Proteasome Inhibition and Aggresome Formation in Sporadic Inclusion-Body Myositis and in Amyloid-β Precursor Protein-Overexpressing Cultured Human Muscle Fibers
Open accessAbstract
The 26S proteasome system is involved in eliminating various proteins, including ubiquitinated misfolded/unfolded proteins, and its inhibition results in cellular accumulation of protein aggregates. Intramuscle-fiber ubiquitinated multiprotein-aggregates are characteristic of sporadic inclusion-body myositis (s-IBM) muscle fibers. Two major types of aggregates exist, containing either amyloid-beta (Abeta) or phosphorylated tau (p-tau). We have now asked whether abnormalities of the 26S proteasome contribute to s-IBM pathogenesis and whether the multiprotein aggregates have features of aggresomes. Using cultured human muscle fibers we also studied the effect of amyloid-beta precursor protein (AbetaPP) overexpression on proteasome function and the influence of proteasome inhibition on aggresome formation. We report that in s-IBM muscle biopsies 26S proteasome subunits were immunodetected in the gamma-tubulin-associated aggresomes, which also contained Abeta, p-tau, ubiquitin, and HSP70. In addition, a) expression of proteasome subunits was greatly increased, b) the 20Salpha proteasome subunit co-immunoprecipitated with AbetaPP/Abeta, and c) the three major proteasomal proteolytic activities were reduced. In cultured muscle fibers, AbetaPP-overexpressing fibers displayed diminished proteasomal proteolytic activities, and addition of proteasome inhibitor strikingly increased aggresome formation. Accordingly, proteasome dysfunction in s-IBM muscle fibers may play a role in accumulation of misfolded, potentially cytotoxic proteins and may be induced by increased intracellular AbetaPP/Abeta.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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 muscle, an association between proteasome abnormalities and muscle disease has been reported.
“In muscle, an association between proteasome abnormalities and muscle disease has also been reported (Fratta et al., 2005; Askanas and Engel, 2006).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Fratta et al., 2005
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
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 2,192 · see citing works
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 · see citing works
Aggresomes, inclusion bodies and protein aggregation
Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,906 · see citing works
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
Voges, D., Zwickl, P., & Baumeister, W. P. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.1015 · Cited by 1,894 · see citing works
Cellular Defenses against Unfolded Proteins
Sherman, M. Y., & Goldberg, A. L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00177-5 · Cited by 984 · see citing works
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 926 · see citing works
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 · see citing works
Antigen processing by the proteasome
Kloetzel, P. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056572 · Cited by 638 · see citing works
Rapid examination of muscle tissue
Engel, W. K., & Cunningham, G. G. (1963) · Neurology · doi:10.1212/wnl.13.11.919 · Cited by 585 · see citing works
Self-citationAltered 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 · see citing works
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 · 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
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 · see citing works
Self-citationAggresomes 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 421 · see citing works
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 399 · see citing works
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 · see citing works
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 337 · see citing works
Inhibition of the ubiquitin-proteasome system in Alzheimer's disease
Lam, Y. A., Pickart, C. M., Alban, A., Landon, M., Jamieson, C. J., Ramage, R., Mayer, R. J., & Layfield, R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170173897 · Cited by 325 · see citing works
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 · see citing works
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 277 · see citing works
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 232 · see citing works
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 · see citing works
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 · see citing works
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 198 · see citing works
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 184 · see citing works
Self-citationEllis, R. J., & Pinheiro, T. J. T. (2002) · Nature · doi:10.1038/416483a · Cited by 161 · see citing works
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 157 · see citing works
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 · see citing works
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 · see citing works
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 · see citing works
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 141 · see citing works
Self-citationAskanas, 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 · see citing works
Self-citationβ‐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 · see citing works
Self-citationAskanas, V., Engel, W. K., & Alvarez, R. B. (1993) · Neurology · doi:10.1212/wnl.43.6.1265-a · Cited by 114 · see citing works
Self-citationMurata, K., & Dalakas, M. C. (1999) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)65141-3 · Cited by 112 · see citing works
Askanas, V., Engel, W. K., Alvarez, R. B., McFerrin, J., & Broccolini, A. (2000) · Journal of Neuropathology & Experimental Neurology · doi:10.1093/jnen/59.7.592 · Cited by 101 · see citing works
Self-citationFerrer, 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 · see citing works
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 · see citing works
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 · see citing works
Self-citationAskanas, V., & Engel, W. K. (2003) · Current Opinion in Rheumatology · doi:10.1097/00002281-200311000-00009 · Cited by 80 · see citing works
Self-citationADDLs & protofibrils —the missing links?
Klein, W. L. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00312-8 · Cited by 77 · see citing works
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 · see citing works
Self-citationβAPP 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 · see citing works
Self-citationUse 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 · see citing works
Self-citationThe 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 · see citing works
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 · see citing works
Self-citationStructure/function in neuroprotection and apoptosis
Borden, K. L. B. (1998) · Annals of Neurology · doi:10.1002/ana.410440711 · Cited by 21 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- Kim KS, Wen GY, Bancher C, Chen J, Sapienza V, Hong H, Wisniewski HM: Detection and quantitation of amyloid B-peptide with 2 monoclonal antibodies. Neurosci Res Commun 1990, 7:113-122
Cited by
Sorted by citations
How citation distortions create unfounded authority: analysis of a citation network
Greenberg, S. A. (2009) · BMJ · doi:10.1136/bmj.b2680 · Cited by 499 · see citing works
Jung, T., Catalgol, B., & Grune, T. (2009) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2009.04.001 · Cited by 389 · see citing works
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 309 · see citing works
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 · see citing works
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 239 · see citing works
Sporadic inclusion body myositis—diagnosis, pathogenesis and therapeutic strategies
Dalakas, M. C. (2006) · Nature Clinical Practice Neurology · doi:10.1038/ncpneuro0261 · Cited by 229 · see citing works
Review: An update on inflammatory and autoimmune myopathies
Dalakas, M. C. (2010) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2010.01153.x · Cited by 195 · see citing works
Kitajima, Y., Yoshioka, K., & Suzuki, N. (2020) · The Journal of Physiological Sciences · doi:10.1186/s12576-020-00768-9 · Cited by 171 · see citing works
Askanas (2006) · doi:10.1212/01.wnl.0000192128.13875.1e · Cited by 168 · see citing works
Self-citationNogalska, A., Terracciano, C., D’Agostino, C., Engel, W. K., & Askanas, V. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0564-6 · Cited by 144 · see citing works
Self-citationAskanas, V., Engel, W. K., & Nogalska, A. (2009) · Brain Pathology · doi:10.1111/j.1750-3639.2009.00290.x · Cited by 138 · see citing works
Self-citationβ‐Amyloid is a substrate of autophagy in sporadic inclusion body myositis
Lünemann, J. D., Schmidt, J., Schmid, D., Barthel, K., Wrede, A., Dalakas, M. C., & Münz, C. (2007) · Annals of Neurology · doi:10.1002/ana.21115 · Cited by 129 · see citing works
Benvéniste, O., Stenzel, W., Hilton‐Jones, D., Sandri, M., Boyer, O., & van Engelen, B. G. M. (2015) · Acta Neuropathologica · doi:10.1007/s00401-015-1384-5 · Cited by 124 · see citing works
Askanas, V., & Engel, W. K. (2008) · Acta Neuropathologica · doi:10.1007/s00401-008-0449-0 · Cited by 122 · see citing works
Self-citationNogalska, 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
Self-citationThe Immunoproteasome in oxidative stress, aging, and disease
Johnston-Carey, H. K., Pomatto, L. C. D., & Davies, K. J. A. (2016) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2016.1172554 · Cited by 110 · see citing works
Self-citationRoué, G., Pérez‐Galán, P., Mozos, A., López‐Guerra, M., Xargay‐Torrent, S., Rosich, L., Saborit-Villarroya, I., Normant, E., Campo, E., & Colomer, D. (2010) · Blood · doi:10.1182/blood-2010-04-278853 · Cited by 109 · see citing works
Askanas, V., Engel, W. K., & Nogalska, A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2014.09.005 · Cited by 106 · see citing works
Self-citationGrimm, S., Höhn, A., Davies, K. J. A., & Grune, T. (2010) · Free Radical Research · doi:10.3109/10715762.2010.512040 · Cited by 108 · see citing works
Self-citationStefani, M., & Rigacci, S. (2014) · BioFactors · doi:10.1002/biof.1171 · Cited by 105 · see citing works
Weihl, C. C., Miller, S., Hanson, P. I., & Pestronk, A. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm037 · Cited by 103 · see citing works
Askanas, V., & Engel, W. K. (2007) · Current Opinion in Rheumatology · doi:10.1097/bor.0b013e3282efdc7c · Cited by 97 · see citing works
Self-citationDalakas, M. C., Rakočević, G., Shatunov, A., Goldfarb, L. G., Raju, R. P., & Salajegheh, M. K. (2007) · Annals of Neurology · doi:10.1002/ana.21103 · Cited by 96 · see citing works
Mimnaugh, E. G., Xu, W., Vos, M. D., Yuan, X., & Neckers, L. (2006) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0019 · Cited by 96 · see citing works
Nizzari, M., Venezia, V., Repetto, E., Caorsi, V., Magrassi, R., Gagliani, M. C., Carlo, P., Florio, T., Schettini, G., Tacchetti, C., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610146200 · Cited by 93 · see citing works
Inclusion Body Myositis: Update on Pathogenesis and Treatment
Naddaf, E., Barohn, R. J., & Dimachkie, M. M. (2018) · Neurotherapeutics · doi:10.1007/s13311-018-0658-8 · Cited by 89 · see citing works
Parkin Protects against Mitochondrial Toxins and β-Amyloid Accumulation in Skeletal Muscle Cells
Rosen, K. M., Veereshwarayya, V., Moussa, C., Fu, Q., Goldberg, M. S., Schlossmacher, M. G., Shen, J., & Querfurth, H. W. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512649200 · Cited by 84 · see citing works
Proteasome dysfunction induces muscle growth defects and protein aggregation
Kitajima, Y., Tashiro, Y., Suzuki, N., Warita, H., Kato, M., Tateyama, M., Ando, R., Izumi, R., Yamazaki, M., Abe, M., et al. (2014) · Journal of Cell Science · doi:10.1242/jcs.150961 · Cited by 79 · see citing works
“Proteasomal activity in the muscles of patients with sIBM is reported as either activated or suppressed (Ferrer et al., 2005; Fratta et al., 2005); thus, multiple pathological mechanisms might be involved.”
BackgroundAskanas, V., & Engel, W. K. (2011) · La Presse Médicale · doi:10.1016/j.lpm.2010.11.024 · Cited by 76 · see citing works
Self-citationAskanas, V., Engel, W. K., & Nogalska, A. (2012) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31826183c8 · Cited by 72 · see citing works
Self-citationKitazawa, M., Green, K. N., Caccamo, A., & LaFerla, F. M. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.051232 · Cited by 70 · see citing works
Genetics and aetiology of Pagetic disorders of bone
Helfrich, M., & Hocking, L. J. (2008) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2008.02.045 · Cited by 67 · see citing works
Nogalska, A., Engel, W. K., McFerrin, J., Kokame, K., Komano, H., & Askanas, V. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.03668.x · Cited by 63 · see citing works
Self-citationSporadic inclusion body myositis: a continuing puzzle
Needham, M., & Mastaglia, F. L. (2007) · Neuromuscular Disorders · doi:10.1016/j.nmd.2007.11.001 · Cited by 63 · see citing works
D’Agostino, C., Nogalska, A., Cacciottolo, M., Engel, W. K., & Askanas, V. (2011) · Acta Neuropathologica · doi:10.1007/s00401-011-0874-3 · Cited by 58 · see citing works
Self-citationVattemi, G. N. A., Nogalska, A., Engel, W. K., D’Agostino, C., Checler, F., & Askanas, V. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0511-6 · Cited by 58 · see citing works
Self-citationAtkin, T. A., Brandon, N. J., & Kittler, J. T. (2012) · Human Molecular Genetics · doi:10.1093/hmg/dds018 · Cited by 57 · see citing works
Monis, G. F., Schultz, C., Ren, R., Eberhard, J., Costello, C. E., Connors, L. H., Skinner, M. M., & Trinkaus‐Randall, V. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.060183 · Cited by 57 · see citing works
Nogalska, A., Wojcik, S. P., Engel, W. K., McFerrin, J., & Askanas, V. (2006) · Experimental Neurology · doi:10.1016/j.expneurol.2006.12.014 · Cited by 54 · see citing works
Self-citationFunctional Protein Aggregates: Just the Tip of the Iceberg
Villaverde, A., Corchero, J. L., Seras‐Franzoso, J., & García‐Fruitós, E. (2015) · Nanomedicine · doi:10.2217/nnm.15.125 · Cited by 51 · see citing works
Immune and myodegenerative pathomechanisms in inclusion body myositis
Keller, C. W., Schmidt, J., & Lünemann, J. D. (2017) · Annals of Clinical and Translational Neurology · doi:10.1002/acn3.419 · Cited by 51 · see citing works
Molecular pathology and pathogenesis of inclusion‐body myositis
Askanas, V., & Engel, W. K. (2005) · Microscopy Research and Technique · doi:10.1002/jemt.20186 · Cited by 50 · see citing works
Self-citationBhattarai, S., Ghannam, K., Krause, S., Benvéniste, O., Marg, A., de Bruin, G., Xin, B., Overkleeft, H. S., Spuler, S., Stenzel, W., et al. (2016) · Journal of Autoimmunity · doi:10.1016/j.jaut.2016.08.004 · Cited by 46 · see citing works
Unfolded Protein Response and Activated Degradative Pathways Regulation in GNE Myopathy
Li, H., Chen, Q., Liu, F., Zhang, X., Li, W., Liu, S., Zhao, Y., Gong, Y., & Yan, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0058116 · Cited by 41 · see citing works
Novel demonstration of amyloid-β oligomers in sporadic inclusion-body myositis muscle fibers
Nogalska, A., D’Agostino, C., Engel, W. K., Klein, W. L., & Askanas, V. (2010) · Acta Neuropathologica · doi:10.1007/s00401-010-0737-3 · Cited by 42 · see citing works
Self-citationRole of non-immune mechanisms of muscle damage in idiopathic inflammatory myopathies
Coley, W., Rayavarapu, S., & Nagaraju, K. (2012) · Arthritis Research & Therapy · doi:10.1186/ar3791 · Cited by 39 · see citing works
Proteasome function is required to maintain muscle cellular architecture.
Haas, K. F., Woodruff, E., & Broadie, K. (2007) · Biology of the Cell · doi:10.1042/bc20070019 · Cited by 38 · see citing works
Terracciano, C., Nogalska, A., Engel, W. K., & Askanas, V. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06461.x · Cited by 38 · see citing works
Self-citationWojcik, S. P., Engel, W. K., Yan, R., McFerrin, J., & Askanas, V. (2007) · Acta Neuropathologica · doi:10.1007/s00401-007-0281-y · Cited by 38 · see citing works
Self-citationLiu, H.-Y., & Pfleger, C. M. (2013) · PLoS ONE · doi:10.1371/journal.pone.0032835 · Cited by 37 · see citing works
Proteomic Analysis of Inclusion Body Myositis
Li, J., Yin, C., Okamoto, H., Jaffe, H., Oldfield, E. H., Zhuang, Z., Vortmeyer, A. O., & Rushing, E. J. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000228204.19915.69 · Cited by 35 · see citing works
D’Agostino, C., Nogalska, A., Engel, W. K., & Askanas, V. (2010) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2010.01108.x · Cited by 33 · see citing works
Self-citationInclusion body myositis: from immunopathology and degenerative mechanisms to treatment perspectives
Schmidt, J., & Dalakas, M. C. (2013) · Expert Review of Clinical Immunology · doi:10.1586/1744666x.2013.842467 · Cited by 32 · see citing works
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 · see citing works
Self-citationIn inclusion-body myositis muscle fibers Parkinson-associated DJ-1 is increased and oxidized
Terracciano, C., Nogalska, A., Engel, W. K., Wojcik, S. P., & Askanas, V. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2008.05.030 · Cited by 32 · see citing works
Self-citationCacciottolo, M., Nogalska, A., D’Agostino, C., Engel, W. K., & Askanas, V. (2013) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12038 · Cited by 29 · see citing works
Self-citationAntigenemia, RNAemia, and innate immunity in children with acute rotavirus diarrhea
Moon, S.-S., Wang, Y., Dennehy, P. H., Simonsen, K. A., Zhang, J. H., & Jiang, B. (2011) · FEMS Immunology & Medical Microbiology · doi:10.1111/j.1574-695x.2011.00923.x · Cited by 27 · see citing works
DNAJB2 Expression in Normal and Diseased Human and Mouse Skeletal Muscle
Claeys, K. G., Sozanska, M., Martin, J., Lacène, E., Vignaud, L., Stockholm, D., Laforêt, P., Eymard, B., Kichler, A., Scherman, D., et al. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090663 · Cited by 26 · see citing works
Peron, M., Bonvini, P., & Rosolen, A. (2012) · BMC Cancer · doi:10.1186/1471-2407-12-233 · Cited by 25 · see citing works
A Dual Role for HSP90 and HSP70 in the Inflammatory Myopathies
Paepe, B. D., Creus, K. K., Martin, J., Weis, J., & Bleecker, J. D. (2009) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2009.04812.x · Cited by 24 · see citing works
Ikezoe, K., Furuya, H., Arahata, H., Nakagawa, M. M., Tateishi, T., Fujii, N., & Kira, J. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0488-1 · Cited by 24 · see citing works
Guglielmi, V., Cheli, M., Tonin, P., & Vattemi, G. N. A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25052742 · Cited by 20 · see citing works
Decreased SIRT1 deacetylase activity in sporadic inclusion-body myositis muscle fibers
Nogalska, A., D’Agostino, C., Engel, W. K., Davies, K. J. A., & Askanas, V. (2008) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2008.08.021 · Cited by 22 · see citing works
Self-citationAutoimmune Myopathies: Where Do We Stand?
Simon, J.-P., Marié, I., Jouen, F., Boyer, O., & Martinet, J. (2016) · Frontiers in Immunology · doi:10.3389/fimmu.2016.00234 · Cited by 21 · see citing works
Cellular Stress in the Pathogenesis of Muscular Disorders—From Cause to Consequence
Mensch, A., & Zierz, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21165830 · Cited by 21 · see citing works
Inclusion body myositis: The interplay between ageing, muscle degeneration and autoimmunity
McLeish, E., Slater, N., Sooda, A., Wilson, A., Coudert, J. D., Lloyd, T. E., & Needham, M. (2022) · Best Practice & Research Clinical Rheumatology · doi:10.1016/j.berh.2022.101761 · Cited by 20 · see citing works
Innovative pathological network‐based multitarget approaches for Alzheimer's disease treatment
Mayo, P., Pascual-Guerra, J., Crisman, E., Domínguez, C., López, M. G., & Leon, R. M. (2024) · Medicinal Research Reviews · doi:10.1002/med.22045 · Cited by 19 · see citing works
Nogalska, A., D’Agostino, C., Engel, W. K., Cacciottolo, M., Asada, S., Mori, K., & Askanas, V. (2015) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0000000000000196 · Cited by 20 · see citing works
Self-citationZschüntzsch, J., Meyer, S., Shahriyari, M., Kummer, K., Schmidt, M., Kummer, S., & Tiburcy, M. (2022) · Cells · doi:10.3390/cells11071233 · Cited by 18 · see citing works
NLRP3 Inflammasome Activation and Altered Mitophagy Are Key Pathways in Inclusion Body Myositis
Naddaf, E., Nguyen, T. K. O., Watzlawik, J. O., Gao, H., Hou, X., Fiesel, F. C., Mandrekar, J. N., Kokesh, E., Harmsen, W. S., Lanza, I. R., et al. (2024) · Journal of Cachexia Sarcopenia and Muscle · doi:10.1002/jcsm.13672 · Cited by 17 · see citing works
Inclusion Body Myositis: A View from the Caenorhabditis elegans Muscle
Rebolledo, D. L., Minniti, A. N., Grez, P. M., Fadić, R., Kohn, R. E., & Inestrosa, N. C. (2008) · Molecular Neurobiology · doi:10.1007/s12035-008-8041-0 · Cited by 16 · see citing works
Wojcik, S. P., Nogalska, A., McFerrin, J., Engel, W. K., Olędzka, G., & Askanas, V. (2007) · Neuropathology and Applied Neurobiology · doi:10.1111/j.1365-2990.2006.00821.x · Cited by 17 · see citing works
Self-citationInclusion body myositis: new insights into pathogenesis
Garlepp, M. J., & Mastaglia, F. L. (2008) · Current Opinion in Rheumatology · doi:10.1097/bor.0b013e328313644c · Cited by 15 · see citing works
Nogalska, A., D’Agostino, C., Engel, W. K., & Askanas, V. (2012) · Neurobiology of Disease · doi:10.1016/j.nbd.2012.06.008 · Cited by 14 · see citing works
Self-citationNogalska, A., D’Agostino, C., Engel, W. K., & Askanas, V. (2011) · Neuroscience Letters · doi:10.1016/j.neulet.2011.08.042 · Cited by 14 · see citing works
Self-citationInducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy
Kitajima, Y., Suzuki, N., Yoshioka, K., Izumi, R., Tateyama, M., Tashiro, Y., Takahashi, R., Aoki, M., & Ono, Y. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.00859 · Cited by 14 · see citing works
“In muscle, an association between proteasome abnormalities and muscle disease has also been reported (Fratta et al., 2005; Askanas and Engel, 2006).”
BackgroundAdvances in the immunobiology and treatment of inflammatory myopathies
Dalakas, M. C. (2007) · Current Rheumatology Reports · doi:10.1007/s11926-007-0047-5 · Cited by 13 · see citing works
Proteasome Biology: Chemistry and Bioengineering Insights
Račková, L., & Csekes, E. (2020) · Polymers · doi:10.3390/polym12122909 · Cited by 13 · see citing works
Corchero, J. L. (2015) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-015-7107-y · Cited by 12 · see citing works
Spatial sequestration of misfolded proteins in neurodegenerative diseases
Rolli, S., & Sontag, E. M. (2022) · Biochemical Society Transactions · doi:10.1042/bst20210862 · Cited by 13 · see citing works
Idiopathic Inflammatory Myopathies: Recent Evidence Linking Pathogenesis and Clinical Features
Martins, E. F., Cappello, C. H., Shinjo, S. K., Appenzeller, S., & de Souza, J. M. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26073302 · Cited by 10 · see citing works
Pathological mechanisms of vacuolar aggregate myopathy arising from a Casq1 mutation
Hanna, A. D., Lee, C. S., Babcock, L. W., Wang, H. J., Recio, J., & Hamilton, S. L. (2021) · The FASEB Journal · doi:10.1096/fj.202001653rr · Cited by 10 · see citing works
Revisiting the Role of GSK3, A Modulator of Innate Immunity, in Idiopathic Inclusion Body Myositis
Piazzi, M., Bavelloni, A., Cenni, V., Faenza, I., & Blalock, W. L. (2021) · Cells · doi:10.3390/cells10113255 · Cited by 10 · see citing works
Lee, E. H., & Neppl, R. L. (2021) · Genes · doi:10.3390/genes12050688 · Cited by 10 · see citing works
The pathogenesis of osteoclast diseases: Some knowns, but still many unknowns
Helfrich, M., Crockett, J. C., Hocking, L. J., & Coxon, F. P. (2007) · BoneKEy-Osteovision · doi:10.1138/20060249 · Cited by 9 · see citing works
Inclusion-Body Myositis in the Elderly: An Update
Schmidt, J., & Dalakas, M. C. (2010) · Aging Health · doi:10.2217/ahe.10.64 · Cited by 8 · see citing works
Tong, J., Lang, J., & Zhu, L. (2010) · International Urogynecology Journal · doi:10.1007/s00192-010-1222-1 · Cited by 7 · see citing works
Vacuolar myopathy in a dog resembling human sporadic inclusion body myositis
King, J., LeCouteur, R. A., Aleman, M. R., Williams, D. C., Moore, P. F., Guo, L. T., Mizisin, A. P., & Shelton, G. D. (2009) · Acta Neuropathologica · doi:10.1007/s00401-009-0588-y · Cited by 7 · see citing works
Inclusion body myositis and immunosenescence: current evidence and future perspectives
Allameen, N. A., Salam, S., Reddy, V. R., & Machado, P. (2024) · Lara D. Veeken · doi:10.1093/rheumatology/keae614 · Cited by 6 · see citing works
Wu, J., Tang, J., Huang, D., Wang, Y., Zhou, E., Ru, Q., Xu, G., Chen, L., & Wu, Y. (2024) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2024.1482947 · Cited by 7 · see citing works
Treatment strategies for inclusion body myositis
Breithaupt, M., & Schmidt, J. (2014) · Expert Opinion on Orphan Drugs · doi:10.1517/21678707.2014.966688 · Cited by 5 · see citing works
Apoptosis induced by proteasome inhibition in human myoblast cultures.
Sassone, J., Ciammola, A., Tiloca, C., Glionna, M., Meola, G., Mancinelli, E., & Silani, V. (2006) · PubMed · doi:10.4081/981 · Cited by 5 · see citing works
Inflammatory and Autoimmune Features of Inclusion‐Body Myositis
Dalakas, M. C. (2011) · doi:10.1002/9781444398311.ch8 · Cited by 5 · see citing works
Mitochondrial dynamics in degenerative disease and disease models
Merzetti, E. M., & Staveley, B. E. (2013) · Neuroscience Discovery · doi:10.7243/2052-6946-1-8 · Cited by 5 · see citing works
Bannykh, S. I., Balch, W. E., Kelly, J. W., Page, L. J., & Shelton, G. D. (2013) · Ultrastructural Pathology · doi:10.3109/01913123.2013.810684 · Cited by 4 · see citing works
Inclusion body myositis pathomechanism and therapy
Váncsa, A., & Dankó, K. (2008) · Orvosi Hetilap · doi:10.1556/oh.2008.28070 · Cited by 4 · see citing works
Inclusion body myositis: clinical review and current practice
Brady, S., Healy, E. G., Machado, P., Parton, M. J., Holton, J. L., & Hanna, M. G. (2014) · Clinical Practice · doi:10.2217/cpr.14.54 · Cited by 2 · see citing works
The Amyloid _-Protein and Alzheimer's Disease
Teplow, D. B., Yang, M., Roychaudhuri, R., Pang, E. S., Huynh, T. V., Chen, M., & Beroukhim, S. (2012) · Frontiers in neuroscience · doi:10.1201/b11986-2 · Cited by 2 · see citing works
Askanas, V., Engel, W. K., & Nogalska, A. (2011) · Wiley eBooks · doi:10.1002/9781444398311.ch7 · Cited by 2 · see citing works
Self-citationClearance of intracellular aggregation-prone protein fragments
Gillis, J. (2009) · UvA-DARE (University of Amsterdam)
- Authors
- Fratta, P., Engel, W. K., McFerrin, J., Davies, K. J. A., Lin, S. W., & Askanas, V.
- Affiliations
- University of Southern California (US)
- Corresponding author
- Askanas, Valerie
- Venue
- The American Journal of Pathology
- Publisher
- Elsevier BV
- Published
- 2005-08
- Volume
- 167
- Issue
- 2
- Pages
- 517-526
- ISSN
- 0002-9440 (ISSN-L)
- PMC
- PMC1603556
- OpenAlex
- W1987807233
- Cited by
- 111
- References
- 47
- Citations by year
- 2025: 1 · 2024: 5 · 2022: 3 · 2021: 3 · 2020: 4 · 2018: 1 · 2017: 2 · 2016: 3 · 2015: 4 · 2014: 5 · 2013: 7 · 2012: 6
- FWCI
- 9.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- American Journal Of Pathology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Muscular Dystrophy Association (AG16768)
- Myositis Association
- National Institutes of Health
- National Institute on Aging (AG 16768, R37AG016768)
- Topics
- Health Sciences › Medicine › Epidemiology › Inflammatory Myopathies and Dermatomyositis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- sporadic inclusion body myositis, proteasome inhibition, aggresomes, 26S proteasome, amyloid precursor protein, amyloid-beta, phosphorylated tau, protein aggregates, misfolded protein accumulation, HSP70, ubiquitin, proteasome dysfunction
- MeSH terms
- Cells, Cultured, Humans, Amyloid beta-Protein Precursor, tau Proteins, Muscle Fibers, Skeletal, HSP70 Heat-Shock Proteins, Myositis, Inclusion Body, Ubiquitin, Proteasome Endopeptidase Complex, Proteasome Inhibitors
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