Cited by 2,480Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchAmyotrophic Lateral Sclerosis Research

The DOI matches its Crossref record; 242 of the 245 references it cites were found in a registry or an index, and 1 are not checked yet.

Neurodegenerative Tauopathies

Lee, Virginia M-Y, Goedert, Michel, Trojanowski, John Q·2001·Annual Review of Neuroscience

DOI 10.1146/annurev.neuro.24.1.1121

Open this paper in CoChat — free account

Abstract

The defining neuropathological characteristics of Alzheimer's disease are abundant filamentous tau lesions and deposits of fibrillar amyloid beta peptides. Prominent filamentous tau inclusions and brain degeneration in the absence of beta-amyloid deposits are also hallmarks of neurodegenerative tauopathies exemplified by sporadic corticobasal degeneration, progressive supranuclear palsy, and Pick's disease, as well as by hereditary frontotemporal dementia and parkinsonism linked to chromosome 17 (FTDP-17). Because multiple tau gene mutations are pathogenic for FTDP-17 and tau polymorphisms appear to be genetic risk factors for sporadic progressive supranuclear palsy and corticobasal degeneration, tau abnormalities are linked directly to the etiology and pathogenesis of neurodegenerative disease. Indeed, emerging data support the hypothesis that different tau gene mutations are pathogenic because they impair tau functions, promote tau fibrillization, or perturb tau gene splicing, thereby leading to formation of biochemically and structurally distinct aggregates of tau. Nonetheless, different members of the same kindred often exhibit diverse FTDP-17 syndromes, which suggests that additional genetic or epigenetic factors influence the phenotypic manifestations of neurodegenerative tauopathies. Although these and other hypothetical mechanisms of neurodegenerative tauopathies remain to be tested and validated, transgenic models are increasingly available for this purpose, and they…

Integrity signals

Registry

Crossref · 10.1146/annurev.neuro.24.1.1121

Cites

242 of 243 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

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
Prions
Prusiner, S. B. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13363 · Cited by 5,373
Correlative Memory Deficits, Aβ Elevation, and Amyloid Plaques in Transgenic Mice
Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., Yang, F., & Cole, G. (1996) · Science · doi:10.1126/science.274.5284.99 · Cited by 4,210
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
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
Self-citation
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
Amyloid deposition as the central event in the aetiology of Alzheimer’s disease
Hardy, J., & Allsop, D. (1991) · Trends in Pharmacological Sciences · doi:10.1016/0165-6147(91)90609-v · Cited by 2,538
Clinical research criteria for the diagnosis of progressive supranuclear palsy (Steele-Richardson-Olszewski syndrome): Report of the NINDS-SPSP International Workshop*
Litvan, I., Agid, Y., Calne, D., Campbell, G., Dubois, B., Duvoisin, R. C., Goetz, C. G., Golbe, L. I., Grafman, J., Growdon, J. H., et al. (1996) · Neurology · doi:10.1212/wnl.47.1.1 · Cited by 2,538
Alzheimer-type neuropathology in transgenic mice overexpressing V717F β-amyloid precursor protein
Games, D., Adams, D., Alessandrini, R., Barbour, R., Borthelette, P., Blackwell, C., Carr, T., Clemens, J., Donaldson, T., Gillespie, F., et al. (1995) · Nature · doi:10.1038/373523a0 · Cited by 2,516
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
Self-citation

Show all 245 references

Research works printed but not linked: 19

Arrasate M, 1997, Am. J. Pathol., 151, 1115
Brion JP, 1985, Arch. Biol., 95, 229
Feany MB, 1995, Am. J. Pathol., 146, 1388
10.1007/s004010050296 · DOI
10.1128/mcb.9.4.1381 · DOI
Hong M, Trojanowski JQ, Lee VM-Y. 2000.Tau-based neurofibrillary lesions.InNeurodegenerative Dementias, ed. CM Clark, JQ Trojanowski, pp. 161–75. New York: McGraw Hill
10.1007/s004010050140 · DOI
Ksiezak-Reding H, 1994, Am. J. Pathol., 145, 1496
10.1007/s004010050138 · DOI
Pickering-Brown S, 2000, Ann. Neurol., 48, 806, 10.1002/1531-8249(200012)48:6<859::aid-ana6>3.0.co;2-1 · DOI
Rebeiz J, 1967, Trans. Am. Neurol. Assoc., 92, 23
Rep. Work Group Frontotemporal Dementia Pick's Disease. 2001. Clinical and neuropathological diagnosis of frontotemporal dementias.Neurobiol. Aging.In press
Shin RW, 1991, Lab. Invest., 64, 693
Snow AD, 1990, Am. J. Pathol., 137, 1253
10.1002/1531-8249(200012)48:6<939::aid-ana17>3.3.co;2-t · DOI
Trojanowski JQ, 1994, Am. J. Pathol., 144, 449
10.1007/s004010050126 · DOI
Wilhelmsen KC, 1994, Am. J. Hum. Genet., 55, 1159
Wilson DM, 1997, Am. J. Pathol., 150, 2181

Sorted by citations

Items 101–200 of 1,023

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
Neuroinflammatory processes in Alzheimer’s disease
Heneka, M. T., O’Banion, M. K., Terwel, D., & Kummer, M. P. (2010) · Journal of Neural Transmission · doi:10.1007/s00702-010-0438-z · Cited by 433
Peripheral inflammatory markers in Alzheimer’s disease: a systematic review and meta-analysis of 175 studies
Lai, K. S. P., Liu, C. S., Rau, A., Lanctôt, K. L., Köhler, C. A., Pakosh, M., Carvalho, A. F., & Herrmann, N. (2017) · Journal of Neurology, Neurosurgery & Psychiatry · doi:10.1136/jnnp-2017-316201 · Cited by 433
Drosophila as a Model for Human Neurodegenerative Disease
Bilen, J., & Bonini, N. M. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.39.110304.095804 · Cited by 432
Frontotemporal dementia
Olney, N. T., Spina, S., & Miller, B. L. (2017) · Neurologic Clinics · doi:10.1016/j.ncl.2017.01.008 · Cited by 419
Interaction of Akt-phosphorylated ataxin-1 with 14-3-3 mediates neurodegeneration in spinocerebellar ataxia type 1
Chen, H.-K., Fernandez-Funez, P., Acevedo, S. F., Lam, Y. C., Kaytor, M. D., Fernandez, M. H., Aitken, A., Skoulakis, E. M. C., Orr, H. T., Botas, J., et al. (2003) · Cell · doi:10.1016/s0092-8674(03)00349-0 · Cited by 414
Microtubule-binding drugs offset tau sequestration by stabilizing microtubules and reversing fast axonal transport deficits in a tauopathy model
Zhang, B., Maiti, A., Shively, S., Lakhani, F., McDonald-Jones, G., Bruce, J., Lee, E. B., Xie, S. X., Joyce, S., Li, C., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406361102 · Cited by 413
Self-citation
Apolipoprotein e sets the stage: response to injury triggers neuropathology
Mahley, R. W., & Huang, Y. (2012) · Neuron · doi:10.1016/j.neuron.2012.11.020 · Cited by 412
Semaphorin3A signalling is mediated via sequential Cdk5 and GSK3β phosphorylation of CRMP2: implication of common phosphorylating mechanism underlying axon guidance and Alzheimer's disease
Uchida, Y., Ohshima, T., Sasaki, Y., Suzuki, H., Yanai, S., Yamashita, N., Nakamura, F., Takei, K., Ihara, Y., Mikoshiba, K., et al. (2005) · Genes to Cells · doi:10.1111/j.1365-2443.2005.00827.x · Cited by 411
Advances in understanding the molecular basis of frontotemporal dementia
Rademakers, R., Neumann, M., & Mackenzie, I. R. (2012) · Nature Reviews Neurology · doi:10.1038/nrneurol.2012.117 · Cited by 432
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 431
Therapeutic potential of mood stabilizers lithium and valproic acid:Beyond bipolar disorder
Chiu, C.-T., Wang, Z., Hunsberger, J. G., & Chuang, D.-M. (2013) · Pharmacological Reviews · doi:10.1124/pr.111.005512 · Cited by 404
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
Self-citation
Novel tau biomarkers phosphorylated at T181, T217 or T231 rise in the initial stages of the preclinical Alzheimer’s continuum when only subtle changes in Aβ pathology are detected
Suárez‐Calvet, M., Karikari, T. K., Ashton, N. J., Lantero Rodríguez, J., Milà‐Alomà, M., Gispert, J. D., Salvadó, G., Minguillon, C., Fauria, K., Shekari, M., et al. (2020) · EMBO Molecular Medicine · doi:10.15252/emmm.202012921 · Cited by 401
Alzheimer's pathology in human temporal cortex surgically excised after severe brain injury
Ikonomovic, M. D., Uryu, K., Abrahamson, E. E., Ciallella, J. R., Trojanowski, J. Q., Lee, V. M.-Y., Clark, R. S., Marion, D. W., Wisniewski, S. R., & DeKosky, S. T. (2004) · Experimental Neurology · doi:10.1016/j.expneurol.2004.06.011 · Cited by 399
Self-citation
Microtubule-associated protein tau in development, degeneration and protection of neurons
Wang, J., & Liu, F. (2008) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2008.03.002 · Cited by 405
Neuropathology of variants of progressive supranuclear palsy
Dickson, D. W., Ahmed, Z., Algom, A. A., Tsuboi, Y., & Josephs, K. A. (2010) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32833be924 · Cited by 386
The epigenetics of aging and neurodegeneration
Lardenoije, R., Iatrou, A., Kenis, G., Kompotis, K., Steinbusch, H. W. M., Mastroeni, D., Coleman, P., Lemere, C. A., Hof, P. R., van den Hove, D. L. A., et al. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.002 · Cited by 381
Molecular neuropathology of frontotemporal dementia: insights into disease mechanisms from postmortem studies
Mackenzie, I. R., & Neumann, M. (2016) · Journal of Neurochemistry · doi:10.1111/jnc.13588 · Cited by 409
Pathological Tau Strains from Human Brains Recapitulate the Diversity of Tauopathies in Nontransgenic Mouse Brain
Narasimhan, S., Guo, J. L., Changolkar, L., Stieber, A., McBride, J. D., Silva, L. V., He, Z., Zhang, B., Gathagan, R. J., Trojanowski, J. Q., et al. (2017) · The Journal of Neuroscience · doi:10.1523/jneurosci.1230-17.2017 · Cited by 374
Self-citation
The complexity of tau in Alzheimer’s disease
Naseri, N. N., Wang, H., Guo, J. D., Sharma, M., & Luo, W. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.04.022 · Cited by 393
Alzheimer's DiseasePreprint
Selkoe, D. J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004457 · Cited by 384
Review on Alzheimer’s Disease: Inhibition of Amyloid Beta and Tau Tangle Formation
Ashrafian, H., Zadeh, E. H., & Khan, R. H. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.11.192 · Cited by 368
Therapeutic approaches to Alzheimer's disease
Klafki, H., Staufenbiel, M., Kornhuber, J., & Wiltfang, J. (2006) · Brain · doi:10.1093/brain/awl280 · Cited by 362
Neurodegenerative Diseases: Expanding the Prion Concept
Walker, L. C., & Jucker, M. (2015) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-071714-033828 · Cited by 361
Preparation and Characterization of Neurotoxic Tau Oligomers
Lasagna-Reeves, C. A., Castillo-Carranza, D. L., Guerrero-Muñoz, M. J., Jackson, G. R., & Kayed, R. (2010) · Biochemistry · doi:10.1021/bi1016233 · Cited by 359
Protein composition of the intranuclear inclusions of FXTAS
Iwahashi, C., Yasui, D. H., An, H. J., Greco, C., Tassone, F., Nannen, K., Babineau, B. A., Lebrilla, C. B., Hagerman, R. J., & Hagerman, P. J. (2005) · Brain · doi:10.1093/brain/awh650 · Cited by 368
Characterization of Prefibrillar Tau Oligomers in Vitro and in Alzheimer Disease
Patterson, K. R., Remmers, C. L., Fu, Y., Brooker, S. M., Kanaan, N. M., Vana, L., Ward, S., Reyes, J. F., Philibert, K., Glucksman, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.237974 · Cited by 369
Inducible Expression of Tau Repeat Domain in Cell Models of Tauopathy
Khlistunova, I., Biernat, J., Wang, Y., Pickhardt, M., von Bergen�, M., Gažová, Z., Mandelkow�, E., & Mandelkow, E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507753200 · Cited by 366
In Vivo Microdialysis Reveals Age-Dependent Decrease of Brain Interstitial Fluid Tau Levels in P301S Human Tau Transgenic Mice
Yamada, K., Cirrito, J. R., Stewart, F. R., Jiang, H., Finn, M. B., Holmes, B. B., Binder, L. I., Mandelkow, E.-M., Diamond, M. I., Lee, V. M.-Y., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.2569-11.2011 · Cited by 351
Self-citation
The Roles of Cyclin-dependent Kinase 5 and Glycogen Synthase Kinase 3 in Tau Hyperphosphorylation
Plattner, F., Angelo, M., & Giese, K. P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603469200 · Cited by 340
Functional neuroanatomy of the central noradrenergic system
Szabadi, E. (2013) · Journal of Psychopharmacology · doi:10.1177/0269881113490326 · Cited by 366
Repeat motifs of tau bind to the insides of microtubules in the absence of taxol
Kar, S., Fan, J., Smith, M. J., Goedert, M., & Amos, L. A. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg001 · Cited by 355
Self-citation
Anthraquinones Inhibit Tau Aggregation and Dissolve Alzheimer's Paired Helical Filaments in Vitro and in Cells
Pickhardt, M., Gažová, Z., von Bergen�, M., Khlistunova, I., Wang, Y., Hascher, A., Mandelkow, E., Biernat, J., & Mandelkow�, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410984200 · Cited by 334
Functions of intermediate filaments in neuronal development and disease
Larivière, R., & Julien, J. (2003) · Journal of Neurobiology · doi:10.1002/neu.10270 · Cited by 333
18F-THK523: a novel in vivo tau imaging ligand for Alzheimer's disease
Fodero‐Tavoletti, M. T., Okamura, N., Furumoto, S., Mulligan, R. S., Connor, A. R., McLean, C., Cao, D., Rigopoulos, A., Cartwright, G. A., O'Keefe, G. J., et al. (2011) · Brain · doi:10.1093/brain/awr038 · Cited by 340
Proteasomal degradation of tau protein
David, D. C., Layfield, R., Serpell, L., Narain, Y., Goedert, M., & Spillantini, M. G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01137.x · Cited by 327
Self-citation
Prolyl isomerase Pin1 as a molecular switch to determine the fate of phosphoproteins
Liou, Y., Zhou, X. Z., & Lu, K. P. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2011.07.001 · Cited by 333
PAR-1 Kinase Plays an Initiator Role in a Temporally Ordered Phosphorylation Process that Confers Tau Toxicity in Drosophila
Nishimura, I., Yang, Y., & Lu, B. (2004) · Cell · doi:10.1016/s0092-8674(04)00170-9 · Cited by 324
Proteomic Characterization of Postmortem Amyloid Plaques Isolated by Laser Capture Microdissection
Liao, L., Cheng, D., Wang, J., Duong, D. M., Losik, T. G., Gearing, M., Rees, H. D., Lah, J. J., Levey, A. I., & Peng, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403672200 · Cited by 320
Molecular Pathological Classification of Neurodegenerative Diseases: Turning towards Precision Medicine
Kovács, G. G. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17020189 · Cited by 346
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
Self-citation
Oxidative stress mediates tau-induced neurodegeneration in Drosophila
Dias-Santagata, D., Fulga, T. A., Duttaroy, A., & Feany, M. B. (2007) · Journal of Clinical Investigation · doi:10.1172/jci28769 · Cited by 318
Tau pathophysiology in neurodegeneration: a tangled issue
Spires‐Jones, T. L., Stoothoff, W. H., de Calignon, A., Jones, P., & Hyman, B. T. (2009) · Trends in Neurosciences · doi:10.1016/j.tins.2008.11.007 · Cited by 321
Serum interleukin (IL-2, IL-10, IL-6, IL-4), TNFα, and INFγ concentrations are elevated in patients with atypical and idiopathic parkinsonism
Brodacki, B., Staszewski, J., Toczyłowska, B., Kozłowska, E., Drela, N., Chalimoniuk, M., & Stępien, A. (2008) · Neuroscience Letters · doi:10.1016/j.neulet.2008.06.040 · Cited by 316
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
Novobiocin and Additional Inhibitors of the Hsp90 C-Terminal Nucleotide- binding Pocket
Donnelly, A. C., & Blagg, B. S. J. (2008) · Current Medicinal Chemistry · doi:10.2174/092986708786242895 · Cited by 316
Alzheimer Disease-specific Conformation of Hyperphosphorylated Paired Helical Filament-Tau Is Polyubiquitinated through Lys-48, Lys-11, and Lys-6 Ubiquitin Conjugation
Cripps, D., Thomas, S. N., Jeng, Y., Yang, F., Davies, P., & Yang, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512786200 · Cited by 312
Microtubule-associated protein tau is essential for long-term depression in the hippocampus
Kimura, T., Whitcomb, D. J., Jo, J., Regan, P., Piers, T., Heo, S., Brown, C., Hashikawa, T., Murayama, M., Seok, H., et al. (2014) · Philosophical Transactions of the Royal Society B: Biological Sciences · doi:10.1098/rstb.2013.0144 · Cited by 307
The Genetics of Parkinson Disease
Bekris, L. M., Mata, I. F., & Zabetian, C. P. (2010) · Journal of Geriatric Psychiatry and Neurology · doi:10.1177/0891988710383572 · Cited by 314
α-Lipoic acid improves abnormal behavior by mitigation of oxidative stress, inflammation, ferroptosis, and tauopathy in P301S Tau transgenic mice
Zhang, Y., Wang, D., Xu, S., Zhang, S., Fan, Y., Yang, Y., Guo, S., Wang, S., Guo, T., Wang, Z., et al. (2017) · Redox Biology · doi:10.1016/j.redox.2017.11.001 · Cited by 312
Abnormal tau, mitochondrial dysfunction, impaired axonal transport of mitochondria, and synaptic deprivation in Alzheimer's disease
Reddy, P. H. (2011) · Brain Research · doi:10.1016/j.brainres.2011.07.052 · Cited by 311
Tau-induced defects in synaptic plasticity, learning, and memory are reversible in transgenic mice after switching off the toxic Tau mutant
Sydow, A., Van der Jeugd, A., Zheng, F., Ahmed, T., Balschun, D., Petrova, O., Drexler, D., Zhou, L., Rune, G., Mandelkow, E., et al. (2011) · The Journal of Neuroscience · doi:10.1523/jneurosci.5245-10.2011 · Cited by 302
Increased levels of granular tau oligomers: An early sign of brain aging and Alzheimer's disease
Maeda, S., Sahara, N., Saito, Y., Murayama, S., Ikai, A., & Takashima, A. (2006) · Neuroscience Research · doi:10.1016/j.neures.2005.11.009 · Cited by 301
Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement
Schipper, H. M., Song, W., Zukor, H., Hascalovici, J. R., & Zeligman, D. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06160.x · Cited by 298
AMPK is abnormally activated in tangle- and pre-tangle-bearing neurons in Alzheimer’s disease and other tauopathies
Vingtdeux, V., Davies, P., Dickson, D. W., & Marambaud, P. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0759-x · Cited by 297
The Potential for β-Structure in the Repeat Domain of Tau Protein Determines Aggregation, Synaptic Decay, Neuronal Loss, and Coassembly with Endogenous Tau in Inducible Mouse Models of Tauopathy
Mocanu, M.-M., Nissen, A., Eckermann, K., Khlistunova, I., Biernat, J., Drexler, D., Petrova, O., Schönig, K., Bujard, H., Mandelkow, E., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.2824-07.2008 · Cited by 297
Missorting of Tau in Neurons Causes Degeneration of Synapses That Can Be Rescued by the Kinase MARK2/Par-1
Thies, E., & Mandelkow, E.-M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4674-06.2007 · Cited by 293
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 299
Olfactory Dysfunction Correlates with Amyloid-β Burden in an Alzheimer's Disease Mouse Model
Wesson, D. W., Levy, E., Nixon, R. A., & Wilson, D. A. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.4622-09.2010 · Cited by 290
High-fat diet aggravates amyloid-beta and tau pathologies in the 3xTg-AD mouse model
Julien, C., Tremblay, C., Phivilay, A., Berthiaume, L., Émond, V., Julien, P., & Calon, F. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.08.022 · Cited by 288
GABAergic Interneuron Dysfunction Impairs Hippocampal Neurogenesis in Adult Apolipoprotein E4 Knockin Mice
Li, G., Bien-Ly, N., Andrews-Zwilling, Y., Xu, Q., Bernardo, A., Ring, K., Halabisky, B., Deng, C., Mahley, R. W., & Huang, Y. (2009) · Cell Stem Cell · doi:10.1016/j.stem.2009.10.015 · Cited by 288
The role of DYRK1A in neurodegenerative diseases
Węgiel, J., Gong, C., & Hwang, Y. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07955.x · Cited by 307
Possible Implications of Insulin Resistance and Glucose Metabolism in Alzheimer's Disease Pathogenesis
Bosco, D., Fava, A., Plastino, M., Montalcini, T., & Pujia, A. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01318.x · Cited by 283
Tau phosphorylation and aggregation in Alzheimer's disease pathology
Ávila, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.02.067 · Cited by 288
Acetylated tau, a novel pathological signature in Alzheimer's disease and other tauopathies
Irwin, D. J., Cohen, T. J., Grossman, M., Arnold, S. E., Xie, S. X., Lee, V. M.-Y., & Trojanowski, J. Q. (2012) · Brain · doi:10.1093/brain/aws013 · Cited by 281
Self-citation
Differential regulation of microtubule dynamics by three- and four-repeat tau: implications for the onset of neurodegenerative disease
Panda, D., Samuel, J. C., Massie, M., Feinstein, S. C., & Wilson, L. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1633508100 · Cited by 280
High-Contrast In Vivo Imaging of Tau Pathologies in Alzheimer’s and Non-Alzheimer’s Disease Tauopathies
Tagai, K., Ono, M., Kubota, M., Kitamura, S., Takahata, K., Seki, C., Takado, Y., Shinotoh, H., Sano, Y., Yamamoto, Y., et al. (2020) · Neuron · doi:10.1016/j.neuron.2020.09.042 · Cited by 276
Self-citation
Neuroinflammation in Alzheimer’s disease
Zhang, F., & Jiang, L. (2015) · Neuropsychiatric Disease and Treatment · doi:10.2147/ndt.s75546 · Cited by 276
Template-assisted filament growth by parallel stacking of tau
Margittai, M., & Langen, R. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401911101 · Cited by 276
FTD and ALS: A Tale of Two Diseases
Ferrari, R., Kapogiannis, D., Huey, E. D., & Momeni, P. (2011) · Current Alzheimer Research · doi:10.2174/156720511795563700 · Cited by 285
Tau Pathology Induces Excitatory Neuron Loss, Grid Cell Dysfunction, and Spatial Memory Deficits Reminiscent of Early Alzheimer’s Disease
Fu, H., Rodriguez, G. A., Herman, M., Emrani, S., Nahmani, E., Barrett, G., Figueroa, H. Y., Goldberg, E., Hussaini, S. A., & Duff, K. E. (2017) · Neuron · doi:10.1016/j.neuron.2016.12.023 · Cited by 264
Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies
Luo, W., Dou, F., Rodina, A., Chip, S., Kim, J., Zhao, Q., Moulick, K., Aguirre, J., Wu, N. F., Greengard, P., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701055104 · Cited by 274
Hydrogen sulfide is neuroprotective in Alzheimer’s disease by sulfhydrating GSK3β and inhibiting Tau hyperphosphorylation
Giovinazzo, D., Bursać, B. N., Sbodio, J. I., Nalluru, S., Vignane, T., Snowman, A. M., Albacarys, L. M., Sedlak, T. W., Torregrossa, R., Whiteman, M., et al. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2017225118 · Cited by 274
Transgenic animal models of Alzheimer's disease and related disorders: histopathology, behavior and therapy
Götz, J., Streffer, J. R., David, D. C., Schild, A., Hoerndli, F. J., Pennanen, L., Kurosinski, P., & Chen, F. (2004) · Molecular Psychiatry · doi:10.1038/sj.mp.4001508 · Cited by 284
Changed Conformation of Mutant Tau-P301L Underlies the Moribund Tauopathy, Absent in Progressive, Nonlethal Axonopathy of Tau-4R/2N Transgenic Mice
Terwel, D., Lasrado, R., Snauwaert, J., Vandeweert, E., Haesendonck, C. V., Borghgraef, P., & LEUVEN, F. V. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409876200 · Cited by 267
-Synuclein Phosphorylation Enhances Eosinophilic Cytoplasmic Inclusion Formation in SH-SY5Y Cells
Smith, W. W. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0482-05.2005 · Cited by 274
TOR-Mediated Cell-Cycle Activation Causes Neurodegeneration in a Drosophila Tauopathy Model
Khurana, V., Lu, Y., Steinhilb, M. L., Oldham, S., Shulman, J. M., & Feany, M. B. (2006) · Current Biology · doi:10.1016/j.cub.2005.12.042 · Cited by 266
Differential induction and spread of tau pathology in young PS19 tau transgenic mice following intracerebral injections of pathological tau from Alzheimer’s disease or corticobasal degeneration brains
Boluda, S., Iba, M., Zhang, B., Raible, K. M., Lee, V. M. ‐., & Trojanowski, J. Q. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1373-0 · Cited by 268
Self-citation
Unconventional Secretion Mediates the Trans-cellular Spreading of Tau
Katsinelos, T., Zeitler, M., Dimou, E., Karakatsani, A., Müller, H., Nachman, E., Steringer, J. P., de Almodóvar, C. R., Nickel, W., & Jahn, T. R. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.04.056 · Cited by 274
Hippocampal phosphorylated tau induced cognitive decline, dendritic spine loss and mitochondrial abnormalities in a mouse model of Alzheimer’s disease
Kandimalla, R. J. L., Mańczak, M., Yin, X., Wang, R., & Reddy, P. H. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx381 · Cited by 256
Retracted
Tau seeding activity begins in the transentorhinal/entorhinal regions and anticipates phospho-tau pathology in Alzheimer’s disease and PART
Kaufman, S. K., Del Tredici, K., Thomas, T. L., Braak, H., & Diamond, M. I. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1855-6 · Cited by 259
Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression
Hamano, T., Gendron, T. F., Causevic, E., Yen, S., Lin, W., Isidoro, C., DeTure, M., & Ko, L. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06084.x · Cited by 283
Mechanisms of Cell-to-Cell Transmission of Pathological Tau: A Review
Gibbons, G. S., Lee, V. M. Y., & Trojanowski, J. Q. (2019) · JAMA Neurology · doi:10.1001/jamaneurol.2018.2505 · Cited by 257
Self-citation
Genetic modifiers of tauopathy in Drosophila
Shulman, J. M., & Feany, M. B. (2003) · Genetics · doi:10.1093/genetics/165.3.1233 · Cited by 256
A Long Journey into Aging, Brain Aging, and Alzheimer’s Disease Following the Oxidative Stress Tracks
Mecocci, P., Boccardi, V., Cecchetti, R., Bastiani, P., Scamosci, M., Ruggiero, C., & Baroni, M. (2018) · Journal of Alzheimer s Disease · doi:10.3233/jad-170732 · Cited by 259
Role of metabolism in neurodegenerative disorders
Procaccini, C., Santopaolo, M., Faicchia, D., Colamatteo, A., Formisano, L., de Candia, P., Galgani, M., De Rosa, V., & Matarese, G. (2016) · Metabolism · doi:10.1016/j.metabol.2016.05.018 · Cited by 258
Conformation Determines the Seeding Potencies of Native and Recombinant Tau Aggregates
Falcon, B., Cavallini, A., Angers, R. C., Glover, S. J., Murray, T. K., Barnham, L., Jackson, S., O'Neill, M. J., Isaacs, A. M., Hutton, M. L., et al. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.589309 · Cited by 265
Self-citation
Splicing Regulation in Neurologic Disease
Licatalosi, D. D., & Darnell, R. B. (2006) · Neuron · doi:10.1016/j.neuron.2006.09.017 · Cited by 250
Oxidative modification and down-regulation of Pin1 in Alzheimer's disease hippocampus: A redox proteomics analysis
Rukhsana Sultana, A., Debra Boyd-kimball, A., Poon, H. F., Cai, J., Pierce, W. M. J., Klein, J. B., Markesbery, W. R., Zhou, X. Z., Lu, K. P., & Butterfield, D. A. (2005) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.05.005 · Cited by 255
Chemoenzymatic Semisynthesis of Proteins
Thompson, R. E., & Muir, T. W. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.9b00450 · Cited by 245
Tau oligomers and tau toxicity in neurodegenerative disease
Ward, S., Himmelstein, D. S., Lancia, J. K., & Binder, L. I. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120134 · Cited by 244
Drosophila Models of Neurodegenerative Diseases
Lu, B., & Vogel, H. S. (2008) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev.pathol.3.121806.151529 · Cited by 257
The involvement of microRNAs in neurodegenerative diseases
Maciotta, S., Meregalli, M., & Torrente, Y. (2013) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2013.00265 · Cited by 260
MicroRNA Pathways Modulate Polyglutamine-Induced Neurodegeneration
Bilen, J., Liu, N., Burnett, B. G., Pittman, R. N., & Bonini, N. M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.07.030 · Cited by 246
Examining the potential clinical value of curcumin in the prevention and diagnosis of Alzheimer’s disease
Goozee, K. G., Shah, T. M., Sohrabi, H. R., Rainey‐Smith, S. R., Brown, B. M., Verdile, G., & Martins, R. N. (2015) · British Journal Of Nutrition · doi:10.1017/s0007114515004687 · Cited by 260
Neuronal excitation/inhibition imbalance: core element of a translational perspective on Alzheimer pathophysiology
Maestú, F., de Haan, W., Busche, M. A., & DeFelipe, J. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101372 · Cited by 245
Protein misfolding and aggregation in Alzheimer’s disease and type 2 diabetes mellitus
Ashraf, G., Greig, N., Khan, T., Hassan, I., Tabrez, S., Shakil, S., Sheikh, I., Zaidi, S., Akram, M., Jabir, N., et al. (2014) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527313666140917095514 · Cited by 236
Targeting Hsp90/Hsp70-Based Protein Quality Control for Treatment of Adult Onset Neurodegenerative Diseases
Pratt, W. B., Gestwicki, J. E., Osawa, Y., & Lieberman, A. P. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-010814-124332 · Cited by 244
Autophagy Induction as a Therapeutic Strategy for Neurodegenerative Diseases
Djajadikerta, A., Keshri, S., Tanasa, M. P., Prestil, R., Ryan, L., & Rubinsztein, D. C. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.035 · Cited by 244

Authors: Lee, V. M.-Y., Goedert, M., & Trojanowski, J. Q.
Affiliations: MRC Laboratory of Molecular Biology (GB)
ORCID: Lee, Virginia M-Y
Goedert, Michel
Trojanowski, John Q
Venue: Annual Review of Neuroscience
Publisher: Annual Reviews
Published: 2001-03
Volume: 24
Issue: 1
Pages: 1121-1159
ISSN: 0147-006X (ISSN-L)
1545-4126
DOI: 10.1146/annurev.neuro.24.1.1121
OpenAlex: W4230565756
Semantic Scholar: 8eb6355272daf41b8da72a5b18a4d8c67d8509cc
Cited by: 2,480
References: 245
Citations by year: 2026: 60 · 2025: 81 · 2024: 102 · 2023: 112 · 2022: 133 · 2021: 130 · 2020: 126 · 2019: 107 · 2018: 114 · 2017: 94 · 2016: 100 · 2015: 115 · 2014: 99 · 2013: 100 · 2012: 92
FWCI: 9.22
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Neuroscience (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
Keywords: tau protein, tau gene mutations, FTDP-17, progressive supranuclear palsy, corticobasal degeneration, Pick's disease, Alzheimer's disease, tau fibrillization, genetic risk factors, transgenic animal models, neurodegeneration
MeSH terms: Animals, Brain, Brain Diseases, Dementia, Humans, Neurofibrillary Tangles, tau Proteins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Neurodegenerative Tauopathies

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks