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Volumn 642, Issue , 2008, Pages 131-164

Intermediate filament diseases: Desminopathy

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; DESMIN;

EID: 60549106181     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-0-387-84847-1_11     Document Type: Article
Times cited : (109)

References (119)
  • 1
    • 0028016523 scopus 로고
    • Immunohistologic and electron microscopic abnormalities of desmin and dystrophin in familial cardiomyopathy and myopathy
    • Goebel HH, Voit T, Warlo I et al. Immunohistologic and electron microscopic abnormalities of desmin and dystrophin in familial cardiomyopathy and myopathy. Rev Neurol (Paris) 1994; 150:452-459. (Pubitemid 24254848)
    • (1994) Revue Neurologique , vol.150 , Issue.6-7 , pp. 452-459
    • Goebel, H.H.1    Voit, T.2    Warlo, I.3    Jacobs, K.4    Johannsen, U.5    Muller, C.R.6
  • 2
    • 0742305818 scopus 로고    scopus 로고
    • Myofibrillar myopathy: Clinical, morphological and genetic studies in 63 patients
    • DOI 10.1093/brain/awh052
    • Selcen D, Ohno K, Engel AG. Myofibrillar myopathy: Clinical, morphological and genetic studies in 63 patients Brain 2004; 127:439-451. (Pubitemid 38160328)
    • (2004) Brain , vol.127 , Issue.2 , pp. 439-451
    • Selcen, D.1    Ohno, K.2    Engel, A.G.3
  • 3
    • 0033746702 scopus 로고    scopus 로고
    • Desmin splice variants causing cardiac and skeletal myopathy
    • Park KY, Dalakas MC, Goebel HH et al. Desmin splice variants causing cardiac and skeletal myopathy. J Med Genet 2000; 37:851-857.
    • (2000) J. Med. Genet. , vol.37 , pp. 851-857
    • Park, K.Y.1    Dalakas, M.C.2    Goebel, H.H.3
  • 5
    • 5144228375 scopus 로고    scopus 로고
    • The biology of desmin filaments: How do mutations affect their structure, assembly, and organisation?
    • DOI 10.1016/j.jsb.2004.04.003, PII S1047847704000978
    • Bar H, Strelkov SV, Sjoberg G et al. The biology of desmin filaments: How do mutations affect their structure, assembly and organization. J Struct Biol 2004; 148:137-152. (Pubitemid 39346004)
    • (2004) Journal of Structural Biology , vol.148 , Issue.2 , pp. 137-152
    • Bar, H.1    Strelkov, S.V.2    Sjoberg, G.3    Aebi, U.4    Herrmann, H.5
  • 6
    • 3042778127 scopus 로고    scopus 로고
    • A missense mutation in the desmin rod domain is associated with autosomal dominant distal myopathy, and exerts a dominant negative effect on filament formation
    • DOI 10.1093/hmg/8.12.2191
    • Sjoberg G, Saavedra-Matiz CA, Rosen DR et al. Missense mutation in the desmin rod domain is associated with autosomal dominant distal myopathy and exerts a dominant negative effect on filament formation. Hum Mol Genet 1999; 8:2191-2198. (Pubitemid 29525333)
    • (1999) Human Molecular Genetics , vol.8 , Issue.12 , pp. 2191-2198
    • Sjoberg, G.1    Saavedra-Matiz, C.A.2    Rosen, D.R.3    Wijsman, E.M.4    Borg, K.5    Horowitz, S.H.6    Sejersen, T.7
  • 15
    • 84883771822 scopus 로고    scopus 로고
    • Myofibrillar myopathy
    • Selcen D, Engel AG. Myofibrillar myopathy. GeneReviews (http://www.genereviews.org/) 2006.
    • (2006) GeneReviews
    • Selcen, D.1    Engel, A.G.2
  • 16
    • 0028283501 scopus 로고
    • Intermediate filaments: Structure dynamics function and disease
    • Fuchs E, Weber K. Intermediate filaments: Structure, dynamics, function and disease. Annu Rev Biochem 1994; 63:345-382.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 345-382
    • Fuchs, E.1    Weber, K.2
  • 17
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate Filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • DOI 10.1146/annurev.biochem.73.011303.073823
    • Herrmann H, Aebi U. Intermediate filaments: Molecular structure, assembly mechanism and integration into functionally distinct intracellular scaffolds. Annu Rev Biochem 2004; 73:749-789. (Pubitemid 39050385)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 18
    • 0018842868 scopus 로고
    • Intermediate filaments as mechanical integrators of cellular space
    • DOI 10.1038/283249a0
    • Lazarides E. Intermediate filaments as mechanical integrators of cellular space. Nature 1980; 238:249-256. (Pubitemid 10177899)
    • (1980) Nature , vol.283 , Issue.5744 , pp. 249-256
    • Lazarides, E.1
  • 20
    • 0021323422 scopus 로고
    • Molecular analysis of intermediate filament cytoskeleton-putative load-bearing structure
    • Price MG. Molecular analysis of intermediate filament cytoskeleton-Putative load-bearing structure. Am J Physiol 1984; 246:566-572.
    • (1984) Am. J. Physiol. , vol.246 , pp. 566-572
    • Price, M.G.1
  • 22
    • 0030966537 scopus 로고    scopus 로고
    • Desmin in muscle formation and maintenance: Knockouts and consequences
    • Capetanaki Y, Milner DJ, Weitzer G. Desmin in muscle formation and maintenance: Knockouts and consequences. Cell Struct Funct 1997; 22:103-116. (Pubitemid 27223251)
    • (1997) Cell Structure and Function , vol.22 , Issue.1 , pp. 103-116
    • Capetanaki, Y.1    Milner, D.J.2    Weitzer, G.3
  • 23
    • 0029738727 scopus 로고    scopus 로고
    • Disruption of muscle architecture and myocardial degeneration in mice lacking desmin
    • Milner DJ, Weitzer G, Tran D et al. Disruption of muscle architecture and myocardial degeneration in mice lacking desmin. J Cell Biol 1996; 134:1255-1270. (Pubitemid 26300170)
    • (1996) Journal of Cell Biology , vol.134 , Issue.5 , pp. 1255-1270
    • Milner, D.J.1    Weitzer, G.2    Tran, D.3    Bradley, A.4    Capetanaki, Y.5
  • 24
    • 0036517816 scopus 로고    scopus 로고
    • Ischemia-induced association of the stress protein αB-crystallin with I-band portion of cardiac titin
    • DOI 10.1006/jmcc.2001.1513
    • Golenhofen N, Arbeiter A, Koob R et al. Ischemia-induced association of the stress protein alpha B-crystallin with I-band portion of cardiac titin. J Mol Cell Cardiol 2002; 34:309-319. (Pubitemid 37162423)
    • (2002) Journal of Molecular and Cellular Cardiology , vol.34 , Issue.3 , pp. 309-319
    • Golenhofen, N.1    Arbeiter, A.2    Koob, R.3    Drenckhahn, D.4
  • 27
    • 0024379475 scopus 로고
    • Assignment of human desmin gene to band 2q35 by nonradioactive in situ hybridization
    • Viegas-Péquignot E, Li Z, Dutrillaux B et al. Assignment of human desmin gene to band 2q35 by nonradioactive in situ hybridization. Hum Genet 1989; 83:33-36. (Pubitemid 19206038)
    • (1989) Human Genetics , vol.83 , Issue.1 , pp. 33-36
    • Viegas-Pequignot, E.1    Li, Z.-L.2    Dutrillaux, B.3    Apiou, F.4    Paulin, D.5
  • 28
    • 0024401230 scopus 로고
    • Human desmin-coding gene: Complete nucleotide sequence, characterization and regulation of expression during myogenesis and development
    • DOI 10.1016/0378-1119(89)90227-8
    • Li Z, Lilienbaum A, Butler-Browne G et al. Human desmin-coding gene: Complete nucleotide sequence, characterization and regulation of expression during myogenesis and development. Gene 1989: 78:243-254 (Pubitemid 19154203)
    • (1989) Gene , vol.78 , Issue.2 , pp. 243-254
    • Li, Z.1    Lilienbaum, A.2    Butler-Browne, G.3    Paulin, D.4
  • 29
  • 30
    • 0029957901 scopus 로고    scopus 로고
    • Heptad breaks in α-helical coiled coils: Stutters and stammers
    • DOI 10.1002/(SICI)1097-0134(199610)26:2<134::AID-PROT3>3.0.CO;2-G
    • Brown JH, Cohen C, Parry DAD. Heptad breaks in α̃helical coiled coils: Stutters and stammers. Proteins 1996; 26:134-145. (Pubitemid 26365307)
    • (1996) Proteins: Structure, Function and Genetics , vol.26 , Issue.2 , pp. 134-145
    • Brown, J.H.1    Cohen, C.2    Parry, D.A.D.3
  • 31
    • 0037086445 scopus 로고    scopus 로고
    • Conserved segments 1A and 2B of the intermediate filament dimer: Their atomic structures and role in filament assembly
    • DOI 10.1093/emboj/21.6.1255
    • Strelkov SV, Herrmann H, Geisler N et al. Conserved segments 1A and 2B of the intermediate filamentdimer: their atomic structures and role in filament assembly. EMBO J 2002; 21:1255-1266. (Pubitemid 34246505)
    • (2002) EMBO Journal , vol.21 , Issue.6 , pp. 1255-1266
    • Strelkov, S.V.1    Herrmann, H.2    Geisler, N.3    Wedig, T.4    Zimbelmann, R.5    Aebi, U.6    Burkhard, P.7
  • 32
    • 0036445512 scopus 로고    scopus 로고
    • Analysis of α-helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation
    • DOI 10.1006/jsbi.2002.4454
    • Strelkov SV, Burkhard P. Analysis of α̃helical coiled coils with the program TWISTER reveals a structural mechanism for stutter compensation. J Struct Biol 2002; 137:54-64. (Pubitemid 35430421)
    • (2002) Journal of Structural Biology , vol.137 , Issue.1-2 , pp. 54-64
    • Strelkov, S.V.1    Burkhard, P.2
  • 33
    • 0034685607 scopus 로고    scopus 로고
    • The intermediate filament protein consensus motif of helix 2B: Its atomic structure and contribution to assembly
    • Herrmann H, Strelkov SV, Feja B et al. The intermediate filament protein consensus motif of helix 2B: Its atomic structure and contribution to assembly. J Mol Biol 2000; 298:817-832.
    • (2000) J. Mol. Biol. , vol.298 , pp. 817-832
    • Herrmann, H.1    Strelkov, S.V.2    Feja, B.3
  • 35
    • 0030019825 scopus 로고    scopus 로고
    • Specific recognition of coiled coils by infrared spectroscopy: Analysis of the three structural domains of type III intermediate filament proteins
    • DOI 10.1021/bi9515883
    • Heimburg T, Schuenemann J, Weber K et al. Specific recognition of coiled coils by infrared spectroscopy: Analysis of the three structural domains of type III intermediate filament proteins. Biochemistry 1996; 35:1375-1382. (Pubitemid 26055273)
    • (1996) Biochemistry , vol.35 , Issue.5 , pp. 1375-1382
    • Heimburg, T.1    Schuenemann, J.2    Weber, K.3    Geisler, N.4
  • 36
    • 0028984981 scopus 로고
    • Truncation mutagenesis of the non-alpha-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly
    • Rogers KR, Eckelt A, Nimmrich V et al. Truncation mutagenesis of the non-alpha-helical carboxyterminal tail domain of vimentin reveals contributions to cellular localization but not to filament assembly. Eur J Cell Biol 1995; 66:136-150.
    • (1995) Eur. J. Cell Biol. , vol.66 , pp. 136-150
    • Rogers, K.R.1    Eckelt, A.2    Nimmrich, V.3
  • 39
    • 33747159811 scopus 로고    scopus 로고
    • Familial restrictive cardiomyopathy caused by a missense mutation in the desmin gene
    • abstract #1304
    • Bowles NE, Jimenez S, Vatta M et al. Familial restrictive cardiomyopathy caused by a missense mutation in the desmin gene. Pediatric Res 2002; 51:Suppl, p 2, abstract #1304. ]
    • (2002) Pediatric. Res. , vol.51 , pp. 2
    • Bowles, N.E.1    Jimenez, S.2    Vatta, M.3
  • 41
    • 83455166417 scopus 로고    scopus 로고
    • Genotype-morphotype correlations in myofibrillar myopathies
    • Bushby et al. Genotype-morphotype correlations in myofibrillar myopathies. In preparation.
    • Preparation
    • Bushby1
  • 43
    • 18344374698 scopus 로고    scopus 로고
    • The enlarging spectrum of desminopathies: New morphological findings, eastward geographic spread, novel exon 3 desmin mutation
    • DOI 10.1007/s00401-005-0980-1
    • Vrabie A, Goldfarb LG, Shatunov A et al. Th e enlarging s spectrum of desminopathies: New morphological findings, eastward geographic spread, novel exon 3 desmin mutation. Acta Neuropathol (Berl) 2005; 109:411-417. (Pubitemid 40637315)
    • (2005) Acta Neuropathologica , vol.109 , Issue.4 , pp. 411-417
    • Vrabie, A.1    Goldfarb, L.G.2    Shatunov, A.3    Nagele, A.4    Fritz, P.5    Kaczmarek, I.6    Goebel, H.H.7
  • 44
    • 83455253589 scopus 로고    scopus 로고
    • Desmin splice variants causing cardiac and skeletal myopathy
    • Suppl, Abstract.
    • Shatunov A, Dalakas MC, Park K-Y et al. Desmin splice variants causing cardiac and skeletal myopathy. Amer J Hum Genet 2003; 73:Suppl, Abstract.
    • (2003) Amer. J. Hum. Genet. , vol.73
    • Shatunov, A.1    Dalakas, M.C.2    Park, K.-Y.3
  • 52
    • 0034633685 scopus 로고    scopus 로고
    • A novel de novo mutation in the desmin gene causes desmin myopathy with toxic aggregates
    • Sugawara M, Kato K, Komatsu M et al. A novel de novo mutation in the desmin gene causes desmin myopathy with toxic aggregates. Neurology 2000; 55:986-990.
    • (2000) Neurology , vol.55 , pp. 986-990
    • Sugawara, M.1    Kato, K.2    Komatsu, M.3
  • 55
    • 33947517125 scopus 로고    scopus 로고
    • Restrictive cardiomyopathy with atrioventricular conduction block resulting from a desmin mutation
    • Pruszczyk P, Kostera-Pruszczyk A, Shatunov A et al. Restrictive cardiomyopathy with atrioventricular conduction block resulting from a desmin mutation. Int J Cardiol 2006; 117:244-253.
    • (2006) Int. J. Cardiol. , vol.117 , pp. 244-253
    • Pruszczyk, P.1    Kostera-Pruszczyk, A.2    Shatunov, A.3
  • 60
    • 33646232231 scopus 로고    scopus 로고
    • Disease severity in dominant emery dreifuss is increased by mutations in both emerin and desmin proteins
    • Muntoni F, Bonne G, Goldfarb LG et al. Disease severity in dominant Emery Dreifuss is increased by mutations in both emerin and desmin proteins. Brain 2006; 129:1260-1268.
    • (2006) Brain , vol.129 , pp. 1260-1268
    • Muntoni, F.1    Bonne, G.2    Goldfarb, L.G.3
  • 62
    • 18744397819 scopus 로고    scopus 로고
    • Molecular dissection of the interaction of desmin with the C-terminal region of nebulin
    • DOI 10.1006/jsbi.2002.4457
    • Bang ML, Gregorio C, Labeit S. Molecular dissection of the interaction of desmin with the C-terminal region of nebulin. J Struct Biol 2002; 137:119-127. (Pubitemid 35430427)
    • (2002) Journal of Structural Biology , vol.137 , Issue.1-2 , pp. 119-127
    • Bang, M.-L.1    Gregorio, C.2    Labeit, S.3
  • 63
    • 0025890946 scopus 로고
    • Influence of proline residues on protein conformation
    • MacArthur MW, Thornton JM. Influence of proline residues on protein conformation. J Mol Biol 1991; 218:397-412. (Pubitemid 121003355)
    • (1991) Journal of Molecular Biology , vol.218 , Issue.2 , pp. 397-412
    • MacArthur, M.W.1    Thornton, J.M.2
  • 64
    • 0026012625 scopus 로고
    • Assembly of carboxy-terminally deleted desmin in vimentin- free cells
    • Raats JMH, Henderik JBJ, Verdijk M et al. Assembly of carboxy-terminally deleted desmin in vimentin- free cells. Eur J Cell Biol 1991; 56:84-103.
    • (1991) Eur. J. Cell Biol. , vol.56 , pp. 84-103
    • Raats, J.M.H.1    Henderik, J.B.J.2    Verdijk, M.3
  • 66
    • 0024989296 scopus 로고
    • Human αB-Crystallin gene and preferential promoter function in lens
    • DOI 10.1016/0888-7543(90)90204-8
    • Dubin RA, Ally AH, Chung S et al. Human alpha-B-crystallin gene and preferential promoter function in lens. Genomics 1990; 7:594-601. (Pubitemid 20244464)
    • (1990) Genomics , vol.7 , Issue.4 , pp. 594-601
    • Dubin, R.A.1    Ally, A.H.2    Chung, S.3    Piatigorsky, J.4
  • 67
    • 0034486034 scopus 로고    scopus 로고
    • The function of alpha-crystallin in vision
    • DOI 10.1006/scdb.1999.0351
    • Horwitz J. The function of alpha-crystallin in vision. Semin Cell Dev Biol 2000; 11:53-60. (Pubitemid 32098002)
    • (2000) Seminars in Cell and Developmental Biology , vol.11 , Issue.1 , pp. 53-60
    • Horwitz, J.1
  • 68
    • 0033104818 scopus 로고    scopus 로고
    • Binding of the stress protein αB-crystallin to cardiac myofibrils correlates with the degree of myocardial damage during ischemia/reperfusion in vivo
    • DOI 10.1006/jmcc.1998.0892
    • Golenhofen N, Htun P, Ness W et al. Binding of the stress protein alpha B-crystallin to cardiac myofibrils correlates with the degree of myocardial damage during ischemia/reperfusion in vivo. J Mol Cell Cardiol 1999; 31:569-580. (Pubitemid 29121643)
    • (1999) Journal of Molecular and Cellular Cardiology , vol.31 , Issue.3 , pp. 569-580
    • Golenhofen, N.1    Htun, P.2    Ness, W.3    Koob, R.4    Schaper, W.5    Drenckhahn, D.6
  • 69
    • 0031469110 scopus 로고    scopus 로고
    • Small heat shock proteins and protection against ischemic injury in cardiac myocytes
    • Martin JL, Mestril R, Hilal-Dandan R et al. Small heat shock proteins and protection against ischemic injury in cardiac myocytes. Circulation 1997; 96:4343-4348. (Pubitemid 28007464)
    • (1997) Circulation , vol.96 , Issue.12 , pp. 4343-4348
    • Martin, J.L.1    Mestril, R.2    Hilal-Dandan, R.3    Brunton, L.L.4    Dillmann, W.H.5
  • 70
    • 0034294838 scopus 로고    scopus 로고
    • Five novel genetic variants in the promoter and coding region of the alphaB-crystallin gene CRYAB: -652G>A -650C>G, -249G> C S41Y P51L
    • Hahner A, Erdmann J, Kallisch H et al. Five novel genetic variants in the promoter and coding region of the alphaB-crystallin gene (CRYAB): -652G>A, -650C>G, -249G>C, S41Y, P51L. Hum Mutat 2000; 16:374-377.
    • (2000) Hum. Mutat. , vol.16 , pp. 374-377
    • Hahner, A.1    Erdmann, J.2    Kallisch, H.3
  • 71
    • 0018068469 scopus 로고
    • UNE NOUVELLE AFFECTION MUSCULAIRE FAMILIALE, DEFINIE PAR L'ACCUMULATION INTRA-SARCO-PLASMIQUE D'UN MATERIEL GRANULO-FILAMENTAIRE DENSE EN MICROSCOPIE ELECTRONIQUE
    • Fardeau M, Godet-Guillain J, Tome FM et al. Une nouvelle affection musculaire familiale, definie par laccumulation intra-sarco-plasmique dun materiel granulo-filamentaire dense en microscopie electronique. Rev Neurol 1978 ; 134:411-425. (Pubitemid 9010013)
    • (1978) Revue Neurologique , vol.134 , Issue.6-7 , pp. 411-425
    • Fardeau, M.1    Godet Guillain, J.2    Tome, F.M.S.3
  • 73
    • 0038104369 scopus 로고    scopus 로고
    • Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G αB-crystallin mutant
    • DOI 10.1093/hmg/ddg173
    • Chavez Zobel AT, Loranger A, Marceau N et al. Distinct chaperone mechanisms can delay the formation of aggresomes by the myopathy-causing R120G alpha-B-crystallin mutant. Hum Molec Genet 2003; 12:1609-1620. (Pubitemid 36857307)
    • (2003) Human Molecular Genetics , vol.12 , Issue.13 , pp. 1609-1620
    • Zobel, A.T.C.1    Loranger, A.2    Marceau, N.3    Theriault, J.R.4    Lambert, H.5    Landry, J.6
  • 74
    • 0037336078 scopus 로고    scopus 로고
    • Alteration of protein-protein interactions of congenital cataract crystallin mutants
    • DOI 10.1167/iovs.02-0950
    • Fu L, Liang JJ-N. Alteration of protein-protein interactions of congenital cataract crystallin mutants. Invest Ophthal Vis Sci 2003; 44:1155-1159. (Pubitemid 36297835)
    • (2003) Investigative Ophthalmology and Visual Science , vol.44 , Issue.3 , pp. 1155-1159
    • Fu, L.1    Liang, J.J.-N.2
  • 75
    • 0344664368 scopus 로고    scopus 로고
    • Myofibrillar Myopathy Caused by Novel Dominant Negative αB-Crystallin Mutations
    • DOI 10.1002/ana.10767
    • Selcen D, Engel AG. Myofibrillar myopathy caused by novel dominant negative alpha-B-crystallin mutations. Ann Neurol 2003; 54:804-810. (Pubitemid 37498963)
    • (2003) Annals of Neurology , vol.54 , Issue.6 , pp. 804-810
    • Selcen, D.1    Engel, A.G.2
  • 79
    • 33646144211 scopus 로고    scopus 로고
    • Forced expression of desmin and desmin mutants in cultured cells: Impact of myopathic missense mutations in the central coiled-coil domain on network formation
    • Bar H, Kostareva A, Sjoberg G et al. Forced expression of desmin and desmin mutants in cultured cells: Impact of myopathic missense mutations in the central coiled-coil domain on network formation. Exp Cell Res 2006; 312:1554-1565.
    • (2006) Exp. Cell Res. , vol.312 , pp. 1554-1565
    • Bar, H.1    Kostareva, A.2    Sjoberg, G.3
  • 80
    • 3943078618 scopus 로고    scopus 로고
    • Intermediate Filaments: Molecular structure, assembly mechanism, and integration into functionally distinct intracellular scaffolds
    • DOI 10.1146/annurev.biochem.73.011303.073823
    • Herrmann H, Aebi U. Intermediate filaments: Molecular structure, assembly mechanism and integration into functionally distinct intracellular scaffolds. Annu Rev Biochem 2004; 73:749-789. (Pubitemid 39050385)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 749-789
    • Herrmann, H.1    Aebi, U.2
  • 82
    • 0035318422 scopus 로고    scopus 로고
    • Abnormal desmin protein in myofibrillar myopathies caused by desmin gene mutations desmin protein in myofibrillar myopathies
    • Li M, Dalakas MC. Abnormal desmin protein in myofibrillar myopathies caused by desmin gene mutations. Desmin protein in myofibrillar myopathies. Ann Neurol 2001; 49:532-536.
    • (2001) Ann. Neurol. , vol.49 , pp. 532-536
    • Li, M.1    Dalakas, M.C.2
  • 86
    • 0000834504 scopus 로고    scopus 로고
    • Analysis of skeletal and cardiac muscle from desmin knock-out and normal mice by high resolution separation of myosin heavy-chain isoforms
    • Agbulut O, Li Z, Mouly V et al. Analysis of skeletal and cardiac muscle from desmin knock-out and normal mice by high resolution separation of myosin heavy-chain isoforms. Biol Cell 1996; 88:131-135. (Pubitemid 126820243)
    • (1996) Biology of the Cell , vol.88 , Issue.3 , pp. 131-135
    • Agbulut, O.1    Li, Z.2    Mouly, V.3    Butler-Browne, G.S.4
  • 88
    • 0028224508 scopus 로고
    • Truncated desmin in PtK2 cells induces desmin-vimentin-cytokeratin coprecipitation involution of intermediate filament networks and nuclear fragmentation: A model for many degenerative diseases
    • USA
    • Yu KR, Hijikata T, Lin ZX et al. Truncated desmin in PtK2 cells induces desmin-vimentin-cytokeratin coprecipitation, involution of intermediate filament networks and nuclear fragmentation: A model for many degenerative diseases. Proc Natl Acad Sci USA 1994; 91:2497-2501.
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 2497-2501
    • Yu, K.R.1    Hijikata, T.2    Lin, Z.X.3
  • 89
    • 0000843475 scopus 로고    scopus 로고
    • The cardiomyopathy and lens cataract mutation in αB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro
    • Perng MD, Muchowski PJ, van den Ijssel P et al. The cardiomyopathy and lens cataract mutation in alpha B-crystallin alters its protein structure, chaperone activity and interaction with intermediate filaments in vitro. J Biol Chem 1999, 274:33235-33243. (Pubitemid 129511621)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.47 , pp. 33235-33243
    • Der Perng, M.1    Muchowski, P.J.2    Van Den Ijssel, P.3    Wu, G.J.S.4    Hutcheson, A.M.5    Clark, J.I.6    Quinlan, R.A.7
  • 90
    • 0036951869 scopus 로고    scopus 로고
    • Desmin filaments and cardiac disease: Establishing causality
    • DOI 10.1054/jcaf.2002.129279
    • Wang X, Osinska H, Gerdes AM et al. Desmin filaments and cardiac disease: Establishing causality. J Cardiac Failure 2002; 8:S287-S292. (Pubitemid 36083073)
    • (2002) Journal of Cardiac Failure , vol.8 , Issue.6 SUPPL.
    • Wang, X.1    Osinska, H.2    Gerdes, A.M.3    Robbins, J.4
  • 94
    • 0032768982 scopus 로고    scopus 로고
    • Desmin phosphorylation abnormalities in cytoplasmic body and desmin- related myopathies
    • DOI 10.1002/(SICI)1097-4598(199908)22:8<1122::AID-MUS17>3.0.CO;2-T
    • Caron A, Chapon F. Desmin phosphorylation abnormalities in cytoplasmic body and desmin-related myopathies. Muscle Nerve 1999; 22:1122-1125. (Pubitemid 29360259)
    • (1999) Muscle and Nerve , vol.22 , Issue.8 , pp. 1122-1125
    • Caron, A.1    Chapon, F.2
  • 95
    • 0023918541 scopus 로고
    • Storage of phosphorylated desmin in a familial myopathy
    • Rappaport L, Contard F, Samuel JL et al. Storage of phosphorylated desmin in a familial myopathy. FEBS Lett 1988; 231:421-415.
    • (1988) FEBS Lett. , vol.231 , pp. 421-415
    • Rappaport, L.1    Contard, F.2    Samuel, J.L.3
  • 98
    • 0034995762 scopus 로고    scopus 로고
    • Desmin integrates the three-dimensional mechanical properties of muscles
    • Boriek AM, Capetanaki Y, Hwang W et al. Desmin integrates the three-dimensional mechanical properties of muscles. Am J Physiol Cell Physiol 2001; 280:C46-C52.
    • (2001) Am. J. Physiol. Cell Physiol , vol.280
    • Boriek, A.M.1    Capetanaki, Y.2    Hwang, W.3
  • 99
    • 0037050022 scopus 로고    scopus 로고
    • The failing heart
    • DOI 10.1038/415227a
    • Towbin JA, Bowles NE. The failing heart. Nature 2002; 415:227-233. (Pubitemid 34059529)
    • (2002) Nature , vol.415 , Issue.6868 , pp. 227-233
    • Towbin, J.A.1    Bowles, N.E.2
  • 100
    • 0042857127 scopus 로고    scopus 로고
    • Cardiomyopathy: Molecular and immunological aspects review
    • Takeda N. Cardiomyopathy: Molecular and immunological aspects (review). Int J Mol Med 2003; 11:13-16.
    • (2003) Int. J. Mol. Med. , vol.11 , pp. 13-16
    • Takeda, N.1
  • 101
    • 0028120746 scopus 로고
    • Autosomal dominant distal myopathy with desmin storage: A clinicopathologic and electrophysiologic study of a large kinship
    • Horowitz SH, Schmalbruch H. Autosomal dominant distal myopathy with desmin storage: a clinicopathologic and electrophysiologic study of a large kinship. Muscle Nerve 1994; 17:151-160. (Pubitemid 24040219)
    • (1994) Muscle and Nerve , vol.17 , Issue.2 , pp. 151-160
    • Horowitz, S.H.1    Schmalbruch, H.2
  • 102
    • 0029133882 scopus 로고
    • Desmin myopathy: A multisystem disorder involving skeletal cardiac and smooth muscle
    • Ariza A, Coll J, Fernandez-Figueras MT et al. Desmin myopathy: A multisystem disorder involving skeletal, cardiac and smooth muscle. Hum Pathol 1995; 26:1032-1037.
    • (1995) Hum. Pathol. , vol.26 , pp. 1032-1037
    • Ariza, A.1    Coll, J.2    Fernandez-Figueras, M.T.3
  • 104
    • 0028857926 scopus 로고
    • Desmin-related neuromuscular disorders
    • Goebel HH. Desmin-related neuromuscular disorders. Muscle Nerve 1995; 18:1306-1320.
    • (1995) Muscle. Nerve. , vol.18 , pp. 1306-1320
    • Goebel, H.H.1
  • 105
    • 0026744205 scopus 로고
    • Vimentin and desmin in maturing skeletal muscle and developmental myopathies
    • Sarnat HB. Vimentin and desmin in maturing skeletal muscle and developmental myopathies. Neurology 1992; 42:1616-1624.
    • (1992) Neurology , vol.42 , pp. 1616-1624
    • Sarnat, H.B.1
  • 106
    • 0018969921 scopus 로고
    • The distribution of intermediate filament protein (skeletin) in normal and diseased human skeletal muscle. An immunohistochemical and electron-microscopic study
    • DOI 10.1016/0022-510X(80)90001-5
    • Thornell LE, Edstrom L, Eriksson A et al. The distribution of intermediate filament protein (skeletin) in normal and diseased human skeletal muscle-An immunohistochemical and electron-microscopic study. J Neurol Sci 1980; 47:153-170. (Pubitemid 10046294)
    • (1980) Journal of the Neurological Sciences , vol.47 , Issue.2 , pp. 153-170
    • Thornell, L.E.1    Edstrom, L.2    Eriksson, A.3
  • 107
    • 0025337552 scopus 로고
    • Immunocytochemical localization of desmin at human neuromuscular junctions
    • Askanas V, Bornemann A, Engel WK. Immunocytochemical localization of desmin at human neuromuscular junction. Neurology 1990; 40:949-953. (Pubitemid 20201822)
    • (1990) Neurology , vol.40 , Issue.6 , pp. 949-953
    • Askanas, V.1    Bornemann, A.2    Engel, W.K.3
  • 108
    • 0026742189 scopus 로고
    • Desmin at myotendinous junctions
    • Tidball JC. Desmin at myotendinous junctions. Exp Cell Res 1992; 199:341-348.
    • (1992) Exp. Cell Res. , vol.199 , pp. 341-348
    • Tidball, J.C.1
  • 110
    • 0032729924 scopus 로고    scopus 로고
    • Myofibrillar myopathy
    • DOI 10.1002/1531-8249(199911)46:5<681::AID-ANA1>3.0.CO;2-B
    • Engel AG. Myofibrillar myopathy. Ann Neurol 1999; 46:681-683. (Pubitemid 29518127)
    • (1999) Annals of Neurology , vol.46 , Issue.5 , pp. 681-683
    • Engel, A.G.1
  • 111
    • 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. (Pubitemid 38526050)
    • (2004) Neurology , vol.62 , Issue.8 , pp. 1363-1371
    • Selcen, D.1    Engel, A.G.2
  • 112
    • 26044435388 scopus 로고    scopus 로고
    • Myotilinopathy: Refining the clinical and myopathological phenotype
    • DOI 10.1093/brain/awh576
    • OlivürM, Goldfarb LG, Shatunov A et al. Myotilinopathy: Refining the clinical and myopathological phenotype. Brain 2005; 128: 2315-2326. (Pubitemid 41407972)
    • (2005) Brain , vol.128 , Issue.10 , pp. 2315-2326
    • Olive, M.1    Goldfarb, L.G.2    Shatunov, A.3    Fischer, D.4    Ferrer, I.5
  • 115
    • 13144260646 scopus 로고    scopus 로고
    • Mutations in ZASP define a novel form of muscular dystrophy in humans
    • DOI 10.1002/ana.20376
    • Selcen D, Engel AG. Mutations in ZASP define a novel form of muscular dystrophy in humans. Ann Neurol 2005; 57:269-276. (Pubitemid 40179865)
    • (2005) Annals of Neurology , vol.57 , Issue.2 , pp. 269-276
    • Selcen, D.1    Engel, A.G.2


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