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

Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,209

Aggresomes: A Cellular Response to Misfolded Proteins

Johnston, J. A., Ward, C. L., & Kopito, R. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1883 · Cited by 2,148

Aggresomes, inclusion bodies and protein aggregation

Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,942

The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis

Voges, D., Zwickl, P., & Baumeister, W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.1015 · Cited by 1,608

Cellular Defenses against Unfolded Proteins

Sherman, M. Y., & Goldberg, A. L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00177-5 · Cited by 996

Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity

Meng, L., Mohan, R., Kwok, B. H. B., Elofsson, M., Sin, N., & Crews, C. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10403 · Cited by 938

Impaired Proteasome Function in Alzheimer's Disease

Keller, J. N., Hanni, K. B., & Markesbery, W. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750436.x · Cited by 848

Antigen processing by the proteasome

Kloetzel, P. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056572 · Cited by 638

Rapid examination of muscle tissue

Engel, W. K., & Cunningham, G. G. (1963) · Neurology · doi:10.1212/wnl.13.11.919 · Cited by 585

Altered proteasomal function in sporadic Parkinson’s disease

St. P. McNaught, K., Belizaire, R., Isacson, O., Jenner, P., & Olanow, C. W. (2003) · Experimental Neurology · doi:10.1006/exnr.2002.8050 · Cited by 573

Dynamic Association of Proteasomal Machinery with the Centrosome

Wigley, W. C., Fabunmi, R. P., Lee, M. G., Marino, C. R., Muallem, S., Demartino, G., & Thomas, P. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.145.3.481 · Cited by 513

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

Ubiquitin Conjugation Is Not Required for the Degradation of Oxidized Proteins by Proteasome

Shringarpure, R., Grune, T., Mehlhase, J., & Davies, K. J. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206279200 · Cited by 438

Aggresomes Formed by α-Synuclein and Synphilin-1 Are Cytoprotective

Tanaka, M., Kim, Y. M., Lee, G., Junn, E., Iwatsubo, T., & Mouradian, M. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m310994200 · Cited by 434

Proteasomal Inhibition by α-Synuclein Filaments and Oligomers

Lindersson, E., Beedholm, R., Højrup, P., Moos, T., Gai, W., Hendil, K. B., & Jensen, P. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m306390200 · Cited by 409

Hassles with Taking Out the Garbage: Aggravating Aggresomes

García‐Mata, R., Gao, Y., & Sztul, E. S. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.30602.x · Cited by 387

Protein degradation and the generation of MHC class I-presented peptides

Rock, K. L., York, I. A., Šarić, T., & Goldberg, A. L. (2002) · Advances in immunology · doi:10.1016/s0065-2776(02)80012-8 · Cited by 342

Inhibition of the ubiquitin-proteasome system in Alzheimer's disease

Lam, Y. A., Pickart, C. M., Alban, A., Landon, M., Jamieson, C., Ramage, R., Mayer, R. J., & Layfield, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170173897 · Cited by 329

Sequential phosphorylation of Tau by glycogen synthase kinase‐3β and protein kinase A at Thr212 and Ser214 generates the Alzheimer‐specific epitope of antibody AT100 and requires a paired‐helical‐filament‐like conformation

Zheng‐Fischhöfer, Q., Biernat, J., Mandelkow, E., Illenberger, S., Godemann, R., & Mandelkow�, E. (1998) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1998.2520542.x · Cited by 322

Aggresome‐related biogenesis of Lewy bodies

McNaught, K. S. P., Shashidharan, P., Perl, D. P., Jenner, P. G., & Olanow, C. W. (2002) · European Journal of Neuroscience · doi:10.1046/j.1460-9568.2002.02301.x · Cited by 279

Amyloid β-Protein Inhibits Ubiquitin-dependent Protein Degradation in Vitro

Gregori, L. L., Fuchs, C., Figueiredo‐Pereira, M. E., Nostrand, W. E. V., & Goldgaber, D. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.34.19702 · Cited by 239

Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation

Lindsten, K., de Vrij, F. M. S., Verhoef, L. G. G. C., Fischer, D. F., van Leeuwen, F. W., Hol, E. M., Masucci, M. G., & Dantuma, N. P. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200111034 · Cited by 220

Altered proteasome function and subunit composition in aged muscle

Husom, A. D., Peters, E. A., Kolling, E. A., Fugere, N. A., Thompson, L. V., & Ferrington, D. A. (2003) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2003.10.010 · Cited by 203

Recognition of Alzheimer paired helical filaments by monoclonal neurofilament antibodies is due to crossreaction with tau protein.

Nukina, N., Kosik, K. S., & Selkoe, D. J. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.10.3415 · Cited by 199

Endoplasmic Reticulum Stress and Unfolded Protein Response in Inclusion Body Myositis Muscle

Vattemi, G. N. A., Engel, W. K., McFerrin, J., & Askanas, V. (2004) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)63089-1 · Cited by 186

Danger — misfolding proteins

Ellis, R. J., & Pinheiro, T. J. T. (2002) · Nature · doi:10.1038/416483a · Cited by 162

Relationship between β-amyloid degradation and the 26S proteasome in neural cells

Salon, M. L., Pasquini, L. A., Moreno, M. B., Pasquini, J. M., & Soto, E. F. (2003) · Experimental Neurology · doi:10.1016/s0014-4886(02)00060-2 · Cited by 161

Ubiquitinylation Is Not an Absolute Requirement for Degradation of c-Jun Protein by the 26 S Proteasome

Jariel‐Encontre, I., Pariât, M., Carillo, S., Salvai, C., Piechaczyk, M., & Martini, F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.19.11623 · Cited by 147

Protein surveillance machinery in brains with spinocerebellar ataxia type 3: Redistribution and differential recruitment of 26S proteasome subunits and chaperones to neuronal intranuclear inclusions

Schmidt, T., Lindenberg, K. S., Krebs, A., Schöls, L. J., Laccone, F. A., Herms, J. W., Rechsteiner, M., Rieß, O., & Landwehrmeyer, G. B. (2002) · Annals of Neurology · doi:10.1002/ana.10101 · Cited by 146

Parkin Accumulation in Aggresomes Due to Proteasome Impairment

Junn, E., Lee, S. S., Suhr, U. T., & Mouradian, M. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203159200 · Cited by 144

Transfer of beta-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle.

Askanas, V., McFerrin, J., Baqué, S., Alvarez, R. B., Sarkozi, E., & Engel, W. K. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.3.1314 · Cited by 140

β‐Amyloid precursor epitopes in muscle fibers of inclusion body myositis

Askanas, V., Alvarez, R. B., & Engel, W. K. (1993) · Annals of Neurology · doi:10.1002/ana.410340408 · Cited by 139

Inclusion-Body Myositis: Newest Concepts of Pathogenesis and Relation to Aging and Alzheimer Disease

Askanas, V., & Engel, W. K. (2001) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/60.1.1 · Cited by 139

Expression of the Costimulatory Molecule BB-1, the Ligands CTLA-4 and CD28, and their mRNA in Inflammatory Myopathies

Murata, K., & Dalakas, M. C. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65141-3 · Cited by 112

Enhanced detection of Congo‐red‐positive amyloid deposits in muscle fibers of inclusion body myositis and brain of Alzheimer's disease using fluorescence technique

Askanas, V., Engel, W. K., & Alvarez, R. B. (1993) · Neurology · doi:10.1212/wnl.43.6.1265-a · Cited by 112

Novel Immunolocalization of α‐Synuclein in Human Muscle of Inclusion‐Body Myositis, Regenerating and Necrotic Muscle Fibers, and at Neuromuscular Junctions

Askanas, V., Engel, W., Alvarez, R. B., Mcferrin, J., & Broccolini, A. (2000) · Journal of Neuropathology and Experimental Neurology · doi:10.1093/jnen/59.7.592 · Cited by 107

Proteasomal Expression, Induction of Immunoproteasome Subunits, and Local MHC Class I Presentation in Myofibrillar Myopathy and Inclusion Body Myositis

Ferrer, I., Martín, B., Castaño, J. G., Lucas, J. J., Moreno, D., & Olivé, M. (2004) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/63.5.484 · Cited by 95

The unfolding of substrates and ubiquitin-independentprotein degradation by proteasomes

Benaroudj, N., Tarcsa, E., Cascio, P., & Goldberg, A. L. (2001) · Biochimie · doi:10.1016/s0300-9084(01)01244-5 · Cited by 93

Glutathiolation of the Proteasome Is Enhanced by Proteolytic Inhibitors

Demasi, M., Shringarpure, R., & Davies, K. J. A. (2001) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2332 · Cited by 84

Proposed pathogenetic cascade of inclusion-body myositis: importance of amyloid-β, misfolded proteins, predisposing genes, and aging

Askanas, V., & Engel, W. K. (2003) · Current Opinion in Rheumatology · doi:10.1097/00002281-200311000-00009 · Cited by 80

ADDLs & protofibrils —the missing links?

Klein, W. L. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00312-8 · Cited by 77

Mutant ubiquitin UBB +1 is accumulated in sporadic inclusion-body myositis muscle fibers

Fratta, P., Engel, W. K., van Leeuwen, F. W., Hol, E. M., Vattemi, G. N. A., & Askanas, V. (2004) · Neurology · doi:10.1212/01.wnl.0000138574.56908.5d · Cited by 60

βAPP gene transfer into cultured human muscle induces inclusion-body myositis aspects

Askanas, V., McFerrin, J., Alvarez, R. B., Baqué, S., & Engel, W. K. (1997) · Neuroreport · doi:10.1097/00001756-199707070-00012 · Cited by 59

Use of anti‐neurofilament antibody to identify paired‐helical filaments in inclusion‐body myositis

Askanas, V., Alvarez, R. B., Massimiliano Mirabella, A., & Engel, W. K. (1996) · Annals of Neurology · doi:10.1002/ana.410390318 · Cited by 55

The molecular and cellular pathology of inflammatory muscle diseases

Dalakas, M. C. (2001) · Current Opinion in Pharmacology · doi:10.1016/s1471-4892(01)00053-4 · Cited by 51

Cystatin C colocalizes with amyloid‐β and coimmunoprecipitates with amyloid‐β precursor protein in sporadic inclusion‐body myositis muscles

Vattemi, G. N. A., Engel, W. K., McFerrin, J., & Askanas, V. (2003) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2003.01798.x · Cited by 37

Structure/function in neuroprotection and apoptosis

Borden, K. L. B. (1998) · Annals of Neurology · doi:10.1002/ana.410440711 · Cited by 21

How citation distortions create unfounded authority: analysis of a citation network

Greenberg, S. A. (2009) · BMJ · doi:10.1136/bmj.b2680 · Cited by 499

The proteasomal system

Jung, T., Catalgol, B., & Grune, T. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.04.001 · Cited by 401

Mechanisms of proteasome inhibitor action and resistance in cancer

McConkey, D. J., & Zhu, K. (2008) · Drug Resistance Updates · doi:10.1016/j.drup.2008.08.002 · Cited by 313

Inclusion body myositis: current pathogenetic concepts and diagnostic and therapeutic approaches

Needham, M., & Mastaglia, F. L. (2007) · The Lancet Neurology · doi:10.1016/s1474-4422(07)70171-0 · Cited by 269

Protein Folding and Aggregation into Amyloid: The Interference by Natural Phenolic Compounds

Stefani, M., & Rigacci, S. (2013) · International Journal of Molecular Sciences · doi:10.3390/ijms140612411 · Cited by 245

Novel identification of aggresomes in sporadic inclusion-body myositis (s-IBM) muscle fibers suggests that inhibition of 26S/20S proteasome and misfolded proteins play a pathogenic role

Fratta, P., Engel, W. K., & Askanas, V (2003) · UCL Discovery (University College London) · Cited by 2

AβPP-overexpression and proteasome inhibition increase αB-crystallin in cultured human muscle: Relevance to inclusion-body myositis

Wojcik, S. P., Engel, W. K., McFerrin, J., Paciello, O., & Askanas, V. (2006) · Neuromuscular Disorders · doi:10.1016/j.nmd.2006.08.009 · Cited by 31

G.P.2 02 In cultured human muscle fibers (CHMFs) amyloid-β precursor protein (AβPP) and proteasome inhibition increase αB-crystallin (αBC). Relevance to sporadic inclusion-body myositis (s-IBM)

Wojcik, S. P., Engel, W. K., McFerrin, J., Paciello, O., & Askanas, V. (2006) · Neuromuscular Disorders · doi:10.1016/j.nmd.2006.05.056 · Cited by 1

Sporadic inclusion-body myositis: a proposed key pathogenetic role of the abnormalities of the ubiquitin-proteasome system, and protein misfolding and aggregation.

Askanas, V., & Engel, W. K. (2005) · PubMed · Cited by 12

Inclusion Body Myositis: A Degenerative Muscle Disease Associated with Intra‐Muscle Fiber Multi‐Protein Aggregates, Proteasome Inhibition, Endoplasmic Reticulum Stress and Decreased Lysosomal Degradation

Askanas, V., Engel, W. K., & Nogalska, A. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2009.00290.x · Cited by 139