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Volumn 68, Issue 3, 2009, Pages 262-273

TAR DNA-binding protein 43 accumulation in protein aggregate myopathies

Author keywords

Desminopathy; Inclusion body myositis with Paget disease of bone and frontotemporal dementia; Myotilinopathy; Sporadic inclusion body myositis; TDP 43; Valosin

Indexed keywords

MICRORNA; TAR DNA BINDING PROTEIN; UBIQUITIN; VALOSIN CONTAINING PROTEIN; CYTOSKELETON PROTEIN; DNA BINDING PROTEIN; MUSCLE PROTEIN; MYOT PROTEIN, HUMAN; PEPTIDE; PROTEIN TDP-43; VALOSIN;

EID: 65349175153     PISSN: 00223069     EISSN: None     Source Type: Journal    
DOI: 10.1097/NEN.0b013e3181996d8f     Document Type: Article
Times cited : (91)

References (68)
  • 1
    • 0035139109 scopus 로고    scopus 로고
    • Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative disease
    • Sherman MY, Goldberg Al. Cellular defenses against unfolded proteins: A cell biologist thinks about neurodegenerative disease. Neuron 2001; 29:15-32
    • (2001) Neuron , vol.29 , pp. 15-32
    • Sherman, M.Y.1    Goldberg, Al.2
  • 2
    • 0037041441 scopus 로고    scopus 로고
    • Danger-misfolded proteins
    • Ellis RJ, Pinheiro TJT. Danger-misfolded proteins. Nature 2002;416: 483-484
    • (2002) Nature , vol.416 , pp. 483-484
    • Ellis, R.J.1    Pinheiro, T.J.T.2
  • 3
    • 0030841343 scopus 로고    scopus 로고
    • Conformational disease
    • Carrell RW, Lomas DA. Conformational disease. Lancet 1997;350: 134-138
    • (1997) Lancet , vol.350 , pp. 134-138
    • Carrell, R.W.1    Lomas, D.A.2
  • 4
    • 33344465659 scopus 로고    scopus 로고
    • Conformational diseases: An umbrella for various neurological disorders with an impaired ubiquitin-proteasome system
    • de Pril R, Fischer DF, van Leeuwen FW. Conformational diseases: An umbrella for various neurological disorders with an impaired ubiquitin-proteasome system. Neurobiol Aging 2006;27:515-523.
    • (2006) Neurobiol Aging , vol.27 , pp. 515-523
    • De Pril, R.1    Fischer, D.F.2    Van Leeuwen, F.W.3
  • 6
    • 46449104777 scopus 로고    scopus 로고
    • 156th ENMC International Workshop: Desmin and protein aggregate myopathies
    • 9-11 November 2007, Naarden, The Netherlands
    • Goebel HH, Fardeau M, Olive M, et al. 156th ENMC International Workshop: Desmin and protein aggregate myopathies, 9-11 November 2007, Naarden, The Netherlands. Neuromuscul Disord 2008;18: 583-592
    • (2008) Neuromuscul Disord , vol.18 , pp. 583-592
    • Goebel, H.H.1    Fardeau, M.2    Olive, M.3
  • 7
    • 0029875349 scopus 로고    scopus 로고
    • Myofibrillar myopathy with abnormal foci of desmin positivity. I. Light and electron microscopy analysis of 10 cases
    • Nakano S, Engel AG, Waclawik AJ, et al. Myofibrillar myopathy with abnormal foci of desmin positivity. I. Light and electron microscopy analysis of 10 cases. J Neuropathol Exp Neurol 1996; 55:549-562
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 549-562
    • Nakano, S.1    Engel, A.G.2    Waclawik, A.J.3
  • 8
    • 0029925575 scopus 로고    scopus 로고
    • Myofibrillar myopathy with foci of desmin positivity.II. Immunocytochemical analysis reveals accumulation of multiple other proteins
    • De Bleecker JL, Engel AG, Ertl B. Myofibrillar myopathy with foci of desmin positivity. II. Immunocytochemical analysis reveals accumulation of multiple other proteins. J Neuropathol Exp Neurol 1996;55: 563-577
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 563-577
    • De Bleecker, J.L.1    Engel, A.G.2    Ertl, B.3
  • 9
    • 0742305818 scopus 로고    scopus 로고
    • Myofibrillar myopathy: Clinical, morphological and genetic studies in 63 patients
    • Selcen D, Ohno K, Engel AG. Myofibrillar myopathy: Clinical, morphological and genetic studies in 63 patients. Brain 2004;127: 439-451
    • (2004) Brain , vol.127 , pp. 439-451
    • Selcen, D.1    Ohno, K.2    Engel, A.G.3
  • 10
    • 51349145767 scopus 로고    scopus 로고
    • Molecular pathology of myofibrillar myopathies.
    • Ferrer I, Olivé M. Molecular pathology of myofibrillar myopathies. Expert Rev Mol Med 2008;10:25
    • (2008) Expert Rev Mol Med , vol.10 , pp. 25
    • Ferrer, I.1    Olivé, M.2
  • 11
    • 1942473823 scopus 로고    scopus 로고
    • Mutations in myotilin cause myofibrillar myopathy
    • Selcen D, Engel AG. Mutations in myotilin cause myofibrillar myopathy. Neurology 2004;62:1363-1371
    • (2004) Neurology , vol.62 , pp. 1363-1371
    • Selcen, D.1    Engel, A.G.2
  • 12
    • 26044435388 scopus 로고    scopus 로고
    • Myotilinopathy: Refining the clinical and myopathological phenotype
    • Olive M, Goldfarb LG, Shatunov A, et al. Myotilinopathy: Refining the clinical and myopathological phenotype. Brain 2005;128:2315-2326
    • (2005) Brain , vol.128 , pp. 2315-2326
    • Olive, M.1    Goldfarb, L.G.2    Shatunov, A.3
  • 13
    • 17344373157 scopus 로고    scopus 로고
    • Missense mutations in desmin associated with familial cardiac and skeletal myopathy
    • Goldfarb LG, Park KY, Cervenakova L, et al. Missense mutations in desmin associated with familial cardiac and skeletal myopathy. Nat Genet 1998;19:402-403
    • (1998) Nat Genet , vol.19 , pp. 402-403
    • Goldfarb, L.G.1    Park, K.Y.2    Cervenakova, L.3
  • 14
    • 0038669889 scopus 로고    scopus 로고
    • A dysfunctional desmin mutation in a patient with severe generalised myopathy
    • Muñoz-Mármol AM, Strasser G, Isamat M, et al. A dysfunctional desmin mutation in a patient with severe generalised myopathy. Proc Natl Acad Sci U S A 1998;95:11312-11317
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 11312-11317
    • Muñoz-Mármol, A.M.1    Strasser, G.2    Isamat, M.3
  • 15
    • 35348870927 scopus 로고    scopus 로고
    • Abnormal up-regulation of neuron-restrictive silencer factor target genes in human myotilinopathy
    • Barrachina M, Moreno J, Juves S, et al. Abnormal up-regulation of neuron-restrictive silencer factor target genes in human myotilinopathy. Am J Pathol 2007;171:1312-1323
    • (2007) Am J Pathol , vol.171 , pp. 1312-1323
    • Barrachina, M.1    Moreno, J.2    Juves, S.3
  • 16
    • 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:S39-48.
    • (2006) Neurology , vol.66
    • Askanas, V.1    Engel, W.K.2
  • 17
    • 33746530058 scopus 로고    scopus 로고
    • Sporadic inclusion body myositis-diagnosis, pathogenesis and therapeutic strategies
    • Dalakas MC. Sporadic inclusion body myositis-diagnosis, pathogenesis and therapeutic strategies. Nat Clin Pract Neurol 2006;2:437-447
    • (2006) Nat Clin Pract Neurol , vol.2 , pp. 437-447
    • Dalakas, M.C.1
  • 18
    • 0029066110 scopus 로고
    • Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs
    • Ou SH, Wu F, Harrich D, et al. Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. J Virol 1995;69:3584-3596
    • (1995) J Virol , vol.69 , pp. 3584-3596
    • Ou, S.H.1    Wu, F.2    Harrich, D.3
  • 19
    • 0035965309 scopus 로고    scopus 로고
    • Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9
    • Buratti E, Baralle FE. Characterization and functional implications of the RNA binding properties of nuclear factor TDP-43, a novel splicing regulator of CFTR exon 9. J Biol Chem 2001;276:36337-36343
    • (2001) J Biol Chem , vol.276 , pp. 36337-36343
    • Buratti, E.1    Baralle, F.E.2
  • 20
    • 27844514227 scopus 로고    scopus 로고
    • TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing
    • Buratti E, Brindisi A, Giombi M, et al. TDP-43 binds heterogeneous nuclear ribonucleoprotein A/B through its C-terminal tail: An important region for the inhibition of cystic fibrosis transmembrane conductance regulator exon 9 splicing. J Biol Chem 2005;280:37572-37584
    • (2005) J Biol Chem , vol.280 , pp. 37572-37584
    • Buratti, E.1    Brindisi, A.2    Giombi, M.3
  • 21
    • 38449102667 scopus 로고    scopus 로고
    • Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease
    • Buratti E, Baralle FE. Multiple roles of TDP-43 in gene expression, splicing regulation, and human disease. Front Biosci 2008;13: 867-878
    • (2008) Front Biosci , vol.13 , pp. 867-878
    • Buratti, E.1    Baralle, F.E.2
  • 22
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Neumann M, Sampathu DM, Kwong LK, et al. Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 2006;314:130-133
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3
  • 23
    • 33750716074 scopus 로고    scopus 로고
    • TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Arai T, Hasegawa M, Akiyama H, et al. TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Biochem de Munain, Biophys Res Commun 2006;351:602-611
    • (2006) Biochem de Munain, Biophys Res Commun , vol.351 , pp. 602-611
    • Arai, T.1    Hasegawa, M.2    Akiyama, H.3
  • 24
    • 34249946466 scopus 로고    scopus 로고
    • Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations
    • Mackenzie IR, Bigio EH, Ince PG, et al. Pathological TDP-43 distinguishes sporadic amyotrophic lateral sclerosis from amyotrophic lateral sclerosis with SOD1 mutations. Ann Neurol 2007;61:427-434
    • (2007) Ann Neurol , vol.61 , pp. 427-434
    • MacKenzie, I.R.1    Bigio, E.H.2    Ince, P.G.3
  • 25
    • 35348853257 scopus 로고    scopus 로고
    • TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: Protein misfolding diseases without amyloidosis
    • Neumann M, Kwong LK, Sampathu DM, et al. TDP-43 proteinopathy in frontotemporal lobar degeneration and amyotrophic lateral sclerosis: Protein misfolding diseases without amyloidosis. Arch Neurol 2007;64: 1388-1394
    • (2007) Arch Neurol , vol.64 , pp. 1388-1394
    • Neumann, M.1    Kwong, L.K.2    Sampathu, D.M.3
  • 28
    • 1842483843 scopus 로고    scopus 로고
    • Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein
    • Watts GD, Wymer J, Kovach MJ, et al. Inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia is caused by mutant valosin-containing protein. Nat Genet 2004;36: 377-381
    • (2004) Nat Genet , vol.36 , pp. 377-381
    • Watts, G.D.1    Wymer, J.2    Kovach, M.J.3
  • 29
    • 35348909072 scopus 로고    scopus 로고
    • Novel VCP mutations in inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia
    • Watts GD, Thomasova D, Ramdeen SK, et al. Novel VCP mutations in inclusion body myopathy associated with Paget disease of bone and frontotemporal dementia. Clin Genet 2007;72:420-426
    • (2007) Clin Genet , vol.72 , pp. 420-426
    • Watts, G.D.1    Thomasova, D.2    Ramdeen, S.K.3
  • 30
    • 40449133507 scopus 로고    scopus 로고
    • Clinical studies in familial VCP myopathy associated with Paget disease of bone and frontotem-poral dementia
    • Kimonis VE, Mehta SG, Fulchiero EC, et al. Clinical studies in familial VCP myopathy associated with Paget disease of bone and frontotem-poral dementia. Am J Med Genet 2008;146A:745-757
    • (2008) Am J Med Genet , vol.146 A , pp. 745-757
    • Kimonis, V.E.1    Mehta, S.G.2    Fulchiero, E.C.3
  • 31
    • 33846570913 scopus 로고    scopus 로고
    • Pathological consequences of VCP mutations on human striated muscle
    • Hübbers CU, Clemen CS, Kesper K, et al. Pathological consequences of VCP mutations on human striated muscle. Brain 2007;130:381-393
    • (2007) Brain , vol.130 , pp. 381-393
    • Hübbers, C.U.1    Clemen, C.S.2    Kesper, K.3
  • 32
    • 33846815066 scopus 로고    scopus 로고
    • TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations
    • Neumann M, Mackenzie IR, Cairns NJ, et al. TDP-43 in the ubiquitin pathology of frontotemporal dementia with VCP gene mutations. J Neuropathol Exp Neurol 2007;66:152-157
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 152-157
    • Neumann, M.1    MacKenzie, I.R.2    Cairns, N.J.3
  • 33
    • 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 Psychiat 2008;79:1186-1189
    • (2008) J Neurol Neurosurg Psychiat , vol.79 , pp. 1186-1189
    • Weihl, C.C.1    Temiz, P.2    Miller, S.E.3
  • 34
    • 34249026071 scopus 로고    scopus 로고
    • Phenotypic patterns of desminopathy associated with three novel mutations in the desmin gene
    • Olivé M, Armstrong J, Miralles F, et al. Phenotypic patterns of desminopathy associated with three novel mutations in the desmin gene. Neuromusc Disord 2007;17:443-450
    • (2007) Neuromusc Disord , vol.17 , pp. 443-450
    • Olivé, M.1    Armstrong, J.2    Miralles, F.3
  • 35
    • 38149099865 scopus 로고    scopus 로고
    • Expression of mutant ubiquitin (UBB+1) and p62 in myotilinopathies and desminopathies
    • Olivé M, van Leeuwen FW, Janué A, et al. Expression of mutant ubiquitin (UBB+1) and p62 in myotilinopathies and desminopathies. Neuropathol Appl Neurobiol 2008;34:76-87
    • (2008) Neuropathol Appl Neurobiol , vol.34 , pp. 76-87
    • Olivé, M.1    Van Leeuwen, F.W.2    Janué, A.3
  • 36
    • 37349034999 scopus 로고    scopus 로고
    • Evidence that TDP-43 is not the major ubiquitinated target within the pathological inclusions of amyotrophic lateral sclerosis
    • Sanelli T, Xiao S, Horne P, et al. Evidence that TDP-43 is not the major ubiquitinated target within the pathological inclusions of amyotrophic lateral sclerosis. J Neuropathol Exp Neurol 2007;66:1147-1153
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 1147-1153
    • Sanelli, T.1    Xiao, S.2    Horne, P.3
  • 37
  • 38
    • 43049133705 scopus 로고    scopus 로고
    • Anterior horn cells with abnormal TDP-43 immunoreactivities show fragmentation of the Golgi apparatus in ALS
    • Fujita Y, Mizuno Y, Takamata M, Okamoto K. Anterior horn cells with abnormal TDP-43 immunoreactivities show fragmentation of the Golgi apparatus in ALS. J Neurol Sci 2008;269:30-34
    • (2008) J Neurol Sci , vol.269 , pp. 30-34
    • Fujita, Y.1    Mizuno, Y.2    Takamata, M.3    Okamoto, K.4
  • 39
    • 47949096734 scopus 로고    scopus 로고
    • Sporadic amyotrophic lateral sclerosis: Two pathological patterns shown by analysis of distribution of TDP-43-immunoreactive neuronal and glial cytoplasmic inclusions
    • Nishihara Y, Tan CF, Onodera O, et al. Sporadic amyotrophic lateral sclerosis: Two pathological patterns shown by analysis of distribution of TDP-43-immunoreactive neuronal and glial cytoplasmic inclusions. Acta Neuropathol 2008;116;169-182
    • (2008) Acta Neuropathol , vol.116 , pp. 169-182
    • Nishihara, Y.1    Tan, C.F.2    Onodera, O.3
  • 40
    • 41149180753 scopus 로고    scopus 로고
    • TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis
    • Sreedharan J, Blair IP, Tripathi VB, et al. TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis. Science 2008;319:1668-1672
    • (2008) Science , vol.319 , pp. 1668-1672
    • Sreedharan, J.1    Blair, I.P.2    Tripathi, V.B.3
  • 41
    • 42649120983 scopus 로고    scopus 로고
    • TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis
    • Kabashi E, Valdmanis PN, Dion P, et al. TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis. Nat Genet 2008;40:572-574
    • (2008) Nat Genet , vol.40 , pp. 572-574
    • Kabashi, E.1    Valdmanis, P.N.2    Dion, P.3
  • 42
    • 41949119043 scopus 로고    scopus 로고
    • TDP-43 A315T mutation in familial motor neuron disease
    • Gitcho MA, Baloh RH, Chakraverty S, et al. TDP-43 A315T mutation in familial motor neuron disease. Ann Neurol 2008;63:435-438
    • (2008) Ann Neurol , vol.63 , pp. 435-438
    • Gitcho, M.A.1    Baloh, R.H.2    Chakraverty, S.3
  • 43
    • 37349039461 scopus 로고    scopus 로고
    • TDP-43 proteinopathies: Neurodegenerative protein misfolding diseases without amyloidosis
    • Kwong LK, Uryu K, Trojanowski JQ, et al. TDP-43 proteinopathies: Neurodegenerative protein misfolding diseases without amyloidosis. Neurosignals 2008;16:41-51
    • (2008) Neurosignals , vol.16 , pp. 41-51
    • Kwong, L.K.1    Uryu, K.2    Trojanowski, J.Q.3
  • 44
    • 44649137415 scopus 로고    scopus 로고
    • Concomitant TARYDNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies
    • Uryu K, Nakashima-Yasuda H, Forman MS, et al. Concomitant TARYDNA-binding protein 43 pathology is present in Alzheimer disease and corticobasal degeneration but not in other tauopathies. J Neuropathol Exp Neurol 2008;67:555-564
    • (2008) J Neuropathol Exp Neurol , vol.67 , pp. 555-564
    • Uryu, K.1    Nakashima-Yasuda, H.2    Forman, M.S.3
  • 45
    • 70349154791 scopus 로고    scopus 로고
    • Pathological TDP-43 in parkinsonism-dementia complex and amyotrophic lateral sclerosis of Guam
    • Geser F, Wintion MJ, Kwong LK, et al. Pathological TDP-43 in parkinsonism-dementia complex and amyotrophic lateral sclerosis of Guam. Acta Neuropathol 2008;67:33-45
    • (2008) Acta Neuropathol , vol.67 , pp. 33-45
    • Geser, F.1    Wintion, M.J.2    Kwong, L.K.3
  • 46
    • 36348972414 scopus 로고    scopus 로고
    • Concurrence of TDP-43, tau and synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies
    • Higashi S, Iseki E, Yamamoto R, et al. Concurrence of TDP-43, tau and synuclein pathology in brains of Alzheimer's disease and dementia with Lewy bodies. Brain Res 2007;1184:284-294
    • (2007) Brain Res , vol.1184 , pp. 284-294
    • Higashi, S.1    Iseki, E.2    Yamamoto, R.3
  • 48
    • 39749083266 scopus 로고    scopus 로고
    • TDP-43 immunoreactivity in anoxic, ischemic and neoplastic lesions of the central nervous system
    • Lee EB, Lee VM, Trojanowski JQ, et al. TDP-43 immunoreactivity in anoxic, ischemic and neoplastic lesions of the central nervous system. Acta Neuropathol. 2008;115:305-311
    • (2008) Acta Neuropathol. , vol.115 , pp. 305-311
    • Lee, E.B.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 49
    • 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, Mártýn 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 Neuropath Exp Neurol 2004;63:484-498
    • (2004) J Neuropath Exp Neurol , vol.63 , pp. 484-498
    • Ferrer, I.1    Mártýn, B.2    Castaño, J.G.3
  • 50
    • 17444418324 scopus 로고    scopus 로고
    • Involvement of clusterin and the aggresome in abnormal protein deposits in myofibrillar myopathies and inclusion body myositis
    • Ferrer I, Carmona M, Blanco R, et al. Involvement of clusterin and the aggresome in abnormal protein deposits in myofibrillar myopathies and inclusion body myositis. Brain Pathol 2005;15:101-108
    • (2005) Brain Pathol , vol.15 , pp. 101-108
    • Ferrer, I.1    Carmona, M.2    Blanco, R.3
  • 51
    • 34548321645 scopus 로고    scopus 로고
    • Desmin is oxidized and nitrated in affected muscles in myotilinopathies and desminopathies
    • Janué A, Odena MA, Oliveira E, et al. Desmin is oxidized and nitrated in affected muscles in myotilinopathies and desminopathies. J Neuropath Exp Neurol 2007;66:711-723
    • (2007) J Neuropath Exp Neurol , vol.66 , pp. 711-723
    • Janué, A.1    Odena, M.A.2    Oliveira, E.3
  • 52
    • 35148847303 scopus 로고    scopus 로고
    • Oxidative stress in desminopathies and myotilinopathies: A link between oxidative damage and abnormal protein aggregation
    • Janue A, Olivé M, Ferrer I. Oxidative stress in desminopathies and myotilinopathies: A link between oxidative damage and abnormal protein aggregation. Brain Pathol 2007;17:377-388
    • (2007) Brain Pathol , vol.17 , pp. 377-388
    • Janue, A.1    Olivé, M.2    Ferrer, I.3
  • 53
    • 44749091997 scopus 로고    scopus 로고
    • Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation
    • Winton MJ, Igaz LM, Wong MM, et al. Disturbance of nuclear and cytoplasmic TAR DNA-binding protein (TDP-43) induces disease-like redistribution, sequestration, and aggregate formation. J Biol Chem 2008;283:13302-13309
    • (2008) J Biol Chem , vol.283 , pp. 13302-13309
    • Winton, M.J.1    Igaz, L.M.2    Wong, M.M.3
  • 54
    • 47949086625 scopus 로고    scopus 로고
    • Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • Hasegawa M, Arai T, Nonaka T, et al. Phosphorylated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Ann Neurol 2008;64:60-70
    • (2008) Ann Neurol , vol.64 , pp. 60-70
    • Hasegawa, M.1    Arai, T.2    Nonaka, T.3
  • 55
    • 48749088629 scopus 로고    scopus 로고
    • Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS
    • Inukai Y, Nonaka T, Yoshida M, et al. Abnormal phosphorylation of Ser409/410 of TDP-43 in FTLD-U and ALS. FEBS Lett 2008;582: 2899-2904
    • (2008) FEBS Lett , vol.582 , pp. 2899-2904
    • Inukai, Y.1    Nonaka, T.2    Yoshida, M.3
  • 57
    • 0038374249 scopus 로고    scopus 로고
    • Selective loss of rans-acting instability determinants of neurofilament mRNA in amyotrophic lateral sclerosis spinal cord
    • Ge WW, Leystra-Lantz C, Wen W, Strong MJ. Selective loss of rans-acting instability determinants of neurofilament mRNA in amyotrophic lateral sclerosis spinal cord. J Biol Chem 2003;278: 26558-26563
    • (2003) J Biol Chem , vol.278 , pp. 26558-26563
    • Ge, W.W.1    Leystra-Lantz, C.2    Wen, W.3    Strong, M.J.4
  • 58
    • 9144225636 scopus 로고    scopus 로고
    • The Microprocessor complex mediates the genesis of microRNAs
    • Gregory RI, Yan KP, Amuthan G, et al. The Microprocessor complex mediates the genesis of microRNAs. Nature 2004;432:235-240
    • (2004) Nature , vol.432 , pp. 235-240
    • Gregory, R.I.1    Yan, K.P.2    Amuthan, G.3
  • 59
    • 33845242919 scopus 로고    scopus 로고
    • MicroRNAs: Regulators of gene expression and cell differentiation
    • Shivdasani RA. MicroRNAs: Regulators of gene expression and cell differentiation. Blood 2006;108:3636-3653
    • (2006) Blood , vol.108 , pp. 3636-3653
    • Shivdasani, R.A.1
  • 60
    • 34249874344 scopus 로고    scopus 로고
    • RNA in brain disease: No longer just Bthe messenger in the middle
    • Nelson PT, Keller JN. RNA in brain disease: No longer just Bthe messenger in the middle. J Neuropathol Exp Neurol 2007;66:461-468
    • (2007) J Neuropathol Exp Neurol , vol.66 , pp. 461-468
    • Nelson, P.T.1    Keller, J.N.2
  • 61
    • 52449116560 scopus 로고    scopus 로고
    • MicroRNAs: Novel regulators in cardiac development and disease
    • Thum T, Cataluci D, Bauersachs J. MicroRNAs: Novel regulators in cardiac development and disease. Cardiovasc Res 2008;79: 562-570
    • (2008) Cardiovasc Res , vol.79 , pp. 562-570
    • Thum, T.1    Cataluci, D.2    Bauersachs, J.3
  • 62
    • 33846153786 scopus 로고    scopus 로고
    • MicroRNA-1 and microRNA-133a expression are decreased during skeletal muscle hypertrophy
    • McCarthy JJ, Esser KA. MicroRNA-1 and microRNA-133a expression are decreased during skeletal muscle hypertrophy. J Appl Physiol 2007; 102:306-313
    • (2007) J Appl Physiol , vol.102 , pp. 306-313
    • McCarthy, J.J.1    Esser, K.A.2
  • 63
    • 34147153781 scopus 로고    scopus 로고
    • Dysregulation of cardiogenesis, cardiac conduction, and cell cycle in mice lacking miRNA-1-2
    • Zhao Y, Ransom JF, Li A, et al. Dysregulation of cardiogenesis, cardiac conduction, and cell cycle in mice lacking miRNA-1-2. Cell 2007;129: 303-317
    • (2007) Cell , vol.129 , pp. 303-317
    • Zhao, Y.1    Ransom, J.F.2    Li, A.3
  • 67
    • 55249117284 scopus 로고    scopus 로고
    • MicroRNA-206: The skeletal muscle-specific myomir
    • McCarthy JJ. MicroRNA-206: The skeletal muscle-specific myomir. Biochem Biophys Acta 2008;1779:682-691
    • (2008) Biochem Biophys Acta , vol.1779 , pp. 682-691
    • McCarthy, J.J.1
  • 68
    • 51449101459 scopus 로고    scopus 로고
    • Specific requirements of MRFs for the expression of muscle specific microRNAs, mir-1, miur-206 and miR-133
    • Sweetman D, Goljanek K, Rathjen T, et al. Specific requirements of MRFs for the expression of muscle specific microRNAs, mir-1, miur-206 and miR-133. Dev Biol 2008;321:491-499
    • (2008) Dev Biol , vol.321 , pp. 491-499
    • Sweetman, D.1    Goljanek, K.2    Rathjen, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.