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

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 · see citing works

In situ immune response and mechanisms of cell damage in central nervous system of fatal cases microcephaly by Zika virus

Azevedo, R. S. S., de Sousa, J. R., Araujo, M. T. F., Martins Filho, A. J., de Alcantara, B. N., Araujo, F. M. C., Queiroz, M. G. L., Cruz, A. C. R., Vasconcelos, B. H. B., Chiang, J. O., et al. (2018) · Scientific Reports · doi:10.1038/s41598-017-17765-5 · Cited by 3,478 · see citing works

The neuropathological diagnosis of Alzheimer's disease

DeTure, M. A., & Dickson, D. W. (2019) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0333-5 · Cited by 3,329 · see citing works

A protein factor essential for microtubule assembly

Weingarten, M. D., Lockwood, A. H., Hwo, S. Y., & Kirschner, M. W. (1975) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.72.5.1858 · Cited by 3,089 · see citing works

Exosomes: Extracellular organelles important in intercellular communication

Mathivanan, S., Ji, H. L., & Simpson, R. J. (2010) · Journal of Proteomics · doi:10.1016/j.jprot.2010.06.006 · Cited by 2,539 · see citing works

Standardization of sample collection, isolation and analysis methods in extracellular vesicle research

Witwer, K. W., Buzás, E. I., Bemis, L., Bora, A., Lässer, C., Lötvall, J. O., Hoen, E. N. M. N., Piper, M. G., Sivaraman, S., Skog, J., et al. (2013) · Journal of Extracellular Vesicles · doi:10.3402/jev.v2i0.20360 · Cited by 2,424 · see citing works

Tau in physiology and pathology

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

Untitled work

Bloom (2014) · doi:10.1001/jamaneurol.2013.5847 · Cited by 2,194 · 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

Orexin activation counteracts decreases in nonexercise activity thermogenesis (NEAT) caused by high-fat diet

Bunney, P. E., Zink, A. N., Holm, A. A., Billington, C. J., & Kotz, C. M. (2017) · Physiology & Behavior · doi:10.1016/j.physbeh.2017.03.040 · Cited by 2,104 · see citing works

The role of autophagy in neurodegenerative disease

Nixon, R. A. (2013) · Nature Medicine · doi:10.1038/nm.3232 · Cited by 2,059 · see citing works

Nanotubular Highways for Intercellular Organelle Transport

Rustom, A., Saffrich, R., Markovic, I., Walther, P., & Gerdes, H.-H. (2004) · Science · doi:10.1126/science.1093133 · Cited by 2,038 · see citing works

Amyloid Beta: Structure, Biology and Structure-Based Therapeutic Development

Chen, G.-F., Xu, T.-H., Yan, Y., Zhou, Y.-R., Jiang, Y., Melcher, K., & Xu, H. E. (2017) · Acta Pharmacologica Sinica · doi:10.1038/aps.2017.28 · Cited by 1,965 · see citing works

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

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

Transmission and spreading of tauopathy in transgenic mouse brain

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

Confocal Imaging–Guided Laser Ablation of Basal Cell Carcinomas: An Ex Vivo Study

Sierra, H., Cordova, M., Chen, C.-S. J., & Rajadhyaksha, M. (2015) · Journal of Investigative Dermatology · doi:10.1038/jid.2014.371 · Cited by 1,703 · 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

Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP

Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611 · see citing works

Depletion of microglia and inhibition of exosome synthesis halt tau propagation

Asai, H., Ikezu, S., Tsunoda, S., Medalla, M., Luebke, J., Haydar, T., Wolozin, B., Butovsky, O., Kügler, S., & Ikezu, T. (2015) · Nature Neuroscience · doi:10.1038/nn.4132 · Cited by 1,591 · see citing works

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 · see citing works

Formation of Neurofibrillary Tangles in P301L Tau Transgenic Mice Induced by Aβ42 Fibrils

Götz, J., Chen, F., van Dorpe, J., & Nitsch, R. M. (2001) · Science · doi:10.1126/science.1062097 · Cited by 1,526 · see citing works

Amyloid-β and tau — a toxic pas de deux in Alzheimer's disease

Ittner, L. M., & Götz, J. (2010) · Nature reviews. Neuroscience · doi:10.1038/nrn2967 · Cited by 1,357 · see citing works

Alzheimer’s disease β-amyloid peptides are released in association with exosomes

Rajendran, L., Honsho, M., Zahn, T. R., Keller, P., Geiger, K. D., Verkade, P., & Simons, K. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603838103 · Cited by 1,343 · see citing works

Autophagy Induction and Autophagosome Clearance in Neurons: Relationship to Autophagic Pathology in Alzheimer's Disease

Boland, B., Kumar, A., Lee, S., Platt, F. M., Wegiel, J., Yu, W. H., & Nixon, R. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0800-08.2008 · Cited by 1,119 · 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

The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid β accumulation in mice

Pickford, F., Masliah, E., Britschgi, M., Lucin, K. M., Narasimhan, R., Jaeger, P. A., Small, S. A., Spencer, B. J., Rockenstein, E. M., Levine, B., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci33585 · Cited by 1,072 · see citing works

Neurotoxicity induces cleavage of p35 to p25 by calpain

Lee, M.-S., Kwon, Y. T., Li, M., Peng, J., Friedlander, R. M., & Tsai, L. (2000) · Nature · doi:10.1038/35012636 · Cited by 1,057 · see citing works

Inhibition of mTOR by Rapamycin Abolishes Cognitive Deficits and Reduces Amyloid-β Levels in a Mouse Model of Alzheimer's Disease

Spilman, P., Podlutskaya, N., Hart, M. J., Debnath, J., Gorostiza, O., Bredesen, D., Richardson, A., Strong, R., & Galvan, V. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009979 · Cited by 1,033 · see citing works

Origins of Cell Polarity

Drubin, D. G., & Nelson, W. J. (1996) · Cell · doi:10.1016/s0092-8674(00)81278-7 · Cited by 1,030 · see citing works

Hippocampal synaptic loss in early Alzheimer's disease and mild cognitive impairment

Scheff, S. W., Price, D. A., Schmitt, F. A., & Mufson, E. J. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.09.012 · Cited by 1,017 · see citing works

Roles of tau protein in health and disease

Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · 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

Lithium induces autophagy by inhibiting inositol monophosphatase

Sarkar, S., Floto, R. A., Berger, Z., Imarisio, S., Cordenier, A., Pasco, M., Cook, L. J., & Rubinsztein, D. C. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504035 · Cited by 985 · see citing works

A critical appraisal of amyloid-β-targeting therapies for Alzheimer disease

Panza, F., Lozupone, M., Logroscino, G., & Imbimbo, B. P. (2019) · Nature Reviews Neurology · doi:10.1038/s41582-018-0116-6 · Cited by 965 · see citing works

Tau in Alzheimer's disease.

Mandelkow, E., & Mandelkow, E. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01368-3 · Cited by 951 · see citing works

Exosomes and Ectosomes in Intercellular Communication

Meldolesi, J. (2018) · Current Biology · doi:10.1016/j.cub.2018.01.059 · Cited by 944 · see citing works

Phosphorylation affects the ability of tau protein to promote microtubule assembly.

Lindwall, G., & Cole, R. D. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)42989-9 · Cited by 901 · see citing works

Molecular Interplay between Mammalian Target of Rapamycin (mTOR), Amyloid-β, and Tau

Caccamo, A., Majumder, S., Richardson, A., Strong, R., & Oddo, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100420 · Cited by 881 · see citing works

Evidence for the Conformation of the Pathologic Isoform of the Prion Protein Enciphering and Propagating Prion Diversity

Telling, G. C., Parchi, P., DeArmond, S. J., Cortelli, P., Montagna, P., Gabizon, R., Mastrianni, J. A., Lugaresi, E., Gambetti, P. L., & Prusiner, S. B. (1996) · Science · doi:10.1126/science.274.5295.2079 · Cited by 865 · 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

Exosomal cell-to-cell transmission of alpha synuclein oligomers

Danzer, K. M., Kranich, L. R., Ruf, W. P., Cagsal‐Getkin, O., Winslow, A. R., Zhu, L., Vanderburg, C. R., & McLean, P. J. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-42 · Cited by 852 · see citing works

Reconsideration of Amyloid Hypothesis and Tau Hypothesis in Alzheimer's Disease

Kametani, F., & Hasegawa, M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00025 · Cited by 836 · see citing works

Synaptic alterations in CA1 in mild Alzheimer disease and mild cognitive impairment

Scheff, S. W., Price, D. A., Schmitt, F. A., DeKosky, S. T., & Mufson, E. J. (2007) · Neurology · doi:10.1212/01.wnl.0000260698.46517.8f · Cited by 824 · see citing works

Neuronal activity enhances tau propagation and tau pathology in vivo

Wu, J. W., Hussaini, S. A., Bastille, I. M., Rodriguez, G. A., Mrejeru, A., Rilett, K., Sanders, D. W., Cook, C., Fu, H., Boonen, R. A. C. M., et al. (2016) · Nature Neuroscience · doi:10.1038/nn.4328 · Cited by 820 · see citing works

Tau is essential to β-amyloid-induced neurotoxicity

Rapoport, M., Dawson, H. N., Binder, L. I., Vitek, M. P., & Ferreira, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.092136199 · Cited by 807 · see citing works

Tau and neurodegenerative disease: the story so far

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

Circulating microparticles: pathophysiology and clinical implications

Piccin, A., Murphy, W. G., & Smith, O. P. (2006) · Blood Reviews · doi:10.1016/j.blre.2006.09.001 · Cited by 799 · see citing works

Contributions of protein phosphatases PP1, PP2A, PP2B and PP5 to the regulation of tau phosphorylation

Liu, F., Grundke‐Iqbal, I., Iqbal, K., & Gong, C. (2005) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2005.04391.x · Cited by 759 · see citing works

Autophagy, amyloidogenesis and Alzheimer disease

Nixon, R. A. (2007) · Journal of Cell Science · doi:10.1242/jcs.019265 · Cited by 749 · see citing works

Therapeutics of Alzheimer's disease: Past, present and future

Anand, R., Gill, K. D., & Mahdi, A. A. (2013) · Neuropharmacology · doi:10.1016/j.neuropharm.2013.07.004 · Cited by 748 · 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

Mono- and Di-Quaternized 4,4′-Bipyridine Derivatives as Key Building Blocks for Medium- and Environment-Responsive Compounds and Materials

Papadakis, R. (2019) · Molecules · doi:10.3390/molecules25010001 · Cited by 662 · see citing works

Alzheimer amyloid-β oligomer bound to postsynaptic prion protein activates Fyn to impair neurons

Um, J. W., Nygaard, H. B., Heiss, J. K., Kostylev, M. A., Stagi, M., Vortmeyer, A. O., Wısnıewskı, T., Gunther, E. C., & Strittmatter, S. M. (2012) · Nature Neuroscience · doi:10.1038/nn.3178 · Cited by 654 · see citing works

Structural Polymorphism of 441-Residue Tau at Single Residue Resolution

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

Hyperphosphorylation of Microtubule-Associated Protein Tau: A Promising Therapeutic Target for Alzheimer Disease

Gong, C., & Iqbal, K. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708785909111 · Cited by 649 · 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 protein kinases: Involvement in Alzheimer's disease

Martin, L., Latypova, X., Wilson, C. M., Magnaudeix, A., Perrin, M.-L., Yardin, C., & Terro, F. (2013) · Ageing Research Reviews · doi:10.1016/j.arr.2012.06.003 · Cited by 631 · see citing works

Amyloid β oligomers in Alzheimer’s disease pathogenesis, treatment, and diagnosis

Viola, K. L., & Klein, W. L. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1386-3 · Cited by 628 · see citing works

Interaction of tau with the neural plasma membrane mediated by tau's amino-terminal projection domain.

Brandt, R., Léger, J. G., & Lee, G. S. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.131.5.1327 · Cited by 624 · see citing works

Tau phosphorylation in neuronal cell function and dysfunction

Johnson, G. V. W., & Stoothoff, W. H. (2004) · Journal of Cell Science · doi:10.1242/jcs.01558 · Cited by 624 · see citing works

Role of Tau as a Microtubule-Associated Protein: Structural and Functional Aspects

Barbier, P., Zejneli, O., Martinho, M., Lasorsa, A., Belle, V., Smet‐Nocca, C., Tsvetkov, P. O., Devred, F., & Landrieu, I. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00204 · Cited by 622 · see citing works

Aberrant Cdk5 activation by p25 triggers pathological events leading to neurodegeneration and neurofibrillary tangles

Cruz, J. C., Tseng, H.-C., Goldman, J. A., Shih, H., & Tsai, L.-H. (2003) · Neuron · doi:10.1016/s0896-6273(03)00627-5 · Cited by 609 · see citing works

β-Amyloid fibrils induce tau phosphorylation and loss of microtubule binding

Busciglio, J., Lorenzo, A., Yeh, J., & Yankner, B. A. (1995) · Neuron · doi:10.1016/0896-6273(95)90232-5 · Cited by 595 · see citing works

Release of exosomes from differentiated neurons and its regulation by synaptic glutamatergic activity

Lachenal, G. M., Pernet‐Gallay, K., Chivet, M., Hemming, F. J., Belly, A., Bodon, G., Blot, B., Haase, G., Goldberg, Y., & Sadoul, R. (2010) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2010.11.004 · Cited by 595 · see citing works

Neuronal activity regulates extracellular tau in vivo

Yamada, K., Holth, J. K., Liao, F., Stewart, F. R., Mahan, T. E., Jiang, H., Cirrito, J. R., Patel, T. K., Hochgräfe, K., Mandelkow, E., et al. (2014) · The Journal of Experimental Medicine · doi:10.1084/jem.20131685 · Cited by 574 · 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

Aβ42 Is Essential for Parenchymal and Vascular Amyloid Deposition in Mice

McGowan, E., Pickford, F., Kim, J., Onstead, L., Eriksen, J., Yu, C., Skipper, L., Murphy, M. P., Beard, J., Das, P., et al. (2005) · Neuron · doi:10.1016/j.neuron.2005.06.030 · Cited by 565 · see citing works

Kinases and phosphatases and tau sites involved in Alzheimer neurofibrillary degeneration

Wang, J., Grundke, I., & Iqbal, K. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2006.05226.x · Cited by 553 · 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

Cdk5 Is a Key Factor in Tau Aggregation and Tangle Formation In Vivo

Noble, W. J., Olm, V., Takata, K., Casey, E., Mary, O., Meyerson, J. L., Gaynor, K., LaFrancois, J. J., Wang, L., Kondo, T., et al. (2003) · Neuron · doi:10.1016/s0896-6273(03)00259-9 · Cited by 511 · 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

The microtubule binding domain of tau protein

Lee, G., Neve, R. L., & Kosik, K. S. (1989) · Neuron · doi:10.1016/0896-6273(89)90050-0 · Cited by 500 · see citing works

The role of tau in neurodegeneration

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

Structure and Pathology of Tau Protein in Alzheimer Disease

Kolarova, M., García‐Sierra, F., Bartoš, A., Říčný, J., & Řı́pová, D. (2012) · International Journal of Alzheimer s Disease · doi:10.1155/2012/731526 · Cited by 473 · see citing works

The Role of Tau in Alzheimer's Disease and Related Disorders

Medeiros, R., Baglietto‐Vargas, D., & LaFerla, F. M. (2010) · CNS Neuroscience & Therapeutics · doi:10.1111/j.1755-5949.2010.00177.x · Cited by 449 · see citing works

Autophagy in neurodegenerative diseases: pathogenesis and therapy

Guo, F., Liu, X., Cai, H., & Le, W. (2017) · Brain Pathology · doi:10.1111/bpa.12545 · Cited by 444 · see citing works

Role of the prolyl isomerase Pin1 in protecting against age-dependent neurodegeneration

Liou, Y., Sun, A., Ryo, A., Zhou, X. Z., Yu, Z.-X., Huang, H.-K., Uchida, T., Bronson, R. T., Bing, G., Li, X., et al. (2003) · Nature · doi:10.1038/nature01832 · Cited by 432 · see citing works

Animal Models of Alzheimer Disease

LaFerla, F. M., & Green, K. N. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006320 · Cited by 419 · see citing works

Tau Protein Modifications and Interactions: Their Role in Function and Dysfunction

Mietelska‐Porowska, A., Wasik, U., Goras, M., Filipek, A., & Niewiadomska, G. (2014) · International Journal of Molecular Sciences · doi:10.3390/ijms15034671 · Cited by 407 · see citing works

Presenilin 1 associates with glycogen synthase kinase-3β and its substrate tau

Takashima, A., Murayama, M., Murayama, O., Kohno, T., Honda, T., Yasutake, K., Nihonmatsu, N., Mercken, M. H., Yamaguchi, H., Sugihara, S., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9637 · Cited by 404 · see citing works

Spatial navigational strategies correlate with gray matter in the hippocampus of healthy older adults tested in a virtual maze

Konishi, K., & Bohbot, V. D. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00001 · Cited by 404 · see citing works

The microtubule-stabilizing agent, epothilone D, reduces axonal dysfunction, neurotoxicity, cognitive deficits, and Alzheimer-like pathology in an interventional study with aged tau transgenic mice

Zhang, B., Carroll, J., Trojanowski, J. Q., Yao, Y., Iba, M., Potuzak, J. S., Hogan, A.-M. L., Xie, S. X., Ballatore, C., Smith, A. B., et al. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.4922-11.2012 · Cited by 401 · see citing works

Inducing Autophagy by Rapamycin Before, but Not After, the Formation of Plaques and Tangles Ameliorates Cognitive Deficits

Majumder, S., Richardson, A. G., Strong, R., & Oddo, S. (2011) · PLoS ONE · doi:10.1371/journal.pone.0025416 · Cited by 401 · see citing works

Phosphorylation of different tau sites during progression of Alzheimer’s disease

Neddens, J., Temmel, M., Flunkert, S., Kerschbaumer, B., Hoeller, C., Loeffler, T., Niederkofler, V., Daum, G., Attems, J., & Hutter-Paier, B. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0557-6 · Cited by 384 · see citing works

Tau protein kinase I is essential for amyloid beta-protein-induced neurotoxicity.

Takashima, A., Noguchi, K., Sato, K., Hoshino, T., & Imahori, K. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.16.7789 · Cited by 381 · see citing works

Prediction of conversion from mild cognitive impairment to dementia with neuronally derived blood exosome protein profile

Winston, C. N., Goetzl, E. J., Akers, J. C., Carter, B. S., Rockenstein, E. M., Galasko, D. R., Masliah, E., & Rissman, R. A. (2016) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1016/j.dadm.2016.04.001 · Cited by 379 · see citing works

Weight Loss and Malnutrition in Patients with Parkinson's Disease: Current Knowledge and Future Prospects

Ma, K., Xiong, N., Shen, Y., Han, C., Liu, L., Zhang, G., Wang, L., Guo, S., Guo, X., Xia, Y. F., et al. (2018) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2018.00001 · Cited by 379 · see citing works

Axonal transport defects: a common theme in neurodegenerative diseases

Roy, S., Zhang, B., Lee, V. M. ‐., & Trojanowski, J. Q. (2005) · Acta Neuropathologica · doi:10.1007/s00401-004-0952-x · Cited by 372 · see citing works

Regulation of autophagy by mTOR-dependent and mTOR-independent pathways: autophagy dysfunction in neurodegenerative diseases and therapeutic application of autophagy enhancers

Sarkar, S. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130134 · Cited by 367 · see citing works

Regulation and localization of tyrosine 216 phosphorylation of glycogen synthase kinase-3β in cellular and animal models of neuronal degeneration

Bhat, R. V., Shanley, J. R., Correll, M. P., Fieles, W. E., Keith, R. A., Scott, C. W., & Lee, C. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.190297597 · Cited by 367 · see citing works

<scp>mTOR</scp> regulates tau phosphorylation and degradation: implications for Alzheimer's disease and other tauopathies

Caccamo, A., Magrì, A., Medina, D. X., Wisely, E. V., López‐Aranda, M. F., Silva, A. J., & Oddo, S. (2013) · Aging Cell · doi:10.1111/acel.12057 · Cited by 362 · see citing works

Tau Aggregation and Its Interplay with Amyloid-β

Nisbet, R. M., Polanco, J.-C., Ittner, L. M., & Götz, J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-014-1371-2 · Cited by 359 · see citing works

Aβ deposition is associated with increases in soluble and phosphorylated tau that precede a positive tau PET in Alzheimer's disease

Mattsson-Carlgren, N., Andersson, E., Janelidze, S., Ossenkoppele, R., Insel, P., Strandberg, O., Zetterberg, H., Rosen, H. J., Rabinovici, G., Chai, X., et al. (2020) · Science Advances · doi:10.1126/sciadv.aaz2387 · Cited by 359 · see citing works

Autophagy flux in CA1 neurons of Alzheimer hippocampus: Increased induction overburdens failing lysosomes to propel neuritic dystrophy

Bordi, M., Berg, M. J., Mohan, P. S., Peterhoff, C. M., Alldred, M. J., Che, S., Ginsberg, S. D., & Nixon, R. A. (2016) · Autophagy · doi:10.1080/15548627.2016.1239003 · Cited by 353 · see citing works

Tau and neuroinflammation: what impact for Alzheimer's disease and tauopathies?

Laurent, C., Buée, L., & Blum, D. (2018) · Biomedical Journal · doi:10.1016/j.bj.2018.01.003 · Cited by 348 · see citing works

Cerebrovascular Smooth Muscle Cells as the Drivers of Intramural Periarterial Drainage of the Brain

Aldea, R., Weller, R. O., Wilcock, D. M., Carare, R. O., & Richardson, G. W. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00001 · Cited by 335 · see citing works

Tau exon 10 alternative splicing and tauopathies

Liu, F., & Gong, C.-X. (2008) · Molecular Neurodegeneration · doi:10.1186/1750-1326-3-8 · Cited by 323 · see citing works

Accelerated neurodegeneration through chaperone-mediated oligomerization of tau

Blair, L. J., Nordhues, B. A., Hill, S. E., Scaglione, K. M., O’Leary, J. C., Fontaine, S. N., Breydo, L., Zhang, B., Li, P., Wang, L., et al. (2013) · Journal of Clinical Investigation · doi:10.1172/jci69003 · Cited by 322 · see citing works

Epothilone D Improves Microtubule Density, Axonal Integrity, and Cognition in a Transgenic Mouse Model of Tauopathy

Brunden, K. R., Zhang, B., Carroll, J., Yao, Y., Potuzak, J. S., Hogan, A.-M. L., Iba, M., James, M. J., Xie, S. X., Ballatore, C., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.3059-10.2010 · Cited by 320 · 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

Fyn kinase induces synaptic and cognitive impairments in a transgenic mouse model of Alzheimer’s disease

Chin, J., Palop, J. J., Puoliväli, J., Massaro, C., Bien-Ly, N., Gerstein, H., Scearce-Levie, K., Masliah, E., & Mucke, L. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2980-05.2005 · Cited by 312 · see citing works

Tau protein as a differential biomarker of tauopathies

Sergeant, N., Delacourte, A., & Buée, L. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.06.020 · Cited by 312 · see citing works

Tau gene alternative splicing: expression patterns, regulation and modulation of function in normal brain and neurodegenerative diseases

Andreadis, A. (2005) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2004.08.010 · Cited by 311 · see citing works

Tunneling nanotube (TNT)-mediated neuron-to neuron transfer of pathological Tau protein assemblies

Tardivel, M., Bégard, S., Bousset, L., Dujardin, S., Coens, A., Melki, R., Buée, L., & Colin, M. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0386-4 · Cited by 305 · see citing works

Protein phosphatase 2A dysfunction in Alzheimer’s disease

Sontag, J.-M., & Sontag, E. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00016 · Cited by 304 · 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

Galacto‐conjugation of Navitoclax as an efficient strategy to increase senolytic specificity and reduce platelet toxicity

González‐Gualda, E., Pàez‐Ribes, M., Lozano‐Torres, B., Macias, D., Wilson, J. R., González‐López, C., Ou, H., Mirón‐Barroso, S., Zhang, Z., Lérida‐Viso, A., et al. (2020) · Aging Cell · doi:10.1111/acel.13142 · Cited by 303 · see citing works

Physiological and pathological phosphorylation of tau by Cdk5

Kimura, T., Ishiguro, K., & Hisanaga, S. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00065 · Cited by 297 · see citing works

Alpha-synuclein and tau: teammates in neurodegeneration?

Moussaud, S., Jones, D. R., Moussaud-Lamodière, E. L., Delenclos, M., Ross, O. A., & McLean, P. J. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-43 · Cited by 291 · see citing works

Glycogen synthase kinase-3 beta is a dual specificity kinase differentially regulated by tyrosine and serine/threonine phosphorylation.

Wang, Q. M., Fiol, C. J., DePaoli-Roach, A. A., & Roach, P. J. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)36661-9 · Cited by 289 · see citing works

Activation of tau protein kinase I/glycogen synthase kinase-3β by amyloid β peptide (25–35) enhances phosphorylation of tau in hippocampal neurons

Takashima, A., Honda, T., Yasutake, K., Michel, G., Murayama, O., Murayama, M., Ishiguro, K., & Yamaguchi, H. (1998) · Neuroscience Research · doi:10.1016/s0168-0102(98)00061-3 · Cited by 287 · see citing works

A walk through tau therapeutic strategies

Jadhav, S., Ávila, J., Schöll, M., Kovács, G. G., Kövari, E., Škrabana, R., Evans, L., Kontseková, E., Malawska, B., de Silva, R., et al. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0664-z · Cited by 286 · see citing works

Accuracy of ARGOS Locations of Pinnipeds at-Sea Estimated Using Fastloc GPS

da Costa, D. P., Robinson, P. W., Arnould, J. P. Y., Harrison, A., Simmons, S. E., Hassrick, J. L., Hoskins, A. J., Kirkman, S. P., Oosthuizen, H., Villegas‐Amtmann, S., et al. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008677 · Cited by 282 · see citing works

Assessing Neurocognition via Gamified Experimental Logic: A Novel Approach to Simultaneous Acquisition of Multiple ERPs

Nair, A. K., Sasidharan, A., John, J. P., Mehrotra, S., & Kutty, B. M. (2016) · Frontiers in Neuroscience · doi:10.3389/fnins.2016.00001 · Cited by 282 · see citing works

Induction of Tau Pathology by Intracerebral Infusion of Amyloid-β-Containing Brain Extract and by Amyloid-β Deposition in APP × Tau Transgenic Mice

Bolmont, T., Clavaguera, F., Meyer-Luehmann, M., Herzig, M. C., Radde, R., Staufenbiel, M., Lewis, J., Hutton, M., Tolnay, M., & Jucker, M. (2007) · The American Journal of Pathology · doi:10.2353/ajpath.2007.070403 · Cited by 281 · see citing works

Hyperphosphorylation of Tau Associates With Changes in Its Function Beyond Microtubule Stability

Alonso, A. D., Cohen, L. S., Corbo, C., Morozova, V., ElIdrissi, A., Phillips, G., & Kleiman, F. E. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00338 · Cited by 278 · see citing works

Molecular Pathogenesis of the Tauopathies

Götz, J., Halliday, G., & Nisbet, R. M. (2019) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012418-012936 · Cited by 276 · see citing works

Synaptic Contacts Enhance Cell-to-Cell Tau Pathology Propagation

Calafate, S., Buist, A., Miśkiewicz, K., Vijayan, V. A., Daneels, G., Strooper, B. D., de Wit, J., Verstreken, P., & Moechars, D. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.043 · Cited by 257 · see citing works

Intermittent Fasting Alleviates the Increase of Lipoprotein Lipase Expression in Brain of a Mouse Model of Alzheimer's Disease: Possibly Mediated by β-hydroxybutyrate

Zhang, J., Li, X., Ren, Y., Zhao, Y., Xing, A., Jiang, C., Chen, Y., & An, L. (2018) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2018.00001 · Cited by 257 · see citing works

Models of β-amyloid induced Tau-pathology: The long and “folded” road to understand the mechanism

Stancu, I.-C., Vasconcelos, B., Terwel, D., & Dewachter, I. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-51 · Cited by 256 · see citing works

Heat shock protein 90 in neurodegenerative diseases

Luo, W., Sun, W., Taldone, T., Rodina, A., & Chiosis, G. (2010) · Molecular Neurodegeneration · doi:10.1186/1750-1326-5-24 · Cited by 249 · see citing works

Tau Proteins and Tauopathies in Alzheimer’s Disease

Chong, F. P., Ng, K. Y., Koh, R. Y., & Chye, S. M. (2018) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-017-0574-1 · Cited by 248 · 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

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

GABA Potency at GABAA Receptors Found in Synaptic and Extrasynaptic Zones

Mortensen, M., Patel, B., & Smart, T. G. (2012) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2012.00001 · Cited by 244 · see citing works

Tau phosphorylation in Alzheimer's disease: pathogen or protector?

Lee, H., Perry, G. L., Moreira, P. I., Garrett, M. R., Liu, Q., Zhu, X., Takeda, A., Nunomura, A., & Smith, M. A. (2005) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2005.02.008 · Cited by 240 · see citing works

Phosphorylated Map Kinase (ERK1, ERK2) Expression is Associated with Early Tau Deposition in Neurones and Glial Cells, but not with Increased Nuclear DNA Vulnerability and Cell Death, in Alzheimer Disease, Pick's Disease, Progressive Supranuclear Palsy and Corticobasal Degeneration

Ferrer, I., Blanco, R., Carmona, M., Ribera, R., Goutan, E., Puig, B., Rey, M. J., Cardozo, A., Viñals, F., & Ribalta, T. (2001) · Brain Pathology · doi:10.1111/j.1750-3639.2001.tb00387.x · Cited by 239 · see citing works

Kinesin is the motor for microtubule-mediated Golgi-to-ER membrane traffic [published errata appear in J Cell Biol 1995 Mar;128(5):following 988 and 1995 May;129(3):893]

Lippincott‐Schwartz, J. (1995) · The Journal of Cell Biology · doi:10.1083/jcb.128.3.293 · Cited by 237 · see citing works

Clinicopathologic assessment and imaging of tauopathies in neurodegenerative dementias

Murray, M. E., Kouri, N., Lin, W.-L., Jack, C. R., Dickson, D. W., & Vemuri, P. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt231 · Cited by 237 · see citing works

Transfer Function between EEG and BOLD Signals of Epileptic Activity

Leite, M., Leal, A., & Figueiredo, P. (2013) · Frontiers in Neurology · doi:10.3389/fneur.2013.00001 · Cited by 234 · 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

Inhibition of tau phosphorylating protein kinase cdk5 prevents β‐amyloid‐induced neuronal death

Alvarez, A. R., Toro, R., Cáceres, A., & Maccioni, R. B. (1999) · FEBS Letters · doi:10.1016/s0014-5793(99)01279-x · Cited by 228 · see citing works

Accumulation of cyclin-dependent kinase 5 (cdk5) in neurons with early stages of Alzheimer's disease neurofibrillary degeneration

Pei, J.-J., Grundke-Iqbal, I., Iqbal, K., Bogdanovic, N., Winblad, B., & Cowburn, R. F. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00296-0 · Cited by 226 · see citing works

Interaction of Tau with the Neural Membrane Cortex Is Regulated by Phosphorylation at Sites That Are Modified in Paired Helical Filaments

Maas, T., Eidenmüller, J., & Brandt, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000389200 · Cited by 226 · see citing works

Differential effects of 24-hydroxycholesterol and 27-hydroxycholesterol on β-amyloid precursor protein levels and processing in human neuroblastoma SH-SY5Y cells

Prasanthi, J. R. P., Huls, A., Thomasson, S., Thompson, A. J., Schommer, E., & Ghribi, O. (2009) · Molecular Neurodegeneration · doi:10.1186/1750-1326-4-1 · Cited by 223 · see citing works

Ectosomes: A New Mechanism for Non-Exosomal Secretion of Tau Protein

Dujardin, S., Bégard, S., Caillierez, R., Lachaud, C., Delattre, L., Carrier, S., Loyens, A., Galas, M., Bousset, L., Melki, R., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0100760 · Cited by 215 · 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

Are tau aggregates toxic or protective in tauopathies?

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

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

Site-specific effects of tau phosphorylation on its microtubule assembly activity and self-aggregation

Liu, F., Li, B., Tung, E., Grundke‐Iqbal, I., Iqbal, K., & Gong, C. (2007) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2007.05955.x · Cited by 208 · see citing works

Atypical, non-standard functions of the microtubule associated Tau protein

Sotiropoulos, I., Galas, M., Silva, J. M., Skoulakis, E. M. C., Wegmann, S., Maina, M. B., Blum, D. L., Sayas, C. L., Mandelkow, E., Mandelkow�, E., et al. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0489-6 · Cited by 207 · see citing works

Tunneling nanotubes: A possible highway in the spreading of tau and other prion-like proteins in neurodegenerative diseases

Abounit, S., Wu, J. W., Duff, K., Victoria, G. S., & Zurzolo, C. (2016) · Prion · doi:10.1080/19336896.2016.1223003 · Cited by 206 · see citing works

DnaJ/Hsc70 chaperone complexes control the extracellular release of neurodegenerative‐associated proteins

Fontaine, S. N., Zheng, D., Sabbagh, J. J., Martin, M. D., Chaput, D., Darling, A. L., Trotter, J. H., Stothert, A. R., Nordhues, B. A., Lussier, A. L., et al. (2016) · The EMBO Journal · doi:10.15252/embj.201593489 · Cited by 203 · see citing works

Prion-like Properties of Tau Protein: The Importance of Extracellular Tau as a Therapeutic Target

Holmes, B. B., & Diamond, M. I. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.r114.549295 · Cited by 202 · see citing works

The identification of mitochondrial DNA variants in glioblastoma multiforme

Yeung, K. Y., Dickinson, A., Donoghue, J. F., Polekhina, G., White, S. J., Grammatopoulos, D. K., McKenzie, M., Johns, T. G., & John, J. C. S. (2014) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-2-1 · Cited by 202 · see citing works

Therapeutic targeting of autophagy in neurodegenerative and infectious diseases

Rubinsztein, D. C., Bento, C. F., & Deretic, V. (2015) · Journal of Experimental Medicine · doi:10.1084/jem.20150956 · Cited by 202 · see citing works

Fyn kinase inhibition as a novel therapy for Alzheimer’s disease

Nygaard, H. B., van Dyck, C. H., & Strittmatter, S. M. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt238 · Cited by 201 · see citing works

Molecular mechanism of membrane constriction and tubulation mediated by the F-BAR protein Pacsin/Syndapin

Wang, Q., Navarro, M. V. A. S., Peng, G., Molinelli, E., Lin Goh, S., Judson, B. L., Rajashankar, K. R., & Sondermann, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902974106 · Cited by 200 · see citing works

Glycogen synthase kinase-3 is associated with neuronal and glial hyperphosphorylated tau deposits in Alzheimer's disease, Pick's disease, progressive supranuclear palsy and corticobasal degeneration

Ferrer, I., Barrachina, M., & Puig, B. (2002) · Acta Neuropathologica · doi:10.1007/s00401-002-0587-8 · Cited by 197 · see citing works

Spatial genomic heterogeneity in diffuse intrinsic pontine and midline high-grade glioma: implications for diagnostic biopsy and targeted therapeutics

Hoffman, L. M., DeWire, M. D., Ryall, S. T., Buczkowicz, P., Leach, J., Miles, L., Ramani, A. K., Brudno, M., Kumar, S. S., Drissi, R., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0269-0 · Cited by 196 · see citing works

Pathways by Which Aβ Facilitates Tau Pathology

Blurton-Jones, M. M., & LaFerla, F. M. (2006) · Current Alzheimer Research · doi:10.2174/156720506779025242 · Cited by 195 · see citing works

Tau oligomers and aggregation in Alzheimer’s disease

Meraz‐Ríos, M. A., León, K. I. L.-D., Campos‐Peña, V., Anda-Hernández, M. A. D., & Mena‐López, R. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06511.x · Cited by 193 · see citing works

From the prion-like propagation hypothesis to therapeutic strategies of anti-tau immunotherapy

Colin, M., Dujardin, S., Schraen-Maschke, S., Meno-Tetang, G., Duyckaerts, C., Courade, J.-P., & Buée, L. (2020) · Acta Neuropathologica · doi:10.1007/s00401-019-02087-9 · Cited by 187 · see citing works

CSF biomarkers of Alzheimer disease in HIV-associated neurologic disease

Clifford, D. B., Fagan, A. M., Holtzman, D. M., Morris, J. C., Teshome, M., Shah, A. R., & Kauwe, J. S. K. (2009) · Neurology · doi:10.1212/wnl.0b013e3181c5b445 · Cited by 186 · see citing works

Phosphorylation of microtubule‐associated protein tau by isoforms of c‐Jun N‐terminal kinase (JNK)

Yoshida, H., Hastie, C. J., McLauchlan, H., Cohen, P., & Goedert, M. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02479.x · Cited by 185 · see citing works

Motors and membrane traffic

Goodson, H. V. (1997) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(97)80147-0 · Cited by 185 · see citing works

Differential Assembly of Human Tau Isoforms in the Presence of Arachidonic Acid

King, M. E., Gamblin, T. C., Kuret, J., & Binder, L. I. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0741749.x · Cited by 179 · see citing works

Validation of Suitable Housekeeping Genes for the Normalization of mRNA Expression for Studying Tumor Acidosis

Lemma, S., Avnet, S., Meade, M., Chano, T., & Baldini, N. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19102930 · Cited by 178 · see citing works

Heat Shock Proteins in Alzheimer’s Disease: Role and Targeting

Campanella, C., Pace, A., Bavisotto, C. C., Marzullo, P., Marino, A., Buscemi, S., & Piccionello, A. P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19092603 · Cited by 175 · see citing works

The role of tau kinases in Alzheimer's disease.

Dolan, P. J., & Johnson, G. V. W. (2010) · PubMed · Cited by 174 · 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

Levels of normal and abnormally phosphorylated tau in different cellular and regional compartments of Alzheimer disease and control brains

Khatoon, S., Grundke, I., & Iqbal, K. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00829-9 · Cited by 167 · see citing works

A Becn1 mutation mediates hyperactive autophagic sequestration of amyloid oligomers and improved cognition in Alzheimer's disease

Rocchi, A., Yamamoto, S., Ting, T., Fan, Y., Sadleir, K., Wang, Y., Zhang, W., Huang, S., Levine, B., Vassar, R., et al. (2017) · PLOS Genetics · doi:10.1371/journal.pgen.1006962 · Cited by 166 · see citing works

ALZHEIMER'S DISEASE: PAIRED HELICAL FILAMENTS AND CYTOMEMBRANES

Gray, E. G., Paula-Barbosa, M., & Roher, A. (1987) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.1987.tb00174.x · Cited by 165 · 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

Casein Kinase 1 Delta Phosphorylates Tau and Disrupts Its Binding to Microtubules

Li, G., Yin, H., & Kuret, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314116200 · Cited by 159 · see citing works

An Overview on the Clinical Development of Tau-Based Therapeutics

Medina, M. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19041160 · Cited by 156 · see citing works

Toxic tau: structural origins of tau aggregation in Alzheimer's disease

Mamun, A. A., Uddin, M. S., Mathew, B., & Ashraf, G. M. (2020) · Neural Regeneration Research · doi:10.4103/1673-5374.274329 · Cited by 156 · see citing works

The microtubule network and neuronal morphogenesis: Dynamic and coordinated orchestration through multiple players

Poulain, F. E., & Sobel, A. (2009) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2009.07.012 · Cited by 153 · see citing works

Biomarker-based prediction of progression in MCI: comparison of AD signature and hippocampal volume with spinal fluid amyloid-β and tau

Dickerson, B. C. (2013) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2013.00055 · Cited by 151 · see citing works

GSK‐3: A key player in neurodegeneration and memory

Giese, K.-P. (2009) · IUBMB Life · doi:10.1002/iub.187 · Cited by 150 · see citing works

Endo‐lysosomal and autophagic dysfunction: a driving factor in Alzheimer's disease?

Whyte, L. S., Lau, A. A., Hemsley, K. M., Hopwood, J. J., & Sargeant, T. J. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13935 · Cited by 150 · see citing works

The spread of prion-like proteins by lysosomes and tunneling nanotubes: Implications for neurodegenerative diseases

Victoria, G. S., & Zurzolo, C. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701047 · Cited by 150 · see citing works

Molecular basis for SH3 domain regulation of F-BAR–mediated membrane deformation

Rao, Y., Ma, Q., Vahedi-Faridi, A., Sundborger, A., Pechstein, A., Puchkov, D., Luo, L., Shupliakov, O., Saenger, W., & Haucke, V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003478107 · Cited by 149 · see citing works

Dynamic association of tau with neuronal membranes is regulated by phosphorylation

Pooler, A. M., Usardi, A., Evans, C. J., Philpott, K. L., Noble, W., & Hanger, D. P. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.01.005 · Cited by 148 · see citing works

Effect of AZD0530 on Cerebral Metabolic Decline in Alzheimer Disease

van Dyck, C. H., Nygaard, H. B., Chen, K., Donohue, M., Raman, R., Rissman, R. A., Brewer, J. B., Koeppe, R. A., Chow, T. W., Rafii, M. S., et al. (2019) · JAMA Neurology · doi:10.1001/jamaneurol.2019.2050 · Cited by 144 · see citing works

Chaperone signalling complexes in Alzheimer's disease

Koren, J., Jinwal, U. K., Lee, D. C., Jones, J. R., Shults, C. L., Johnson, A. G., Anderson, L. J., & Dickey, C. A. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00557.x · Cited by 140 · see citing works

A role for FKBP52 in tau protein function

Chambraud, B., Sardin, E., Giustiniani, J., Dounane, O., Schumacher, M., Goedert, M., & Baulieu, E.-E. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914957107 · Cited by 140 · see citing works

Activation of the DNA Damage Response by RNA Viruses

Ryan, E. L., Hollingworth, R., & Grand, R. J. A. (2016) · Biomolecules · doi:10.3390/biom6010002 · Cited by 136 · see citing works

Induction of a transmissible tau pathology by traumatic brain injury

Zanier, E. R., Bertani, I., Sammali, E., Pischiutta, F., Chiaravalloti, M. A., Vegliante, G., Masone, A., Corbelli, A., Smith, D. H., Menon, D. K., et al. (2018) · Brain · doi:10.1093/brain/awy193 · Cited by 136 · see citing works

Trehalose rescues Alzheimer's disease phenotypes in APP/PS1 transgenic mice

Du, J., Liang, Y., Xu, F., Sun, B., & Wang, Z. (2013) · Journal of Pharmacy and Pharmacology · doi:10.1111/jphp.12108 · Cited by 134 · see citing works

Tau‐targeted treatment strategies in Alzheimer's disease

Götz, J., Ittner, A., & Ittner, L. M. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01713.x · Cited by 127 · see citing works

The Role of the Lipid Bilayer in Tau Aggregation

Elbaum‐Garfinkle, S., Ramlall, T. F., & Rhoades, E. R. (2010) · Biophysical Journal · doi:10.1016/j.bpj.2010.03.013 · Cited by 127 · see citing works

Double-Edged Sword of Tumour Suppressor Genes in Schizophrenia

Zhuo, C., Wang, D., Zhou, C., Chen, C., Li, J., Tian, H., Li, S., Ji, F., Liu, C., Chen, M., et al. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00001 · Cited by 127 · see citing works

Exosomal miRNAs as potential biomarkers of cardiovascular risk in children

Khalyfa, A., & Gozal, D. (2014) · Journal of Translational Medicine · doi:10.1186/1479-5876-12-162 · Cited by 126 · see citing works

Synaptic alterations in the rTg4510 mouse model of tauopathy

Kopeikina, K. J., Polydoro, M., Tai, H., Yaeger, E., Carlson, G. A., Pitstick, R., Hyman, B. T., & Spires‐Jones, T. L. (2012) · The Journal of Comparative Neurology · doi:10.1002/cne.23234 · Cited by 125 · see citing works

Pathological Tau From Alzheimer’s Brain Induces Site-Specific Hyperphosphorylation and SDS- and Reducing Agent-Resistant Aggregation of Tau in vivo

Miao, J., Shi, R., Li, L., Chen, F., Zhou, Y., Tung, Y. C., Hu, W. H., Gong, C., Iqbal, K., & Liu, F. (2019) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2019.00034 · Cited by 125 · see citing works

Soluble Aβ Promotes Wild-Type Tau Pathology<i>In Vivo</i>

Chabrier, M. A., Blurton-Jones, M., Agazaryan, A. A., Nerhus, J. L., Martinez-Coria, H., & LaFerla, F. M. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0172-12.2012 · Cited by 123 · see citing works

Propagation of tau pathology in Alzheimer’s disease: identification of novel therapeutic targets

Pooler, A. M., Polydoro, M., Wegmann, S., Nicholls, S. B., Spires‐Jones, T. L., & Hyman, B. T. (2013) · Alzheimer s Research & Therapy · doi:10.1186/alzrt214 · Cited by 122 · see citing works

Acetylation changes tau interactome to degrade tau in Alzheimer’s disease animal and organoid models

Choi, H., Kim, H. J., Yang, J., Chae, S., Lee, W., Chung, S., Kim, J., Choi, H., Song, H., Lee, C. K., et al. (2019) · Aging Cell · doi:10.1111/acel.13081 · Cited by 122 · see citing works

Phosphodiesterase-4 (PDE4) Molecular Pharmacology and Alzheimer's Disease

Gurney, M. E., D'Amato, E. C., & Burgin, A. B. (2015) · Neurotherapeutics · doi:10.1007/s13311-014-0309-7 · Cited by 121 · see citing works

Survival of adult neurons lacking cholesterol synthesis in vivo

Fünfschilling, U., Saher, G., Xiao, L., Möbius, W., & Nave, K.-A. (2007) · BMC Neuroscience · doi:10.1186/1471-2202-8-1 · Cited by 120 · see citing works

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 · see citing works

The case for soluble Aβ oligomers as a drug target in Alzheimer's disease

Hefti, F. F., Goure, W. F., Jerecı̀ć, J., Iverson, K. S., Walicke, P. A., & Krafft, G. A. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.03.002 · Cited by 119 · see citing works

Neurofibrillary Pathology in Transgenic Mice Overexpressing V717F β-Amyloid Precursor Protein

Masliah, E., Sisk, A., Mallory, M. E., & Games, D. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.4.357 · Cited by 117 · see citing works

Spreading of α-Synuclein and Tau: A Systematic Comparison of the Mechanisms Involved

Vasili, E., Dominguez‐Meijide, A., & Outeiro, T. F. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00107 · Cited by 117 · see citing works

Pin1 has opposite effects on wild-type and P301L tau stability and tauopathy

Lim, J., Balaštík, M., Lee, T. H., Nakamura, K., Liou, Y., Sun, A., Finn, G., Pastorino, L., Lee, V. M. ‐., & Lu, K. P. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34308 · Cited by 116 · see citing works

Phosphorylated, but not native, tau protein assembles following reaction with the lipid peroxidation product, 4‐hydroxy‐2‐nonenal

Pérez, M., Cuadros, R., Smith, M. A., Perry, G. L., & Ávila, J. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02323-1 · Cited by 116 · see citing works

Alzheimer’s disease as type 3 diabetes: understanding the link and implications

Kciuk, M., Kruczkowska, W., Gałęziewska, J., Wanke, K., Kałuzińska-Kołat, Ż., Aleksandrowicz, M., & Kontek, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252211955 · Cited by 98 · see citing works

The neuroinflammatory role of microglia in Alzheimer's disease and their associated therapeutic targets

AmeliMojarad, M., & AmeliMojarad, M. (2024) · CNS Neuroscience &amp; Therapeutics · doi:10.1111/cns.14856 · Cited by 73 · see citing works

Recent Advances in Therapeutics for the Treatment of Alzheimer’s Disease

Thawabteh, A. M., Ghanem, A. W., AbuMadi, S., Thaher, D., Jaghama, W., Karaman, D., & Karaman, R. (2024) · Molecules · doi:10.3390/molecules29215131 · Cited by 56 · see citing works

The Interaction Between NF-κB and Estrogen in Alzheimer’s Disease

Mishra, P., Davies, D. A., & Albensi, B. C. (2023) · Molecular Neurobiology · doi:10.1007/s12035-022-03152-3 · Cited by 51 · see citing works

Toward a Unified Framework in Molecular Neurobiology of Alzheimer’s Disease: Revisiting the Pathophysiological Hypotheses

Hein, Z. M., Karikalan, B., Gopalakrishna, P. K., Dhevi, K., Alkatiri, A., Hussan, F., Mohd Moklas, M. A., Jagadeesan, S., Che Ramli, M. D., Che Mohd Nassir, C. M. N., et al. (2026) · Molecular Neurobiology · doi:10.1007/s12035-025-05602-0 · Cited by 43 · see citing works

Reelin links Apolipoprotein E4, Tau, and Amyloid‐β in Alzheimer’s disease

Yi, L. X., Zeng, L., Wang, Q., Tan, E. K., & Zhou, Z. D. (2024) · Ageing Research Reviews · doi:10.1016/j.arr.2024.102339 · Cited by 41 · see citing works

Amelioration of Amyloid‐β Induced Alzheimer's Disease by <i>Bacopa monnieri</i> through Modulation of Mitochondrial Dysfunction and GSK‐3β/Wnt/β‐Catenin Signaling

Sushma, Sahu, M. R., Murugan, N. A., & Mondal, A. C. (2024) · Molecular Nutrition &amp; Food Research · doi:10.1002/mnfr.202300245 · Cited by 17 · see citing works

Molecular mechanisms of Alzheimer’s disease: From therapeutic targets to promising drugs

Alan, E., Kerry, Z., & Sevin, G. (2023) · Fundamental &amp; Clinical Pharmacology · doi:10.1111/fcp.12861 · Cited by 17 · see citing works

The application of artificial intelligence in diagnosis of Alzheimer’s disease: a bibliometric analysis

An, X., He, J., Bi, B., Wu, G., Xu, J., Yu, W., & Ren, Z. (2024) · Frontiers in Neurology · doi:10.3389/fneur.2024.1510729 · Cited by 16 · see citing works

Short-term exposure to dim light at night disrupts rhythmic behaviors and causes neurodegeneration in fly models of tauopathy and Alzheimer's disease

Kim, M., Subramanian, M., Cho, Y.-H., Kim, G.-H., Lee, E., & Park, J. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.12.021 · Cited by 51 · see citing works

P-tau217 correlates with neurodegeneration in Alzheimer’s disease, and targeting p-tau217 with immunotherapy ameliorates murine tauopathy

Zhang, D., Zhang, W., Chen, M., Gao, X., Yuan, H., Lin, X., Mao, X., Wang, C., Guo, X., Du, Y., et al. (2024) · Neuron · doi:10.1016/j.neuron.2024.02.017 · Cited by 74 · see citing works

A Genomic Screen for Modifiers of Tauopathy Identifies Puromycin-Sensitive Aminopeptidase as an Inhibitor of Tau-Induced Neurodegeneration

Karsten, S. L., Sang, T.-K., Gehman, L. T., Chatterjee, S., Liu, J., Lawless, G. M., Sengupta, S., Berry, R. W., Pomakian, J., Oh, H. S., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.019 · Cited by 147 · see citing works

The inhibition of LSD1 via sequestration contributes to tau-mediated neurodegenerationPreprint

Engstrom, A. K., Walker, A. C., Moudgal, R. A., et al. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/745133

Amphiphysin-1 protein level changes associated with tau-mediated neurodegeneration

Jesús‐Cortés, H. D., Nogueras‐Ortiz, C. J., Gearing, M., Arnold, S. E., & Vega, I. E. (2012) · Neuroreport · doi:10.1097/wnr.0b013e32835982ce · Cited by 31 · see citing works