Tau and tauopathies

Neuropathological stageing of Alzheimer-related changes.

Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · see citing works

Gene Dose of Apolipoprotein E Type 4 Allele and the Risk of Alzheimer's Disease in Late Onset Families

Corder, E. H., Saunders, A. M., Strittmatter, W. J., Schmechel, D. E., Gaskell, P. C., Small, G. W., Roses, A. D., Haines, J. L., & Pericak-Vance, M. A. (1993) · Science · doi:10.1126/science.8346443 · Cited by 9,429 · see citing works

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes

MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366 · see citing works

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis

Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576 · see citing works

Novel Proteinaceous Infectious Particles Cause Scrapie

Prusiner, S. B. (1982) · Science · doi:10.1126/science.6801762 · Cited by 5,121 · see citing works

Frontotemporal lobar degeneration: A consensus on clinical diagnostic criteria

Neary, D., Snowden, J. S., Gustafson, L., Passant, U., Stuss, D., Black, S., Freedman, M., Kertesz, A., Robert, P. H., Albert, M., et al. (1998) · Neurology · doi:10.1212/wnl.51.6.1546 · Cited by 5,047 · see citing works

Interactive tree of life (iTOL) v3: an online tool for the display and annotation of phylogenetic and other trees

Letunic, I., & Bork, P. (2016) · Nucleic Acids Res. · doi:10.1093/nar/gkw290 · Cited by 4,851 · see citing works

Hypothetical model of dynamic biomarkers of the Alzheimer's pathological cascade

Jack, C. R., Knopman, D. S., Jagust, W. J., Shaw, L. M., Aisen, P. S., Weiner, M. W., Petersen, R. C., & Trojanowski, J. Q. (2010) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70299-6 · Cited by 4,806 · see citing works

Tracking pathophysiological processes in Alzheimer's disease: an updated hypothetical model of dynamic biomarkers

Jack, C. R., Knopman, D. S., Jagust, W. J., Petersen, R. C., Weiner, M. W., Aisen, P. S., Shaw, L. M., Vemuri, P., Wiste, H. J., Weigand, S. D., et al. (2013) · The Lancet Neurology · doi:10.1016/s1474-4422(12)70291-0 · Cited by 4,396 · see citing works

Genetic instabilities in human cancers

Lengauer, C., Kinzler, K. W., & Vogelstein, B. (1998) · Nature · doi:10.1038/25292 · Cited by 4,168 · see citing works

BioGRID: a general repository for interaction datasets

Stark, C. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj109 · Cited by 3,960 · see citing works

Clinical and biomarker changes in dominantly inherited Alzheimer's disease

Bateman, R. J., Xiong, C., Benzinger, T. L. S., Fagan, A. M., Goate, A., Fox, N. C., Marcus, D. S., Cairns, N. J., Xie, X., Blazey, T. M., et al. (2012) · New England Journal of Medicine · doi:10.1056/nejmoa1202753 · Cited by 3,814 · see citing works

Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory

Shankar, G. M., Li, S., Mehta, T. H., Garcia-Munoz, A., Shepardson, N. E., Smith, I., Brett, F. M., Farrell, M. A., Rowan, M. J., Lemere, C. A., et al. (2008) · Nature Medicine · doi:10.1038/nm1782 · Cited by 3,685 · see citing works

Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology.

Grundke-Iqbal, I., Iqbal, K., Tung, Y. C., Quinlan, M., Wisniewski, H. M., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.13.4913 · Cited by 3,676 · see citing works

Association of missense and 5′-splice-site mutations in tau with the inherited dementia FTDP-17

Hutton, M., Lendon, C. L., Rizzu, P., Baker, M., Froelich, S., Houlden, H., Pickering-Brown, S., Chakraverty, S., Isaacs, A., Grover, A., et al. (1998) · Nature · doi:10.1038/31508 · Cited by 3,498 · see citing works

Protein aggregation and neurodegenerative disease

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

The Blood-Brain Barrier in Health and Chronic Neurodegenerative Disorders

Zlokovic, B. V. (2008) · Neuron · doi:10.1016/j.neuron.2008.01.003 · Cited by 3,280 · see citing works

PhosphoSitePlus, 2014: mutations, PTMs and recalibrations

Hornbeck, P. V., Zhang, B., Murray, B., Kornhauser, J. M., Latham, V. M., & Skrzypek, E. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1267 · Cited by 3,243 · see citing works

Human Protein Reference Database--2009 update

Prasad, T. S. K., Goel, R., Kandasamy, K., Keerthikumar, S., Kumar, S., Mathivanan, S., Telikicherla, D., Raju, R., Shafreen, R. B., Venugopal, A., et al. (2008) · Nucleic Acids Research · doi:10.1093/nar/gkn892 · Cited by 3,241 · see citing works

Staging of Alzheimer disease-associated neurofibrillary pathology using paraffin sections and immunocytochemistry

Braak, H., Alafuzoff, I., Arzberger, T., Kretzschmar, H., & Del Tredici, K. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0127-z · Cited by 3,172 · 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

Mutations in LRRK2 Cause Autosomal-Dominant Parkinsonism with Pleomorphic Pathology

Zimprich, A. A., Biskup, S., Leitner, P., Lichtner, P., Farrer, M. J., Lincoln, S., Kachergus, J. M., Hulihan, M., Uitti, R. J., Calne, D. B., et al. (2004) · Neuron · doi:10.1016/j.neuron.2004.11.005 · Cited by 3,024 · see citing works

<i>TREM2</i> Variants in Alzheimer's Disease

Guerreiro, R., Wojtas, A., Bras, J., Carrasquillo, M., Rogaeva, E., Majounie, E., Cruchaga, C., Sassi, C., Kauwe, J. S. K., Younkin, S., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1211851 · Cited by 3,020 · see citing works

Primary Progressive Aphasia

Weıntraub, S. (1990) · Archives of Neurology · doi:10.1001/archneur.1990.00530120075013 · Cited by 3,012 · see citing works

National Institute on Aging–Alzheimer’s Association guidelines for the neuropathologic assessment of Alzheimer’s disease: a practical approach

Montine, T. J., Phelps, C. H., Beach, T. G., Bigio, E. H., Cairns, N. J., Dickson, D. W., Duyckaerts, C., Frosch, M. P., Masliah, E., Mirra, S. S., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-011-0910-3 · Cited by 2,992 · see citing works

TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis

Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732 · 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

Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6

Vance, C. A., Rogelj, B., Hortobágyi, T., Vos, K. J. D., Nishimura, A. L., Sreedharan, J., Hu, X., Smith, B. N., Ruddy, D., Wright, P. D., et al. (2009) · Science · doi:10.1126/science.1165942 · Cited by 2,567 · see citing works

Variant of <i>TREM2</i> Associated with the Risk of Alzheimer's Disease

Jonsson, T., Stefansson, H., Steinberg, S., Jonsdottir, I., Jonsson, P. V., Snaedal, J., Bjornsson, S., Huttenlocher, J., Levey, A. I., Lah, J. J., et al. (2013) · New England Journal of Medicine · doi:10.1056/nejmoa1211103 · Cited by 2,558 · see citing works

Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis

Kwiatkowski, T. J., Bosco, D. A., LeClerc, A. L., Tamrazian, E., Vanderburg, C. R., Russ, C., Davis, A., Gilchrist, J. M., Kasarskis, E. J., Munsat, T. L., et al. (2009) · Science · doi:10.1126/science.1166066 · Cited by 2,555 · see citing works

Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease

Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492 · see citing works

Neurodegenerative Tauopathies

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

Neurodegenerative Diseases Target Large-Scale Human Brain Networks

Seeley, W. W., Crawford, R. K., Zhou, J., Miller, B. L., & Greicius, M. D. (2009) · Neuron · doi:10.1016/j.neuron.2009.03.024 · Cited by 2,350 · see citing works

Chronic traumatic encephalopathy in athletes: Progressive tauopathy after repetitive head injury

McKee, A. C., Cantu, R. C., Nowinski, C. J., Hedley-Whyte, E. T., Gavett, B. E., Budson, A. E., Santini, V. E., Lee, H.-S., Kubilus, C. A., & Stern, R. A. (2009) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/nen.0b013e3181a9d503 · Cited by 2,295 · 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

Stages of the Pathologic Process in Alzheimer Disease: Age Categories From 1 to 100 Years

Braak, H., Thal, D. R., Ghebremedhin, E., & Del Tredici, K. (2011) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/nen.0b013e318232a379 · 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

The spectrum of disease in chronic traumatic encephalopathy

McKee, A. C., Stein, T. D., Nowinski, C. J., Stern, R. A., Daneshvar, D. H., Alvarez, V. E., Lee, H.-S., Hall, G., Wojtowicz, S. M., Baugh, C. M., et al. (2013) · Brain · doi:10.1093/brain/aws307 · Cited by 2,098 · see citing works

Correlation of Alzheimer Disease Neuropathologic Changes With Cognitive Status: A Review of the Literature

Nelson, P. T., Alafuzoff, I., Bigio, E. H., Bouras, C., Braak, H., Cairns, N. J., Castellani, R. J., Crain, B. J., Davies, P., Tredici, K. D., et al. (2012) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/nen.0b013e31825018f7 · Cited by 2,050 · see citing works

Tau Suppression in a Neurodegenerative Mouse Model Improves Memory Function

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

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 2,007 · see citing works

Common variants at ABCA7, MS4A6A/MS4A4E, EPHA1, CD33 and CD2AP are associated with Alzheimer's disease

Initiative, T. A. D. N., Hollingworth, P., CHARGE consortium, EADI1 consortium, Harold, D., Sims, R., Gerrish, A., Lambert, J.-C., Carrasquillo, M. M., Abraham, R., et al. (2011) · Nature Genetics · doi:10.1038/ng.803 · Cited by 1,997 · see citing works

Common variants at MS4A4/MS4A6E, CD2AP, CD33 and EPHA1 are associated with late-onset Alzheimer's disease

Naj, A. C., Jun, G., Beecham, G. W., Wang, L.-S., Vardarajan, B. N., Buros, J., Gallins, P. J., Buxbaum, J. D., Jarvik, G. P., Crane, P. K., et al. (2011) · Nature Genetics · doi:10.1038/ng.801 · Cited by 1,901 · see citing works

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 · see citing works

Oxidative stress in neurodegeneration: Cause or consequence?

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

The MIntAct project—IntAct as a common curation platform for 11 molecular interaction databases

Orchard, S. E., Ammari, M. G., Aranda, B., Breuza, L., Briganti, L., Broackes-Carter, F. C., Campbell, N. H., Chavali, G. B., Chen, C. C. L., del‐Toro, N., et al. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt1115 · Cited by 1,835 · 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

Microtubule-associated protein tau. A component of Alzheimer paired helical filaments.

Grundke, I., Iqbal, K., Quinlan, M., Tung, Y. C., Zaidi, M. S., & Wisniewski, H. M. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38495-8 · Cited by 1,780 · see citing works

A tissue-specific atlas of mouse protein phosphorylation and expression

Huttlin, E. L., Jedrychowski, M. P., Elias, J. E., Goswami, T., Rad, R., Beausoleil, S. A., Villén, J., Haas, W., Sowa, M. E., & Gygi, S. P. (2010) · Cell · doi:10.1016/j.cell.2010.12.001 · Cited by 1,778 · 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

Frequency of Stages of Alzheimer-Related Lesions in Different Age Categories

Braak, H., & Braak, E. (1997) · Neurobiology of Aging · doi:10.1016/s0197-4580(97)00056-0 · Cited by 1,656 · 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

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

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

Clinical and Pathological Diagnosis of Frontotemporal Dementia

McKhann, G. M. (2001) · Archives of Neurology · doi:10.1001/archneur.58.11.1803 · Cited by 1,475 · see citing works

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

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

Primary age-related tauopathy (PART): a common pathology associated with human aging

Crary, J. F., Trojanowski, J. Q., Schneider, J. A., Abisambra, J. F., Abner, E. L., Alafuzoff, I., Arnold, S. E., Attems, J., Beach, T. G., Bigio, E. H., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1349-0 · Cited by 1,467 · see citing works

Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease.

Kosik, K. S., Joachim, C. L., & Selkoe, D. J. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4044 · Cited by 1,462 · see citing works

Mechanisms of specificity in protein phosphorylation

Ubersax, J. A., & Ferrell Jr, J. E. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2203 · Cited by 1,451 · 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

A68: a Major Subunit of Paired Helical Filaments and Derivatized Forms of Normal Tau

Lee, V. M.-Y., Balin, B. J., Otvos, L., & Trojanowski, J. Q. (1991) · Science · doi:10.1126/science.1899488 · Cited by 1,418 · see citing works

Tau is a candidate gene for chromosome 17 frontotemporal dementia

Poorkaj, P., Bird, T. D., Wijsman, E., Nemens, E., Garruto, R. M., Anderson, L., Andreadis, A., Wiederholt, W. C., Raskind, M., & Schellenberg, G. D. (1998) · Annals of Neurology · doi:10.1002/ana.410430617 · Cited by 1,374 · 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

The Human Gene Mutation Database: building a comprehensive mutation repository for clinical and molecular genetics, diagnostic testing and personalized genomic medicine

Stenson, P. D., Mort, M. E., Ball, E. V., Shaw, K., Phillips, A. D., & Cooper, D. N. (2013) · Human Genetics · doi:10.1007/s00439-013-1358-4 · Cited by 1,350 · 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

Genome-wide Analysis of Genetic Loci Associated With Alzheimer Disease

Seshadri, S. (2010) · JAMA · doi:10.1001/jama.2010.574 · Cited by 1,219 · see citing works

Axonopathy and Transport Deficits Early in the Pathogenesis of Alzheimer’s Disease

Stokin, G. B., Lillo, C., Falzone, T. L., Brusch, R. G., Rockenstein, E., Mount, S. L., Raman, R., Davies, P., Masliah, E., Williams, D. S., et al. (2005) · Science · doi:10.1126/science.1105681 · Cited by 1,214 · see citing works

PET Imaging of Tau Deposition in the Aging Human Brain

Schöll, M., Lockhart, S. N., Schonhaut, D. R., O’Neil, J. P., Janabi, M., Ossenkoppele, R., Baker, S. L., Vogel, J. W., Faria, J., Schwimmer, H. D., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.01.028 · Cited by 1,214 · see citing works

Tau PET patterns mirror clinical and neuroanatomical variability in Alzheimer’s disease

Ossenkoppele, R., Schonhaut, D. R., Schöll, M., Lockhart, S. N., Ayakta, N., Baker, S. L., O’Neil, J. P., Janabi, M., Lazaris, A., Cantwell, A., et al. (2016) · Brain · doi:10.1093/brain/aww027 · Cited by 1,185 · see citing works

Metabolic Rate and Body Temperature Reduction During Hibernation and Daily Torpor

Geiser, F. (2004) · Annual Review of Physiology · doi:10.1146/annurev.physiol.66.032102.115105 · Cited by 1,135 · see citing works

Cloning and sequencing of the cDNA encoding a core protein of the paired helical filament of Alzheimer disease: identification as the microtubule-associated protein tau

Goedert, M., Wischik, C. M., Crowther, R. A., Walker, J. E., & Klug, A. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.11.4051 · Cited by 1,134 · see citing works

Tau pathology and neurodegeneration

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

Tau Mislocalization to Dendritic Spines Mediates Synaptic Dysfunction Independently of Neurodegeneration

Hoover, B. R., Reed, M. N., Su, J., Penrod, R. D., Kotilinek, L. A., Grant, M. K., Pitstick, R., Carlson, G. A., Lanier, L. M., Yuan, L.-L., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.11.030 · Cited by 1,118 · see citing works

Tangle and neuron numbers, but not amyloid load, predict cognitive status in Alzheimer’s disease

Giannakopoulos, P., Herrmann, F. R., Bussière, T., Bouras, C., Kövari, E., Perl, D. P., Morrison, J. H., Gold, G., & Hof, P. R. (2003) · Neurology · doi:10.1212/01.wnl.0000063311.58879.01 · Cited by 1,118 · see citing works

Tau proteins of alzheimer paired helical filaments: Abnormal phosphorylation of all six brain isoforms

Goedert, M., Spillantini, M. G., Cairns, N. J., & Crowther, R. A. (1992) · Neuron · doi:10.1016/0896-6273(92)90117-v · Cited by 1,114 · see citing works

Neuropathologic diagnostic and nosologic criteria for frontotemporal lobar degeneration: consensus of the Consortium for Frontotemporal Lobar Degeneration

Cairns, N. J., Bigio, E. H., Mackenzie, I. R. A., Neumann, M., Lee, V. M.-Y., Hatanpaa, K. J., White, C. L., Schneider, J. A., Grinberg, L. T., Halliday, G., et al. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0237-2 · Cited by 1,110 · see citing works

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

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

Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans

Goedert, M., Jakes, R., Spillantini, M. G., Hasegawa, M., Smith, M. J., & Crowther, R. A. (1996) · Nature · doi:10.1038/383550a0 · Cited by 1,036 · see citing works

Classification and basic pathology of Alzheimer disease

Duyckaerts, C., Delatour, B., & Potier, M.-C. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0532-1 · Cited by 1,031 · see citing works

Paired Helical Filaments in Electron Microscopy of Alzheimer's Disease

KIDD, M. (1963) · Nature · doi:10.1038/197192b0 · Cited by 1,012 · see citing works

Differential Regulation of Dynein and Kinesin Motor Proteins by Tau

Dixit, R., Ross, J. L., Goldman, Y. E., & Holzbaur, E. L. F. (2008) · Science · doi:10.1126/science.1152993 · Cited by 1,012 · see citing works

Nomenclature and nosology for neuropathologic subtypes of frontotemporal lobar degeneration: an update

Mackenzie, I. R. A., Neumann, M., Bigio, E. H., Cairns, N. J., Alafuzoff, I., Kril, J., Kovacs, G. G., Ghetti, B., Halliday, G., Holm, I. E., et al. (2010) · Acta Neuropathologica · doi:10.1007/s00401-009-0612-2 · Cited by 1,012 · 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

Trans-Synaptic Spread of Tau Pathology In Vivo

Liu, L., Drouet, V., Wu, J., Witter, M. P., Small, S. A., Clelland, C. L. T., & Duff, K. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031302 · Cited by 994 · see citing works

Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies

Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., et al. (2014) · Neuron · doi:10.1016/j.neuron.2014.04.047 · Cited by 986 · see citing works

What does it mean to be natively unfolded?

Uversky, V. N. (2002) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02649.x · Cited by 985 · 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

Alzheimer’s and Parkinson’s diseases: The prion concept in relation to assembled Aβ, tau, and α-synuclein

Goedert, M. (2015) · Science · doi:10.1126/science.1255555 · Cited by 977 · see citing works

Neuropathologically defined subtypes of Alzheimer's disease with distinct clinical characteristics: a retrospective study

Murray, M. E., Graff-Radford, N. R., Ross, O. A., Petersen, R. C., Duara, R., & Dickson, D. W. (2011) · The Lancet Neurology · doi:10.1016/s1474-4422(11)70156-9 · Cited by 972 · see citing works

The MAP1 family of microtubule-associated proteins.

Dehmelt (2004) · Genome biology · doi:10.1186/gb-2004-6-1-204 · Cited by 972 · see citing works

Modulation of the dynamic instability of tubulin assembly by the microtubule-associated protein tau.

Drechsel, D. N., Hyman, A. A., Cobb, M. H., & Kirschner, M. W. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.10.1141 · Cited by 971 · see citing works

Ultradeep Human Phosphoproteome Reveals a Distinct Regulatory Nature of Tyr and Ser/Thr-Based Signaling

Sharma, K., D’Souza, R. C. J., Tyanova, S., Schaab, C., Wiśniewski, J. R., Cox, J., & Mann, M. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.07.036 · Cited by 971 · see citing works

Dentritic spines : structure, dynamics and regulation

Hering, H., & Sheng, M. (2001) · Nature Reviews Neuroscience · doi:10.1038/35104061 · Cited by 961 · see citing works

Identification of preclinical Alzheimer's disease by a profile of pathogenic proteins in neurally derived blood exosomes: A case‐control study

Fiandaca, M. S., Kapogiannis, D., Mapstone, M., Boxer, A., Eitan, E., Schwartz, J. B., Abner, E. L., Petersen, R. C., Federoff, H. J., Miller, B. L., et al. (2015) · Alzheimer's &amp; Dementia · doi:10.1016/j.jalz.2014.06.008 · Cited by 959 · see citing works

Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949 · see citing works

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

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

Expression of separate isoforms of human tau protein: correlation with the tau pattern in brain and effects on tubulin polymerization.

Goedert, M., & Jakes, R. (1990) · The EMBO Journal · doi:10.1002/j.1460-2075.1990.tb07870.x · Cited by 929 · see citing works

Abnormal tau phosphorylation at Ser396 in Alzheimer's disease recapitulates development and contributes to reduced microtubule binding

Bramblett, G. T., Goedert, M., Jakes, R., Merrick, S. E., Trojanowski, J. Q., & Lee, V. M. Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90057-x · Cited by 903 · see citing works

The many faces of tau

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

Physical and chemical properties of purified tau factor and the role of tau in microtubule assembly

Cleveland, D. W., Hwo, S. Y., & Kirschner, M. W. (1977) · Journal of Molecular Biology · doi:10.1016/0022-2836(77)90214-5 · Cited by 881 · see citing works

Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein

Giasson, B. I., Forman, M. S., Higuchi, M., Golbe, L. I., Graves, C. L., Kotzbauer, P. T., Trojanowski, J. Q., & Lee, V. M.-Y. (2003) · Science · doi:10.1126/science.1082324 · Cited by 879 · see citing works

MARK, a Novel Family of Protein Kinases That Phosphorylate Microtubule-Associated Proteins and Trigger Microtubule Disruption

Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80208-1 · Cited by 878 · see citing works

Postnatal development of locomotion in the laboratory rat

Altman, J., & Sudarshan, K. (1975) · Animal Behaviour · doi:10.1016/0003-3472(75)90114-1 · Cited by 861 · 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 848 · see citing works

Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease

Mori, H., Kondo, J., & Ihara, Y. (1987) · Science · doi:10.1126/science.3029875 · Cited by 843 · see citing works

The aftermath of boxing

Corsellis, J. A. N., Bruton, C. J., & Freeman-Browne, D. (1973) · Psychological Medicine · doi:10.1017/s0033291700049588 · Cited by 836 · see citing works

Actin in action: the interplay between the actin cytoskeleton and synaptic efficacy.

Cingolani, L. A., & Goda, Y. (2008) · Nature Reviews Neuroscience · doi:10.1038/nrn2373 · Cited by 831 · see citing works

Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease

Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., Lu, M., Fu, Y., Garcia-Sierra, F., LaPointe, N., et al. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1630428100 · Cited by 831 · see citing works

A common inversion under selection in Europeans

Stefánsson, H., Helgason, A., Þorleifsson, G., Steinthórsdóttir, V., Másson, G., Barnard, J., Baker, A., Jónasdóttir, Á., Ingason, A., Gudnadottir, V. G., et al. (2005) · Nature Genetics · doi:10.1038/ng1508 · Cited by 830 · see citing works

Overexpression of tau protein inhibits kinesin-dependent trafficking of vesicles, mitochondria, and endoplasmic reticulum: Implications for Alzheimer’s disease

Ebneth, A., Godemann, R., Stamer, K., Illenberger, S., Trinczek, B., Mandelkow, E.-M., & Mandelkow, E. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.3.777 · Cited by 820 · 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

Accumulation of abnormally phosphorylated τ precedes the formation of neurofibrillary tangles in Alzheimer's disease

Bancher, C., Brunner, C., Lassmann, H., Budka, H., Jellinger, K., Wiche, G., Seitelberger, F., Grundke-Iqbal, I., Iqbal, K., & Wisniewski, H. M. (1989) · Brain Research · doi:10.1016/0006-8993(89)91396-6 · Cited by 818 · see citing works

The pathological process underlying Alzheimer’s disease in individuals under thirty

Braak, H., & Del Tredici, K. (2011) · Acta Neuropathologica · doi:10.1007/s00401-010-0789-4 · Cited by 812 · see citing works

Conformational disease

Carrell, R. W., & Lomas, D. A. (1997) · The Lancet · doi:10.1016/s0140-6736(97)02073-4 · Cited by 811 · 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

Altered microtubule organization in small-calibre axons of mice lacking tau protein

Harada, A., Oguchi, K., Okabe, S., Kuno, J., Terada, S., Ohshima, T., Sato-Yoshitake, R., Takei, Y., Noda, T., & Hirokawa, N. (1994) · Nature · doi:10.1038/369488a0 · Cited by 806 · see citing works

Phosphorylation of Ser262 strongly reduces binding of tau to microtubules: Distinction between PHF-like immunoreactivity and microtubule binding

Biernat, J., Gustke, N., Drewes, G., Mandelkow, E., & Mandelkow, E. (1993) · Neuron · doi:10.1016/0896-6273(93)90279-z · Cited by 796 · see citing works

Spreading of pathology in neurodegenerative diseases: a focus on human studies

Brettschneider, J., Tredici, K. D., Lee, V. M.-Y., & Trojanowski, J. Q. (2015) · Nature Reviews Neuroscience · doi:10.1038/nrn3887 · Cited by 790 · see citing works

Association of an Extended Haplotype in the Tau Gene with Progressive Supranuclear Palsy

Baker, M., Litvan, I., Houlden, H., Adamson, J., Dickson, D., Perez-Tur, J., Hardy, J., Lynch, T., Bigio, E., & Hutton, M. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.4.711 · Cited by 781 · see citing works

Microtubule-associated protein tau. Abnormal phosphorylation of a non-paired helical filament pool in Alzheimer disease.

Köpke, E., Tung, Y. C., Shaikh, S., Alonso, A. C., Iqbal, K., & Grundke-Iqbal, I. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80536-5 · Cited by 779 · see citing works

O-GlcNAcylation regulates phosphorylation of tau: A mechanism involved in Alzheimer's disease

Liu, F., Iqbal, K., Grundke-Iqbal, I., Hart, G. W., & Gong, C.-X. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400348101 · Cited by 775 · see citing works

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

Braak, F., Braak, H., & Mandelkow, E. (1994) · Acta Neuropathologica · doi:10.1007/bf00293315 · Cited by 773 · see citing works

The case for rejecting the amyloid cascade hypothesis

Herrup, K. (2015) · Nature Neuroscience · doi:10.1038/nn.4017 · Cited by 768 · see citing works

Imaging of Tau Pathology in a Tauopathy Mouse Model and in Alzheimer Patients Compared to Normal Controls

Maruyama, M., Shimada, H., Suhara, T., Shinotoh, H., Ji, B., Maeda, J., Zhang, M.-R., Trojanowski, J. Q., Lee, V. M.-Y., Ono, M., et al. (2013) · Neuron · doi:10.1016/j.neuron.2013.07.037 · Cited by 760 · 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

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 759 · see citing works

The Pathogenesis of Senile Plaques

DICKSON, D. W. (1997) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199704000-00001 · Cited by 753 · see citing works

Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau)

Wood, J. G., Mirra, S. S., Pollock, N. J., & Binder, L. I. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.11.4040 · Cited by 749 · see citing works

Abundant Tau Filaments and Nonapoptotic Neurodegeneration in Transgenic Mice Expressing Human P301S Tau Protein

Allen, B., Ingram, E., Takao, M., Smith, M. J., Jakes, R., Virdee, K., Yoshida, H., Holzer, M., Craxton, M., Emson, P. C., et al. (2002) · Journal of Neuroscience · doi:10.1523/jneurosci.22-21-09340.2002 · Cited by 746 · see citing works

Glycogen synthase kinase-3 induces Alzheimer's disease-like phosphorylation of tau: Generation of paired helical filament epitopes and neuronal localisation of the kinase

Hanger, D. P., Hughes, K., Woodgett, J. R., Brion, J.-P., & Anderton, B. H. (1992) · Neuroscience Letters · doi:10.1016/0304-3940(92)90774-2 · Cited by 737 · see citing works

Characteristics of two distinct clinical phenotypes in pathologically proven progressive supranuclear palsy: Richardson's syndrome and PSP-parkinsonism

Williams, D. R., de Silva, R., Paviour, D. C., Pittman, A. M., Watt, H., Kilford, L., Holton, J. L., Révész, T., & Lees, A. J. (2005) · Brain · doi:10.1093/brain/awh488 · Cited by 733 · see citing works

A preparation of Alzheimer paired helical filaments that displays distinct tau proteins by polyacrylamide gel electrophoresis.

Greenberg, S. G., & Davies, P. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.15.5827 · Cited by 732 · see citing works

Office of Rare Diseases Neuropathologic Criteria for Corticobasal Degeneration

Dickson, D. W., Bergeron, C., Chin, S. S., Duyckaerts, C., Horoupian, D., Ikeda, K., Jellinger, K., Lantos, P. L., Lippa, C. F., Mirra, S. S., et al. (2002) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1093/jnen/61.11.935 · Cited by 724 · see citing works

The acetylation of tau inhibits its function and promotes pathological tau aggregation

Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., & Lee, V. M. Y. (2011) · Nature Communications · doi:10.1038/ncomms1255 · Cited by 724 · see citing works

A new subtype of frontotemporal lobar degeneration with FUS pathology

Neumann, M., Rademakers, R., Roeber, S., Baker, M., Kretzschmar, H. A., & Mackenzie, I. R. A. (2009) · Brain · doi:10.1093/brain/awp214 · Cited by 722 · see citing works

The prolyl isomerase Pin1 restores the function of Alzheimer-associated phosphorylated tau protein

Lu, P.-J., Wulf, G., Zhou, X. Z., Davies, P., & Lu, K. P. (1999) · Nature · doi:10.1038/21650 · Cited by 721 · see citing works

über eigenartige Krankheitsfälle des späteren Alters

Alzheimer, A. (1911) · Zeitschrift für die gesamte Neurologie und Psychiatrie · doi:10.1007/bf02866241 · Cited by 717 · see citing works

Advanced Maillard reaction end products are associated with Alzheimer disease pathology.

Smith, M. A., Taneda, S., Richey, P. L., Miyata, S., Yan, S. D., Stern, D., Sayre, L. M., Monnier, V. M., & Perry, G. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.12.5710 · Cited by 715 · see citing works

Critical role of soluble amyloid-β for early hippocampal hyperactivity in a mouse model of Alzheimer’s disease

Busche, M. A., Chen, X., Henning, H. A., Reichwald, J., Staufenbiel, M., Sakmann, B., & Konnerth, A. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1206171109 · Cited by 715 · see citing works

Predicting Regional Neurodegeneration from the Healthy Brain Functional Connectome

Zhou, J., Gennatas, E. D., Kramer, J. H., Miller, B. L., & Seeley, W. W. (2012) · Neuron · doi:10.1016/j.neuron.2012.03.004 · Cited by 706 · see citing works

Tau Protein Hyperphosphorylation and Aggregation in Alzheimer’s Disease and Other Tauopathies, and Possible Neuroprotective Strategies

Šimić, G., Leko, M. B., Wray, S., Harrington, C. R., Delalle, I., Milošević, N. J., Bažadona, D., Buée, L., de Silva, R., Giovanni, G. D., et al. (2016) · Biomolecules · doi:10.3390/biom6010006 · Cited by 698 · see citing works

Psychiatrie: Ein Lehrbuch für Studierende und Ärzte

Kraepelin, E. (1939) · JAMA · doi:10.1001/jama.1939.02800520075036 · Cited by 689 · see citing works

Aβ Oligomers Cause Localized Ca ²⁺ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines

Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686 · see citing works

Epilepsy and Cognitive Impairments in Alzheimer Disease

Palop, J. J. (2009) · Archives of Neurology · doi:10.1001/archneurol.2009.15 · Cited by 684 · see citing works

Tau protein pathology in neurodegenerative diseases

Spillantini, M. G., & Goedert, M. (1998) · Trends in Neurosciences · doi:10.1016/s0166-2236(98)01337-x · Cited by 683 · see citing works

Early Clinical PET Imaging Results with the Novel PHF-Tau Radioligand [F18]-T808

Chien, D. T., Szardenings, A. K., Bahri, S., Walsh, J. C., Mu, F., Xia, C. A., Shankle, W. R., Lerner, A. J., Su, M., Elizarov, A. M., et al. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-130098 · Cited by 676 · 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

Cerebrospinal Fluid Levels ofβ-Amyloid 1-42, but Not of Tau, Are Fully Changed Already 5 to 10 Years Before the Onset of Alzheimer Dementia

Buchhave, P. (2012) · Archives of General Psychiatry · doi:10.1001/archgenpsychiatry.2011.155 · Cited by 664 · see citing works

TDP-43 proteinopathy and motor neuron disease in chronic traumatic encephalopathy

McKee, A. C., Gavett, B. E., Stern, R. A., Nowinski, C. J., Cantu, R. C., Kowall, N. W., Perl, D. P., Hedley-Whyte, E. T., Price, B., Sullivan, C., et al. (2010) · Journal of Neuropathology &amp; Experimental Neurology · doi:10.1097/nen.0b013e3181ee7d85 · Cited by 659 · see citing works

Use of structural magnetic resonance imaging to predict who will get Alzheimer's disease

Killiany, R., Gómez‐Isla, T., Moss, M. B., Kikinis, R., Sándor, T., Jolesz, F. A., Tanzi, R. E., Jones, K. J., Hyman, B. T., & Albert, M. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200004)47:4 · Cited by 659 · see citing works

Clinicopathologic Studies in Cognitively Healthy Aging and Alzheimer Disease: Relation of Histologic Markers to Dementia Severity, Age, Sex, and Apolipoprotein E Genotype

Berg, L., McKeel, D. W., Miller, J. P., Storandt, M., Rubin, E. H., Morris, J. C., Baty, J., Coats, M., Norton, J., Goate, A. M., et al. (1998) · Archives of Neurology · doi:10.1001/archneur.55.3.326 · Cited by 657 · see citing works

Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons

Cáceres, A., & Kosik, K. S. (1990) · Nature · doi:10.1038/343461a0 · Cited by 657 · see citing works

Domains of tau Protein and Interactions with Microtubules

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

Amyloid-β/Fyn–Induced Synaptic, Network, and Cognitive Impairments Depend on Tau Levels in Multiple Mouse Models of Alzheimer's Disease

Roberson, E. D., Halabisky, B., Yoo, J. W., Yao, J., Chin, J., Yan, F., Wu, T., Hamto, P., Devidze, N., Yu, G.-Q., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.4152-10.2011 · Cited by 654 · see citing works

Early clinical PET imaging results with the novel PHF-tau radioligand [F-18]-T807

Chien, D. T., Bahri, S., Szardenings, A. K., Walsh, J. C., Mu, F., Su, M.-Y., Shankle, W. R., Elizarov, A., & Kolb, H. C. (2013) · Journal of Alzheimer's Disease · doi:10.3233/jad-122059 · Cited by 651 · see citing works

The high-affinity HSP90–CHIP complex recognizes and selectively degrades phosphorylated tau client proteins

Dickey, C. A., Kamal, A., Lundgren, K., Klosak, N., Bailey, R. M., Dunmore, J., Ash, P., Shoraka, S., Zlatkovic, J., Eckman, C. B., et al. (2007) · Journal of Clinical Investigation · doi:10.1172/jci29715 · Cited by 642 · 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

Cell-to-cell transmission of pathogenic proteins in neurodegenerative diseases

Guo, J. L., & Lee, V. M. Y. (2014) · Nature Medicine · doi:10.1038/nm.3457 · Cited by 641 · 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

Structure and novel exons of the human .tau. gene

Andreadis, A., Brown, W. M., & Kosik, K. S. (1992) · Biochemistry · doi:10.1021/bi00158a027 · Cited by 625 · 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 fragmentation, aggregation and clearance: the dual role of lysosomal processing

Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617 · 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

Plaques, tangles and dementia

Wilcock, G. K., & Esiri, M. M. (1982) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(82)90155-1 · Cited by 608 · see citing works

[ ¹⁸ F]T807, a novel tau positron emission tomography imaging agent for Alzheimer's disease

Xia, C., Arteaga, J., Chen, G., Gangadharmath, U., Gomez, L. F., Kasi, D., Lam, C., Liang, Q., Liu, C., Mocharla, V. P., et al. (2013) · Alzheimer's &amp; Dementia · doi:10.1016/j.jalz.2012.11.008 · Cited by 605 · see citing works

Identification of common variants influencing risk of the tauopathy progressive supranuclear palsy

PSP Genetics Study Group, Höglinger, G. U., Melhem, N. M., Dickson, D. W., Sleiman, P. M. A., Wang, L.-S., Klei, L., Rademakers, R., de Silva, R., Litvan, I., et al. (2011) · Nature Genetics · doi:10.1038/ng.859 · Cited by 603 · see citing works

Projection domains of MAP2 and tau determine spacings between microtubules in dendrites and axons

Chen, J., Kanai, Y., Cowan, N. J., & Hirokawa, N. (1992) · Nature · doi:10.1038/360674a0 · Cited by 601 · see citing works

Developmentally regulated expression of specific tau sequences

Kosik, K. S., Orecchio, L. D., Bakalis, S., & Neve, R. L. (1989) · Neuron · doi:10.1016/0896-6273(89)90077-9 · Cited by 598 · see citing works

Reactive microglia drive tau pathology and contribute to the spreading of pathological tau in the brain

Maphis, N., Xu, G., Kokiko-Cochran, O. N., Jiang, S., Cardona, A., Ransohoff, R. M., Lamb, B. T., & Bhaskar, K. (2015) · Brain · doi:10.1093/brain/awv081 · Cited by 595 · see citing works

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

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

Natural hypometabolism during hibernation and daily torpor in mammals

Heldmaier, G., Ortmann, S., & Elvert, R. (2004) · Respiratory Physiology & Neurobiology · doi:10.1016/j.resp.2004.03.014 · Cited by 589 · see citing works

Biopsy-derived adult human brain tau is phosphorylated at many of the same sites as Alzheimer's disease paired helical filament tau.

Matsuo, E. S., Shin, R., Billingsley, M., de Voorde, A. V., O'Connor, M., Trojanowski, J., & Lee, V. (1994) · Neuron · doi:10.1016/0896-6273(94)90264-x · Cited by 588 · 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 584 · see citing works

Neurofibrillary Tangles, Amyloid, and Memory in Aging and Mild Cognitive Impairment

Guillozet-Bongaarts, A. L., Weıntraub, S., Mash, D. C., & Mesulam, M. M. (2003) · Archives of Neurology · doi:10.1001/archneur.60.5.729 · Cited by 572 · see citing works

Identification of cDNA clones for the human microtubule-associated protein tau and chromosomal localization of the genes for tau and microtubule-associated protein 2

Neve, R. L., Harris, P. K. W., Kosik, K. S., Kurnit, D. M., & Donlon, T. A. (1986) · Molecular Brain Research · doi:10.1016/0169-328x(86)90033-1 · Cited by 565 · see citing works

Mitogen activated protein (MAP) kinase transforms tau protein into an Alzheimer‐like state.

Drewes, G., Lichtenberg‐Kraag, B., Döring, F., Mandelkow, E. M., Biernat, J., Goris, J., Dorée, M., & Mandelkow, E. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05272.x · Cited by 565 · see citing works

Age-Dependent Emergence and Progression of a Tauopathy in Transgenic Mice Overexpressing the Shortest Human Tau Isoform

Ishihara, T., Hong, M., Zhang, B., Nakagawa, Y., Lee, M. K., Trojanowski, J. Q., & Lee, V. M.-Y. (1999) · Neuron · doi:10.1016/s0896-6273(00)81127-7 · Cited by 564 · see citing works

Phosphorylation that Detaches Tau Protein from Microtubules (Ser262, Ser214) Also Protects It against Aggregation into Alzheimer Paired Helical Filaments

Schneider, A., Biernat, J., von Bergen, M., Mandelkow, E., & Mandelkow, E.-M. (1999) · Biochemistry · doi:10.1021/bi981874p · Cited by 564 · see citing works

Tau protein binds to microtubules through a flexible array of distributed weak sites.

Butner, K. A., & Kirschner, M. W. (1991) · The Journal of cell biology · doi:10.1083/jcb.115.3.717 · Cited by 550 · see citing works

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

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

Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements.

D'Souza, I., Poorkaj, P., Hong, M., Nochlin, D., Lee, V., Bird, T., & Schellenberg, G. (1999) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.96.10.5598 · Cited by 545 · see citing works

Ectopic Cell Cycle Proteins Predict the Sites of Neuronal Cell Death in Alzheimer’s Disease Brain

Busser, J., Geldmacher, D. S., & Herrup, K. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-08-02801.1998 · Cited by 543 · see citing works

Pin1-Dependent Prolyl Isomerization Regulates Dephosphorylation of Cdc25C and Tau Proteins

Zhou, X. Z., Kops, O., Werner, A., Lu, P., Shen, M., Stoller, G., Küllertz, G., Stark, M. J. R., Fischer, G. S., & Lu, K. P. (2000) · Molecular Cell · doi:10.1016/s1097-2765(05)00083-3 · Cited by 543 · see citing works

Hydrofluoric acid-treated tau PHF proteins display the same biochemical properties as normal tau.

Greenberg, S. G., Davies, P., Schein, J., & Binder, L. I. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48531-6 · Cited by 542 · see citing works

The preclinical phase of the pathological process underlying sporadic Alzheimer’s disease

Braak, H., & Del Tredici, K. (2015) · Brain · doi:10.1093/brain/awv236 · Cited by 540 · see citing works

The heritability and genetics of frontotemporal lobar degeneration

Rohrer, J. D., Guerreiro, R., Vandrovcova, J., Uphill, J., Reiman, D., Beck, J., Isaacs, A. M., Authier, A., Ferrari, R., Fox, N. C., et al. (2009) · Neurology · doi:10.1212/wnl.0b013e3181bf997a · Cited by 536 · see citing works

The stress of dieting

Hutchinson, E. (2011) · Nature reviews. Neuroscience · doi:10.1038/nrn2985 · Cited by 534 · see citing works

Aging-related tau astrogliopathy (ARTAG): Harmonized evaluation strategy

Kovacs, G. G., Ferrer, I., Grinberg, L. T., Alafuzoff, I., Attems, J., Budka, H., Cairns, N. J., Crary, J. F., Duyckaerts, C., Ghetti, B., et al. (2016) · Acta Neuropathologica · doi:10.1007/s00401-015-1509-x · Cited by 532 · see citing works

Quantitative Phosphoproteomics Identifies Substrates and Functional Modules of Aurora and Polo-Like Kinase Activities in Mitotic Cells

Kettenbach, A. N., Schweppe, D. K., Faherty, B. K., Pechenick, D. A., Pletnev, A. A., & Gerber, S. A. (2011) · Science Signaling · doi:10.1126/scisignal.2001497 · Cited by 531 · see citing works

Abnormal Hyperphosphorylation of Tau: Sites, Regulation, and Molecular Mechanism of Neurofibrillary Degeneration

Wang, J., Xia, Y., Grundke, I., & Iqbal, K. (2012) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-129031 · Cited by 530 · see citing works

Inhibition of neuronal maturation in primary hippocampal neurons from tau deficient mice

Dawson, H. N., Ferreira, A., Eyster, M. V., Ghoshal, N., Binder, L. I., & Vitek, M. P. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.6.1179 · Cited by 527 · see citing works

Phosphorylated Tau Protein Is Integrated into Paired Helical Filaments in Alzheimer's Disease1

Ihara, Y., Nukina, N., Miura, R., & OGAWARA, M. (1986) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135662 · Cited by 527 · see citing works

Phosphoprotein Phosphatase Activities in Alzheimer Disease Brain

Gong, C., Singh, T. J., Grundke‐Iqbal, I., & Iqbal, K. (1993) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1993.tb03603.x · Cited by 527 · see citing works

Neurotrophins are required for nerve growth during development

Tucker, K. L., Meyer, M., & Barde, Y. (2001) · Nature Neuroscience · doi:10.1038/82868 · Cited by 526 · see citing works

Tau stabilizes microtubules by binding at the interface between tubulin heterodimers

Kadavath, H., Hofele, R. V., Biernat, J., Kumar, S., Tepper, K., Urlaub, H., Mandelkow, E., & Zweckstetter, M. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504081112 · Cited by 524 · see citing works

Tau promotes neurodegeneration through global chromatin relaxation

Frost, B., Hemberg, M., Lewis, J., & Feany, M. B. (2014) · Nature Neuroscience · doi:10.1038/nn.3639 · Cited by 519 · see citing works

Hallmarks of Brain Aging: Adaptive and Pathological Modification by Metabolic States

Mattson, M. P., & Arumugam, T. V. (2018) · Cell Metabolism · doi:10.1016/j.cmet.2018.05.011 · Cited by 1,242 · 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

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

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

Alzheimer’s disease: Recent treatment strategies

Vaz, M., & Silvestre, S. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173554 · Cited by 547 · see citing works

Glial contributions to neurodegeneration in tauopathies

Leyns, C. E. G., & Holtzman, D. M. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0192-x · Cited by 409 · see citing works

Local Nucleation of Microtubule Bundles through Tubulin Concentration into a Condensed Tau Phase

Hernández-Vega, A., Braun, M., Scharrel, L., Jahnel, M., Wegmann, S., Hyman, B. T., Alberti, S., Diez, S., & Hyman, A. A. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.08.042 · Cited by 395 · see citing works

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

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

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

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

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

Role of Amyloid-β and Tau Proteins in Alzheimer’s Disease: Confuting the Amyloid Cascade

Gulisano, W., Maugeri, D., Baltrons, M. A., Fà, M., Amato, A., Palmeri, A., D’Adamio, L., Grassi, C., Devanand, D. P., Honig, L. S., et al. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179935 · Cited by 313 · 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

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

A novel small-molecule PROTAC selectively promotes tau clearance to improve cognitive functions in Alzheimer-like models

Wang, W., Zhou, Q., Jiang, T., Li, S., Ye, J., Zheng, J., Wang, X., Liu, Y., Deng, M., Ke, D., et al. (2021) · Theranostics · doi:10.7150/thno.55680 · Cited by 242 · see citing works

Propagation of Tau aggregates

Goedert, M., & Spillantini, M. G. (2017) · Molecular Brain · doi:10.1186/s13041-017-0298-7 · Cited by 213 · see citing works

Tau deletion promotes brain insulin resistance

Marciniak, E., Leboucher, A., Caron, E., Ahmed, T., Tailleux, A., Dumont, J., Issad, T., Gerhardt, E., Pagesy, P., Vileno, M., et al. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20161731 · Cited by 205 · see citing works

Traumatic Brain Injury Induces Tau Aggregation and Spreading

Edwards, G., Zhao, J., Dash, P. K., Soto, C., & Moreno-Gonzalez, I. (2020) · Journal of Neurotrauma · doi:10.1089/neu.2018.6348 · Cited by 195 · see citing works

Review: Tau in biofluids – relation to pathology, imaging and clinical features

Zetterberg, H. (2017) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12378 · Cited by 157 · see citing works

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 · see citing works

Tau biology, tauopathy, traumatic brain injury, and diagnostic challenges

Castellani, R. J., & Perry, G. (2019) · Journal of Alzheimer’s Disease · doi:10.3233/jad-180721 · Cited by 110 · see citing works

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 · see citing works

Targeting tau: clinical trials and novel therapeutic approaches

VandeVrede, L., Boxer, A. L., & Polydoro, M. (2020) · Neuroscience Letters · doi:10.1016/j.neulet.2020.134919 · Cited by 90 · 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

Identification of Conserved Proteomic Networks in Neurodegenerative Dementia

Swarup, V., Chang, T. S., Duong, D. M., Dammer, E. B., Dai, J., Lah, J. J., Johnson, E. C. B., Seyfried, N. T., Levey, A. I., & Geschwind, D. H. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.107807 · Cited by 78 · see citing works

Identification of conserved proteomic networks in neurodegenerative dementia

Swarup, V., Chang, T. S., Duong, D. M., Dammer, E. B., Lah, J. J., Johnson, E. E. C. B., Seyfried, N. T., Levey, A. I., & Geschwind, D. H. (2019) · doi:10.1101/825802 · Cited by 78 · see citing works

Potential Role of Natural Polyphenols against Protein Aggregation Toxicity: In Vitro, In Vivo, and Clinical Studies

Henríquez, G., Gomez, A., Guerrero, E., & Narayan, M. (2020) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.0c00381 · Cited by 83 · see citing works

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

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

Plasma ATN(I) classification and precision pharmacology in Alzheimer's disease

Imbimbo, B. P., Watling, M., Imbimbo, C., & Nisticò, R. (2023) · Alzheimer's &amp; Dementia · doi:10.1002/alz.13084 · Cited by 34 · see citing works

Tau; One Protein, So Many Diseases

Tabeshmehr, P., & Eftekharpour, E. (2023) · Biology · doi:10.3390/biology12020244 · Cited by 33 · see citing works

Clinical development of passive tau-based immunotherapeutics for treating primary and secondary tauopathies

Panza, F., Dibello, V., Sardone, R., Castellana, F., Zupo, R., Lampignano, L., Bortone, I., Stallone, R., Cirillo, N., Damiani, C., et al. (2023) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2023.2233892 · Cited by 22 · see citing works

A Chronological Review of Potential Disease-Modifying Therapeutic Strategies for Alzheimer’s Disease

Ettcheto, M., Busquets, O., Espinosa-Jiménez, T., Verdaguer, E., Auladell, C., & Camins, A. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200211121416 · Cited by 13 · 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

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 32 · see citing works

ApoE isoform– and microbiota-dependent progression of neurodegeneration in a mouse model of tauopathy

Seo, D.-O., O’Donnell, D., Jain, N., Ulrich, J. D., Herz, J., Li, Y., Lemieux, M., Cheng, J., Hu, H., Serrano, J. R., et al. (2023) · Science · doi:10.1126/science.add1236 · Cited by 254 · see citing works