메뉴 건너뛰기




Volumn 71, Issue 8, 2012, Pages 680-693

Pathogenic considerations in sporadic inclusion-body myositis, a degenerative muscle disease associated with aging and abnormalities of myoproteostasis

Author keywords

Aging; Autophagy; Inclusion body myositis; Misfolded proteins; Multiprotein aggregates; Proteasome; Proteostasis

Indexed keywords

4 PHENYLBUTYRIC ACID; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; CASEIN KINASE I; CYTOCHROME C OXIDASE; GLYCOGEN SYNTHASE KINASE 3BETA; LITHIUM; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 1; MITOCHONDRIAL DNA; OLIGOMER; POLYPHENOL; PROTEASOME; TAU PROTEIN;

EID: 84864434515     PISSN: 00223069     EISSN: 15546578     Source Type: Journal    
DOI: 10.1097/NEN.0b013e31826183c8     Document Type: Review
Times cited : (63)

References (127)
  • 1
    • 33644850570 scopus 로고    scopus 로고
    • Inclusion-body myositis: Clinical, diagnostic, and pathologic aspects
    • Engel WK, Askanas V. Inclusion-body myositis: Clinical, diagnostic, and pathologic aspects. Neurology 2006;66:S20-29
    • (2006) Neurology , vol.66
    • Engel, W.K.1    Askanas, V.2
  • 2
    • 84864451207 scopus 로고    scopus 로고
    • Pathogenesis of sporadic inclusionbody myositis; Role of ageing and muscle-fibre degeneration, and accumulation of the same proteins as in alzheimer and parkinson brains
    • Askanas V, Engel WK, eds Oxford, UK: Wiley-Blackwell
    • Askanas V, Engel WK, Nogalska A. Pathogenesis of sporadic inclusionbody myositis; Role of ageing and muscle-fibre degeneration, and accumulation of the same proteins as in Alzheimer and Parkinson brains. In: Askanas V, Engel WK, eds. Muscle Ageing, Inclusion-Body Myositis and Myopathies. Oxford, UK: Wiley-Blackwell, 2012:111-45
    • (2012) Muscle Ageing, Inclusion-Body Myositis and Myopathies , pp. 111-145
    • Askanas, V.1    Engel, W.K.2    Nogalska, A.3
  • 3
    • 84864495509 scopus 로고    scopus 로고
    • Sporadic inclusion-body myositis: Clinical symptoms, physical findings, and diagnostic intvestigations
    • Askanas V, Engel WK, eds Oxford, UK: Wiley-Blackwell
    • Mastaglia F. Sporadic inclusion-body myositis: Clinical symptoms, physical findings, and diagnostic intvestigations. In: Askanas V, Engel WK, eds. Muscle Aging, Inclusion-Body Myositis and Myopathies. Oxford, UK: Wiley-Blackwell, 2012:159-67
    • (2012) Muscle Aging, Inclusion-Body Myositis and Myopathies , pp. 159-167
    • Mastaglia, F.1
  • 4
    • 81055125519 scopus 로고    scopus 로고
    • Long-term observational study of sporadic inclusion body myositis
    • Benveniste O, Guiguet M, Freebody J, et al. Long-term observational study of sporadic inclusion body myositis. Brain 2011;134:3176-84
    • (2011) Brain , vol.134 , pp. 3176-3184
    • Benveniste, O.1    Guiguet, M.2    Freebody, J.3
  • 5
    • 84864463632 scopus 로고    scopus 로고
    • Inflammatory and autoimmune features of inclusion-body myositis
    • Askanas V, Engel WK, eds Oxford, UK: Wiley-Blackwell
    • Dalakas MC. Inflammatory and autoimmune features of inclusion-body myositis. In: Askanas V, Engel WK, eds. Muscle Aging, Inclusion-Body Myositis and Myopathies. Oxford, UK: Wiley-Blackwell, 2012:146-58
    • (2012) Muscle Aging, Inclusion-Body Myositis and Myopathies , pp. 146-158
    • Dalakas, M.C.1
  • 6
    • 79953792495 scopus 로고    scopus 로고
    • Sporadic inclusion-body myositis: Conformational multifactorial ageingyrelated degenerative muscle disease associated with proteasomal and lysosomal inhibition, endoplasmic reticulum stress, and accumulation of amyloid-beta42 oligomers and phosphorylated tau
    • Askanas V, Engel WK. Sporadic inclusion-body myositis: Conformational multifactorial ageingYrelated degenerative muscle disease associated with proteasomal and lysosomal inhibition, endoplasmic reticulum stress, and accumulation of amyloid-beta42 oligomers and phosphorylated tau. Presse Med 2011;40:219-35
    • (2011) Presse Med , vol.40 , pp. 219-235
    • Askanas, V.1    Engel, W.K.2
  • 7
    • 33644852538 scopus 로고    scopus 로고
    • Pilot trial of etanercept in the treatment of inclusion-body myositis
    • Barohn RJ, Herbelin L, Kissel JT, et al. Pilot trial of etanercept in the treatment of inclusion-body myositis. Neurology 2006;66:S123-24
    • (2006) Neurology , vol.66
    • Barohn, R.J.1    Herbelin, L.2    Kissel, J.T.3
  • 8
    • 17044385422 scopus 로고    scopus 로고
    • Allelic heterogeneity of GNE gene mutation in two tunisian families with autosomal recessive inclusion body myopathy
    • Amouri R, Driss A, Murayama K, et al. Allelic heterogeneity of GNE gene mutation in two Tunisian families with autosomal recessive inclusion body myopathy. Neuromuscul Disord 2005;15:361-63
    • (2005) Neuromuscul Disord , vol.15 , pp. 361-363
    • Amouri, R.1    Driss, A.2    Murayama, K.3
  • 9
    • 0346219378 scopus 로고    scopus 로고
    • A novel homozygous missense mutation in the GNE gene of A patient with quadriceps-sparing hereditary inclusion body myopathy associated with muscle inflammation
    • Krause S, Schlotter-Weigel B, Walter MC, et al. A novel homozygous missense mutation in the GNE gene of a patient with quadriceps-sparing hereditary inclusion body myopathy associated with muscle inflammation. Neuromuscul Disord 2003;13:830-34
    • (2003) Neuromuscul Disord , vol.13 , pp. 830-834
    • Krause, S.1    Schlotter-Weigel, B.2    Walter, M.C.3
  • 10
    • 0036797633 scopus 로고    scopus 로고
    • Inclusion-body myositis and myopathies: Different etiologies, possibly similar pathogenic mechanisms
    • Askanas V, Engel WK. Inclusion-body myositis and myopathies: Different etiologies, possibly similar pathogenic mechanisms. Curr Opin Neurol 2002;15:525-31
    • (2002) Curr Opin Neurol , vol.15 , pp. 525-531
    • Askanas, V.1    Engel, W.K.2
  • 11
    • 84864492093 scopus 로고    scopus 로고
    • Consequences of the hereditary inclusionbody myopathy-characteristic GNE mutations on muscle proteins in vivo and in vitro
    • Askanas V, Engel WK, eds Oxford, UK: Wiley-Blackwell
    • Broccolini A, Mirabella M. Consequences of the hereditary inclusionbody myopathy-characteristic GNE mutations on muscle proteins in vivo and in vitro. In: Askanas V, Engel WK, eds. Muscle Ageing, Inclusion-Body Myositis and Myopathies. Oxford, UK: Wiley-Blackwell, 2012:199-205
    • (2012) Muscle Ageing, Inclusion-Body Myositis and Myopathies , pp. 199-205
    • Broccolini, A.1    Mirabella, M.2
  • 12
    • 67650497775 scopus 로고    scopus 로고
    • Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins
    • Page LJ, Suk JY, Bazhenova L, et al. Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins. Proc Natl Acad Sci USA 2009;106: 11125-30
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11125-11130
    • Page, L.J.1    Suk, J.Y.2    Bazhenova, L.3
  • 13
    • 56749104288 scopus 로고    scopus 로고
    • Inclusion-body myositis: Muscle fiber molecular pathology and possible pathogenic significance of its similarity to alzheimer's and parkinson's disease brains
    • Askanas V, Engel WK. Inclusion-body myositis: Muscle fiber molecular pathology and possible pathogenic significance of its similarity to Alzheimer's and Parkinson's disease brains. Acta Neuropathol 2008; 116:583-95
    • (2008) Acta Neuropathol , vol.116 , pp. 583-595
    • Askanas, V.1    Engel, W.K.2
  • 14
    • 33644869497 scopus 로고    scopus 로고
    • Inclusion-body myositis: A myodegenerative conformational disorder associated with abeta, protein misfolding, and proteasome inhibition
    • Askanas V, Engel WK. Inclusion-body myositis: A myodegenerative conformational disorder associated with Abeta, protein misfolding, and proteasome inhibition. Neurology 2006;66:S39YS48
    • (2006) Neurology , vol.66
    • Askanas, V.1    Engel, W.K.2
  • 15
    • 33750958343 scopus 로고    scopus 로고
    • Myod expression restores defective myogenic differentiation of human mesoangioblasts from inclusion-body myositis muscle
    • Morosetti R, Mirabella M, Gliubizzi C, et al. MyoD expression restores defective myogenic differentiation of human mesoangioblasts from inclusion-body myositis muscle. Proc Natl Acad Sci USA 2006;103: 16995-7000
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16995-17000
    • Morosetti, R.1    Mirabella, M.2    Gliubizzi, C.3
  • 16
    • 33847055006 scopus 로고    scopus 로고
    • Progressive myopathy with up-regulation of MHC-I associated with statin therapy
    • Needham M, Fabian V, Knezevic W, et al. Progressive myopathy with up-regulation of MHC-I associated with statin therapy. Neuromuscul Disord 2007;17:194-200
    • (2007) Neuromuscul Disord , vol.17 , pp. 194-200
    • Needham, M.1    Fabian, V.2    Knezevic, W.3
  • 17
    • 0001698695 scopus 로고
    • Rapid examination of muscle tissue and improved trichrome method for fresh-frozen biopsy sections
    • Engel WK, Cunningham GG. Rapid examination of muscle tissue and improved trichrome method for fresh-frozen biopsy sections. Neurology 1963;13:919-23
    • (1963) Neurology , vol.13 , pp. 919-923
    • Engel, W.K.1    Cunningham, G.G.2
  • 18
    • 0027240930 scopus 로고
    • Enhanced detection of congo-redypositive amyloid deposits in muscle fibers of inclusion body myositis and brain of alzheimer's disease using fluorescence technique
    • Askanas V, Engel WK, Alvarez RB. Enhanced detection of Congo-RedYpositive amyloid deposits in muscle fibers of inclusion body myositis and brain of Alzheimer's disease using fluorescence technique. Neurology 1993;43:1265-67
    • (1993) Neurology , vol.43 , pp. 1265-1267
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3
  • 19
    • 0035145398 scopus 로고    scopus 로고
    • Inclusion-body myositis: Newest concepts of pathogenesis and relation to aging and alzheimer disease
    • Askanas V, Engel WK. Inclusion-body myositis: Newest concepts of pathogenesis and relation to aging and Alzheimer disease. J Neuropathol Exp Neurol 2001;60:1-14
    • (2001) J Neuropathol Exp Neurol , vol.60 , pp. 1-14
    • Askanas, V.1    Engel, W.K.2
  • 20
    • 64449088789 scopus 로고    scopus 로고
    • Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusionbody myositis
    • Vattemi G, Nogalska A, Engel WK, et al. Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusionbody myositis. Acta Neuropathol 2009;117:569-74
    • (2009) Acta Neuropathol , vol.117 , pp. 569-574
    • Vattemi, G.1    Nogalska, A.2    Engel, W.K.3
  • 21
    • 66949145779 scopus 로고    scopus 로고
    • Inclusion body myositis: A degenerative muscle disease associated with intra-muscle fiber multiprotein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradation
    • Askanas V, Engel WK, Nogalska A. Inclusion body myositis: A degenerative muscle disease associated with intra-muscle fiber multiprotein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradation. Brain Pathol 2009;19:493-506
    • (2009) Brain Pathol , vol.19 , pp. 493-506
    • Askanas, V.1    Engel, W.K.2    Nogalska, A.3
  • 22
    • 68349097450 scopus 로고    scopus 로고
    • P62/sqstm1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis
    • Nogalska A, Terracciano C, D'Agostino C, et al. p62/SQSTM1 is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis muscle fibers, and can help differentiating it from polymyositis and dermatomyositis. Acta Neuropathol 2009;118:407-13
    • (2009) Acta Neuropathol , vol.118 , pp. 407-413
    • Nogalska, A.1    Terracciano, C.2    D'Agostino, C.3
  • 23
    • 27944504351 scopus 로고    scopus 로고
    • P62/sqstm1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G, Lamark T, Brech A, et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol 2005;171:603-14
    • (2005) J Cell Biol , vol.171 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3
  • 24
    • 4444220680 scopus 로고    scopus 로고
    • Sequestosome 1/P62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation
    • Seibenhener ML, Babu JR, Geetha T, et al. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol Cell Biol 2004;24:8055-68
    • (2004) Mol Cell Biol , vol.24 , pp. 8055-8068
    • Seibenhener, M.L.1    Babu, J.R.2    Geetha, T.3
  • 25
    • 53149138951 scopus 로고    scopus 로고
    • Tdp-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia
    • Weihl CC, Temiz P, Miller SE, et al. TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia. J Neurol Neurosurg Psychiatry 2008;79: 1186-89
    • (2008) J Neurol Neurosurg Psychiatry , vol.79 , pp. 1186-1189
    • Weihl, C.C.1    Temiz, P.2    Miller, S.E.3
  • 26
    • 59249094498 scopus 로고    scopus 로고
    • Tdp-43 accumulation is common in myopathies with rimmed vacuoles
    • Küsters B, van Hoeve BJ, Schelhaas HJ, et al. TDP-43 accumulation is common in myopathies with rimmed vacuoles. Acta Neuropathol 2009; 117:209-11
    • (2009) Acta Neuropathol , vol.117 , pp. 209-211
    • Küsters, B.1    Van Hoeve, B.J.2    Schelhaas, H.J.3
  • 27
    • 65349175153 scopus 로고    scopus 로고
    • TAR dna-binding protein 43 accumulation in protein aggregate myopathies
    • Olivé M, Janué A, Moreno D, et al. TAR DNA-binding protein 43 accumulation in protein aggregate myopathies. J Neuropathol Exp Neurol 2009;68:262-73
    • (2009) J Neuropathol Exp Neurol , vol.68 , pp. 262-273
    • Olivé, M.1    Janué, A.2    Moreno, D.3
  • 28
    • 67650264666 scopus 로고    scopus 로고
    • Sarcoplasmic redistribution of nuclear tdp-43 in inclusion body myositis
    • Salajegheh M, Pinkus JL, Taylor JP, et al. Sarcoplasmic redistribution of nuclear TDP-43 in inclusion body myositis. Muscle Nerve 2009;40:19-31
    • (2009) Muscle Nerve , vol.40 , pp. 19-31
    • Salajegheh, M.1    Pinkus, J.L.2    Taylor, J.P.3
  • 29
    • 79951804430 scopus 로고    scopus 로고
    • In sporadic inclusion body myositis muscle fibres tdp-43ypositive inclusions are less frequent and robust than p62 inclusions, and are not associated with paired helical filaments
    • D'Agostino C, Nogalska A, Engel WK, et al. In sporadic inclusion body myositis muscle fibres TDP-43Ypositive inclusions are less frequent and robust than p62 inclusions, and are not associated with paired helical filaments. Neuropathol Appl Neurobiol 2011;37:315-20
    • (2011) Neuropathol Appl Neurobiol , vol.37 , pp. 315-320
    • D'Agostino, C.1    Nogalska, A.2    Engel, W.K.3
  • 30
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch WE, Morimoto RI, Dillin A, et al. Adapting proteostasis for disease intervention. Science 2008;319:916-19
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3
  • 31
    • 77956362155 scopus 로고    scopus 로고
    • Protein homeostasis and aging in neurodegeneration
    • Douglas PM, Dillin A. Protein homeostasis and aging in neurodegeneration. J Cell Biol 2010;190:719-29
    • (2010) J Cell Biol , vol.190 , pp. 719-729
    • Douglas, P.M.1    Dillin, A.2
  • 32
    • 0027232988 scopus 로고
    • Beta-amyloid precursor protein mrna is increased in inclusion-body myositis muscle
    • Sarkozi E, Askanas V, Johnson SA, et al. Beta-Amyloid precursor protein mRNA is increased in inclusion-body myositis muscle. Neuroreport 1993;4:815-18
    • (1993) Neuroreport , vol.4 , pp. 815-818
    • Sarkozi, E.1    Askanas, V.2    Johnson, S.A.3
  • 33
    • 0024847273 scopus 로고
    • Tissue-specific expression of three types of beta-protein precursor mrna: Enhancement of protease inhibitoryharboring types in alzheimer's disease brain
    • Tanaka S, Shiojiri S, Takahashi Y, et al. Tissue-specific expression of three types of beta-protein precursor mRNA: Enhancement of protease inhibitorYharboring types in Alzheimer's disease brain. Biochem Biophys Res Commun 1989;165:1406-14
    • (1989) Biochem Biophys Res Commun , vol.165 , pp. 1406-1414
    • Tanaka, S.1    Shiojiri, S.2    Takahashi, Y.3
  • 34
    • 72849122715 scopus 로고    scopus 로고
    • In abetapp-overexpressing cultured human muscle fibers proteasome inhibition enhances phosphorylation of abetapp751 and gsk3beta activation: Effects mitigated by lithium and apparently relevant to sporadic inclusion-body myositis
    • Terracciano C, Nogalska A, Engel WK, et al. In AbetaPP-overexpressing cultured human muscle fibers proteasome inhibition enhances phosphorylation of AbetaPP751 and GSK3beta activation: Effects mitigated by lithium and apparently relevant to sporadic inclusion-body myositis. J Neurochem 2010;112:389-96
    • (2010) J Neurochem , vol.112 , pp. 389-396
    • Terracciano, C.1    Nogalska, A.2    Engel, W.K.3
  • 35
    • 0035830290 scopus 로고    scopus 로고
    • Presence of bace1 and bace2 in muscle fibres of patients with sporadic inclusion-body myositis
    • Vattemi G, Engel WK, McFerrin J, et al. Presence of BACE1 and BACE2 in muscle fibres of patients with sporadic inclusion-body myositis. Lancet 2001;358:1962-64
    • (2001) Lancet , vol.358 , pp. 1962-1964
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3
  • 36
    • 34948899795 scopus 로고    scopus 로고
    • NOGO is increased and binds to bace1 in sporadic inclusion-body myositis and in A beta pp-overexpressing cultured human muscle fibers
    • Wojcik S, Engel WK, Yan R, et al. NOGO is increased and binds to BACE1 in sporadic inclusion-body myositis and in A beta PP-overexpressing cultured human muscle fibers. Acta Neuropathol 2007;114: 517-26
    • (2007) Acta Neuropathol , vol.114 , pp. 517-526
    • Wojcik, S.1    Engel, W.K.2    Yan, R.3
  • 37
    • 84655166491 scopus 로고    scopus 로고
    • Regulation of beta-site app-cleaving enzyme 1 gene expression and its role in alzheimer's disease
    • Sun X, Bromley-Brits K, Song W. Regulation of beta-site APP-cleaving enzyme 1 gene expression and its role in Alzheimer's disease. J Neurochem 2012;120(Suppl 1):62-70
    • (2012) J Neurochem , vol.120 , Issue.SUPPL. 1 , pp. 62-70
    • Sun, X.1    Bromley-Brits, K.2    Song, W.3
  • 38
    • 78049374467 scopus 로고    scopus 로고
    • Novel research horizons for presenilins and gamma-secretases in cell biology and disease
    • De Strooper B, Annaert W. Novel research horizons for presenilins and gamma-secretases in cell biology and disease. Annu Rev Cell Dev Biol 2010;26:235-60
    • (2010) Annu Rev Cell Dev Biol , vol.26 , pp. 235-260
    • De Strooper, B.1    Annaert, W.2
  • 39
    • 77951499020 scopus 로고    scopus 로고
    • Increased bace1 mrna and noncoding bace1-antisense transcript in sporadic inclusion-body myositis muscle fibersvpossibly caused by endoplasmic reticulum stress
    • Nogalska A, Engel WK, Askanas V. Increased BACE1 mRNA and noncoding BACE1-antisense transcript in sporadic inclusion-body myositis muscle fibersVPossibly caused by endoplasmic reticulum stress. Neurosci Lett 2010;474:140-43
    • (2010) Neurosci Lett , vol.474 , pp. 140-143
    • Nogalska, A.1    Engel, W.K.2    Askanas, V.3
  • 40
    • 46749083733 scopus 로고    scopus 로고
    • Expression of a noncoding RNA is elevated in alzheimer's disease and drives rapid feed-forward regulation of beta-secretase
    • Faghihi MA, Modarresi F, Khalil AM, et al. Expression of a noncoding RNA is elevated in Alzheimer's disease and drives rapid feed-forward regulation of beta-secretase. Nat Med 2008;14:723-30
    • (2008) Nat Med , vol.14 , pp. 723-730
    • Faghihi, M.A.1    Modarresi, F.2    Khalil, A.M.3
  • 41
    • 0027444952 scopus 로고
    • Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis
    • Askanas V, Alvarez RB, Engel WK. Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis. Ann Neurol 1993;34:551-60
    • (1993) Ann Neurol , vol.34 , pp. 551-560
    • Askanas, V.1    Alvarez, R.B.2    Engel, W.K.3
  • 42
    • 0026595194 scopus 로고
    • Beta-amyloid protein immunoreactivity in muscle of patients with inclusion-body myositis
    • Askanas V, Engel WK, Alvarez RB, et al. Beta-amyloid protein immunoreactivity in muscle of patients with inclusion-body myositis. Lancet 1992;339:560-61
    • (1992) Lancet , vol.339 , pp. 560-561
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3
  • 43
    • 0031597431 scopus 로고    scopus 로고
    • Does overexpression of betaapp in aging muscle have a pathogenic role and a relevance to alzheimer's disease? Clues from inclusion body myositis, cultured human muscle, and transgenic mice
    • Askanas V, Engel WK. Does overexpression of betaAPP in aging muscle have a pathogenic role and a relevance to Alzheimer's disease? Clues from inclusion body myositis, cultured human muscle, and transgenic mice. Am J Pathol 1998;153:1673-77
    • (1998) Am J Pathol , vol.153 , pp. 1673-1677
    • Askanas, V.1    Engel, W.K.2
  • 44
    • 0142021035 scopus 로고    scopus 로고
    • Aging, amyloid, and alzheimer's diseas; A perspective in honor of Carl Cotman
    • Selkoe DJ. Aging, amyloid, and Alzheimer's diseas; A perspective in honor of Carl Cotman. Neurochem Res 2003;28:1705-13
    • (2003) Neurochem Res , vol.28 , pp. 1705-1713
    • Selkoe, D.J.1
  • 45
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in alzheimer's disease
    • LaFerla FM, Green KN, Oddo S. Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci 2007;8:499-509
    • (2007) Nat Rev Neurosci , vol.8 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 46
    • 84655162704 scopus 로고    scopus 로고
    • Soluble abeta oligomer production and toxicity
    • Larson ME, Lesne SE. Soluble Abeta oligomer production and toxicity. J Neurochem 2012;120(Suppl 1):125-39
    • (2012) J Neurochem , vol.120 , Issue.SUPPL. 1 , pp. 125-139
    • Larson, M.E.1    Lesne, S.E.2
  • 47
    • 60349121505 scopus 로고    scopus 로고
    • Identification of physiological and toxic conformations in abeta42 aggregates
    • Masuda Y, Uemura S, Ohashi R, et al. Identification of physiological and toxic conformations in Abeta42 aggregates. Chembiochem 2009; 10:287-95
    • (2009) Chembiochem , vol.10 , pp. 287-295
    • Masuda, Y.1    Uemura, S.2    Ohashi, R.3
  • 48
    • 78149406278 scopus 로고    scopus 로고
    • Novel demonstration of amyloid-beta oligomers in sporadic inclusion-body myositis muscle fibers
    • Nogalska A, D'Agostino C, Engel WK, et al. Novel demonstration of amyloid-beta oligomers in sporadic inclusion-body myositis muscle fibers. Acta Neuropathol 2010;120:661-66
    • (2010) Acta Neuropathol , vol.120 , pp. 661-666
    • Nogalska, A.1    D'Agostino, C.2    Engel, W.K.3
  • 49
    • 68349096299 scopus 로고    scopus 로고
    • Increased plasma amyloidbeta42 protein in sporadic inclusion body myositis
    • Abdo WF, van Mierlo T, Hengstman GJ, et al. Increased plasma amyloidbeta42 protein in sporadic inclusion body myositis. Acta Neuropathol 2009;118:429-31
    • (2009) Acta Neuropathol , vol.118 , pp. 429-431
    • Abdo, W.F.1    Van Mierlo, T.2    Hengstman, G.J.3
  • 50
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in alzheimer's disease
    • Klein WL, Stine WB Jr, Teplow DB. Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging 2004;25:569-80
    • (2004) Neurobiol Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine Jr., W.B.2    Teplow, D.B.3
  • 51
    • 33646708456 scopus 로고
    • Plasma-cell dyscrasic amyloid neuropathy: A parasparafucile phenomenon?
    • Serratrice G, Roux H, eds New York, NY: Masson Publishing Co.
    • Engel WK, Trotter JL. Plasma-cell dyscrasic amyloid neuropathy: A parasparafucile phenomenon? In: Serratrice G, Roux H, eds. Peroneal Atrophies and Related Disorders. New York, NY: Masson Publishing Co., 1979:333-38
    • (1979) Peroneal Atrophies and Related Disorders , pp. 333-338
    • Engel, W.K.1    Trotter, J.L.2
  • 52
    • 49149117491 scopus 로고    scopus 로고
    • Tau aggregation and toxicity in tauopathic neurodegenerative diseases
    • Honson NS, Kuret J. Tau aggregation and toxicity in tauopathic neurodegenerative diseases. J Alzheimers Dis 2008;14:417-22
    • (2008) J Alzheimers Dis , vol.14 , pp. 417-422
    • Honson, N.S.1    Kuret, J.2
  • 53
    • 67349142329 scopus 로고    scopus 로고
    • Mechanisms of tau-induced neurodegeneration
    • Iqbal K, Liu F, Gong CX, et al. Mechanisms of tau-induced neurodegeneration. Acta Neuropathol 2009;118:53-69
    • (2009) Acta Neuropathol , vol.118 , pp. 53-69
    • Iqbal, K.1    Liu, F.2    Gong, C.X.3
  • 54
    • 0029971055 scopus 로고    scopus 로고
    • Difference in expression of phosphorylated tau epitopes between sporadic inclusion-body myositis and hereditary inclusion-body myopathies
    • Mirabella M, Alvarez RB, Bilak M, et al. Difference in expression of phosphorylated tau epitopes between sporadic inclusion-body myositis and hereditary inclusion-body myopathies. J Neuropathol Exp Neurol 1996;55:774-86
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 774-786
    • Mirabella, M.1    Alvarez, R.B.2    Bilak, M.3
  • 55
    • 0030783142 scopus 로고    scopus 로고
    • A conformation-and phosphorylationdependent antibody recognizing the paired helical filaments of alzheimer's disease
    • Jicha GA, Lane E, Vincent I, et al. A conformation-and phosphorylationdependent antibody recognizing the paired helical filaments of Alzheimer's disease. J Neurochem 1997;69:2087-95
    • (1997) J Neurochem , vol.69 , pp. 2087-2095
    • Jicha, G.A.1    Lane, E.2    Vincent, I.3
  • 56
    • 77955949134 scopus 로고    scopus 로고
    • Alzheimer's disease neurofibrillary degeneration: Pivotal and multifactorial
    • Iqbal K, Wang X, Blanchard J, et al. Alzheimer's disease neurofibrillary degeneration: Pivotal and multifactorial. Biochem Soc Trans 2010;38: 962-66
    • (2010) Biochem Soc Trans , vol.38 , pp. 962-966
    • Iqbal, K.1    Wang, X.2    Blanchard, J.3
  • 57
    • 0033897261 scopus 로고    scopus 로고
    • Association of active extracellular signalyregulated protein kinase with paired helical filaments of inclusion-body myositis muscle suggests its role in inclusion-body myositis tau phosphorylation
    • Wilczynski GM, Engel WK, Askanas V. Association of active extracellular signalYregulated protein kinase with paired helical filaments of inclusion-body myositis muscle suggests its role in inclusion-body myositis tau phosphorylation. Am J Pathol 2000;156:1835-40
    • (2000) Am J Pathol , vol.156 , pp. 1835-1840
    • Wilczynski, G.M.1    Engel, W.K.2    Askanas, V.3
  • 58
    • 0034693413 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 colocalizes with phosphorylated tau in human inclusion-body myositis paired-helical filaments and may play a role in tau phosphorylation
    • Wilczynski GM, Engel WK, Askanas V. Cyclin-dependent kinase 5 colocalizes with phosphorylated tau in human inclusion-body myositis paired-helical filaments and may play a role in tau phosphorylation. Neurosci Lett 2000;293:33-6
    • (2000) Neurosci Lett , vol.293 , pp. 33-36
    • Wilczynski, G.M.1    Engel, W.K.2    Askanas, V.3
  • 59
    • 38349050020 scopus 로고    scopus 로고
    • Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis
    • Kannanayakal TJ, Mendell JR, Kuret J. Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis. Neurosci Lett 2008;431:141-45
    • (2008) Neurosci Lett , vol.431 , pp. 141-145
    • Kannanayakal, T.J.1    Mendell, J.R.2    Kuret, J.3
  • 60
    • 75949083202 scopus 로고    scopus 로고
    • Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates
    • Martinez A, Portero-Otin M, Pamplona R, et al. Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates. Brain Pathol 2010;20:281-97
    • (2010) Brain Pathol , vol.20 , pp. 281-297
    • Martinez, A.1    Portero-Otin, M.2    Pamplona, R.3
  • 61
    • 54949129369 scopus 로고    scopus 로고
    • In inclusion-body myositis muscle fibers parkinson-associated dj-1 is increased and oxidized
    • Terracciano C, Nogalska A, Engel WK, et al. In inclusion-body myositis muscle fibers Parkinson-associated DJ-1 is increased and oxidized. Free Radic Biol Med 2008;45:773-79
    • (2008) Free Radic Biol Med , vol.45 , pp. 773-779
    • Terracciano, C.1    Nogalska, A.2    Engel, W.K.3
  • 62
    • 0030942146 scopus 로고    scopus 로고
    • Increase of nitric oxide synthases and nitrotyrosine in inclusion-body myositis
    • Yang CC, Alvarez RB, Engel WK, et al. Increase of nitric oxide synthases and nitrotyrosine in inclusion-body myositis. Neuroreport 1996; 8:153-58
    • (1996) Neuroreport , vol.8 , pp. 153-158
    • Yang, C.C.1    Alvarez, R.B.2    Engel, W.K.3
  • 63
    • 13444287877 scopus 로고    scopus 로고
    • Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrit; implications for alzheimer's disease
    • Reynolds MR, Berry RW, Binder LI. Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrit; Implications for Alzheimer's disease. Biochemistry 2005;44:1690-700
    • (2005) Biochemistry , vol.44 , pp. 1690-1700
    • Reynolds, M.R.1    Berry, R.W.2    Binder, L.I.3
  • 64
    • 17644393495 scopus 로고    scopus 로고
    • Nitration and oligomerization of tau induced by peroxynitrite inhibit its microtubule-binding activity
    • Zhang YJ, Xu YF, Chen XQ, et al. Nitration and oligomerization of tau induced by peroxynitrite inhibit its microtubule-binding activity. FEBS Lett 2005;579:2421-27
    • (2005) FEBS Lett , vol.579 , pp. 2421-2427
    • Zhang, Y.J.1    Xu, Y.F.2    Chen, X.Q.3
  • 65
    • 70349895344 scopus 로고    scopus 로고
    • Role of synucleins in alzheimer's disease
    • Crews L, Tsigelny I, Hashimoto M, et al. Role of synucleins in Alzheimer's disease. Neurotox Res 2009;16:306-17
    • (2009) Neurotox Res , vol.16 , pp. 306-317
    • Crews, L.1    Tsigelny, I.2    Hashimoto, M.3
  • 66
    • 80055082804 scopus 로고    scopus 로고
    • Parkinson's disease and alpha-synuclein expression
    • Devine MJ, Gwinn K, Singleton A, et al. Parkinson's disease and alpha-synuclein expression. Mov Disord 2011;26:2160-68
    • (2011) Mov Disord , vol.26 , pp. 2160-2168
    • Devine, M.J.1    Gwinn, K.2    Singleton, A.3
  • 67
    • 80054755695 scopus 로고    scopus 로고
    • Pathological roles of alpha-synuclein in neurological disorders
    • Vekrellis K, Xilouri M, Emmanouilidou E, et al. Pathological roles of alpha-synuclein in neurological disorders. Lancet Neurol 2011;10: 1015-25
    • (2011) Lancet Neurol , vol.10 , pp. 1015-1025
    • Vekrellis, K.1    Xilouri, M.2    Emmanouilidou, E.3
  • 68
    • 0033934231 scopus 로고    scopus 로고
    • Novel immunolocalization of alpha-synuclein in human muscle of inclusion-body myositis, regenerating and necrotic muscle fibers, and at neuromuscular junctions
    • Askanas V, Engel WK, Alvarez RB, et al. Novel immunolocalization of alpha-synuclein in human muscle of inclusion-body myositis, regenerating and necrotic muscle fibers, and at neuromuscular junctions. J Neuropathol Exp Neurol 2000;59:592-98
    • (2000) J Neuropathol Exp Neurol , vol.59 , pp. 592-598
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3
  • 69
    • 33747477123 scopus 로고    scopus 로고
    • Parkin and its association with alpha-synuclein and abetapp in inclusion-body myositis and abetappoverexpressing cultured human muscle fibers
    • Paciello O, Wojcik S, Engel WK, et al. Parkin and its association with alpha-synuclein and AbetaPP in inclusion-body myositis and AbetaPPoverexpressing cultured human muscle fibers. Acta Myol 2006;25: 13-22
    • (2006) Acta Myol , vol.25 , pp. 13-22
    • Paciello, O.1    Wojcik, S.2    Engel, W.K.3
  • 70
    • 82755161734 scopus 로고    scopus 로고
    • Autophagy and disease; Always two sides to a problem
    • Sridhar S, Botbol Y, Macian F, et al. Autophagy and disease; Always two sides to a problem. J Pathol 2012;226:255-73
    • (2012) J Pathol , vol.226 , pp. 255-273
    • Sridhar, S.1    Botbol, Y.2    MacIan, F.3
  • 71
    • 77949504405 scopus 로고    scopus 로고
    • Selective molecular alterations in the autophagy pathway in patients with lewy body disease and in models of alpha-synucleinopathy
    • Crews L, Spencer B, Desplats P, et al. Selective molecular alterations in the autophagy pathway in patients with Lewy body disease and in models of alpha-synucleinopathy. PLoS One 2010;5:e9313
    • (2010) PLoS One , vol.5
    • Crews, L.1    Spencer, B.2    Desplats, P.3
  • 72
    • 71949090833 scopus 로고    scopus 로고
    • Mitochondrial trafficking of APP and Alpha synuclein: Relevance to mitochondrial dysfunction in Alzheimer's and Parkinson's diseases
    • Devi L, Anandatheerthavarada HK. Mitochondrial trafficking of APP and alpha synuclein: Relevance to mitochondrial dysfunction in Alzheimer's and Parkinson's diseases. Biochim Biophys Acta 2010; 1802:11-19
    • (2010) Biochim Biophys Acta , vol.1802 , pp. 11-19
    • Devi, L.1    Anandatheerthavarada, H.K.2
  • 73
    • 82755177802 scopus 로고    scopus 로고
    • Stimulatory effect of alpha-synuclein on the tau-phosphorylation by gsk-3beta
    • Kawakami F, Suzuki M, Shimada N, et al. Stimulatory effect of alpha-synuclein on the tau-phosphorylation by GSK-3beta. FEBS J 2011; 278:4895-904
    • (2011) FEBS J , vol.278 , pp. 4895-4904
    • Kawakami, F.1    Suzuki, M.2    Shimada, N.3
  • 74
    • 33646676002 scopus 로고
    • Ragged-red fibers" in opthamoplegia syndromes and their differential diagnosis
    • Engel WK. "Ragged-red fibers" in opthamoplegia syndromes and their differential diagnosis. Excerpta Med Inter Cong Series 1971;237;28
    • (1971) Excerpta Med Inter Cong Series , vol.237 , pp. 28
    • Engel, W.K.1
  • 75
    • 33644860811 scopus 로고    scopus 로고
    • Mitochondrial abnormalities in inclusion-body myositis
    • Oldfors A, Moslemi AR, Jonasson L, et al. Mitochondrial abnormalities in inclusion-body myositis. Neurology 2006;66:S49-55
    • (2006) Neurology , vol.66
    • Oldfors, A.1    Moslemi, A.R.2    Jonasson, L.3
  • 76
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D, Tanaka A, Suen DF, et al. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 2008; 183:795-803
    • (2008) J Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3
  • 77
    • 79955945927 scopus 로고    scopus 로고
    • Mitochondrial autophagy in neural function, neurodegenerative disease, neuron cell death, and aging
    • Batlevi Y, La Spada AR. Mitochondrial autophagy in neural function, neurodegenerative disease, neuron cell death, and aging. Neurobiol Dis 2011;43:46-51
    • (2011) Neurobiol Dis , vol.43 , pp. 46-51
    • Batlevi, Y.1    La Spada, A.R.2
  • 78
    • 0037428241 scopus 로고    scopus 로고
    • Mutations in the dj-1 gene associated with autosomal recessive early-onset parkinsonism
    • Bonifati V, Rizzu P, van Baren MJ, et al. Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism. Science 2003;299:256-59
    • (2003) Science , vol.299 , pp. 256-259
    • Bonifati, V.1    Rizzu, P.2    Van Baren, M.J.3
  • 79
    • 33646826619 scopus 로고    scopus 로고
    • Oxidative damage of dj-1 is linked to sporadic parkinson and alzheimer diseases
    • Choi J, Sullards MC, Olzmann JA, et al. Oxidative damage of DJ-1 is linked to sporadic Parkinson and Alzheimer diseases. J Biol Chem 2006;281:0816-24
    • (2006) J Biol Chem , vol.281 , pp. 0816-0824
    • Choi, J.1    Sullards, M.C.2    Olzmann, J.A.3
  • 80
    • 1642527499 scopus 로고    scopus 로고
    • Dj-1 has a role in antioxidative stress to prevent cell death
    • Taira T, Saito Y, Niki T, et al. DJ-1 has a role in antioxidative stress to prevent cell death. EMBO Rep 2004;5:213-18
    • (2004) EMBO Rep , vol.5 , pp. 213-218
    • Taira, T.1    Saito, Y.2    Niki, T.3
  • 81
    • 33644859083 scopus 로고    scopus 로고
    • The ubiquitin proteolytic system: From a vague idea, through basic mechanisms, and onto human diseases and drug targeting
    • Ciechanover A. The ubiquitin proteolytic system: From a vague idea, through basic mechanisms, and onto human diseases and drug targeting. Neurology 2006;66:S7-19
    • (2006) Neurology , vol.66
    • Ciechanover, A.1
  • 82
    • 79955955066 scopus 로고    scopus 로고
    • Proteasomal dysfunction in aging and huntington disease
    • Li XJ, Li S. Proteasomal dysfunction in aging and Huntington disease. Neurobiol Dis 2011;43:4-8
    • (2011) Neurobiol Dis , vol.43 , pp. 4-8
    • Li, X.J.1    Li, S.2
  • 83
    • 79955969705 scopus 로고    scopus 로고
    • Autophagy failure in alzheimer's diseasev locating the primary defect
    • Nixon RA, Yang DS. Autophagy failure in Alzheimer's diseaseV Locating the primary defect. Neurobiol Dis 2011;43:38-45
    • (2011) Neurobiol Dis , vol.43 , pp. 38-45
    • Nixon, R.A.1    Yang, D.S.2
  • 84
    • 42349089604 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in alzheimer's disease
    • Oddo S. The ubiquitin-proteasome system in Alzheimer's disease. J Cell Mol Med 2008;12:363-73
    • (2008) J Cell Mol Med , vol.12 , pp. 363-373
    • Oddo, S.1
  • 85
    • 24144489814 scopus 로고    scopus 로고
    • Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in aapp-overexpressing cultured human muscle fibers
    • Fratta P, Engel WK, McFerrin J, et al. Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in AAPP-overexpressing cultured human muscle fibers. Am J Pathol 2005; 167:517-26
    • (2005) Am J Pathol , vol.167 , pp. 517-526
    • Fratta, P.1    Engel, W.K.2    McFerrin, J.3
  • 86
    • 2442651500 scopus 로고    scopus 로고
    • Proteasomal expression, induction of immunoproteasome subunits, and local MHC class i presentation in myofibrillar myopathy and inclusion body myositis
    • Ferrer I, Mart'n B, Castaño JG, et al. Proteasomal expression, induction of immunoproteasome subunits, and local MHC class I presentation in myofibrillar myopathy and inclusion body myositis. J Neuropathol Exp Neurol 2004;63:484-98
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 484-498
    • Ferrer, I.1    Mart'N, B.2    Castaño, J.G.3
  • 87
    • 4644328932 scopus 로고    scopus 로고
    • Mutant ubiquitin ubb+1 is accumulated in sporadic inclusion-body myositis muscle fibers
    • Fratta P, Engel WK, Van Leeuwen FW, et al. Mutant ubiquitin UBB+1 is accumulated in sporadic inclusion-body myositis muscle fibers. Neurology 2004;63:1114-17
    • (2004) Neurology , vol.63 , pp. 1114-1117
    • Fratta, P.1    Engel, W.K.2    Van Leeuwen, F.W.3
  • 88
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with alzheimer's disease
    • Keck S, Nitsch R, Grune T, et al. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J Neurochem 2003;85:115-22
    • (2003) J Neurochem , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3
  • 89
    • 1842424791 scopus 로고    scopus 로고
    • Proteasomal inhibition by alpha-synuclein filaments and oligomers
    • Lindersson E, Beedholm R, Hojrup P, et al. Proteasomal inhibition by alpha-synuclein filaments and oligomers. J Biol Chem 2004;279:12924-34
    • (2004) J Biol Chem , vol.279 , pp. 12924-12934
    • Lindersson, E.1    Beedholm, R.2    Hojrup, P.3
  • 90
    • 76749094093 scopus 로고    scopus 로고
    • Misframed proteins and neurodegeneration: A novel view on alzheimer's and parkinson's diseases
    • Dennissen FJA, Kholod N, Steinbusch HWM, et al. Misframed proteins and neurodegeneration: A novel view on Alzheimer's and Parkinson's diseases. Neurodegenerative Dis 2010;7:76-79
    • (2010) Neurodegenerative Dis , vol.7 , pp. 76-79
    • Dennissen, F.J.A.1    Kholod, N.2    Steinbusch, H.W.M.3
  • 91
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • Lehman NL. The ubiquitin proteasome system in neuropathology. Acta Neuropathol 2009;118:329-47
    • (2009) Acta Neuropathol , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 92
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He C, Klionsky DJ. Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet 2009;43:67-93
    • (2009) Annu Rev Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 93
    • 0017861736 scopus 로고
    • Inclusion body myositis: A distinct variety of idiopathic inflammatory myopathy
    • Carpenter S, Karpati G, Heller I, et al. Inclusion body myositis: A distinct variety of idiopathic inflammatory myopathy. Neurology 1978;28:8-17
    • (1978) Neurology , vol.28 , pp. 8-17
    • Carpenter, S.1    Karpati, G.2    Heller, I.3
  • 94
    • 77956498664 scopus 로고    scopus 로고
    • Impaired autophagy in sporadic inclusion-body myositis and in endoplasmic reticulum stressy provoked cultured human muscle fibers
    • Nogalska A, D'Agostino C, Terracciano C, et al. Impaired autophagy in sporadic inclusion-body myositis and in endoplasmic reticulum stressY provoked cultured human muscle fibers. Am J Pathol 2010;177:1377-87
    • (2010) Am J Pathol , vol.177 , pp. 1377-1387
    • Nogalska, A.1    D'Agostino, C.2    Terracciano, C.3
  • 95
    • 41149085729 scopus 로고    scopus 로고
    • Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wildtype tau expression
    • Hamano T, Gendron TF, Causevic E, et al. Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wildtype tau expression. Eur J Neurosci 2008;27:1119-30
    • (2008) Eur J Neurosci , vol.27 , pp. 1119-1130
    • Hamano, T.1    Gendron, T.F.2    Causevic, E.3
  • 96
    • 33748524564 scopus 로고    scopus 로고
    • Antiamyloidogenic and neuroprotective functions of cathepsin B: Implications for alzheimer's disease
    • Mueller-Steiner S, Zhou Y, Arai H, et al. Antiamyloidogenic and neuroprotective functions of cathepsin B: Implications for Alzheimer's disease. Neuron 2006;51:703-14
    • (2006) Neuron , vol.51 , pp. 703-714
    • Mueller-Steiner, S.1    Zhou, Y.2    Arai, H.3
  • 97
    • 26444587508 scopus 로고    scopus 로고
    • Macroautophagyva novel beta-amyloid peptideygenerating pathway activated in alzheimer's disease
    • Yu WH, Cuervo AM, Kumar A, et al. MacroautophagyVA novel beta-amyloid peptideYgenerating pathway activated in Alzheimer's disease. J Cell Biol 2005;171:87-98
    • (2005) J Cell Biol , vol.171 , pp. 87-98
    • Yu, W.H.1    Cuervo, A.M.2    Kumar, A.3
  • 98
    • 60849099049 scopus 로고    scopus 로고
    • A role for nbr1 in autophagosomal degradation of ubiquitinated substrates
    • Kirkin V, Lamark T, Sou YS, et al. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol Cell 2009;33:505-16
    • (2009) Mol Cell , vol.33 , pp. 505-516
    • Kirkin, V.1    Lamark, T.2    Sou, Y.S.3
  • 99
    • 82355175806 scopus 로고    scopus 로고
    • Abnormalities of nbr1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis
    • D'Agostino C, Nogalska A, Cacciottolo M, et al. Abnormalities of NBR1, a novel autophagy-associated protein, in muscle fibers of sporadic inclusion-body myositis. Acta Neuropathol 2011;122:627-36
    • (2011) Acta Neuropathol , vol.122 , pp. 627-636
    • D'Agostino, C.1    Nogalska, A.2    Cacciottolo, M.3
  • 100
    • 0035919837 scopus 로고    scopus 로고
    • Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies
    • Kuusisto E, Salminen A, Alafuzoff I. Ubiquitin-binding protein p62 is present in neuronal and glial inclusions in human tauopathies and synucleinopathies. Neuroreport 2001;12:2085-90
    • (2001) Neuroreport , vol.12 , pp. 2085-2090
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 101
    • 0036284021 scopus 로고    scopus 로고
    • Early accumulation of p62 in neurofibrillary tangles in alzheimer's disease; possible role in tangle formation
    • Kuusisto E, Salminen A, Alafuzoff I. Early accumulation of p62 in neurofibrillary tangles in Alzheimer's disease; Possible role in tangle formation. Neuropathol App Neurobiol 2002;28:228-37
    • (2002) Neuropathol App Neurobiol , vol.28 , pp. 228-237
    • Kuusisto, E.1    Salminen, A.2    Alafuzoff, I.3
  • 102
    • 0031772229 scopus 로고    scopus 로고
    • Amyloid-beta deposition in skeletal muscle of transgenic mice; possible model of inclusion body myopathy
    • Fukuchi K, Pham D, Hart M, et al. Amyloid-beta deposition in skeletal muscle of transgenic mice; Possible model of inclusion body myopathy. Am J Pathol 1998;153:1687-93
    • (1998) Am J Pathol , vol.153 , pp. 1687-1693
    • Fukuchi, K.1    Pham, D.2    Hart, M.3
  • 103
    • 0031740915 scopus 로고    scopus 로고
    • Transgenic mice over-expressing the c-99 fragment of betapp with an alpha-secretase site mutation develop a myopathy similar to human inclusion body myositis
    • Jin LW, Hearn MG, Ogburn CE, et al. Transgenic mice over-expressing the C-99 fragment of betaPP with an alpha-secretase site mutation develop a myopathy similar to human inclusion body myositis. Am J Pathol 1998;153:1679-86
    • (1998) Am J Pathol , vol.153 , pp. 1679-1686
    • Jin, L.W.1    Hearn, M.G.2    Ogburn, C.E.3
  • 104
    • 33744739867 scopus 로고    scopus 로고
    • Genetically augmenting abeta42 levels in skeletal muscle exacerbates inclusion body myositislike pathology and motor deficits in transgenic mice
    • Kitazawa M, Green KN, Caccamo A, et al. Genetically augmenting Abeta42 levels in skeletal muscle exacerbates inclusion body myositislike pathology and motor deficits in transgenic mice. Am J Pathol 2006; 168:1986-97
    • (2006) Am J Pathol , vol.168 , pp. 1986-1997
    • Kitazawa, M.1    Green, K.N.2    Caccamo, A.3
  • 105
    • 33845599412 scopus 로고    scopus 로고
    • Transgenic expression of A-APP in fast-twitch skeletal muscle leads to calcium dyshomeostasis and ibmlike pathology
    • Moussa CE-H, Fu Q, Kumar P, et al. Transgenic expression of A-APP in fast-twitch skeletal muscle leads to calcium dyshomeostasis and IBMlike pathology. FASEB J 2006;20:2165-67
    • (2006) FASEB J , vol.20 , pp. 2165-2167
    • Moussa, C.E.-H.1    Fu, Q.2    Kumar, P.3
  • 106
    • 78149300132 scopus 로고    scopus 로고
    • Intracellular a-amyloid accumulation leads to age-dependent progression of ca2+ dysregulation in skeletal muscle
    • Lopez JR, Shtifman A. Intracellular A-amyloid accumulation leads to age-dependent progression of Ca2+ dysregulation in skeletal muscle. Muscle Nerve 2010;42:731-38
    • (2010) Muscle Nerve , vol.42 , pp. 731-738
    • Lopez, J.R.1    Shtifman, A.2
  • 107
    • 78650171972 scopus 로고    scopus 로고
    • Amyloid-A protein impairs ca2+ release and contractility in skeletal muscle
    • Shtifman A, Ward CW, Laver DR, et al. Amyloid-A protein impairs Ca2+ release and contractility in skeletal muscle. Neurobiol Aging 2010; 31:2080-90
    • (2010) Neurobiol Aging , vol.31 , pp. 2080-2090
    • Shtifman, A.1    Ward, C.W.2    Laver, D.R.3
  • 108
    • 70449927247 scopus 로고    scopus 로고
    • Autophagy is required to maintain muscle mass
    • Masiero E, Agatea L, Mammucari C, et al. Autophagy is required to maintain muscle mass. Cell Metab 2009;10:507-15
    • (2009) Cell Metab , vol.10 , pp. 507-515
    • Masiero, E.1    Agatea, L.2    Mammucari, C.3
  • 109
    • 0029671441 scopus 로고    scopus 로고
    • Transfer of beta-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle
    • Askanas V, McFerrin J, Baque S, et al. Transfer of beta-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle. Proc Natl Acad Sci USA 1996;93:1314-19
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1314-1319
    • Askanas, V.1    McFerrin, J.2    Baque, S.3
  • 110
    • 0030857085 scopus 로고    scopus 로고
    • Beta APP gene transfer into cultured human muscle induces inclusion-body myositis aspects
    • Askanas V, McFerrin J, Alvarez RB, et al. Beta APP gene transfer into cultured human muscle induces inclusion-body myositis aspects. Neuroreport 1997;8:2155-58
    • (1997) Neuroreport , vol.8 , pp. 2155-2158
    • Askanas, V.1    McFerrin, J.2    Alvarez, R.B.3
  • 111
    • 0032487428 scopus 로고    scopus 로고
    • Impaired innervation of cultured human muscle overexpressing betaapp experimentally and genetically: Relevance to inclusion-body myopathies
    • McFerrin J, Engel WK, Askanas V. Impaired innervation of cultured human muscle overexpressing betaAPP experimentally and genetically: Relevance to inclusion-body myopathies. Neuroreport 1998;9: 3201-5
    • (1998) Neuroreport , vol.9 , pp. 3201-3205
    • McFerrin, J.1    Engel, W.K.2    Askanas, V.3
  • 112
    • 0742271866 scopus 로고    scopus 로고
    • Combined influence of amyloidbeta precursor protein (AbPP) gene transfer and cholesterol excess on cultured humen muscle fibers abstract
    • McFerrin J, Engel WK, Leclerc N, et al. Combined influence of amyloidbeta precursor protein (AbPP) gene transfer and cholesterol excess on cultured humen muscle fibers abstract. Neurology 2002;58:489
    • (2002) Neurology , vol.58 , pp. 489
    • McFerrin, J.1    Engel, W.K.2    Leclerc, N.3
  • 113
    • 33847717940 scopus 로고    scopus 로고
    • Myostatin precursor protein is increased and associates with amyloid-beta precursor protein in inclusionbody myositis culture model
    • Wojcik S, Nogalska A, McFerrin J, et al. Myostatin precursor protein is increased and associates with amyloid-beta precursor protein in inclusionbody myositis culture model. Neuropathol Appl Neurobiol 2007;33: 238-42
    • (2007) Neuropathol Appl Neurobiol , vol.33 , pp. 238-242
    • Wojcik, S.1    Nogalska, A.2    McFerrin, J.3
  • 114
    • 33845217281 scopus 로고    scopus 로고
    • Abetapp-overexpression and proteasome inhibition increase alphab-crystallin in cultured human muscl; relevance to inclusion-body myositis
    • Wojcik S, Engel WK, McFerrin J, et al. AbetaPP-overexpression and proteasome inhibition increase alphaB-crystallin in cultured human muscl; relevance to inclusion-body myositis. Neuromuscul Disord 2006;16:839-44
    • (2006) Neuromuscul Disord , vol.16 , pp. 839-844
    • Wojcik, S.1    Engel, W.K.2    McFerrin, J.3
  • 115
    • 4243615593 scopus 로고    scopus 로고
    • Ultrastructural abnormalities of neuromuscular juunctions in sporadic inclusion-body myositis abstract
    • Alvarez RB, Engel W, Askanas V. Ultrastructural abnormalities of neuromuscular juunctions in sporadic inclusion-body myositis abstract. Neurology 2000;54(Suppl 3):240-41
    • (2000) Neurology , vol.54 , Issue.SUPPL. 3 , pp. 240-241
    • Alvarez, R.B.1    Engel, W.2    Askanas, V.3
  • 116
    • 84864432040 scopus 로고    scopus 로고
    • Experimental impairment of the autophagosomal-lysosomal pathway (ALP) in our cultured human-muscle-fibers model of S-IBM (IBM-CHMFs Model) activates f-secretase, resulting in adversely increased production of amyloid-A 42 (AA42) and its subsequent detrimental oligomerization. Relevance to sporadic inclusion-body myositis (s-IBM) pathogenesis abstract
    • Nogalska A, D'Agostino C, Engel WK, et al. Experimental impairment of the autophagosomal-lysosomal pathway (ALP) in our cultured human-muscle-fibers model of s-IBM (IBM-CHMFs Model) activates F-secretase, resulting in adversely increased production of amyloid-A 42 (AA42) and its subsequent detrimental oligomerization. Relevance to sporadic inclusion-body myositis (s-IBM) pathogenesis abstract. Neurology 2011;76:106
    • (2011) Neurology , vol.76 , pp. 106
    • Nogalska, A.1    D'Agostino, C.2    Engel, W.K.3
  • 117
    • 77954953341 scopus 로고    scopus 로고
    • Decreased sirt1 deacetylase activity in sporadic inclusion-body myositis muscle fibers
    • Nogalska A, D'Agostino C, Engel WK, et al. Decreased SIRT1 deacetylase activity in sporadic inclusion-body myositis muscle fibers. Neurobiol Aging 2010;31:1637-48
    • (2010) Neurobiol Aging , vol.31 , pp. 1637-1648
    • Nogalska, A.1    D'Agostino, C.2    Engel, W.K.3
  • 118
    • 33947622602 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress induces myostatin precursor protein and nf-kappab in cultured human muscle fibers: Relevance to inclusion body myositis
    • Nogalska A, Wojcik S, Engel WK, et al. Endoplasmic reticulum stress induces myostatin precursor protein and NF-kappaB in cultured human muscle fibers: relevance to inclusion body myositis. Exp Neurol 2007; 204:610-18
    • (2007) Exp Neurol , vol.204 , pp. 610-618
    • Nogalska, A.1    Wojcik, S.2    Engel, W.K.3
  • 119
    • 33645107853 scopus 로고    scopus 로고
    • Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in sporadic inclusion-body myositis and in endoplasmic reticulum stressyinduced cultured human muscle fibers
    • Nogalska A, Engel WK, McFerrin J, et al. Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in sporadic inclusion-body myositis and in endoplasmic reticulum stressYinduced cultured human muscle fibers. J Neurochem 2006;96:1491-99
    • (2006) J Neurochem , vol.96 , pp. 1491-1499
    • Nogalska, A.1    Engel, W.K.2    McFerrin, J.3
  • 120
    • 40349116865 scopus 로고    scopus 로고
    • Lithium, a potential protective drug in alzheimer's disease
    • Engel T, Goni-Oliver P, Gomez de Barreda E, et al. Lithium, a potential protective drug in Alzheimer's disease. Neurodegener Dis 2008;5: 247-49
    • (2008) Neurodegener Dis , vol.5 , pp. 247-249
    • Engel, T.1    Goni-Oliver, P.2    Gomez De Barreda, E.3
  • 121
    • 48949086699 scopus 로고    scopus 로고
    • Inflammation induces tau pathology in inclusion body myositis model via glycogen synthase kinase-3beta
    • Kitazawa M, Trinh DN, LaFerla FM. Inflammation induces tau pathology in inclusion body myositis model via glycogen synthase kinase-3beta. Ann Neurol 2008;64:15-24
    • (2008) Ann Neurol , vol.64 , pp. 15-24
    • Kitazawa, M.1    Trinh, D.N.2    LaFerla, F.M.3
  • 122
    • 35848963616 scopus 로고    scopus 로고
    • Resveratrol: From basic science to the clinic
    • Cucciolla V, Borriello A, Oliva A, et al. Resveratrol: From basic science to the clinic. Cell Cycle 2007;6:2495-510
    • (2007) Cell Cycle , vol.6 , pp. 2495-2510
    • Cucciolla, V.1    Borriello, A.2    Oliva, A.3
  • 123
    • 56749102328 scopus 로고    scopus 로고
    • Resveratrol, a polyphenol found in red wine, reduces NF-JB activation and myostatin in endoplasmic reticulum stress (ERS)yprovoked cultured human muscle fibers: Relevance to treatment of sporadic inclusion-body myositis. (Abstract)
    • Nogalska A, D'Agostino C, Engel WK, et al. Resveratrol, a polyphenol found in red wine, reduces NF-JB activation and myostatin in endoplasmic reticulum stress (ERS)Yprovoked cultured human muscle fibers: Relevance to treatment of sporadic inclusion-body myositis. (Abstract) Ann Neurol 2008;64:S9
    • (2008) Ann Neurol , vol.64
    • Nogalska, A.1    D'Agostino, C.2    Engel, W.K.3
  • 124
    • 73549106551 scopus 로고    scopus 로고
    • Phenolic compounds prevent alzheimer's pathology through different effects on the amyloid-beta aggregation pathway
    • Hamaguchi T, Ono K, Murase A, et al. Phenolic compounds prevent Alzheimer's pathology through different effects on the amyloid-beta aggregation pathway. Am J Pathol 2009;175:2557-65
    • (2009) Am J Pathol , vol.175 , pp. 2557-2565
    • Hamaguchi, T.1    Ono, K.2    Murase, A.3
  • 125
    • 33646008876 scopus 로고    scopus 로고
    • Chemical chaperones: Mechanisms of action and potential use
    • Papp E, Csermely P. Chemical chaperones: Mechanisms of action and potential use. Handb Exp Pharmacol 2006;405-16
    • (2006) Handb Exp Pharmacol , pp. 405-416
    • Papp, E.1    Csermely, P.2
  • 127
    • 36248970599 scopus 로고    scopus 로고
    • Sodium phenylbutyrate in huntington's disease; A dose-finding study
    • Hogarth P, Lovrecic L, Krainc D. Sodium phenylbutyrate in Huntington's disease; A dose-finding study. Mov Disord 2007;22:1962-64
    • (2007) Mov Disord , vol.22 , pp. 1962-1964
    • Hogarth, P.1    Lovrecic, L.2    Krainc, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.