메뉴 건너뛰기




Volumn 40, Issue 4, 2011, Pages

Sporadic inclusion-body myositis: Conformational multifactorial ageing-related degenerative muscle disease associated with proteasomal and lysosomal inhibition, endoplasmic reticulum stress, and accumulation of amyloid-β42 oligomers and phosphorylated tau

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN[1-42]; HEAT SHOCK PROTEIN; MYOSTATIN; OLIGOMER; PARKIN; PROTEASOME; PROTEIN P62; SIRTUIN 1; TAR DNA BINDING PROTEIN; TAU PROTEIN; UBIQUITIN;

EID: 79953792495     PISSN: 07554982     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lpm.2010.11.024     Document Type: Short Survey
Times cited : (65)

References (162)
  • 1
    • 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 W.K. 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(6):583-595.
    • (2008) Acta Neuropathol , vol.116 , Issue.6 , pp. 583-595
    • Askanas, V.1    Engel, W.K.2
  • 2
    • 66949145779 scopus 로고    scopus 로고
    • Inclusion body myositis: a degenerative muscle disease associated with intramuscle fiber multi-protein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradation
    • Askanas V., Engel W.K., Nogalska A. Inclusion body myositis: a degenerative muscle disease associated with intramuscle fiber multi-protein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradation. Brain Pathol 2009, 19(3):493-506.
    • (2009) Brain Pathol , vol.19 , Issue.3 , pp. 493-506
    • Askanas, V.1    Engel, W.K.2    Nogalska, A.3
  • 3
    • 34948816592 scopus 로고    scopus 로고
    • Inclusion-body myositis, a multifactorial muscle disease associated with aging: current concepts of pathogenesis
    • Askanas V., Engel W.K. Inclusion-body myositis, a multifactorial muscle disease associated with aging: current concepts of pathogenesis. Curr Opin Rheumatol. 2007, 19(6):550-559.
    • (2007) Curr Opin Rheumatol. , vol.19 , Issue.6 , pp. 550-559
    • Askanas, V.1    Engel, W.K.2
  • 4
    • 33644869497 scopus 로고    scopus 로고
    • Inclusion-body myositis: a myodegenerative conformational disorder associated with Abeta, protein misfolding, and proteasome inhibition
    • Askanas V., Engel W.K. Inclusion-body myositis: a myodegenerative conformational disorder associated with Abeta, protein misfolding, and proteasome inhibition. Neurology. 2006, 66(2):S39-S48.
    • (2006) Neurology. , vol.66 , Issue.2
    • Askanas, V.1    Engel, W.K.2
  • 5
    • 0035145398 scopus 로고    scopus 로고
    • Inclusion-body myositis: newest concepts of pathogenesis and relation to aging and Alzheimer disease
    • Askanas V., Engel W.K. Inclusion-body myositis: newest concepts of pathogenesis and relation to aging and Alzheimer disease. J Neuropathol Exp Neurol. 2001, 60(1):1-14.
    • (2001) J Neuropathol Exp Neurol. , vol.60 , Issue.1 , pp. 1-14
    • Askanas, V.1    Engel, W.K.2
  • 6
    • 0742321934 scopus 로고    scopus 로고
    • Proposed pathogenetic cascade of inclusion-body myositis: importance of amyloid-beta, misfolded proteins, predisposing genes, and aging
    • Askanas V., Engel W.K. Proposed pathogenetic cascade of inclusion-body myositis: importance of amyloid-beta, misfolded proteins, predisposing genes, and aging. Curr Opin Rheumatol. 2003, 15(6):737-744.
    • (2003) Curr Opin Rheumatol. , vol.15 , Issue.6 , pp. 737-744
    • Askanas, V.1    Engel, W.K.2
  • 7
    • 33644850570 scopus 로고    scopus 로고
    • Inclusion-body myositis: clinical, diagnostic, and pathologic aspects
    • Engel W.K., Askanas V. Inclusion-body myositis: clinical, diagnostic, and pathologic aspects. Neurology. 2006, 66(2):S20-S29.
    • (2006) Neurology. , vol.66 , Issue.2
    • Engel, W.K.1    Askanas, V.2
  • 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., Kefi M., Nishino I., Hentati F. Allelic heterogeneity of GNE gene mutation in two Tunisian families with autosomal recessive inclusion body myopathy. Neuromuscul Disord. 2005, 15(5):361-363.
    • (2005) Neuromuscul Disord. , vol.15 , Issue.5 , pp. 361-363
    • Amouri, R.1    Driss, A.2    Murayama, K.3    Kefi, M.4    Nishino, I.5    Hentati, F.6
  • 9
    • 79953800442 scopus 로고    scopus 로고
    • Hereditary inclusion body myopathies
    • Lippincott Williams & Wilkins, Wolters Kluver, R.N. Rosenberg, S. Di Mauro, H.L. Paulson, L. Ptacek, E.J. Nestler (Eds.)
    • Askanas V., Engel W.K. Hereditary inclusion body myopathies. The molecular and genetic basis of neurologic and psychiatric disease 2008, 524-531. Lippincott Williams & Wilkins, Wolters Kluver. 4th ed. R.N. Rosenberg, S. Di Mauro, H.L. Paulson, L. Ptacek, E.J. Nestler (Eds.).
    • (2008) The molecular and genetic basis of neurologic and psychiatric disease , pp. 524-531
    • Askanas, V.1    Engel, W.K.2
  • 10
    • 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 M.C., Najmabadi H., Wiendl H., Muller-Hocker J., 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(10):830-834.
    • (2003) Neuromuscul Disord. , vol.13 , Issue.10 , pp. 830-834
    • Krause, S.1    Schlotter-Weigel, B.2    Walter, M.C.3    Najmabadi, H.4    Wiendl, H.5    Muller-Hocker, J.6
  • 11
    • 0036797633 scopus 로고    scopus 로고
    • Inclusion-body myositis and myopathies: different etiologies, possibly similar pathogenic mechanisms
    • Askanas V., Engel W.K. Inclusion-body myositis and myopathies: different etiologies, possibly similar pathogenic mechanisms. Curr Opin Neurol. 2002, 15(5):525-531.
    • (2002) Curr Opin Neurol. , vol.15 , Issue.5 , pp. 525-531
    • Askanas, V.1    Engel, W.K.2
  • 12
    • 0038407678 scopus 로고    scopus 로고
    • Unfolding story of inclusion-body myositis and myopathies: role of misfolded proteins, amyloid-beta, cholesterol, and aging
    • Askanas V., Engel W.K. Unfolding story of inclusion-body myositis and myopathies: role of misfolded proteins, amyloid-beta, cholesterol, and aging. J Child Neurol. 2003, 18(3):185-190.
    • (2003) J Child Neurol. , vol.18 , Issue.3 , pp. 185-190
    • Askanas, V.1    Engel, W.K.2
  • 14
    • 77957740872 scopus 로고    scopus 로고
    • Autoimmunity in a genetic disease-a cautionary tale
    • Moore M.J., Flotte T.R. Autoimmunity in a genetic disease-a cautionary tale. N Engl J Med. 2010, 363(15):1473-1475.
    • (2010) N Engl J Med. , vol.363 , Issue.15 , pp. 1473-1475
    • Moore, M.J.1    Flotte, T.R.2
  • 15
    • 67650497775 scopus 로고    scopus 로고
    • Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins
    • Page L.J., Suk J.Y., Bazhenova L., Fleming S.M., Wood M., Jiang Y., et al. Secretion of amyloidogenic gelsolin progressively compromises protein homeostasis leading to the intracellular aggregation of proteins. Proc Natl Acad Sci U S A 2009, 106(27):11125-11130.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , Issue.27 , pp. 11125-11130
    • Page, L.J.1    Suk, J.Y.2    Bazhenova, L.3    Fleming, S.M.4    Wood, M.5    Jiang, Y.6
  • 16
    • 79953780883 scopus 로고    scopus 로고
    • Immunosupresive-treatment does not alter natural history of sporadic-inclusion body myositis (sIBM): the Pitie-Salpetriere/Oxford study
    • Benveniste O., Guiguet M., Freebody J., Herson S., Dubourg O., Squier W., et al. Immunosupresive-treatment does not alter natural history of sporadic-inclusion body myositis (sIBM): the Pitie-Salpetriere/Oxford study. Acta Myol. 2010, 29:144-1445.
    • (2010) Acta Myol. , vol.29 , pp. 144-1445
    • Benveniste, O.1    Guiguet, M.2    Freebody, J.3    Herson, S.4    Dubourg, O.5    Squier, W.6
  • 17
    • 77949269483 scopus 로고    scopus 로고
    • Immunotherapy of myositis: issues, concerns and future prospects
    • Dalakas M.C. Immunotherapy of myositis: issues, concerns and future prospects. Nat Rev Rheumatol. 2010, 6(3):129-137.
    • (2010) Nat Rev Rheumatol. , vol.6 , Issue.3 , pp. 129-137
    • Dalakas, M.C.1
  • 18
    • 33644864328 scopus 로고    scopus 로고
    • The current status of treatment for inclusion-body myositis
    • Griggs R.C. The current status of treatment for inclusion-body myositis. Neurology. 2006, 66(2 Suppl. 1):S30-S32.
    • (2006) Neurology. , vol.66 , Issue.2 SUPPL. 1
    • Griggs, R.C.1
  • 20
    • 24144489814 scopus 로고    scopus 로고
    • Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in AbPP-overexpressing cultured human muscle fibers
    • Fratta P., Engel W.K., McFerrin J., Davies K.J.A., Lin S.W., Askanas V. Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in AbPP-overexpressing cultured human muscle fibers. Am J Pathol. 2005, 167:517-526.
    • (2005) Am J Pathol. , vol.167 , pp. 517-526
    • Fratta, P.1    Engel, W.K.2    McFerrin, J.3    Davies, K.J.A.4    Lin, S.W.5    Askanas, V.6
  • 21
    • 77949407188 scopus 로고    scopus 로고
    • Ageing neurodegeneration and Parkinson's disease
    • Hindle J.V. Ageing neurodegeneration and Parkinson's disease. Age Ageing. 2010, 39(2):156-161.
    • (2010) Age Ageing. , vol.39 , Issue.2 , pp. 156-161
    • Hindle, J.V.1
  • 22
    • 0034131044 scopus 로고    scopus 로고
    • Impaired proteasome function in Alzheimer's disease
    • Keller J.N., Hanni K.B., Markesbery W.R. Impaired proteasome function in Alzheimer's disease. J Neurochem. 2000, 75:436-439.
    • (2000) J Neurochem. , vol.75 , pp. 436-439
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 23
    • 33645141853 scopus 로고    scopus 로고
    • ER stress and neurodegenerative diseases
    • Lindholm D., Wootz H., Korhonen L. ER stress and neurodegenerative diseases. Cell Death Differ. 2006, 13(3):385-392.
    • (2006) Cell Death Differ. , vol.13 , Issue.3 , pp. 385-392
    • Lindholm, D.1    Wootz, H.2    Korhonen, L.3
  • 24
    • 77956498664 scopus 로고    scopus 로고
    • Impaired autophagy in sporadic inclusion-body myositis and in endoplasmic reticulum stress-provoked cultured human muscle fibers
    • Nogalska A., D'Agostino C., Terracciano C., Engel W.K., Askanas V. Impaired autophagy in sporadic inclusion-body myositis and in endoplasmic reticulum stress-provoked cultured human muscle fibers. Am J Pathol. 2010, 177:1377-1387.
    • (2010) Am J Pathol. , vol.177 , pp. 1377-1387
    • Nogalska, A.1    D'Agostino, C.2    Terracciano, C.3    Engel, W.K.4    Askanas, V.5
  • 25
    • 33645107853 scopus 로고    scopus 로고
    • Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in sporadic inclusion-body myositis and in endoplasmic reticulum stress-induced cultured human muscle fibers
    • Nogalska A., Engel W.K., McFerrin J., Kokame K., Komano H., Askanas V. Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in sporadic inclusion-body myositis and in endoplasmic reticulum stress-induced cultured human muscle fibers. J Neurochem. 2006, 96(5):1491-1499.
    • (2006) J Neurochem. , vol.96 , Issue.5 , pp. 1491-1499
    • Nogalska, A.1    Engel, W.K.2    McFerrin, J.3    Kokame, K.4    Komano, H.5    Askanas, V.6
  • 26
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases
    • Sherman M.Y., Goldberg A.L. Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseases. Neuron 2001, 29(1):15-32.
    • (2001) Neuron , vol.29 , Issue.1 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 27
    • 54949129369 scopus 로고    scopus 로고
    • In inclusion-body myositis muscle fibers Parkinson-associated DJ-1 is increased and oxidized
    • Terracciano C., Nogalska A., Engel W.K., Wojcik S., Askanas V. In inclusion-body myositis muscle fibers Parkinson-associated DJ-1 is increased and oxidized. Free Radic Biol Med. 2008, 45(6):773-779.
    • (2008) Free Radic Biol Med. , vol.45 , Issue.6 , pp. 773-779
    • Terracciano, C.1    Nogalska, A.2    Engel, W.K.3    Wojcik, S.4    Askanas, V.5
  • 28
    • 1542784578 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle
    • Vattemi G., Engel W.K., McFerrin J., Askanas V. Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am J Pathol. 2004, 164(1):1-7.
    • (2004) Am J Pathol. , vol.164 , Issue.1 , pp. 1-7
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 29
    • 33847652900 scopus 로고    scopus 로고
    • Autophagy and neurodegeneration: when the cleaning crew goes on strike
    • Martinez-Vicente M., Cuervo A.M. Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurol. 2007, 6(4):352-361.
    • (2007) Lancet Neurol. , vol.6 , Issue.4 , pp. 352-361
    • Martinez-Vicente, M.1    Cuervo, A.M.2
  • 30
    • 0001698695 scopus 로고
    • Rapid examination of muscle tissue and improved trichrome method for fresh-frozen biopsy sections
    • Engel W.K., Cunningham G.G. Rapid examination of muscle tissue and improved trichrome method for fresh-frozen biopsy sections. Neurology. 1963, 13:919-923.
    • (1963) Neurology. , vol.13 , pp. 919-923
    • Engel, W.K.1    Cunningham, G.G.2
  • 31
    • 0000504097 scopus 로고
    • The essentiality of histo- and cytochemical studies of skeletal muscle in the investigation of neuromuscular disease
    • Engel W.K. The essentiality of histo- and cytochemical studies of skeletal muscle in the investigation of neuromuscular disease. Neurology. 1962, 12:778-794.
    • (1962) Neurology. , vol.12 , pp. 778-794
    • Engel, W.K.1
  • 32
    • 0027240930 scopus 로고
    • Enhanced detection of congo-red-positive amyloid deposits in muscle fibers of inclusion body myositis and brain of Alzheimer's disease using fluorescence technique
    • Askanas V., Engel W.K., Alvarez R.B. Enhanced detection of congo-red-positive amyloid deposits in muscle fibers of inclusion body myositis and brain of Alzheimer's disease using fluorescence technique. Neurology. 1993, 43(6):1265-1267.
    • (1993) Neurology. , vol.43 , Issue.6 , pp. 1265-1267
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3
  • 33
    • 64449088789 scopus 로고    scopus 로고
    • Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis
    • Vattemi G., Nogalska A., King Engel W., D'Agostino C., Checler F., Askanas V. Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis. Acta Neuropathol. 2009, 117(5):569-574.
    • (2009) Acta Neuropathol. , vol.117 , Issue.5 , pp. 569-574
    • Vattemi, G.1    Nogalska, A.2    King Engel, W.3    D'Agostino, C.4    Checler, F.5    Askanas, V.6
  • 34
    • 0037041441 scopus 로고    scopus 로고
    • Medicine: danger-misfolding proteins
    • Ellis R.J., Pinheiro T.J. Medicine: danger-misfolding proteins. Nature. 2002, 416(6880):483-484.
    • (2002) Nature. , vol.416 , Issue.6880 , pp. 483-484
    • Ellis, R.J.1    Pinheiro, T.J.2
  • 35
    • 48149108245 scopus 로고    scopus 로고
    • Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases
    • Irvine G.B., El-Agnaf O.M., Shankar G.M., Walsh D.M. Protein aggregation in the brain: the molecular basis for Alzheimer's and Parkinson's diseases. Mol Med 2008, 14(7-8):451-464.
    • (2008) Mol Med , vol.14 , Issue.7-8 , pp. 451-464
    • Irvine, G.B.1    El-Agnaf, O.M.2    Shankar, G.M.3    Walsh, D.M.4
  • 36
    • 0029925575 scopus 로고    scopus 로고
    • Myofibrillar myopathy with abnormal foci of desmin positivity. II. Immunocytochemical analysis reveals accumulation of multiple other proteins
    • De Bleecker J.L., Engel A.G., Ertl B.B. Myofibrillar myopathy with abnormal foci of desmin positivity. II. Immunocytochemical analysis reveals accumulation of multiple other proteins. J Neuropathol Exp Neurol. 1996, 55(5):563-577.
    • (1996) J Neuropathol Exp Neurol. , vol.55 , Issue.5 , pp. 563-577
    • De Bleecker, J.L.1    Engel, A.G.2    Ertl, B.B.3
  • 37
    • 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., Outzen H., Perander M., Overvatn 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(4):603-614.
    • (2005) J Cell Biol. , vol.171 , Issue.4 , pp. 603-614
    • Bjorkoy, G.1    Lamark, T.2    Brech, A.3    Outzen, H.4    Perander, M.5    Overvatn, A.6
  • 38
    • 4444220680 scopus 로고    scopus 로고
    • Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation
    • Seibenhener M.L., Babu J.R., Geetha T., Wong H.C., Krishna N.R., Wooten M.W. Sequestosome 1/p62 is a polyubiquitin chain binding protein involved in ubiquitin proteasome degradation. Mol Cell Biol. 2004, 24(18):8055-8068.
    • (2004) Mol Cell Biol. , vol.24 , Issue.18 , pp. 8055-8068
    • Seibenhener, M.L.1    Babu, J.R.2    Geetha, T.3    Wong, H.C.4    Krishna, N.R.5    Wooten, M.W.6
  • 39
    • 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., King Engel W., Askanas V. 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(3):407-413.
    • (2009) Acta Neuropathol. , vol.118 , Issue.3 , pp. 407-413
    • Nogalska, A.1    Terracciano, C.2    D'Agostino, C.3    King Engel, W.4    Askanas, V.5
  • 40
    • 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 R.B., Bilak M., Engel W.K., Askanas V. Difference in expression of phosphorylated tau epitopes between sporadic inclusion-body myositis and hereditary inclusion-body myopathies. J Neuropathol Exp Neurol. 1996, 55(7):774-786.
    • (1996) J Neuropathol Exp Neurol. , vol.55 , Issue.7 , pp. 774-786
    • Mirabella, M.1    Alvarez, R.B.2    Bilak, M.3    Engel, W.K.4    Askanas, V.5
  • 41
    • 0029944817 scopus 로고    scopus 로고
    • Use of anti-neurofilament antibody to identify paired-helical filaments in inclusion-body myositis
    • Askanas V., Alvarez R.B., Mirabella M., Engel W.K. Use of anti-neurofilament antibody to identify paired-helical filaments in inclusion-body myositis. Ann Neurol. 1996, 39(3):389-391.
    • (1996) Ann Neurol. , vol.39 , Issue.3 , pp. 389-391
    • Askanas, V.1    Alvarez, R.B.2    Mirabella, M.3    Engel, W.K.4
  • 42
    • 0026556331 scopus 로고
    • Immunocytochemical localization of ubiquitin in inclusion body myositis allows its light-microscopic distinction from polymyositis
    • Askanas V., Serdaroglu P., Engel W.K., Alvarez R.B. Immunocytochemical localization of ubiquitin in inclusion body myositis allows its light-microscopic distinction from polymyositis. Neurology. 1992, 42(2):460-461.
    • (1992) Neurology. , vol.42 , Issue.2 , pp. 460-461
    • Askanas, V.1    Serdaroglu, P.2    Engel, W.K.3    Alvarez, R.B.4
  • 43
    • 0030769397 scopus 로고    scopus 로고
    • Ubiquitin immunostaining and inclusion body myositis: study of 30 patients with inclusion body myositis
    • Prayson R.A., Cohen M.L. Ubiquitin immunostaining and inclusion body myositis: study of 30 patients with inclusion body myositis. Hum Pathol. 1997, 28:887-892.
    • (1997) Hum Pathol. , vol.28 , pp. 887-892
    • Prayson, R.A.1    Cohen, M.L.2
  • 44
    • 0014709081 scopus 로고
    • Alkaline phosphatase-positive abnormal muscle fibers of humans
    • Engel W.K., Cunningham G.G. Alkaline phosphatase-positive abnormal muscle fibers of humans. J Histochem Cytochem. 1970, 18(1):55-57.
    • (1970) J Histochem Cytochem. , vol.18 , Issue.1 , pp. 55-57
    • Engel, W.K.1    Cunningham, G.G.2
  • 45
    • 0031768071 scopus 로고    scopus 로고
    • Sporadic inclusion-body myositis and hereditary inclusion-body myopathies: current concepts of diagnosis and pathogenesis
    • Askanas V., Engel W.K. Sporadic inclusion-body myositis and hereditary inclusion-body myopathies: current concepts of diagnosis and pathogenesis. Curr Opin Rheumatol. 1998, 10(6):530-542.
    • (1998) Curr Opin Rheumatol. , vol.10 , Issue.6 , pp. 530-542
    • Askanas, V.1    Engel, W.K.2
  • 46
    • 0027444952 scopus 로고
    • Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis
    • Askanas V., Alvarez R.B., Engel W.K. Beta-amyloid precursor epitopes in muscle fibers of inclusion body myositis. Ann Neurol. 1993, 34(4):551-560.
    • (1993) Ann Neurol. , vol.34 , Issue.4 , pp. 551-560
    • Askanas, V.1    Alvarez, R.B.2    Engel, W.K.3
  • 49
    • 53149138951 scopus 로고    scopus 로고
    • TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia
    • Weihl C.C., Temiz P., Miller S.E., Watts G., Smith C., Forman M., et al. TDP-43 accumulation in inclusion body myopathy muscle suggests a common pathogenic mechanism with frontotemporal dementia. J Neurol Neurosurg Psychiatry. 2008, 79(10):1186-1189.
    • (2008) J Neurol Neurosurg Psychiatry. , vol.79 , Issue.10 , pp. 1186-1189
    • Weihl, C.C.1    Temiz, P.2    Miller, S.E.3    Watts, G.4    Smith, C.5    Forman, M.6
  • 51
    • 79953792404 scopus 로고    scopus 로고
    • In sporadic inclusion-body myositis muscle fibres TDP-43-positive inclusions are less frequent and robust than p62-inclusions, and are not associated with paired helical filaments
    • doi:10.1111/j.365-2990.010.01108.x
    • D'Agostino C, Nogalska A, Engel WK, Askanas V. In sporadic inclusion-body myositis muscle fibres TDP-43-positive inclusions are less frequent and robust than p62-inclusions, and are not associated with paired helical filaments. Neuropathol Appl Neurobiol. 2010: doi:10.1111/j.365-2990.010.01108.x.
    • (2010) Neuropathol Appl Neurobiol.
    • D'Agostino, C.1    Nogalska, A.2    Engel, W.K.3    Askanas, V.4
  • 52
    • 33644859083 scopus 로고    scopus 로고
    • Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting, Neurology
    • Ciechanover A. Intracellular protein degradation: from a vague idea thru the lysosome and the ubiquitin-proteasome system and onto human diseases and drug targeting. Neurology 2006;(66):7-19.
    • (2006) , Issue.66 , pp. 7-19
    • Ciechanover, A.1
  • 53
    • 77953463398 scopus 로고    scopus 로고
    • Protein degradation, aggregation, and misfolding
    • Cuervo A.M., Wong E.S., Martinez-Vicente M. Protein degradation, aggregation, and misfolding. Mov Disord. 2010, 25(S1):S49-S54.
    • (2010) Mov Disord. , vol.25 , Issue.1
    • Cuervo, A.M.1    Wong, E.S.2    Martinez-Vicente, M.3
  • 54
    • 38449091923 scopus 로고    scopus 로고
    • The autophagy-lysosomal degradation pathway: role in neurodegenerative disease and therapy
    • Shacka J.J., Roth K.A., Zhang J. The autophagy-lysosomal degradation pathway: role in neurodegenerative disease and therapy. Front Biosci. 2008, 13:718-736.
    • (2008) Front Biosci. , vol.13 , pp. 718-736
    • Shacka, J.J.1    Roth, K.A.2    Zhang, J.3
  • 55
    • 77954116814 scopus 로고    scopus 로고
    • Autophagy gone awry in neurodegenerative diseases
    • Wong E., Cuervo A.M. Autophagy gone awry in neurodegenerative diseases. Nat Neurosci. 2010, 13(7):805-811.
    • (2010) Nat Neurosci. , vol.13 , Issue.7 , pp. 805-811
    • Wong, E.1    Cuervo, A.M.2
  • 56
    • 56349168452 scopus 로고    scopus 로고
    • Autophagy and aging: keeping that old broom working
    • Cuervo A.M. Autophagy and aging: keeping that old broom working. Trends Genet. 2008, 24(12):604-612.
    • (2008) Trends Genet. , vol.24 , Issue.12 , pp. 604-612
    • Cuervo, A.M.1
  • 57
    • 33644861975 scopus 로고    scopus 로고
    • Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis
    • Glabe C.G., Kayed R. Common structure and toxic function of amyloid oligomers implies a common mechanism of pathogenesis. Neurology. 2006, 66(2 Suppl. 1):S74-S78.
    • (2006) Neurology. , vol.66 , Issue.2 SUPPL. 1
    • Glabe, C.G.1    Kayed, R.2
  • 58
    • 0033773935 scopus 로고    scopus 로고
    • Conformational disease
    • Kopito R.R., Ron D. Conformational disease. Nat Cell Biol. 2000, 2(11):E207-E209.
    • (2000) Nat Cell Biol. , vol.2 , Issue.11
    • Kopito, R.R.1    Ron, D.2
  • 59
    • 84885492217 scopus 로고    scopus 로고
    • Pathogenesis of sporadic inclusion-body myositis: role of cellular ageing and muscle-fibre degeneration associated with proteasomal and lysosomal inhibition, and accumulation of proteins that are also accumulated in brains of Alzheimer and Parkinson patients. Possible treatment avenues. In: Askanas V, Engel WK, editors. Muscle ageing, inclusion-body myositis and my
    • Askanas V, Engel WK, Nogalska A. Pathogenesis of sporadic inclusion-body myositis: role of cellular ageing and muscle-fibre degeneration associated with proteasomal and lysosomal inhibition, and accumulation of proteins that are also accumulated in brains of Alzheimer and Parkinson patients. Possible treatment avenues. In: Askanas V, Engel WK, editors. Muscle ageing, inclusion-body myositis and myopathies. Wiley-Blackwell; 2011 (in press).
    • Askanas, V.1    Engel, W.K.2    Nogalska, A.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., Ferrer I. Protein targets of oxidative damage in human neurodegenerative diseases with abnormal protein aggregates. Brain Pathol. 2010, 20(2):281-297.
    • (2010) Brain Pathol. , vol.20 , Issue.2 , pp. 281-297
    • Martinez, A.1    Portero-Otin, M.2    Pamplona, R.3    Ferrer, I.4
  • 61
    • 0030942146 scopus 로고    scopus 로고
    • Increase of nitric oxide synthases and nitrotyrosine in inclusion-body myositis
    • Yang C.C., Alvarez R.B., Engel W.K., Askanas V. Increase of nitric oxide synthases and nitrotyrosine in inclusion-body myositis. Neuroreport. 1996, 8(1):153-158.
    • (1996) Neuroreport. , vol.8 , Issue.1 , pp. 153-158
    • Yang, C.C.1    Alvarez, R.B.2    Engel, W.K.3    Askanas, V.4
  • 62
    • 13444287877 scopus 로고    scopus 로고
    • Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrite: implications for Alzheimer's disease
    • Reynolds M.R., Berry R.W., Binder L.I. Site-specific nitration and oxidative dityrosine bridging of the tau protein by peroxynitrite: implications for Alzheimer's disease. Biochemistry. 2005, 44(5):1690-1700.
    • (2005) Biochemistry. , vol.44 , Issue.5 , pp. 1690-1700
    • Reynolds, M.R.1    Berry, R.W.2    Binder, L.I.3
  • 63
    • 17644393495 scopus 로고    scopus 로고
    • Nitration and oligomerization of tau induced by peroxynitrite inhibit its microtubule-binding activity
    • Zhang Y.J., Xu Y.F., Chen X.Q., Wang X.C., Wang J.Z. Nitration and oligomerization of tau induced by peroxynitrite inhibit its microtubule-binding activity. FEBS Lett. 2005, 579(11):2421-2427.
    • (2005) FEBS Lett. , vol.579 , Issue.11 , pp. 2421-2427
    • Zhang, Y.J.1    Xu, Y.F.2    Chen, X.Q.3    Wang, X.C.4    Wang, J.Z.5
  • 64
    • 0026695045 scopus 로고
    • Light and electron microscopic localization of beta-amyloid protein in muscle biopsies of patients with inclusion-body myositis
    • Askanas V., Engel W.K., Alvarez R.B. Light and electron microscopic localization of beta-amyloid protein in muscle biopsies of patients with inclusion-body myositis. Am J Pathol. 1992, 141(1):31-36.
    • (1992) Am J Pathol. , vol.141 , Issue.1 , pp. 31-36
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3
  • 65
    • 0026595194 scopus 로고
    • Beta-amyloid protein immunoreactivity in muscle of patients with inclusion-body myositis
    • Askanas V., Engel W.K., Alvarez R.B., Glenner G.G. Beta-amyloid protein immunoreactivity in muscle of patients with inclusion-body myositis. Lancet. 1992, 339(8792):560-561.
    • (1992) Lancet. , vol.339 , Issue.8792 , pp. 560-561
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3    Glenner, G.G.4
  • 66
    • 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 W.K. 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(6):1673-1677.
    • (1998) Am J Pathol. , vol.153 , Issue.6 , pp. 1673-1677
    • Askanas, V.1    Engel, W.K.2
  • 67
    • 0031897126 scopus 로고    scopus 로고
    • Light and electron microscopic immunolocalization of presenilin 1 in abnormal muscle fibers of patients with sporadic inclusion-body myositis and autosomal-recessive inclusion-body myopathy
    • Askanas V., Engel W.K., Yang C.C., Alvarez R.B., Lee V.M., Wisniewski T. Light and electron microscopic immunolocalization of presenilin 1 in abnormal muscle fibers of patients with sporadic inclusion-body myositis and autosomal-recessive inclusion-body myopathy. Am J Pathol. 1998, 152(4):889-895.
    • (1998) Am J Pathol. , vol.152 , Issue.4 , pp. 889-895
    • Askanas, V.1    Engel, W.K.2    Yang, C.C.3    Alvarez, R.B.4    Lee, V.M.5    Wisniewski, T.6
  • 68
    • 0035830290 scopus 로고    scopus 로고
    • Presence of BACE1 and BACE2 in muscle fibres of patients with sporadic inclusion-body myositis
    • Vattemi G., Engel W.K., McFerrin J., Buxbaum J.D., Pastorino L., Askanas V. Presence of BACE1 and BACE2 in muscle fibres of patients with sporadic inclusion-body myositis. Lancet. 2001, 358(9297):1962-1964.
    • (2001) Lancet. , vol.358 , Issue.9297 , pp. 1962-1964
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Buxbaum, J.D.4    Pastorino, L.5    Askanas, V.6
  • 70
    • 0742289304 scopus 로고    scopus 로고
    • Nicastrin, a novel protein participating in amyloid-beta production, is overexpressed in sporadic inclusion-body myositis muscle
    • Vattemi G., Kefi M., Engel W.K., Askanas V. Nicastrin, a novel protein participating in amyloid-beta production, is overexpressed in sporadic inclusion-body myositis muscle. Neurology. 2003, 60:A315.
    • (2003) Neurology. , vol.60
    • Vattemi, G.1    Kefi, M.2    Engel, W.K.3    Askanas, V.4
  • 71
    • 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 W.K., Askanas V. 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, 112:389-396.
    • (2010) J Neurochem. , vol.112 , pp. 389-396
    • Terracciano, C.1    Nogalska, A.2    Engel, W.K.3    Askanas, V.4
  • 72
    • 33646862834 scopus 로고    scopus 로고
    • Phosphorylation of amyloid precursor protein (APP) at Thr668 regulates the nuclear translocation of the APP intracellular domain and induces neurodegeneration
    • Chang K.A., Kim H.S., Ha T.Y., Ha J.W., Shin K.Y., Jeong Y.H., et al. Phosphorylation of amyloid precursor protein (APP) at Thr668 regulates the nuclear translocation of the APP intracellular domain and induces neurodegeneration. Mol Cell Biol. 2006, 26(11):4327-4338.
    • (2006) Mol Cell Biol. , vol.26 , Issue.11 , pp. 4327-4338
    • Chang, K.A.1    Kim, H.S.2    Ha, T.Y.3    Ha, J.W.4    Shin, K.Y.5    Jeong, Y.H.6
  • 73
    • 0142123260 scopus 로고    scopus 로고
    • APP processing is regulated by cytoplasmic phosphorylation
    • Lee M.S., Kao S.C., Lemere C.A., Xia W., Tseng H.C., Zhou Y., et al. APP processing is regulated by cytoplasmic phosphorylation. J Cell Biol. 2003, 163(1):83-95.
    • (2003) J Cell Biol. , vol.163 , Issue.1 , pp. 83-95
    • Lee, M.S.1    Kao, S.C.2    Lemere, C.A.3    Xia, W.4    Tseng, H.C.5    Zhou, Y.6
  • 75
    • 0034647786 scopus 로고    scopus 로고
    • Oligomerization and toxicity of beta-amyloid-42 implicated in Alzheimer's disease
    • El-Agnaf O.M., Mahil D.S., Patel B.P., Austen B.M. Oligomerization and toxicity of beta-amyloid-42 implicated in Alzheimer's disease. Biochem Biophys Res Commun. 2000, 273(3):1003-1007.
    • (2000) Biochem Biophys Res Commun. , vol.273 , Issue.3 , pp. 1003-1007
    • El-Agnaf, O.M.1    Mahil, D.S.2    Patel, B.P.3    Austen, B.M.4
  • 76
    • 34248547813 scopus 로고    scopus 로고
    • Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases
    • Ferreira S.T., Vieira M.N., De Felice F.G. Soluble protein oligomers as emerging toxins in Alzheimer's and other amyloid diseases. IUBMB Life. 2007, 59(4-5):332-345.
    • (2007) IUBMB Life. , vol.59 , Issue.4-5 , pp. 332-345
    • Ferreira, S.T.1    Vieira, M.N.2    De Felice, F.G.3
  • 77
    • 0035159785 scopus 로고    scopus 로고
    • Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease
    • Glabe C. Intracellular mechanisms of amyloid accumulation and pathogenesis in Alzheimer's disease. J Mol Neurosci. 2001, 17(2):137-145.
    • (2001) J Mol Neurosci. , vol.17 , Issue.2 , pp. 137-145
    • Glabe, C.1
  • 78
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-beta in Alzheimer's disease
    • LaFerla F.M., Green K.N., Oddo S. Intracellular amyloid-beta in Alzheimer's disease. Nat Rev Neurosci. 2007, 8(7):499-509.
    • (2007) Nat Rev Neurosci. , vol.8 , Issue.7 , pp. 499-509
    • LaFerla, F.M.1    Green, K.N.2    Oddo, S.3
  • 79
    • 78149406278 scopus 로고    scopus 로고
    • Novel demonstration of amyloid-beta oligomers in sporadic inclusion-body myositis muscle fibers
    • Nogalska A., D'Agostino C., Engel W.K., Klein W.L., Askanas V. Novel demonstration of amyloid-beta oligomers in sporadic inclusion-body myositis muscle fibers. Acta Neuropathol. 2010, 120:661-666.
    • (2010) Acta Neuropathol. , vol.120 , pp. 661-666
    • Nogalska, A.1    D'Agostino, C.2    Engel, W.K.3    Klein, W.L.4    Askanas, V.5
  • 80
    • 11544279355 scopus 로고    scopus 로고
    • Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins
    • Lambert M.P., Barlow A.K., Chromy B.A., Edwards C., Freed R., Liosatos M., et al. Diffusible, nonfibrillar ligands derived from Abeta1-42 are potent central nervous system neurotoxins. Proc Natl Acad Sci U S A 1998, 95(11):6448-6453.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.11 , pp. 6448-6453
    • Lambert, M.P.1    Barlow, A.K.2    Chromy, B.A.3    Edwards, C.4    Freed, R.5    Liosatos, M.6
  • 81
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease
    • Klein W.L., Stine W.B., Teplow D.B. Small assemblies of unmodified amyloid beta-protein are the proximate neurotoxin in Alzheimer's disease. Neurobiol Aging. 2004, 25(5):569-580.
    • (2004) Neurobiol Aging. , vol.25 , Issue.5 , pp. 569-580
    • Klein, W.L.1    Stine, W.B.2    Teplow, D.B.3
  • 82
    • 0038472441 scopus 로고    scopus 로고
    • Colocalizes with amyloid-beta and coimmunoprecipitates with amyloid-beta precursor protein in sporadic inclusion-body myositis muscles
    • Vattemi G., Engel W.K., McFerrin J., Askanas V., Cystatin C colocalizes with amyloid-beta and coimmunoprecipitates with amyloid-beta precursor protein in sporadic inclusion-body myositis muscles. J Neurochem. 2003, 85(6):1539-1546.
    • (2003) J Neurochem. , vol.85 , Issue.6 , pp. 1539-1546
    • Vattemi, G.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4    Cystatin, C.5
  • 83
    • 0040190385 scopus 로고    scopus 로고
    • Sporadic inclusion body myositis correlates with increased expression and cross-linking by transglutaminases 1 and 2
    • Choi Y.C., Park G.T., Kim T.S., Sunwoo I.N., Steinert P.M., Kim S.Y. Sporadic inclusion body myositis correlates with increased expression and cross-linking by transglutaminases 1 and 2. J Biol Chem. 2000, 275(12):8703-8710.
    • (2000) J Biol Chem. , vol.275 , Issue.12 , pp. 8703-8710
    • Choi, Y.C.1    Park, G.T.2    Kim, T.S.3    Sunwoo, I.N.4    Steinert, P.M.5    Kim, S.Y.6
  • 85
    • 33845217281 scopus 로고    scopus 로고
    • AbetaPP-overexpression and proteasome inhibition increase alphaB-crystallin in cultured human muscle: relevance to inclusion-body myositis
    • Wojcik S., Engel W.K., McFerrin J., Paciello O., Askanas V. AbetaPP-overexpression and proteasome inhibition increase alphaB-crystallin in cultured human muscle: relevance to inclusion-body myositis. Neuromuscul Disord. 2006, 16(12):839-844.
    • (2006) Neuromuscul Disord. , vol.16 , Issue.12 , pp. 839-844
    • Wojcik, S.1    Engel, W.K.2    McFerrin, J.3    Paciello, O.4    Askanas, V.5
  • 86
    • 0032986520 scopus 로고    scopus 로고
    • Alpha-crystallin as a molecular chaperone
    • Derham B.K., Harding J.J. Alpha-crystallin as a molecular chaperone. Prog Retin Eye Res. 1999, 18(4):463-509.
    • (1999) Prog Retin Eye Res. , vol.18 , Issue.4 , pp. 463-509
    • Derham, B.K.1    Harding, J.J.2
  • 87
    • 20444478694 scopus 로고    scopus 로고
    • The small heat shock proteins and their role in human disease
    • Sun Y., MacRae T.H. The small heat shock proteins and their role in human disease. FEBS J. 2005, 272(11):2613-2627.
    • (2005) FEBS J. , vol.272 , Issue.11 , pp. 2613-2627
    • Sun, Y.1    MacRae, T.H.2
  • 88
    • 49149117491 scopus 로고    scopus 로고
    • Tau aggregation and toxicity in tauopathic neurodegenerative diseases
    • Honson N.S., Kuret J. Tau aggregation and toxicity in tauopathic neurodegenerative diseases. J Alzheimers Dis. 2008, 14(4):417-422.
    • (2008) J Alzheimers Dis. , vol.14 , Issue.4 , pp. 417-422
    • Honson, N.S.1    Kuret, J.2
  • 90
    • 0342519699 scopus 로고
    • Recognition of tau epitopes by anti-neurofilament antibodies that bind to Alzheimer neurofibrillary tangles
    • Ksiezak-Reding H., Dickson D.W., Davies P., Yen S.H. Recognition of tau epitopes by anti-neurofilament antibodies that bind to Alzheimer neurofibrillary tangles. Proc Natl Acad Sci U S A 1987, 84(10):3410-3414.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , Issue.10 , pp. 3410-3414
    • Ksiezak-Reding, H.1    Dickson, D.W.2    Davies, P.3    Yen, S.H.4
  • 91
    • 0028246491 scopus 로고
    • Twisted tubulofilaments of inclusion body myositis muscle resemble paired helical filaments of Alzheimer brain and contain hyperphosphorylated tau
    • Askanas V., Engel W.K., Bilak M., Alvarez R.B., Selkoe D.J. Twisted tubulofilaments of inclusion body myositis muscle resemble paired helical filaments of Alzheimer brain and contain hyperphosphorylated tau. Am J Pathol. 1994, 144(1):177-187.
    • (1994) Am J Pathol. , vol.144 , Issue.1 , pp. 177-187
    • Askanas, V.1    Engel, W.K.2    Bilak, M.3    Alvarez, R.B.4    Selkoe, D.J.5
  • 92
    • 0030783142 scopus 로고    scopus 로고
    • A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease
    • Jicha G.A., Lane E., Vincent I., Otvos L., Hoffmann R., Davies P. A conformation- and phosphorylation-dependent antibody recognizing the paired helical filaments of Alzheimer's disease. J Neurochem. 1997, 69(5):2087-2095.
    • (1997) J Neurochem. , vol.69 , Issue.5 , pp. 2087-2095
    • Jicha, G.A.1    Lane, E.2    Vincent, I.3    Otvos, L.4    Hoffmann, R.5    Davies, P.6
  • 93
    • 0032521599 scopus 로고    scopus 로고
    • Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation
    • Zheng-Fischhèofer Q., Biernat J., Mandelkow E.M., Illenberger S., Godemann R., Mandelkow E. Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation. Eur J Biochem. 1998, 252(3):542-552.
    • (1998) Eur J Biochem. , vol.252 , Issue.3 , pp. 542-552
    • Zheng-Fischhèofer, Q.1    Biernat, J.2    Mandelkow, E.M.3    Illenberger, S.4    Godemann, R.5    Mandelkow, E.6
  • 95
    • 0033897261 scopus 로고    scopus 로고
    • Association of active extracellular signal-regulated protein kinase with paired helical filaments of inclusion-body myositis muscle suggests its role in inclusion-body myositis tau phosphorylation
    • Wilczynski G.M., Engel W.K., Askanas V. Association of active extracellular signal-regulated 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(6):1835-1840.
    • (2000) Am J Pathol. , vol.156 , Issue.6 , pp. 1835-1840
    • Wilczynski, G.M.1    Engel, W.K.2    Askanas, V.3
  • 96
    • 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 G.M., Engel W.K., 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(1):33-36.
    • (2000) Neurosci Lett. , vol.293 , Issue.1 , pp. 33-36
    • Wilczynski, G.M.1    Engel, W.K.2    Askanas, V.3
  • 97
    • 4243616488 scopus 로고    scopus 로고
    • Novel proposed role of glycogen synthase kinase 3beta in the pathogenesis of inclusion body myositis
    • Wilczynski G.M., Broccolini A., Engel W.K., Askanas V. Novel proposed role of glycogen synthase kinase 3beta in the pathogenesis of inclusion body myositis. Neurology. 2001, 56(Suppl. 3):A464.
    • (2001) Neurology. , vol.56 , Issue.SUPPL. 3
    • Wilczynski, G.M.1    Broccolini, A.2    Engel, W.K.3    Askanas, V.4
  • 98
    • 38349050020 scopus 로고    scopus 로고
    • Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis
    • Kannanayakal T.J., Mendell J.R., Kuret J. Casein kinase 1 alpha associates with the tau-bearing lesions of inclusion body myositis. Neurosci Lett. 2008, 431(2):141-145.
    • (2008) Neurosci Lett. , vol.431 , Issue.2 , pp. 141-145
    • Kannanayakal, T.J.1    Mendell, J.R.2    Kuret, J.3
  • 99
    • 0033849528 scopus 로고    scopus 로고
    • Paired helical filaments of inclusion-body myositis muscle contain RNA and survival motor neuron protein
    • Broccolini A., Engel W.K., Alvarez R.B., Askanas V. Paired helical filaments of inclusion-body myositis muscle contain RNA and survival motor neuron protein. Am J Pathol. 2000, 156(4):1151-1155.
    • (2000) Am J Pathol. , vol.156 , Issue.4 , pp. 1151-1155
    • Broccolini, A.1    Engel, W.K.2    Alvarez, R.B.3    Askanas, V.4
  • 101
    • 33744739867 scopus 로고    scopus 로고
    • Genetically augmenting Abeta42 levels in skeletal muscle exacerbates inclusion body myositis-like pathology and motor deficits in transgenic mice
    • Kitazawa M., Green K.N., Caccamo A., LaFerla F.M. Genetically augmenting Abeta42 levels in skeletal muscle exacerbates inclusion body myositis-like pathology and motor deficits in transgenic mice. Am J Pathol. 2006, 168(6):1986-1997.
    • (2006) Am J Pathol. , vol.168 , Issue.6 , pp. 1986-1997
    • Kitazawa, M.1    Green, K.N.2    Caccamo, A.3    LaFerla, F.M.4
  • 102
    • 68349108020 scopus 로고    scopus 로고
    • The ubiquitin proteasome system in neuropathology
    • Lehman N.L. The ubiquitin proteasome system in neuropathology. Acta Neuropathol. 2009, 118:329-347.
    • (2009) Acta Neuropathol. , vol.118 , pp. 329-347
    • Lehman, N.L.1
  • 103
    • 77957001697 scopus 로고    scopus 로고
    • Acetylation of tau inhibits its degradation and contributes to tauopathy
    • Min S.W., Cho S.H., Zhou Y., Schroeder S., Haroutunian V., Seeley W.W., et al. Acetylation of tau inhibits its degradation and contributes to tauopathy. Neuron. 2010, 67(6):953-966.
    • (2010) Neuron. , vol.67 , Issue.6 , pp. 953-966
    • Min, S.W.1    Cho, S.H.2    Zhou, Y.3    Schroeder, S.4    Haroutunian, V.5    Seeley, W.W.6
  • 104
    • 70349987102 scopus 로고    scopus 로고
    • Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing
    • Wang Y., Martinez-Vicente M., Kruger U., Kaushik S., Wong E., Mandelkow E.M., et al. Tau fragmentation, aggregation and clearance: the dual role of lysosomal processing. Hum Mol Genet. 2009, 18(21):4153-4170.
    • (2009) Hum Mol Genet. , vol.18 , Issue.21 , pp. 4153-4170
    • Wang, Y.1    Martinez-Vicente, M.2    Kruger, U.3    Kaushik, S.4    Wong, E.5    Mandelkow, E.M.6
  • 105
    • 77954953341 scopus 로고    scopus 로고
    • Decreased SIRT1 deacetylase activity in sporadic inclusion-body myositis muscle fibers
    • Nogalska A., D'Agostino C., Engel W.K., Davies K.J., Askanas V. Decreased SIRT1 deacetylase activity in sporadic inclusion-body myositis muscle fibers. Neurobiol Aging. 2010, 31:1637-1648.
    • (2010) Neurobiol Aging. , vol.31 , pp. 1637-1648
    • Nogalska, A.1    D'Agostino, C.2    Engel, W.K.3    Davies, K.J.4    Askanas, V.5
  • 107
    • 68649095418 scopus 로고    scopus 로고
    • Molecular mechanisms of [alpha]-synuclein neurodegeneration
    • Waxman E.A., Giasson B.I. Molecular mechanisms of [alpha]-synuclein neurodegeneration. Biochim Biophys Acta Mol Basis Dis. 2009, 1792(7):616-624.
    • (2009) Biochim Biophys Acta Mol Basis Dis. , vol.1792 , Issue.7 , pp. 616-624
    • Waxman, E.A.1    Giasson, B.I.2
  • 108
    • 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 W.K., Alvarez R.B., McFerrin J., Broccolini A. 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(7):592-598.
    • (2000) J Neuropathol Exp Neurol. , vol.59 , Issue.7 , pp. 592-598
    • Askanas, V.1    Engel, W.K.2    Alvarez, R.B.3    McFerrin, J.4    Broccolini, A.5
  • 109
    • 33747477123 scopus 로고    scopus 로고
    • Parkin and its association with alpha-synuclein and AbetaPP in inclusion-body myositis and AbetaPP-overexpressing cultured human muscle fibers
    • Paciello O., Wojcik S., Engel W.K., McFerrin J., Askanas V. Parkin and its association with alpha-synuclein and AbetaPP in inclusion-body myositis and AbetaPP-overexpressing cultured human muscle fibers. Acta Myol 2006, 25(1):13-22.
    • (2006) Acta Myol , vol.25 , Issue.1 , pp. 13-22
    • Paciello, O.1    Wojcik, S.2    Engel, W.K.3    McFerrin, J.4    Askanas, V.5
  • 110
    • 0035854437 scopus 로고    scopus 로고
    • Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease
    • Shimura H., Schlossmacher M.G., Hattori N., Frosch M.P., Trockenbacher A., Schneider R., et al. Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease. Science 2001, 293(5528):263-269.
    • (2001) Science , vol.293 , Issue.5528 , pp. 263-269
    • Shimura, H.1    Schlossmacher, M.G.2    Hattori, N.3    Frosch, M.P.4    Trockenbacher, A.5    Schneider, R.6
  • 111
    • 33646713455 scopus 로고    scopus 로고
    • Inclusion-body myositis: clinical and pathologic aspects, and basic research potentially relevant to treatment
    • Askanas V., Dalakas M.C., Engel W.K. Inclusion-body myositis: clinical and pathologic aspects, and basic research potentially relevant to treatment. Neurology. 2006, 66(2 Suppl. 1):Si.
    • (2006) Neurology. , vol.66 , Issue.2 SUPPL. 1
    • Askanas, V.1    Dalakas, M.C.2    Engel, W.K.3
  • 112
    • 0036095285 scopus 로고    scopus 로고
    • Parkin localizes to the Lewy bodies of Parkinson disease and dementia with Lewy bodies
    • Schlossmacher M.G., Frosch M.P., Gai W.P., Medina M., Sharma N., Forno L., et al. Parkin localizes to the Lewy bodies of Parkinson disease and dementia with Lewy bodies. Am J Pathol. 2002, 160:1655-1667.
    • (2002) Am J Pathol. , vol.160 , pp. 1655-1667
    • Schlossmacher, M.G.1    Frosch, M.P.2    Gai, W.P.3    Medina, M.4    Sharma, N.5    Forno, L.6
  • 113
    • 0038159253 scopus 로고    scopus 로고
    • Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function
    • Tsai Y.C., Fishman P.S., Thakor N.V., Oyler G.A. Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function. J Biol Chem. 2003, 278(24):22044-22055.
    • (2003) J Biol Chem. , vol.278 , Issue.24 , pp. 22044-22055
    • Tsai, Y.C.1    Fishman, P.S.2    Thakor, N.V.3    Oyler, G.A.4
  • 114
    • 79953780709 scopus 로고    scopus 로고
    • Alpha-synuclein and Parkin are novel proteins accumulated in ragged-red fibers
    • Paciello O., Wojcik S., Engel W.K., Askanas V. Alpha-synuclein and Parkin are novel proteins accumulated in ragged-red fibers. Neuromuscul Disord. 2006, 16:657.
    • (2006) Neuromuscul Disord. , vol.16 , pp. 657
    • Paciello, O.1    Wojcik, S.2    Engel, W.K.3    Askanas, V.4
  • 115
    • 33646676002 scopus 로고
    • "Ragged-red fibers" in opthamoplegia syndromes and their differential diagnosis
    • Engel W.K. "Ragged-red fibers" in opthamoplegia syndromes and their differential diagnosis. Excerpta Med Int Cong Series 1971, 237:28.
    • (1971) Excerpta Med Int Cong Series , vol.237 , pp. 28
    • Engel, W.K.1
  • 117
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D., Tanaka A., Suen D.F., Youle R.J. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol. 2008, 183(5):795-803.
    • (2008) J Cell Biol. , vol.183 , Issue.5 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 118
    • 75949104449 scopus 로고    scopus 로고
    • Mitochondria get a Parkin' ticket
    • Wild P., Dikic I. Mitochondria get a Parkin' ticket. Nat Cell Biol. 2010, 12(2):104-106.
    • (2010) Nat Cell Biol. , vol.12 , Issue.2 , pp. 104-106
    • Wild, P.1    Dikic, I.2
  • 120
    • 24344458115 scopus 로고    scopus 로고
    • Myostatin is increased and complexes with amyloid-beta within sporadic inclusion-body myositis muscle fibers
    • Wojcik S., Engel W.K., McFerrin J., Askanas V. Myostatin is increased and complexes with amyloid-beta within sporadic inclusion-body myositis muscle fibers. Acta Neuropathol. 2005, 110(2):173-177.
    • (2005) Acta Neuropathol. , vol.110 , Issue.2 , pp. 173-177
    • Wojcik, S.1    Engel, W.K.2    McFerrin, J.3    Askanas, V.4
  • 121
    • 33847717940 scopus 로고    scopus 로고
    • Myostatin precursor protein is increased and associates with amyloid-beta precursor protein in inclusion-body myositis culture model
    • Wojcik S., Nogalska A., McFerrin J., Engel W.K., Oledzka G., Askanas V. Myostatin precursor protein is increased and associates with amyloid-beta precursor protein in inclusion-body myositis culture model. Neuropathol Appl Neurobiol. 2007, 33(2):238-242.
    • (2007) Neuropathol Appl Neurobiol. , vol.33 , Issue.2 , pp. 238-242
    • Wojcik, S.1    Nogalska, A.2    McFerrin, J.3    Engel, W.K.4    Oledzka, G.5    Askanas, V.6
  • 122
    • 77949466236 scopus 로고    scopus 로고
    • Cytotoxic aggregation and amyloid formation by the myostatin precursor protein
    • Starck C.S., Sutherland-Smith A.J. Cytotoxic aggregation and amyloid formation by the myostatin precursor protein. PLoS ONE. 2010, 5(2):e9170.
    • (2010) PLoS ONE. , vol.5 , Issue.2
    • Starck, C.S.1    Sutherland-Smith, A.J.2
  • 123
    • 38949096081 scopus 로고    scopus 로고
    • Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome
    • Ding W.X., Yin X.M. Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome. Autophagy. 2008, 4(2):141-150.
    • (2008) Autophagy. , vol.4 , Issue.2 , pp. 141-150
    • Ding, W.X.1    Yin, X.M.2
  • 124
    • 38349046973 scopus 로고    scopus 로고
    • Autophagy, amyloidogenesis and Alzheimer disease
    • Nixon R.A. Autophagy, amyloidogenesis and Alzheimer disease. J Cell Sci. 2007, 120(Pt 23):4081-4091.
    • (2007) J Cell Sci. , vol.120 , Issue.PART 23 , pp. 4081-4091
    • Nixon, R.A.1
  • 126
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: a molecular machine designed for controlled proteolysis
    • Voges D., Zwickl P., Baumeister W. The 26S proteasome: a molecular machine designed for controlled proteolysis. Annu Rev Biochem 1999, 68:1015-1068.
    • (1999) Annu Rev Biochem , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 127
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: a molecular machine designed for controlled PRoteolysis
    • Voges D., Zwickl P., Baumeister W. The 26S proteasome: a molecular machine designed for controlled PRoteolysis. Annu Rev Biochem 1999, 68(1):1015-1068.
    • (1999) Annu Rev Biochem , vol.68 , Issue.1 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 129
    • 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(2):363-373.
    • (2008) J Cell Mol Med. , vol.12 , Issue.2 , pp. 363-373
    • Oddo, S.1
  • 130
    • 42749092968 scopus 로고    scopus 로고
    • Amyloid peptides in different assembly states and related effects on isolated and cellular proteasomes
    • Cecarini V., Bonfili L., Amici M., Angeletti M., Keller J.N., Eleuteri A.M. Amyloid peptides in different assembly states and related effects on isolated and cellular proteasomes. Brain Res. 2008, 1209:8-18.
    • (2008) Brain Res. , vol.1209 , pp. 8-18
    • Cecarini, V.1    Bonfili, L.2    Amici, M.3    Angeletti, M.4    Keller, J.N.5    Eleuteri, A.M.6
  • 131
    • 51449096696 scopus 로고    scopus 로고
    • A[beta] inhibits the proteasome and enhances amyloid and tau accumulation
    • Tseng B.P., Green K.N., Chan J.L., Blurton-Jones M., LaFerla F.M. A[beta] inhibits the proteasome and enhances amyloid and tau accumulation. Neurobiol Aging. 2008, 29(11):1607-1618.
    • (2008) Neurobiol Aging. , vol.29 , Issue.11 , pp. 1607-1618
    • Tseng, B.P.1    Green, K.N.2    Chan, J.L.3    Blurton-Jones, M.4    LaFerla, F.M.5
  • 132
    • 4644328932 scopus 로고    scopus 로고
    • 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., Askanas V. Mutant ubiquitin UBB+1 is accumulated in sporadic inclusion-body myositis muscle fibers. Neurology. 2004, 63(6):1114-1117.
    • (2004) Neurology. , vol.63 , Issue.6 , pp. 1114-1117
    • Fratta, P.1    Engel, W.K.2    Van Leeuwen, F.W.3    Hol, E.M.4    Vattemi, G.5    Askanas, V.6
  • 133
    • 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., Ullrich O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J Neurochem. 2003, 85(1):115-122.
    • (2003) J Neurochem. , vol.85 , Issue.1 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 134
    • 1842424791 scopus 로고    scopus 로고
    • Proteasomal inhibition by alpha-synuclein filaments and oligomers
    • Lindersson E., Beedholm R., Hojrup P., Moos T., Gai W., Hendil K.B., et al. Proteasomal inhibition by alpha-synuclein filaments and oligomers. J Biol Chem. 2004, 279(13):12924-12934.
    • (2004) J Biol Chem. , vol.279 , Issue.13 , pp. 12924-12934
    • Lindersson, E.1    Beedholm, R.2    Hojrup, P.3    Moos, T.4    Gai, W.5    Hendil, K.B.6
  • 135
    • 76749094093 scopus 로고    scopus 로고
    • Misframed Proteins and Neurodegeneration: A Novel View on Alzheimer's and Parkinson's Diseases
    • Dennissen F.J.A., Kholod N., Steinbusch H.W.M., Van Leeuwen F.W. Misframed Proteins and Neurodegeneration: A Novel View on Alzheimer's and Parkinson's Diseases. Neurodegener Dis. 2010, 7(1-3):76-79.
    • (2010) Neurodegener Dis. , vol.7 , Issue.1-3 , pp. 76-79
    • Dennissen, F.J.A.1    Kholod, N.2    Steinbusch, H.W.M.3    Van Leeuwen, F.W.4
  • 136
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He C., Klionsky D.J. 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
  • 137
    • 33747881231 scopus 로고    scopus 로고
    • Autophagy in neurodegenerative disease: friend, foe or turncoat?
    • Nixon R.A. Autophagy in neurodegenerative disease: friend, foe or turncoat?. Trends Neurosci. 2006, 29(9):528-535.
    • (2006) Trends Neurosci. , vol.29 , Issue.9 , pp. 528-535
    • Nixon, R.A.1
  • 138
    • 14844303381 scopus 로고    scopus 로고
    • Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study
    • Nixon R.A., Wegiel J., Kumar A., Yu W.H., Peterhoff C., Cataldo A., et al. Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study. J Neuropathol Exp Neurol. 2005, 64(2):113-122.
    • (2005) J Neuropathol Exp Neurol. , vol.64 , Issue.2 , pp. 113-122
    • Nixon, R.A.1    Wegiel, J.2    Kumar, A.3    Yu, W.H.4    Peterhoff, C.5    Cataldo, A.6
  • 139
    • 26944443274 scopus 로고    scopus 로고
    • Inclusion body myositis. In: Engel AG, editor. Myology. 3rd ed. McGraw-Hill Professional
    • Mikol J, Engel AG. Inclusion body myositis. In: Engel AG, editor. Myology. 3rd ed. McGraw-Hill Professional; 2004. p. 1367-88.
    • (2004) , pp. 1367-88
    • Mikol, J.1    Engel, A.G.2
  • 140
    • 38949108670 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes
    • Klionsky D.J., Abeliovich H., Agostinis P., Agrawal D.K., Aliev G., Askew D.S., et al. Guidelines for the use and interpretation of assays for monitoring autophagy in higher eukaryotes. Autophagy. 2008, 4(2):151-175.
    • (2008) Autophagy. , vol.4 , Issue.2 , pp. 151-175
    • Klionsky, D.J.1    Abeliovich, H.2    Agostinis, P.3    Agrawal, D.K.4    Aliev, G.5    Askew, D.S.6
  • 141
    • 41149085729 scopus 로고    scopus 로고
    • Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression
    • Hamano T., Gendron T.F., Causevic E., Yen S.H., Lin W.L., Isidoro C., et al. Autophagic-lysosomal perturbation enhances tau aggregation in transfectants with induced wild-type tau expression. Eur J Neurosci. 2008, 27(5):1119-1130.
    • (2008) Eur J Neurosci. , vol.27 , Issue.5 , pp. 1119-1130
    • Hamano, T.1    Gendron, T.F.2    Causevic, E.3    Yen, S.H.4    Lin, W.L.5    Isidoro, C.6
  • 143
    • 26444587508 scopus 로고    scopus 로고
    • Macroautophagy: a novel Beta-amyloid peptide-generating pathway activated in Alzheimer's disease
    • Yu W.H., Cuervo A.M., Kumar A., Peterhoff C.M., Schmidt S.D., Lee J.H., et al. Macroautophagy: a novel Beta-amyloid peptide-generating pathway activated in Alzheimer's disease. J Cell Biol. 2005, 171(1):87-98.
    • (2005) J Cell Biol. , vol.171 , Issue.1 , pp. 87-98
    • Yu, W.H.1    Cuervo, A.M.2    Kumar, A.3    Peterhoff, C.M.4    Schmidt, S.D.5    Lee, J.H.6
  • 144
    • 33644858343 scopus 로고    scopus 로고
    • The unfolded protein response: a stress signaling pathway critical for health and disease
    • Zhang K., Kaufman R.J. The unfolded protein response: a stress signaling pathway critical for health and disease. Neurology. 2006, 66(2 Suppl. 1):S102-S109.
    • (2006) Neurology. , vol.66 , Issue.2 SUPPL. 1
    • Zhang, K.1    Kaufman, R.J.2
  • 145
    • 47949099916 scopus 로고    scopus 로고
    • From endoplasmic-reticulum stress to the inflammatory response
    • Zhang K., Kaufman R.J. From endoplasmic-reticulum stress to the inflammatory response. Nature. 2008, 454(7203):455-462.
    • (2008) Nature. , vol.454 , Issue.7203 , pp. 455-462
    • Zhang, K.1    Kaufman, R.J.2
  • 146
    • 79953783269 scopus 로고    scopus 로고
    • Putative pathogenic role of the endoplasmic reticulum stress in sporadic inclusion-body myositis
    • Nogalska A., Engel W.K., Askanas V. Putative pathogenic role of the endoplasmic reticulum stress in sporadic inclusion-body myositis. Acta Myol. 2010, 29:143-144.
    • (2010) Acta Myol. , vol.29 , pp. 143-144
    • Nogalska, A.1    Engel, W.K.2    Askanas, V.3
  • 147
    • 75149192820 scopus 로고    scopus 로고
    • Sirtuins as novel targets for Alzheimer's disease and other neurodegenerative disorders: experimental and genetic evidence
    • Albani D., Polito L., Forloni G. Sirtuins as novel targets for Alzheimer's disease and other neurodegenerative disorders: experimental and genetic evidence. J Alzheimers Dis. 2010, 19(1):11-26.
    • (2010) J Alzheimers Dis. , vol.19 , Issue.1 , pp. 11-26
    • Albani, D.1    Polito, L.2    Forloni, G.3
  • 148
    • 77049098395 scopus 로고    scopus 로고
    • Sirt1's complex roles in neuroprotection
    • Tang B.L. Sirt1's complex roles in neuroprotection. Cell Mol Neurobiol. 2009, 29(8):1093-1103.
    • (2009) Cell Mol Neurobiol. , vol.29 , Issue.8 , pp. 1093-1103
    • Tang, B.L.1
  • 149
    • 33746824192 scopus 로고    scopus 로고
    • Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction
    • Qin W., Yang T., Ho L., Zhao Z., Wang J., Chen L., et al. Neuronal SIRT1 activation as a novel mechanism underlying the prevention of Alzheimer disease amyloid neuropathology by calorie restriction. J Biol Chem. 2006, 281(31):21745-21754.
    • (2006) J Biol Chem. , vol.281 , Issue.31 , pp. 21745-21754
    • Qin, W.1    Yang, T.2    Ho, L.3    Zhao, Z.4    Wang, J.5    Chen, L.6
  • 150
    • 28844474597 scopus 로고    scopus 로고
    • SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling
    • Chen J., Zhou Y., Mueller-Steiner S., Chen L.F., Kwon H., Yi S., et al. SIRT1 protects against microglia-dependent amyloid-beta toxicity through inhibiting NF-kappaB signaling. J Biol Chem. 2005, 280(48):40364-40374.
    • (2005) J Biol Chem. , vol.280 , Issue.48 , pp. 40364-40374
    • Chen, J.1    Zhou, Y.2    Mueller-Steiner, S.3    Chen, L.F.4    Kwon, H.5    Yi, S.6
  • 152
    • 3242719545 scopus 로고    scopus 로고
    • Modulation of NF-kappaBdependent transcription and cell survival by the SIRT1 deacetylase
    • Yeung F., Hoberg J.E., Ramsey C.S., Keller M.D., Jones D.R., Frye R.A., et al. Modulation of NF-kappaBdependent transcription and cell survival by the SIRT1 deacetylase. EMBO J 2004, 23(12):2369-2380.
    • (2004) EMBO J , vol.23 , Issue.12 , pp. 2369-2380
    • Yeung, F.1    Hoberg, J.E.2    Ramsey, C.S.3    Keller, M.D.4    Jones, D.R.5    Frye, R.A.6
  • 153
    • 24144484625 scopus 로고    scopus 로고
    • Molecular pathology and pathogenesis of inclusion-body myositis
    • Askanas V., Engel W.K. Molecular pathology and pathogenesis of inclusion-body myositis. Microsc Res Tech. 2005, 67(3-4):114-120.
    • (2005) Microsc Res Tech. , vol.67 , Issue.3-4 , pp. 114-120
    • Askanas, V.1    Engel, W.K.2
  • 154
    • 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 W.K., McFerrin J., Askanas V. Endoplasmic reticulum stress induces myostatin precursor protein and NF-kappaB in cultured human muscle fibers: relevance to inclusion body myositis. Exp Neurol. 2007, 204(2):610-618.
    • (2007) Exp Neurol. , vol.204 , Issue.2 , pp. 610-618
    • Nogalska, A.1    Wojcik, S.2    Engel, W.K.3    McFerrin, J.4    Askanas, V.5
  • 155
    • 33646826619 scopus 로고    scopus 로고
    • Oxidative damage of DJ-1 is linked to sporadic Parkinson and Alzheimer diseases
    • Choi J., Sullards M.C., Olzmann J.A., Rees H.D., Weintraub S.T., Bostwick D.E., et al. Oxidative damage of DJ-1 is linked to sporadic Parkinson and Alzheimer diseases. J Biol Chem. 2006, 281(16):10816-10824.
    • (2006) J Biol Chem. , vol.281 , Issue.16 , pp. 10816-10824
    • Choi, J.1    Sullards, M.C.2    Olzmann, J.A.3    Rees, H.D.4    Weintraub, S.T.5    Bostwick, D.E.6
  • 156
    • 33644543761 scopus 로고    scopus 로고
    • Expanding insights of mitochondrial dysfunction in Parkinson's disease
    • Abou-Sleiman P.M., Muqit M.M., Wood N.W. Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nat Rev Neurosci. 2006, 7(3):207-219.
    • (2006) Nat Rev Neurosci. , vol.7 , Issue.3 , pp. 207-219
    • Abou-Sleiman, P.M.1    Muqit, M.M.2    Wood, N.W.3
  • 157
    • 0032924105 scopus 로고    scopus 로고
    • Chaperone-mediated protein folding
    • Fink A.L. Chaperone-mediated protein folding. Physiol Rev. 1999, 79(2):425-449.
    • (1999) Physiol Rev. , vol.79 , Issue.2 , pp. 425-449
    • Fink, A.L.1
  • 158
    • 85012430068 scopus 로고    scopus 로고
    • Heat shock proteins in health and disease: therapeutic targets or therapeutic agents?
    • Pockley A.G. Heat shock proteins in health and disease: therapeutic targets or therapeutic agents?. Expert Rev Mol Med. 2001, 3(23):1-21.
    • (2001) Expert Rev Mol Med. , vol.3 , Issue.23 , pp. 1-21
    • Pockley, A.G.1
  • 159
    • 79953791177 scopus 로고    scopus 로고
    • HSP70 chaperone machinery in sporadic-inclusion-body myositis muscle fibers
    • Ozturk A., McFerrin J., Engel W., Askanas V. HSP70 chaperone machinery in sporadic-inclusion-body myositis muscle fibers. Neurology. 2004, 62:A154.
    • (2004) Neurology. , vol.62
    • Ozturk, A.1    McFerrin, J.2    Engel, W.3    Askanas, V.4
  • 160
    • 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., Alvarez R.B., Sarkozi E., Engel W.K. Transfer of beta-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle. Proc Natl Acad Sci U S A 1996, 93(3):1314-1319.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , Issue.3 , pp. 1314-1319
    • Askanas, V.1    McFerrin, J.2    Baque, S.3    Alvarez, R.B.4    Sarkozi, E.5    Engel, W.K.6
  • 161
    • 0142200947 scopus 로고    scopus 로고
    • Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases
    • Hashimoto M., Rockenstein E., Crews L., Masliah E. Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases. Neuromolecular Med. 2003, 4(1-2):21-36.
    • (2003) Neuromolecular Med. , vol.4 , Issue.1-2 , pp. 21-36
    • Hashimoto, M.1    Rockenstein, E.2    Crews, L.3    Masliah, E.4
  • 162
    • 34347376745 scopus 로고    scopus 로고
    • Amyloid-beta-peptide reduces the expression level of mitochondrial cytochrome oxidase subunits
    • Hong W.K., Han E.H., Kim D.G., Ahn J.Y., Park J.S., Han B.G. Amyloid-beta-peptide reduces the expression level of mitochondrial cytochrome oxidase subunits. Neurochem Res. 2007, 32(9):1483-1488.
    • (2007) Neurochem Res. , vol.32 , Issue.9 , pp. 1483-1488
    • Hong, W.K.1    Han, E.H.2    Kim, D.G.3    Ahn, J.Y.4    Park, J.S.5    Han, B.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.