The DOI matches its Crossref record; 102 of the 102 references it cites were found in a registry or an index.
Degradation of tau protein by autophagy and proteasomal pathways
Abstract
Tau aggregates are present in several neurodegenerative diseases and correlate with the severity of memory deficit in AD (Alzheimer's disease). However, the triggers of tau aggregation and tau-induced neurodegeneration are still elusive. The impairment of protein-degradation systems might play a role in such processes, as these pathways normally keep tau levels at a low level which may prevent aggregation. Some proteases can process tau and thus contribute to tau aggregation by generating amyloidogenic fragments, but the complete clearance of tau mainly relies on the UPS (ubiquitin–proteasome system) and the ALS (autophagy–lysosome system). In the present paper, we focus on the regulation of the degradation of tau by the UPS and ALS and its relation to tau aggregation. We anticipate that stimulation of these two protein-degradation systems might be a potential therapeutic strategy for AD and other tauopathies.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
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?
In the citing paper
“As tau is a target of autophagy80, any deficiencies in processing could lead to increased levels of intracellular tau, including misfolded, damaged or aggregated protein.”
From Tau-targeting therapies for Alzheimer disease (2018) · cites this paper as [80]
Citations
Cites
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Loss of autophagy in the central nervous system causes neurodegeneration in mice
Komatsu, M., Waguri, S., Chiba, T., Murata, S., Iwata, J.-I., Tanida, I., Ueno, T., Koike, M., Uchiyama, Y., Kominami, E., et al. (2006) · Nature · doi:10.1038/nature04723 · Cited by 3,500
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
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
Tau-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
Decreased Clearance of CNS β-Amyloid in Alzheimer’s Disease
Mawuenyega, K. G., Sigurdson, W., Ovod, V., Munsell, L., Kasten, T., Morris, J. C., Yarasheski, K. E., & Bateman, R. J. (2010) · Science · doi:10.1126/science.1197623 · Cited by 2,078
Recognition of the polyubiquitin proteolytic signal
Thrower, J. S., Hoffman, L. M., Rechsteiner, M., & Pickart, C. M. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,769
The roles of intracellular protein-degradation pathways in neurodegeneration
Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625
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
Macroautophagy—a novel β-amyloid peptide-generating pathway activated in Alzheimer's disease
Yu, W. H., Cuervo, A. M., Kumar, A., Peterhoff, C. M., Schmidt, S. D., Lee, J.-H., Mohan, P. S., Mercken, M., Farmery, M. R., Tjernberg, L. O., et al. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200505082 · Cited by 967
Flagged first, then by citations
Cited by
Sorted by citations
Tau in physiology and pathology
Wang, Y., & Mandelkow, E. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2015.1 · Cited by 2,251
Self-citationTau-targeting therapies for Alzheimer disease
Congdon, E. E., & Sigurdsson, E. M. (2018) · Nature Reviews Neurology · doi:10.1038/s41582-018-0013-z · Cited by 1,113
Roles of tau protein in health and disease
Guo, T., Noble, W., & Hanger, D. P. (2017) · Acta Neuropathologica · doi:10.1007/s00401-017-1707-9 · Cited by 1,003
Critical role of acetylation in tau-mediated neurodegeneration and cognitive deficits
Min, S.-W., Chen, X., Tracy, T. E., Li, Y., Zhou, Y., Wang, C., Shirakawa, K., Minami, S. S., Defensor, E., Mok, S. A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3951 · Cited by 516
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
Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367
Salminen, A., Kaarniranta, K., Kauppinen, A., Ojala, J. O., Haapasalo, A., Soininen, H. S., & Hiltunen, M. O. (2013) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2013.06.002 · Cited by 371
Role of lysosomes in physiological activities, diseases, and therapy
Zhang, Z., Yue, P., Lu, T., Wang, Y., Wei, Y., & Wei, X. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01087-1 · Cited by 375
Self-citationTargeted degradation of aberrant tau in frontotemporal dementia patient-derived neuronal cell models
Silva, M. C., Ferguson, F. M., Cai, Q., Donovan, K. A., Nandi, G., Patnaik, D., Zhang, T., Huang, H.-T., Lucente, D. E., Dickerson, B. C., et al. (2019) · eLife · doi:10.7554/elife.45457 · Cited by 283
Phospholipase D Signaling Pathways and Phosphatidic Acid as Therapeutic Targets in Cancer
Bruntz, R. C., Lindsley, C. W., & Brown, H. A. (2014) · Pharmacological Reviews · doi:10.1124/pr.114.009217 · Cited by 286
Lost after translation: missorting of Tau protein and consequences for Alzheimer disease
Zempel, H., & Mandelkow�, E. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.08.004 · Cited by 284
Self-citationPiras, A., Collin, L., Grüninger, F., Graff, C., & Rönnbäck, A. (2016) · Acta Neuropathologica Communications · doi:10.1186/s40478-016-0292-9 · Cited by 271
Diabetes and Alzheimer’s disease crosstalk
Baglietto‐Vargas, D., Shi, J. J., Yaeger, D. M., Ager, R. R., & LaFerla, F. M. (2016) · Neuroscience & Biobehavioral Reviews · doi:10.1016/j.neubiorev.2016.03.005 · Cited by 263
Specific Knockdown of Endogenous Tau Protein by Peptide-Directed Ubiquitin-Proteasome Degradation
Chu, T.-T., Gao, N., Li, Q.-Q., Chen, P.-G., Yang, X.-F., Chen, Y.-X., Zhao, Y.-F., & Li, Y.-M. (2016) · Cell Chemical Biology · doi:10.1016/j.chembiol.2016.02.016 · Cited by 247
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 231
Bhatia, V., & Sharma, S. (2020) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2020.117253 · Cited by 228
Clearance of Amyloid Beta and Tau in Alzheimer’s Disease: from Mechanisms to Therapy
Xin, S.-H., Tan, L., Cao, X., Yu, J.-T., & Tan, L. (2018) · Neurotoxicity Research · doi:10.1007/s12640-018-9895-1 · Cited by 222
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
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 221
Tapia‐Rojas, C., Cabezas-Opazo, F., Deaton, C. A., Vergara, E. H., Johnson, G. V. W., & Quintanilla, R. A. (2018) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2018.12.005 · Cited by 207
The Autophagy Lysosomal Pathway and Neurodegeneration
Finkbeiner, S. (2020) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a033993 · Cited by 196
Limorenko, G., & Lashuel, H. A. (2021) · Chemical Society Reviews · doi:10.1039/d1cs00127b · Cited by 168
Targeting Autophagy for the Treatment of Alzheimer’s Disease: Challenges and Opportunities
Liu, J., & Li, L. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00203 · Cited by 162
Chiasseu, M., Alarcón-Martínez, L., Belforte, N., Quintero, H., Dotigny, F., Destroismaisons, L., Velde, C. V., Panayi, F., Louis, C., & Polo, A. D. (2017) · Molecular Neurodegeneration · doi:10.1186/s13024-017-0199-3 · Cited by 158
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
SIRT1 Deacetylates Tau and Reduces Pathogenic Tau Spread in a Mouse Model of Tauopathy
Min, S., Sohn, P., Li, Y., Devidze, N., Johnson, J. R., Krogan, N. J., Masliah, E., Mok, S., Gestwicki, J. E., & Gan, L. (2018) · Journal of Neuroscience · doi:10.1523/jneurosci.2369-17.2018 · Cited by 151
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
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
Acetylation: a new key to unlock tau’s role in neurodegeneration
Cook, C. N., Stankowski, J. N., Carlomagno, Y., Stetler, C. T., & Petrucelli, L. (2014) · Alzheimer s Research & Therapy · doi:10.1186/alzrt259 · Cited by 140
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
The Role of Tau Oligomers in the Onset of Alzheimer's Disease Neuropathology
Cárdenas-Aguayo, M. D. C., Gómez-Virgilio, L., DeRosa, S., & Meraz-Ríos, M. A. (2014) · ACS Chemical Neuroscience · doi:10.1021/cn500148z · Cited by 120
New perspectives on the role of tau in Alzheimer's disease. Implications for therapy
Medina, M., & Ávila, J. (2014) · Biochemical Pharmacology · doi:10.1016/j.bcp.2014.01.013 · Cited by 123
The ubiquitin proteasomal system: a potential target for the management of Alzheimer's disease
Gadhave, K., Bolshette, N. B., Ahire, A., Pardeshi, R., Thakur, K. K., Trandafir, C.-M., Istrate, A., Ahmed, S., Lahkar, M., Muresanu, D. F., et al. (2016) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12817 · Cited by 122
Microbiota modulation as preventative and therapeutic approach in Alzheimer’s disease
Bonfili, L., Cecarini, V., Gogoi, O., Gong, C., Cuccioloni, M., Angeletti, M., Rossi, G., & Eleuteri, A. M. (2020) · FEBS Journal · doi:10.1111/febs.15571 · Cited by 123
Jiang, S., & Bhaskar, K. (2020) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2020.586731 · Cited by 119
Tau Protein Squired by Molecular Chaperones During Alzheimer’s Disease
Gorantla, N. V., & Chinnathambi, S. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1174-3 · Cited by 113
Glucose metabolism and AD: evidence for a potential diabetes type 3
González, A., Calfío, C., Churruca, M., & Maccioni, R. B. (2022) · Alzheimer's Research & Therapy · doi:10.1186/s13195-022-00996-8 · Cited by 112
Song, X., Hu, J.-F., Chu, S., Zhang, Z., Xu, S., Yuan, Y., Han, N., Liu, Y., Niu, F., He, X., et al. (2013) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2013.03.051 · Cited by 107
Tau Accumulation, Altered Phosphorylation, and Missorting Promote Neurodegeneration in Glaucoma
Chiasseu, M., Vargas, J. L. C., Destroismaisons, L., Velde, C. V., Leclerc, N. M., & Polo, A. D. (2016) · Journal of Neuroscience · doi:10.1523/jneurosci.3986-15.2016 · Cited by 105
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
The role of ubiquitin proteasomal system and autophagy-lysosome pathway in Alzheimer’s disease
Zhang, Y., Chen, X., Zhao, Y., Ponnusamy, M., & Liu, Y. (2017) · Reviews in the Neurosciences · doi:10.1515/revneuro-2017-0013 · Cited by 99
Kumar, S., Tepper, K., Kaniyappan, S., Biernat, J., Wegmann, S., Mandelkow, E., Müller, D. J., & Mandelkow�, E. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.554725 · Cited by 88
Self-citationTauopathies: 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 89
Gentry, E. G., Henderson, B. W., Arrant, A. E., Gearing, M., Feng, Y., Riddle, N. C., & Herskowitz, J. H. (2016) · The Journal of Neuroscience · doi:10.1523/jneurosci.2336-15.2016 · Cited by 90
Human Herpesviruses 6A and 6B in Brain Diseases: Association versus Causation
Komaroff, A. L., Pellett, P. E., & Jacobson, S. (2020) · Clinical Microbiology Reviews · doi:10.1128/cmr.00143-20 · Cited by 77
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
The Role of Post-Translational Modifications on the Structure and Function of Tau Protein
Ye, H., Han, Y., Li, P., Su, Z., & Huang, Y. (2022) · Journal of Molecular Neuroscience · doi:10.1007/s12031-022-02002-0 · Cited by 76
Joshi, V., Amanullah, A., Upadhyay, A., Mishra, R., Kumar, A., & Mishra, A. (2016) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2016.00093 · Cited by 77
Impaired protein degradation in FTLD and related disorders
Götzl, J. K., Lang, C. M., Haass, C., & Capell, A. (2016) · Ageing Research Reviews · doi:10.1016/j.arr.2016.04.008 · Cited by 75
The mammalian target of rapamycin at the crossroad between cognitive aging and Alzheimer’s disease
Talboom, J. S., Velázquez, R., & Oddo, S. (2015) · npj Aging and Mechanisms of Disease · doi:10.1038/npjamd.2015.8 · Cited by 67
Filamentous Aggregates Are Fragmented by the Proteasome Holoenzyme
Cliffe, R., Sang, J. C., Kundel, F., Finley, D. J., Klenerman, D., & Ye, Y. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.01.096 · Cited by 62
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
Jahangiri, B., Saei, A. K., Obi, P. O., Asghari, N., Lorzadeh, S., Hekmatirad, S., Rahmati, M., Velayatipour, F., Asghari, M. H., Saleem, A., et al. (2022) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2022.166484 · Cited by 62
Protein Quality Control and the Amyotrophic Lateral Sclerosis/Frontotemporal Dementia Continuum
Shahheydari, H., Ragagnin, A., Walker, A. K., Toth, R. P., Vidal, M., Jagaraj, C. J., Perri, E. R., Konopka, A., Sultana, J. M., & Atkin, J. D. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00119 · Cited by 61
Tau-Targeted Multifunctional Nanoinhibitor for Alzheimer’s Disease
Zhu, L., Xu, L., Wu, X., Dèng, F., Ma, R., Liu, Y., Huang, F., & Shi, L. (2021) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.1c00257 · Cited by 59
Chaperone-assisted E3 ligase CHIP: A double agent in cancer
Kumar, S., Basu, M., & Ghosh, M. K. (2021) · Genes & Diseases · doi:10.1016/j.gendis.2021.08.003 · Cited by 59
The potential roles of deubiquitinating enzymes in brain diseases
Lim, K., Joo, J., & Baek, K. (2020) · Ageing Research Reviews · doi:10.1016/j.arr.2020.101088 · Cited by 59
Chronic Administration of Dimebon Ameliorates Pathology in Tau P301S Transgenic Mice
Peters, O. M., Connor‐Robson, N., Sokolov, V. B., Aksinenko, A. Y., Kukharsky, M. S., Бачурин, С. О., Ninkina, N. N., & Buchman, V. L. (2013) · Journal of Alzheimer s Disease · doi:10.3233/jad-2012-121732 · Cited by 54
Fontaine, S. N., Rauch, J. N., Nordhues, B. A., Assimon, V. A., Stothert, A. R., Jinwal, U. K., Sabbagh, J. J., Chang, L., Stevens, S. M., Zuiderweg, E. R. P., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.637595 · Cited by 50
Schroeder, S. K., Joly‐Amado, A., Gordon, M. N., & Morgan, D. (2015) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-015-9637-6 · Cited by 51
Qneibi, M., Bdir, S., Maayeh, C., Bdair, M., Sandouka, D., Basit, D., & Hallak, M. (2023) · Neurochemical Research · doi:10.1007/s11064-023-04032-5 · Cited by 55
Chaperones—A New Class of Potential Therapeutic Targets in Alzheimer’s Disease
Batko, J., Antosz, K., Miśków, W., Pszczołowska, M., Walczak, K., & Leszek, J. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25063401 · Cited by 50
Jung, H.-J., Kim, Y.-J., Eggert, S., Chung, K. C., Choi, K. S., & Park, S. A. (2013) · Experimental Neurology · doi:10.1016/j.expneurol.2013.07.013 · Cited by 47
Oba, T., Saito, T., Asada, A., Shimizu, S., Iijima, K., & Ando, K. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014420 · Cited by 44
Fan, L., Qiu, X., Zhu, Z., Lv, J., Lu, J., Mao, F., Zhu, J., Wang, J., Guan, X., Chen, J., et al. (2019) · Acta Pharmacologica Sinica · doi:10.1038/s41401-019-0220-1 · Cited by 46
Axonal dystrophy in the brain of mice with Sanfilippo syndrome
Beard, H., Hassiotis, S., Gai, W., Parkinson-Lawrence, E. J., Hopwood, J. J., & Hemsley, K. M. (2017) · Experimental Neurology · doi:10.1016/j.expneurol.2017.06.010 · Cited by 43
LRRK2 Promotes Tau Accumulation, Aggregation and Release
Guerreiro, P. S., Gerhardt, E., da Fonseca, T. L., Bähr, M., Outeiro, T. F., & Eckermann, K. (2015) · Molecular Neurobiology · doi:10.1007/s12035-015-9209-z · Cited by 46
Implication of type 4 NADPH oxidase (NOX4) in tauopathy
Luengo, E., Trigo-Alonso, P., Fernández‐Mendívil, C., Núñez, Á., del Campo, M., Porrero, C., García‐Magro, N., Negredo, P., Senar, S., Sánchez‐Ramos, C., et al. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.redox.2021.102210 · Cited by 44
Making the Brain Glow: In Vivo Bioluminescence Imaging to Study Neurodegeneration
Hochgräfe, K., & Mandelkow, E. (2012) · Molecular Neurobiology · doi:10.1007/s12035-012-8379-1 · Cited by 41
Self-citationRed Ginseng Inhibits Tau Aggregation and Promotes Tau Dissociation In Vitro
Shin, S. J., Park, Y. H., Jeon, S. G., Kim, S., Nam, Y., Oh, S., Lee, Y. Y., & Moon, M. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/7829842 · Cited by 38
Mechanisms and therapeutic potential of interactions between human amyloids and viruses
Michiels, E., Rousseau, F., & Schymkowitz, J. W. H. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03711-8 · Cited by 37
Wu, D., Gao, D., Yu, H.-T., Pi, G.-L., Xiong, R., Lei, H., Wang, X., Liu, E.-J., Ye, J.-W., Yu, H.-L., et al. (2021) · Clinical and Translational Medicine · doi:10.1002/ctm2.428 · Cited by 30
Remodeling of the conformational ensemble of the repeat domain of tau by an aggregation enhancer
Akoury, E., Mukrasch, M. D., Biernat, J., Tepper, K., Ozenne, V., Mandelkow�, E., Blackledge, M. J., & Zweckstetter, M. (2016) · Protein Science · doi:10.1002/pro.2911 · Cited by 32
Self-citationSaidi, L.-J., Polydoro, M., Kay, K. R., Sanchez, L., Mandelkow, E., Hyman, B. T., & Spires‐Jones, T. L. (2015) · Journal of Alzheimer s Disease · doi:10.3233/jad-142094 · Cited by 34
Self-citationPhadwal, K., Kurian, D., Salamat, M. K. F., MacRae, V. E., Diack, A. B., & Manson, J. C. (2018) · Scientific Reports · doi:10.1038/s41598-018-28296-y · Cited by 33
PEG-Ceramide Nanomicelles Induce Autophagy and Degrade Tau Proteins in N2a Cells
Gao, J., Chen, X., Ma, T., He, B., Li, P., Zhao, Y., Ma, Y., Zhuang, J., & Yin, Y. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s258311 · Cited by 28
Tseng, J., Ajit, A., Tabassum, Z., Patel, N., Tian, X., Chen, Y., Prevatte, A. W., Ling, K., Rigo, F., Meeker, R. B., et al. (2020) · Cell Reports · doi:10.1016/j.celrep.2021.109037 · Cited by 27
Tau mRNA 3′UTR-to-CDS ratio is increased in Alzheimer disease
García‐Escudero, V., Gargini, R., Martín-Maestro, P., García, E., García‐Escudero, R., & Ávila, J. (2017) · Neuroscience Letters · doi:10.1016/j.neulet.2017.07.007 · Cited by 25
Physiological and pathophysiological functions of Swiprosin-1/EFhd2 in the nervous system
Mielenz, D., & Gunn-Moore, F. (2016) · Biochemical Journal · doi:10.1042/bcj20160168 · Cited by 24
Tau Protein as Therapeutic Target for Cancer? Focus on Glioblastoma
Hedna, R., Kovacic, H., Pagano, A., Peyrot, V., Robin, M., Devred, F., & Breuzard, G. (2022) · Cancers · doi:10.3390/cancers14215386 · Cited by 25
Defective proteostasis in induced pluripotent stem cell models of frontotemporal lobar degeneration
Mahali, S., Martinez, R., King, M., Verbeck, A., Harari, O., Benitez, B. A., Horie, K., Sato, C., Temple, S., & Karch, C. M. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-02274-5 · Cited by 33
Could autophagy dysregulation link neurotropic viruses to Alzheimer’s disease?
Romeo, M. A., Faggioni, A., & Cirone, M. (2019) · Neural Regeneration Research · doi:10.4103/1673-5374.253508 · Cited by 22
Loss of TMEM106B exacerbates Tau pathology and neurodegeneration in PS19 mice
Feng, T., Du, H., Yang, C., Wang, Y., & Hu, F. (2024) · Acta Neuropathologica · doi:10.1007/s00401-024-02702-4 · Cited by 22
Self-citationThe Co-chaperone BAG2 Mediates Cold-Induced Accumulation of Phosphorylated Tau in SH-SY5Y Cells
de Paula, C. A. D., Santiago, F. E., Oliveira, A. S., Oliveira, F. A., Almeida, M. C., & Carrettiero, D. C. (2015) · Cellular and Molecular Neurobiology · doi:10.1007/s10571-015-0239-x · Cited by 21
Guo, F., He, X., Li, S., & Le, W. (2016) · Molecular Neurobiology · doi:10.1007/s12035-016-0260-1 · Cited by 21
Liu, Q. R., Wang, X., Fang, Z., Zhao, J.-N., RUI, X., Zhang, B., He, Y., Liu, R., Chen, J., Chai, G., et al. (2024) · Autophagy · doi:10.1080/15548627.2024.2431472 · Cited by 20
Xu, H., Zhu, Y., Chen, X., Yang, T., Wang, X., Xu, S., Xie, X., Hu, M., Jiang, L., Cheng, J., et al. (2021) · Archives of Toxicology · doi:10.1007/s00204-021-03131-y · Cited by 20
Athanasiou, E., Gargalionis, A. N., Anastassopoulou, C. G., Tsakris, A., & Boufidou, F. (2022) · Brain Sciences · doi:10.3390/brainsci12081010 · Cited by 20
Francesco, M. A. D. (2024) · Viruses · doi:10.3390/v16010133 · Cited by 22
Decreased Proteasomal Function Induces Neuronal Loss and Memory Impairment
Tomaru, U., Ito, T., Ohmura, Y., Higashikawa, K., Miyajima, S., Tomatsu, R., Higashi, T., Ishizu, A., Kuge, Y., Yoshioka, M., et al. (2020) · American Journal Of Pathology · doi:10.1016/j.ajpath.2020.10.004 · Cited by 20
Deng, Y., Wang, S., Wang, Q., Xu, Z., Peng, Q., Chen, S., Zhu, L., Zhang, Y., & Duan, R. (2023) · Journal of Inflammation Research · doi:10.2147/jir.s392599 · Cited by 18
Majumder, P., Roy, K., Singh, B. K., Jana, N. R., & Mukhopadhyay, D. (2017) · Disease Models & Mechanisms · doi:10.1242/dmm.027748 · Cited by 19
NPAS4 Facilitates the Autophagic Clearance of Endogenous Tau in Rat Cortical Neurons
Fan, W., Long, Y., Lai, Y., Wang, X., Chen, G., & Zhu, B. (2015) · Journal of Molecular Neuroscience · doi:10.1007/s12031-015-0692-5 · Cited by 18
Inflammasome links traumatic brain injury, chronic traumatic encephalopathy, and Alzheimer’s disease
Seplovich, G., Bouchi, Y., Vaccari, J. P. D. R., Pareja, J. C. M., Reisner, A., Blackwell, L. S., Mechref, Y. S., Wang, K., Tyndall, J. A., Tharakan, B., et al. (2024) · Neural Regeneration Research · doi:10.4103/nrr.nrr-d-24-00107 · Cited by 21
Molecular Basis of Neuronal Autophagy in Ageing: Insights from Caenorhabditis elegans
Konstantinidis, G., & Tavernarakis, N. (2021) · Cells · doi:10.3390/cells10030694 · Cited by 19
Age-dependent changes in synaptic plasticity enhance tau oligomerization in the mouse hippocampus
Kimura, T., Suzuki, M., & Akagi, T. (2017) · Acta Neuropathologica Communications · doi:10.1186/s40478-017-0469-x · Cited by 17
Testing the link between isoaspartate and Alzheimer's disease etiology
Wang, J., Guo, C., Meng, Z., Zwan, M. D., Chen, X., Seelow, S., Lundström, S. L., Rodin, S., Teunissen, C. E., & Zubarev, R. A. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12735 · Cited by 16
Novel Cell Model for Tauopathy Induced by a Cell-Permeable Tau-Related Peptide
Veloria, J. R., Li, L., Breen, G. A. M., & Goux, W. J. (2017) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.7b00275 · Cited by 16
Lee, J., Lee, B., Lee, H. G., Kim, E. J. E., Kim, S. S., Kwon, H. C., Lee, H., Lee, G., Hong, W., Ham, S., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2505217122 · Cited by 15
Bin1 antibody lowers the expression of phosphorylated Tau in Alzheimer's disease
Thomas, S., Hoxha, K., Tran, A., & Prendergast, G. C. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.29142 · Cited by 15
Metadata
- Authors
- Wang, Y., & Mandelkow, E.
- Affiliations
- German Center for Neurodegenerative Diseases (DE)
- German Center for Neurodegenerative Diseases (DZNE), Bonn, Germany
- Corresponding author
- Wang, Yipeng
- ORCID
- Wang, Yipeng
- Venue
- Biochemical Society Transactions
- Publisher
- Portland Press Ltd.
- Published
- 2012-07-20
- Volume
- 40
- Issue
- 4
- Pages
- 644-652
- ISSN
- 0300-5127 (ISSN-L)
- 1470-8752
- OpenAlex
- W2149107089
- Semantic Scholar
- d284a357b1c845f43f0ed4c30e07818cb0344a3c
- Cited by
- 166
- References
- 102
- Citations by year
- 2026: 2 · 2025: 8 · 2024: 10 · 2023: 6 · 2022: 18 · 2021: 16 · 2020: 25 · 2019: 11 · 2018: 13 · 2017: 12 · 2016: 16 · 2015: 14 · 2014: 7 · 2013: 6 · 2012: 2
- FWCI
- 0.98
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Biochemical Society Transactions (publishedVersion)
- PubMed (publishedVersion)
- Max Planck Institute for Plasma Physics (submittedVersion)
- DZNE Pub (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Wellcome Trust
- Bundesministerium für Bildung und Forschung
- Tau Consortium
- Medical Research Council (MC_G1000734)
- 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 › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- tau protein, tau aggregation, protein degradation, ubiquitin-proteasome system, autophagy-lysosome system, Alzheimer's disease, tauopathy, neurodegeneration, proteolytic enzymes, therapeutic target
- MeSH terms
- Animals, Autophagy, Humans, Signal Transduction, tau Proteins, Proteasome Endopeptidase Complex
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