The DOI matches its Crossref record; 85 of the 85 references it cites were found in a registry or an index.
Amyloid-β oligomers induce synaptic damage via Tau-dependent microtubule severing by TTLL6 and spastin
Open accessAbstract
Mislocalization and aggregation of Aβ and Tau combined with loss of synapses and microtubules (MTs) are hallmarks of Alzheimer disease. We exposed mature primary neurons to Aβ oligomers and analysed changes in the Tau/MT system. MT breakdown occurs in dendrites invaded by Tau (Tau missorting) and is mediated by spastin, an MT-severing enzyme. Spastin is recruited by MT polyglutamylation, induced by Tau missorting triggered translocalization of TTLL6 (Tubulin-Tyrosine-Ligase-Like-6) into dendrites. Consequences are spine loss and mitochondria and neurofilament mislocalization. Missorted Tau is not axonally derived, as shown by axonal retention of photoconvertible Dendra2-Tau, but newly synthesized. Recovery from Aβ insult occurs after Aβ oligomers lose their toxicity and requires the kinase MARK (Microtubule-Affinity-Regulating-Kinase). In neurons derived from Tau-knockout mice, MTs and synapses are resistant to Aβ toxicity because TTLL6 mislocalization and MT polyglutamylation are prevented; hence no spastin recruitment and no MT breakdown occur, enabling faster recovery. Reintroduction of Tau re-establishes Aβ-induced toxicity in TauKO neurons, which requires phosphorylation of Tau's KXGS motifs. Transgenic mice overexpressing Tau show TTLL6 translocalization into dendrites and decreased MT stability. The results provide a rationale for MT stabilization as a therapeutic approach.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
Cultured neurons from Tau−/− mice are not susceptible to Aβ-induced synaptic damage and neurotoxicity.
“Thus, cultured neurons from tau knockout (Tau−/−) mice are not susceptible to Aβ-induced synaptic damage and neurotoxicity (Rapoport et al., 2002; Nussbaum et al., 2012; Zempel et al., 2013) or to Aβ-induced defects in axonal transport (Vossel et al., 2011).”
From Wild-Type, but Not Mutant N296H, Human Tau Restores Aβ-Mediated Inhibition of LTP in Tau−/− mice (2017) · cites this paper as Zempel et al., 2013
The discussion reports dramatically reduced Aβ-induced toxicity in TauKO neurons, including protection against microtubule breakdown and mitochondrial mislocalization. But the Results and Figure 6 report that Aβ still caused moderate spine loss in these neurons, so they were not wholly unsusceptible to synaptic damage. Page numbers are not provided in our copy's passages. (LLM, conf=0.90)
Experimental — accuracy not yet measuredIn primary neurons, CIP2A promotes tau translocalization to dendrites and spines.
“In primary neurons, we further observed that CIP2A promoted tau translocalization to dendrites and spines, which is considered to be the key event mediating the synaptic toxicity of tau (Pooler et al., 2014; Zempel et al., 2013).”
From CIP2A Causes Tau/APP Phosphorylation, Synaptopathy, and Memory Deficits in Alzheimer’s Disease (2018) · cites this paper as Zempel et al., 2013
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Neuropathological stageing of Alzheimer-related changes.
Braak, H., & Braak, E. (1991) · Acta Neuropathologica · doi:10.1007/bf00308809 · Cited by 16,123 · cited 2×
“In the present study, we focussed on the link between A b O and the neuronal cytoskeleton, notably the phosphorylation/ missorting of Tau and breakdown of MTs because these features are early hallmarks of AD (Braak and Braak, 1991; Spires-Jones et al , 2009).”
Amyloid oligomers exacerbate tau pathology in a mouse model of tauopathy
Selenica, M.-L. B., Brownlow, M., Jimenez, J. P., Lee, D. C., Pena, G., Dickey, C. A., Gordon, M. N., & Morgan, D. (2013) · Neurodegenerative Diseases · doi:10.1159/000337230 · Cited by 10,359
Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid β-peptide
Haass, C., & Selkoe, D. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2101 · Cited by 4,744
Karran, E., Mercken, M., & Strooper, B. D. (2011) · Nature Reviews Drug Discovery · doi:10.1038/nrd3505 · Cited by 2,188 · cited 1×
“In familial AD, genetic evidence points to a master role of A b aggregation, leading to downstream events including Tau hyperphosphorylation and aggregation (Haass and Selkoe, 2007; Karran et al , 2011).”
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
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
Shankar, G. M., Bloodgood, B. L., Townsend, M., Walsh, D. M., Selkoe, D. J., & Sabatini, B. L. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4970-06.2007 · Cited by 1,592
Amyloid-β Dynamics Are Regulated by Orexin and the Sleep-Wake Cycle
Kang, J.-E., Lim, M. M., Bateman, R. J., Lee, J. J., Smyth, L. P., Cirrito, J. R., Fujiki, N., Nishino, S., & Holtzman, D. M. (2009) · Science · doi:10.1126/science.1180962 · Cited by 1,565
Regulation of NMDA receptor trafficking by amyloid-β
Snyder, E. M., Nong, Y., Almeida, C. G., Paul, S., Moran, T., Choi, E. Y., Nairn, A. C., Salter, M. W., Lombroso, P. J., Gouras, G. K., et al. (2005) · Nature Neuroscience · doi:10.1038/nn1503 · Cited by 1,561 · cited 4×
“This is indeed the case, since blockage of both global and Tau protein synthesis strongly reduces dendritic missorting of Tau after A b O exposure.”
InfluentialCellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., & Strittmatter, S. M. (2009) · Nature · doi:10.1038/nature07761 · Cited by 1,560
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
Microtubule assembly, organization and dynamics in axons and dendrites
Conde, C., & Cáceres, A. (2009) · Nature Reviews Neuroscience · doi:10.1038/nrn2631 · Cited by 1,086
Neurotoxicity of Amyloid -Protein: Synaptic and Network Dysfunction
Mucke, L., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006338 · Cited by 1,000
Augustinack, J. C., Schneider, A., Mandelkow, E.-M., & Hyman, B. T. (2002) · Acta Neuropathologica · doi:10.1007/s004010100423 · Cited by 998
Self-citationCalcium dyshomeostasis and intracellular signalling in alzheimer's disease
LaFerla, F. M. (2002) · Nature reviews. Neuroscience · doi:10.1038/nrn960 · Cited by 988
Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways
Schulman, B. A., & Harper, J. W. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2673 · Cited by 981
Morris, M., Maeda, S., Vossel, K., & Mucke, L. (2011) · Neuron · doi:10.1016/j.neuron.2011.04.009 · Cited by 899
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 895
Stamer, K., Vogel, R., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200108057 · Cited by 885
Neuronal activity regulates the regional vulnerability to amyloid-β deposition
Bero, A. W., Yan, P., Roh, J. H., Cirrito, J. R., Stewart, F. R., Raichle, M. E., Lee, J.-M., & Holtzman, D. M. (2011) · Nature Neuroscience · doi:10.1038/nn.2801 · Cited by 880
Drewes, G., Ebneth, A., Preuss, U., Mandelkow, E.-M., & Mandelkow, E. (1997) · Cell · doi:10.1016/s0092-8674(00)80208-1 · Cited by 878
Self-citationThe Mechanism of Ca2+-Dependent Regulation of Kinesin-Mediated Mitochondrial Motility
Wang, X., & Schwarz, T. L. (2009) · Cell · doi:10.1016/j.cell.2008.11.046 · Cited by 871
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
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
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
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 802
Braak, F., Braak, H., & Mandelkow, E. (1994) · Acta Neuropathologica · doi:10.1007/bf00293315 · Cited by 769
Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686 · cited 5×
“Light and electron microscopy set-ups, live-imaging conditions, photoconversion, and quantification procedures were described previously (Zempel et al , 2010; Li et al , 2011).”
InfluentialSelf-citationEpilepsy and Cognitive Impairments in Alzheimer Disease
Palop, J. J. (2009) · Archives of Neurology · doi:10.1001/archneurol.2009.15 · Cited by 684
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
Dynamic microtubules regulate dendritic spine morphology and synaptic plasticity
Jaworski, J., Kapitein, L. C., Gouveia, S. M., Dortland, B. R., Wulf, P. S., Grigoriev, I., Camera, P., Spangler, S. A., Di Stefano, P., Demmers, J., et al. (2009) · Neuron · doi:10.1016/j.neuron.2008.11.013 · Cited by 643
Tau deficiency induces parkinsonism with dementia by impairing APP-mediated iron export
Lei, P., Ayton, S., Finkelstein, D. I., Spoerri, L., Ciccotosto, G. D., Wright, D. K., Wong, B. X. W., Adlard, P. A., Cherny, R. A., Lam, L. Q., et al. (2012) · Nature Medicine · doi:10.1038/nm.2613 · Cited by 594
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
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
Kuperstein, I., Broersen, K., Benilova, I., Rozenski, J., Jonckheere, W., Debulpaep, M., Vandersteen, A., Segers‐Nolten, I., Van Der Werf, K., Subramaniam, V., et al. (2010) · The EMBO Journal · doi:10.1038/emboj.2010.211 · Cited by 532
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
Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
Fulga, T. A., Elson-Schwab, I., Khurana, V., Steinhilb, M. L., Spires, T. L., Hyman, B. T., & Feany, M. B. (2007) · Nature Cell Biology · doi:10.1038/ncb1528 · Cited by 452
Small-molecule conversion of toxic oligomers to nontoxic β-sheet–rich amyloid fibrils
Bieschke, J., Herbst, M., Wiglenda, T., Friedrich, R. P., Boeddrich, A., Schiele, F., Kleckers, D., del Amo, J. M. L., Grüning, B. A., Wang, Q., et al. (2011) · Nature Chemical Biology · doi:10.1038/nchembio.719 · Cited by 451
Nuclear Tau, a Key Player in Neuronal DNA Protection
Sultan, A., Nesslany, F., Violet, M., Bégard, S., Loyens, A., Talahari, S., Mansuroglu, Z., Marzin, D., Sergeant, N., Humez, S., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.199976 · Cited by 421 · cited 2×
“This is indeed the case, since blockage of both global and Tau protein synthesis strongly reduces dendritic missorting of Tau after A b O exposure.”
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
Amyloid beta from axons and dendrites reduces local spine number and plasticity
Wei, W., Nguyen, L. N., Kessels, H. W., Hagiwara, H., Sisodia, S., & Malinow, R. (2010) · Nature Neuroscience · doi:10.1038/nn.2476 · Cited by 357
Janke, C., & Kneussel, M. (2010) · Trends in Neurosciences · doi:10.1016/j.tins.2010.05.001 · Cited by 354
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
Ca 2+ Signals and Neuronal Death in Brain Ischemia
Bano, D., & Nicotera, P. (2007) · Stroke · doi:10.1161/01.str.0000256294.46009.29 · Cited by 318
Tubulin polyglutamylation stimulates spastin-mediated microtubule severing
Lacroix, B., van Dijk, J., Gold, N. D., Guizetti, J., Aldrian, G., Rogowski, K., Gerlich, D. W., & Janke, C. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201001024 · Cited by 315
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
Thies, E., & Mandelkow, E.-M. (2007) · The Journal of Neuroscience · doi:10.1523/jneurosci.4674-06.2007 · Cited by 293
Roll‐Mecak, A., & McNally, F. J. (2009) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2009.11.001 · Cited by 291
Calcium lability of cytoplasmic microtubules and its modulation by microtubule-associated proteins.
Schliwa, M., Euteneuer, U., Bulinski, J. C., & Izant, J. G. (1981) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.78.2.1037 · Cited by 239
The tau of MARK: a polarized view of the cytoskeleton
Matenia, D., & Mandelkow, E. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.03.008 · Cited by 236
Tau Protects Microtubules in the Axon from Severing by Katanin
Qiang, L., Yu, W., Andreadis, A., Luo, M., & Baas, P. W. (2006) · Journal of Neuroscience · doi:10.1523/jneurosci.5392-05.2006 · Cited by 235
Wogulis, M., Wright, S., Cunningham, D., Chilcote, T., Powell, K., & Rydel, R. E. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.2381-04.2005 · Cited by 233
Novel diffusion barrier for axonal retention of Tau in neurons and its failure in neurodegeneration
Li, X., Kumar, Y., Zempel, H., Mandelkow, E., Biernat, J., & Mandelkow, E. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.376 · Cited by 232
Calcium Signaling in Dendrites and Spines: Practical and Functional Considerations
Higley, M. J., & Sabatini, B. L. (2008) · Neuron · doi:10.1016/j.neuron.2008.08.020 · Cited by 227
Tau-dependent microtubule disassembly initiated by prefibrillar β-amyloid
King, M. E., Kan, H.-M., Baas, P. W., Erişir, A., Glabe, C. G., & Bloom, G. S. (2006) · The Journal of Cell Biology · doi:10.1083/jcb.200605187 · Cited by 215
Differential Localization of MAP‐2 and Tau in Mammalian Neurons in Situ a
Binder, L. I., Frankfurter, A. J., & Rebhun, L. I. (1986) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1986.tb38392.x · Cited by 210
Cytoskeletal pathologies of Alzheimer disease
Bamburg, J. R., & Bloom, G. S. (2009) · Cell Motility and the Cytoskeleton · doi:10.1002/cm.20388 · Cited by 175
Control of neuronal polarity and plasticity – a renaissance for microtubules?
Hoogenraad, C. C., & Bradke, F. (2009) · Trends in Cell Biology · doi:10.1016/j.tcb.2009.08.006 · Cited by 173
Swimming against the Tide: Mobility of the Microtubule-Associated Protein Tau in Neurons
Konzack, S., Thies, E., Marx, A., Mandelkow, E., & Mandelkow�, E. (2007) · Journal of Neuroscience · doi:10.1523/jneurosci.0927-07.2007 · Cited by 165
Aronov, S., Aranda, G., Behar, L., & Ginzburg, I. (2001) · Journal of Neuroscience · doi:10.1523/jneurosci.21-17-06577.2001 · Cited by 165
Nakata, T., Niwa, S., Okada, Y., Perez, F., & Hirokawa, N. (2011) · Journal of Cell Biology · doi:10.1083/jcb.201104034 · Cited by 156
Baas, P. W., Karabay, A., & Qiang, L. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.08.004 · Cited by 156
Kanai, Y., & Hirokawa, N. (1995) · Neuron · doi:10.1016/0896-6273(95)90298-8 · Cited by 144 · cited 1×
“The basis for axonal Tau sorting in mature neurons is still not well understood, and several protein-based or mRNA-based mechanisms may work in parallel (Kanai and Hirokawa, 1995; Aronov et al , 2001; Nakata et al , 2011), including a retrograde barrier for Tau at the AIS (Li et al , 2011).”
Loss of tau elicits axonal degeneration in a mouse model of Alzheimer's disease
Dawson, H. N., Cantillana, V., Jansen, M., Wang, H., Vitek, M. P., Wilcock, D. M., Lynch, J., & Laskowitz, D. T. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.04.037 · Cited by 137
Cognitive defects are reversible in inducible mice expressing pro-aggregant full-length human Tau
Van der Jeugd, A., Hochgräfe, K., Ahmed, T., Decker, J. M., Sydow, A., Hofmann, A., Wu, D., Messing, L., Balschun, D., D’Hooge, R., et al. (2012) · Acta Neuropathologica · doi:10.1007/s00401-012-0987-3 · Cited by 135
Self-citationMembrane‐bound β‐amyloid oligomers are recruited into lipid rafts by a fyn‐dependent mechanism
Williamson, R., Usardi, A., Hanger, D. P., & Anderton, B. H. (2007) · The FASEB Journal · doi:10.1096/fj.07-9766com · Cited by 123
Regulation of Microtubule Severing by Katanin Subunits during Neuronal Development
Yu, W. (2005) · Journal of Neuroscience · doi:10.1523/jneurosci.0834-05.2005 · Cited by 109
Synaptic targeting by Aβ oligomers (ADDLS) as a basis for memory loss in early Alzheimer's disease
Klein, W. L. (2006) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2005.11.003 · Cited by 109
Pleiotropic effects of spastin on neurite growth depending on expression levels
Riano, E., Martignoni, M., Mancuso, G., Cartelli, D., Crippa, F., Toldo, I., Siciliano, G., Bella, D. D., Taroni, F., Bassi, M. T., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.05875.x · Cited by 100
Sarkar, M., Kuret, J., & Lee, G. S. (2008) · Journal of Neuroscience Research · doi:10.1002/jnr.21721 · Cited by 96
PAK5 Kinase Is an Inhibitor of MARK/Par-1, Which Leads to Stable Microtubules and Dynamic Actin
Matenia, D., Griesshaber, B., Li, X., Thiessen, A., Johne, C., Jiao, J., Mandelkow�, E., & Mandelkow, E. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-01-0081 · Cited by 93
Whiteman, I. T., Gervasio, O. L., Cullen, K. M., Guillemin, G. J., Jeong, E. V., Witting, P. K., Antao, S. T., Minamide, L. S., Bamburg, J. R., & Goldsbury, C. (2009) · The Journal of Neuroscience · doi:10.1523/jneurosci.3531-09.2009 · Cited by 92
Zempel, H., & Mandelkow, E. (2011) · Neurodegenerative Diseases · doi:10.1159/000332816 · Cited by 90
Sudo, H., & Baas, P. W. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq521 · Cited by 77
Tau impacts on growth-factor-stimulated actin remodeling
Sharma, V. M., Litersky, J. M., Bhaskar, K., & Lee, G. S. (2007) · Journal of Cell Science · doi:10.1242/jcs.03378 · Cited by 75
The microtubule cytoskeleton and the development of neuronal polarity
Mandell, J. W., & Banker, G. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(94)00164-v · Cited by 69
Human spastin has multiple microtubule‐related functions
Salinas, S., Salas, R. E. C., Proukakis, C., Cooper, J. A. D., Weston, A., Schiavo, G., & Warner, T. T. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03472.x · Cited by 66
Differential Regulation of Dendritic and Axonal Development by the Novel Krüppel-Like Factor Dar1
Ye, B., Kim, J. H., Yang, L., McLachlan, I. G., Younger, S. H., Jan, L. Y., & Jan, Y. N. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.6307-10.2011 · Cited by 57
Antagonistic Effects of Doublecortin and MARK2/Par-1 in the Developing Cerebral Cortex
Sapir, T., Shmueli, A., Levy, T., Timm, T., Elbaum, M., Mandelkow, E., & Reiner, O. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.2363-08.2008 · Cited by 52
Pattern of tau isoforms expression during development in vivo
Bullmann, T., Holzer, M., Mori, H., & Arendt, T. (2009) · International Journal of Developmental Neuroscience · doi:10.1016/j.ijdevneu.2009.06.001 · Cited by 48
Sudo, H., & Maru, Y. (2007) · The FASEB Journal · doi:10.1096/fj.06-7254com · Cited by 46
Timm, T., von Kries, J. P., Li, X., Zempel, H., Mandelkow�, E., & Mandelkow, E.-M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.257865 · Cited by 43
Hayashi, K., Suzuki, A., Hirai, S.-I., Kurihara, Y., Hoogenraad, C. C., & Ohno, S. (2011) · Journal of Neuroscience · doi:10.1523/jneurosci.0751-11.2011 · Cited by 36
Rui, Y., Li, R., Liu, Y., Zhu, S., Yu, X., Sheng, Z., & Xie, Z. (2006) · Cell Biology International · doi:10.1016/j.cellbi.2006.05.005 · Cited by 21
Iwaya, N., Akiyama, K., Goda, N., Tenno, T., Fujiwara, Y., Hamada, D., Ikura, T., Shirakawa, M., & Hiroaki, H. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08528.x · Cited by 14
Flagged first, then by citations
Cited by
Sorted by citations
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
Bloom (2014) · doi:10.1001/jamaneurol.2013.5847 · Cited by 2,194
The Intersection of Amyloid Beta and Tau at Synapses in Alzheimer’s Disease
Spires-Jones, T. L., & Hyman, B. T. (2014) · Neuron · doi:10.1016/j.neuron.2014.05.004 · Cited by 1,201
Fricker, M., Tolkovsky, A. M., Borutaitė, V., Coleman, M. P., & Brown, G. C. (2018) · Physiological Reviews · doi:10.1152/physrev.00011.2017 · Cited by 1,148
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
The Amyloid-β Oligomer Hypothesis: Beginning of the Third Decade
Cline, E. N., Bicca, M. A., Viola, K. L., & Klein, W. L. (2018) · Journal of Alzheimer's Disease · doi:10.3233/jad-179941 · Cited by 870
Stress granules and neurodegeneration
Wolozin, B., & Ivanov, P. (2019) · Nature Reviews Neuroscience · doi:10.1038/s41583-019-0222-5 · Cited by 810
Building the Neuronal Microtubule Cytoskeleton
Kapitein, L. C., & Hoogenraad, C. C. (2015) · Neuron · doi:10.1016/j.neuron.2015.05.046 · Cited by 684
Epileptic activity in Alzheimer’s disease: Causes and clinical relevance
Vossel, K. A., Tartaglia, M. C., Nygaard, H. B., Zeman, A. Z., & Miller, B. L. (2017) · The Lancet Neurology · doi:10.1016/s1474-4422(17)30044-3 · Cited by 590
Amyloid β Protein and Alzheimer’s Disease: When Computer Simulations Complement Experimental Studies
Nasica-Labouze, J., Nguyen, P. H., Sterpone, F., Berthoumieu, O., Buchete, N., Côté, S., Simone, A. D., Doig, A. J., Faller, P., Garcı́a, A. E., et al. (2015) · Chemical Reviews · doi:10.1021/cr500638n · Cited by 591
Dejanovic, B., Huntley, M. A., De Mazière, A., Meilandt, W. J., Wu, T., Srinivasan, K., Jiang, Z., Gandham, V., Friedman, B. A., Ngu, H., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.10.014 · Cited by 517
Synaptic degeneration in Alzheimer disease
Tzioras, M., McGeachan, R. I., Durrant, C. S., & Spires-Jones, T. L. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-022-00749-z · Cited by 504
Tau imaging: early progress and future directions
Villemagne, V. L., Fodero-Tavoletti, M. T., Masters, C. L., & Rowe, C. C. (2015) · The Lancet Neurology · doi:10.1016/s1474-4422(14)70252-2 · Cited by 501
Morris, M., Knudsen, G. M., Maeda, S., Trinidad, J. C., Ioanoviciu, A., Burlingame, A. L., & Mucke, L. (2015) · Nature Neuroscience · doi:10.1038/nn.4067 · Cited by 472
Kent, S. A., Spires-Jones, T. L., & Durrant, C. S. (2020) · Acta Neuropathologica · doi:10.1007/s00401-020-02196-w · Cited by 446
Systemic administration of epothilone B promotes axon regeneration after spinal cord injury
Ruschel, J., Hellal, F., Flynn, K. C., Dupraz, S., Elliott, D. A., Tedeschi, A., Bates, M., Sliwinski, C., Brook, G. A., Dobrindt, K., et al. (2015) · Science · doi:10.1126/science.aaa2958 · Cited by 444
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
Amyloid-β and tau complexity — towards improved biomarkers and targeted therapies
Polanco, J. C., Li, C., Bodea, L., Martínez‐Mármol, R., Meunier, F. A., & Götz, J. (2017) · Nature Reviews Neurology · doi:10.1038/nrneurol.2017.162 · Cited by 383
Ferreira, S. T., Lourenco, M. V., Oliveira, M. M., & De Felice, F. G. (2015) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2015.00191 · Cited by 373
Interaction of tau with the RNA-Binding Protein TIA1 Regulates tau Pathophysiology and Toxicity
Vanderweyde, T. E., Apicco, D. J., Youmans-Kidder, K., Ash, P. E. A., Cook, C. N., da Rocha, E. L., Jansen‐West, K. R., Frame, A. A., Citro, A., Leszyk, J., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.04.045 · Cited by 346
Molecular Basis of Familial and Sporadic Alzheimer's Disease
Dorszewska, J., Prendecki, M., Oczkowska, A., Dezor, M., & Kozubski, W. P. (2016) · Current Alzheimer Research · doi:10.2174/1567205013666160314150501 · Cited by 340
Sadleir, K. R., Kandalepas, P. C., Buggia-Prévot, V., Nicholson, D. A., Thinakaran, G., & Vassar, R. (2016) · Acta Neuropathologica · doi:10.1007/s00401-016-1558-9 · Cited by 294
Dendritic Tau in Alzheimer’s Disease
Ittner, A., & Ittner, L. M. (2018) · Neuron · doi:10.1016/j.neuron.2018.06.003 · Cited by 278
Stability properties of neuronal microtubules
Baas, P. W., Rao, A. N., Matamoros, A. J., & Leo, L. (2016) · Cytoskeleton · doi:10.1002/cm.21286 · Cited by 315
A critical appraisal of the pathogenic protein spread hypothesis of neurodegeneration
Walsh, D. M., & Selkoe, D. J. (2016) · Nature reviews. Neuroscience · doi:10.1038/nrn.2016.13 · Cited by 300
Lost after translation: missorting of Tau protein and consequences for Alzheimer disease
Zempel, H., & Mandelkow�, E. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.08.004 · Cited by 284
Graded Control of Microtubule Severing by Tubulin Glutamylation
Valenstein, M. L., & Roll‐Mecak, A. (2016) · Cell · doi:10.1016/j.cell.2016.01.019 · Cited by 268
Synaptic dysfunction in Alzheimer's disease: Mechanisms and therapeutic strategies
Chen, Y., Fu, A. K. Y., & Ip, N. Y. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.11.006 · Cited by 258
Pathogenesis of synaptic degeneration in Alzheimer's disease and Lewy body disease
Overk, C. R., & Masliah, E. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.015 · Cited by 242
Analyzing dendritic spine pathology in Alzheimer’s disease: Problems and opportunities
Dorostkar, M. M., Zou, C., Blazquez-Llorca, L., & Herms, J. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1449-5 · Cited by 235
Dendritic Spine Pathology in Neurodegenerative Diseases
Herms, J., & Dorostkar, M. M. (2016) · Annual Review of Pathology: Mechanisms of Disease · doi:10.1146/annurev-pathol-012615-044216 · Cited by 201
Untangling the association of amyloid-β and tau with synaptic and axonal loss in Alzheimer’s disease
Pereira, J. B., Janelidze, S., Ossenkoppele, R., Kvartsberg, H., Brinkmalm, A., Mattsson, N., Stomrud, E., Smith, R. A., Zetterberg, H., Blennow, K., et al. (2020) · Brain · doi:10.1093/brain/awaa395 · Cited by 206
Amyloid-β and Tau at the Crossroads of Alzheimer’s Disease
Gallardo, G., & Holtzman, D. M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_16 · Cited by 210
Yau, K. W., Schätzle, P., Tortosa, E., Pagès, S., Holtmaat, A. J. D. G., Kapitein, L. C., & Hoogenraad, C. C. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.2430-15.2016 · Cited by 194
Goure, W. F., Krafft, G. A., Jerecic, J., & Hefti, F. (2014) · Alzheimer's Research & Therapy · doi:10.1186/alzrt272 · Cited by 190
Detection of Aggregation-Competent Tau in Neuron-Derived Extracellular Vesicles
Guix, F. X., Corbett, G. T., Cha, D., Mustapić, M., Liu, W., Mengel, D., Chen, Z., Aïkawa, E., Young‐Pearse, T. L., Kapogiannis, D., et al. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030663 · Cited by 186
Izzo, N. J., Staniszewski, A., To, L., Fa, M., Teich, A. F., Saeed, F., Wostein, H., Walko, T., Vaswani, A., Wardius, M., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0111898 · Cited by 180
Li, C., & Götz, J. (2017) · The EMBO Journal · doi:10.15252/embj.201797724 · Cited by 178
Metabolism: A Novel Shared Link between Diabetes Mellitus and Alzheimer’s Disease
Sun, Y., Ma, C., Sun, H. J., Wang, H., Wei, P., Zhou, Z., Wang, H., Pi, C., Shi, Y., & He, X. (2020) · Journal of Diabetes Research · doi:10.1155/2020/4981814 · Cited by 179
Sohn, P. D., Tracy, T. E., Son, H.-I., Zhou, Y., Leite, R. E. P., Miller, B. L., Seeley, W. W., Grinberg, L. T., & Gan, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0109-0 · Cited by 160
Tau reduction prevents Aβ-induced axonal transport deficits by blocking activation of GSK3β
Vossel, K. A., Xu, J. C., Fomenko, V., Miyamoto, T., Suberbielle, E., Knox, J. A., Ho, K., Kim, D. H., Yu, G.-Q., & Mucke, L. (2015) · Journal of Cell Biology · doi:10.1083/jcb.201407065 · Cited by 167
Curcumin Inhibits Tau Aggregation and Disintegrates Preformed Tau Filaments in vitro
Rane, J. S., Bhaumik, P., & Panda, D. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170351 · Cited by 168
Oligomer Formation of Tau Protein Hyperphosphorylated in Cells
Tepper, K., Biernat, J., Kumar, S., Wegmann, S., Timm, T., Hübschmann, S., Redecke, L., Mandelkow, E., Müller, D. J., & Mandelkow�, E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.611368 · Cited by 159
Hall, A., Throesch, B. T., Buckingham, S. C., Markwardt, S. J., Peng, Y., Wang, Q., Hoffman, D., & Roberson, E. (2015) · Journal of Neuroscience · doi:10.1523/jneurosci.2552-14.2015 · Cited by 152
SIRT1 Deacetylates Tau and Reduces Pathogenic Tau Spread in a Mouse Model of Tauopathy
Min, S., Sohn, P., Li, Y., Devidze, N., Johnson, J. R., Krogan, N. J., Masliah, E., Mok, S., Gestwicki, J. E., & Gan, L. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.2369-17.2018 · Cited by 151
UB‐311, a novel UBITh ® amyloid β peptide vaccine for mild Alzheimer's disease
Wang, C. Y., Wang, P., Chiu, M., Finstad, C. L., Lin, F., Lynn, S., Tai, Y., De Fang, X., Zhao, K., Hung, C., et al. (2017) · Alzheimer's & Dementia: Translational Research & Clinical Interventions · doi:10.1016/j.trci.2017.03.005 · Cited by 150
Schützmann, M. P., Hasecke, F., Bachmann, S., Zielinski, M., Hänsch, S., Schroeder, G. F., Zempel, H., & Hoyer, W. (2021) · Nature Communications · doi:10.1038/s41467-021-24900-4 · Cited by 148
Zempel, H., Dennissen, F. J. A., Kumar, Y., Luedtke, J., Biernat, J., Mandelkow, E., & Mandelkow�, E. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.784702 · Cited by 147
Buchholz, S., & Zempel, H. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13784 · Cited by 154
Microtubules in health and degenerative disease of the nervous system
Matamoros, A. J., & Baas, P. W. (2016) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2016.06.016 · Cited by 137
Pagano, K., Tomaselli, S., Molinari, H., & Ragona, L. (2020) · Frontiers in Neuroscience · doi:10.3389/fnins.2020.619667 · Cited by 139
Derisbourg, M. J., Leghay, C., Chiappetta, G., Fernández-Gómez, F.-J., Laurent, C., Demeyer, D., Carrier, S., Buée‐Scherrer, V., Blum, D. L., Vinh, J., et al. (2015) · Scientific Reports · doi:10.1038/srep09659 · Cited by 133
Miller, E. C., Teravskis, P. J., Dummer, B. W., Zhao, X., Huganir, R. L., & Liao, D. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12507 · Cited by 131
Microtubule Dysfunction: A Common Feature of Neurodegenerative Diseases
Sferra, A., Nicita, F., & Bertini, E. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197354 · Cited by 138
Savioz, A., Leuba, G., & Vallet, P. G. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.09.004 · Cited by 127
The dendritic hypothesis for Alzheimer's disease pathophysiology
Cochran, J. N., Hall, A. M., & Roberson, E. D. (2014) · Brain Research Bulletin · doi:10.1016/j.brainresbull.2013.12.004 · Cited by 114
Benseny‐Cases, N., Klementieva, O. L., Cotte, M., Ferrer, I., & Cladera, J. (2014) · Analytical Chemistry · doi:10.1021/ac502667b · Cited by 122
Shi, Z., Zhang, K., Zhou, H., Jiang, L., Xie, B., Wang, R., Xia, W., Yin, Y., Gao, Z., Cui, D., et al. (2020) · Aging Cell · doi:10.1111/acel.13125 · Cited by 115
Tau Accumulation, Altered Phosphorylation, and Missorting Promote Neurodegeneration in Glaucoma
Chiasseu, M., Vargas, J. L. C., Destroismaisons, L., Velde, C. V., Leclerc, N. M., & Polo, A. D. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3986-15.2016 · Cited by 105
The cytoskeleton as a novel therapeutic target for old neurodegenerative disorders
Eira, J., Silva, C. S., Sousa, M. M., & Liz, M. A. (2016) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2016.04.007 · Cited by 109
The Role of Protein Misfolding and Tau Oligomers (TauOs) in Alzheimer′s Disease (AD)
Mroczko, B., Groblewska, M., & Litman‐Zawadzka, A. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20194661 · Cited by 111
Ondrejčák, T., Klyubin, I. V., Corbett, G. T., Fraser, G. M., Hong, W., Mably, A. J., Gardener, M. J., Hammersley, J., Perkinton, M. S., Billinton, A., et al. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1700-18.2018 · Cited by 110
Alzheimer's disease pathophysiology in the Retina
Gaire, B. P., Koronyo, Y., Fuchs, D.-T. S., Shi, H., Rentsendorj, A., Danziger, R., Vit, J., Mirzaei, N., Doustar, J., Sheyn, J., et al. (2024) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2024.101273 · Cited by 106
Tubulin post‐translational modifications control neuronal development and functions
Moutin, M., Bosc, C., Peris, L., & Andrieux, A. (2020) · Developmental Neurobiology · doi:10.1002/dneu.22774 · Cited by 97
Cheng, J. S., Craft, R., Yu, G.-Q., Ho, K., Wang, X., Mohan, G., Mangnitsky, S., Ponnusamy, R., & Mucke, L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0115765 · Cited by 100
Brill, M. S., Kleele, T., Ruschkies, L., Wang, M., Marahori, N. A., Reuter, M. S., Hausrat, T. J., Weigand, E. E., Fisher, M., Ahles, A., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.049 · Cited by 105
Transport and diffusion of Tau protein in neurons
Scholz, T., & Mandelkow�, E. (2014) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-014-1610-7 · Cited by 105
Kaniyappan, S., Chandupatla, R., Mandelkow, E., & Mandelkow, E. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.04.002 · Cited by 100
Axonal Degeneration in AD: The Contribution of Aβ and Tau
Salvadores, N., Gerónimo‐Olvera, C., & Court, F. A. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.581767 · Cited by 100
Zempel, H., & Mandelkow, E. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0064-1 · Cited by 93
CIP2A Causes Tau/APP Phosphorylation, Synaptopathy, and Memory Deficits in Alzheimer’s Disease
Shentu, Y.-P., Huo, Y., Feng, X.-L., Gilbert, J., Zhang, Q., Liuyang, Z.-Y., Wang, X.-L., Wang, G., Zhou, H., Wang, X.-C., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.06.009 · Cited by 90
“In primary neurons, we further observed that CIP2A promoted tau translocalization to dendrites and spines, which is considered to be the key event mediating the synaptic toxicity of tau (Pooler et al., 2014; Zempel et al., 2013).”
BackgroundMicrotubule Dynamics in Neuronal Development, Plasticity, and Neurodegeneration
Penazzi, L., Bakota, L., & Brandt, R. (2015) · International review of cytology · doi:10.1016/bs.ircmb.2015.09.004 · Cited by 97
The Ubiquitin-Proteasome System and Molecular Chaperone Deregulation in Alzheimer’s Disease
Sulistio, Y. A., & Heese, K. (2015) · Molecular Neurobiology · doi:10.1007/s12035-014-9063-4 · Cited by 93
Bell, M. J., & Zempel, H. (2021) · Reviews in the Neurosciences · doi:10.1515/revneuro-2020-0152 · Cited by 92
Brandt, R., Trushina, N. I., & Bakota, L. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.590059 · Cited by 88
Xia, D., Li, C., & Götz, J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.12.017 · Cited by 91
Justice, N. J., Huang, L., Tian, J.-B., Cole, A., Pruski, M., Hunt, A. J., Flores, R., Zhu, M. X., Arenkiel, B. R., & Zheng, H. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.3333-14.2015 · Cited by 81
Do, T. D., Economou, N. J., Chamas, A., Buratto, S. K., Shea, J., & Bowers, M. T. (2014) · The Journal of Physical Chemistry B · doi:10.1021/jp506258g · Cited by 81
Zhao, Y., Chen, X., Wu, Y., Wang, Y., Li, Y., & Xiang, C. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00140 · Cited by 79
Kanno, T., Tsuchiya, A., & Nishizaki, T. (2014) · Behavioural Brain Research · doi:10.1016/j.bbr.2014.08.034 · Cited by 76
Kobayashi, S., Tanaka, T., Soeda, Y., Almeida, O. F. X., & Takashima, A. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.05.012 · Cited by 74
Structural basis for polyglutamate chain initiation and elongation by TTLL family enzymes
Mahalingan, K. K., Keenan, E. K., Strickland, M., Li, Y., Liu, Y., Ball, H. L., Tanner, M. E., Tjandra, N., & Roll‐Mecak, A. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0462-0 · Cited by 70
Physiological and Pathophysiological Implications of Synaptic Tau
Regan, P. L., Whitcomb, D. J., & Cho, K. (2016) · The Neuroscientist · doi:10.1177/1073858416633439 · Cited by 75
Vargas, L. M., Cerpa, W. F., Muñoz, F. J., Zanlungo, S., & Alvarez, A. R. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2018.01.023 · Cited by 71
Tau imaging in the study of ageing, Alzheimer's disease, and other neurodegenerative conditions
Villemagne, V. L., & Okamura, N. (2015) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2015.09.002 · Cited by 70
FRET-based Tau seeding assay does not represent prion-like templated assembly of Tau filaments
Kaniyappan, S., Tepper, K., Biernat, J., Chandupatla, R., Hübschmann, S., Irsen, S. H., Bicher, S., Klatt, C., Mandelkow, E., & Mandelkow�, E. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-020-00389-1 · Cited by 65
Tau neurotoxicity and rescue in animal models of human Tauopathies
Krüger, L., & Mandelkow, E. (2015) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2015.09.004 · Cited by 63
Fernandez-Valenzuela, J. J., Sanchez-Varo, R. M., Muñoz‐Castro, C., Castro, V. D., Sánchez‐Mejías, E., Navarro, V., Jiménez, S., Nuñez‐Diaz, C., Gómez-Arboledas, Á., Moreno‐González, I., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-71767-4 · Cited by 60
The interaction of α-synuclein and Tau: A molecular conspiracy in neurodegeneration?
Xu, Y., Uronen, R., & Huttunen, H. J. (2018) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2018.05.005 · Cited by 61
Stabilization of dynamic microtubules by mDia1 drives Tau-dependent Aβ1–42 synaptotoxicity
Qu, X., Yuan, F. N., Corona, C., Pasini, S., Pero, M. E., Gundersen, G. G., Shelanski, M. L., & Bartolini, F. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701045 · Cited by 62
Shati, A. A., & Alfaifi, M. Y. (2018) · Neurochemical Research · doi:10.1007/s11064-018-2683-8 · Cited by 58
Synaptic vesicle cycle and amyloid β: Biting the hand that feeds
Ovsepian, S. V., O’Leary, V. B., Záborszky, L., Ntziachristos, V., & Dolly, J. O. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.01.011 · Cited by 57
Tau acts as a mediator forAlzheimer's disease‐related synaptic deficits
Liao, D., Miller, E. C., & Teravskis, P. J. (2014) · European Journal of Neuroscience · doi:10.1111/ejn.12504 · Cited by 53
AAA ATPases as therapeutic targets: Structure, functions, and small-molecule inhibitors
Zhang, G., Li, S., Cheng, K.-W., & Chou, T. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113446 · Cited by 53
Penazzi, L., Tackenberg, C., Ghori, A., Golovyashkina, N., Niewidok, B., Selle, K., Ballatore, C., Smith, A. B., Bakota, L., & Brandt, R. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.01.002 · Cited by 50
Hu, S., Wang, H., Chen, K., Cheng, P., Gao, S., Liu, J., Li, X., & Sun, X. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-150432 · Cited by 50
Wu, Z., Yang, B., Liu, C., Liang, G., Liu, W., Pickup, S., Meng, Q., Tian, Y., Li, S., Eckenhoff, M. F., et al. (2015) · Alzheimer Disease & Associated Disorders · doi:10.1097/wad.0000000000000075 · Cited by 46
Langerscheidt, F., Wied, T., Kabbani, M. A. A., van Eimeren, T., Wunderlich, G., & Zempel, H. (2024) · Journal of Neurology · doi:10.1007/s00415-024-12314-3 · Cited by 48
Tau Mislocation in Glucocorticoid-Triggered Hippocampal Pathology
Pinheiro, S., Silva, J. M., Mota, C., Vaz‐Silva, J., Veloso, A., Pinto, V., Sousa, N., Cerqueira, J., & Sotiropoulos, I. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9356-2 · Cited by 47
Metadata
- Authors
- Zempel, H., Luedtke, J., Kumar, Y., Biernat, J., Dawson, H., Mandelkow, E., & Mandelkow, E.
- Affiliations
- German Center for Neurodegenerative Diseases (DE)
- Duke Medical Center (US)
- Center of Advanced European Studies and Research (DE)
- Corresponding author
- Mandelkow, Eva‐Maria
- Venue
- The EMBO Journal
- Published
- 2013-09-24
- Volume
- 32
- Issue
- 22
- Pages
- 2920-2937
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- PMC
- PMC3831312
- OpenAlex
- W2122620510
- Cited by
- 283
- References
- 85
- Citations by year
- 2026: 15 · 2025: 18 · 2024: 23 · 2023: 15 · 2022: 24 · 2021: 17 · 2020: 25 · 2019: 16 · 2018: 22 · 2017: 18 · 2016: 34 · 2015: 26 · 2014: 26 · 2013: 3
- FWCI
- 20.60
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- Locations
- The EMBO Journal (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- DZNE Pub (submittedVersion)
- Funders
- Wellcome Trust (089703)
- Deutsches Zentrum für Neurodegenerative Erkrankungen
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta oligomers, tau protein, Alzheimer's disease, microtubule severing, spastin, synaptic damage, dendritic microtubules, MARK kinases, tau phosphorylation, synaptic loss, microtubule stabilization
- MeSH terms
- Spastin, Adenosine Triphosphatases, Animals, Cells, Cultured, Microtubules, Peptide Synthases, Synapses, Amyloid beta-Peptides, tau Proteins, Mice, Knockout, Glutamic Acid, Mice, Rats
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
