Degradation of tau protein by autophagy and proteasomal pathways

Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice

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Molecular chaperones in protein folding and proteostasis

Hartl, F. U., Bracher, A., & Hayer-Hartl, M. K. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,523 · see citing works

Loss of autophagy in the central nervous system causes neurodegeneration in mice

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Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease

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Tau-mediated neurodegeneration in Alzheimer’s disease and related disorders

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Decreased Clearance of CNS β-Amyloid in Alzheimer’s Disease

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Recognition of the polyubiquitin proteolytic signal

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The roles of intracellular protein-degradation pathways in neurodegeneration

Rubinsztein, D. C. (2006) · Nature · doi:10.1038/nature05291 · Cited by 1,625 · see citing works

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 · see citing works

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 · see citing works

Acetylation of Tau Inhibits Its Degradation and Contributes to Tauopathy

Min, S.-W., Cho, S.-H., Zhou, Y., Schroeder, S., Haroutunian, V., Seeley, W. W., Huang, E. J., Shen, Y., Masliah, E., Mukherjee, C., et al. (2010) · Neuron · doi:10.1016/j.neuron.2010.08.044 · Cited by 949 · see citing works

Enhancement of proteasome activity by a small-molecule inhibitor of USP14

Lee, B., Lee, M. J., Park, S., Oh, D., Elsasser, S., Chen, P., Gartner, C. A., Dimova, N. V., Hanna, J. W., Gygi, S. P., et al. (2010) · Nature · doi:10.1038/nature09299 · Cited by 943 · see citing works

Molecular Interplay between Mammalian Target of Rapamycin (mTOR), Amyloid-β, and Tau

Caccamo, A., Majumder, S., Richardson, A., Strong, R., & Oddo, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.100420 · Cited by 881 · see citing works

Impaired Proteasome Function in Alzheimer's Disease

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Ubiquitin Is a Component of Paired Helical Filaments in Alzheimer's Disease

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Aβ Immunotherapy Leads to Clearance of Early, but Not Late, Hyperphosphorylated Tau Aggregates via the Proteasome

Oddo, S., Billings, L., Kesslak, J. P., Cribbs, D. H., & LaFerla, F. M. (2004) · Neuron · doi:10.1016/j.neuron.2004.07.003 · Cited by 780 · see citing works

CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation

Petrucelli, L. (2004) · Human Molecular Genetics · doi:10.1093/hmg/ddh083 · Cited by 735 · see citing works

The acetylation of tau inhibits its function and promotes pathological tau aggregation

Cohen, T. J., Guo, J. L., Hurtado, D. E., Kwong, L. K., Mills, I. P., Trojanowski, J. Q., & Lee, V. M. Y. (2011) · Nature Communications · doi:10.1038/ncomms1255 · Cited by 724 · see citing works

Aβ Oligomers Cause Localized Ca ²⁺ Elevation, Missorting of Endogenous Tau into Dendrites, Tau Phosphorylation, and Destruction of Microtubules and Spines

Zempel, H., Thies, E., Mandelkow, E., & Mandelkow, E.-M. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.2357-10.2010 · Cited by 686 · see citing works

Rapamycin alleviates toxicity of different aggregate-prone proteins

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The high-affinity HSP90–CHIP complex recognizes and selectively degrades phosphorylated tau client proteins

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Ubiquitin is detected in neurofibrillary tangles and senile plaque neurites of Alzheimer disease brains.

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Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing

Wang, Y., Martinez-Vicente, M., Krüger, U., Kaushik, S., Wong, E., Mandelkow, E.-M., Cuervo, A. M., & Mandelkow, E. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp367 · Cited by 617 · see citing works

Selective inhibition of Alzheimer disease-like tau aggregation by phenothiazines.

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Inhibition of Heparin-induced Tau Filament Formation by Phenothiazines, Polyphenols, and Porphyrins

Taniguchi, S., Suzuki, N., Masuda, M., Hisanaga, S., Iwatsubo, T., Goedert, M., & Hasegawa, M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408714200 · Cited by 542 · see citing works

Proteasome inhibition by paired helical filament‐tau in brains of patients with Alzheimer's disease

Keck, S., Nitsch, R., Grune, T., & Ullrich, O. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01642.x · Cited by 483 · see citing works

CHIP-Hsc70 Complex Ubiquitinates Phosphorylated Tau and Enhances Cell Survival

Shimura, H., Schwartz, D., Gygi, S. P., & Kosik, K. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305838200 · Cited by 469 · see citing works

Chaperones increase association of tau protein with microtubules

Dou, F., Netzer, W. J., Tanemura, K., Li, F., Hartl, F. U., Takashima, A., Gouras, G. K., Greengard, P., & Xu, H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.242720499 · Cited by 462 · see citing works

Lysine 63-linked ubiquitination promotes the formation and autophagic clearance of protein inclusions associated with neurodegenerative diseases

Tan, J. M. M., Wong, E. S. P., Kirkpatrick, D. S., Pletniková, O., Ko, H. S., Tay, S.-P., Ho, M. W. L., Troncoso, J. C., Gygi, S. P., Lee, M. K., et al. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm320 · Cited by 445 · see citing works

Ubiquitin–proteasome pathway and cellular responses to oxidative stress

Shang, F., & Taylor, A. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.03.031 · Cited by 436 · see citing works

“Lest we forget you — methylene blue …”

Schirmer, R. H., Adler, H., Pickhardt, M., & Mandelkow�, E. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.12.012 · Cited by 416 · see citing works

Ubiquitin Enters the New Millennium

Pickart, C. M. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00347-1 · Cited by 393 · see citing works

Aβ inhibits the proteasome and enhances amyloid and tau accumulation

Tseng, B. P., Green, K. N., Chan, J. L., Blurton-Jones, M., & LaFerla, F. M. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2007.04.014 · Cited by 384 · see citing works

Alzheimer's DiseasePreprint

Selkoe, D. J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004457 · Cited by 371 · see citing works

Ubiquitin is conjugated with amino-terminally processed tau in paired helical filaments

Morishima-Kawashima, M., Hasegawa, M., Takio, K., Suzuki, M., Titani, K., & Ihara, Y. (1993) · Neuron · doi:10.1016/0896-6273(93)90063-w · Cited by 332 · see citing works

Proteasomal degradation of tau protein

David, D. C., Layfield, R., Serpell, L., Narain, Y., Goedert, M., & Spillantini, M. G. (2002) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2002.01137.x · Cited by 327 · see citing works

Sequestosome 1/p62 shuttles polyubiquitinated tau for proteasomal degradation

Babu, J. R., Geetha, T., & Wooten, M. W. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03181.x · Cited by 315 · see citing works

Alzheimer Disease-specific Conformation of Hyperphosphorylated Paired Helical Filament-Tau Is Polyubiquitinated through Lys-48, Lys-11, and Lys-6 Ubiquitin Conjugation

Cripps, D., Thomas, S. N., Jeng, Y., Yang, F., Davies, P., & Yang, A. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512786200 · Cited by 312 · see citing works

Integration of Clearance Mechanisms: The Proteasome and AutophagyPreprint

Wong, E. S. P., & Cuervo, A. M. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a006734 · Cited by 302 · see citing works

Trehalose ameliorates dopaminergic and tau pathology in parkin deleted/tau overexpressing mice through autophagy activation

Rodríguez-Navarro, J. A., Rodríguez, L., Casarejos, M. J., Solano, R. M., Gómez, A., Perucho, J., Cuervo, A. M., García de Yébenes, J., & Mena, M. A. (2010) · Neurobiology of Disease · doi:10.1016/j.nbd.2010.05.014 · Cited by 298 · see citing works

Autophagic degradation of tau in primary neurons and its enhancement by trehalose

Krüger, U., Wang, Y., Kumar, S., & Mandelkow, E.-M. (2012) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2011.11.009 · Cited by 297 · see citing works

Methylthioninium chloride (methylene blue) induces autophagy and attenuates tauopathy in vitro and in vivo

Congdon, E. E., Wu, J. W., Myeku, N., Figueroa, Y. H., Herman, M., Marinec, P. S., Gestwicki, J. E., Dickey, C. A., Yu, W. H., & Duff, K. E. (2012) · Autophagy · doi:10.4161/auto.19048 · Cited by 297 · see citing works

Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression

Hamano, T., Gendron, T. F., Causevic, E., Yen, S., Lin, W., Isidoro, C., DeTure, M., & Ko, L. (2008) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2008.06084.x · Cited by 283 · see citing works

Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies

Luo, W., Dou, F., Rodina, A., Chip, S., Kim, J., Zhao, Q., Moulick, K., Aguirre, J., Wu, N. F., Greengard, P., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701055104 · Cited by 274 · see citing works

A small-molecule scaffold induces autophagy in primary neurons and protects against toxicity in a Huntington disease model

Tsvetkov, A. S., Miller, J., Arrasate, M., Wong, J. S., Pleiss, M. A., & Finkbeiner, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004498107 · Cited by 266 · see citing works

The Generation of a 17 kDa Neurotoxic Fragment: An Alternative Mechanism by which Tau Mediates β-Amyloid-Induced Neurodegeneration

Park, S.-Y., & Ferreira, A. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.1125-05.2005 · Cited by 262 · see citing works

Deletion of the Ubiquitin Ligase CHIP Leads to the Accumulation, But Not the Aggregation, of Both Endogenous Phospho- and Caspase-3-Cleaved Tau Species

Dickey, C. A., Yue, M., Lin, W.-L., Dickson, D. W., Dunmore, J. H., Lee, W. C., Zehr, C., West, G., Cao, S., Clark, A. M. K., et al. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.0746-06.2006 · Cited by 248 · see citing works

Chemical Manipulation of Hsp70 ATPase Activity Regulates Tau Stability

Jinwal, U. K., Miyata, Y., Koren, J., Jones, J. R., Trotter, J. H., Chang, L., O’Leary, J. C., Morgan, D., Lee, D. C., Shults, C. L., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.3345-09.2009 · Cited by 231 · see citing works

The tau of MARK: a polarized view of the cytoskeleton

Matenia, D., & Mandelkow, E. (2009) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2009.03.008 · Cited by 228 · see citing works

A small‐molecule enhancer of autophagy decreases levels of Aβ and APP‐CTF via Atg5‐dependent autophagy pathway

Tian, Y., Bustos, V., Flajolet, M., & Greengard, P. (2011) · The FASEB Journal · doi:10.1096/fj.10-175158 · Cited by 224 · see citing works

Novel diffusion barrier for axonal retention of Tau in neurons and its failure in neurodegeneration

Li, X., Kumar, Y., Zempel, H., Mandelkow, E., Biernat, J., & Mandelkow, E. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.376 · Cited by 222 · see citing works

FTDP-17 mutations in tau transgenic mice provoke lysosomal abnormalities and Tau filaments in forebrain.

Lim, F., Hernández, F., Lucas, J., Gómez-Ramos, P., Morán, M., & Ávila, J. (2001) · Molecular and cellular neurosciences · doi:10.1006/mcne.2001.1051 · Cited by 215 · see citing works

In vivo evidence of CHIP up‐regulation attenuating tau aggregation

Sahara, N., Murayama, M., Mizoroki, T., Urushitani, M., Imai, Y., Takahashi, R., Murata, S., Tanaka, K., & Takashima, A. (2005) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2005.03272.x · Cited by 208 · see citing works

Pathophysiology of chaperone-mediated autophagy

Massey, A. C., Kiffin, R., & Cuervo, A. M. (2004) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2004.04.010 · Cited by 202 · see citing works

Rilmenidine attenuates toxicity of polyglutamine expansions in a mouse model of Huntington's disease

Rose, C., Menzies, F. M., Renna, M., Acevedo‐Arozena, A., Corrochano, S., Sadiq, O., Brown, S. D. M., & Rubinsztein, D. C. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq093 · Cited by 200 · see citing works

Ubiquitin-independent degradation of proteins by the proteasome

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BAG-2 Acts as an Inhibitor of the Chaperone-associated Ubiquitin Ligase CHIP

Arndt, V., Daniel, C., Nastainczyk, W., Alberti, S., & Höhfeld, J. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-07-0660 · Cited by 187 · see citing works

The Cochaperone BAG2 Sweeps Paired Helical Filament- Insoluble Tau from the Microtubule

Carrettiero, D. C., Hernández, I., Neveu, P. A., Papagiannakopoulos, T. Y., & Kosik, K. S. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.4660-08.2009 · Cited by 177 · see citing works

Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress

Poppek, D., Keck, S., Ermak, G., Jung, T., Stolzing, A., Ullrich, O., Davies, K. J. A., & Grune, T. (2006) · Biochemical Journal · doi:10.1042/bj20060463 · Cited by 174 · see citing works

Aging perturbs 26S proteasome assembly in Drosophila melanogaster

Vernace, V. A., Arnaud, L. T., Schmidt‐Glenewinkel, T., & Figueiredo‐Pereira, M. E. (2007) · The FASEB Journal · doi:10.1096/fj.06-6751com · Cited by 165 · see citing works

Frontotemporal Dementia: Implications for Understanding Alzheimer DiseasePreprint

Goedert, M., Ghetti, B. F., & Spillantini, M. G. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006254 · Cited by 151 · see citing works

Alzheimer Disease in 2020Preprint

Holtzman, D. M., Mandelkow, E., & Selkoe, D. J. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a011585 · Cited by 151 · see citing works

A Genomic Screen for Modifiers of Tauopathy Identifies Puromycin-Sensitive Aminopeptidase as an Inhibitor of Tau-Induced Neurodegeneration

Karsten, S. L., Sang, T.-K., Gehman, L. T., Chatterjee, S., Liu, J., Lawless, G. M., Sengupta, S., Berry, R. W., Pomakian, J., Oh, H. S., et al. (2006) · Neuron · doi:10.1016/j.neuron.2006.07.019 · Cited by 147 · see citing works

A Caspase Cleaved Form of Tau Is Preferentially Degraded through the Autophagy Pathway

Dolan, P. J., & Johnson, G. V. W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.110940 · Cited by 147 · see citing works

Human BAG-1/RAP46 protein is generated as four isoforms by alternative translation initiation and overexpressed in cancer cells

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Tau-Based Treatment Strategies in Neurodegenerative Diseases

Schneider, A., & Mandelkow�, E. (2008) · Neurotherapeutics · doi:10.1016/j.nurt.2008.05.006 · Cited by 142 · see citing works

Proteolytic processing of tau

Wang, Y., Garg, S., Mandelkow, E., & Mandelkow�, E. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380955 · Cited by 140 · see citing works

U‐box protein carboxyl terminus of Hsc70‐interacting protein (CHIP) mediates poly‐ubiquitylation preferentially on four‐repeat Tau and is involved in neurodegeneration of tauopathy

Hatakeyama, S., Matsumoto, M., Kamura, T., Murayama, M., Chui, D.-H., Planel, E., Takahashi, R., Nakayama, K. I., & Takashima, A. (2004) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2004.02713.x · Cited by 127 · see citing works

Ultrastructural neuronal pathology in transgenic mice expressing mutant (P301L) human tau

Lin, W.-L., Lewis, J. M., Yen, S.-H. C., Hutton, M. L., & Dickson, D. W. (2003) · Journal of Neurocytology · doi:10.1023/b:neur.0000021904.61387.95 · Cited by 125 · see citing works

Dual modification of Alzheimer’s disease PHF-tau protein by lysine methylation and ubiquitylation: a mass spectrometry approach

Thomas, S. N., Funk, K. E., Wan, Y., Liao, Z., Davies, P., Kuret, J., & Yang, A. J. (2012) · Acta Neuropathologica · doi:10.1007/s00401-011-0893-0 · Cited by 123 · see citing works

BAG-1 Associates with Hsc70·Tau Complex and Regulates the Proteasomal Degradation of Tau Protein

Elliott, E., Tsvetkov, P., & Ginzburg, I. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706379200 · Cited by 114 · see citing works

Calpain-Mediated Tau Cleavage: A Mechanism Leading to Neurodegeneration Shared by Multiple Tauopathies

Ferreira, A., & Bigio, E. H. (2011) · Molecular Medicine · doi:10.2119/molmed.2010.00220 · Cited by 112 · see citing works

Aging and regulated protein degradation: who has the UPPer hand?

Vernace, V. A., Schmidt‐Glenewinkel, T., & Figueiredo‐Pereira, M. E. (2007) · Aging Cell · doi:10.1111/j.1474-9726.2007.00329.x · Cited by 110 · see citing works

Increased Membrane Cholesterol Might Render Mature Hippocampal Neurons More Susceptible to β-Amyloid-Induced Calpain Activation and Tau Toxicity

Nicholson, A. M., & Ferreira, A. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.0862-09.2009 · Cited by 106 · see citing works

Cleavage of Tau by calpain in Alzheimer's disease: the quest for the toxic 17 kD fragment

Garg, S., Timm, T., Mandelkow, E.-M., Mandelkow, E., & Wang, Y. (2011) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.09.008 · Cited by 103 · see citing works

MRI is a sensitive marker of subtle white matter pathology in hypoperfused mice

Holland, P. R., Bastin, M. E., Jansen, M. A., Merrifield, G. D., Coltman, R., Scott, F., Nowers, H., Khallout, K., Marshall, I., Wardlaw, J. M., et al. (2010) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2010.11.009 · Cited by 102 · see citing works

Inhibition of Hsp70 by Methylene Blue Affects Signaling Protein Function and Ubiquitination and Modulates Polyglutamine Protein Degradation

Wang, A. M., Morishima, Y., Clapp, K. M., Peng, H., Pratt, W. B., Gestwicki, J. E., Osawa, Y., & Lieberman, A. P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.098806 · Cited by 91 · see citing works

Peroxynitrite induces Alzheimer‐like tau modifications and accumulation in rat brain and its underlying mechanisms

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Tau protein degradation is catalyzed by the ATP/ubiquitin-independent 20S proteasome under normal cell conditions

Grune, T., Botzen, D., Engels, M., Voß, P., Kaiser, B., Jung, T., Grimm, S., Ermak, G., & Davies, K. J. A. (2010) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2010.05.008 · Cited by 85 · see citing works

Distinct Isoforms of the Cofactor BAG-1 Differentially Affect Hsc70 Chaperone Function

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Puromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagy

Menzies, F. M., Hourez, R., Imarisio, S., Raspe, M. A., Sadiq, O., Chandraratna, D., O’Kane, C. J., Rock, K. L., Reits, E. A., Goldberg, A. L., et al. (2010) · Human Molecular Genetics · doi:10.1093/hmg/ddq385 · Cited by 81 · see citing works

Microtubule-associated protein tau is a substrate of ATP/Mg2+-dependent proteasome protease system

Zhang, J. Y., Liu, S. J., Li, H., & Wang, J. (2004) · Journal of Neural Transmission · doi:10.1007/s00702-004-0196-x · Cited by 73 · see citing works

Overexpression of Wild-Type Murine Tau Results in Progressive Tauopathy and Neurodegeneration

Adams, S. J., Crook, R., Deture, M. A., Randle, S. J., Innes, A. E., Yu, X., Lin, W.-L., Dugger, B. N., McBride, M., Hutton, M., et al. (2009) · American Journal Of Pathology · doi:10.2353/ajpath.2009.090462 · Cited by 71 · see citing works

Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver

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Degradation of Tau Protein by Puromycin-Sensitive Aminopeptidase in Vitro

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