Cited by 226Alzheimer's disease research and treatmentsAutophagy in Disease and TherapyNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.

Rapamycin attenuates the progression of tau pathology in P301S tau transgenic mice.

Open access

Ozcelik, Sefika, Fraser, Graham, Castets, Perrine, Schaeffer, Véronique, Skachokova, Zhiva, Breu, Karin, Clavaguera, Florence, Sinnreich, Michael, Kappos, Ludwig, Goedert, Michel, Tolnay, Markus, Winkler, David Theo·2013·PLoS ONE

DOI 10.1371/journal.pone.0062459PMC PMC3646815

Open this paper in CoChat — free account Open PDF

Abstract

Altered autophagy contributes to the pathogenesis of Alzheimer's disease and other tauopathies, for which curative treatment options are still lacking. We have recently shown that trehalose reduces tau pathology in a tauopathy mouse model by stimulation of autophagy. Here, we studied the effect of the autophagy inducing drug rapamycin on the progression of tau pathology in P301S mutant tau transgenic mice. Rapamycin treatment resulted in a significant reduction in cortical tau tangles, less tau hyperphosphorylation, and lowered levels of insoluble tau in the forebrain. The favourable effect of rapamycin on tau pathology was paralleled by a qualitative reduction in astrogliosis. These effects were visible with early preventive or late treatment. We further noted an accumulation of the autophagy associated proteins p62 and LC3 in aged tangle bearing P301S mice that was lowered upon rapamycin treatment. Thus, rapamycin treatment defers the progression of tau pathology in a tauopathy animal model and autophagy stimulation may constitute a therapeutic approach for patients suffering from tauopathies.

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 · 10.1371/journal.pone.0062459

Cites

38 of 38 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.

Repertoires of Autophagy in the Pathogenesis of Ocular Diseases
Li, Y., Jiang, Q. L., Cao, G.-F., Yao, J., & Yan, B. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000373980 · Cited by 16,351
Autophagy fights disease through cellular self-digestion
Mizushima, N., Levine, B., Cuervo, A. M., & Klionsky, D. J. (2008) · Nature · doi:10.1038/nature06639 · Cited by 6,452
Unbiased stereological estimation of the total number of neurons in the subdivisions of the rat hippocampus using the optical fractionator
West, M. J., Slomianka, L., & Gundersen, H. J. G. (1991) · The Anatomical Record · doi:10.1002/ar.1092310411 · Cited by 2,994
Multiple isoforms of human microtubule-associated protein tau: sequences and localization in neurofibrillary tangles of Alzheimer's disease
Goedert, M., Spillantini, M. G., Jakes, R., Rutherford, D., & Crowther, R. A. (1989) · Neuron · doi:10.1016/0896-6273(89)90210-9 · Cited by 2,492
Self-citation
Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease
Ravikumar, B., Vacher, C., Berger, Z., Davies, J. E., Luo, S., Oroz, L. G., Scaravilli, F., Easton, D. F., Duden, R., O'Kane, C. J., et al. (2004) · Nature Genetics · doi:10.1038/ng1362 · Cited by 2,347
Synapse Loss and Microglial Activation Precede Tangles in a P301S Tauopathy Mouse Model
Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S.-M., Iwata, N., Saido, T. C., Maeda, J., Suhara, T., Trojanowski, J. Q., & Lee, V. M.-Y. (2007) · Neuron · doi:10.1016/j.neuron.2007.01.010 · Cited by 2,208
A Century of Alzheimer's Disease
Goedert, M., & Spillantini, M. G. (2006) · Science · doi:10.1126/science.1132814 · Cited by 2,150
Self-citation
The roles of intracellular protein-degradation pathways in neurodegeneration
Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625
Autophagy Induction and Autophagosome Clearance in Neurons: Relationship to Autophagic Pathology in Alzheimer's Disease
Boland, B., Kumar, A., Lee, S., Platt, F. M., Wegiel, J., Yu, W. H., & Nixon, R. A. (2008) · Journal of Neuroscience · doi:10.1523/jneurosci.0800-08.2008 · Cited by 1,119
Alzheimer's disease: strategies for disease modification
Citron, M. (2010) · Nature Reviews Drug Discovery · doi:10.1038/nrd2896 · Cited by 1,075

Flagged first, then by citations

Show all 38 references

Sorted by citations

Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
Autophagy and Neurodegeneration: Pathogenic Mechanisms and Therapeutic Opportunities
Menzies, F. M., Fleming, A., Caricasole, A., Bento, C. F., Andrews, S. P., Ashkenazi, A., Füllgrabe, J., Jackson, A., Jimenez Sanchez, M., Karabiyik, C., et al. (2017) · Neuron · doi:10.1016/j.neuron.2017.01.022 · Cited by 1,134
The mechanistic target of rapamycin: the grand conducTOR of metabolism and aging
Kennedy, B. K., & Lamming, D. W. (2016) · Cell Metabolism · doi:10.1016/j.cmet.2016.05.009 · Cited by 544
The quest to slow ageing through drug discovery
Partridge, L., Fuentealba, M., & Kennedy, B. K. (2020) · Nature Reviews Drug Discovery · doi:10.1038/s41573-020-0067-7 · Cited by 468
The Autophagy–Lysosomal Pathway in Neurodegeneration: A TFEB Perspective
Martini-Stoica, H., Xu, Y., Ballabio, A., & Zheng, H. (2016) · Trends in Neurosciences · doi:10.1016/j.tins.2016.02.002 · Cited by 436
Transcription factor NFE2L2/NRF2 is a regulator of macroautophagy genes
Pajares, M., Jiménez-Moreno, N., García-Yagüe, Á. J., Escoll, M., de Ceballos, M. L., Van Leuven, F., Rábano, A., Yamamoto, M., Rojo, A. I., & Cuadrado, A. (2016) · Autophagy · doi:10.1080/15548627.2016.1208889 · Cited by 392
Autophagy in Alzheimer’s disease pathogenesis: Therapeutic potential and future perspectives
Zhang, Z., Yang, X., Song, Y., & Tu, J. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101464 · Cited by 386
Regulation of autophagy by mTOR-dependent and mTOR-independent pathways: autophagy dysfunction in neurodegenerative diseases and therapeutic application of autophagy enhancers
Sarkar, S. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130134 · Cited by 379
Autophagy as an essential cellular antioxidant pathway in neurodegenerative disease
Giordano, S. S., Darley-Usmar, V. M., & Zhang, J. (2013) · Redox Biology · doi:10.1016/j.redox.2013.12.013 · Cited by 372
Selective clearance of aberrant tau proteins and rescue of neurotoxicity by transcription factor EB
Polito, V. A., Li, H., Martini‐Stoica, H., Wang, B., Li, Y., Xu, Y., Swartzlander, D. B., Palmieri, M., di Ronza, A., Lee, V. M. ‐., et al. (2014) · EMBO Molecular Medicine · doi:10.15252/emmm.201303671 · Cited by 351
Effect of rapamycin on aging and age-related diseases—past and future
Selvarani, R., Mohammed, S., & Richardson, A. (2021) · GeroScience · doi:10.1007/s11357-020-00274-1 · Cited by 290
Tau-based therapies in neurodegeneration: opportunities and challenges
Li, C., & Götz, J. (2017) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2017.155 · Cited by 272
Autophagic and lysosomal defects in human tauopathies: analysis of post-mortem brain from patients with familial Alzheimer disease, corticobasal degeneration and progressive supranuclear palsy
Piras, A., Collin, L., Grüninger, F., Graff, C., & Rönnbäck, A. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0292-9 · Cited by 271
Alzheimer's disease and type 2 diabetes: a critical assessment of the shared pathological traits
Chatterjee, S., & Mudher, A. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00383 · Cited by 270
Rapamycin: An InhibiTOR of Aging Emerges From the Soil of Easter Island
Apelo, S. I. A., & Lamming, D. W. (2016) · The Journals of Gerontology Series A · doi:10.1093/gerona/glw090 · Cited by 241
Autophagy Induction as a Therapeutic Strategy for Neurodegenerative Diseases
Djajadikerta, A., Keshri, S., Tanasa, M. P., Prestil, R., Ryan, L., & Rubinsztein, D. C. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.035 · Cited by 243
Insulin Resistance and Diabetes Mellitus in Alzheimer’s Disease
Burillo, J., Marqués, P., Jiménez, B., González-Blanco, C., Benito, M., & Guillén, C. (2021) · Cells · doi:10.3390/cells10051236 · Cited by 242
miR-132/212 deficiency impairs tau metabolism and promotes pathological aggregation in vivo
Smith, P. Y., Hernandez-Rapp, J., Jolivette, F., Lecours, C., Bisht, K., Goupil, C., Dorval, V., Parsi, S., Morin, F., Planel, E., et al. (2015) · Human Molecular Genetics · doi:10.1093/hmg/ddv377 · Cited by 220
A Brief Overview of Tauopathy: Causes, Consequences, and Therapeutic Strategies
Orr, M. E., Sullivan, A. C., & Frost, B. E. (2017) · Trends in Pharmacological Sciences · doi:10.1016/j.tips.2017.03.011 · Cited by 242
Lysosome dysfunction as a cause of neurodegenerative diseases: Lessons from frontotemporal dementia and amyotrophic lateral sclerosis
Root, J. T., Merino, P., Nuckols, A., Johnson, M. A., & Kukar, T. L. (2021) · Neurobiology of Disease · doi:10.1016/j.nbd.2021.105360 · Cited by 240
Role of mitochondrial dysfunction, oxidative stress and autophagy in progression of Alzheimer's disease
Bhatia, V., & Sharma, S. (2020) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2020.117253 · Cited by 228
Tau in neurodegenerative disease
Gao, Y.-L., Wang, N., Sun, F.-R., Cao, X.-P., Zhang, W., & Yu, J.-T. (2018) · Annals of Translational Medicine · doi:10.21037/atm.2018.04.23 · Cited by 222
Four-repeat tauopathies
Rösler, T. W., Marvian, A. T., Brendel, M., Nykänen, N.-P., Höllerhage, M., Schwarz, S. C., Hopfner, F., Koeglsperger, T., Respondek, G., Schweyer, K., et al. (2019) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2019.101644 · Cited by 230
Impairment of the autophagy–lysosomal pathway in Alzheimer's diseases: Pathogenic mechanisms and therapeutic potential
Zhang, W., Xu, C., Sun, J., Shen, H., Wang, J., & Yang, C. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2022.01.008 · Cited by 219
The Ambiguous Relationship of Oxidative Stress, Tau Hyperphosphorylation, and Autophagy Dysfunction in Alzheimer’s Disease
Liu, Z., Li, T., Li, P., Wei, N., Zhao, Z., Liang, H., Ji, X., Chen, W., Xue, M., & Wei, J. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2015/352723 · Cited by 217
A novel rapamycin analog is highly selective for mTORC1 in vivo
Schreiber, K. H., Arriola Apelo, S. I., Yu, D., Brinkman, J. A., Velarde, M. C., Syed, F. A., Liao, C.-Y., Baar, E. L., Carbajal, K. A., Sherman, D. S., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-11174-0 · Cited by 177
Association Between Autophagy and Neurodegenerative Diseases
Fujikake, N., Shin, M., & Shimizu, S. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00255 · Cited by 197
Rapamycin and Alzheimer’s disease: Time for a clinical trial?
Kaeberlein, M. R., & Galván, V. (2019) · Science Translational Medicine · doi:10.1126/scitranslmed.aar4289 · Cited by 171
Autophagy in the presynaptic compartment in health and disease
Vijayan, V., & Verstreken, P. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201611113 · Cited by 170
Calorie restriction mimetics: Can you have your cake and eat it, too?
Ingram, D. K., & Roth, G. S. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.11.005 · Cited by 164
Prolonged tau clearance and stress vulnerability rescue by pharmacological activation of autophagy in tauopathy neurons
Silva, M. C., Nandi, G. A., Tentarelli, S., Gurrell, I. K., Jamier, T., Lucente, D., Dickerson, B. C., Brown, D. G., Brandon, N. J., & Haggarty, S. J. (2020) · Nature Communications · doi:10.1038/s41467-020-16984-1 · Cited by 157
Neurodegenerative Disease Tauopathies
Creekmore, B. C., Watanabe, R., & Lee, E. B. (2023) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-051222-120750 · Cited by 146
Endo-lysosomal dysfunction: a converging mechanism in neurodegenerative diseases
Wang, C., Telpoukhovskaia, M. A., Bahr, B. A., Chen, X., & Gan, L. (2017) · Current Opinion in Neurobiology · doi:10.1016/j.conb.2017.09.005 · Cited by 144
Autophagic dysfunction in Alzheimer’s disease: Cellular and molecular mechanistic approaches to halt Alzheimer’s pathogenesis
Uddin, M. S., Mamun, A. A., Labu, Z. K., Hidalgo‐Lanussa, O., Barreto, G. E., & Ashraf, G. M. (2018) · Journal of Cellular Physiology · doi:10.1002/jcp.27588 · Cited by 141
A toolbox for the longitudinal assessment of healthspan in aging mice
Bellantuono, I., de Cabo, R., Ehninger, D., Di Germanio, C., Lawrie, A., Miller, J., Mitchell, S. J., Navas-Enamorado, I., Potter, P. K., Tchkonia, T., et al. (2020) · Nature Protocols · doi:10.1038/s41596-019-0256-1 · Cited by 145
Intermittent Administration of Rapamycin Extends the Life Span of Female C57BL/6J Mice
Apelo, S. I. A., Pumper, C. P., Baar, E. L., Richardson, N. E., & Lamming, D. W. (2016) · The Journals of Gerontology Series A · doi:10.1093/gerona/glw064 · Cited by 136
Probing the correlation of neuronal loss, neurofibrillary tangles, and cell death markers across the Alzheimer's disease Braak stages: a quantitative study in humans
Theofilas, P., Ehrenberg, A. J., Nguy, A. K., Thackrey, J. M., Dunlop, S. R., Mejia, M. B., Alho, A. T. D. L., Leite, R. E. P., Rodriguez, R. D., Suemoto, C. K., et al. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.09.007 · Cited by 134
Metformin promotes tau aggregation and exacerbates abnormal behavior in a mouse model of tauopathy
Barini, E., Antico, O., Zhao, Y., Asta, F., Tucci, V., Catelani, T., Marotta, R., Xu, H., & Gasparini, L. (2016) · Molecular Neurodegeneration · doi:10.1186/s13024-016-0082-7 · Cited by 126
Cholesterol impairs autophagy-mediated clearance of amyloid beta while promoting its secretion
Barbero-Camps, E., Roca-Agujetas, V., Bartolessis, I., de Dios, C., Fernández-Checa, J. C., Marí, M., Morales, A., Hartmann, T., & Colell, A. (2018) · Autophagy · doi:10.1080/15548627.2018.1438807 · Cited by 125
Rifampicin is a candidate preventive medicine against amyloid-β and tau oligomers
Umeda, T., Ono, K., Sakai, A., Yamashita, M., Mizuguchi, M., Klein, W. L., Yamada, M., Mori, H., & Tomiyama, T. (2016) · Brain · doi:10.1093/brain/aww042 · Cited by 124
The mTOR Inhibitor Rapamycin Mitigates Perforant Pathway Neurodegeneration and Synapse Loss in a Mouse Model of Early-Stage Alzheimer-Type Tauopathy
Siman, R., Cocca, R., & Dong, Y. (2015) · PLoS ONE · doi:10.1371/journal.pone.0142340 · Cited by 122
Development of disease-modifying drugs for frontotemporal dementia spectrum disorders
Panza, F., Lozupone, M., Seripa, D., Daniele, A., Watling, M., Giannelli, G., & Imbimbo, B. P. (2020) · Nature Reviews Neurology · doi:10.1038/s41582-020-0330-x · Cited by 122
Defective lysosomal acidification: a new prognostic marker and therapeutic target for neurodegenerative diseases
Lo, C. H., & Zeng, J. (2023) · Translational Neurodegeneration · doi:10.1186/s40035-023-00362-0 · Cited by 117
Autophagy and Tau Protein
Hamano, T., Enomoto, S., Shirafuji, N., Ikawa, M., Yamamura, O., Yen, S.-H. C., & Nakamoto, Y. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22147475 · Cited by 122
Promoting tau secretion and propagation by hyperactive p300/CBP via autophagy-lysosomal pathway in tauopathy
Chen, X., Li, Y., Wang, C., Tang, Y., Mok, S.-A., Tsai, R. M., Rojas, J. C., Karydas, A., Miller, B. L., Boxer, A. L., et al. (2020) · Molecular Neurodegeneration · doi:10.1186/s13024-019-0354-0 · Cited by 107
Therapeutic strategies for the treatment of tauopathies: Hopes and challenges
Khanna, M. R., Kovalevich, J., Lee, V. M. ‐., Trojanowski, J. Q., & Brunden, K. R. (2016) · Alzheimer s & Dementia · doi:10.1016/j.jalz.2016.06.006 · Cited by 116
Repeated ultrasound treatment of tau transgenic mice clears neuronal tau by autophagy and improves behavioral functions
Pandit, R., Leinenga, G., & Götz, J. (2019) · Theranostics · doi:10.7150/thno.34388 · Cited by 114
Galectin-8–mediated selective autophagy protects against seeded tau aggregation
Falcon, B., Noad, J., McMahon, H. T., Randow, F., & Goedert, M. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.m117.809293 · Cited by 119
Self-citation
mTOR-Related Brain Dysfunctions in Neuropsychiatric Disorders
Ryskalin, L., Limanaqi, F., Frati, A., Busceti, C. L., & Fornai, F. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082226 · Cited by 110
Long-term treadmill exercise attenuates tau pathology in P301S tau transgenic mice
Ohia-Nwoko, O., Montazari, S., Lau, Y., & Eriksen, J. L. (2014) · Molecular Neurodegeneration · doi:10.1186/1750-1326-9-54 · Cited by 108
Human iPSC-derived neuronal model of Tau-A152T frontotemporal dementia reveals tau-mediated mechanisms of neuronal vulnerability
Silva, M. C., Cheng, C., Mair, W., Almeida, S., Fong, H., Biswas, M. H. U., Zhang, Z., Huang, Y., Temple, S., Coppola, G., et al. (2016) · Stem Cell Reports · doi:10.1016/j.stemcr.2016.08.001 · Cited by 103
mTOR signaling and Alzheimer's disease: What we know and where we are?
Davoody, S., Asgari Taei, A., Khodabakhsh, P., & Dargahi, L. (2024) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.14463 · Cited by 96
Therapeutic implication of autophagy in neurodegenerative diseases
Rahman, M. A., & Rhim, H. (2017) · BMB Reports · doi:10.5483/bmbrep.2017.50.7.069 · Cited by 100
Small molecule therapeutics for tauopathy in Alzheimer’s disease: Walking on the path of most resistance
Wang, L., Bharti, Kumar, R., Pavlov, P. F., & Winblad, B. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112915 · Cited by 92
Enhancing autophagy in Alzheimer's disease through drug repositioning
Eshraghi, M., Ahmadi, M., Afshar, S., Lorzadeh, S., Adlimoghaddam, A., Rezvani Jalal, N., West, R., Dastghaib, S., Igder, S., Torshizi, S. R. N., et al. (2022) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2022.108171 · Cited by 89
Autophagy stimulation as a promising approach in treatment of neurodegenerative diseases
Pierzynowska, K., Gaffke, L., Cyske, Z., Puchalski, M., Rintz, E., Bartkowski, M., Osiadły, M., Pierzynowski, M., Mantej, J., Piotrowska, E., et al. (2018) · Metabolic Brain Disease · doi:10.1007/s11011-018-0214-6 · Cited by 93
Tauopathies: Deciphering Disease Mechanisms to Develop Effective Therapies
Silva, M. C., & Haggarty, S. J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238948 · Cited by 87
Using Human iPSC-Derived Neurons to Model TAU Aggregation
Verheyen, A., Diels, A., Dijkmans, J., Oyelami, T., Meneghello, G., Mertens, L., Versweyveld, S., Borgers, M., Buist, A., Peeters, P., et al. (2015) · PLOS ONE · doi:10.1371/journal.pone.0146127 · Cited by 86
Pharmacogenomics of Alzheimer’s Disease: Novel Therapeutic Strategies for Drug Development
Cacabelos, R., Cacabelos, P., Torrellas, C., Tellado, I., & Carril, J. C. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-0956-8_13 · Cited by 86
Autophagy in axonal degeneration in glaucomatous optic neuropathy
Munemasa, Y., & Kitaoka, Y. (2015) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2015.03.002 · Cited by 82
Angiotensin-(1-7) is Reduced and Inversely Correlates with Tau Hyperphosphorylation in Animal Models of Alzheimer’s Disease
Jiang, T., Zhang, Y., Zhou, J., Zhu, X., Tian, Y., Zhao, H.-D., Lu, H., Gao, Q., Tan, L., & Yu, J. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9260-9 · Cited by 79
Molecular Mechanisms of Lithium Action: Switching the Light on Multiple Targets for Dementia Using Animal Models
Kerr, F., Bjedov, I., & Sofola-Adesakin, O. (2018) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2018.00297 · Cited by 80
AMPK activation does not enhance autophagy in neurons in contrast to MTORC1 inhibition: different impact on β-amyloid clearance
Benito‐Cuesta, I., Ordóñez‐Gutiérrez, L., & Wandosell, F. G. (2020) · Autophagy · doi:10.1080/15548627.2020.1728095 · Cited by 80
TFEB Overexpression in the P301S Model of Tauopathy Mitigates Increased PHF1 Levels and Lipofuscin Puncta and Rescues Memory Deficits
Wang, H., Wang, R., Carrera, I., Xu, S., & Lakshmana, M. K. (2016) · eNeuro · doi:10.1523/eneuro.0042-16.2016 · Cited by 76
Autophagy in Astrocytes and its Implications in Neurodegeneration
Sung, K., & Jiménez-Sánchez, M. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.12.041 · Cited by 76
Crosstalk between the mTOR and Nrf2/ARE signaling pathways as a target in the improvement of long-term potentiation
Gureev, A. P., Popov, V. N., & Starkov, A. A. (2020) · Experimental Neurology · doi:10.1016/j.expneurol.2020.113285 · Cited by 75
A critical appraisal of tau‐targeting therapies for primary and secondary tauopathies
Imbimbo, B. P., Ippati, S., Watling, M., & Balducci, C. (2021) · Alzheimer s & Dementia · doi:10.1002/alz.12453 · Cited by 75
Neuroinflammatory Gene Regulation, Mitochondrial Function, Oxidative Stress, and Brain Lipid Modifications With Disease Progression in Tau P301S Transgenic Mice as a Model of Frontotemporal Lobar Degeneration-Tau
López‐González, I., Aso, E., Carmona, M., Armand‐Ugón, M., Blanco, R., Naudí, A., Cabré, R., Portero‐Otín, M., Pamplona, R., & Ferrer, I. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000241 · Cited by 71
Rapamycin Ester Analog CCI-779/Temsirolimus Alleviates Tau Pathology and Improves Motor Deficit in Mutant Tau Transgenic Mice
Frédérick, C., Ando, K., Leroy, K., Héraud, C., Suain, V., Buée, L., & Brion, J. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142097 · Cited by 69
The cargo receptor SQSTM1 ameliorates neurofibrillary tangle pathology and spreading through selective targeting of pathological MAPT (microtubule associated protein tau)
Xu, Y., Zhang, S., & Zheng, H. (2018) · Autophagy · doi:10.1080/15548627.2018.1532258 · Cited by 69
Linking pathways in the developing and aging brain with neurodegeneration
Kovács, G. G., Adle‐Biassette, H., Milenković, I., Cipriani, S., van Scheppingen, J., & Aronica, E. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.03.045 · Cited by 69
Alzheimer's Disease: From Mitochondrial Perturbations to Mitochondrial Medicine
Cardoso, S., Carvalho, C., Correia, S. C., Seiça, R. M. F., & Moreira, P. I. (2016) · Brain Pathology · doi:10.1111/bpa.12402 · Cited by 69
Translational geroscience: A new paradigm for 21st century medicine
Kaeberlein, M. R. (2017) · Translational Medicine of Aging · doi:10.1016/j.tma.2017.09.004 · Cited by 69
The Emerging Roles of Autophagy in Human Diseases
Lei, Y., & Klionsky, D. J. (2021) · Biomedicines · doi:10.3390/biomedicines9111651 · Cited by 66
Pharmacological Inhibition of O-GlcNAcase Enhances Autophagy in Brain through an mTOR-Independent Pathway
Zhu, Y., Shan, X., Safarpour, F., Go, N. E., Li, N., Shan, A., Huang, M. C., Deen, M. C., Holicek, V., Ashmus, R. A., et al. (2018) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.8b00015 · Cited by 66
mTOR signaling as a molecular target for the alleviation of Alzheimer's disease pathogenesis
Rapaka, D., Bitra, V. R., Challa, S. R., & Adiukwu, P. C. (2022) · Neurochemistry International · doi:10.1016/j.neuint.2022.105311 · Cited by 65
TFEB in Alzheimer's disease: From molecular mechanisms to therapeutic implications
Gu, Z., Cao, H., Zuo, C., Huang, Y., Miao, J., Song, Y., Yang, Y., Zhu, L., & Wang, F. (2022) · Neurobiology of Disease · doi:10.1016/j.nbd.2022.105855 · Cited by 66
Alzheimer's Disease-Related Misfolded Proteins and Dysfunctional Organelles on Autophagy Menu
Correia, S. C., Resende, R., Moreira, P. I., & Pereira, C. (2015) · DNA and Cell Biology · doi:10.1089/dna.2014.2757 · Cited by 66
Exploring the multifunctional role of melatonin in regulating autophagy and sleep to mitigate Alzheimer’s disease neuropathology
Hossain, M. F., Wang, N., Chen, R., Li, S., Roy, J., Uddin, M. G., Li, Z., Lim, L. W., & Song, Y. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101304 · Cited by 62
Rab7A regulates tau secretion
Rodríguez, L. C. D. L. C., Mohamed, N., Desjardins, A., Lippé, R., Fon, E. A., & Leclerc, N. M. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13994 · Cited by 66
Pharmacological modulation of autophagy for Alzheimer's disease therapy: Opportunities and obstacles
Deng, Z., Dong, Y., Zhou, X., Lu, J.-H., & Yue, Z. (2022) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.12.009 · Cited by 58
Behind the curtain of tauopathy: a show of multiple players orchestrating tau toxicity
Huang, Y., Wu, Z., & Zhou, B. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-2042-8 · Cited by 58
Targeting Aggrephagy for the Treatment of Alzheimer’s Disease
Malampati, S., Song, J., Tong, B. C., Nalluri, A., Yang, C., Wang, Z., Sreenivasmurthy, S. G., Zhu, Z., Liu, J., Su, C.-F., et al. (2020) · Cells · doi:10.3390/cells9020311 · Cited by 60
mTOR Attenuation with Rapamycin Reverses Neurovascular Uncoupling and Memory Deficits in Mice Modeling Alzheimer's Disease
Skike, C. E. V., Hussong, S. A., Hernandez, S. F., Banh, A. Q., DeRosa, N., & Galván, V. (2021) · Journal of Neuroscience · doi:10.1523/jneurosci.2144-20.2021 · Cited by 60
The effects of caloric restriction and its mimetics in Alzheimer's disease through autophagy pathways
Yang, Y., & Zhang, L. (2020) · Food & Function · doi:10.1039/c9fo02611h · Cited by 57
Clinically Precedented Protein Kinases: Rationale for Their Use in Neurodegenerative Disease
Benn, C., & Dawson, L. A. (2020) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2020.00242 · Cited by 59
MEK1/2 inhibition rescues neurodegeneration by TFEB-mediated activation of autophagic lysosomal function in a model of Alzheimer’s Disease
Chun, Y. S., Kim, M., Lee, S., Kim, M. J., Hong, T.-J., Jeon, J. K., Ganbat, D., Kim, H. T., Kim, S. S., Kam, T., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01713-5 · Cited by 56
Role of Tau in Various Tauopathies, Treatment Approaches, and Emerging Role of Nanotechnology in Neurodegenerative Disorders
Kaur, P., Khera, A., Alajangi, H. K., Sharma, A., Jaiswal, P. K., Singh, G., & Barnwal, R. P. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-03164-z · Cited by 54
Chemical Screening Approaches Enabling Drug Discovery of Autophagy Modulators for Biomedical Applications in Human Diseases
Panda, P. K., Fahrner, A., Vats, S., Seranova, E., Sharma, V., Chipara, M., Desai, P., Torresi, J., Rosenstock, T., Kumar, D., et al. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00038 · Cited by 50
Robust LC3B lipidation analysis by precisely adjusting autophagic flux
Liebl, M. P., Meister, S. C., Frey, L., Hendrich, K., Klemmer, A., Wohlfart, B., Untucht, C., Nuber, J., Pohl, C., & Lakics, V. (2022) · Scientific Reports · doi:10.1038/s41598-021-03875-8 · Cited by 51
Hallmarks of neurodegenerative disease: A systems pharmacology perspective
Bloomingdale, P., Karelina, T., Ramakrishnan, V., Bakshi, S., Véronneau‐Veilleux, F., Moye, M., Sekiguchi, K., Meno‐Tetang, G. M. L., Mohan, A., Maithreye, R., et al. (2022) · CPT Pharmacometrics & Systems Pharmacology · doi:10.1002/psp4.12852 · Cited by 54
Rapamycin Attenuated Zinc-Induced Tau Phosphorylation and Oxidative Stress in Rats: Involvement of Dual mTOR/p70S6K and Nrf2/HO-1 Pathways
Lai, C., Chen, Z., Ding, Y., Qian, C., Su, S., Liu, H., Ni, R., & Tang, Z. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.782434 · Cited by 47
Prion degradation pathways: Potential for therapeutic intervention
Goold, R., McKinnon, C., & Tabrizi, S. J. (2015) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2014.12.009 · Cited by 51
Alzheimer's disease genes and autophagy
Yoon, S.-Y., & Kim, D.-H. (2016) · Brain Research · doi:10.1016/j.brainres.2016.03.018 · Cited by 42
Modulating autophagic flux via ROS-responsive targeted micelles to restore neuronal proteostasis in Alzheimer's disease
Xu, S., Yang, P., Qian, K., Li, Y., Guo, Q., Wang, P., Meng, R., Wu, J., Cao, J., Cheng, Y., et al. (2021) · Bioactive Materials · doi:10.1016/j.bioactmat.2021.09.017 · Cited by 48
Central role for p62/SQSTM1 in the elimination of toxic tau species in a mouse model of tauopathy
Ono, M., Komatsu, M., Ji, B., Takado, Y., Shimojo, M., Minamihisamatsu, T., Warabi, E., Yanagawa, T., Matsumoto, G., Aoki, I., et al. (2022) · Aging Cell · doi:10.1111/acel.13615 · Cited by 45
Tau as a potential therapeutic target for ischemic stroke
Chen, X., & Jiang, H. (2019) · Aging · doi:10.18632/aging.102547 · Cited by 45
Rapamycin and Alzheimer disease: a hypothesis for the effective use of rapamycin for treatment of neurodegenerative disease
Carosi, J. M., & Sargeant, T. J. (2023) · Autophagy · doi:10.1080/15548627.2023.2175569 · Cited by 41
Vascular mTOR-dependent mechanisms linking the control of aging to Alzheimer's disease
Galván, V., & Hart, M. J. (2015) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2015.11.010 · Cited by 41
Autophagic receptor p62 protects against glycation‐derived toxicity and enhances viability
Aragonès, G., Dasuri, K., Olukorede, O., Francisco, S. G., Renneburg, C., Kumsta, C., Hansen, M., Kageyama, S., Komatsu, M., Rowan, S., et al. (2020) · Aging Cell · doi:10.1111/acel.13257 · Cited by 41

Authors: Ozcelik, S., Fraser, G., Castets, P., Schaeffer, V., Skachokova, Z., Breu, K., Clavaguera, F., Sinnreich, M., Kappos, L., Goedert, M., Tolnay, M., & Winkler, D. T.
Affiliations: MRC Laboratory of Molecular Biology (GB)
University Hospital of Basel (CH)
Corresponding author: Winkler, David Theo
ORCID: Fraser, Graham
Castets, Perrine
Schaeffer, Véronique
Sinnreich, Michael
Kappos, Ludwig
Goedert, Michel
Tolnay, Markus
Winkler, David Theo
Venue: PLoS ONE
Publisher: Public Library of Science (PLoS)
Published: 2013-05-07
Volume: 8
Issue: 5
Pages: e62459
ISSN: 1932-6203 (ISSN-L)
DOI: 10.1371/journal.pone.0062459
PMC: PMC3646815
OpenAlex: W1989723790
Cited by: 226
References: 38
Citations by year: 2026: 7 · 2025: 16 · 2024: 9 · 2023: 15 · 2022: 27 · 2021: 26 · 2020: 31 · 2019: 17 · 2018: 17 · 2017: 17 · 2016: 18 · 2015: 17 · 2014: 7 · 2013: 2
FWCI: 10.42
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (unspecified)
Locations: PLoS ONE (publishedVersion, cc-by)
Europe PMC (PubMed Central) (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
Archive ouverte UNIGE (University of Geneva) (submittedVersion, cc-by)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Figshare (submittedVersion, cc-by)
Funders: National Science Foundation
University of Pennsylvania
Velux Stiftung
Parkinson's UK (K-1012)
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung (135214, 123812, 310030)
Topics: Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords: rapamycin, tau pathology, P301S tau transgenic mice, tauopathy, Alzheimer's disease, autophagy, tau hyperphosphorylation, tau tangles, astrocyte activation, p62, LC3, trehalose, neuroprotection
MeSH terms: Animals, Astrocytes, Humans, Mice, Transgenic, Phosphorylation, Solubility, Time Factors, tau Proteins, Disease Progression, Sirolimus, Tauopathies, Mice

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

Rapamycin attenuates the progression of tau pathology in P301S tau transgenic mice.

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