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Aβ Oligomers Cause Localized Ca 2+ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines
Open accessAbstract
Aggregation of amyloid-β (Aβ) and Tau protein are hallmarks of Alzheimer's disease (AD), and according to the Aβ-cascade hypothesis, Aβ is considered toxic for neurons and Tau a downstream target of Aβ. We have investigated differentiated primary hippocampal neurons for early localized changes following exposure to Aβ oligomers. Initial events become evident by missorting of endogenous Tau into the somatodendritic compartment, in contrast to axonal sorting in normal neurons. In missorted dendritic regions there is a depletion of spines and local increase in Ca 2+ , and breakdown of microtubules. Tau in these regions shows elevated phosphorylation at certain sites diagnostic of AD-Tau (e.g., epitope of antibody 12E8, whose phosphorylation causes detachment of Tau from microtubules, and AT8 epitope), and local elevation of certain kinase activities (e.g., MARK/par-1, BRSK/SADK, p70S6K, cdk5, but not GSK3β, JNK, MAPK). These local effects occur without global changes in Tau, tubulin, or kinase levels. Somatodendritic missorting occurs not only with Tau, but also with other axonal proteins such as neurofilaments, and correlates with pronounced depletion of microtubules and mitochondria. The Aβ-induced effects on microtubule and mitochondria depletion, Tau missorting, and loss of spines are prevented by taxol, indicating that Aβ-induced microtubule destabilization and corresponding traffic defects are key factors in incipient degeneration. By contrast, the rise in Ca 2+ levels, kinase activities, and Tau phosphorylation cannot be prevented by taxol. Incipient and local changes similar to those of Aβ oligomers can be evoked by cell stressors (e.g., H 2 O 2 , glutamate, serum deprivation), suggesting some common mechanism of signaling.
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“mis-localization to dendrites and spines causing neurotoxicity [52]”
From Astrocytic APOE3-Christchurch expression ameliorates brain amyloid-β pathology in 5xFAD mice (2026) · cites this paper as [52]
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“Under normal conditions, tau is primarily localized to axons and promotes formation and stabilization of microtubules; however, in AD, tau becomes hyperphosphorylated and mislocalizes to somatodendritic compartments (Avila et al., 2004, Ittner et al., 2010, Zempel et al., 2010).”
From Dendritic Spine Remodeling and Synaptic Tau Levels in PS19 Tauopathy Mice (2021) · cites this paper as Zempel et al., 2010
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“the activities of two major tau kinases, GSK3 and PAR-1/microtubule affinity-regulating kinases (MARKs), are often associated with tau detachment from microtubules and Aβ-induced augmentation of tau toxicity [37, 39, 43–45].”
From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [39]
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“Notably, studies in cultured neurons and transgenic Drosophila showed that Aβ-induced augmentation of tau toxicity caused by Aβ depends on tau phosphorylation at these sites [39, 45, 56–58].”
From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [39]
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“Aβ promotes tau phosphorylation at disease-associated sites in in vitro and in vivo models of AD [2, 35–41].”
From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [39]
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“In cellular and animal models, co-expression of Aβ augments tau phosphorylation at these sites and increases the levels of active GSK3 and PAR-1/MARK [2, 35–41, 43, 44].”
From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [39]
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“Ab oligomers also cause tau mislocalization (77,78).”
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“Under normal conditions, tau is primarily localized to axons and promotes formation and stabilization of microtubules; however, in AD, tau becomes hyperphosphorylated and mislocalizes to somatodendritic compartments (Avila et al., 2004, Ittner et al., 2010, Zempel et al., 2010).”
From Dendritic Spine Remodeling and Synaptic Tau Levels in PS19 Tauopathy Mice (2021) · cites this paper as Zempel et al., 2010
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1 retracted
RETRACTED ARTICLE: A specific amyloid-β protein assembly in the brain impairs memory
Lesné, S., Koh, M. T., Kotilinek, L., Kayed, R., Glabe, C. G., Yang, A., Gallagher, M., & Ashe, K. H. (2006) · Nature · doi:10.1038/nature04533 · Cited by 2,769 · cited 1×
“We also note that in our preparations we did not consistently observe a band at 56 kDa, a species that has been reported to be toxic for transgenic mice (Lesné et al., 2006) but can be visualized in certain conditions (Walsh et al., 2005; Ashe, 2006; Bernstein et al., 2009).”
BackgroundRetractedSoluble 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 · cited 1×
“Despite numerous studies on the pathway of APP misprocessing and its consequences for neurons the modes of A toxicity have remained enigmatic (Haass and Selkoe, 2007; Small and Duff, 2008).”
BackgroundCommon structure of soluble amyloid oligomers implies common mechanism of pathogenesis
Kayed, R., Head, E., Thompson, J. L., McIntire, T. M., Milton, S. C., Cotman, C. W., & Glabe, C. G. (2003) · Science · doi:10.1126/science.1079469 · Cited by 4,064 · cited 1×
“Nevertheless, there were differences in structure because dot blots with antibody A11, which recognizes a more toxic generic amyloid conformation (Kayed et al., 2003), were more intense for F12 medium than for Nb (Fig.”
BackgroundDiffusible, nonfibrillar ligands derived from Aβ 1–42 are potent central nervous system neurotoxins
Lambert, M. P., Barlow, A. K., Chromy, B. A., Edwards, C., Freed, R., Liosatos, M., Morgan, T. E., Rozovsky, I., Trommer, B., Viola, K. L., et al. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6448 · Cited by 3,506 · cited 3×
“There is a moderate decrease of ATP which is more apparent with F12 than with Nb medium, suggesting that F12, which was used in the original procedure (Lambert et al., 1998), could have some toxic effects on its own.”
BackgroundMethodTau-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 · cited 1×
“These include loss of synapses and neurons, deficiency in neurotransmitters and metabolism, aggregation of amyloid- (A )-peptides into extracellular “amyloid plaques” and Tau protein into intracellular “neurofibrillary tangles” (Selkoe, 2004; Binder et al., 2005; Ballatore et al., 2007).”
BackgroundReducing 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 · cited 1×
“…conversely Tau is considered necessary for the progression of neurodegeneration, as seen in cell and animal models (Rapoport et al., 2002; King et al., 2006; Roberson et al., 2007), and indeed the Tau pathology correlates well with clinical symptoms (Braak and Braak, 1991; Clavaguera et al., 2009).”
BackgroundTransmission 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
Physiology and Pathophysiology of Purinergic Neurotransmission
Burnstock, G. (2007) · Physiological Reviews · doi:10.1152/physrev.00043.2006 · Cited by 1,609 · cited 1×
“We also tested extracellular ATP (100 M, 3 h), which functions as a stress signal and induces Ca 2 influx via P2 receptors and has been implicated in neurodegenerative disease (Burnstock, 2007).”
MethodShankar, 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 · cited 1×
“4e,f), and involving NMDA receptors and others (De Felice et al., 2007; Shankar et al., 2007).”
BackgroundThe axonal transport of mitochondria
Saxton, W. M., & Hollenbeck, P. J. (2012) · Journal of Cell Science · doi:10.1242/jcs.053850 · Cited by 1,218 · cited 1×
“As shown previously (Stamer et al., 2002; Hollenbeck and Saxton, 2005; Thies and Mandelkow, 2007), such mitochondrial traffic jams cause a local drop of energy (ATP) and consequently spine destruction through the perturbation of the actin network and loss of synaptic components (Whiteman et al.,…”
Background
Research works printed but not linked: 3
- 10.1242/jcs.02745 · DOI · Paper page
- 10.1074/jbc.R800036200 · DOI
- 10.1186/1750-1326-4-48 · DOI · Paper page
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Items 101–200 of 593
Spines, plasticity, and cognition in Alzheimer's model mice
Spires-Jones, T., & Knafo, S. (2012) · Neural Plasticity · doi:10.1155/2012/319836 · Cited by 133
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
“Missorting of Tau into dendrites and spines compromised transport of mitochondria, leading to the breakdown of MTs and the decay of spines [80].”
BackgroundSelf-citationMolecular mechanisms linking amyloid β toxicity and Tau hyperphosphorylation in Alzheimer׳s disease
Lloret, A., Fuchsberger, T., Giraldo, E., & Viña, J. (2015) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2015.02.028 · Cited by 135
The synapse as a treatment avenue for Alzheimer’s Disease
Peng, L., Bestard‐Lorigados, I., & Song, W. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01565-z · Cited by 162
“For instance, endogenous tau was found to move to the somatodendritic area after treatment with Aβ oligomers, causing spinal density loss [30].”
BackgroundResearch Progress in the Pathogenesis of Alzheimer's Disease
Chen, Y. (2018) · Chinese Medical Journal · doi:10.4103/0366-6999.235112 · Cited by 141
Rosenblum, W. I. (2013) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2013.10.085 · Cited by 142
“In vitro, Ab oligomers cause missorting of tau into dendrites and phosphorylation of tau (Zempel et al., 2010).”
Calcium channel blocking as a therapeutic strategy for Alzheimer's disease: The case for isradipine
Anekonda, T. S., & Quinn, J. F. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2011.08.013 · Cited by 139
“2 can also lead to mislocalization of tau into somatodendritic regions instead of normal axonal localization [64].”
BackgroundKurbatskaya, K., Phillips, E. C., Croft, C. L., Dentoni, G., Hughes, M. M., Wade, M. A., Al‐Sarraj, S., Troakes, C., O’Neill, M. J., Perez‐Nievas, B. G., et al. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0299-2 · Cited by 133
“and tau kinase activity Previous studies have linked elevated intracellular Ca to Aβ overproduction, tau phosphorylation and synaptic dysfunction in AD [38, 83].”
BackgroundBiometals and Their Therapeutic Implications in Alzheimer's Disease
Ayton, S., Lei, P., & Bush, A. I. (2014) · Neurotherapeutics · doi:10.1007/s13311-014-0312-z · Cited by 134
“Aβ-induced tau hyperphosphorylation consequently caused microtubule disassembly [41, 43], reduction of total soluble tau and an increase in tau fragments [44], missorting of tau into dendritic areas [41], activation of the nuclear transcription factor of activated T cells’ apoptotic pathways [45, 46], and cell toxicit…”
BackgroundAlzheimer’s disease as oligomeropathy
Ono, K. (2018) · Neurochemistry International · doi:10.1016/j.neuint.2017.08.010 · Cited by 129
“Similar to the results of a cell culture study (Zempel et al., 2010),”
InfluentialPetry, F. R., Pelletier, J., Bretteville, A., Morin, F., Calon, F., Hébert, S. S., Whittington, R. A., & Planel, E. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094251 · Cited by 142
“Peter Davies (Feinstein Institute for Medical Research, Manhasset, NY, USA): CP13 (pSer(202)), CP27 (human Tau(130-150)), DA9 (Tau(102-140)), MC1 (Tau conformational antibody), MC6 (pSer(235)), PHF-1 (pSer(396)/pSer(404)), TG3 (pThr(231)) and TG5 (Tau (220-242)) [14,15,16,17,18,19,20,21].”
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 169
Tackenberg, C., Grinschgl, S., Trutzel, A., Santuccione, A. C., Frey, M. C., Konietzko, U., Grimm, J., Brandt, R., & Nitsch, R. M. (2013) · Cell Death & Disease · doi:10.1038/cddis.2013.129 · Cited by 130
“Furthermore, several in vitro and in vivo studies support abnormal gain of toxic function for tau caused by hyperphosphorylation.(2,23,33,36,45)”
BackgroundResultGolgi fragmentation in Alzheimer's disease
Joshi, G. S., Bekier, M. E., & Wang, Y. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00340 · Cited by 129
“At the molecular level, Aβ accumulation triggers Ca2+ influx (Zempel et al., 2010), which activates Calpain, a protease known to increase the cleavage of p35 to p25 (Lee et al., 2000), p25 then activates Cdk5.”
BackgroundMiller, 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
“Tau is typically localized to the axons of neurons; however, in its phosphorylated state tau has been shown to mislocalize to the dendritic compartment (Avila et al., 2004; Ittner et al., 2010; Zempel et al., 2010).”
BackgroundInfluentialDevelopmental vulnerability of synapses and circuits associated with neuropsychiatric disorders
Penzes, P., Buonanno, A., Passafaro, M., Sala, C., & Sweet, R. A. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12261 · Cited by 125
“2011), its dendritic mechanisms are just emerging (Zempel et al. 2010), leaving unclear how it may interact with other LTP and LTD mediators impacted by soluble Ab.”
BackgroundConnecting the dots between tau dysfunction and neurodegeneration
Frost, B., Götz, J., & Feany, M. B. (2015) · Trends in Cell Biology · doi:10.1016/j.tcb.2014.07.005 · Cited by 124
Amyloid-β signals through tau to drive ectopic neuronal cell cycle re-entry in Alzheimer's disease
Seward, M. E., Swanson, E., Norambuena, A., Reimann, A., Cochran, J. N., Li, R., Roberson, E. D., & Bloom, G. S. (2013) · Journal of Cell Science · doi:10.1242/jcs.1125880 · Cited by 178
“…examples include cytotoxicity (Nussbaum et al., 2012; Rapoport et al., 2002), disassembly of microtubules (Jin et al., 2011; King et al., 2006; Zempel et al., 2010), learning and memory deficits (Roberson et al., 2007), excitation/inhibition imbalance (Roberson et al., 2011), and impaired…”
BackgroundResultInfluentialSoluble Aβ Promotes Wild-Type Tau Pathology In Vivo
Chabrier, M. A., Blurton-Jones, M., Agazaryan, A. A., Nerhus, J. L., Martinez-Coria, H., & LaFerla, F. M. (2012) · The Journal of Neuroscience · doi:10.1523/jneurosci.0172-12.2012 · Cited by 123
“Interestingly, A oligomers can induce tau mislocalization and phosphorylation in vitro, providing intriguing evidence that soluble A modulates the development of tau pathology (Deshpande et al., 2006; Zempel et al., 2010).”
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
Self-citationSIRT1 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
“…tauopathy mouse model remains to be established, but increased tau levels in the dendritic spine could lead to disruption of the postsynaptic spines (Zempel et al., 2010, 2013) and concomitant loss of presynaptic boutons due to lack of stabilizing interaction at the synapse (Lin and Koleske, 2010).”
BackgroundSavioz, A., Leuba, G., & Vallet, P. G. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.09.004 · Cited by 127
The Role of ADAM10 in Alzheimer’s Disease
Yuan, X., Sun, S., Tan, C., Yu, J., & Tan, L. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-170061 · Cited by 160
Synaptic alterations in the rTg4510 mouse model of tauopathy
Kopeikina, K. J., Polydoro, M., Tai, H., Yaeger, E., Carlson, G. A., Pitstick, R., Hyman, B. T., & Spires‐Jones, T. L. (2012) · The Journal of Comparative Neurology · doi:10.1002/cne.23234 · Cited by 129
“…and Yao, 2003; Hollenbeck and Saxton, 2005; Thies and Mandelkow, 2007; Cuchillo-Ibanez et al., 2008; Dixit et al., 2008; Morfini et al., 2009; Zempel et al., 2010), ultimately leading to axonal and dendritic ‘‘dying back’’ and neuronal death (Coleman and Yao, 2003; Yoshiyama et al., 2007;…”
BackgroundSynapses and Dendritic Spines as Pathogenic Targets in Alzheimer’s Disease
Yu, W., & Lu, B. (2012) · Neural Plasticity · doi:10.1155/2012/247150 · Cited by 123
“It is possible that some common pathogenic mechanisms may underlie the synaptic and dendritic spine pathology in neurodegenerative diseases.”
BackgroundJaworski, T., Lechat, B., Demedts, D., Gielis, L., Devijver, H., Borghgraef, P., Duimel, H., Verheyen, F., Kügler, S., & LEUVEN, F. V. (2011) · American Journal Of Pathology · doi:10.1016/j.ajpath.2011.06.025 · Cited by 121
Are Tangles as Toxic as They Look?
Spires-Jones, T. L., Kopeikina, K. J., Koffie, R. M., de Calignon, A., & Hyman, B. T. (2011) · Journal of Molecular Neuroscience · doi:10.1007/s12031-011-9566-7 · Cited by 104
“In a more recent study, Zempel et al. (2010) extended this finding to show that oligomeric amyloid beta induced loss of dendritic spines and mitochondrial distribution correlate with mislocalization of tau to dendrites in cultured neurons.”
Polydoro, M., Dzhala, V. I., Pooler, A. M., Nicholls, S. B., McKinney, A. P., Sanchez, L., Pitstick, R., Carlson, G. A., Staley, K. J., Spires-Jones, T. L., et al. (2014) · Acta Neuropathologica · doi:10.1007/s00401-013-1215-5 · Cited by 117
“Indeed, recent studies suggest that more soluble forms of tau, rather than fibrillar tangles, may be involved in neuronal dysfunction [28, 29, 44, 45, 50, 63].”
BackgroundResultLuo, J., Wärmländer, S. K. T. S., Gräslund, A., & Abrahams, J. P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.714576 · Cited by 142
“Extracellular fibrillar and oligomeric A peptides seem to promote tau hyperphosphorylation, thereby inducing loss of tau’s microtubule binding activity, leading to neural dysfunction and degeneration (30).”
BackgroundDecker, J. M., Krüger, L., Sydow, A., Dennissen, F. J. A., Šišková, Z., Mandelkow�, E., & Mandelkow, E. (2016) · EMBO Reports · doi:10.15252/embr.201541439 · Cited by 130
“It was reported earlier that mis-sorted, phosphorylated Tau within dendritic spines of primary neurons impairs synaptic transmission by altering the densities of postsynaptic receptors such as AMPARs and NMDARs [12] and causes abnormal changes in intracellular Ca ([Ca]i) [17].”
BackgroundSelf-citationThe 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
Schützmann, M. P., Hasecke, F., Bachmann, S., Zielinski, M., Hänsch, S., Schröder, G., Zempel, H., & Hoyer, W. (2020) · Nature Communications · doi:10.1101/2020.06.28.175885 · Cited by 113
Self-citationMitochondrial Dysfunction in Neural Injury
Zhao, X., Lu, M., Yuan, D., Xu, D.-E., Yao, P.-P., Ji, W., Chen, H., Liu, W., Yan, C.-X., Xia, Y., et al. (2019) · Frontiers in Neuroscience · doi:10.3389/fnins.2019.00030 · Cited by 132
“In this regard, hyperphosphorylated tau causes disruption of preformed microtubules and mitochondrial perinuclear distribution (Zempel et al., 2010; Amadoro et al., 2014; Musiek and Holtzman, 2015).”
BackgroundBarbero-Camps, E., Fernández, A., Martínez, L., Fernández-Checa, J. C., & Colell, A. (2013) · Human Molecular Genetics · doi:10.1093/hmg/ddt201 · Cited by 114
Tokutake, T., Kasuga, K., Yajima, R., Sekine, Y., Tezuka, T., Nishizawa, M., & Ikeuchi, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.348300 · Cited by 124
Impaired regulation of synaptic actin cytoskeleton in Alzheimer's disease
Penzes, P., & VanLeeuwen, J. (2011) · Brain Research Reviews · doi:10.1016/j.brainresrev.2011.01.003 · Cited by 121
Amyloid-β-Induced Dysregulation of AMPA Receptor Trafficking
Guntupalli, S., Widagdo, J., & Anggono, V. (2016) · Neural Plasticity · doi:10.1155/2016/3204519 · Cited by 110
The Essential Role of Soluble Aβ Oligomers in Alzheimer’s Disease
Wang, Z.-X., Tan, L., Liu, J., & Yu, J.-T. (2016) · Molecular Neurobiology · doi:10.1007/s12035-015-9143-0 · Cited by 110
“onstrating mislocalization display decreased spine density [28].”
Progress and Developments in Tau Aggregation Inhibitors for Alzheimer Disease
Bulic, B., Pickhardt, M., & Mandelkow�, E. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm3017317 · Cited by 119
Self-citationLjungberg, M. C., Ali, Y. O., Zhu, J., Wu, C.-S., Oka, K., Zhai, R. G., & Lu, H.-C. (2012) · Human Molecular Genetics · doi:10.1093/hmg/ddr492 · Cited by 107
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
“In the case of Alzheimer disease, Tau together with Amyloid-β are believed to be the two key factors contributing to neurodegeneration [121] (reviews [46, 59, 78]).”
BackgroundSelf-citationAlzheimer's Disease and the Amyloid β-Protein
Walsh, D. M., & Teplow, D. B. (2012) · Progress in molecular biology and translational science · doi:10.1016/b978-0-12-385883-2.00012-6 · Cited by 121
“Implications for viral capsid assembly from crystal structures of HIV-1 Gag(1-278) and CA(N)(133-278).”
BackgroundYu, W., Polepalli, J., Wagh, D., Rajadas, J., Malenka, R., & Lu, B. (2012) · Human Molecular Genetics · doi:10.1093/hmg/ddr576 · Cited by 103
“It also remains to be determined whether Ab oligomers act by directly activating transmembrane receptors, changing neuronal membrane properties or, simply, causing cellular stress (4,34).”
BackgroundResultInfluentialTorres, M., Jiménez, S., Sanchez-Varo, R. M., Navarro, V., Trujillo‐Estrada, L., Sánchez‐Mejías, E., Carmona, I., Dávila, J. C., Vizuete, M., Gutiérrez, A., et al. (2012) · Molecular Neurodegeneration · doi:10.1186/1750-1326-7-59 · Cited by 103
Ando, K., Maruko-Otake, A., Ohtake, Y., Hayashishita, M., Sekiya, M., & Iijima, K. M. (2016) · PLOS Genetics · doi:10.1371/journal.pgen.1005917 · Cited by 105
New Insights Into Drug Discovery Targeting Tau Protein
Soeda, Y., & Takashima, A. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.590896 · Cited by 136
“Tau hyperphosphorylation induces accumulation of tau in the somatodendritic compartment (mis-sorting), self-aggregation, polymerization, defects of axonal mitochondrial trafficking, ultimately leading to neuronal toxicity (Zempel et al., 2010; Zempel and Mandelkow, 2019; Lauretti and Praticò, 2020).”
BackgroundThe Role of microRNAs in Alzheimer’s Disease and Their Therapeutic Potentials
Shaik, M. M., Tamargo, I. A., Abubakar, M. B., Kamal, M. A., Greig, N. H., & Gan, S. H. (2018) · Genes · doi:10.3390/genes9040174 · Cited by 117
Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment
Garg, S., Timm, T., Mandelkow, E.-M., Mandelkow, E., & Wang, Y. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.09.008 · Cited by 103
Self-citationSynaptic Dysfunction in Alzheimer’s Disease: Aβ, Tau, and Epigenetic Alterations
Li, K., Wei, Q., Liu, F., Hu, F., Xie, A., Zhu, L., & Liu, D. (2017) · Molecular Neurobiology · doi:10.1007/s12035-017-0533-3 · Cited by 121
“In cultured neurons, Aβ-induced destruction of microtubules and spines can also be attenuated by RNAi knockdown of Tau [48, 49].”
BackgroundThe case for soluble Aβ oligomers as a drug target in Alzheimer's disease
Hefti, F. F., Goure, W. F., Jerecìć, J., Iverson, K. S., Walicke, P. A., & Krafft, G. A. (2013) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2013.03.002 · Cited by 122
Amar, F., Sherman, M. A., Rush, T., Larson, M. E., Boyle, G. E., Liu, C., Götz, J., Buisson, A., & Lesné, S. (2017) · Science Signaling · doi:10.1126/scisignal.aal2021 · Cited by 114
RetractedAmadoro, G., Corsetti, V., Atlante, A., Florenzano, F., Capsoni, S., Bussani, R., Mercanti, D., & Calissano, P. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.08.001 · Cited by 95
“2G—may reflect the neuronal traffic jamming, likely due to the A -induced microtubule destabilization (Zempel et al., 2010) and to the loss of extreme N-terminal tau domain which is directly involved in axonal transport by binding to the C-terminus of the p150 subunit of the dynactin complex…”
BackgroundWang, X., Zeng, J., Yang, Y., Xiong, Y., Zhang, Z., Qiu, M., Xiong, Y., Sun, X., Tuo, Q., Liu, R., et al. (2014) · Journal of Alzheimer s Disease · doi:10.3233/jad-140198 · Cited by 109
“Tau is an axonal microtubule associated protein; hyperphosphorylation and mislocalization of tau play an important role in NFTs formation and synaptic dysfunction in AD [7, 8].”
BackgroundDesale, S. E., Chidambaram, H., & Chinnathambi, S. (2021) · Molecular Biomedicine · doi:10.1186/s43556-021-00036-1 · Cited by 99
The Role of Tau in Neurodegenerative Diseases and Its Potential as a Therapeutic Target
Wolfe, M. S. (2012) · Scientifica · doi:10.6064/2012/796024 · Cited by 105
Glutamate receptors in preclinical research on Alzheimer's disease: Update on recent advances
Hu, N., Ondrejčák, T., & Rowan, M. J. (2011) · Pharmacology Biochemistry and Behavior · doi:10.1016/j.pbb.2011.04.013 · Cited by 99
Chabrier, M. A., Cheng, D., Castello, N. A., Green, K. N., & LaFerla, F. M. (2014) · Neurobiology of Disease · doi:10.1016/j.nbd.2014.01.007 · Cited by 97
“Soluble Aβ oligomers are potent mediators of synaptotoxicity, and localize rapidly to the synapse in cultured neurons and mouse models of AD (Deshpande et al., 2006; Zempel et al., 2010).”
BackgroundHuang, H., Tang, D., Xu, K., & Jiang, Z.-F. (2013) · Journal of Receptors and Signal Transduction · doi:10.3109/10799893.2013.848891 · Cited by 103
Current Status of Clinical Trials on Tau Immunotherapies
Ji, C., & Sigurdsson, E. M. (2021) · Drugs · doi:10.1007/s40265-021-01546-6 · Cited by 96
The interactions of p53 with tau and Aß as potential therapeutic targets for Alzheimer’s disease
Jembrek, M. J., Slade, N., Hof, P. R., & Šimić, G. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.05.001 · Cited by 101
Phospho-Tau Bar Code: Analysis of Phosphoisotypes of Tau and Its Application to Tauopathy
Kimura, T., Sharma, G., Ishiguro, K., & Hisanaga, S. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00044 · Cited by 116
“For example, the treatment of neurons with Aβ oligomers induces the transfer of tau to dendrites with enhanced phosphorylation at 12E8 sites (Ser262 and Ser356), which are mediated by MARK, SAD or p70S6K localized in dendrites and spines (Zempel et al., 2010).”
BackgroundMiyamoto, T., Stein, L. R., Thomas, R., Djukic, B., Taneja, P., Knox, J. A., Vossel, K. A., & Mucke, L. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0176-x · Cited by 106
The Deacetylase HDAC6 Mediates Endogenous Neuritic Tau Pathology
Tseng, J.-H., Xie, L., Song, S., Xie, Y., Allen, L., Ajit, D., Hong, J.-S., Chen, X., Meeker, R. B., & Cohen, T. J. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.082 · Cited by 93
“Tau-Fyn mislocalization to the dendritic compartment facilitates NMDAR subunit phosphorylation (Ittner et al., 2010; Zempel et al., 2010).”
BackgroundPossible Mechanisms of Tau Spread and Toxicity in Alzheimer’s Disease
Zhang, H., Cao, Y., Ma, L., Wei, Y., & Li, H. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.707268 · Cited by 109
“Tau phosphorylation, mislocalization, and conformational changes can alter Ca2+ homeostasis, induce dendritic spine loss, impair organelle trafficking (particularly mitochondria), and lead to cell death (Dixit et al., 2008; Zempel et al., 2010; Li et al., 2011; Spires-Jones et al., 2011).”
BackgroundEndolysosomal degradation of Tau and its role in glucocorticoid-driven hippocampal malfunction
Vaz‐Silva, J., Gomes, P., Jin, Q., Zhu, M., Zhuravleva, V., Quintremil, S., Meira, T., Silva, J., Dioli, C., Soares‐Cunha, C., et al. (2018) · The EMBO Journal · doi:10.15252/embj.201899084 · Cited by 104
“…and triggers these events by disrupting axonal trafficking (Vossel et al , 2010), promoting GluN2B-related excitotoxicity (Ittner et al , 2010; Zempel et al , 2010), and suppressing nuclear CREB-mediated synthesis of synapse-and memory-related proteins (Yin et al , 2016), among other effects.”
Emerging Therapeutics for Alzheimer's Disease
Chiang, K., & Koo, E. H. (2014) · The Annual Review of Pharmacology and Toxicology · doi:10.1146/annurev-pharmtox-011613-135932 · Cited by 95
Wang, D., Fu, Q., Zhou, Y., Xu, B. Y., Shi, Q., Igwe, B., Matt, L., Hell, J. W., Wisely, E. V., Oddo, S., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.415141 · Cited by 101
Kaniyappan, S., Chandupatla, R., Mandelkow, E., & Mandelkow, E. (2017) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2017.04.002 · Cited by 100
“After the incubation, the cells were lysed as described earlier (Zempel et al., 2010 [30]).”
BackgroundMethodInfluentialSelf-citationSynaptic activity and Alzheimer's disease: a critical update
Tampellini, D. (2015) · Frontiers in Neuroscience · doi:10.3389/fnins.2015.00423 · Cited by 110
“The localization of tau in dendrites is considered to be pathologic, because it is associated with loss of spines, as mentioned above (Zempel et al., 2010), and because it targets the kinase Fyn to post-synaptic compartments (Ittner et al., 2010).”
BackgroundCalcium flux-independent NMDA receptor activity is required for Aβ oligomer-induced synaptic loss
Birnbaum, J. H., Bali, J., Rajendran, L., Nitsch, R. M., & Tackenberg, C. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.160 · Cited by 101
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
Zempel, H., & Mandelkow, E. (2011) · Neurodegenerative Diseases · doi:10.1159/000332816 · Cited by 90
Self-citationJi, C., Tang, M., Zeidler, C., Höhfeld, J., & Johnson, G. V. W. (2019) · Autophagy · doi:10.1080/15548627.2019.1580096 · Cited by 95
“Given that MAPT phosphorylated at Ser262 displays increased sorting to dendritic compartments compared to other MAPT species [28, 29], we further investigated the spatial localization of p-Ser262.”
BackgroundLau, D. H. W., Hogseth, M., Phillips, E. C., O’Neill, M. J., Pooler, A. M., Noble, W. J., & Hanger, D. P. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0317-4 · Cited by 93
“Recent evidence however, suggests that tau is also present in dendrites where it may play a role in synaptic function [1–3].”
BackgroundXia, 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
“Aβwas found to change the phosphorylation status of Tau and alter its subcellular localization [40,42], with a specific role reported for the S262 epitope of Tau (a site recognized by the antibody 12E8) [29].”
BackgroundRasool, S., Martínez‐Coria, H., Wu, J., LaFerla, F. M., & Glabe, C. G. (2013) · Journal of Neurochemistry · doi:10.1111/jnc.12305 · Cited by 74
“More recently, it has been shown that Aβ oligomers cause abnormal tau phosphorylation and morphology changes of spines by missorting of endogenous tau into dendrites (Zempel et al. 2010).”
Nussbaum, J. M., Seward, M. E., & Bloom, G. S. (2013) · Prion · doi:10.4161/pri.22118 · Cited by 128
Zempel, H., & Mandelkow, E. (2015) · Molecular Neurodegeneration · doi:10.1186/s13024-015-0064-1 · Cited by 100
“motifs in the repeat domain of Tau [71, 81].”
InfluentialSelf-citationAxonal Transport Defects in Alzheimer’s Disease
Wang, Z., Tan, L., & Yu, J. (2014) · Molecular Neurobiology · doi:10.1007/s12035-014-8810-x · Cited by 92
“Despite the fact that the GSK-3-dependent mechanism plays an important role in the AT defects induced by Aβ, a recent study showed that extracellular Aβ can bind to a so far unknown receptor causing localized Ca2 elevation, activation of several kinases including MARK, CDK5, and JNK (but not GSK3β), and tau phosphoryl…”
Starvation and inhibition of lysosomal function increased tau secretion by primary cortical neurons
Mohamed, N., Plouffe, V., Rémillard‐Labrosse, G., Planel, E., & Leclerc, N. M. (2014) · Scientific Reports · doi:10.1038/srep05715 · Cited by 92
Sun, Y., Wang, Y., Chen, S., Chen, Y., Shen, J., Yao, W., Gao, X., & Chen, S. (2020) · Theranostics · doi:10.7150/thno.44370 · Cited by 95
“Studies have indicated that Aβ plaques promote tau protein pathology, neuronal damage, and eventually AD [51, 52].”
BackgroundVerma, M., Wills, Z. P., & Chu, C. T. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00523 · Cited by 103
“For example, elevated calcium plays a key role in promoting tau pathology (Zempel et al., 2010), a component of neurofibrillary tangles that characterize an intermediate step in AD progression, through activation of numerous kinases thought to mediate tau’s effects (Mairet-Coello et al., 2013).”
BackgroundUematsu, M., Nakamura, A., Ebashi, M., Hirokawa, K., Takahashi, R., & Uchihara, T. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0501-1 · Cited by 96
“Moreover, reports suggest that Aβ is essential for the initiation of synaptic and neuronal tau pathology [32, 60].”
BackgroundMitochondrial traffic jams in Alzheimer's disease - pinpointing the roadblocks
Correia, S. C., Perry, G. L., & Moreira, P. I. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2016.07.010 · Cited by 92
Warmus, B. A., Sekar, D. R., McCutchen, E., Schellenberg, G. D., Roberts, R. C., McMahon, L. L., & Roberson, E. D. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.3418-14.2014 · Cited by 82
“We looked at phosphorylation residues on tau that have been linked to somatodendritic mislocalization (Zempel et al., 2010).”
BackgroundRecent Progress in Alzheimer’s Disease Research, Part 1: Pathology
Hane, F. T., Lee, B. Y., & Leonenko, Z. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-160882 · Cited by 92
“However, amyloidderived diffusible ligands (ADDLs) appear to induce tau hyperphosphorylation and disruptions of microtubules impairing the cytoskeleton [147].”
BackgroundNew therapeutic targets in Alzheimer's disease: brain deregulation of calcium and zinc
Corona, C., Pensalfini, A., Frazzini, V., & Sensi, S. L. (2011) · Cell Death and Disease · doi:10.1038/cddis.2011.57 · Cited by 81
“phosphorylation has been shown in neurons exposed to oxidative or excitotoxic stress, suggesting a common signaling cascade that culminates in regional tau pathology and eventually in the breakdown of neuronal architecture.(61)”
BackgroundInfluentialNeuropathogenic role of adenylate kinase-1 in Aβ-mediated tau phosphorylation via AMPK and GSK3β
Park, H., Kam, T., Kim, Y., Choi, H., Gwon, Y., Kim, C., Koh, J., & Jung, Y. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds100 · Cited by 89
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
“…by A signals progressing disease Soluble A oligomers have been shown to have a wide range of toxic effects on neurons, including synaptic destabilization, dendritic spine loss, and reduced LTP (Walsh et al., 2002; Shankar et al., 2007, 2008; Zempel et al., 2010, 2013; Mairet-Coello et al., 2013).”
BackgroundEvidence of intraneuronal Aβ accumulation preceding tau pathology in the entorhinal cortex
Welikovitch, L. A., Carmo, S. D., Maglóczky, Z., Szocsics, P., Lőke, J., Freund, T. F., & Cuello, A. C. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1922-z · Cited by 84
Phosphorylation of microtubule‐associated protein tau by AMPK‐related kinases
Yoshida, H., & Goedert, M. (2011) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2011.07523.x · Cited by 85
Pitt, J. E., Wilcox, K. C., Tortelli, V., Diniz, L. P., Oliveira, M. S., Dobbins, C., Yu, X., Nandamuri, S., Gomes, F. C. A., DiNunno, N., et al. (2017) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-06-0416 · Cited by 87
“In the absence of astrocytes, neurons exposed to AβOs exhibited 0.33 ± 0.03 spinophilin puncta per micrometer, a 44% decrease compared with control neurons Koffie et al., 2009; Tomiyama et al., 2010; Zempel et al., 2010; Figueiredo et al., 2013).”
BackgroundMethodInfluentialOrigins of Alzheimerʼs disease
Musiek, E. S., & Holtzman, D. M. (2012) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32835a30f4 · Cited by 85
Role of dietary fatty acids in microglial polarization in Alzheimer’s disease
Desale, S. E., & Chinnathambi, S. (2020) · Journal of Neuroinflammation · doi:10.1186/s12974-020-01742-3 · Cited by 112
“Due to hyperphosphorylation, Tau disrupts from microtubule filaments affecting the axonal stability, and Tau bundles up to form NFTs; accumulation of this leads to death of neurons, which prevails neurodegeneration [12, 15, 16].”
Kodis, E. J., Choi, S. H., Swanson, E., Ferreira, G., & Bloom, G. S. (2018) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2018.05.017 · Cited by 93
“In addition, it has been shown that NMDAR can be influenced by tau upstream of calcium influx, by recruiting the nonreceptor tyrosine kinase, fyn, which phosphorylates NMDAR and thereby facilitates excess calcium influx provoked by AbOs [3,29,36].”
BackgroundThe 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
“It was observed that this missorting of Tau into dendrites may be caused by AβOs exposure of primary hippocampal neurons [96].”
BackgroundInfluentialPharmacological Inhibition of Soluble Epoxide Hydrolase as a New Therapy for Alzheimer's Disease
Griñán‐Ferré, C., Codony, S., Pujol, E., Yang, J., Leiva, R., Escolano, C., Puigoriol‐Illamola, D., Companys‐Alemany, J., Corpas, R., Sanfeliu, C., et al. (2020) · Neurotherapeutics · doi:10.1007/s13311-020-00854-1 · Cited by 99
Pro-aggregant Tau impairs mossy fiber plasticity due to structural changes and Ca++ dysregulation
Decker, J. M., Krüger, L., Sydow, A., Zhao, S., Frotscher, M., Mandelkow�, E., & Mandelkow, E. (2015) · Acta Neuropathologica Communications · doi:10.1186/s40478-015-0193-3 · Cited by 86
“Primary hippocampal neurons were isolated from embryonic E18 Sprague Dawley rats and plated on polyD-lysine-coated glass coverslips (50 g/ml) at a density of 50,000 cells per well in 24 well plates (Corning or Sarstedt) as described previously [28].”
MethodSelf-citationAnand, A., Sharma, N., Gulati, M., & Khurana, N. (2018) · Advances in medical diagnosis, treatment, and care (AMDTC) book series · doi:10.4018/978-1-5225-5282-6.ch011 · Cited by 2
Alzheimer's Disease and Amyloid: Culprit or Coincidence?
Skaper, S. D. (2012) · International review of neurobiology · doi:10.1016/b978-0-12-386986-9.00011-9 · Cited by 82
“In APP transgenicmice, Ab formation causes tau hyperphosphorylation, whereas tau transgenic mice do not show Ab plaque pathology (Götz et al., 2004; Hussain, 2010; Zempel et al., 2010).”
Background
Metadata
- Authors
- Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M.
- Affiliations
- Max Planck Unit for Structural Molecular Biology (DE)
- German Center for Neurodegenerative Diseases (DE)
- Corresponding author
- Mandelkow, Eva-Maria
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2010-09-08
- Volume
- 30
- Issue
- 36
- Pages
- 11938-11950
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6633549
- OpenAlex
- W2041956586
- Cited by
- 686
- References
- 70
- Citations by year
- 2026: 29 · 2025: 33 · 2024: 27 · 2023: 22 · 2022: 30 · 2021: 38 · 2020: 54 · 2019: 46 · 2018: 49 · 2017: 46 · 2016: 50 · 2015: 51 · 2014: 61 · 2013: 54 · 2012: 50
- FWCI
- 32.49
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- DZNE Pub (submittedVersion)
- Funders
- European Commission
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta oligomers, Alzheimer's disease, tau phosphorylation, dendrites, microtubule destabilization, dendritic spines, neurofilaments, mitochondria, paclitaxel, p70S6K, cyclin-dependent kinase 5, hippocampal neurons, axonal transport, oxidative stress, glutamate, serum deprivation
- MeSH terms
- Adenosine Triphosphate, Analysis of Variance, Animals, Calcium, Cells, Cultured, Dendrites, Embryo, Mammalian, Hippocampus, L-Lactate Dehydrogenase, Microtubules, Mitochondria, Neurons, Peptide Fragments, Phosphorylation, Protein Kinases, Time Factors, Amyloid beta-Peptides, tau Proteins, Neurofilament Proteins, Rats, Sprague-Dawley, Protein Transport, Microscopy, Electron, Transmission, Dendritic Spines, Rats
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