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Volumn 201, Issue 4, 2013, Pages 499-510

Cellular and molecular mechanisms underlying muscular dystrophy

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA DYSTROGLYCAN; CAVEOLIN 3; DYSFERLIN; DYSTROGLYCAN; DYSTROPHIN; DYSTROPHIN ASSOCIATED PROTEIN COMPLEX; LIPOCORTIN 1; LIPOCORTIN 2; MESSENGER RNA; MYOTONIC DYSTROPHY PROTEIN KINASE; PROTEIN BAX; PROTEIN BCL 2;

EID: 84878544086     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201212142     Document Type: Article
Times cited : (189)

References (118)
  • 2
    • 32244440192 scopus 로고    scopus 로고
    • Dystroglycan: from biosynthesis to pathogenesis of human disease
    • Barresi, R., and K.P. Campbell. 2006. Dystroglycan: from biosynthesis to pathogenesis of human disease. J. Cell Sci., 119:199-207. http://dx.doi.org/10.1242/jcs.02814
    • (2006) J. Cell Sci. , vol.119 , pp. 199-207
    • Barresi, R.1    Campbell, K.P.2
  • 3
    • 17344363640 scopus 로고    scopus 로고
    • A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B
    • Bashir, R., S. Britton, T. Strachan, S. Keers, E. Vafiadaki, M. Lako, I. Richard, S. Marchand, N. Bourg, Z. Argov, et al. 1998. A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B. Nat. Genet., 20:37-42. http://dx.doi.org/10.1038/1689
    • (1998) Nat. Genet. , vol.20 , pp. 37-42
    • Bashir, R.1    Britton, S.2    Strachan, T.3    Keers, S.4    Vafiadaki, E.5    Lako, M.6    Richard, I.7    Marchand, S.8    Bourg, N.9    Argov, Z.10
  • 4
    • 0035943673 scopus 로고    scopus 로고
    • Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres
    • Bellin, R.M., T.W. Huiatt, D.R. Critchley, and R.M. Robson. 2001. Synemin may function to directly link muscle cell intermediate filaments to both myofibrillar Z-lines and costameres. J. Biol. Chem., 276:32330-32337. http://dx.doi.org/10.1074/jbc.M104005200
    • (2001) J. Biol. Chem. , vol.276 , pp. 32330-32337
    • Bellin, R.M.1    Huiatt, T.W.2    Critchley, D.R.3    Robson, R.M.4
  • 6
    • 0027985787 scopus 로고
    • Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy
    • Bione, S., E. Maestrini, S. Rivella, M. Mancini, S. Regis, G. Romeo, and D. Toniolo. 1994. Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy. Nat. Genet., 8:323-327. http://dx.doi.org/10.1038/ng1294-323
    • (1994) Nat. Genet. , vol.8 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, S.3    Mancini, M.4    Regis, S.5    Romeo, G.6    Toniolo, D.7
  • 7
    • 76249096210 scopus 로고    scopus 로고
    • Recessive mutations in the putative calcium-activated chloride channel Anoctamin 5 cause proximal LGMD2L and distal MMD3 muscular dystrophies
    • Bolduc, V., G. Marlow, K.M. Boycott, K. Saleki, H. Inoue, J. Kroon, M. Itakura, Y. Robitaille, L. Parent, F. Baas, et al. 2010. Recessive mutations in the putative calcium-activated chloride channel Anoctamin 5 cause proximal LGMD2L and distal MMD3 muscular dystrophies. Am. J. Hum. Genet., 86:213-221. http://dx.doi.org/10.1016/j.ajhg.2009.12.013
    • (2010) Am. J. Hum. Genet. , vol.86 , pp. 213-221
    • Bolduc, V.1    Marlow, G.2    Boycott, K.M.3    Saleki, K.4    Inoue, H.5    Kroon, J.6    Itakura, M.7    Robitaille, Y.8    Parent, L.9    Baas, F.10
  • 9
    • 79960101359 scopus 로고    scopus 로고
    • The collagen VI-related myopathies: muscle meets its matrix
    • Bönnemann, C.G. 2011. The collagen VI-related myopathies: muscle meets its matrix. Nat. Rev. Neurol., 7:379-390. http://dx.doi.org/10.1038/nrneurol.2011.81
    • (2011) Nat. Rev. Neurol. , vol.7 , pp. 379-390
    • Bönnemann, C.G.1
  • 11
    • 0029149471 scopus 로고
    • Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy
    • Brenman, J.E., D.S. Chao, H. Xia, K. Aldape, and D.S. Bredt. 1995. Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell., 82:743-752. http://dx.doi.org/10.1016/0092-8674(95)90471-9
    • (1995) Cell. , vol.82 , pp. 743-752
    • Brenman, J.E.1    Chao, D.S.2    Xia, H.3    Aldape, K.4    Bredt, D.S.5
  • 12
    • 0035212037 scopus 로고    scopus 로고
    • Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan
    • Brockington, M., D.J. Blake, P. Prandini, S.C. Brown, S. Torelli, M.A. Benson, C.P. Ponting, B. Estournet, N.B. Romero, E. Mercuri, et al. 2001. Mutations in the fukutin-related protein gene (FKRP) cause a form of congenital muscular dystrophy with secondary laminin alpha2 deficiency and abnormal glycosylation of alpha-dystroglycan. Am. J. Hum. Genet., 69: 1198-1209. http://dx.doi.org/10.1086/324412
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 1198-1209
    • Brockington, M.1    Blake, D.J.2    Prandini, P.3    Brown, S.C.4    Torelli, S.5    Benson, M.A.6    Ponting, C.P.7    Estournet, B.8    Romero, N.B.9    Mercuri, E.10
  • 13
    • 0026566108 scopus 로고
    • Molecular basis of myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3 end of a transcript encoding a protein kinase family member
    • Brook, J.D., M.E. McCurrach, H.G. Harley, A.J. Buckler, D. Church, H. Aburatani, K. Hunter, V.P. Stanton, J.P. Thirion, T. Hudson, et al. 1992. Molecular basis of myotonic dystrophy: expansion of a trinucleotide (CTG) repeat at the 3 end of a transcript encoding a protein kinase family member. Cell., 68:799-808. http://dx.doi.org/10.1016/0092-8674(92)90154-5
    • (1992) Cell. , vol.68 , pp. 799-808
    • Brook, J.D.1    McCurrach, M.E.2    Harley, H.G.3    Buckler, A.J.4    Church, D.5    Aburatani, H.6    Hunter, K.7    Stanton, V.P.8    Thirion, J.P.9    Hudson, T.10
  • 14
    • 0023274891 scopus 로고
    • A cDNA clone from the Duchenne/Becker muscular dystrophy gene
    • Burghes, A.H., C. Logan, X. Hu, B. Belfall, R.G. Worton, and P.N. Ray. 1987. A cDNA clone from the Duchenne/Becker muscular dystrophy gene. Nature., 328:434-437. http://dx.doi.org/10.1038/328434a0
    • (1987) Nature. , vol.328 , pp. 434-437
    • Burghes, A.H.1    Logan, C.2    Hu, C.3    Belfall, B.4    Worton, R.G.5    Ray, P.N.6
  • 15
    • 0035911960 scopus 로고    scopus 로고
    • Enhanced expression of the α7β1 integrin reduces muscular dystrophy and restores viability in dystrophic mice
    • Burkin, D.J., G.Q. Wallace, K.J. Nicol, D.J. Kaufman, and S.J. Kaufman. 2001. Enhanced expression of the α7β1 integrin reduces muscular dystrophy and restores viability in dystrophic mice. J. Cell Biol., 152:1207-1218. http://dx.doi.org/10.1083/jcb.152.6.1207
    • (2001) J. Cell Biol. , vol.152 , pp. 1207-1218
    • Burkin, D.J.1    Wallace, G.Q.2    Nicol, K.J.3    Kaufman, D.J.4    Kaufman, S.J.5
  • 18
    • 67650133653 scopus 로고    scopus 로고
    • Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin
    • Cai, C., N. Weisleder, J.K. Ko, S. Komazaki, Y. Sunada, M. Nishi, H. Takeshima, and J. Ma. 2009b. Membrane repair defects in muscular dystrophy are linked to altered interaction between MG53, caveolin-3, and dysferlin. J.Biol.Chem., 284:15894-15902. http://dx.doi.org/10.1074/jbc.M109.009589
    • (2009) J.Biol.Chem. , vol.284 , pp. 15894-15902
    • Cai, C.1    Weisleder, N.2    Ko, J.K.3    Komazaki, S.4    Sunada, Y.5    Nishi, M.6    Takeshima, H.7    Ma, J.8
  • 19
    • 0036347927 scopus 로고    scopus 로고
    • Loss of the muscle-specific chloride channel in type 1 myotonic dystrophy due to misregulated alternative splicing
    • Charlet-B, N., R.S. Savkur, G. Singh, A.V. Philips, E.A. Grice, and T.A. Cooper. 2002. Loss of the muscle-specific chloride channel in type 1 myotonic dystrophy due to misregulated alternative splicing. Mol. Cell., 10:45-53. http://dx.doi.org/10.1016/S1097-2765(02)00572-5
    • (2002) Mol. Cell. , vol.10 , pp. 45-53
    • Charlet-B, N.1    Savkur, R.S.2    Singh, G.3    Philips, A.V.4    Grice, E.A.5    Cooper, T.A.6
  • 20
    • 22744438723 scopus 로고    scopus 로고
    • Stem cell function, self-renewal, and behavioral heterogeneity of cells from the adult muscle satellite cell niche
    • Collins, C.A., I. Olsen, P.S. Zammit, L. Heslop, A. Petrie, T.A. Partridge, and J.E. Morgan. 2005. Stem cell function, self-renewal, and behavioral heterogeneity of cells from the adult muscle satellite cell niche. Cell., 122:289-301. http://dx.doi.org/10.1016/j.cell.2005.05.010
    • (2005) Cell , vol.122 , pp. 289-301
    • Collins, C.A.1    Olsen, I.2    Zammit, P.S.3    Heslop, L.4    Petrie, A.5    Partridge, T.A.6    Morgan, J.E.7
  • 21
    • 0030841672 scopus 로고    scopus 로고
    • Expansion of a CUG trinucleotide repeat in the 3 untranslated region of myotonic dystrophy protein kinase transcripts results in nuclear retention of transcripts
    • USA
    • Davis, B.M., M.E. McCurrach, K.L. Taneja, R.H. Singer, and D.E. Housman. 1997. Expansion of a CUG trinucleotide repeat in the 3 untranslated region of myotonic dystrophy protein kinase transcripts results in nuclear retention of transcripts. Proc. Natl. Acad. Sci. USA., 94:7388-7393. http://dx.doi.org/10.1073/pnas.94.14.7388
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 7388-7393
    • Davis, B.M.1    McCurrach, M.E.2    Taneja, K.L.3    Singer, R.H.4    Housman, D.E.5
  • 24
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti, J.M., and K.P. Campbell. 1993. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol., 122:809-823. http://dx.doi.org/10.1083/jcb.122.4.809
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 25
    • 0025272250 scopus 로고
    • Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
    • Ervasti, J.M., K. Ohlendieck, S.D. Kahl, M.G. Gaver, and K.P. Campbell. 1990. Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle. Nature., 345:315-319. http://dx.doi.org/10.1038/345315a0
    • (1990) Nature. , vol.345 , pp. 315-319
    • Ervasti, J.M.1    Ohlendieck, K.2    Kahl, S.D.3    Gaver, M.G.4    Campbell, K.P.5
  • 26
    • 0036179479 scopus 로고    scopus 로고
    • Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene
    • Frosk, P., T. Weiler, E. Nylen, T. Sudha, C.R. Greenberg, K. Morgan, T.M. Fujiwara, and K. Wrogemann. 2002. Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene. Am. J. Hum. Genet., 70:663-672. http://dx.doi.org/10.1086/339083
    • (2002) Am. J. Hum. Genet. , vol.70 , pp. 663-672
    • Frosk, P.1    Weiler, T.2    Nylen, E.3    Sudha, T.4    Greenberg, C.R.5    Morgan, K.6    Fujiwara, T.M.7    Wrogemann, K.8
  • 29
    • 85047693919 scopus 로고    scopus 로고
    • Inhibition of apoptosis improves outcome in a model of congenital muscular dystrophy
    • Girgenrath, M., J.A. Dominov, C.A. Kostek, and J.B. Miller. 2004. Inhibition of apoptosis improves outcome in a model of congenital muscular dystrophy. J. Clin. Invest., 114:1635-1639.
    • (2004) J. Clin. Invest. , vol.114 , pp. 1635-1639
    • Girgenrath, M.1    Dominov, J.A.2    Kostek, C.A.3    Miller, J.B.4
  • 30
    • 0033175570 scopus 로고    scopus 로고
    • Role for alpha-dystrobrevin in the pathogenesis of dystrophin-dependent muscular dystrophies
    • Grady, R.M., R.W. Grange, K.S. Lau, M.M. Maimone, M.C. Nichol, J.T. Stull, and J.R. Sanes. 1999. Role for alpha-dystrobrevin in the pathogenesis of dystrophin-dependent muscular dystrophies. Nat. Cell Biol., 1:215- 220. http://dx.doi.org/10.1038/12034
    • (1999) Nat. Cell Biol. , vol.1 , pp. 215-220
    • Grady, R.M.1    Grange, R.W.2    Lau, K.S.3    Maimone, M.M.4    Nichol, M.C.5    Stull, J.T.6    Sanes, J.R.7
  • 31
    • 84856147995 scopus 로고    scopus 로고
    • Etiology of limb girdle muscular dystrophy 1D/1E determined by laser capture microdissection proteomics
    • Greenberg, S.A., M. Salajegheh, D.P. Judge, M.W. Feldman, R.W. Kuncl, Z. Waldon, H. Steen, and K.R. Wagner. 2012. Etiology of limb girdle muscular dystrophy 1D/1E determined by laser capture microdissection proteomics. Ann. Neurol., 71:141-145. http://dx.doi.org/10.1002/ana.22649
    • (2012) Ann. Neurol. , vol.71 , pp. 141-145
    • Greenberg, S.A.1    Salajegheh, M.2    Judge, D.P.3    Feldman, M.W.4    Kuncl, R.W.5    Waldon, Z.6    Steen, H.7    Wagner, K.R.8
  • 33
    • 78649796969 scopus 로고    scopus 로고
    • Mutation in exon 1f of PLEC, leading to disruption of plectin isoform 1f, causes autosomal-recessive limbgirdle muscular dystrophy
    • Gundesli, H., B. Talim, P. Korkusuz, B. Balci-Hayta, S. Cirak, N.A. Akarsu, H. Topaloglu, and P. Dincer. 2010. Mutation in exon 1f of PLEC, leading to disruption of plectin isoform 1f, causes autosomal-recessive limbgirdle muscular dystrophy. Am. J. Hum. Genet., 87:834-841. http://dx.doi.org/10.1016/j.ajhg.2010.10.017
    • (2010) Am. J. Hum. Genet. , vol.87 , pp. 834-841
    • Gundesli, H.1    Talim, B.2    Korkusuz, P.3    Balci-Hayta, B.4    Cirak, S.5    Akarsu, N.A.6    Topaloglu, H.7    Dincer, P.8
  • 36
    • 80052565758 scopus 로고    scopus 로고
    • The cell biology of disease: cellular mechanisms of cardiomyopathy
    • Harvey, P.A., and L.A. Leinwand. 2011. The cell biology of disease: cellular mechanisms of cardiomyopathy. J. Cell Biol., 194:355-365. http://dx.doi.org/10.1083/jcb.201101100
    • (2011) J. Cell Biol. , vol.194 , pp. 355-365
    • Harvey, P.A.1    Leinwand, L.A.2
  • 41
    • 0023614188 scopus 로고
    • Dystrophin: the protein product of the Duchenne muscular dystrophy locus
    • Hoffman, E.P., R.H. Brown Jr., and L.M. Kunkel. 1987. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell., 51:919-928. http://dx.doi.org/10.1016/0092-8674(87)90579-4
    • (1987) Cell. , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown, R.H.2    Kunkel, L.M.3
  • 43
    • 0026543686 scopus 로고
    • Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix
    • Ibraghimov-Beskrovnaya, O., J.M. Ervasti, C.J. Leveille, C.A. Slaughter, S.W. Sernett, and K.P. Campbell. 1992. Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature., 355: 696-702. http://dx.doi.org/10.1038/355696a0
    • (1992) Nature. , vol.355 , pp. 696-702
    • Ibraghimov-Beskrovnaya, O.1    Ervasti, J.M.2    Leveille, C.J.3    Slaughter, C.A.4    Sernett, S.W.5    Campbell, K.P.6
  • 44
    • 84867068988 scopus 로고    scopus 로고
    • Facioscapulohumeral muscular dystrophy family studies of DUX4 expression: evidence for disease modifiers and a quantitative model of pathogenesis
    • Jones, T.I., J.C. Chen, F. Rahimov, S. Homma, P. Arashiro, M.L. Beermann, O.D. King, J.B. Miller, L.M. Kunkel, C.P. Emerson Jr., et al. 2012. Facioscapulohumeral muscular dystrophy family studies of DUX4 expression: evidence for disease modifiers and a quantitative model of pathogenesis. Hum. Mol. Genet., 21:4419-4430. http://dx.doi.org/10.1093/hmg/dds284
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 4419-4430
    • Jones, T.I.1    Chen, J.C.2    Rahimov, F.3    Homma, S.4    Arashiro, P.5    Beermann, M.L.6    King, O.D.7    Miller, J.B.8    Kunkel, L.M.9    Emerson, C.P.10
  • 46
    • 84877726997 scopus 로고    scopus 로고
    • The 2013 version of the gene table of monogenic neuromuscular disorders (nuclear genome)
    • Kaplan, J.-C., and D. Hamroun. 2012. The 2013 version of the gene table of monogenic neuromuscular disorders (nuclear genome). Neuromuscul. Disord., 22:1108-1135. http://dx.doi.org/10.1016/j.nmd.2012.10.021
    • (2012) Neuromuscul. Disord. , vol.22 , pp. 1108-1135
    • Kaplan, J.-C.1    Hamroun, D.2
  • 50
    • 0028046502 scopus 로고
    • Nitric oxide in skeletal muscle
    • Kobzik, L., M.B. Reid, D.S. Bredt, and J.S. Stamler. 1994. Nitric oxide in skeletal muscle. Nature., 372:546-548. http://dx.doi.org/10.1038/372546a0
    • (1994) Nature. , vol.372 , pp. 546-548
    • Kobzik, L.1    Reid, M.B.2    Bredt, D.S.3    Stamler, J.S.4
  • 51
    • 0023614271 scopus 로고
    • Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals
    • Koenig, M., E.P. Hoffman, C.J. Bertelson, A.P. Monaco, C. Feener, and L.M. Kunkel. 1987. Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals. Cell., 50:509-517. http://dx.doi.org/10.1016/0092-8674(87)90504-6
    • (1987) Cell. , vol.50 , pp. 509-517
    • Koenig, M.1    Hoffman, E.P.2    Bertelson, C.J.3    Monaco, A.P.4    Feener, C.5    Kunkel, L.M.6
  • 54
    • 34948834723 scopus 로고    scopus 로고
    • Increased steady-state levels of CUGBP1 in myotonic dystrophy 1 are due to PKCmediated hyperphosphorylation
    • Kuyumcu-Martinez, N.M., G.S. Wang, and T.A. Cooper. 2007. Increased steady-state levels of CUGBP1 in myotonic dystrophy 1 are due to PKCmediated hyperphosphorylation. Mol. Cell., 28:68-78. http://dx.doi.org/10.1016/j.molcel.2007.07.027
    • (2007) Mol. Cell. , vol.28 , pp. 68-78
    • Kuyumcu-Martinez, N.M.1    Wang, G.S.2    Cooper, T.A.3
  • 55
    • 65649111197 scopus 로고    scopus 로고
    • Dystrophins carrying spectrin-like repeats 16 and 17 anchor nNOS to the sarcolemma and enhance exercise performance in a mouse model of muscular dystrophy
    • Lai, Y., G.D. Thomas, Y. Yue, H.T. Yang, D. Li, C. Long, L. Judge, B. Bostick, J.S. Chamberlain, R.L. Terjung, and D. Duan. 2009. Dystrophins carrying spectrin-like repeats 16 and 17 anchor nNOS to the sarcolemma and enhance exercise performance in a mouse model of muscular dystrophy. J. Clin. Invest., 119:624-635. http://dx.doi.org/10.1172/JCI36612
    • (2009) J. Clin. Invest. , vol.119 , pp. 624-635
    • Lai, Y.1    Thomas, G.D.2    Yue, Y.3    Yang, H.T.4    Li, D.5    Long, C.6    Judge, L.7    Bostick, B.8    Chamberlain, J.S.9    Terjung, R.L.10    Duan, D.11
  • 56
    • 84872175513 scopus 로고    scopus 로고
    • 2 and 3 helices of dystrophin R16 and R17 frame a microdomain in the 1 helix of dystrophin R17 for neuronal NOS binding
    • Lai, Y., J. Zhao, Y. Yue, and D. Duan. 2013. 2 and 3 helices of dystrophin R16 and R17 frame a microdomain in the 1 helix of dystrophin R17 for neuronal NOS binding. Proc. Natl. Acad. Sci. USA., 110:525-530. http://dx.doi.org/10.1073/pnas.1211431109
    • (2013) Proc. Natl. Acad. Sci. USA. , vol.110 , pp. 525-530
    • Lai, Y.1    Zhao, J.2    Yue, Y.3    Duan, D.4
  • 57
    • 0036788610 scopus 로고    scopus 로고
    • Facioscapulohumeral muscular dystrophy is uniquely associated with one of the two variants of the 4q subtelomere
    • Lemmers, R.J., P. de Kievit, L. Sandkuijl, G.W. Padberg, G.J. van Ommen, R.R. Frants, and S.M. van der Maarel. 2002. Facioscapulohumeral muscular dystrophy is uniquely associated with one of the two variants of the 4q subtelomere. Nat. Genet., 32:235-236. http://dx.doi.org/10.1038/ng999
    • (2002) Nat. Genet. , vol.32 , pp. 235-236
    • Lemmers, R.J.1    de Kievit, P.2    Sandkuijl, L.3    Padberg, G.W.4    van Ommen, G.J.5    Frants, R.R.6    van der Maarel, S.M.7
  • 60
    • 0347379869 scopus 로고    scopus 로고
    • Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing
    • Lennon, N.J., A. Kho, B.J. Bacskai, S.L. Perlmutter, B.T. Hyman, and R.H. Brown Jr. 2003. Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing. J. Biol. Chem., 278:50466-50473. http://dx.doi.org/10.1074/jbc.M307247200
    • (2003) J. Biol. Chem. , vol.278 , pp. 50466-50473
    • Lennon, N.J.1    Kho, A.2    Bacskai, B.J.3    Perlmutter, S.L.4    Hyman, B.T.5    Brown, R.H.6
  • 65
    • 84863257178 scopus 로고    scopus 로고
    • 1D chain increases 71 integrin and laminin and protects against sarcolemmal damage in mdx mice
    • Liu, J., D.J. Milner, M.D. Boppart, R.S. Ross, and S.J. Kaufman. 2012. 1D chain increases 71 integrin and laminin and protects against sarcolemmal damage in mdx mice. Hum. Mol. Genet., 21:1592-1603. http://dx.doi.org/10.1093/hmg/ddr596
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 1592-1603
    • Liu, J.1    Milner, D.J.2    Boppart, M.D.3    Ross, R.S.4    Kaufman, S.J.5
  • 66
    • 10744226857 scopus 로고    scopus 로고
    • Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan
    • Longman, C., M. Brockington, S. Torelli, C. Jimenez-Mallebrera, C. Kennedy, N. Khalil, L. Feng, R.K. Saran, T. Voit, L. Merlini, et al. 2003. Mutations in the human LARGE gene cause MDC1D, a novel form of congenital muscular dystrophy with severe mental retardation and abnormal glycosylation of alpha-dystroglycan. Hum. Mol. Genet., 12:2853-2861. http://dx.doi.org/10.1093/hmg/ddg307
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2853-2861
    • Longman, C.1    Brockington, M.2    Torelli, S.3    Jimenez-Mallebrera, C.4    Kennedy, C.5    Khalil, N.6    Feng, L.7    Saran, R.K.8    Voit, T.9    Merlini, L.10
  • 70
    • 0345526827 scopus 로고    scopus 로고
    • Ribonuclear inclusions in skeletal muscle in myotonic dystrophy types 1 and 2
    • Mankodi, A., P. Teng-Umnuay, M. Krym, D. Henderson, M. Swanson, and C.A. Thornton. 2003. Ribonuclear inclusions in skeletal muscle in myotonic dystrophy types 1 and 2. Ann. Neurol., 54:760-768. http://dx.doi.org/10.1002/ana.10763
    • (2003) Ann. Neurol. , vol.54 , pp. 760-768
    • Mankodi, A.1    Teng-Umnuay, P.2    Krym, M.3    Henderson, D.4    Swanson, M.5    Thornton, C.A.6
  • 73
    • 0000642664 scopus 로고
    • Satellite cell of skeletal muscle fibers
    • Mauro, A. 1961. Satellite cell of skeletal muscle fibers. J. Biophys. Biochem. Cytol., 9:493-495. http://dx.doi.org/10.1083/jcb.9.2.493
    • (1961) J. Biophys. Biochem. Cytol. , vol.9 , pp. 493-495
    • Mauro, A.1
  • 75
    • 84873855851 scopus 로고    scopus 로고
    • Genetic mutations and mechanisms in dilated cardiomyopathy
    • McNally, E.M., J.R. Golbus, and M.J. Puckelwartz. 2013. Genetic mutations and mechanisms in dilated cardiomyopathy. J. Clin. Invest., 123:19-26. http://dx.doi.org/10.1172/JCI62862
    • (2013) J. Clin. Invest. , vol.123 , pp. 19-26
    • McNally, E.M.1    Golbus, J.R.2    Puckelwartz, M.J.3
  • 77
    • 0034282958 scopus 로고    scopus 로고
    • Recruitment of human muscleblind proteins to (CUG)(n) expansions associated with myotonic dystrophy
    • Miller, J.W., C.R. Urbinati, P. Teng-Umnuay, M.G. Stenberg, B.J. Byrne, C.A. Thornton, and M.S. Swanson. 2000. Recruitment of human muscleblind proteins to (CUG)(n) expansions associated with myotonic dystrophy. EMBO J., 19:4439-4448. http://dx.doi.org/10.1093/emboj/19.17.4439
    • (2000) EMBO J. , vol.19 , pp. 4439-4448
    • Miller, J.W.1    Urbinati, C.R.2    Teng-Umnuay, P.3    Stenberg, M.G.4    Byrne, B.J.5    Thornton, C.A.6    Swanson, M.S.7
  • 79
    • 84872415036 scopus 로고    scopus 로고
    • Expression of DUX4 in zebrafish development recapitulates facioscapulohumeral muscular dystrophy
    • Mitsuhashi, H., S. Mitsuhashi, T. Lynn-Jones, G. Kawahara, and L.M. Kunkel. 2013. Expression of DUX4 in zebrafish development recapitulates facioscapulohumeral muscular dystrophy. Hum. Mol. Genet., 22:568-577. http://dx.doi.org/10.1093/hmg/dds467
    • (2013) Hum. Mol. Genet. , vol.22 , pp. 568-577
    • Mitsuhashi, H.1    Mitsuhashi, S.2    Lynn-Jones, T.3    Kawahara, G.4    Kunkel, L.M.5
  • 80
    • 0022496289 scopus 로고
    • Isolation of candidate cDNAs for portions of the Duchenne muscular dystrophy gene
    • Monaco, A.P., R.L. Neve, C. Colletti-Feener, C.J. Bertelson, D.M. Kurnit, and L.M. Kunkel. 1986. Isolation of candidate cDNAs for portions of the Duchenne muscular dystrophy gene. Nature., 323:646-650. http://dx.doi.org/10.1038/323646a0
    • (1986) Nature. , vol.323 , pp. 646-650
    • Monaco, A.P.1    Neve, R.L.2    Colletti-Feener, C.3    Bertelson, C.J.4    Kurnit, D.M.5    Kunkel, L.M.6
  • 81
    • 0023718118 scopus 로고
    • An explanation for the phenotypic differences between patients bearing partial deletions of the DMD locus
    • Monaco, A.P., C.J. Bertelson, S. Liechti-Gallati, H. Moser, and L.M. Kunkel. 1988. An explanation for the phenotypic differences between patients bearing partial deletions of the DMD locus. Genomics., 2:90-95. http://dx.doi.org/10.1016/0888-7543(88)90113-9
    • (1988) Genomics. , vol.2 , pp. 90-95
    • Monaco, A.P.1    Bertelson, C.J.2    Liechti-Gallati, S.3    Moser, H.4    Kunkel, L.M.5
  • 84
    • 0034702027 scopus 로고    scopus 로고
    • Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B)
    • Muchir, A., G. Bonne, A.J. van der Kooi, M. van Meegen, F. Baas, P.A. Bolhuis, M. de Visser, and K. Schwartz. 2000. Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B). Hum. Mol. Genet., 9:1453-1459. http://dx.doi.org/10.1093/hmg/9.9.1453
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1453-1459
    • Muchir, A.1    Bonne, G.2    van der Kooi, A.J.3    van Meegen, M.4    Baas, F.5    Bolhuis, P.A.6    de Visser, M.7    Schwartz, K.8
  • 85
  • 87
    • 77953141955 scopus 로고    scopus 로고
    • Nebulin regulates actin filament lengths by a stabilization mechanism
    • Pappas, C.T., P.A. Krieg, and C.C. Gregorio. 2010. Nebulin regulates actin filament lengths by a stabilization mechanism. J. Cell Biol., 189:859-870. http://dx.doi.org/10.1083/jcb.201001043
    • (2010) J. Cell Biol. , vol.189 , pp. 859-870
    • Pappas, C.T.1    Krieg, P.A.2    Gregorio, C.C.3
  • 88
    • 0027460658 scopus 로고
    • Dystrophin protects the sarcolemma from stresses developed during muscle contraction
    • Petrof, B.J., J.B. Shrager, H.H. Stedman, A.M. Kelly, and H.L. Sweeney. 1993. Dystrophin protects the sarcolemma from stresses developed during muscle contraction. Proc. Natl. Acad. Sci. USA., 90:3710-3714. http://dx.doi.org/10.1073/pnas.90.8.3710
    • (1993) Proc. Natl. Acad. Sci. USA. , vol.90 , pp. 3710-3714
    • Petrof, B.J.1    Shrager, J.B.2    Stedman, H.H.3    Kelly, A.M.4    Sweeney, H.L.5
  • 89
    • 0032076126 scopus 로고    scopus 로고
    • Disruption of splicing regulated by a CUG-binding protein in myotonic dystrophy
    • Philips, A.V., L.T. Timchenko, and T.A. Cooper. 1998. Disruption of splicing regulated by a CUG-binding protein in myotonic dystrophy. Science., 280:737-741. http://dx.doi.org/10.1126/science.280.5364.737
    • (1998) Science. , vol.280 , pp. 737-741
    • Philips, A.V.1    Timchenko, L.T.2    Cooper, T.A.3
  • 90
    • 0036479311 scopus 로고    scopus 로고
    • Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin- associated protein complex
    • Poon, E., E.V. Howman, S.E. Newey, and K.E. Davies. 2002. Association of syncoilin and desmin: linking intermediate filament proteins to the dystrophin- associated protein complex. J. Biol. Chem., 277:3433-3439. http://dx.doi.org/10.1074/jbc.M105273200
    • (2002) J. Biol. Chem. , vol.277 , pp. 3433-3439
    • Poon, E.1    Howman, E.V.2    Newey, S.E.3    Davies, K.E.4
  • 92
    • 33947722764 scopus 로고    scopus 로고
    • Plectin 1f scaffolding at the sarcolemma of dystrophic (mdx) muscle fibers through multiple interactions with -dystroglycan
    • Rezniczek, G.A., P. Konieczny, B. Nikolic, S. Reipert, D. Schneller, C. Abrahamsberg, K.E. Davies, S.J. Winder, and G. Wiche. 2007. Plectin 1f scaffolding at the sarcolemma of dystrophic (mdx) muscle fibers through multiple interactions with -dystroglycan. J. Cell Biol., 176:965-977. http://dx.doi.org/10.1083/jcb.200604179
    • (2007) J. Cell Biol. , vol.176 , pp. 965-977
    • Rezniczek, G.A.1    Konieczny, P.2    Nikolic, B.3    Reipert, S.4    Schneller, D.5    Abrahamsberg, C.6    Davies, K.E.7    Winder, S.J.8    Wiche, G.9
  • 95
    • 0030662379 scopus 로고    scopus 로고
    • Altered phosphorylation and intracellular distribution of a (CUG)n triplet repeat RNA-binding protein in patients with myotonic dystrophy and in myotonin protein kinase knockout mice
    • Roberts, R., N.A. Timchenko, J.W. Miller, S. Reddy, C.T. Caskey, M.S. Swanson, and L.T. Timchenko. 1997. Altered phosphorylation and intracellular distribution of a (CUG)n triplet repeat RNA-binding protein in patients with myotonic dystrophy and in myotonin protein kinase knockout mice. Proc. Natl. Acad. Sci. USA., 94:13221-13226. http://dx.doi.org/10.1073/pnas.94.24.13221
    • (1997) Proc. Natl. Acad. Sci. USA. , vol.94 , pp. 13221-13226
    • Roberts, R.1    Timchenko, N.A.2    Miller, J.W.3    Reddy, S.4    Caskey, C.T.5    Swanson, M.S.6    Timchenko, L.T.7
  • 96
    • 84858198502 scopus 로고    scopus 로고
    • In vivo imaging of molecular interactions at damaged sarcolemma
    • Roostalu, U., and U. Strähle. 2012. In vivo imaging of molecular interactions at damaged sarcolemma. Dev. Cell., 22:515-529. http://dx.doi.org/10.1016/j.devcel.2011.12.008
    • (2012) Dev. Cell. , vol.22 , pp. 515-529
    • Roostalu, U.1    Strähle, U.2
  • 98
    • 0034605070 scopus 로고    scopus 로고
    • The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin
    • Rybakova, I.N., J.R. Patel, and J.M. Ervasti. 2000. The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J. Cell Biol., 150:1209-1214. http://dx.doi.org/10.1083/jcb.150.5.1209
    • (2000) J. Cell Biol. , vol.150 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 100
    • 0034610326 scopus 로고    scopus 로고
    • Functional muscle ischemia in neuronal nitric oxide synthase-deficient skeletal muscle of children with Duchenne muscular dystrophy
    • Sander, M., B. Chavoshan, S.A. Harris, S.T. Iannaccone, J.T. Stull, G.D. Thomas, and R.G. Victor. 2000. Functional muscle ischemia in neuronal nitric oxide synthase-deficient skeletal muscle of children with Duchenne muscular dystrophy. Proc. Natl. Acad. Sci. USA., 97:13818-13823. http://dx.doi.org/10.1073/pnas.250379497
    • (2000) Proc. Natl. Acad. Sci. USA. , vol.97 , pp. 13818-13823
    • Sander, M.1    Chavoshan, B.2    Harris, S.A.3    Iannaccone, S.T.4    Stull, J.T.5    Thomas, G.D.6    Victor, R.G.7
  • 102
    • 0034873099 scopus 로고    scopus 로고
    • Aberrant regulation of insulin receptor alternative splicing is associated with insulin resistance in myotonic dystrophy
    • Savkur, R.S., A.V. Philips, and T.A. Cooper. 2001. Aberrant regulation of insulin receptor alternative splicing is associated with insulin resistance in myotonic dystrophy. Nat. Genet., 29:40-47. http://dx.doi.org/10.1038/ng704
    • (2001) Nat. Genet. , vol.29 , pp. 40-47
    • Savkur, R.S.1    Philips, A.V.2    Cooper, T.A.3
  • 106
    • 0028947317 scopus 로고
    • Foci of trinucleotide repeat transcripts in nuclei of myotonic dystrophy cells and tissues
    • Taneja, K.L., M. McCurrach, M. Schalling, D. Housman, and R.H. Singer. 1995. Foci of trinucleotide repeat transcripts in nuclei of myotonic dystrophy cells and tissues. J. Cell Biol., 128:995-1002. http://dx.doi.org/10.1083/jcb.128.6.995
    • (1995) J. Cell Biol. , vol.128 , pp. 995-1002
    • Taneja, K.L.1    McCurrach, M.2    Schalling, M.3    Housman, D.4    Singer, R.H.5
  • 107
    • 84872236421 scopus 로고    scopus 로고
    • Anoctamins are a family of Ca2+-activated C1- channels
    • Tian, Y., R. Schreiber, and K. Kunzelmann. 2012. Anoctamins are a family of Ca2+-activated C1- channels. J. Cell Sci., 125:4991-4998. http://dx.doi.org/10.1242/jcs.109553
    • (2012) J. Cell Sci. , vol.125 , pp. 4991-4998
    • Tian, Y.1    Schreiber, R.2    Kunzelmann, K.3
  • 108
    • 77950355215 scopus 로고    scopus 로고
    • Genetics and pathogenesis of distal muscular dystrophies
    • Udd, B. 2009. Genetics and pathogenesis of distal muscular dystrophies. Adv. Exp. Med. Biol., 652:23-38. http://dx.doi.org/10.1007/978-90-481-2813-6_3
    • (2009) Adv. Exp. Med. Biol. , vol.652 , pp. 23-38
    • Udd, B.1
  • 116
    • 0025242185 scopus 로고
    • Glycoprotein complex anchoring dystrophin to sarcolemma
    • Yoshida, M., and E. Ozawa. 1990. Glycoprotein complex anchoring dystrophin to sarcolemma. J. Biochem., 108:748-752.
    • (1990) J. Biochem. , vol.108 , pp. 748-752
    • Yoshida, M.1    Ozawa, E.2
  • 117
    • 0028302369 scopus 로고
    • Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl beta-D-glucoside
    • Yoshida, M., A. Suzuki, H. Yamamoto, S. Noguchi, Y. Mizuno, and E. Ozawa. 1994. Dissociation of the complex of dystrophin and its associated proteins into several unique groups by n-octyl beta-D-glucoside. Eur. J. Biochem., 222:1055-1061. http://dx.doi.org/10.1111/j.1432-1033.1994.tb18958.x
    • (1994) Eur. J. Biochem. , vol.222 , pp. 1055-1061
    • Yoshida, M.1    Suzuki, A.2    Yamamoto, H.3    Noguchi, S.4    Mizuno, Y.5    Ozawa, E.6


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