Cited by 111

Neurogranin as a cognitive biomarker in cerebrospinal fluid and blood exosomes for Alzheimer’s disease and mild cognitive impairment

Liu, W., Lin, H., He, X., Chen, L., Dai, Y., Jia, W., Xue, X., Tao, J., & Chen, L. (2020) · Translational Psychiatry · doi:10.1038/s41398-020-0801-2 · Cited by 117

Biomarker discovery in neurodegenerative diseases: A proteomic approach

Shi, M. Y., Caudle, W. M., & Zhang, J. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.09.004 · Cited by 115

Glial Tau Pathology in Tauopathies: Functional Consequences

Kahlson, M. A., & Colodner, K. J. (2015) · Journal of Experimental Neuroscience · doi:10.4137/jen.s25515 · Cited by 119

Transgenic Drosophila models of Alzheimer’s disease and tauopathies

Iijima‐Ando, K., & Iijima, K. (2009) · Brain Structure and Function · doi:10.1007/s00429-009-0234-4 · Cited by 118

Alcohol drinking exacerbates neural and behavioral pathology in the 3xTg-AD mouse model of Alzheimer's disease

Hoffman, J. L., Faccidomo, S., Kim, M., Taylor, S. M., Agoglia, A. E., May, A. M., Smith, E. N., Wong, L. C., & Hodge, C. W. (2019) · International review of neurobiology · doi:10.1016/bs.irn.2019.10.017 · Cited by 113

Targeting histone K4 trimethylation for treatment of cognitive and synaptic deficits in mouse models of Alzheimer’s disease

Cao, Q., Wang, W., Williams, J. B., Yang, F., Wang, Z.-J., & Yan, Z. (2020) · Science Advances · doi:10.1126/sciadv.abc8096 · Cited by 108

Association between tau deposition and antecedent amyloid-β accumulation rates in normal and early symptomatic individuals

Tosun, D., Landau, S. M., Aisen, P. S. S., Petersen, R. C., Mintun, M. A., Jagust, W., Weiner, M. W., & Initiative, A. D. N. (2017) · Brain · doi:10.1093/brain/awx046 · Cited by 110

Gut Microbiota: From the Forgotten Organ to a Potential Key Player in the Pathology of Alzheimer’s Disease

Seo, D.-O., & Holtzman, D. M. (2019) · The Journals of Gerontology Series A · doi:10.1093/gerona/glz262 · Cited by 109

Roles of brain-derived neurotrophic factor/tropomyosin-related kinase B (BDNF/TrkB) signalling in Alzheimer’s disease

Zhang, F., Kang, Z., Li, W., Xiao, Z., & Zhou, X. (2012) · Journal of Clinical Neuroscience · doi:10.1016/j.jocn.2011.12.022 · Cited by 110

Argyrophilic grain disease differs from other tauopathies by lacking tau acetylation

Grinberg, L. T., Wang, X., Wang, C., Sohn, P., Theofilas, P., Sidhu, M., Arevalo, J. B., Heinsen, H., Huang, E. J., Rosen, H. J., et al. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1080-2 · Cited by 110

Non-invasive brain stimulation to assess and modulate neuroplasticity in Alzheimer's disease

Boggio, P. S., Valasek, C. A., Campanhã, C., Giglio, A. C. A., Baptista, N. I., Lapenta, O. M., & Fregni, F. (2011) · Neuropsychological Rehabilitation · doi:10.1080/09602011.2011.617943 · Cited by 111

Extracellular Vesicle Biology in Alzheimer’s Disease and Related Tauopathy

DeLeo, A. M., & Ikezu, T. (2017) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-017-9768-z · Cited by 109

Icariin attenuates β-amyloid-induced neurotoxicity by inhibition of tau protein hyperphosphorylation in PC12 cells

Zeng, K., Ko, H., Yang, H. O., & Wang, X. (2010) · Neuropharmacology · doi:10.1016/j.neuropharm.2010.07.020 · Cited by 106

Biomarkers in Sporadic and Familial Alzheimer’s Disease

Lista, S., O’Bryant, S. E., Blennow, K., Dubois, B., Hugon, J., Zetterberg, H., & Hampel, H. (2015) · Journal of Alzheimer's Disease · doi:10.3233/jad-143006 · Cited by 106

Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity

Ando, K., Maruko-Otake, A., Ohtake, Y., Hayashishita, M., Sekiya, M., & Iijima, K. M. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1005917 · Cited by 105

Tau Accumulation, Altered Phosphorylation, and Missorting Promote Neurodegeneration in Glaucoma

Chiasseu, M., Vargas, J. L. C., Destroismaisons, L., Velde, C. V., Leclerc, N. M., & Polo, A. D. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3986-15.2016 · Cited by 105

Altered microtubule dynamics in neurodegenerative disease: Therapeutic potential of microtubule-stabilizing drugs

Brunden, K. R., Lee, V. M. ‐., Smith, A. B., Trojanowski, J. Q., & Ballatore, C. (2016) · Neurobiology of Disease · doi:10.1016/j.nbd.2016.12.021 · Cited by 109

Intelligently thermoresponsive flower-like hollow nano-ruthenium system for sustained release of nerve growth factor to inhibit hyperphosphorylation of tau and neuronal damage for the treatment of Alzheimer's disease

Zhou, H., Gong, Y., Liu, Y., Huang, A., Zhu, X., Liu, J., Yuan, G., Zhang, L., Wei, J., & Liu, J. (2020) · Biomaterials · doi:10.1016/j.biomaterials.2020.119822 · Cited by 107

Gut Microbiota Composition in Patients with Neurodegenerative Disorders (Parkinson’s and Alzheimer’s) and Healthy Controls: A Systematic Review

Heravi, F. S., Naseri, K., & Hu, H. (2023) · Nutrients · doi:10.3390/nu15204365 · Cited by 113

Regulation of alternative splicing of tau exon 10

Qian, W., & Liu, F. (2014) · Neuroscience Bulletin · doi:10.1007/s12264-013-1411-2 · Cited by 108

Inclusion body formation, macroautophagy, and the role of HDAC6 in neurodegeneration

Richter‐Landsberg, C., & Leyk, J. (2013) · Acta Neuropathologica · doi:10.1007/s00401-013-1158-x · Cited by 106

Human CDC2-Like Kinase 1 (CLK1): A Novel Target for Alzheimer’s Disease

Jain, P., Karthikeyan, C., Moorthy, N. S. H. N., Waiker, D. K., Jain, A. K., & Trivedi, P. (2014) · Current Drug Targets · doi:10.2174/1389450115666140226112321 · Cited by 104

Truncation of Tau selectively facilitates its pathological activities

Gu, J., Xu, W., Jin, N., Li, L., Zhou, Y., Chu, D., Gong, C., Iqbal, K., & Liu, F. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.012587 · Cited by 108

Iron homeostasis imbalance and ferroptosis in brain diseases

Long, H., Zhu, W., Wei, L., & Zhao, J. (2023) · MedComm · doi:10.1002/mco2.298 · Cited by 108

Fyn-Tau-Amyloid: A Toxic Triad

Haass, C., & Mandelkow�, E. (2010) · Cell · doi:10.1016/j.cell.2010.07.032 · Cited by 105

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

Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment

Garg, S., Timm, T., Mandelkow, E.-M., Mandelkow, E., & Wang, Y. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.09.008 · Cited by 103

Lithium treatment arrests the development of neurofibrillary tangles in mutant tau transgenic mice with advanced neurofibrillary pathology.

Leroy, K., Ando, K., Héraud, C., Yilmaz, Z., Authelet, M., Boeynaems, J.-M., Buée, L., De Decker, R., & Brion, J.-P. (2010) · Journal of Alzheimer's Disease · doi:10.3233/jad-2010-1276 · Cited by 103

Characteristics of Tau and Its Ligands in PET Imaging

Harada, R., Okamura, N., Furumoto, S., Tago, T., Yanai, K., Arai, H., & Kudo, Y. (2016) · Biomolecules · doi:10.3390/biom6010007 · Cited by 104

HGF Mediates Clinical‐Grade Human Umbilical Cord‐Derived Mesenchymal Stem Cells Improved Functional Recovery in a Senescence‐Accelerated Mouse Model of Alzheimer's Disease

Jia, Y., Cao, N., Zhai, J., Zeng, Q., Zheng, P. Z., Su, R., Liao, T., Liu, J., Pei, H., Fan, Z., et al. (2020) · Advanced Science · doi:10.1002/advs.201903809 · Cited by 106

Mechanisms of microcystin-LR-induced cytoskeletal disruption in animal cells

Zhou, M., Tu, W.-W., & Xu, J. (2015) · Toxicon · doi:10.1016/j.toxicon.2015.05.005 · Cited by 107

Axonal degeneration in tauopathies: disease relevance and underlying mechanisms

Kneynsberg, A., Combs, B., Christensen, K., Morfini, G., & Kanaan, N. M. (2017) · Frontiers in Neuroscience · doi:10.3389/fnins.2017.00572 · Cited by 102

Alzheimer’s Disease: Mechanism and Approach to Cell Therapy

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

Axonal Stress Kinase Activation and Tau Misbehavior Induced by Kinesin-1 Transport Defects

Falzone, T. L., Stokin, G. B., Lillo, C., Rodrigues, E. M., Westerman, E. L., Williams, D. S., & Goldstein, L. S. B. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0780-09.2009 · Cited by 102

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

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

Insights into Disease-Associated Tau Impact on Mitochondria

Szabo, L., Eckert, A., & Grimm, A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21176344 · Cited by 107

Mechanisms and Therapeutic Implications of GSK-3 in Treating Neurodegeneration

Rippin, I., & Eldar-Finkelman, H. (2021) · Cells · doi:10.3390/cells10020262 · Cited by 102

Alzheimer's disease pathophysiology in the Retina

Gaire, B. P., Koronyo, Y., Fuchs, D.-T. S., Shi, H., Rentsendorj, A., Danziger, R., Vit, J., Mirzaei, N., Doustar, J., Sheyn, J., et al. (2024) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2024.101273 · Cited by 107

Novel function of Tau in regulating the effects of external stimuli on adult hippocampal neurogenesis

Pallas‐Bazarra, N., Jurado‐Arjona, J., Navarrete, M., Esteban, J. A., Hernández, F., Ávila, J., & Llorens‐Martín, M. (2016) · The EMBO Journal · doi:10.15252/embj.201593518 · Cited by 101

Dissecting the potential molecular mechanisms underlying α-synuclein cell-to-cell transfer in Parkinson's disease

Angot, É., & Brundin, P. (2009) · Parkinsonism & Related Disorders · doi:10.1016/s1353-8020(09)70802-8 · Cited by 107

Does Ceruloplasmin Defend Against Neurodegenerative Diseases?

Wang, B., & Wang, X. (2018) · Current Neuropharmacology · doi:10.2174/1570159x16666180508113025 · Cited by 104

Oxidative stress induced by glutathione depletion reproduces pathological modifications of TDP-43 linked to TDP-43 proteinopathies

Iguchi, Y., Katsuno, M., Takagi, S., Ishigaki, S., Niwa, J., Hasegawa, M., Tanaka, F., & Sobue, G. (2011) · Neurobiology of Disease · doi:10.1016/j.nbd.2011.12.002 · Cited by 107

Identification of Aminothienopyridazine Inhibitors of Tau Assembly by Quantitative High-Throughput Screening

Crowe, A., Huang, W., Ballatore, C., Johnson, R. L., Hogan, A. L., Huang, R., Wichterman, J., McCoy, J. G., Huryn, D. M., Auld, D. S., et al. (2009) · Biochemistry · doi:10.1021/bi9006435 · Cited by 104

Multitracer PET imaging of amyloid plaques and neurofibrillary tangles in Alzheimer's disease

Shin, J., Lee, S., Kim, S., Kim, Y.-B., & Cho, S. (2008) · NeuroImage · doi:10.1016/j.neuroimage.2008.07.022 · Cited by 104

Reducing AD-Like Pathology in 3xTg-AD Mouse Model by DNA Epitope Vaccine — A Novel Immunotherapeutic Strategy

Movsesyan, N., Ghochikyan, A., Mkrtichyan, M., Petrushina, I., Davtyan, H., Olkhanud, P. B., Head, E., Biragyn, A., Cribbs, D. H., & Agadjanyan, M. G. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002124 · Cited by 103

Neurodegenerative diseases linked to misfolded proteins and their therapeutic approaches: A review

Khanam, H., Ali, A., Asif, M., & Shamsuzzaman (2016) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2016.08.006 · Cited by 103

Regulation of the alternative splicing of tau exon 10 by SC35 and Dyrk1A

Wu, Q., Liang, H., Shi, J., Jin, N., Grundke, I., Iqbal, K., Gong, C., & Liu, F. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr195 · Cited by 100

Overexpression, purification, and functional analysis of recombinant human tubulin dimer

Minoura, I., Hachikubo, Y., Yamakita, Y., Takazaki, H., Ayukawa, R., Uchimura, S., & Muto, E. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.08.032 · Cited by 100

The Proteasome and Oxidative Stress in Alzheimer's Disease

Bonet-Costa, V., Pomatto, L. C.-D., & Davies, K. J. A. (2016) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6802 · Cited by 99

The interactions of p53 with tau and Aß as potential therapeutic targets for Alzheimer’s disease

Jembrek, M. J., Slade, N., Hof, P. R., & Šimić, G. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.05.001 · Cited by 101

GSK3β-mediated tau hyperphosphorylation triggers diabetic retinal neurodegeneration by disrupting synaptic and mitochondrial functions

Zhu, H., Zhang, W., Zhao, Y., Shu, X., Wang, W., Wang, D., Yang, Y., He, Z., Wang, X., & Ying, Y. (2018) · Molecular Neurodegeneration · doi:10.1186/s13024-018-0295-z · Cited by 99

Transport and diffusion of Tau protein in neurons

Scholz, T., & Mandelkow�, E. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1610-7 · Cited by 105

The neurobiology of memory based predictions

Eichenbaum, H., & Fortin, N. J. (2009) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2008.0306 · Cited by 101

Appoptosin-Mediated Caspase Cleavage of Tau Contributes to Progressive Supranuclear Palsy Pathogenesis

Zhao, Y., Tseng, I.-C., Heyser, C. J., Rockenstein, E., Mante, M., Adame, A., Zheng, Q., Huang, T., Wang, X., Arslan, P. E., et al. (2015) · Neuron · doi:10.1016/j.neuron.2015.08.020 · Cited by 98

Death-associated protein kinase 1 has a critical role in aberrant tau protein regulation and function

Kim, B. M., You, M.-H., Chen, C.-H., Lee, S., Hong, Y., Hong, Y., Kimchi, A., Zhou, X. Z., & Lee, T. H. (2014) · Cell Death & Disease · doi:10.1038/cddis.2014.216 · Cited by 98

Corticotropin-releasing factor receptor-dependent effects of repeated stress on tau phosphorylation, solubility, and aggregation

Rissman, R. A., Staup, M. A., Lee, A. R., Justice, N. J., Rice, K. C., Vale, W., & Sawchenko, P. E. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1203140109 · Cited by 99

Connecting the dots between tau dysfunction and neurodegeneration

Frost, B., Götz, J., & Feany, M. B. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.07.005 · Cited by 124

The role of tau in neurodegeneration

Gendron, T. F., & Petrucelli, L. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-13 · Cited by 478

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

Phosphorylated Tau in Alzheimer’s Disease and Other Tauopathies

Rawat, P., Sehar, U., Bisht, J., Selman, A., Culberson, J., & Reddy, P. H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232112841 · Cited by 509

Role of tau protein in Alzheimer’s disease: The prime pathological player

Muralidar, S., Ambi, S. V., Sekaran, S., Thirumalai, D., & Palaniappan, B. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.07.327 · Cited by 278