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?
The source backs part of the claim, not all of it — or backs it for a different population, condition or comparison.
In the citing paper
“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
Experimental — accuracy not yet measuredIn the citing paper
“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
Flagged first, then by citations
Cited by
Sorted by citations
Items 201–284 of 284
Lu, S., Qiu, S., Yu, G., Zhang, A., & Zhao, Q. (2026) · Ageing Research Reviews · doi:10.1016/j.arr.2026.103097 · Cited by 8
Advances in the drug treatment of Alzheimer’s disease: pathophysiology and mechanisms of action
Nowell, J., Crook, H., de Leon, M. J., & Edison, P. (2026) · BMJ · doi:10.1136/bmj-2023-078881 · Cited by 7
The Role of Tau in the Post-synapse
Regan, P. L., & Cho, K. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_10 · Cited by 7
Bell-Simons, M., Buchholz, S., Klimek, J., & Zempel, H. (2023) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-023-01359-z · Cited by 8
Amyloid β Hypothesis in the Development of Therapeutic Agents for Alzheimer’s Disease
Adeniji, A. O., Adams, P. W., & Mody, V. V. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802810-0.00007-6 · Cited by 7
Tanaka, T., Ohashi, S., Takashima, A., & Kobayashi, S. (2020) · Neurochemistry International · doi:10.1016/j.neuint.2020.104808 · Cited by 7
Kabbani, M. A. A., Köhler, C. N., & Zempel, H. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-23-01742 · Cited by 6
Aderibigbe, O., Wood, L. B., & Margulies, S. S. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26083531 · Cited by 6
Fourrière, L., & Gleeson, P. A. (2025) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2025.1550211 · Cited by 6
Tau Protein Modulates Perineuronal Extracellular Matrix Expression in the TauP301L-acan Mouse Model
Schmidt, S., Holzer, M., Arendt, T., Sonntag, M., & Morawski, M. (2022) · Biomolecules · doi:10.3390/biom12040505 · Cited by 8
Li, S., & Bhalla, R. (2024) · Neurochemical Research · doi:10.1007/s11064-024-04178-w · Cited by 8
Villemagne, V. L., Okamura, N., & Rowe, C. C. (2016) · Alzheimer s & Dementia Diagnosis Assessment & Disease Monitoring · doi:10.1016/j.dadm.2016.05.001 · Cited by 7
Buchholz, S., & Zempel, H. (2023) · Neural Regeneration Research · doi:10.4103/1673-5374.389644 · Cited by 6
Ahmed, G. A.-R., Khalil, S., hotaby, W. E., Abbas, L., Farrag, A. R. H., AbdEl-Aal, W. E., Sherif, H. H. A., Abdel‐Rahman, E. A., Saber, S. H., Hassan, M. A. E., et al. (2020) · Chemistry and Physics of Lipids · doi:10.1016/j.chemphyslip.2020.104931 · Cited by 6
Atsmon‐Raz, Y., & Miller, Y. (2015) · Israel Journal of Chemistry · doi:10.1002/ijch.201400162 · Cited by 6
The mitotic tensegrity guardian tau protects mammary epithelia from katanin-like1-induced aneuploidy
Sudo, H., & Nakajima, K. (2016) · Oncotarget · doi:10.18632/oncotarget.10728 · Cited by 6
Zimmer‐Bensch, G., & Zempel, H. (2021) · Preprints.org · doi:10.20944/preprints202105.0717.v1 · Cited by 6
Buchholz, S., Bell, M. J., Kabbani, M. A. A., Kluge, L., Cagkmak, C., Klimek, J., & Zempel, H. (2022) · Research Square · doi:10.21203/rs.3.rs-2277268/v1 · Cited by 6
Wang, K., Na, L., & Duan, M. (2020) · Current Topics in Medicinal Chemistry · doi:10.2174/1568026620666200916123000 · Cited by 5
Qiu, Y., Wu, C., Li, J., Tang, M., Zhang, S., Jing, T., Liao, Y., & Wang, H. (2020) · Journal of Cancer · doi:10.7150/jca.47694 · Cited by 5
Yu, Y., Zhao, Y., Feng, J., Lian, N., Yu, J., Yang, Y., Yao, J., & Yu, Y. (2025) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.70376 · Cited by 4
Jhanji, M., Bhan, A., Arrowood, C. A., Yakout, D. W., Shroff, A., McManus, D., Gifford, H., Vacharasin, J. M., Lizarraga, S. B., Nazarko, T. Y., et al. (2025) · IUBMB Life · doi:10.1002/iub.70030 · Cited by 4
Seizures and Epilepsy in Dementia: Diagnosis and Management
Ritter, L. M., & Nilsson, C. (2021) · Springer eBooks · doi:10.1007/978-3-030-77904-7_12 · Cited by 4
Buchholz, S., Bell, M. J., Haag, N., & Zempel, H. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3629-9_29 · Cited by 4
Tubulin glutamylation is key to axon guidance via selective tuning of microtubule-severing enzymesPreprint
Martín, D. T., Jardin, N., Vougny, J., Giudicelli, F., Gasmi, L., Henriot, V., Lebrun, L., Haumaître, C., Kneussel, M., Nicol, X., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.01.20.477127 · Cited by 4
Breuer, H., Bell-Simons, M., & Zempel, H. (2024) · Open Life Sciences · doi:10.1515/biol-2022-1010 · Cited by 3
Molecular Pathways in Alzheimer’s Disease and Cognitive Function
Chen, X., Reichert, M. C., & Gan, L. (2016) · Elsevier eBooks · doi:10.1016/b978-0-12-802851-3.00005-x · Cited by 3
Cut Your Losses: Spastin Mediates Branch-Specific Axon Loss
Meltzer, H., & Schuldiner, O. (2016) · Neuron · doi:10.1016/j.neuron.2016.11.004 · Cited by 3
Galeotti, A. A., Santucci, L., Klimek, J., Kabbani, M. A. A., Zempel, H., & Raffa, V. (2025) · Frontiers in Medicine · doi:10.3389/fmed.2025.1519628 · Cited by 2
Bell‐Simons, M., Breuer, H., Wunderlich, L., Chmes, H., Adam, D., Klimek, J., Buchholz, S., & Zempel, H. (2025) · Aging Cell · doi:10.1111/acel.70215 · Cited by 2
Randomized, double-blind study of zervimesine in mild to moderate Alzheimer's disease
Vijverberg, E. G. B., Scharre, D. W., Woodward, M., Catalano, S., Hamby, M. E., Grundman, M., Morgan, R. E., Iaci, J., Devins, T., & Caggiano, A. O. (2026) · Journal of Alzheimer’s Disease · doi:10.1177/13872877261437145 · Cited by 2
The aggregation of amyloid-β: from condensation, nucleation, and conformation to targeting therapy
Chen, B., Chen, T., Sun, Z., Liu, L., Jia, Y., Ji, Y., Wang, J., Sun, F., & Huang, Y. (2026) · Life Sciences · doi:10.1016/j.lfs.2026.124397 · Cited by 2
Tam, J. H. K., & Pasternak, S. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-801942-9.00004-5 · Cited by 2
Tau Pathology and Neurodegenerative Disorders
Takashima, A., Soeda, Y., Koike, R., & Maeda, S. (2022) · Springer eBooks · doi:10.1007/978-981-16-7977-3_22 · Cited by 2
Anand, 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
Neurodegenerative damage reduces firing coherence in a continuous attractor model of grid cells
Zhi, Y., & Cox, D. L. (2021) · Physical review. E · doi:10.1103/physreve.104.044414 · Cited by 1
Bell-Simons, M., Buchholz, S., Klimek, J., & Zempel, H. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.28.601286 · Cited by 3
Mechanisms of Intracellular Communication in Cancer and Pathogen Spreading
Valdebenito, S., Ajasin, D., Valerdi, K. M., Liu, Y. R., Rao, S., & Eugenín, E. A. (2024) · Results and problems in cell differentiation · doi:10.1007/978-3-031-62036-2_13 · Cited by 1
Vijayalakshmi, A., & Vengadasamy, P. (2026) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/0118715273448693251223103034 · Cited by 1
Flores-Melivilu, D., Carrazana, E., García, N., Alarcón, S., Caru-Ruiz, M., Chacón-Fuentes, M., Santos, N., Ahumada, M., Nova, E., Díaz‐Espinoza, R., et al. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05855-3 · Cited by 1
Tau and amyloid-β imaging with proteomics and genomics
Chinnathambi, S., Baisya, U., & Ananthanarayana, V. (2026) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2026.02.009 · Cited by 1
Francis, D., Paonessa, F., Hewitt, V. L., Southall, M., Peset, I., Whitworth, A. J., Livesey, F. J., Fabre, C. C. G., & Palacios, I. M. (2026) · Open Biology · doi:10.1098/rsob.250319 · Cited by 1
Traits and Trammels of Tau Tracer Imaging
Villemagne, V. L., Lopresti, B. J., Doré, V., Minhas, D. S., Gogola, A., Nadkarni, N. K., Mason, N. S., Bourgeat, P., López, O. L., Ikonomović, M. D., et al. (2023) · Springer eBooks · doi:10.1007/978-3-031-35098-6_6 · Cited by 1
Break and accelerator—The mechanics of Tau (and amyloid) toxicity
Cruz, E., Nisbet, R. M., & Götz, J. (2023) · Cytoskeleton · doi:10.1002/cm.21781 · Cited by 1
Investigating Tau pathology in an in vitro model for Alzheimer’s disease
Powrie, Y. S. L. (2016) · SUNScholar (Stellenbosch University) · Cited by 1
The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylationPreprint
Cummings, S. W., Li, Y., Spector, J. O., Kim, C., & Roll‐Mecak, A. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.31.587457 · Cited by 1
The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylationPreprint
Cummings, S. W., Li, Y., Spector, J. O., Kim, C., & Roll‐Mecak, A. (2024) · eLife · doi:10.7554/elife.98040 · Cited by 1
Knockdown of TTLL1 reduces Aβ-induced TAU pathology in human iPSC-derived cortical neuronsPreprint
Kabbani, M. A. A., Köhler, L., Wied, T., Adam, D., Klimek, J., & Zempel, H. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.11.19.624324 · Cited by 1
Pisa, R., Cupido, T., Steinman, J. B., Jones, N. H., & Kapoor, T. M. (2019) · SSRN Electronic Journal · doi:10.2139/ssrn.3372968
Effects of anle138b treatment on amyloid-β neurotoxicity
Thomas, C. (2020) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-8233
Melo‐Hanchuk, T. D. (2015) · doi:10.47749/t/unicamp.2015.947952
Post-Translational Tubulin Modifications in Differentiated Human Neural Stem CellsPreprint
Knight, V. B., Jogalekar, M. P., & Serrano, E. E. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.12.31.474563
Anand, A., Sharma, N., Gulati, M., & Khurana, N. (2020) · IGI Global eBooks · doi:10.4018/978-1-7998-3441-0.ch001
Alzheimer’s disease as a syndrome of overloaded amyloidic synaptic tagging in memory networksPreprint
Murphy, N. (2021) · OSF Preprints (OSF Preprints) · doi:10.31219/osf.io/7gsaz
Kaniyappan, S., Balaji, V., Wang, Y., & Mandelkow�, E. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-2597-2_9
Buchholz, S., Bell, M. J., Haag, N., & Zempel, H. (2022) · Research Square · doi:10.21203/rs.3.pex-2085/v1
An update to: Tracking TAU in neurons: How to transfect and track exogenous TAU in primary neuronsPreprint
Buchholz, S., Bell, M. J., & Zempel, H. (2023) · Research Square · doi:10.21203/rs.3.pex-2145/v1
Davies, D., Arthur, A. T., Aitken, H., Crossett, B., & Goldsbury, C. S. (2024) · Biology Open · doi:10.1242/bio.060067
Tracking Tau in Neurons: How to Transfect and Track Exogenous Tau in Primary Neurons
Buchholz, S., Bell, M. J., & Zempel, H. (2024) · Methods in molecular biology · doi:10.1007/978-1-0716-3629-9_28
Essential conserved neuronal motors kinesin-1 and kinesin-3 regulate Aβ42 toxicity in vivoPreprint
Francis, D., Paonessa, F., Fabre, C. C. G., Hewitt, V. L., Giannakou, M. E., Peset, I., Whitworth, A. J., Livesey, F. J., & Palacios, I. M. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.04.23.590704
The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylationPreprint
Cummings, S. W., Li, Y., Spector, J. O., Kim, C., & Roll‐Mecak, A. (2024) · eLife · doi:10.7554/elife.98040.1
Yadav, R., Mani, R. J., Kumar, A. H. S., Ahmad, S., & Katare, D. P. (2024) · Biomedical & Pharmacology Journal · doi:10.13005/bpj/2990 · Cited by 1
Chang, X., Zhuang, X., Feng, J., Yu, Y., & Yu, Y. (2025) · Experimental Brain Research · doi:10.1007/s00221-025-07017-8
Li, S., & Bhalla, R. (2025) · Medicinal Chemistry Research · doi:10.1007/s00044-025-03448-8
Hoshino, A., Castle, B. T., Shetty, M., Khan, H., Meints, J. P., Pletniková, O., Lee, M. K., Troncoso, J. C., Odde, D. J., & Bazzaro, M. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.08.26.671351
The TTLL10 polyglycylase is stimulated by tubulin glutamylation and inhibited by polyglycylationPreprint
Cummings, S. W., Li, Y., Spector, J. O., Kim, C., & Roll‐Mecak, A. (2025) · eLife · doi:10.7554/elife.98040.2
Amyloid β hypothesis in the development of therapeutic agents for Alzheimer's disease
Adeniji, A. O., Johnson, C., & Mody, V. V. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-30008-0.00020-x
TTLL6-mediated Polyglutamylation of PurA Maintains Colonic Crypt IntegrityPreprint
Pires, V., Pangault, C., Paul, C., Finetti, P., Bertucci, F., Mamessier, É., Jardin, C., Numnoi, N., Cicalini, I., Pieragostino, D., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.15.694360
Lathuilière, A., Jo, Y., Perbet, R., Donahue, C., Commins, C., Quittot, N., Fan, Z., Bennett, R. E., & Hyman, B. T. (2023) · Figshare · doi:10.6084/m9.figshare.23908793
Rôle de la polyglutamylation des microtubules dans le système nerveux de Drosophile
Devambez, I. (2014) · theses.fr (ABES) · doi:10.70675/694cb4c9z7551z4442zb054z40981eb0ad05
Etude de l'implication des microtubules dans le trafic intracellulaire
Fourrière, L. (2016) · theses.fr (ABES) · doi:10.70675/1d94d1cdze6b7z41ccz80baz3c7fa8e55e69
Microtubule affinity-regulating kinases in neurodegenerative disorders
Shahwan, M. J., Anwar, S., Alrouji, M., AlOmeir, O., Dinislam, K., & Shamsi, A. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-44173-8.00014-0
Mechanobiology of hippocampal neurogenesis: directing neural stem cell fate through physical cues
Akyel, I., Moeendarbary, E., & Sheridan, G. K. (2026) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2026.1868741 · Cited by 1
Kabbani, M. A. A., Köhler, L., Wied, T., Adam, D., Klimek, J., & Zempel, H. (2026) · Pharmaceutics · doi:10.3390/pharmaceutics18081038 · Cited by 1
Li, K., & Sun, S. (2026) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2026.109100
Peng, X., Li, X., Duan, S., Shi, J., & Cen, J. (2026) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2026.109107
Jajin, E. A., & Zempel, H. (2026) · Research Square · doi:10.21203/rs.3.rs-11112521/v1
BindingDB (2023) · UC San Diego · doi:10.7270/q24q7zxf
Investigation of BACE1 as a stress-induced regulator of neuronal metabolism
Findlay, J. A. (2014) · Discovery Research Portal (University of Dundee)
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