Impaired Proteasome Function in Alzheimer's Disease

Cellular actions of beta-amyloid precursor protein and its soluble and fibrillogenic derivatives

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Brain Regional Correspondence Between Alzheimer's Disease Histopathology and Biomarkers of Protein Oxidation

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Four-hydroxynonenal, a product of lipid peroxidation, is increased in the brain in Alzheimer's disease

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Comparative resistance of the 20S and 26S proteasome to oxidative stress

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Oxidative stress, dysfunctional glucose metabolism and Alzheimer disease

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Extensive Involvement of Autophagy in Alzheimer Disease: An Immuno-Electron Microscopy Study

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Role of Free Radicals in the Neurodegenerative Diseases: Therapeutic Implications for Antioxidant Treatment

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The Biology of Proteostasis in Aging and Disease

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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 · see citing works

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

Amyloid β-peptide (1-42)-induced Oxidative Stress and Neurotoxicity: Implications for Neurodegeneration in Alzheimer's Disease Brain. A Review

Allan Butterfield, D. (2002) · Free Radical Research · doi:10.1080/1071576021000049890 · Cited by 786 · see citing works

Proteasomal function is impaired in substantia nigra in Parkinson’s disease

McNaught, K. S. P., & Jenner, P. (2001) · Neuroscience Letters · doi:10.1016/s0304-3940(00)01701-8 · Cited by 653 · see citing works

The Unfolded Protein Response Is Activated in Pretangle Neurons in Alzheimer's Disease Hippocampus

Hoozemans, J. J. M., van Haastert, E. S., Nijholt, D. A. T., Rozemuller, A. J. M., Eikelenboom, P., & Scheper, W. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.080814 · Cited by 600 · see citing works

Proteomic identification of oxidatively modified proteins in Alzheimer’s disease brain. Part I: Creatine kinase BB, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1

Castegna, A., Aksenov, M., Aksenova, M., Thongboonkerd, V., Klein, J. B., Pierce, W. M., Booze, R., Markesbery, W. R., & Butterfield, D. A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00914-0 · Cited by 581 · see citing works

Roles of amyloid β-peptide-associated oxidative stress and brain protein modifications in the pathogenesis of Alzheimer's disease and mild cognitive impairment

Butterfield, D. A., Reed, T., Newman, S. F., & Sultana, R. (2007) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.05.037 · Cited by 564 · 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

Microbiota modulation counteracts Alzheimer’s disease progression influencing neuronal proteolysis and gut hormones plasma levels

Bonfili, L., Cecarini, V., Berardi, S., Scarpona, S., Suchodolski, J. S., Nasuti, C., Fiorini, D., Boarelli, M. C., Rossi, G., & Eleuteri, A. M. (2017) · Scientific Reports · doi:10.1038/s41598-017-02587-2 · Cited by 453 · see citing works

Tau-driven 26S proteasome impairment and cognitive dysfunction can be prevented early in disease by activating cAMP-PKA signaling

Myeku, N., Clelland, C. L., Emrani, S., Kukushkin, N. V., Yu, W. H., Goldberg, A. L., & Duff, K. E. (2016) · Nature Medicine · doi:10.1038/nm.4011 · Cited by 446 · see citing works

Advances in tau-focused drug discovery for Alzheimer's disease and related tauopathies

Brunden, K. R., Trojanowski, J. Q., & Lee, V. M.-Y. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2959 · Cited by 440 · see citing works

Animal Models of Alzheimer Disease

LaFerla, F. M., & Green, K. N. (2012) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006320 · Cited by 419 · see citing works

Elevated risk of type 2 diabetes for development of Alzheimer disease: A key role for oxidative stress in brain

Butterfield, D. A., Di Domenico, F., & Barone, E. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.06.010 · Cited by 402 · see citing works

Oxidative Stress, Amyloid-β Peptide, and Altered Key Molecular Pathways in the Pathogenesis and Progression of Alzheimer’s Disease

Butterfield, D. A., & Boyd-Kimball, D. (2018) · Journal of Alzheimer’s Disease · doi:10.3233/jad-170543 · Cited by 403 · 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

Tau-targeting therapies for Alzheimer disease: Current status and future directions

Congdon, E. E., Ji, C., Tetlow, A. M., Jiang, Y., & Sigurdsson, E. M. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00883-2 · Cited by 371 · see citing works

Tau Post-translational Modifications: Dynamic Transformers of Tau Function, Degradation, and Aggregation

Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367 · see citing works

Neuronal cell death in neurodegenerative diseases: recurring themes around protein handling

Gorman, A. M. (2008) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2008.00402.x · Cited by 362 · see citing works

Cholesterol Metabolism Is a Druggable Axis that Independently Regulates Tau and Amyloid-β in iPSC-Derived Alzheimer’s Disease Neurons

van der Kant, R., Langness, V. F., Herrera, C. M., Williams, D. A., Fong, L. K., Leestemaker, Y., Steenvoorden, E., Rynearson, K. D., Brouwers, J. F., Helms, J. B., et al. (2019) · Cell Stem Cell · doi:10.1016/j.stem.2018.12.013 · Cited by 350 · see citing works

Causes of oxidative stress in Alzheimer disease

Zhu, X., Su, B., Wang, X., Smith, M. A., & Perry, G. (2007) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-007-7218-4 · Cited by 336 · see citing works

Proteasomal degradation of tau protein

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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

β-Amyloid Accumulation Impairs Multivesicular Body Sorting by Inhibiting the Ubiquitin-Proteasome System

Almeida, C. G., Takahashi, R. H., & Gouras, G. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.5078-05.2006 · Cited by 316 · see citing works

Deconstruction for Reconstruction: The Role of Proteolysis in Neural Plasticity and Disease

Bingol, B., & Sheng, M. (2011) · Neuron · doi:10.1016/j.neuron.2010.11.006 · Cited by 275 · see citing works

Age-related macular degeneration (AMD): Alzheimer's disease in the eye?

Kaarniranta, K., Salminen, A., Haapasalo, A., Soininen, H., & Hiltunen, M. (2011) · Journal of Alzheimer s Disease · doi:10.3233/jad-2011-101908 · Cited by 248 · see citing works

Early neuronal accumulation of DNA double strand breaks in Alzheimer’s disease

Shanbhag, N. M., Evans, M. D., Mao, W., Nana, A. L., Seeley, W. W., Adame, A., Rissman, R. A., Masliah, E., & Mucke, L. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0723-5 · Cited by 214 · see citing works

4-Hydroxy-2-nonenal, a reactive product of lipid peroxidation, and neurodegenerative diseases: a toxic combination illuminated by redox proteomics studies

Perluigi, M., Coccia, R., & Butterfield, D. A. (2012) · Antioxidants & Redox Signaling · doi:10.1089/ars.2011.4406 · Cited by 229 · see citing works

Protection from Alzheimer's-like disease in the mouse by genetic ablation of inducible nitric oxide synthase

Nathan, C., Calingasan, N., Nezezon, J., Ding, A., Lucia, M. S., La Perle, K., Fuortes, M., Lin, M., Ehrt, S., Kwon, N. S., et al. (2005) · The Journal of Experimental Medicine · doi:10.1084/jem.20051529 · Cited by 214 · see citing works

Mitochondrial impairment triggers cytosolic oxidative stress and cell death following proteasome inhibition

Maharjan, S., Oku, M., Tsuda, M., Hoseki, J., & Sakai, Y. (2014) · Scientific Reports · doi:10.1038/srep05896 · Cited by 212 · see citing works

The pleiotropic neuroprotective effects of resveratrol in cognitive decline and Alzheimer’s disease pathology: From antioxidant to epigenetic therapy

Griñán-Ferré, C., Bellver-Sanchis, A., Izquierdo, V., Corpas, R., Roig-Soriano, J., Chillón, M., Andres-Lacueva, C., Somogyvári, M., Sőti, C., Sanfeliu, C., et al. (2021) · Ageing Research Reviews · doi:10.1016/j.arr.2021.101271 · Cited by 208 · see citing works

Reactive glia show increased immunoproteasome activity in Alzheimer’s disease

Orre, M., Kamphuis, W., Dooves, S., Kooijman, L., Chan, E. T., Kirk, C. J., Dimayuga Smith, V., Koot, S., Mamber, C., Jansen, A. H., et al. (2013) · Brain · doi:10.1093/brain/awt083 · Cited by 180 · see citing works

Defining Alzheimer as a common age-related neurodegenerative process not inevitably leading to dementia

Ferrer, I. (2012) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2012.03.005 · Cited by 174 · see citing works

Effect of Wild-type or Mutant Parkin on Oxidative Damage, Nitric Oxide, Antioxidant Defenses, and the Proteasome

Hyun, D.-H., Lee, M., Hattori, N., Kubo, S.-I., Mizuno, Y., Halliwell, B., & Jenner, P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200666200 · Cited by 172 · see citing works

Degradation of tau protein by autophagy and proteasomal pathways

Wang, Y., & Mandelkow, E. (2012) · Biochemical Society Transactions · doi:10.1042/bst20120071 · Cited by 166 · see citing works

Impaired proteostasis during skeletal muscle aging

Fernando, R., Drescher, C., Nowotny, K., Grune, T., & Castro, J. P. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.08.037 · Cited by 134 · see citing works

Traffic at the intersection of neurotrophic factor signaling and neurodegeneration

Salehi, A., Delcroix, J.-D., & Mobley, W. C. (2003) · Trends in Neurosciences · doi:10.1016/s0166-2236(02)00038-3 · Cited by 131 · see citing works

Amyloid generation and dysfunctional immunoproteasome activation with disease progression in animal model of familial Alzheimer’s disease

Aso, E., Lomoio, S., López‐González, I., Joda, L., Carmona, M., Fernández‐Yagüe, N., Moreno, J., Juvés, S., Pujol, A., Pamplona, R., et al. (2012) · Brain Pathology · doi:10.1111/j.1750-3639.2011.00560.x · Cited by 118 · see citing works

A tripartite motif protein TRIM11 binds and destabilizes Humanin, a neuroprotective peptide against Alzheimer's disease‐relevant insults

Niikura, T., Hashimoto, Y., Tajima, H., Ishizaka, M., Yamagishi, Y., Kawasumi, M., Nawa, M., Terashita, K., Aiso, S., & Nishimoto, I. (2003) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2003.02553.x · Cited by 115 · see citing works

Impaired Autophagy in Sporadic Inclusion-Body Myositis and in Endoplasmic Reticulum Stress-Provoked Cultured Human Muscle Fibers

Nogalska, A., D'Agostino, C., Terracciano, C., Engel, W. K., & Askanas, V. (2010) · The American Journal of Pathology · doi:10.2353/ajpath.2010.100050 · Cited by 114 · see citing works

The Triangle of Death in Alzheimer's Disease Brain: The Aberrant Cross-Talk Among Energy Metabolism, Mammalian Target of Rapamycin Signaling, and Protein Homeostasis Revealed by Redox Proteomics

Di Domenico, F., Barone, E., Perluigi, M., & Butterfield, D. A. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6759 · Cited by 114 · see citing works

Proteasomal activity in brain differs between species and brain regions and changes with age.

Zeng, B.-Y., Medhurst, A. D., Jackson, M., Rose, S., & Jenner, P. (2005) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2005.01.008 · Cited by 113 · see citing works

Proteasome Inhibition and Aggresome Formation in Sporadic Inclusion-Body Myositis and in Amyloid-β Precursor Protein-Overexpressing Cultured Human Muscle Fibers

Fratta, P., Engel, W. K., McFerrin, J., Davies, K. J. A., Lin, S. W., & Askanas, V. (2005) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)62994-x · Cited by 111 · see citing works

Redox proteomics and amyloid β-peptide: Insights into Alzheimer disease

Butterfield, D. A., & Boyd‐Kimball, D. (2019) · Journal of Neurochemistry · doi:10.1111/jnc.14589 · Cited by 105 · see citing works

The Proteasome and Oxidative Stress in Alzheimer's Disease

Bonet-Costa, V., Pomatto, L. C.-D., & Davies, K. J. A. (2016) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6802 · Cited by 99 · see citing works

Glucocorticoids Trigger Alzheimer disease-like pathobiochemistry in rat neuronal cells expressing human tau

Sotiropoulos, I., Catania, C., Riedemann, T., Fry, J. P., Breen, K. C., Michaelidis, T. M., & Almeida, O. F. X. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05613.x · Cited by 97 · see citing works

Proteomic identification of proteins specifically oxidized in Caenorhabditis elegans expressing human Aβ(1-42): Implications for Alzheimer’s Disease

Boyd-Kimball, D., Poon, H. F., Lynn, B. C., Cai, J., Pierce Jr., W. M., Klein, J. B., Ferguson, J., Link, C. D., & Butterfield, D. A. (2006) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2005.07.001 · Cited by 98 · see citing works

The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics

Pritchard, S. M., Dolan, P. J., Vitkus, A., & Johnson, G. V. W. (2011) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2011.01273.x · Cited by 89 · see citing works

17-AAG Induces Cytoplasmic α-Synuclein Aggregate Clearance by Induction of Autophagy

Riedel, M., Goldbaum, O., Schwarz, L., Schmitt, S., & Richter-Landsberg, C. (2010) · PLoS ONE · doi:10.1371/journal.pone.0008753 · Cited by 87 · see citing works

Meta-Analysis of Parkinson’s Disease and Alzheimer’s Disease Revealed Commonly Impaired Pathways and Dysregulation of NRF2-Dependent Genes

Wang, Q., Li, W.-X., Dai, S.-X., Guo, Y.-C., Han, F.-F., Zheng, J.-J., Li, G.-H., & Huang, J.-F. (2017) · Journal of Alzheimer s Disease · doi:10.3233/jad-161032 · Cited by 88 · see citing works

Amyloid precursor protein (APP) May act as a substrate and a recognition unit for CRL4CRBN and Stub1 E3 ligases facilitating ubiquitination of proteins involved in presynaptic functions and neurodegeneration

Del Prete, D., Rice, R. C., Rajadhyaksha, A. M., & D'Adamio, L. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.733626 · Cited by 86 · see citing works

Axotrophin/MARCH7 acts as an E3 ubiquitin ligase and ubiquitinates tau protein in vitro impairing microtubule binding

Flach, K., Ramminger, E., Hilbrich, I., Arsalan-Werner, A., Albrecht, F., Herrmann, L., Goedert, M., Arendt, T., & Holzer, M. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.05.029 · Cited by 58 · see citing works

Oxidative Stress and Proteostasis Network: Culprit and Casualty of Alzheimer’s-Like Neurodegeneration

Di Domenico, F., Head, E., Butterfield, D. A., & Perluigi, M. (2014) · Advances in Geriatrics · doi:10.1155/2014/527518 · Cited by 50 · see citing works

Polyubiquitinylation Profile in Down Syndrome Brain Before and After the Development of Alzheimer Neuropathology

Tramutola, A., Di Domenico, F., Barone, E., Arena, A., Giorgi, A., di Francesco, L., Schininà, M. E., Coccia, R., Head, E., Butterfield, D. A., et al. (2017) · Antioxidants & Redox Signaling · doi:10.1089/ars.2016.6686 · Cited by 49 · see citing works

Proteomic identification of specifically carbonylated brain proteins in APPNLh/APPNLh×PS-1P264L/PS-1P264L human double mutant knock-in mice model of Alzheimer disease as a function of age

Sultana, R., Robinson, R. A. S., Di Domenico, F., Abdul, H. M., Clair, D. K. S., Markesbery, W. R., Cai, J., Pierce, W. M., & Butterfield, D. A. (2011) · Journal of Proteomics · doi:10.1016/j.jprot.2011.06.015 · Cited by 41 · see citing works

Mutant ubiquitin decreases amyloid β plaque formation in a transgenic mouse model of Alzheimer’s disease

van Tijn, P., Dennissen, F. J. A., Gentier, R. J. G., Hobo, B., Hermes, D., Steinbusch, H. W. M., Van Leeuwen, F. W., & Fischer, D. F. (2012) · Neurochemistry International · doi:10.1016/j.neuint.2012.07.007 · Cited by 39 · see citing works