Cited by 230Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.

Human secreted tau increases amyloid-beta production

Open access

Bright, Jessica, Hussain, Sami, Dang, Vu, Wright, Sarah, Cooper, Bonnie, Byun, Tony, Ramos, Carla, Singh, Andrew, Parry, Graham, Stagliano, Nancy, Griswold-Prenner, Irene·2015·Neurobiology of Aging

DOI 10.1016/j.neurobiolaging.2014.09.007

Open this paper in CoChat — free account Open PDF

Abstract

The interaction of amyloid-beta (Aβ) and tau in the pathogenesis of Alzheimer's disease is a subject of intense inquiry, with the bulk of evidence indicating that changes in tau are downstream of Aβ. It has been shown however, that human tau overexpression in amyloid precursor protein transgenic mice increases Aβ plaque deposition. Here, we confirm that human tau increases Aβ levels. To determine if the observed changes in Aβ levels were because of intracellular or extracellular secreted tau (eTau for extracellular tau), we affinity purified secreted tau from Alzheimer's disease patient-derived cortical neuron conditioned media and analyzed it by liquid chromatography-mass spectrometry. We found the extracellular species to be composed predominantly of a series of N-terminal fragments of tau, with no evidence of C-terminal tau fragments. We characterized a subset of high affinity tau antibodies, each capable of engaging and neutralizing eTau. We found that neutralizing eTau reduces Aβ levels in vitro in primary human cortical neurons where exogenously adding eTau increases Aβ levels. In vivo, neutralizing human tau in 2 human tau transgenic models also reduced Aβ levels. We show that the human tau insert sequence is sufficient to cause the observed increase in Aβ levels. Our data furthermore suggest that neuronal hyperactivity may be the mechanism by which this regulation occurs. We show that neuronal hyperactivity regulates both eTau secretion and Aβ production. Electrophysiological analysis shows for the first time that secreted eTau causes neuronal hyperactivity. Its induction of hyperactivity may be the mechanism by which eTau regulates Aβ production. Together with previous findings, these data posit a novel connection between tau and Aβ, suggesting a dynamic mechanism of positive feed forward regulation. Aβ drives the disease pathway through tau, with eTau further increasing Aβ levels, perpetuating a destructive cycle.

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

Crossref · 10.1016/j.neurobiolaging.2014.09.007

Cites

41 of 41 references verified0 citation errors · 0 not checkable

Statistics

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?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Induction of Pluripotent Stem Cells from Adult Human Fibroblasts by Defined Factors
Takahashi, K., Tanabe, K., Ohnuki, M., Narita, M., Ichisaka, T., Tomoda, K., & Yamanaka, S. (2007) · Cell · doi:10.1016/j.cell.2007.11.019 · Cited by 20,221
The Amyloid Hypothesis of Alzheimer’s Disease: Progress and Problems on the Road to Therapeutics
Hardy, J., & Selkoe, D. J. (2002) · Science · doi:10.1126/science.1072994 · Cited by 13,864
Alzheimer's disease: the amyloid cascade hypothesis
Hardy, J. A., & Higgins, G. A. (1992) · Science · doi:10.1126/science.1566067 · Cited by 7,484
Highly efficient neural conversion of human ES and iPS cells by dual inhibition of SMAD signaling
Chambers, S. M., Fasano, C. A., Papapetrou, E. P., Tomishima, M., Sadelain, M., & Studer, L. (2009) · Nature Biotechnology · doi:10.1038/nbt.1529 · Cited by 3,620
Staging of alzheimer's disease-related neurofibrillary changes
Braak, H., & Braak, E. (1995) · Neurobiology of Aging · doi:10.1016/0197-4580(95)00021-6 · Cited by 2,357
Induced Pluripotent Stem Cells Generated from Patients with ALS Can Be Differentiated into Motor Neurons
Dimos, J. T., Rodolfa, K. T., Niakan, K. K., Weisenthal, L. M., Mitsumoto, H., Chung, W. K., Croft, G. F., Saphier, G., Leibel, R. L., Goland, R., et al. (2008) · Science · doi:10.1126/science.1158799 · Cited by 2,019
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
APP Processing and Synaptic Function
Kamenetz, F., Tomita, T., Hsieh, H., Seabrook, G., Borchelt, D., Iwatsubo, T., Sisodia, S., & Malinow, R. (2003) · Neuron · doi:10.1016/s0896-6273(03)00124-7 · Cited by 1,644
Enhanced neurofibrillary degeneration in transgenic mice expressing mutant tau and APP
Lewis, J., Dickson, D. W., Lin, W.-L., Chisholm, L., Corral, A., Jones, G., Yen, S.-H., Sahara, N., Skipper, L., Yager, D., et al. (2001) · Science · doi:10.1126/science.1058189 · Cited by 1,611

Flagged first, then by citations

Show all 41 references

Sorted by citations

Items 101–200 of 230

The application of in vitro ‐derived human neurons in neurodegenerative disease modeling
D’Souza, G. X., Rose, S. E., Knupp, A., Nicholson, D. A., Keene, C. D., & Young, J. E. (2020) · Journal of Neuroscience Research · doi:10.1002/jnr.24615 · Cited by 36
Internalization of tau antibody and pathological tau protein detected with a flow cytometry multiplexing approach
Shamir, D. B., Rosenqvist, N., Rasool, S., Pedersen, J. T., & Sigurdsson, E. M. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.01.013 · Cited by 34
Integrated generation of induced pluripotent stem cells in a low-cost device
Lin, H., Li, Q., Du, Q., Wang, O., Wang, Z., Akert, L., Carlson, M. A., Zhang, C., Subramanian, A., Zhang, C., et al. (2018) · Biomaterials · doi:10.1016/j.biomaterials.2018.10.027 · Cited by 35
Reciprocal Predictive Relationships between Amyloid and Tau Biomarkers in Alzheimer's Disease Progression: An Empirical Model
Krance, S. H., Cogo‐Moreira, H., Rabin, J. S., Black, S. E., & Swardfager, W. (2019) · Journal of Neuroscience · doi:10.1523/jneurosci.1056-19.2019 · Cited by 36
Progressive Supranuclear Palsy and Corticobasal Degeneration
Coughlin, D. G., Dickson, D. W., Josephs, K. A., & Litvan, I. (2021) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-51140-1_11 · Cited by 33
Spatiotemporal activation of the C/EBPβ/δ-secretase axis regulates the pathogenesis of Alzheimer’s disease
Wang, H., Liu, X., Chen, S., & Ye, K. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1815915115 · Cited by 32
MultiTEP platform-based DNA epitope vaccine targeting N-terminus of tau induces strong immune responses and reduces tau pathology in THY-Tau22 mice
Davtyan, H., Chen, W. W., Zagorski, K., Davis, J., Petrushina, I., Kazarian, K., Cribbs, D. H., Agadjanyan, M. G., Blurton-Jones, M., & Ghochikyan, A. (2017) · Vaccine · doi:10.1016/j.vaccine.2017.03.020 · Cited by 30
Complicated Role of Post-translational Modification and Protease-Cleaved Fragments of Tau in Alzheimer’s Disease and Other Tauopathies
Yang, J., Shen, N., Shen, J., Yang, Y., & Li, H.-L. (2023) · Molecular Neurobiology · doi:10.1007/s12035-023-03867-x · Cited by 32
Induced Pluripotent Stem Cells
Fakoya, A. O. J., Omole, A. E., Satyadev, N., & Haider, K. H. (2022) · Springer eBooks · doi:10.1007/978-981-16-6016-0_40-1 · Cited by 29
Selective targeting of 3 repeat Tau with brain penetrating single chain antibodies for the treatment of neurodegenerative disorders
Spencer, B. J., Brüschweiler, S., Sealey‐Cardona, M., Rockenstein, E. M., Adame, A., Florio, J. B., Mante, M., Trinh, I., Rissman, R. A., Konrat, R., et al. (2018) · Acta Neuropathologica · doi:10.1007/s00401-018-1869-0 · Cited by 30
A framework for translating tauopathy therapeutics: Drug discovery to clinical trials
Feldman, H., Cummings, J. L., Boxer, A. L., Staffaroni, A. M., Knopman, D. S., Rizzo, S. J. S., Territo, P. R., Arnold, S. E., Ballard, C. G., Beher, D., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.14250 · Cited by 27
A Theoretical Analysis of the Synergy of Amyloid and Tau in Alzheimer’s Disease
Han, P., & Shi, J. (2016) · Journal of Alzheimer s Disease · doi:10.3233/jad-151206 · Cited by 29
Tau in the brain interstitial fluid is fragmented and seeding–competent
Barini, E., Plotzky, G., Mordashova, Y., Hoppe, J., Rodriguez-Correa, E., Julier, S., Prieult, F. L., Mairhofer, I., Mezler, M., Biesinger, S., et al. (2021) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2021.09.013 · Cited by 28
Promising therapies for the treatment of frontotemporal dementia clinical phenotypes: from symptomatic to disease-modifying drugs
Logroscino, G., Imbimbo, B. P., Lozupone, M., Sardone, R., Capozzo, R., Battista, P., Zecca, C., Dibello, V., Giannelli, G., Bellomo, A., et al. (2019) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2019.1598377 · Cited by 30
Monoclonal antibody Y01 prevents tauopathy progression induced by lysine 280–acetylated tau in cell and mouse models
Song, H.-L., Kim, N.-Y., Park, J., Kim, M. I., Jeon, Y.-N., Lee, S.-J., Cho, K., Shim, Y.-L., Lee, K.-H., Mun, Y.-S., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci156537 · Cited by 26
Emerging Developments in Targeting Proteotoxicity in Neurodegenerative Diseases
McAlary, L., Plotkin, S. S., & Cashman, N. R. (2019) · CNS Drugs · doi:10.1007/s40263-019-00657-9 · Cited by 26
Lumboperitoneal Shunts for the Treatment of Idiopathic Normal Pressure Hydrocephalus: A Comparison of Small-Lumen Abdominal Catheters to Gravitational Add-On Valves in a Single Center
Nakajima, M., Miyajima, M., Akiba, C., Ogino, I., Kawamura, K., Sugano, H., Hara, T., Tange, Y., Fusegi, K., Karagiozov, K. L., et al. (2018) · Operative Neurosurgery · doi:10.1093/ons/opy044 · Cited by 27
Challenges and opportunities for novel combination therapies in Alzheimer's disease: a report from the EU/US CTAD Task Force
Angioni, D., Middleton, L. T., Bateman, R. J., Aisen, P. S. S., Boxer, A. L., Sha, S. J., Zhou, J., Gerlach, I., Raman, R., Fillit, H. M., et al. (2025) · The Journal of Prevention of Alzheimer s Disease · doi:10.1016/j.tjpad.2025.100163 · Cited by 27
“Tau immunotherapy: Hopes and hindrances”
Shahpasand, K., Shamloo, A. S., Nabavi, S. M., Lu, K. P., & Zhou, X. Z. (2017) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2017.1393594 · Cited by 25
Recent advances in tau-directed immunotherapy against Alzheimer’s disease: an overview of pre-clinical and clinical development
Ng, P. Y., Chang, I. S., Koh, R. Y., & Chye, S. M. (2020) · Metabolic Brain Disease · doi:10.1007/s11011-020-00591-6 · Cited by 25
PBPK-PD modeling for the preclinical development and clinical translation of tau antibodies for Alzheimer’s disease
Bloomingdale, P., Yadav, D. B., Sugam, J. A., Grauer, S. M., Smith, B. E., Antonenko, S. V., Judo, M., Azadi, G., & Yee, K. L. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.867457 · Cited by 25
Nanotechnology for tau pathology in Alzheimer's disease
Ma, R., Mu, Q., Xi, Y., Liu, G., & Liu, C. (2024) · Materials Today Bio · doi:10.1016/j.mtbio.2024.101145 · Cited by 23
Dangerous Liaisons: Tau Interaction with Muscarinic Receptors
Wysocka, A., Pałasz, E., Steczkowska, M., & Niewiadomska, G. (2020) · Current Alzheimer Research · doi:10.2174/1567205017666200424134311 · Cited by 24
A common antigenic motif recognized by naturally occurring human VH5–51/VL4–1 anti-tau antibodies with distinct functionalities
Apetri, A. C., Crespo, R., Juraszek, J., Pascual, G., Janson, R., Zhu, X., Zhang, H., Keogh, E. A., Holland, T., Wadia, J., et al. (2018) · Acta Neuropathologica Communications · doi:10.1186/s40478-018-0543-z · Cited by 22
Clearance of intracellular tau protein from neuronal cells via VAMP8-induced secretion
Pilliod, J., Desjardins, A., Pernègre, C., Jamann, H., Larochelle, C., Fon, E. A., & Leclerc, N. M. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013553 · Cited by 25
Clinical development of passive tau-based immunotherapeutics for treating primary and secondary tauopathies
Panza, F., Dibello, V., Sardone, R., Castellana, F., Zupo, R., Lampignano, L., Bortone, I., Stallone, R., Cirillo, N., Damiani, C., et al. (2023) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2023.2233892 · Cited by 22
Targeting Tau to Treat Clinical Features of Huntington's Disease
Masnata, M., Salem, S., Jacquet, A. D. R., Anwer, M., & Cicchetti, F. (2020) · Frontiers in Neurology · doi:10.3389/fneur.2020.580732 · Cited by 25
Open Science Meets Stem Cells: A New Drug Discovery Approach for Neurodegenerative Disorders
Han, C., Chaineau, M., Chen, C. X. ‐., Beitel, L. K., & Durcan, T. M. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00047 · Cited by 22
Preclinical, phase I, and phase II investigational clinical trials for treatment of progressive supranuclear palsy
Shoeibi, A., Olfati, N., & Litvan, I. (2018) · Expert Opinion on Investigational Drugs · doi:10.1080/13543784.2018.1460356 · Cited by 23
Tau Secretion
Ruan, Z., & Ikezu, T. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_11 · Cited by 23
Anti-Phospho-Tau Gene Therapy for Chronic Traumatic Encephalopathy
Sacramento, C. B., Sondhi, D., Rosenberg, J. B., Chen, A., Giordano, S., Pey, E. P., Lee, V., Stiles, K. M., Havlicek, D. F., Leopold, P. L., et al. (2019) · Human Gene Therapy · doi:10.1089/hum.2019.174 · Cited by 22
Gut Microbiota and Immunotherapy for Alzheimer’s Disease
Dai, C., Liu, F., Iqbal, K., & Gong, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232315230 · Cited by 22
Disease-modifying therapies for tauopathies: agents in the pipeline
Panza, F., Imbimbo, B. P., Lozupone, M., Greco, A., Seripa, D., Logroscino, G., Daniele, A., & Colosimo, C. (2019) · Expert Review of Neurotherapeutics · doi:10.1080/14737175.2019.1606715 · Cited by 20
Human Induced Pluripotent Stem Cell Models of Neurodegenerative Disorders for Studying the Biomedical Implications of Autophagy
Seranova, E., Palhegyi, A. M., Verma, S., Dimova, S., Lasry, R., Naama, M., Sun, C., Barrett, T. G., Rosenstock, T. R., Kumar, D., et al. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.01.024 · Cited by 20
Discovery and Functional Characterization of hPT3, a Humanized Anti-Phospho Tau Selective Monoclonal Antibody
Kolen, K. V., Malia, T., Theunis, C., Nanjunda, R. K., Teplyakov, A., Ernst, R., Wu, S., Luo, J., Borgers, M., Vandermeeren, M., et al. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200544 · Cited by 21
Targets, trials and tribulations in Alzheimer therapeutics
Gharat, R., Dixit, G., Khambete, M., & Prabhu, A. (2023) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2023.176230 · Cited by 18
AD-Related N-Terminal Truncated Tau Is Sufficient to Recapitulate In Vivo the Early Perturbations of Human Neuropathology: Implications for Immunotherapy
Borreca, A., Latina, V., Corsetti, V., Middei, S., Piccinin, S., Valle, F. D., Bussani, R., Ammassari‐Teule, M., Nisticò, R., Calissano, P., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0974-3 · Cited by 18
Vitamin E therapy prevents the accumulation of congophilic amyloid plaques and neurofibrillary tangles in the hippocampus in a rat model of Alzheimer's disease.
Jahanshahi, M., Nikmahzar, E., & Sayyahi, A. (2020) · PubMed · doi:10.22038/ijbms.2019.38165.9067 · Cited by 19
Dementia Therapy Targeting Tau
Buée, L. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-32-9358-8_30 · Cited by 18
Secretion of full-length Tau or Tau fragments in cell culture models. Propagation of Tau in vivo and in vitro
Pérez, M., Medina, M., Hernández, F., & Ávila, J. (2018) · BioMolecular Concepts · doi:10.1515/bmc-2018-0001 · Cited by 20
Passive tau-based immunotherapy for tauopathies
Panza, F., Solfrizzi, V., Daniele, A., & Lozupone, M. (2023) · Handbook of clinical neurology · doi:10.1016/b978-0-323-98817-9.00029-6 · Cited by 18
Novel avenues of tau research
Sexton, C. E., Bitan, G., Bowles, K. R., Bryś, M., Buée, L., Maina, M. B., Clelland, C. D., Cohen, A. D., Crary, J. F., Dage, J. L., et al. (2024) · Alzheimer s & Dementia · doi:10.1002/alz.13533 · Cited by 16
Bringing Induced Pluripotent Stem Cell Technology to the Bedside
Karagiannis, P., Nakauchi, A., & Yamanaka, S. (2018) · JMA Journal · doi:10.31662/jmaj.2018-0005 · Cited by 18
Untangling Tau: Molecular Insights into Neuroinflammation, Pathophysiology, and Emerging Immunotherapies
Davidson, R., Krider, R. I., Borsellino, P., Noorda, K., Alhwayek, G., & Vida, T. A. (2023) · Current Issues in Molecular Biology · doi:10.3390/cimb45110553 · Cited by 17
Evolution of Alzheimer's disease research from a health-tech perspective: Insights from text mining
Martinelli, D. D. (2022) · International Journal of Information Management Data Insights · doi:10.1016/j.jjimei.2022.100089 · Cited by 16
Extracellular Tau Oligomers Damage the Axon Initial Segment
Best, M. N., Lim, Y., Ferenc, N. N., Kim, N., Min, L. Y., Wang, D. B., Sharifi, K., Wasserman, A. E., McTavish, S. A., Siller, K. H., et al. (2023) · Journal of Alzheimer s Disease · doi:10.3233/jad-221284 · Cited by 15
Distinct regulation of Tau Monomer and aggregate uptake and intracellular accumulation in human neurons
Marvian, A. T., Strauß, T., Tang, Q., Tuck, B. J., Keeling, S., Rüdiger, D., Dizaji, N. M., Mohammad‐Beigi, H., Nuscher, B., Chakraborty, P., et al. (2024) · Molecular Neurodegeneration · doi:10.1186/s13024-024-00786-w · Cited by 16
Disease-modifying strategies in primary tauopathies
Rösler, T. W., Costa, M., & Höglinger, G. U. (2019) · Neuropharmacology · doi:10.1016/j.neuropharm.2019.107842 · Cited by 16
Dopamine, sleep, and neuronal excitability modulate amyloid-β–mediated forgetting in Drosophila
Kaldun, J. C., Lone, S. R., Camps, A. M. H., Fritsch, C., Widmer, Y. F., Stein, J. V., Tomchik, S. M., & Sprecher, S. G. (2021) · PLoS Biology · doi:10.1371/journal.pbio.3001412 · Cited by 16
Therapeutic Targets for Alzheimer's Disease: Amyloid Vs. Non-Amyloid. Where Does Consensus Lie Today? An CTAD Task Force Report
Gauthier, S. G., Boxer, A. L., Knopman, D. S., Sims, J., Doody, R. S., Aisen, P., Iwatsubo, T., Bateman, R. J., & Vellas, B. J. (2022) · The Journal of Prevention of Alzheimer s Disease · doi:10.14283/jpad.2022.29 · Cited by 14
Immunogenicity of MultiTEP platform technology-based Tau vaccine in non-human primates
Hovakimyan, A., Zagorski, K., Chailyan, G., Antonyan, T., Melikyan, L., Petrushina, I., Batt, D. G., King, O., Ghazaryan, M., Donthi, A., et al. (2022) · npj Vaccines · doi:10.1038/s41541-022-00544-3 · Cited by 14
In Vivo Microdialysis of Brain Interstitial Fluid for the Determination of Extracellular Tau Levels
Yamada, K. (2016) · Methods in molecular biology · doi:10.1007/978-1-4939-6598-4_17 · Cited by 13
Immunotherapy in progressive supranuclear palsy
Vaswani, P. A., & Olsen, A. L. (2020) · Current Opinion in Neurology · doi:10.1097/wco.0000000000000836 · Cited by 13
Tanycytic degeneration impairs tau clearance and contributes to Alzheimer’s disease pathology
Sauvé, F., Gomez-Martínez, R., Mbouamboua, Y., Ternier, G., Nampoothiri, S. S., Dupré, E., Garcia, L., Couralet, M., Dewisme, J., Lebouvier, T., et al. (2026) · Cell Press Blue · doi:10.1016/j.cpblue.2026.100003 · Cited by 15
Glial phagocytosis for synapse and toxic proteins in neurodegenerative diseases
Choi, Y., & Chung, W. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00870-9 · Cited by 14
Requirements for Using iPSC-Based Cell Models for Assay Development in Drug Discovery
Christensen, K., Roudnicky, F., Patsch, C., & Burcin, M. M. (2017) · Advances in biochemical engineering, biotechnology · doi:10.1007/10_2017_23 · Cited by 13
The Fate of Tau Aggregates Between Clearance and Transmission
Seitkazina, A., Kim, K. H., Fagan, E., Sung, Y., Kim, Y. K., & Lim, S. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.932541 · Cited by 10
Tau immunotherapy in Alzheimer’s disease and progressive supranuclear palsy
Karimi, N., Catak, F. B., Arslan, E. O., Saghazadeh, A., & Rezaei, N. (2022) · International Immunopharmacology · doi:10.1016/j.intimp.2022.109445 · Cited by 11
Application of induced pluripotent stem cells to primary immunodeficiency diseases
Karagiannis, P., Yamanaka, S., & Saito, M. K. (2019) · Experimental Hematology · doi:10.1016/j.exphem.2019.01.005 · Cited by 11
Towards a Mechanistic Model of Tau-Mediated Pathology in Tauopathies: What Can We Learn from Cell-Based In Vitro Assays?
Sala‐Jarque, J., Zimkowska, K., Ávila, J., Ferrer, I., & del Río, J. A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms231911527 · Cited by 11
Mechanistic Approach to Immunity and Immunotherapy of Alzheimer’s Disease: A Review
Islam, M. R., Rabbi, M. A., Hossain, T., Sultana, S., & Uddin, S. (2024) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.4c00360 · Cited by 10
Discovery of dual-specificity tyrosine-phosphorylation-regulated kinase 1A (DYRK1A) inhibitors using an artificial intelligence model and their effects on tau and tubulin dynamics
Chen, J. J., Tu, H., Lin, T. E., Peng, Z., Wu, Y., Yen, S., Sung, T.-Y., Hsieh, J., Lee, H., Pan, S., et al. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117688 · Cited by 9
Effective connectivity in individuals with Alzheimer's disease and mild cognitive impairment: A systematic review
Kazemi-Harikandei, S.-Z., Shobeiri, P., Jelodar, M.-R. S., & Tavangar, S. M. (2022) · Neuroscience Informatics · doi:10.1016/j.neuri.2022.100104 · Cited by 9
Early Chronic Stress Induced Changes within the Locus Coeruleus in Sporadic Alzheimer’s Disease
Minné, D., Marnewick, J. L., & Engel-Hills, P. C. (2023) · Current Alzheimer Research · doi:10.2174/1567205020666230811092956 · Cited by 10
Patient-derived iPSCs, a reliable in vitro model for the investigation of Alzheimer’s disease
Asiamah, E. A., Guo, R., Kong, D., Feng, B., He, J., Zhang, W., Liu, X., Du, X., Ma, Z., Liu, B., et al. (2021) · Reviews in the Neurosciences · doi:10.1515/revneuro-2020-0065 · Cited by 9
Tau-based therapies for Alzheimer’s disease: Promising novel neuroprotective approaches
Sayas, C. L. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814037-6.00005-7 · Cited by 9
Drug Design Progress of in Silico, in Vitro and in Vivo Researches
Bai, Q., Li, L., Liu, S., Xiao, S., & Guo, Y. (2018) · Cited by 8
Manipulating cell fate while confronting reproducibility concerns
Osterloh, J. M., & Mullane, K. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.01.016 · Cited by 7
β-Amyloid Accumulation Slows Earlier than Expected in Preclinical Alzheimer's Disease Patients
Camara, H., & De‐Souza, E. A. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.1592-18.2018 · Cited by 7
Intravenous Injection of PHF-Tau Proteins From Alzheimer Brain Exacerbates Neuroinflammation, Amyloid Beta, and Tau Pathologies in 5XFAD Transgenic Mice
Houben, S., de Fisenne, M.-A., Ando, K., Dries, V. V., Poncelet, L., Yilmaz, Z., Mansour, S., Decker, R. D., Brion, J., & Leroy, K. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.00106 · Cited by 9
Lower CSF amyloid-beta1–42 predicts a higher mortality rate in frontotemporal dementia
Vieira, D., Durães, J., Baldeiras, I., Santiago, B., Duro, D., Lima, M., Leitão, M. J., Tábuas-Pereira, M., & Santana, I. (2019) · Diagnostics · doi:10.3390/diagnostics9040162 · Cited by 6
Behavioral, metabolic, and lipidomic characterization of the 5xFADxTg30 mouse model of Alzheimer’s disease
Marshall, J. P. S., Huynh, K., Lancaster, G. I., Ng, J., Collins, J. M., Pernes, G., Liang, A., Featherby, T. J., Mellet, N. A., Drew, B. G., et al. (2024) · iScience · doi:10.1016/j.isci.2024.108800 · Cited by 8
Interactions of Polyphenolic Gallotannins with Amyloidogenic Polypeptides Associated with Alzheimer’s Disease: From Molecular Insights to Physiological Significance
Khalifa, J., Bourgault, S., & Gaudreault, R. (2023) · Current Alzheimer Research · doi:10.2174/0115672050277001231213073043 · Cited by 6
Emerging drugs for progressive supranuclear palsy
Giagkou, N., & Stamelou, M. (2019) · Expert Opinion on Emerging Drugs · doi:10.1080/14728214.2019.1609450 · Cited by 6
Does the Anti‐Tau Strategy in Progressive Supranuclear Palsy Need to Be Reconsidered? No
Höglinger, G. U. (2021) · Movement Disorders Clinical Practice · doi:10.1002/mdc3.13326 · Cited by 6
Sustaining Brain Youth by Neural Stem Cells: Physiological and Therapeutic Perspectives
dos Santos, M. A., Moreira, J. A. F., Santos, S. S., & Solá, S. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04774-z · Cited by 7
Neurobiochemical, Peptidomic, and Bioinformatic Approaches to Characterize Tauopathy Peptidome Biomarker Candidates in Experimental Mouse Model of Traumatic Brain Injury
Yadikar, H., Johnson, C., Pafundi, N., Nguyen, L. T., Kurup, M., Torres, I., Al-Enezy, A., Yang, Z., Yost, R. A., Kobeissy, F. H., et al. (2023) · Molecular Neurobiology · doi:10.1007/s12035-022-03165-y · Cited by 5
Tau and its interactions with other proteins in neurodegenerative diseases
Mroczek, K. H., Annesley, S. J., & Fisher, P. R. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-815950-7.00028-x · Cited by 5
Targeted tau protein degradation: a promising therapeutic approach for tauopathies
Baazaoui, N., Alfaifi, M. Y., Shati, A. A., Saad, R. B., & Garzoli, S. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.11.041 · Cited by 5
The Role of T Cells in Alzheimer's Disease Pathogenesis
Zhao, J., Wang, X., He, Y., Xu, P., Lai, L., Chung, Y., & Pan, X. (2023) · Critical Reviews in Immunology · doi:10.1615/critrevimmunol.2023050145 · Cited by 4
Tau-Targeted Immunotherapy for Alzheimer's Disease: Insight into Clinical Trials
Kadmiri, N. E. (2024) · OBM Neurobiology · doi:10.21926/obm.neurobiol.2403238 · Cited by 4
Passive Immunotherapy in Alzheimer’s Disease
Dolan, P. J., & Zago, W. M. (2018) · InTech eBooks · doi:10.5772/intechopen.76299 · Cited by 4
Unconventional secretion of tau by VAMP8 impacts its intra- and extracellular cleavage
Pilliod, J., Gélinas-Faucher, M., & Leclerc, N. M. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.912118 · Cited by 4
PET Amyloid and Tau Status Are Differently Affected by Patient Features
Tan, M., Initiative, A. D. N., Yang, Y., Wang, H.-F., Xu, W., Tan, C., Zuo, C., Dong, Q., Tan, L., & Yu, J. (2020) · Journal of Alzheimer s Disease · doi:10.3233/jad-200124 · Cited by 4
Potential Use of Stem Cells in Mood Disorders
Colpo, G. D., Stertz, L., Diniz, B. S., & Teixeira, A. L. (2018) · Advances in experimental medicine and biology · doi:10.1007/5584_2018_250 · Cited by 4
A multiscale model to explain the spatiotemporal progression of amyloid beta and tau pathology in Alzheimer's disease
Xu, C., Xu, E., Xiao, Y., Yang, D., Guorong Wu, A., & Chen, M. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142887 · Cited by 3
Acute targeting of N-terminal tau protein has long-lasting beneficial effects in Tg2576 APP/Aβ mouse model by reducing cognitive impairment, cerebral Aβ-amyloidosis, synaptic remodeling and microgliosis later in life
Latina, V., Introna, M. D., Malerba, F., Florio, R., Balzamino, B. O., Natale, G. D., Sciacca, M. F. M., Pappalardo, G., Micera, A., Pignataro, A., et al. (2025) · Acta Neuropathologica Communications · doi:10.1186/s40478-025-02022-y · Cited by 3
A luminescence-based reporter to study tau secretion reveals overlapping mechanisms for the release of healthy and pathological tau
Lopez, D. M., Maltby, C. J., Warming, H., Divecha, N., Vargas‐Caballero, M., Coldwell, M. J., & Deinhardt, K. (2023) · Frontiers in Neuroscience · doi:10.3389/fnins.2023.1196007 · Cited by 4
Induced pluripotent stem cell technology: venturing into the second decade
Shi, Y., Inoue, H., Takahashi, J. B., & Yamanaka, S. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-818422-6.00095-2 · Cited by 4
Tau Immunotherapy
Sigurdsson, E. M. (2016) · Methods in pharmacology and toxicology · doi:10.1007/978-1-4939-3560-4_8 · Cited by 3
Association between CSF Aβ42 and amyloid negativity in patients with different stage mild cognitive impairment
He, B., Wang, L., Xu, B., & Zhang, Y. (2021) · Neuroscience Letters · doi:10.1016/j.neulet.2021.135765 · Cited by 3
Immunotherapeutics for AD: A Work in Progress
Sharma, A., Anand, J. S., & Kumar, Y. (2021) · CNS & Neurological Disorders - Drug Targets · doi:10.2174/1871527320666210903101522 · Cited by 3
Amyloid and tau pathologies cross-talk to promote Alzheimeŕs disease: novel mechanistic insights
Ávila, J., Hernández, F., & Perry, G. L. (2025) · Neuroscience · doi:10.1016/j.neuroscience.2025.07.025 · Cited by 3
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
Frontotemporal lobar degeneration
Kim, B., Viera-Ortiz, A., Phan, J. M., Irwin, D. J., & Lee, E. B. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-85654-6.00041-1 · Cited by 3
New approaches to antibacterial drug discovery
Turan, N. B. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-818480-6.00008-4 · Cited by 2
Why delay in effective treatment for Alzheimer's disease and related conditions
Iqbal, K., Liu, F., Gong, C., Dai, C., & Hu, W. H. (2019) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2019.08.002 · Cited by 1
Human in vitro disease models to aid pathway and target discovery for neurological disorders
Muralidharan, B. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-821972-0.00013-7 · Cited by 1
Antibodies against Alzheimer's: Pioneering a New Era in Treatment Strategies
Verma, M., Singh, N. K., & Siddique, M. U. M. (2025) · Current Bioactive Compounds · doi:10.2174/0115734072347198241226113039 · Cited by 1
Synaptotoxic effects of extracellular tau are mediated by its microtubule-binding region
Ondrejčák, T., Hu, N., Coode, E., Campbell, T., Corbett, G. T., Doykov, I., Mills, K. A., Walsh, D. M., Livesey, F. J., Rowan, M. J., et al. (2025) · Acta Neuropathologica · doi:10.1007/s00401-025-02897-0 · Cited by 1

Authors: Bright, J., Hussain, S., Dang, V., Wright, S., Cooper, B., Byun, T., Ramos, C., Singh, A., Parry, G., Stagliano, N., & Griswold-Prenner, I.
Corresponding author: Stagliano, Nancy
ORCID: Wright, Sarah
Parry, Graham
Venue: Neurobiology of Aging
Publisher: Elsevier BV
Published: 2015-02
Volume: 36
Issue: 2
Pages: 693-709
ISSN: 0197-4580 (ISSN-L)
DOI: 10.1016/j.neurobiolaging.2014.09.007
OpenAlex: W2044321001
Cited by: 230
References: 41
Citations by year: 2026: 5 · 2025: 13 · 2024: 11 · 2023: 17 · 2022: 16 · 2021: 26 · 2020: 31 · 2019: 30 · 2018: 43 · 2017: 12 · 2016: 17 · 2015: 9
FWCI: 8.42
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by-nc-nd
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by-nc-nd/3.0/ (vor)
Locations: Neurobiology of Aging (publishedVersion, cc-by-nc-nd)
PubMed (publishedVersion)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: amyloid-beta production, Alzheimer's disease, neuronal hyperactivity, cortical neurons, amyloid precursor protein transgenic mice, positive feedback loop
MeSH terms: Alzheimer Disease, Animals, Cells, Cultured, Cerebral Cortex, Chromatography, Liquid, Humans, Mice, Transgenic, Neurons, Mass Spectrometry, Amyloid beta-Peptides, tau Proteins

About these checks

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

Statistics and arithmetic are recomputed, not judged.

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

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

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

Human secreted tau increases amyloid-beta production

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks