The proteasomal system

Biochemistry and molecular cell biology of diabetic complications

Brownlee, M. (2001) · Nature · doi:10.1038/414813a · Cited by 9,107

A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes

MACDONALD, M. (1993) · Cell · doi:10.1016/0092-8674(93)90585-e · Cited by 8,366

Inflammation and Atherosclerosis

Libby, P., Ridker, P. M., & Maseri, A. (2002) · Circulation · doi:10.1161/hc0902.104353 · Cited by 7,724

The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis

Maxwell, P. H., Wiesener, M. S., Chang, G.-W., Clifford, S. C., Vaux, E. C., Cockman, M. E., Wykoff, C. C., Pugh, C. W., Maher, E. R., & Ratcliffe, P. J. (1999) · Nature · doi:10.1038/20459 · Cited by 5,180

Function and Activation of NF-kappaB in the Immune System

Baeuerle, P. A., & Henkel, T. (1994) · Annual Review of Immunology · doi:10.1146/annurev.iy.12.040194.001041 · Cited by 4,745

Mdm2 promotes the rapid degradation of p53

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Nitric oxide synthases: structure, function and inhibition

ALDERTON, W. K., COOPER, C. E., & KNOWLES, R. G. (2001) · Biochemical Journal · doi:10.1042/bj3570593 · Cited by 4,110

Identification of ubiquitin ligases required for skeletal muscle atrophy.

Bodine, S. C., Latres, E., Baumhueter, S., Lai, V. K.-M., Nunez, L., Clarke, B. A., Poueymirou, W. T., Panaro, F. J., Na, E., Dharmarajan, K., et al. (2001) · Science · doi:10.1126/science.1065874 · Cited by 3,521

Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy.

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Reactive Oxygen Species and the Central Nervous System

Halliwell, B. (1992) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.1992.tb10990.x · Cited by 2,947

Amyloid deposition as the central event in the aetiology of Alzheimer’s disease

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Role of oxidative stress in diabetic complications: a new perspective on an old paradigm.

Baynes, J. W., & Thorpe, S. R. (1999) · Diabetes · doi:10.2337/diabetes.48.1.1 · Cited by 2,441

Aggresomes: A Cellular Response to Misfolded Proteins

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Noxa, a BH3-Only Member of the Bcl-2 Family and Candidate Mediator of p53-Induced Apoptosis

Oda, E., Ohki, R., Murasawa, H., Nemoto, J., Shibue, T., Yamashita, T., Tokino, T., Taniguchi, T., & Tanaka, †. N. (2000) · Science · doi:10.1126/science.288.5468.1053 · Cited by 2,112

Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., & Finkbeiner, S. (2004) · Nature · doi:10.1038/nature02998 · Cited by 1,979

Oxidative Damage Is the Earliest Event in Alzheimer Disease

Nunomura, A., Perry, G., Aliev, G., Hirai, K., Takeda, A., Balraj, E. K., Jones, P. K., Ghanbari, H., Wataya, T., Shimohama, S., et al. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.8.759 · Cited by 1,885

P ROTOFIBRILS , P ORES , F IBRILS, AND N EURODEGENERATION : Separating the Responsible Protein Aggregates from The Innocent Bystanders

Caughey, B., & Lansbury, P. T. (2003) · Annual Review of Neuroscience · doi:10.1146/annurev.neuro.26.010302.081142 · Cited by 1,650

Oxidative Stress and Vascular Disease

Madamanchi, N. R., Vendrov, A., & Runge, M. S. (2005) · Arteriosclerosis, Thrombosis, and Vascular Biology · doi:10.1161/01.atv.0000150649.39934.13 · Cited by 1,618

Huntingtin-Encoded Polyglutamine Expansions Form Amyloid-like Protein Aggregates In Vitro and In Vivo

Scherzinger, E., Lurz, R., Turmaine, M., Mangiarini, L., Hollenbach, B., Hasenbank, R., Bates, G. P., Davies, S. W., Lehrach, H., & Wanker, E. E. (1997) · Cell · doi:10.1016/s0092-8674(00)80514-0 · Cited by 1,291

An integrated hypothesis that considers drusen as biomarkers of immune-mediated processes at the RPE-Bruch's membrane interface in aging and age-related macular degeneration

Hageman, G. (2001) · Progress in Retinal and Eye Research · doi:10.1016/s1350-9462(01)00010-6 · Cited by 1,265

BH3 Domains of BH3-Only Proteins Differentially Regulate Bax-Mediated Mitochondrial Membrane Permeabilization Both Directly and Indirectly

Kuwana, T., Bouchier-Hayes, L., Chipuk, J. E., Bonzon, C., Sullivan, B. A., Green, D. R., & Newmeyer, D. D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.003 · Cited by 1,185

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

Mattson, M. P. (1997) · Physiological Reviews · doi:10.1152/physrev.1997.77.4.1081 · Cited by 1,006

Protein translocation across the eukaryotic endoplasmic reticulum and bacterial plasma membranes.

Rapoport, T. A. (2007) · Nature · doi:10.1038/nature06384 · Cited by 977

Postprandial Hyperglycemia and Diabetes Complications

Ceriello, A. (2005) · Diabetes · doi:10.2337/diabetes.54.1.1 · Cited by 945

Tauopathy in Drosophila : Neurodegeneration Without Neurofibrillary Tangles

Wittmann, C. W., Wszolek, M. F., Shulman, J. M., Salvaterra, P. M., Lewis, J., Hutton, M., & Feany, M. B. (2001) · Science · doi:10.1126/science.1062382 · Cited by 939

Lipofuscin: mechanisms of age-related accumulation and influence on cell function12 1Guest Editor: Rajindar S. Sohal 2This article is part of a series of reviews on “Oxidative Stress and Aging.” The full list of papers may be found on the homepage of the journal.

Brunk, U. T., & Terman, A. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)00959-0 · Cited by 919

Metal-catalyzed oxidation of proteins. Physiological consequences

Stadtman, E. R., & Oliver, C. N. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)52199-2 · Cited by 862

The N-end rule: functions, mysteries, uses

Varshavsky, A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.22.12142 · Cited by 859

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

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

Hensley, K., Hall, N., Subramaniam, R., Cole, P., Harris, M., Aksenov, M., Aksenova, M., Gabbita, S. P., Wu, J. F., Carney, J. M., et al. (1995) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1995.65052146.x · Cited by 779

Cellular and molecular mechanisms of stress-induced premature senescence (SIPS) of human diploid fibroblasts and melanocytes

Toussaint, O., Medrano, E. E., & von Zglinicki, T. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00180-7 · Cited by 713

Potent and selective inhibitors of the proteasome: Dipeptidyl boronic acids

Adams, J., Behnke, M., Chen, S., Cruickshank, A. A., Dick, L. R., Grenier, L., Klunder, J. M., Ma, Y.-T., Plamondon, L., & Stein, R. L. (1998) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(98)00029-8 · Cited by 685

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

Markesbery, W. R., & Lovell, M. A. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00009-8 · Cited by 680

Diabetes mellitus and free radicals

Wolff, S. P. (1993) · British Medical Bulletin · doi:10.1093/oxfordjournals.bmb.a072637 · Cited by 660

The redox chemistry of the Alzheimer's disease amyloid β peptide

Smith, D. G., Cappai, R., & Barnham, K. J. (2007) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.02.002 · Cited by 608

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

REINHECKEL, T., SITTE, N., ULLRICH, O., KUCKELKORN, U., DAVIES, K. J. A., & GRUNE, T. (1998) · Biochemical Journal · doi:10.1042/bj3350637 · Cited by 447

What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?

Jagoe, R. T., & Goldberg, A. L. (2001) · Current Opinion in Clinical Nutrition and Metabolic Care · doi:10.1097/00075197-200105000-00003 · Cited by 399

Proteomics Analysis of Cellular Response to Oxidative Stress

Rabilloud, T., Heller, M., Gasnier, F., Luche, S., Rey, C., Aebersold, R., Benahmed, M., Louisot, P., & Lunardi, J. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m106585200 · Cited by 393

Membrane fusion and the cell cycle: Cdc48p participates in the fusion of ER membranes

Latterich, M., Fröhlich, K.-U., & Schekman, R. (1995) · Cell · doi:10.1016/0092-8674(95)90268-6 · Cited by 388

Human HRD1 Is an E3 Ubiquitin Ligase Involved in Degradation of Proteins from the Endoplasmic Reticulum

Kikkert, M., Doolman, R., Dai, M., Avner, R., Hassink, G., van Voorden, S., Thanedar, S., Roitelman, J., Chau, V., & Wiertz, E. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307453200 · Cited by 384

BRAIN, SKELETAL MUSCLE AND PLATELET HOMOGENATE MITOCHONDRIAL FUNCTION IN PARKINSON'S DISEASE

MANN, V. M., COOPER, J. M., KRIGE, D., DANIEL, S. E., SCHAPIRA, A. H. V., & MARSDEN, C. D. (1992) · Brain · doi:10.1093/brain/115.2.333 · Cited by 346

Patterns of gene expression in atrophying skeletal muscles: response to food deprivation

Jagoe, R. T., Lecker, S. H., Gomes, M., & Goldberg, A. L. (2002) · The FASEB Journal · doi:10.1096/fj.02-0312com · Cited by 344

Depletion of 26S Proteasomes in Mouse Brain Neurons Causes Neurodegeneration and Lewy-Like Inclusions Resembling Human Pale Bodies

Bedford, L., Hay, D., Devoy, A., Paine, S., Powe, D. G., Seth, R., Gray, T., Topham, I., Fone, K., Rezvani, N., et al. (2008) · The Journal of Neuroscience · doi:10.1523/jneurosci.2218-08.2008 · Cited by 327

Metals and Alzheimer's disease

Adlard, P. A., & Bush, A. I. (2006) · Journal of Alzheimer's Disease · doi:10.3233/jad-2006-102-303 · Cited by 324

Small Ubiquitin-like Modifier (SUMO) Modification of Natively Unfolded Proteins Tau and α-Synuclein

Dorval, V., & Fraser, P. E. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m510127200 · Cited by 319

Lysosomes in iron metabolism, ageing and apoptosis

Kurz, T., Terman, A., Gustafsson, B., & Brunk, U. T. (2008) · Histochemistry and Cell Biology · doi:10.1007/s00418-008-0394-y · Cited by 302

SCFβTrCP-Mediated Degradation of Claspin Regulates Recovery from the DNA Replication Checkpoint Response

Peschiaroli, A., Dorrello, N. V., Guardavaccaro, D., Venere, M., Halazonetis, T., Sherman, N. E., & Pagano, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.013 · Cited by 289

Lysosomes and oxidative stress in aging and apoptosis

Kurz, T., Terman, A., Gustafsson, B., & Brunk, U. T. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.01.009 · Cited by 287

Iron homeostasis and toxicity in retinal degeneration

He, X., Hahn, P., Iacovelli, J., Wong, R., King, C., Bhisitkul, R., Massaro-Giordano, M., & Dunaief, J. L. (2007) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2007.07.004 · Cited by 260

Altered proteasome structure, function, and oxidation in aged muscle.

Ferrington, D. A., Husom, A. D., & Thompson, L. V. (2005) · The FASEB Journal · doi:10.1096/fj.04-2578fje · Cited by 259

Structural Principles of Tau and the Paired Helical Filaments of Alzheimer's Disease

Mandelkow, E., Von Bergen, M., Biernat, J., & Mandelkow, E. (2007) · Brain Pathology · doi:10.1111/j.1750-3639.2007.00053.x · Cited by 243

Extracellular tau is toxic to neuronal cells

Gómez-Ramos, A., Díaz-Hernández, M., Cuadros, R., Hernández, F., & Avila, J. (2006) · FEBS Letters · doi:10.1016/j.febslet.2006.07.078 · Cited by 241

Friedreich ataxia: the oxidative stress paradox

Seznec, H., Simon, D., Bouton, C., Reutenauer, L., Hertzog, A., Golik, P., Procaccio, V., Patel, M., Drapier, J.-C., Koenig, M., et al. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi042 · Cited by 219

Mitochondrial alterations Alzheimer's disease

Baloyannis, S. J., Costa, V., & Michmizos, D. (2004) · American Journal of Alzheimer's Disease & Other Dementias® · doi:10.1177/153331750401900205 · Cited by 206

Drusen deposits associated with aging and age-related macular degeneration contain nonfibrillar amyloid oligomers

Luibl, V. (2006) · Journal of Clinical Investigation · doi:10.1172/jci25843 · Cited by 203

Fibroblast cultures from healthy centenarians have an active proteasome

Chondrogianni, N., Petropoulos, I., Franceschi, C., Friguet, B., & Gonos, E. S. (2000) · Experimental Gerontology · doi:10.1016/s0531-5565(00)00137-6 · Cited by 200

Insulin sensitivity of protein and glucose metabolism in human forearm skeletal muscle

Louard, R. J., Fryburg, D. A., Gelfand, R. A., & Barrett, E. J. (1992) · Journal of Clinical Investigation · doi:10.1172/jci116124 · Cited by 169

Extended peptide-based inhibitors efficiently target the proteasome and reveal overlapping specificities of the catalytic β-subunits

Kessler, B. M., Tortorella, D., Altun, M., Kisselev, A. F., Fiebiger, E., Hekking, B. G., Ploegh, H. L., & Overkleeft, H. S. (2001) · Chemistry & Biology · doi:10.1016/s1074-5521(01)00069-2 · Cited by 163

The lipofuscin fluorophore A2E perturbs cholesterol metabolism in retinal pigment epithelial cells

Lakkaraju, A., Finnemann, S. C., & Rodriguez-Boulan, E. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702504104 · Cited by 162

Iron Induced Oxidative Damage As a Potential Factor in Age-Related Macular Degeneration: The Cogan Lecture

Dunaief, J. L. (2006) · Investigative Opthalmology & Visual Science · doi:10.1167/iovs.06-0568 · Cited by 154

Structural Basis for Catalysis and Inhibition ofN-Glycan Processing Class I α1,2-Mannosidases

Vallée, F., Karaveg, K., Herscovics, A., Moremen, K. W., & Howell, P. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006927200 · Cited by 152

p97: The Cell's Molecular Purgatory?

Halawani, D., & Latterich, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.003 · Cited by 143

Frataxin interacts functionally with mitochondrial electron transport chain proteins

González-Cabo, P., Vázquez-Manrique, R. P., García-Gimeno, M. A., Sanz, P., & Palau, F. (2005) · Human Molecular Genetics · doi:10.1093/hmg/ddi214 · Cited by 140

The role of NF-κB/IκB proteins in cancer: implications for novel treatment strategies

Schwartz, S. A., Hernandez, A., & Mark Evers, B. (1999) · Surgical Oncology · doi:10.1016/s0960-7404(00)00012-8 · Cited by 132

Impact of ageing on proteasome structure and function in human lymphocytes

Carrard, G., Dieu, M., Raes, M., Toussaint, O., & Friguet, B. (2003) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(02)00356-4 · Cited by 131

IRON TOXICITY AS A POTENTIAL FACTOR IN AMD

WONG, R. W., RICHA, D. C., HAHN, P., GREEN, W. R., & DUNAIEF, J. L. (2007) · Retina · doi:10.1097/iae.0b013e318074c290 · Cited by 131

Does cellular iron dysregulation play a causative role in Parkinson’s disease?

Kaur, D., & Andersen, J. (2004) · Ageing Research Reviews · doi:10.1016/j.arr.2004.01.003 · Cited by 123

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

Early Alcoholic Liver Injury: Formation of Protein Adducts with Acetaldehyde and Lipid Peroxidation Products, and Expression of CYP 2E1 AND CYP 3A

Niemelä, O., Parkkila, S., Pasanen, M., Limuro, Y., Bradford, B., & Thurman, R. G. (1998) · Alcoholism: Clinical and Experimental Research · doi:10.1111/j.1530-0277.1998.tb05925.x · Cited by 107

Stress-induced premature senescence and replicative senescence are different phenotypes, proteomic evidence

Dierick, J.-F., Eliaers, F., Remacle, J., Raes, M., Fey, S. J., Larsen, P. M., & Toussaint, O. (2002) · Biochemical Pharmacology · doi:10.1016/s0006-2952(02)01171-1 · Cited by 95

Failure of protein quality control in amyotrophic lateral sclerosis

Kabashi, E., & Durham, H. D. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2006.06.006 · Cited by 90

Frataxin: its role in iron metabolism and the pathogenesis of Friedreich's ataxia

Becker, E., & Richardson, D. R. (2001) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/s1357-2725(00)00067-4 · Cited by 71

Involvement of the p97-Ufd1-Npl4 Complex in the Regulated Endoplasmic Reticulum-associated Degradation of Inositol 1,4,5-Trisphosphate Receptors

Alzayady, K. J., Panning, M. M., Kelley, G. G., & Richard Wojcikiewicz, J. H. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508890200 · Cited by 47

Role of advanced glycation end products in cellular signaling

Ott, C., Jacobs, K., Haucke, E., Navarrete Santos, A., Grune, T., & Simm, A. (2014) · Redox Biology · doi:10.1016/j.redox.2013.12.016 · Cited by 1,150

Advanced Glycation End Products and Oxidative Stress in Type 2 Diabetes Mellitus

Nowotny, K., Jung, T., Höhn, A., Weber, D., & Grune, T. (2015) · Biomolecules · doi:10.3390/biom5010194 · Cited by 1,095

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

Aging and Immune Function: Molecular Mechanisms to Interventions

Ponnappan, S., & Ponnappan, U. (2011) · Antioxidants & Redox Signaling · doi:10.1089/ars.2010.3228 · Cited by 339

Accelerated epithelial cell senescence in IPF and the inhibitory role of SIRT6 in TGF-β-induced senescence of human bronchial epithelial cells

Minagawa, S., Araya, J., Numata, T., Nojiri, S., Hara, H., Yumino, Y., Kawaishi, M., Odaka, M., Morikawa, T., Nishimura, S. L., et al. (2011) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00097.2010 · Cited by 323