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Volumn 14, Issue 8, 2013, Pages 680-697

Proteomics of the Dystrophin-glycoprotein Complex and Dystrophinopathy

Author keywords

Dystrobrevin; Dystroglycan; Dystrophin; Dystrophin glycoprotein complex; Muscular dystrophy; Sarcoglycan; Sarcospan; Syntrophin

Indexed keywords

ACTIN BINDING PROTEIN; ALPHA DYSTROGLYCAN; ALPHA SARCOGLYCAN; BETA DYSTROGLYCAN; BETA SARCOGLYCAN; DYSTROPHIN; DYSTROPHIN ASSOCIATED PROTEIN; GAMMA SARCOGLYCAN; GLYCOPROTEIN; LAMININ; UTROPHIN;

EID: 84891805627     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/13892037113146660083     Document Type: Review
Times cited : (46)

References (231)
  • 1
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit, S.; Kolmerer, B. Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science, 1995, 270, 293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 2
    • 0028837312 scopus 로고
    • The human dystrophin gene requires 16 hours to be transcribed and is cotranscriptionally spliced
    • Tennyson, C.N.; Klamut, H.J.; Worton, R.G. The human dystrophin gene requires 16 hours to be transcribed and is cotranscriptionally spliced. Nat. Genet., 1995, 9, 184-190.
    • (1995) Nat. Genet. , vol.9 , pp. 184-190
    • Tennyson, C.N.1    Klamut, H.J.2    Worton, R.G.3
  • 3
    • 0023614188 scopus 로고
    • Dystrophin: The protein product of the Duchenne muscular dystrophy locus
    • Hoffman, E.P.; Brown, R.H. Jr; Kunkel, L.M. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell, 1987, 51, 919-928.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown Jr., R.H.2    Kunkel, L.M.3
  • 4
    • 0026094250 scopus 로고
    • Dystrophin-related protein is localized to neuromuscular junctions of adult skeletal muscle
    • Ohlendieck, K.; Ervasti, J.M.; Matsumura, K.; Kahl, S.D.; Leveille, C.J.; Campbell, K.P. Dystrophin-related protein is localized to neuromuscular junctions of adult skeletal muscle. Neuron, 1991, 7, 499-508.
    • (1991) Neuron , vol.7 , pp. 499-508
    • Ohlendieck, K.1    Ervasti, J.M.2    Matsumura, K.3    Kahl, S.D.4    Leveille, C.J.5    Campbell, K.P.6
  • 5
    • 0024600620 scopus 로고
    • Association of dystrophin and an integral membrane glycoprotein
    • Campbell, K.P.; Kahl, S.D. Association of dystrophin and an integral membrane glycoprotein. Nature, 1989, 338, 259-262.
    • (1989) Nature , vol.338 , pp. 259-262
    • Campbell, K.P.1    Kahl, S.D.2
  • 6
    • 0026621608 scopus 로고
    • Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle
    • Matsumura, K.; Ervasti, J.M.; Ohlendieck, K.; Kahl, S.D.; Campbell K.P. Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle. Nature, 1992, 360, 588-591.
    • (1992) Nature , vol.360 , pp. 588-591
    • Matsumura, K.1    Ervasti, J.M.2    Ohlendieck, K.3    Kahl, S.D.4    Campbell, K.P.5
  • 7
    • 83755192039 scopus 로고    scopus 로고
    • Skeletal muscle proteomics: Current approaches, technical challenges and emerging techniques
    • Ohlendieck, K. Skeletal muscle proteomics: current approaches, technical challenges and emerging techniques. Skelet. Muscle, 2011, 1 (1), 6.
    • (2011) Skelet. Muscle , vol.1 , Issue.1 , pp. 6
    • Ohlendieck, K.1
  • 8
    • 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.; Hoffman, E.P.; Bertelson, C.J.; Monaco, A.P.; Feener, C.; Kunkel, L.M.; Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals. Cell, 1987, 50, 509-517.
    • (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
  • 9
    • 0023904860 scopus 로고
    • The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein
    • Koenig, M.; Monaco, A.P.; Kunkel, L.M. The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell, 1988, 53, 219-228.
    • (1988) Cell , vol.53 , pp. 219-228
    • Koenig, M.1    Monaco, A.P.2    Kunkel, L.M.3
  • 10
    • 0025272250 scopus 로고
    • Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
    • Ervasti, J.M.; Ohlendieck, K.; Kahl, S.D.; Gaver, M.G.; Campbell, K.P. Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle. Nature, 1990, 345, 315-319.
    • (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
  • 11
    • 0025242185 scopus 로고
    • Glycoprotein complex anchoring dystrophin to sarcolemma
    • Yoshida, M.; Ozawa, E. Glycoprotein complex anchoring dystrophin to sarcolemma. J. Biochem., 1990, 108, 748-752.
    • (1990) J. Biochem. , vol.108 , pp. 748-752
    • Yoshida, M.1    Ozawa, E.2
  • 14
    • 0025017751 scopus 로고
    • The incidence and evolution of cardiomyopathy in Duchenne muscular dystrophy
    • Nigro, G.; Comi, L.I.; Politano, L.; Bain, R.J. The incidence and evolution of cardiomyopathy in Duchenne muscular dystrophy. Int. J. Cardiol., 1990, 26, 271-277.
    • (1990) Int. J. Cardiol. , vol.26 , pp. 271-277
    • Nigro, G.1    Comi, L.I.2    Politano, L.3    Bain, R.J.4
  • 15
    • 77950362202 scopus 로고    scopus 로고
    • Cardiomyopathy in Duchenne muscular dystrophy: Pathogenesis and therapeutics
    • Fayssoil, A.; Nardi, O.; Orlikowski, D.; Annane, D. Cardiomyopathy in Duchenne muscular dystrophy: pathogenesis and therapeutics. Heart Fail. Rev., 2010, 15, 103-107.
    • (2010) Heart Fail. Rev. , vol.15 , pp. 103-107
    • Fayssoil, A.1    Nardi, O.2    Orlikowski, D.3    Annane, D.4
  • 16
    • 0015142051 scopus 로고
    • Mental retardation in patients with Duchenne progressive muscular dystrophy
    • Kozicka, A.; Prot, J.; Wasilewski, R. Mental retardation in patients with Duchenne progressive muscular dystrophy. J. Neurol. Sci., 1971, 14, 209-213.
    • (1971) J. Neurol. Sci. , vol.14 , pp. 209-213
    • Kozicka, A.1    Prot, J.2    Wasilewski, R.3
  • 21
    • 0030568868 scopus 로고    scopus 로고
    • Characterisation of the dystrophin-related protein utrophin in highly purified skeletal muscle sarcolemma vesicles
    • Ohlendieck, K. Characterisation of the dystrophin-related protein utrophin in highly purified skeletal muscle sarcolemma vesicles. Biochim. Biophys. Acta., 1996, 1283, 215-222.
    • (1996) Biochim. Biophys. Acta. , vol.1283 , pp. 215-222
    • Ohlendieck, K.1
  • 22
    • 0041843714 scopus 로고    scopus 로고
    • β-Bungarotoxin Binding to Acetylcholine Receptor Membranes Studied by Low Angle X-Ray Diffraction
    • Young, H.S.; Herbette, L.G.; Skita, V. β-Bungarotoxin Binding to Acetylcholine Receptor Membranes Studied by Low Angle X-Ray Diffraction. Biophys. J., 2003, 85, 943-953.
    • (2003) Biophys. J. , vol.85 , pp. 943-953
    • Young, H.S.1    Herbette, L.G.2    Skita, V.3
  • 23
    • 0028910144 scopus 로고
    • Characterization of revertant muscle fibers in Duchenne muscular dystrophy, using exon-specific monoclonal antibodies against dystrophin
    • Thanh, L.T.; Nguyen, T.M.; Helliwell, T.R.; Morris, G.E. Characterization of revertant muscle fibers in Duchenne muscular dystrophy, using exon-specific monoclonal antibodies against dystrophin. Am. J. Hum. Genet., 1995, 56, 725-731.
    • (1995) Am. J. Hum. Genet. , vol.56 , pp. 725-731
    • Thanh, L.T.1    Nguyen, T.M.2    Helliwell, T.R.3    Morris, G.E.4
  • 24
    • 0016769512 scopus 로고
    • Newborn screening for Duchenne muscular dystrophy
    • Zellweger, H.; Antonik, A. Newborn screening for Duchenne muscular dystrophy. Pediatrics, 1975, 55, 30-34.
    • (1975) Pediatrics , vol.55 , pp. 30-34
    • Zellweger, H.1    Antonik, A.2
  • 26
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeletonextracellular matrix linkage
    • Campbell, K.P. Three muscular dystrophies: loss of cytoskeletonextracellular matrix linkage. Cell, 1995, 80, 675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 27
    • 0038054542 scopus 로고    scopus 로고
    • Muscular dystrophies: Genes to pathogenesis
    • Dalkilic, I.; Kunkel, L.M. Muscular dystrophies: genes to pathogenesis. Curr. Opin. Genet. Dev., 2003, 13, 231-238.
    • (2003) Curr. Opin. Genet. Dev. , vol.13 , pp. 231-238
    • Dalkilic, I.1    Kunkel, L.M.2
  • 28
    • 0344420060 scopus 로고    scopus 로고
    • Dystrophin and mutations: One gene, several proteins, multiple phenotypes
    • Muntoni, F.; Torelli, S.; Ferlini, A. Dystrophin and mutations: one gene, several proteins, multiple phenotypes. Lancet Neurol., 2003, 2, 731-740.
    • (2003) Lancet Neurol. , vol.2 , pp. 731-740
    • Muntoni, F.1    Torelli, S.2    Ferlini, A.3
  • 29
    • 17444415361 scopus 로고    scopus 로고
    • Spectrin, alpha-actinin, and dystrophin
    • Broderick, M.J.; Winder, S.J. Spectrin, alpha-actinin, and dystrophin. Adv. Protein Chem., 2005, 70, 203-246.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 203-246
    • Broderick, M.J.1    Winder, S.J.2
  • 30
    • 0037138385 scopus 로고    scopus 로고
    • The spectrin repeat: A structural platform for cytoskeletal protein assemblies
    • Djinovic-Carugo, K.; Gautel, M.; Ylänne, J.; Young, P. The spectrin repeat: a structural platform for cytoskeletal protein assemblies. FEBS Lett., 2002, 513, 119-23.
    • (2002) FEBS Lett. , vol.513 , pp. 119-123
    • Djinovic-Carugo, K.1    Gautel, M.2    Ylänne, J.3    Young, P.4
  • 34
    • 0025181885 scopus 로고
    • Molecular and functional analysis of the muscle-specific promoter region of the Duchenne muscular dystrophy gene
    • Klamut, H.J.; Gangopadhyay, S.B.; Worton, R.N.; Ray, P.N. Molecular and functional analysis of the muscle-specific promoter region of the Duchenne muscular dystrophy gene. Mol. Cell. Biol., 1990, 10, 193-205.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 193-205
    • Klamut, H.J.1    Gangopadhyay, S.B.2    Worton, R.N.3    Ray, P.N.4
  • 35
    • 0024595610 scopus 로고
    • Duchenne muscular dystrophy gene product is not identical in muscle and brain
    • Nudel, U.; Zuk, D.; Einat, P.; Zeelon, E.; Levy, Z.; Neuman, S.; Yaffe, D. Duchenne muscular dystrophy gene product is not identical in muscle and brain. Nature, 1989, 337, 76-78.
    • (1989) Nature , vol.337 , pp. 76-78
    • Nudel, U.1    Zuk, D.2    Einat, P.3    Zeelon, E.4    Levy, Z.5    Neuman, S.6    Yaffe, D.7
  • 36
  • 38
    • 0028937525 scopus 로고
    • Dp140: A novel 140 kDa cns transcript from the dystrophin locus
    • Lidov, H.G.W.; Selig, S.; Kunkel, L.M. Dp140: a novel 140 kDa cns transcript from the dystrophin locus. Hum. Mol. Genet., 1995, 4, 329-335.
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 329-335
    • Lidov, H.G.W.1    Selig, S.2    Kunkel, L.M.3
  • 39
    • 0027214837 scopus 로고
    • An alternative dystrophin transcript specific to peripheral nerve
    • Byers, T.J.; Lidov, H.G.W.; Kunkel, L.M. An alternative dystrophin transcript specific to peripheral nerve. Nature Genet., 1993, 4, 77-81.
    • (1993) Nature Genet. , vol.4 , pp. 77-81
    • Byers, T.J.1    Lidov, H.G.W.2    Kunkel, L.M.3
  • 40
    • 0025609360 scopus 로고
    • A novel protein product of the Duchenne muscular dystrophy gene which greatly differs from known isoforms in its structure and tissue distribution
    • Bar, S.; Barnea, E.; Lavy, Z.; Neuman, S.; Yaffe, D.; Nudel, U. A novel protein product of the Duchenne muscular dystrophy gene which greatly differs from known isoforms in its structure and tissue distribution. Biochem. J., 1990, 272, 557-560.
    • (1990) Biochem. J. , vol.272 , pp. 557-560
    • Bar, S.1    Barnea, E.2    Lavy, Z.3    Neuman, S.4    Yaffe, D.5    Nudel, U.6
  • 41
    • 0027314922 scopus 로고
    • Apo-dystrophin 3: A 2. 2 kb transcript from the DMD locus encoding the dystrophin glycoprotein binding site
    • Tinsley, J.M.; Blake, D.J.; Davies, K.E. Apo-dystrophin 3: a 2. 2 kb transcript from the DMD locus encoding the dystrophin glycoprotein binding site. Hum. Mol. Genet., 1993, 2, 521-524.
    • (1993) Hum. Mol. Genet. , vol.2 , pp. 521-524
    • Tinsley, J.M.1    Blake, D.J.2    Davies, K.E.3
  • 42
    • 1542381809 scopus 로고    scopus 로고
    • Diversity of the Brain Dystrophin-Glycoprotein Complex
    • Culligan, K.; Ohlendieck, K. Diversity of the Brain Dystrophin-Glycoprotein Complex. J. Biomed. Biotechnol., 2002, 2, 31-36.
    • (2002) J. Biomed. Biotechnol. , vol.2 , pp. 31-36
    • Culligan, K.1    Ohlendieck, K.2
  • 44
    • 79953297552 scopus 로고    scopus 로고
    • The role of alpha-dystrobrevin in striated muscle
    • Nakamori, M.; Takahashi, M.P. The role of alpha-dystrobrevin in striated muscle. Int. J. Mol. Sci., 2011, 12, 1660-1671.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 1660-1671
    • Nakamori, M.1    Takahashi, M.P.2
  • 51
    • 0034657791 scopus 로고    scopus 로고
    • The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy
    • Norwood, F.L.; Sutherland-Smith, A.J.; Keep, N.H.; Kendrick-Jones, J. The structure of the N-terminal actin-binding domain of human dystrophin and how mutations in this domain may cause Duchenne or Becker muscular dystrophy. Structure, 2000, 8, 481-491.
    • (2000) Structure , vol.8 , pp. 481-491
    • Norwood, F.L.1    Sutherland-Smith, A.J.2    Keep, N.H.3    Kendrick-Jones, J.4
  • 52
    • 84864078710 scopus 로고    scopus 로고
    • The Crystal Structures of Dystrophin and Utrophin Spectrin Repeats: Implications for Domain Boundaries
    • Muthu, M.; Richardson, K.A.; Sutherland-Smith, A.J. The Crystal Structures of Dystrophin and Utrophin Spectrin Repeats: Implications for Domain Boundaries. PLoS ONE, 2012, 7 (7), e40066.
    • (2012) PLoS ONE , vol.7 , Issue.7
    • Muthu, M.1    Richardson, K.A.2    Sutherland-Smith, A.J.3
  • 54
    • 0034903234 scopus 로고    scopus 로고
    • The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation
    • Ilsley, J.L.; Sudol, M.; Winder, S.J. The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation. Cell Signal., 2001, 13, 625-632.
    • (2001) Cell Signal. , vol.13 , pp. 625-632
    • Ilsley, J.L.1    Sudol, M.2    Winder, S.J.3
  • 55
    • 0036157980 scopus 로고    scopus 로고
    • The WW domain: Linking cell signalling to the membrane cytoskeleton
    • Ilsley, J.L.; Sudol, M.; Winder, S.J. The WW domain: linking cell signalling to the membrane cytoskeleton. Cell Signal., 2002, 14, 183-189.
    • (2002) Cell Signal. , vol.14 , pp. 183-189
    • Ilsley, J.L.1    Sudol, M.2    Winder, S.J.3
  • 56
    • 0030775377 scopus 로고    scopus 로고
    • Dystrobrevin and dystrophin: An interaction through coiled-coil motifs
    • Sadoulet-Puccio, H.M.; Rajala, M.; Kunkel, L.M. Dystrobrevin and dystrophin: An interaction through coiled-coil motifs. Proc. Natl. Acad. Sci. USA, 1997, 94, 12413-12418.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12413-12418
    • Sadoulet-Puccio, H.M.1    Rajala, M.2    Kunkel, L.M.3
  • 58
    • 80052435477 scopus 로고    scopus 로고
    • Impending therapies for Duchenne muscular dystrophy
    • Partridge, T.A. Impending therapies for Duchenne muscular dystrophy. Curr. Opin. Neurol., 2011, 24, 415-422.
    • (2011) Curr. Opin. Neurol. , vol.24 , pp. 415-422
    • Partridge, T.A.1
  • 59
    • 0025767124 scopus 로고
    • Purification of dystrophin from skeletal muscle
    • Ervasti, J.M.; Kahl, S.D.; Campbell, K.P. Purification of dystrophin from skeletal muscle. J. Biol. Chem., 1991, 266, 9161-9165.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9161-9165
    • Ervasti, J.M.1    Kahl, S.D.2    Campbell, K.P.3
  • 60
    • 0028353971 scopus 로고
    • Dystrophin predominantly localizes to the transverse tubule/Z-line regions of single ventricular myocytes and exhibits distinct associations with the membrane
    • Peri, V.; Ajdukovic, B.; Holland, P.; Tuana, B.S. Dystrophin predominantly localizes to the transverse tubule/Z-line regions of single ventricular myocytes and exhibits distinct associations with the membrane. Mol. Cell. Biochem., 1994, 130, 57-65.
    • (1994) Mol. Cell. Biochem. , vol.130 , pp. 57-65
    • Peri, V.1    Ajdukovic, B.2    Holland, P.3    Tuana, B.S.4
  • 61
    • 0026067790 scopus 로고
    • Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma
    • Ohlendieck, K.; Ervasti, J.M.; Snook, J.B.; Campbell, K.P. Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma. J. Cell Biol., 1991, 112, 135-148.
    • (1991) J. Cell Biol. , vol.112 , pp. 135-148
    • Ohlendieck, K.1    Ervasti, J.M.2    Snook, J.B.3    Campbell, K.P.4
  • 62
    • 0025881734 scopus 로고
    • Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle
    • Ohlendieck, K.; Campbell, K.P. Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle. FEBS Lett., 1991, 283, 230-234.
    • (1991) FEBS Lett. , vol.283 , pp. 230-234
    • Ohlendieck, K.1    Campbell, K.P.2
  • 63
    • 77954457960 scopus 로고    scopus 로고
    • Mass spectrometric identification of dystrophin isoform Dp427 by on-membrane digestion of sarcolemma from skeletal muscle
    • Lewis, C.; Ohlendieck, K. Mass spectrometric identification of dystrophin isoform Dp427 by on-membrane digestion of sarcolemma from skeletal muscle. Anal. Biochem., 2010, 404, 197-203.
    • (2010) Anal. Biochem. , vol.404 , pp. 197-203
    • Lewis, C.1    Ohlendieck, K.2
  • 64
    • 44049093407 scopus 로고    scopus 로고
    • Glycoprotein enrichment through lectin affinity techniques
    • Mechref, Y.; Madera, M.; Novotny, M.V. Glycoprotein enrichment through lectin affinity techniques. Methods Mol. Biol., 2008, 424, 373-396.
    • (2008) Methods Mol. Biol. , vol.424 , pp. 373-396
    • Mechref, Y.1    Madera, M.2    Novotny, M.V.3
  • 65
    • 0015828190 scopus 로고
    • Purification of wheat germ agglutinin by affinity chromatography on a sepharose-bound N-acetylglucosamine derivative
    • Lotan, R.; Gussin, A. E; Lis, H.; Sharon, N. Purification of wheat germ agglutinin by affinity chromatography on a sepharose-bound N-acetylglucosamine derivative. Biochem. Biophys. Res. Commun., 1973, 52, 656-662.
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 656-662
    • Lotan, R.1    Gussin, A.E.2    Lis, H.3    Sharon, N.4
  • 66
    • 0030026119 scopus 로고    scopus 로고
    • Towards an understanding of the dystrophinglycoprotein complex: Linkage between the extracellular matrix and the membrane cytoskeleton in muscle fibers
    • Ohlendieck, K. Towards an understanding of the dystrophinglycoprotein complex: linkage between the extracellular matrix and the membrane cytoskeleton in muscle fibers. Eur. J. Cell Biol., 1996, 69, 1-10.
    • (1996) Eur. J. Cell Biol. , vol.69 , pp. 1-10
    • Ohlendieck, K.1
  • 67
    • 0024300196 scopus 로고
    • Immunoelectron microscopic localization of dystrophin in myofibres
    • Watkins, S.C.; Hoffman, E.P.; Slayter, H.S.; Kunkel, L.M. Immunoelectron microscopic localization of dystrophin in myofibres. Nature, 1988, 333, 863-866.
    • (1988) Nature , vol.333 , pp. 863-866
    • Watkins, S.C.1    Hoffman, E.P.2    Slayter, H.S.3    Kunkel, L.M.4
  • 68
    • 0027275643 scopus 로고
    • A role for the dystrophinglycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti, J.M.; Campbell, K.P. A role for the dystrophinglycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol., 1993, 122, 809-823.
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 69
    • 0030695947 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex is monomeric and stabilizes actin filaments in vitro through lateral association
    • Rybakova, I.N.; Ervasti, J.M. Dystrophin-glycoprotein complex is monomeric and stabilizes actin filaments in vitro through lateral association. J. Biol. Chem., 1997, 272, 28771-28778.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28771-28778
    • Rybakova, I.N.1    Ervasti, J.M.2
  • 70
    • 0031974345 scopus 로고    scopus 로고
    • Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins
    • Gee, S.H.; Gee, R.; Madhaven, S.H.; Levinson, S.R.; Caldwell, J.H.; Sealock, R.; Froehner, S.C. Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins. J. Neurosci., 1998, 18, 128-137.
    • (1998) J. Neurosci. , vol.18 , pp. 128-137
    • Gee, S.H.1    Gee, R.2    Madhaven, S.H.3    Levinson, S.R.4    Caldwell, J.H.5    Sealock, R.6    Froehner, S.C.7
  • 71
    • 0027361264 scopus 로고
    • Primary structure and muscle-specific expression of the 50-kDa dystrophin-associated glycoprotein (adhalin)
    • Roberds, S.L.; Anderson, R.D.; Ibraghimov-Beskrovnaya, O.; Campbell, K.P. Primary structure and muscle-specific expression of the 50-kDa dystrophin-associated glycoprotein (adhalin). J. Biol. Chem., 1993, 268, 23739-23742.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23739-23742
    • Roberds, S.L.1    Anderson, R.D.2    Ibraghimov-Beskrovnaya, O.3    Campbell, K.P.4
  • 73
    • 35148863239 scopus 로고    scopus 로고
    • Sarcoglycan subcomplex in normal and pathological human muscle fibers
    • Anastasi, G.; Cutroneo, G.; Rizzo, G.; Favaloro, A. Sarcoglycan subcomplex in normal and pathological human muscle fibers. Eur. J. Histochem., 2007, 51 (Suppl 1), 29-33.
    • (2007) Eur. J. Histochem. , vol.51 , Issue.SUPPL. 1 , pp. 29-33
    • Anastasi, G.1    Cutroneo, G.2    Rizzo, G.3    Favaloro, A.4
  • 78
    • 84868147762 scopus 로고    scopus 로고
    • The inside and out of dystroglycan posttranslational modification
    • Moore, C.J.; Winder, S.J. The inside and out of dystroglycan posttranslational modification. Neuromuscul. Disord., 2012, 22, 959-965.
    • (2012) Neuromuscul. Disord. , vol.22 , pp. 959-965
    • Moore, C.J.1    Winder, S.J.2
  • 80
    • 38949130017 scopus 로고    scopus 로고
    • Biology of the striated muscle dystrophin-glycoprotein complex
    • Ervasti, J.M.; Sonnemann, K.J. Biology of the striated muscle dystrophin-glycoprotein complex. Int. Rev. Cytol., 2008, 265, 191-225.
    • (2008) Int. Rev. Cytol. , vol.265 , pp. 191-225
    • Ervasti, J.M.1    Sonnemann, K.J.2
  • 81
    • 84855175087 scopus 로고    scopus 로고
    • The dystrophin-glycoprotein complex in the prevention of muscle damage
    • Gumerson, J.D.; Michele, D.E. The dystrophin-glycoprotein complex in the prevention of muscle damage. J. Biomed. Biotechnol., 2011, 2011, 210797.
    • (2011) J. Biomed. Biotechnol. , vol.2011 , pp. 210797
    • Gumerson, J.D.1    Michele, D.E.2
  • 82
    • 0032246520 scopus 로고    scopus 로고
    • Role of dystrophin isoforms and associated proteins in muscular dystrophy (review)
    • Culligan, K.G.; Mackey, A.J.; Finn, D.M.; Maguire, P.B.; Ohlendieck, K. Role of dystrophin isoforms and associated proteins in muscular dystrophy (review). Int. J. Mol. Med., 1998, 2, 639-648.
    • (1998) Int. J. Mol. Med. , vol.2 , pp. 639-648
    • Culligan, K.G.1    McKey, A.J.2    Finn, D.M.3    Maguire, P.B.4    Ohlendieck, K.5
  • 84
    • 0028812128 scopus 로고
    • Transcription of the dystrophin gene in normal tissues and in skeletal muscle of a family with X-linked dilated cardiomyopathy
    • Mutoni, F.; Melis, M.A.; Ganau, A.; Dubowitz, V. Transcription of the dystrophin gene in normal tissues and in skeletal muscle of a family with X-linked dilated cardiomyopathy. Am. J. Hum. Genet., 1995, 56, 151-157.
    • (1995) Am. J. Hum. Genet. , vol.56 , pp. 151-157
    • Mutoni, F.1    Melis, M.A.2    Ganau, A.3    Dubowitz, V.4
  • 85
    • 77955864157 scopus 로고    scopus 로고
    • Limb-girdle and congenital muscular dystrophies: Current diagnostics, management, and emerging technologies
    • Rocha, C.T.; Hoffman, E.P. Limb-girdle and congenital muscular dystrophies: current diagnostics, management, and emerging technologies. Curr. Neurol. Neurosci. Rep., 2010, 10, 267-276.
    • (2010) Curr. Neurol. Neurosci. Rep. , vol.10 , pp. 267-276
    • Rocha, C.T.1    Hoffman, E.P.2
  • 86
    • 82755181721 scopus 로고    scopus 로고
    • Cell-matrix interactions in muscle disease
    • Carmignac, V.; Durbeej, M. Cell-matrix interactions in muscle disease. J. Pathol., 2012, 226, 200-218.
    • (2012) J. Pathol. , vol.226 , pp. 200-218
    • Carmignac, V.1    Durbeej, M.2
  • 89
    • 70349101617 scopus 로고    scopus 로고
    • Abnormal glycosylation of dystroglycan in human genetic disease
    • Hewitt, J.E. Abnormal glycosylation of dystroglycan in human genetic disease. Biochim. Biophys. Acta., 2009, 1792, 853-861.
    • (2009) Biochim. Biophys. Acta. , vol.1792 , pp. 853-861
    • Hewitt, J.E.1
  • 96
    • 0026328022 scopus 로고
    • Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice
    • Ohlendieck, K.; Campbell, K.P. Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice. J. Cell Biol., 1991, 115, 1685-1694.
    • (1991) J. Cell Biol. , vol.115 , pp. 1685-1694
    • Ohlendieck, K.1    Campbell, K.P.2
  • 97
    • 0037631314 scopus 로고    scopus 로고
    • Skeletal muscle basement membranesarcolemma-cytoskeleton interaction minireview series
    • Campbell, K.P.; Stull, J.T. Skeletal muscle basement membranesarcolemma-cytoskeleton interaction minireview series. J. Biol. Chem., 2003, 278, 12599-12600.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12599-12600
    • Campbell, K.P.1    Stull, J.T.2
  • 98
    • 84866076619 scopus 로고    scopus 로고
    • Comparative Proteomic Profiling of Dystroglycan-Associated Proteins in Wild Type, mdx, and Galgt2 Transgenic Mouse Skeletal Muscle
    • Yoon, J.H.; Johnson, E.; Xu, R.; Martin, L.T.; Martin, P.T.; Montanaro, F. Comparative Proteomic Profiling of Dystroglycan-Associated Proteins in Wild Type, mdx, and Galgt2 Transgenic Mouse Skeletal Muscle. J. Proteome Res., 2012, 11, 4413-4424.
    • (2012) J. Proteome Res. , vol.11 , pp. 4413-4424
    • Yoon, J.H.1    Johnson, E.2    Xu, R.3    Martin, L.T.4    Martin, P.T.5    Montanaro, F.6
  • 101
    • 51149109591 scopus 로고    scopus 로고
    • Complementary methods to assist subcellular fractionation in organellar proteomics
    • Gauthier, D.J.; Lazure, C. Complementary methods to assist subcellular fractionation in organellar proteomics. Expert Rev. Proteomics, 2008, 5, 603-617.
    • (2008) Expert Rev. Proteomics , vol.5 , pp. 603-617
    • Gauthier, D.J.1    Lazure, C.2
  • 102
    • 78449275559 scopus 로고    scopus 로고
    • Subcellular fractionation methods and strategies for proteomics
    • Lee, Y.H.; Tan, H.T.; Chung, M.C. Subcellular fractionation methods and strategies for proteomics. Proteomics, 2010, 10, 3935-3956.
    • (2010) Proteomics , vol.10 , pp. 3935-3956
    • Lee, Y.H.1    Tan, H.T.2    Chung, M.C.3
  • 103
    • 84891798175 scopus 로고    scopus 로고
    • Organelle proteomics in skeletal muscle biology
    • Ohlendieck, K. Organelle proteomics in skeletal muscle biology. J. Integr. Omics, 2012, 2, 27-38.
    • (2012) J. Integr. Omics , vol.2 , pp. 27-38
    • Ohlendieck, K.1
  • 104
    • 78650476062 scopus 로고    scopus 로고
    • Proteomics of total membranes and subcellular membranes
    • Groen, A.J.; Lilley, K.S. Proteomics of total membranes and subcellular membranes. Expert Rev. Proteomics, 2010, 7, 867-878.
    • (2010) Expert Rev. Proteomics , vol.7 , pp. 867-878
    • Groen, A.J.1    Lilley, K.S.2
  • 105
    • 84858838369 scopus 로고    scopus 로고
    • Mass spectrometric characterization of the sarcoplasmic reticulum from rabbit skeletal muscle by onmembrane digestion
    • Staunton, L.; Ohlendieck, K. Mass spectrometric characterization of the sarcoplasmic reticulum from rabbit skeletal muscle by onmembrane digestion. Protein Pept. Lett., 2012, 19, 252-263.
    • (2012) Protein Pept. Lett. , vol.19 , pp. 252-263
    • Staunton, L.1    Ohlendieck, K.2
  • 106
    • 0142182391 scopus 로고    scopus 로고
    • Proteomic analysis of mdx skeletal muscle: Great reduction of adenylate kinase 1 expression and enzymatic activity
    • Ge, Y.; Molloy, M.P.; Chamberlain, J.S.; Andrews, P.C. Proteomic analysis of mdx skeletal muscle: Great reduction of adenylate kinase 1 expression and enzymatic activity. Proteomics, 2003, 3, 1895-1903.
    • (2003) Proteomics , vol.3 , pp. 1895-1903
    • Ge, Y.1    Molloy, M.P.2    Chamberlain, J.S.3    Andrews, P.C.4
  • 107
    • 4444267191 scopus 로고    scopus 로고
    • Differential expression of the skeletal muscle proteome in mdx mice at different ages
    • Ge, Y.; Molloy, M.P.; Chamberlain, J.S.; Andrews, P.C. Differential expression of the skeletal muscle proteome in mdx mice at different ages. Electrophoresis, 2004, 25, 2576-2585.
    • (2004) Electrophoresis , vol.25 , pp. 2576-2585
    • Ge, Y.1    Molloy, M.P.2    Chamberlain, J.S.3    Andrews, P.C.4
  • 109
    • 84855685420 scopus 로고    scopus 로고
    • Proteomic assessment of the acute phase of dystrophin deficiency in mdx mice
    • Gardan-Salmon, D.; Dixon, J.M.; Lonergan, S.M.; Selsby, J.T. Proteomic assessment of the acute phase of dystrophin deficiency in mdx mice. Eur. J. Appl. Physiol., 2011, 111, 2763-2773.
    • (2011) Eur. J. Appl. Physiol. , vol.111 , pp. 2763-2773
    • Gardan-Salmon, D.1    Dixon, J.M.2    Lonergan, S.M.3    Selsby, J.T.4
  • 110
    • 84871824209 scopus 로고    scopus 로고
    • Profiling of age-related changes in the tibialis anterior muscle proteome of the mdx mouse model of dystrophinopathy
    • Carberry, S.; Zweyer, M.; Swandulla, D.; Ohlendieck, K. Profiling of age-related changes in the tibialis anterior muscle proteome of the mdx mouse model of dystrophinopathy. J. Biomed. Bioeng., 2012, 2012, 691641.
    • (2012) J. Biomed. Bioeng. , vol.2012 , pp. 691641
    • Carberry, S.1    Zweyer, M.2    Swandulla, D.3    Ohlendieck, K.4
  • 111
    • 84880404341 scopus 로고    scopus 로고
    • Comparative proteomic profiling of soleus, extensor digitorum longus, flexor digitorum brevis and interosseus muscles from the mdx mouse model of Duchenne muscular dystrophy
    • Carberry, S.; Brinkmeier, H.; Zhang, Y.; Winkler, C.K.; Ohlendieck, K. Comparative proteomic profiling of soleus, extensor digitorum longus, flexor digitorum brevis and interosseus muscles from the mdx mouse model of Duchenne muscular dystrophy. Int. J. Mol. Med. 2013, 32, 544-556.
    • (2013) Int. J. Mol. Med. , vol.32 , pp. 544-556
    • Carberry, S.1    Brinkmeier, H.2    Zhang, Y.3    Winkler, C.K.4    Ohlendieck, K.5
  • 112
    • 84892369116 scopus 로고    scopus 로고
    • Comparative proteomic analysis of the contractile protein-depleted fraction from normal versus dystrophic skeletal muscle
    • In press
    • Carberry, S.; Zweyer, M.; Swandulla, D.; Ohlendieck, K. Comparative proteomic analysis of the contractile protein-depleted fraction from normal versus dystrophic skeletal muscle. Anal. Biochem. 2013: In press.
    • (2013) Anal. Biochem.
    • Carberry, S.1    Zweyer, M.2    Swandulla, D.3    Ohlendieck, K.4
  • 113
    • 33646102225 scopus 로고    scopus 로고
    • Reduced expression of regucalcin in young and aged mdx diaphragm indicates abnormal cytosolic calcium handling in dystrophin-deficient muscle
    • Doran, P.; Dowling, P.; Donoghue, P.; Buffini, M.; Ohlendieck, K. Reduced expression of regucalcin in young and aged mdx diaphragm indicates abnormal cytosolic calcium handling in dystrophin-deficient muscle. Biochim. Biophys. Acta, 2006, 1764, 773-785.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 773-785
    • Doran, P.1    Dowling, P.2    Donoghue, P.3    Buffini, M.4    Ohlendieck, K.5
  • 114
    • 33748339008 scopus 로고    scopus 로고
    • Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP
    • Doran, P.; Martin, G.; Dowling, P.; Jockusch, H.; Ohlendieck, K. Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. Proteomics, 2006, 6, 4610-4621.
    • (2006) Proteomics , vol.6 , pp. 4610-4621
    • Doran, P.1    Martin, G.2    Dowling, P.3    Jockusch, H.4    Ohlendieck, K.5
  • 115
    • 60549096114 scopus 로고    scopus 로고
    • Proteomic profiling of antisense-induced exon skipping reveals reversal of pathobiochemical abnormalities in dystrophic mdx diaphragm
    • Doran, P.; Wilton, S.D.; Fletcher, S.; Ohlendieck, K. Proteomic profiling of antisense-induced exon skipping reveals reversal of pathobiochemical abnormalities in dystrophic mdx diaphragm. Proteomics, 2009, 9, 671-685.
    • (2009) Proteomics , vol.9 , pp. 671-685
    • Doran, P.1    Wilton, S.D.2    Fletcher, S.3    Ohlendieck, K.4
  • 116
    • 84863556161 scopus 로고    scopus 로고
    • Proteomics reveals drastic increase of extracellular matrix proteins collagen and dermatopontin in the aged mdx diaphragm model of Duchenne muscular dystrophy
    • Carberry, S.; Zweyer, M.; Swandulla, D.; Ohlendieck, K. Proteomics reveals drastic increase of extracellular matrix proteins collagen and dermatopontin in the aged mdx diaphragm model of Duchenne muscular dystrophy. Int. J. Mol. Med., 2012, 30, 229-234.
    • (2012) Int. J. Mol. Med. , vol.30 , pp. 229-234
    • Carberry, S.1    Zweyer, M.2    Swandulla, D.3    Ohlendieck, K.4
  • 117
    • 77953292369 scopus 로고    scopus 로고
    • Proteomic profiling of naturally protected extraocular muscles from the dystrophin-deficient mdx mouse
    • Lewis, C.; Ohlendieck, K. Proteomic profiling of naturally protected extraocular muscles from the dystrophin-deficient mdx mouse. Biochem. Biophys. Res. Commun., 2010, 396, 1024-1029.
    • (2010) Biochem. Biophys. Res. Commun. , vol.396 , pp. 1024-1029
    • Lewis, C.1    Ohlendieck, K.2
  • 118
    • 52049098971 scopus 로고    scopus 로고
    • A combined metabolomic and proteomic investigation of the effects of a failure to express dystrophin in the mouse heart
    • Gulston, M.K.; Rubtsov, D.V.; Atherton, H.J.; Clarke, K.; Davies, K.E.; Lilley, K.S.; Griffin, J.L. A combined metabolomic and proteomic investigation of the effects of a failure to express dystrophin in the mouse heart. J. Proteome Res., 2008, 7, 2069-2077.
    • (2008) J. Proteome Res. , vol.7 , pp. 2069-2077
    • Gulston, M.K.1    Rubtsov, D.V.2    Atherton, H.J.3    Clarke, K.4    Davies, K.E.5    Lilley, K.S.6    Griffin, J.L.7
  • 119
    • 77953491510 scopus 로고    scopus 로고
    • Proteomic profiling of the dystrophin-deficient MDX heart reveals drastically altered levels of key metabolic and contractile proteins
    • Lewis, C.; Jockusch, H.; Ohlendieck, K. Proteomic profiling of the dystrophin-deficient MDX heart reveals drastically altered levels of key metabolic and contractile proteins. J. Biomed. Biotechnol., 2010, 2010, 648501.
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 648501
    • Lewis, C.1    Jockusch, H.2    Ohlendieck, K.3
  • 120
    • 84881229184 scopus 로고    scopus 로고
    • Proteomic profiling of cardiomyopathic tissue from the aged mdx model of Duchenne muscular dystrophy reveals a drastic decrease in laminin, nidogen and annexin
    • Holland, A.; Dowling, P.; Zweyer, M.; Swandulla, D.; Henry, M.; Clynes, M.; Ohlendieck, K. Proteomic profiling of cardiomyopathic tissue from the aged mdx model of Duchenne muscular dystrophy reveals a drastic decrease in laminin, nidogen and annexin. Proteomics, 2013, 13, 2312-2323.
    • (2013) Proteomics , vol.13 , pp. 2312-2323
    • Holland, A.1    Dowling, P.2    Zweyer, M.3    Swandulla, D.4    Henry, M.5    Clynes, M.6    Ohlendieck, K.7
  • 122
    • 33746263851 scopus 로고    scopus 로고
    • Use of nitrocellulose membranes for protein characterization by matrixassisted laser desorption/ionization mass spectrometry
    • Luque-Garcia, J.L.; Zhou, G.; Sun, T.T.; Neubert, T.A. Use of nitrocellulose membranes for protein characterization by matrixassisted laser desorption/ionization mass spectrometry. Anal. Chem., 2006, 78, 5102-5108.
    • (2006) Anal. Chem. , vol.78 , pp. 5102-5108
    • Luque-Garcia, J.L.1    Zhou, G.2    Sun, T.T.3    Neubert, T.A.4
  • 123
    • 67649171407 scopus 로고    scopus 로고
    • On-membrane tryptic digestion of proteins for mass spectrometry analysis
    • Luque-Garcia, J.L.; Neubert, T.A. On-membrane tryptic digestion of proteins for mass spectrometry analysis. Methods Mol. Biol., 2009, 536, 331-341.
    • (2009) Methods Mol. Biol. , vol.536 , pp. 331-341
    • Luque-Garcia, J.L.1    Neubert, T.A.2
  • 124
    • 79961225194 scopus 로고    scopus 로고
    • On-membrane proteolytic digestion of electroblotted proteins
    • Simspon, R.J. On-membrane proteolytic digestion of electroblotted proteins. Cold Spring Harb. Protoc., 2011, 2011, 995-997.
    • (2011) Cold Spring Harb. Protoc. , vol.2011 , pp. 995-997
    • Simspon, R.J.1
  • 125
    • 80053587125 scopus 로고    scopus 로고
    • Mass spectrometric characterization of proteins transferred from polyacrylamide gels to membrane filters
    • Ino, Y.; Hirano, H. Mass spectrometric characterization of proteins transferred from polyacrylamide gels to membrane filters. FEBS J., 2011, 278, 3807-3814.
    • (2011) FEBS J. , vol.278 , pp. 3807-3814
    • Ino, Y.1    Hirano, H.2
  • 126
    • 84879363265 scopus 로고    scopus 로고
    • On-Membrane Digestion Technology for Muscle Proteomics
    • Ohlendieck, K. On-Membrane Digestion Technology for Muscle Proteomics. J. Membr. Sep. Technol., 2013, 2, 1-12.
    • (2013) J. Membr. Sep. Technol. , vol.2 , pp. 1-12
    • Ohlendieck, K.1
  • 127
    • 78649556615 scopus 로고    scopus 로고
    • Exon-skipped dystrophins for treatment of Duchenne muscular dystrophy: Mass spectrometry mapping of most exons and cooperative domain designs based on single molecule mechanics
    • Krieger, C.C.; Bhasin, N.; Tewari, M.; Brown, A.E.; Safer, D.; Sweeney, H.L.; Discher, D.E. Exon-skipped dystrophins for treatment of Duchenne muscular dystrophy: mass spectrometry mapping of most exons and cooperative domain designs based on single molecule mechanics. Cytoskeleton (Hoboken), 2010, 67, 796-807.
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 796-807
    • Krieger, C.C.1    Bhasin, N.2    Tewari, M.3    Brown, A.E.4    Safer, D.5    Sweeney, H.L.6    Discher, D.E.7
  • 133
    • 79955496674 scopus 로고    scopus 로고
    • Animal models of human genetic diseases: Do they need to be faithful to be useful?
    • Guenet, J.L. Animal models of human genetic diseases: do they need to be faithful to be useful? Mol. Genet. Genomics, 2011, 286, 1-20.
    • (2011) Mol. Genet. Genomics , vol.286 , pp. 1-20
    • Guenet, J.L.1
  • 135
    • 38349131087 scopus 로고    scopus 로고
    • Proteomic profiling of animal models mimicking skeletal muscle disorders
    • Doran, P.; Gannon, J.; O'Connell, K.; Ohlendieck, K. Proteomic profiling of animal models mimicking skeletal muscle disorders. Proteomics Clin. Appl., 2007, 1, 1169-1184.
    • (2007) Proteomics Clin. Appl. , vol.1 , pp. 1169-1184
    • Doran, P.1    Gannon, J.2    O'Connell, K.3    Ohlendieck, K.4
  • 136
    • 58749101371 scopus 로고    scopus 로고
    • The value of mammalian models for Duchenne muscular dystrophy in developing therapeutic strategies
    • Banks, G.B.; Chamberlain, J.S. The value of mammalian models for Duchenne muscular dystrophy in developing therapeutic strategies. Curr. Top. Dev. Biol., 2008, 84, 431-453.
    • (2008) Curr. Top. Dev. Biol. , vol.84 , pp. 431-453
    • Banks, G.B.1    Chamberlain, J.S.2
  • 139
    • 0036591684 scopus 로고    scopus 로고
    • Muscular dystrophies involving the dystrophin-glycoprotein complex: An overview of current mouse models
    • Durbeej, M.; Campbell, K.P. Muscular dystrophies involving the dystrophin-glycoprotein complex: an overview of current mouse models. Curr. Opin. Genet. Dev., 2002, 12, 349-361.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 349-361
    • Durbeej, M.1    Campbell, K.P.2
  • 141
    • 0024263367 scopus 로고
    • Canine X-linked muscular dystrophy. An animal model of Duchenne muscular dystrophy: Clinical studies
    • Valentine, B.A.; Cooper, B.J.; de Lahunta, A.; O'Quinn, R.; Blue, J.T. Canine X-linked muscular dystrophy. An animal model of Duchenne muscular dystrophy: clinical studies. J. Neurol. Sci., 1988, 88, 69-81.
    • (1988) J. Neurol. Sci. , vol.88 , pp. 69-81
    • Valentine, B.A.1    Cooper, B.J.2    de Lahunta, A.3    O'Quinn, R.4    Blue, J.T.5
  • 142
    • 0022870853 scopus 로고
    • Progressive muscular dystrophy in a golden retriever dog: Light microscope and ultrastructural features at 4 and 8 months
    • Valentine, B.A.; Cooper, B.J.; Cummings, J.F.; deLahunta, A. Progressive muscular dystrophy in a golden retriever dog: light microscope and ultrastructural features at 4 and 8 months. Acta Neuropathol., 1986, 71, 301-310.
    • (1986) Acta Neuropathol. , vol.71 , pp. 301-310
    • Valentine, B.A.1    Cooper, B.J.2    Cummings, J.F.3    deLahunta, A.4
  • 144
    • 80052087602 scopus 로고    scopus 로고
    • Physical therapy assessment tools to evaluate disease progression and phenotype variability in Golden Retriever muscular dystrophy
    • Gaiad, T.P.; Silva, M.B.; Silva, G.C.; Caromano, F.A.; Miglino, M.A.; Ambrósio, C.E. Physical therapy assessment tools to evaluate disease progression and phenotype variability in Golden Retriever muscular dystrophy. Res. Vet. Sci., 2011, 91, 188-193.
    • (2011) Res. Vet. Sci. , vol.91 , pp. 188-193
    • Gaiad, T.P.1    Silva, M.B.2    Silva, G.C.3    Caromano, F.A.4    Miglino, M.A.5    Ambrósio, C.E.6
  • 145
    • 79960054904 scopus 로고    scopus 로고
    • Golden retriever muscular dystrophy (GRMD): Developing and maintaining a colony and physiological functional measurements
    • Kornegay, J.N.; Bogan, J.R.; Bogan, D.J.; Childers, M.K.; Grange, R.W. Golden retriever muscular dystrophy (GRMD): Developing and maintaining a colony and physiological functional measurements. Methods Mol. Biol., 2011, 709, 105-123.
    • (2011) Methods Mol. Biol. , vol.709 , pp. 105-123
    • Kornegay, J.N.1    Bogan, J.R.2    Bogan, D.J.3    Childers, M.K.4    Grange, R.W.5
  • 147
    • 0024540879 scopus 로고
    • Conversion of mdx myofibres from dystrophinnegative to-positive by injection of normal myoblasts
    • Partridge, T.A.; Morgan, J.E.; Coulton, G.R.; Hoffman, E.P.; Kunkel, L.M. Conversion of mdx myofibres from dystrophinnegative to-positive by injection of normal myoblasts. Nature, 1989, 337, 176-179.
    • (1989) Nature , vol.337 , pp. 176-179
    • Partridge, T.A.1    Morgan, J.E.2    Coulton, G.R.3    Hoffman, E.P.4    Kunkel, L.M.5
  • 148
    • 0023091942 scopus 로고
    • The mutant mdx: Inherited myopathy in the mouse. Morphological studies of nerves, muscles and endplates
    • Torres, L.F.; Duchen, L.W. The mutant mdx: inherited myopathy in the mouse. Morphological studies of nerves, muscles and endplates. Brain, 1987, 110, 269-299.
    • (1987) Brain , vol.110 , pp. 269-299
    • Torres, L.F.1    Duchen, L.W.2
  • 149
    • 0025662048 scopus 로고
    • Dystrophin-deficient mdx muscle fibers are preferentially vulnerable to necrosis induced by experimental lengthening contractions
    • Weller, B.; Karpati, G.; Carpenter, S. Dystrophin-deficient mdx muscle fibers are preferentially vulnerable to necrosis induced by experimental lengthening contractions. J. Neurol. Sci., 1990, 100, 9-13.
    • (1990) J. Neurol. Sci. , vol.100 , pp. 9-13
    • Weller, B.1    Karpati, G.2    Carpenter, S.3
  • 150
    • 0033695935 scopus 로고    scopus 로고
    • Contraction-induced injury to single permeabilized muscle fibers from mdx, transgenic mdx, and control mice
    • Lynch, G.S.; Rafael, J.A.; Chamberlain, J.S.; Faulkner, J.A. Contraction-induced injury to single permeabilized muscle fibers from mdx, transgenic mdx, and control mice. Am. J. Physiol. Cell. Physiol., 2000, 279, C1290-C1294.
    • (2000) Am. J. Physiol. Cell. Physiol. , vol.279
    • Lynch, G.S.1    Rafael, J.A.2    Chamberlain, J.S.3    Faulkner, J.A.4
  • 151
    • 0026032731 scopus 로고
    • Decreased osmotic stability of dystrophinless muscle cells from the mdx mouse
    • Menke, A.; Jockusch, H. Decreased osmotic stability of dystrophinless muscle cells from the mdx mouse. Nature, 1991, 349, 69-71.
    • (1991) Nature , vol.349 , pp. 69-71
    • Menke, A.1    Jockusch, H.2
  • 152
    • 0023739851 scopus 로고
    • Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice
    • Turner, P.R.; Westwood, T.; Regen, C.M.; Steinhardt, R.A. Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice. Nature, 1988, 335, 735-738.
    • (1988) Nature , vol.335 , pp. 735-738
    • Turner, P.R.1    Westwood, T.2    Regen, C.M.3    Steinhardt, R.A.4
  • 154
    • 38849097891 scopus 로고    scopus 로고
    • Calcium misregulation and the pathogenesis of muscular dystrophy
    • Hopf, F.W.; Turner, P.R.; Steinhardt, R.A. Calcium misregulation and the pathogenesis of muscular dystrophy. Subcell. Biochem., 2007, 45, 429-464.
    • (2007) Subcell. Biochem. , vol.45 , pp. 429-464
    • Hopf, F.W.1    Turner, P.R.2    Steinhardt, R.A.3
  • 156
    • 0036092560 scopus 로고    scopus 로고
    • Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle
    • Culligan, K.; Banville, N.; Dowling, P.; Ohlendieck, K. Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle. J. Appl. Physiol., 2002, 92, 435-445.
    • (2002) J. Appl. Physiol. , vol.92 , pp. 435-445
    • Culligan, K.1    Banville, N.2    Dowling, P.3    Ohlendieck, K.4
  • 157
    • 2342614190 scopus 로고    scopus 로고
    • Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy
    • Dowling, P.; Doran, P.; Ohlendieck, K. Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy. Biochem. J., 2004, 379, 479-488.
    • (2004) Biochem. J. , vol.379 , pp. 479-488
    • Dowling, P.1    Doran, P.2    Ohlendieck, K.3
  • 158
    • 0038823857 scopus 로고    scopus 로고
    • Comparative analysis of Dp427-deficient mdx tissues shows that the milder dystrophic phenotype of extraocular and toe muscle fibres is associated with a persistent expression of beta-dystroglycan
    • Dowling, P.; Lohan, J.; Ohlendieck, K. Comparative analysis of Dp427-deficient mdx tissues shows that the milder dystrophic phenotype of extraocular and toe muscle fibres is associated with a persistent expression of beta-dystroglycan. Eur. J. Cell Biol., 2003, 82, 222-230.
    • (2003) Eur. J. Cell Biol. , vol.82 , pp. 222-230
    • Dowling, P.1    Lohan, J.2    Ohlendieck, K.3
  • 159
    • 0036188005 scopus 로고    scopus 로고
    • Distal mdx muscle groups exhibiting up-regulation of utrophin and rescue of dystrophin-associated glycoproteins exemplify a protected phenotype in muscular dystrophy
    • Dowling, P.; Culligan, K.; Ohlendieck, K. Distal mdx muscle groups exhibiting up-regulation of utrophin and rescue of dystrophin-associated glycoproteins exemplify a protected phenotype in muscular dystrophy. Naturwissenschaften, 2002, 89, 75-78.
    • (2002) Naturwissenschaften , vol.89 , pp. 75-78
    • Dowling, P.1    Culligan, K.2    Ohlendieck, K.3
  • 160
    • 33847684752 scopus 로고    scopus 로고
    • Intrinsic laryngeal muscles are spared from myonecrosis in the mdx mouse model of Duchenne muscular dystrophy
    • Marques, M.J.; Ferretti, R.; Vomero, V.U.; Minatel, E.; Neto, H.S. Intrinsic laryngeal muscles are spared from myonecrosis in the mdx mouse model of Duchenne muscular dystrophy. Muscle Nerve, 2007, 35, 349-353.
    • (2007) Muscle Nerve , vol.35 , pp. 349-353
    • Marques, M.J.1    Ferretti, R.2    Vomero, V.U.3    Minatel, E.4    Neto, H.S.5
  • 163
    • 0036823755 scopus 로고    scopus 로고
    • Gene transfer studies in animals: What do they really tell us about the prospects for gene therapy in DMD?
    • Wells, D.J.; Wells, K.E. Gene transfer studies in animals: what do they really tell us about the prospects for gene therapy in DMD? Neuromuscul. Disord., 2002, 12, S11-S22.
    • (2002) Neuromuscul. Disord. , vol.12
    • Wells, D.J.1    Wells, K.E.2
  • 164
    • 84862635331 scopus 로고    scopus 로고
    • Pharmacologically targeting the primary defect and downstream pathology in Duchenne muscular dystrophy
    • Fairclough, R.J.; Perkins, K.J.; Davies, K.E. Pharmacologically targeting the primary defect and downstream pathology in Duchenne muscular dystrophy. Curr. Gene Ther., 2012, 12, 206-244.
    • (2012) Curr. Gene Ther. , vol.12 , pp. 206-244
    • Fairclough, R.J.1    Perkins, K.J.2    Davies, K.E.3
  • 165
    • 84861702473 scopus 로고    scopus 로고
    • Pre-clinical drug tests in the mdx mouse as a model of dystrophinopathies: An overview
    • De Luca, A. Pre-clinical drug tests in the mdx mouse as a model of dystrophinopathies: an overview. Acta Myol., 2012, 31, 40-47.
    • (2012) Acta Myol. , vol.31 , pp. 40-47
    • De Luca, A.1
  • 166
    • 0029001953 scopus 로고
    • Phenotype of dystrophinopathy in old mdx mice
    • Lefaucheur, J.P.; Pastoret, C.; Sebille, A. Phenotype of dystrophinopathy in old mdx mice. Anat. Rec., 1995, 242, 70-76.
    • (1995) Anat. Rec. , vol.242 , pp. 70-76
    • Lefaucheur, J.P.1    Pastoret, C.2    Sebille, A.3
  • 167
    • 77951160191 scopus 로고    scopus 로고
    • 2+ homeostasis during fatigue
    • 2+ homeostasis during fatigue. Exp. Physiol., 2010, 95, 641-656.
    • (2010) Exp. Physiol. , vol.95 , pp. 641-656
    • Head, S.I.1
  • 168
    • 0028906307 scopus 로고
    • MDX mice show progressive weakness and muscle deterioration with age
    • Pastoret, C.; Sebille, A. MDX mice show progressive weakness and muscle deterioration with age. J. Neurol. Sci., 1995, 129, 97-105.
    • (1995) J. Neurol. Sci. , vol.129 , pp. 97-105
    • Pastoret, C.1    Sebille, A.2
  • 169
    • 0035449110 scopus 로고    scopus 로고
    • Force and power output of fast and slow skeletal muscles from mdx mice 6-28 months old
    • Lynch, G.S.; Hinkle, R.T.; Chamberlain, J.S.; Brooks, S.V.; Faulkner, J.A. Force and power output of fast and slow skeletal muscles from mdx mice 6-28 months old. J. Physiol., 2001, 535, 591-600.
    • (2001) J. Physiol. , vol.535 , pp. 591-600
    • Lynch, G.S.1    Hinkle, R.T.2    Chamberlain, J.S.3    Brooks, S.V.4    Faulkner, J.A.5
  • 170
    • 34347374860 scopus 로고    scopus 로고
    • Dystrophin-deficient mdx mice display a reduced life span and are susceptible to spontaneous rhabdomyosarcoma
    • Chamberlain, J.S.; Metzger, J.; Reyes, M.; Townsend, D.; Faulkner, J.A. Dystrophin-deficient mdx mice display a reduced life span and are susceptible to spontaneous rhabdomyosarcoma. FASEB J., 2007, 21, 2195-2204.
    • (2007) FASEB J. , vol.21 , pp. 2195-2204
    • Chamberlain, J.S.1    Metzger, J.2    Reyes, M.3    Townsend, D.4    Faulkner, J.A.5
  • 171
    • 0030936938 scopus 로고    scopus 로고
    • Impaired functional and structural recovery after muscle injury in dystrophic mdx mice
    • Irintchev, A.; Zweyer, M.; Wernig, A. Impaired functional and structural recovery after muscle injury in dystrophic mdx mice. Neuromuscul. Disord., 1997, 7, 117-125.
    • (1997) Neuromuscul. Disord. , vol.7 , pp. 117-125
    • Irintchev, A.1    Zweyer, M.2    Wernig, A.3
  • 172
    • 77953042829 scopus 로고    scopus 로고
    • Muscle weakness and atrophy are associated with decreased regenerative capacity and changes in mTOR signaling in skeletal muscles of venerable (18-24-month-old) dystrophic mdx mice
    • Mouisel, E.; Vignaud, A.; Hourde, C.; Butler-Browne, G.; Ferry, A. Muscle weakness and atrophy are associated with decreased regenerative capacity and changes in mTOR signaling in skeletal muscles of venerable (18-24-month-old) dystrophic mdx mice. Muscle Nerve, 2010, 41, 809-818.
    • (2010) Muscle Nerve , vol.41 , pp. 809-818
    • Mouisel, E.1    Vignaud, A.2    Hourde, C.3    Butler-Browne, G.4    Ferry, A.5
  • 173
    • 67650360433 scopus 로고    scopus 로고
    • Deconstructing calsequestrin. Complex buffering in the calcium store of skeletal muscle
    • Royer, L.; Ríos, E. Deconstructing calsequestrin. Complex buffering in the calcium store of skeletal muscle. J. Physiol., 2009, 587, 3101-3111.
    • (2009) J. Physiol. , vol.587 , pp. 3101-3111
    • Royer, L.1    Ríos, E.2
  • 174
    • 84879343220 scopus 로고    scopus 로고
    • Proteomic profiling of the contractile apparatus from skeletal muscle
    • Holland, A.; Ohlendieck, K. Proteomic profiling of the contractile apparatus from skeletal muscle. Expert Rev. Proteomics, 2013, 10, 239-257.
    • (2013) Expert Rev. Proteomics , vol.10 , pp. 239-257
    • Holland, A.1    Ohlendieck, K.2
  • 175
    • 84855685417 scopus 로고    scopus 로고
    • Rescue of dystrophic skeletal muscle by PGC-1α involves a fast to slow fiber type shift in the mdx mouse
    • Selsby, J.T.; Morine, K.J.; Pendrak, K.; Barton, E.R.; Sweeney, H.L. Rescue of dystrophic skeletal muscle by PGC-1α involves a fast to slow fiber type shift in the mdx mouse. PLoS One, 2012, 7 (1), e30063.
    • (2012) PLoS One , vol.7 , Issue.1
    • Selsby, J.T.1    Morine, K.J.2    Pendrak, K.3    Barton, E.R.4    Sweeney, H.L.5
  • 176
    • 84891309567 scopus 로고    scopus 로고
    • Muscle as a secretory organ
    • Pedersen, B.K. Muscle as a secretory organ. Compr. Physiol., 2013, 3, 1337-1362.
    • (2013) Compr. Physiol. , vol.3 , pp. 1337-1362
    • Pedersen, B.K.1
  • 178
    • 0034737503 scopus 로고    scopus 로고
    • Role of regucalcin in calcium signaling
    • Yamaguchi, M. Role of regucalcin in calcium signaling. Life Sci., 2000, 66, 1769-1780.
    • (2000) Life Sci. , vol.66 , pp. 1769-1780
    • Yamaguchi, M.1
  • 180
    • 79959282881 scopus 로고    scopus 로고
    • Regucalcin and cell regulation: Role as a suppressor protein in signal transduction
    • Yamaguchi, M. Regucalcin and cell regulation: role as a suppressor protein in signal transduction. Mol. Cell. Biochem., 2011, 353, 101-137.
    • (2011) Mol. Cell. Biochem. , vol.353 , pp. 101-137
    • Yamaguchi, M.1
  • 181
    • 0033939421 scopus 로고    scopus 로고
    • Calcium ion in skeletal muscle: Its crucial role for muscle function, plasticity, and disease
    • Berchtold, M.W.; Brinkmeier, H.; Muntener, M. Calcium ion in skeletal muscle: its crucial role for muscle function, plasticity, and disease. Physiol. Rev., 2000, 80, 1215-1265.
    • (2000) Physiol. Rev. , vol.80 , pp. 1215-1265
    • Berchtold, M.W.1    Brinkmeier, H.2    Muntener, M.3
  • 183
    • 45449104412 scopus 로고    scopus 로고
    • Transient receptor potential cation channels in normal and dystrophic mdx muscle
    • Krüger, J.; Kunert-Keil, C.; Bisping, F.; Brinkmeier, H. Transient receptor potential cation channels in normal and dystrophic mdx muscle. Neuromuscul. Disord., 2008, 18, 501-513.
    • (2008) Neuromuscul. Disord. , vol.18 , pp. 501-513
    • Krüger, J.1    Kunert-Keil, C.2    Bisping, F.3    Brinkmeier, H.4
  • 184
    • 79959811808 scopus 로고    scopus 로고
    • TRP channels in skeletal muscle: Gene expression, function and implications for disease
    • Brinkmeier, H. TRP channels in skeletal muscle: gene expression, function and implications for disease. Adv. Exp. Med. Biol., 2011, 704, 749-758.
    • (2011) Adv. Exp. Med. Biol. , vol.704 , pp. 749-758
    • Brinkmeier, H.1
  • 185
    • 84862277020 scopus 로고    scopus 로고
    • TRP channels in normal and dystrophic skeletal muscle
    • Gailly, P. TRP channels in normal and dystrophic skeletal muscle. Curr. Opin. Pharmacol., 2012, 12, 326-334.
    • (2012) Curr. Opin. Pharmacol. , vol.12 , pp. 326-334
    • Gailly, P.1
  • 187
    • 84874157611 scopus 로고    scopus 로고
    • The protective and therapeutic function of small heat shock proteins in neurological diseases
    • Brownell, S.E.; Becker, R.A.; Steinman, L. The protective and therapeutic function of small heat shock proteins in neurological diseases. Front. Immunol., 2012, 3, 74.
    • (2012) Front. Immunol. , vol.3 , pp. 74
    • Brownell, S.E.1    Becker, R.A.2    Steinman, L.3
  • 189
    • 84555191575 scopus 로고    scopus 로고
    • Proteomic analysis of dystrophic muscle
    • Lewis, C.; Doran, P.; Ohlendieck, K. Proteomic analysis of dystrophic muscle. Methods Mol. Biol., 2012, 798, 357-369.
    • (2012) Methods Mol. Biol. , vol.798 , pp. 357-369
    • Lewis, C.1    Doran, P.2    Ohlendieck, K.3
  • 190
    • 25144461582 scopus 로고    scopus 로고
    • Wrapping the alpha-crystallin domain fold in a chaperone assembly
    • Stamler, R.; Kappe, G.; Boelens, W.; Slingsby, C. Wrapping the alpha-crystallin domain fold in a chaperone assembly. J. Mol. Biol., 2005, 353, 68-79.
    • (2005) J. Mol. Biol. , vol.353 , pp. 68-79
    • Stamler, R.1    Kappe, G.2    Boelens, W.3    Slingsby, C.4
  • 191
    • 12944328888 scopus 로고    scopus 로고
    • Comparison of the small heat shock proteins alphaB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle
    • Golenhofen, N.; Perng, M.D.; Quinlan, R.A.; Drenckhahn, D. Comparison of the small heat shock proteins alphaB-crystallin, MKBP, HSP25, HSP20, and cvHSP in heart and skeletal muscle. Histochem. Cell Biol., 2004, 122, 415-425.
    • (2004) Histochem. Cell Biol. , vol.122 , pp. 415-425
    • Golenhofen, N.1    Perng, M.D.2    Quinlan, R.A.3    Drenckhahn, D.4
  • 192
    • 84873449631 scopus 로고    scopus 로고
    • Proteomic identification of biomarkers of skeletal muscle disorders
    • Ohlendieck, K. Proteomic identification of biomarkers of skeletal muscle disorders. Biomark. Med., 2013, 7, 169-186.
    • (2013) Biomark. Med. , vol.7 , pp. 169-186
    • Ohlendieck, K.1
  • 194
    • 82455201152 scopus 로고    scopus 로고
    • Structural, biochemical, cellular, and functional changes in skeletal muscle extracellular matrix with aging
    • Kragstrup, T.W.; Kjaer, M.; Mackey, A.L. Structural, biochemical, cellular, and functional changes in skeletal muscle extracellular matrix with aging. Scand. J. Med. Sci. Sports, 2011, 21, 749-757.
    • (2011) Scand. J. Med. Sci. Sports , vol.21 , pp. 749-757
    • Kragstrup, T.W.1    Kjaer, M.2    McKey, A.L.3
  • 195
    • 0028332180 scopus 로고
    • Agerelated changes in collagen gene expression in the muscles of mdx dystrophic and normal mice
    • Goldspink, G.; Fernandes K.; Williams, P.E.; Wells, D.J. Agerelated changes in collagen gene expression in the muscles of mdx dystrophic and normal mice. Neuromuscul. Disord., 1994, 4, 183-191.
    • (1994) Neuromuscul. Disord. , vol.4 , pp. 183-191
    • Goldspink, G.1    Fernandes, K.2    Williams, P.E.3    Wells, D.J.4
  • 197
    • 33749076089 scopus 로고    scopus 로고
    • Dermatopontin, a novel player in the biology of the extracellular matrix
    • Okamoto, O.; Fujiwara, S. Dermatopontin, a novel player in the biology of the extracellular matrix. Connect. Tissue Res., 2006, 47, 177-189.
    • (2006) Connect. Tissue Res. , vol.47 , pp. 177-189
    • Okamoto, O.1    Fujiwara, S.2
  • 199
    • 0037276860 scopus 로고    scopus 로고
    • The heart in human dystrophinopathies
    • Finsterer, J.; Stöllberger, C. The heart in human dystrophinopathies. Cardiology, 2003, 99, 1-19.
    • (2003) Cardiology , vol.99 , pp. 1-19
    • Finsterer, J.1    Stöllberger, C.2
  • 201
    • 22544433443 scopus 로고    scopus 로고
    • Deficiency in Cardiac Dystrophin Affects the Abundance of the alpha-/beta-dystroglycan complex
    • Lohan, J.; Culligan, K.; Ohlendieck, K. Deficiency in Cardiac Dystrophin Affects the Abundance of the alpha-/beta-dystroglycan complex. J. Biomed. Biotechnol., 2005, 2005, 28-36.
    • (2005) J. Biomed. Biotechnol. , vol.2005 , pp. 28-36
    • Lohan, J.1    Culligan, K.2    Ohlendieck, K.3
  • 202
    • 3242778524 scopus 로고    scopus 로고
    • 2+-binding proteins calsequestrin and sarcalumenin in dystrophindeficient cardiac muscle
    • 2+-binding proteins calsequestrin and sarcalumenin in dystrophindeficient cardiac muscle. Biochim. Biophys. Acta, 2004, 1689, 252-258.
    • (2004) Biochim. Biophys. Acta , vol.1689 , pp. 252-258
    • Lohan, J.1    Ohlendieck, K.2
  • 204
    • 0022625394 scopus 로고
    • The association of cardiac muscle necrosis and inflammation with the degenerative and persistent myopathy of MDX mice
    • Bridges, L.R. The association of cardiac muscle necrosis and inflammation with the degenerative and persistent myopathy of MDX mice. J. Neurol. Sci., 1986, 72, 147-157.
    • (1986) J. Neurol. Sci. , vol.72 , pp. 147-157
    • Bridges, L.R.1
  • 205
    • 0030272035 scopus 로고    scopus 로고
    • Contractile properties of myocardium are altered in dystrophin-deficient mdx mice
    • Sapp, J.L.; Bobet, J.; Howlett, S.E. Contractile properties of myocardium are altered in dystrophin-deficient mdx mice. J. Neurol. Sci., 1996, 142, 17-24.
    • (1996) J. Neurol. Sci. , vol.142 , pp. 17-24
    • Sapp, J.L.1    Bobet, J.2    Howlett, S.E.3
  • 207
    • 43449105011 scopus 로고    scopus 로고
    • Dystrophin-deficient cardiomyopathy in mouse: Expression of Nox4 and Lox are associated with fibrosis and altered functional parameters in the heart
    • Spurney, C.F.; Knoblach, S.; Pistilli, E.E.; Nagaraju, K.; Martin, G.R.; Hoffman, E.P. Dystrophin-deficient cardiomyopathy in mouse: expression of Nox4 and Lox are associated with fibrosis and altered functional parameters in the heart. Neuromuscul. Disord., 2008, 18, 371-381.
    • (2008) Neuromuscul. Disord. , vol.18 , pp. 371-381
    • Spurney, C.F.1    Knoblach, S.2    Pistilli, E.E.3    Nagaraju, K.4    Martin, G.R.5    Hoffman, E.P.6
  • 209
    • 84859046698 scopus 로고    scopus 로고
    • Glycoproteomic characterization of recombinant mouse α-dystroglycan. Aberrant glycosylation of the protein has been linked to various forms of congenital muscular dystrophy
    • Harrison, R.; Hitchen, P.G.; Panico, M.; Morris, H.R.; Mekhaiel, D.; Pleass, R.J.; Dell, A.; Hewitt, J.E.; Haslam, S.M. Glycoproteomic characterization of recombinant mouse α-dystroglycan. Aberrant glycosylation of the protein has been linked to various forms of congenital muscular dystrophy. Glycobiology, 2012, 22, 662-675.
    • (2012) Glycobiology , vol.22 , pp. 662-675
    • Harrison, R.1    Hitchen, P.G.2    Panico, M.3    Morris, H.R.4    Mekhaiel, D.5    Pleass, R.J.6    Dell, A.7    Hewitt, J.E.8    Haslam, S.M.9
  • 210
    • 0032529083 scopus 로고    scopus 로고
    • Expression of aquaporin-4 in fast-twitch fibers of mammalian skeletal muscle
    • Frigeri, A.; Nicchia, G.P.; Verbavatz, J.M.; Valenti, G.; Svelto, M. Expression of aquaporin-4 in fast-twitch fibers of mammalian skeletal muscle. J. Clin. Invest., 1998, 102, 695-703.
    • (1998) J. Clin. Invest. , vol.102 , pp. 695-703
    • Frigeri, A.1    Nicchia, G.P.2    Verbavatz, J.M.3    Valenti, G.4    Svelto, M.5
  • 211
    • 0035494421 scopus 로고    scopus 로고
    • In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4
    • Adams, M.E.; Mueller, H.A.; Froehner, S.C. In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4. J. Cell Biol., 2001, 155, 113-122.
    • (2001) J. Cell Biol. , vol.155 , pp. 113-122
    • Adams, M.E.1    Mueller, H.A.2    Froehner, S.C.3
  • 215
    • 79955723731 scopus 로고    scopus 로고
    • Absence of aquaporin-4 in skeletal muscle alters proteins involved in bioenergetic pathways and calcium handling
    • Basco, D.; Nicchia, G.P.; D'Alessandro, A.; Zolla, L.; Svelto, M.; Frigeri, A. Absence of aquaporin-4 in skeletal muscle alters proteins involved in bioenergetic pathways and calcium handling. PLoS One, 2011, 6 (4), e19225.
    • (2011) PLoS One , vol.6 , Issue.4
    • Basco, D.1    Nicchia, G.P.2    D'Alessandro, A.3    Zolla, L.4    Svelto, M.5    Frigeri, A.6
  • 218
    • 77954613481 scopus 로고    scopus 로고
    • Stem cell therapies to treat muscular dystrophy: Progress to date
    • Meregalli, M.; Farini, A.; Parolini, D.; Maciotta, S.; Torrente, Y. Stem cell therapies to treat muscular dystrophy: progress to date. BioDrugs, 2010, 24, 237-247.
    • (2010) BioDrugs , vol.24 , pp. 237-247
    • Meregalli, M.1    Farini, A.2    Parolini, D.3    McIotta, S.4    Torrente, Y.5
  • 219
    • 80052513011 scopus 로고    scopus 로고
    • Restoring dystrophin expression in Duchenne muscular dystrophy muscle progress in exon skipping and stop codon read through
    • Hoffman, E.P.; Bronson, A.; Levin, A.A.; Takeda, S.; Yokota, T.; Baudy, A.R.; Connor, E.M. Restoring dystrophin expression in Duchenne muscular dystrophy muscle progress in exon skipping and stop codon read through. Am. J. Pathol., 2011, 179, 12-22.
    • (2011) Am. J. Pathol. , vol.179 , pp. 12-22
    • Hoffman, E.P.1    Bronson, A.2    Levin, A.A.3    Takeda, S.4    Yokota, T.5    Baudy, A.R.6    Connor, E.M.7
  • 220
    • 84862631856 scopus 로고    scopus 로고
    • Gene replacement therapies for duchenne muscular dystrophy using adeno-associated viral vectors
    • Seto, J.T.; Ramos, J.N.; Muir, L.; Chamberlain, J.S.; Odom, G.L. Gene replacement therapies for duchenne muscular dystrophy using adeno-associated viral vectors. Curr. Gene Ther., 2012, 12, 139-151.
    • (2012) Curr. Gene Ther. , vol.12 , pp. 139-151
    • Seto, J.T.1    Ramos, J.N.2    Muir, L.3    Chamberlain, J.S.4    Odom, G.L.5
  • 221
    • 84866342088 scopus 로고    scopus 로고
    • Gene therapy for Duchenne muscular dystrophy
    • Verhaart, I.E.; Aartsma-Rus, A. Gene therapy for Duchenne muscular dystrophy. Curr. Opin. Neurol., 2012, 25, 588-596.
    • (2012) Curr. Opin. Neurol. , vol.25 , pp. 588-596
    • Verhaart, I.E.1    Aartsma-Rus, A.2
  • 222
    • 77449087318 scopus 로고    scopus 로고
    • Personalised genetic intervention for Duchenne muscular dystrophy: Antisense oligomers and exon skipping
    • Mitrpant, C.; Fletcher, S.; Wilton, S.D. Personalised genetic intervention for Duchenne muscular dystrophy: antisense oligomers and exon skipping. Curr. Mol. Pharmacol., 2009, 2, 110-121.
    • (2009) Curr. Mol. Pharmacol. , vol.2 , pp. 110-121
    • Mitrpant, C.1    Fletcher, S.2    Wilton, S.D.3
  • 223
    • 78650916689 scopus 로고    scopus 로고
    • The status of exon skipping as a therapeutic approach to Duchenne muscular dystrophy
    • Lu, Q.L.; Yokota, T.; Takeda, S.; Garcia, L.; Muntoni, F.; Partridge, T. The status of exon skipping as a therapeutic approach to Duchenne muscular dystrophy. Mol. Ther., 2011, 19, 9-15.
    • (2011) Mol. Ther. , vol.19 , pp. 9-15
    • Lu, Q.L.1    Yokota, T.2    Takeda, S.3    Garcia, L.4    Muntoni, F.5    Partridge, T.6
  • 224
    • 84859867996 scopus 로고    scopus 로고
    • Overview on DMD exon skipping
    • Aartsma-Rus, A. Overview on DMD exon skipping. Methods Mol. Biol., 2012, 867, 97-116.
    • (2012) Methods Mol. Biol. , vol.867 , pp. 97-116
    • Aartsma-Rus, A.1
  • 225
    • 84862625633 scopus 로고    scopus 로고
    • Antisense oligonucleotide-mediated exon skipping for Duchenne muscular dystrophy: Progress and challenges
    • Arechavala-Gomeza, V.; Anthony, K.; Morgan, J.; Muntoni, F. Antisense oligonucleotide-mediated exon skipping for Duchenne muscular dystrophy: progress and challenges. Curr. Gene Ther., 2012, 12, 152-160.
    • (2012) Curr. Gene Ther. , vol.12 , pp. 152-160
    • Arechavala-Gomeza, V.1    Anthony, K.2    Morgan, J.3    Muntoni, F.4
  • 231
    • 84877872340 scopus 로고    scopus 로고
    • Clinical trials using antisense oligonucleotides in duchenne muscular dystrophy
    • Koo, T.; Wood, M.J. Clinical trials using antisense oligonucleotides in duchenne muscular dystrophy. Hum. Gene Ther., 2013, 24, 479-488.
    • (2013) Hum. Gene Ther. , vol.24 , pp. 479-488
    • Koo, T.1    Wood, M.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.