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Volumn 81, Issue 11 SUPPL., 2002, Pages

Molecular pathophysiology of myofiber injury in deficiencies of the dystrophin-glycoprotein complex

Author keywords

Congenital muscular dystrophy; Duchenne muscular dystrophy; Dystroglycans; Dystrophin; Limb girdle muscular dystrophy; Merosin; Sarcoglycans

Indexed keywords

CALCIUM; GENES; MUSCLE; MUTAGENESIS; PHYSIOLOGY; PROTEINS;

EID: 0036839039     PISSN: 08949115     EISSN: None     Source Type: Journal    
DOI: 10.1097/00002060-200211001-00017     Document Type: Conference Paper
Times cited : (89)

References (138)
  • 1
    • 0023614188 scopus 로고
    • Dystrophin: The protein product of the Duchenne muscular dystrophy locus
    • Hoffman EP, Brown RHJ, Kunkel LM: Dystrophin: The protein product of the Duchenne muscular dystrophy locus. Cell 1987;51:919-28
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown, R.H.J.2    Kunkel, L.M.3
  • 2
    • 0027470203 scopus 로고
    • The structural and functional diversity of dystrophin
    • Ahn AH, Kunkel LM: The structural and functional diversity of dystrophin. Nat Genet 1993;3:283-91
    • (1993) Nat Genet , vol.3 , pp. 283-291
    • Ahn, A.H.1    Kunkel, L.M.2
  • 3
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti JM, Campbell KP: Membrane organization of the dystrophin-glycoprotein complex. Cell 1991;66:1121-31
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 4
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM, Campbell KP: A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 1993;122:809-23
    • (1993) J Cell Biol , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 5
    • 0029089582 scopus 로고
    • Dystrophin-associated proteins in muscular dystrophy
    • Ozawa E, Yoshida M, Suzuki A, et al: Dystrophin-associated proteins in muscular dystrophy. Hum Mol Genet 1995;4: 1711-6
    • (1995) Hum Mol Genet , vol.4 , pp. 1711-1716
    • Ozawa, E.1    Yoshida, M.2    Suzuki, A.3
  • 6
    • 0028877455 scopus 로고
    • Muscular dystrophies: Diseases of the dystrophin-glycoprotein complex
    • Worton R: Muscular dystrophies: Diseases of the dystrophin-glycoprotein complex. Science 1995;270:755-6
    • (1995) Science , vol.270 , pp. 755-756
    • Worton, R.1
  • 7
    • 0027980295 scopus 로고
    • Increasing complexity of the dystrophin-associated protein complex
    • Tinsley JM, Blake DJ, Zuellig RA, et al: Increasing complexity of the dystrophin-associated protein complex. Proc Natl Acad Sci USA 1994;91:8307-3
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8307-8303
    • Tinsley, J.M.1    Blake, D.J.2    Zuellig, R.A.3
  • 8
    • 0033814140 scopus 로고    scopus 로고
    • Molecular basis of muscular dystrophies
    • Cohn RD, Campbell KP: Molecular basis of muscular dystrophies. Muscle Nerve 2000;23:1456-71
    • (2000) Muscle Nerve , vol.23 , pp. 1456-1471
    • Cohn, R.D.1    Campbell, K.P.2
  • 9
    • 0023904860 scopus 로고
    • The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein
    • Koenig M, Monaco AP, Kunkel LM: The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 1988;53:219-26
    • (1988) Cell , vol.53 , pp. 219-226
    • Koenig, M.1    Monaco, A.P.2    Kunkel, L.M.3
  • 10
    • 0029804981 scopus 로고    scopus 로고
    • A new model for the interaction of dystrophin with F-actin
    • Rybakova IN, Amann KJ, Ervasti JM: A new model for the interaction of dystrophin with F-actin. J Cell Biol 1996; 135:661-72
    • (1996) J Cell Biol , vol.135 , pp. 661-672
    • Rybakova, I.N.1    Amann, K.J.2    Ervasti, J.M.3
  • 11
    • 17344382194 scopus 로고    scopus 로고
    • Biochemical evidence for association of dystrobrevin with the sarcoglycan-sarcospan complex as a basis for understanding sarcoglycanopathy
    • Yoshida M, Hama H, Ishikawa-Sakurai M, et al: Biochemical evidence for association of dystrobrevin with the sarcoglycan-sarcospan complex as a basis for understanding sarcoglycanopathy. Hum Mol Genet 2000;9:1033-40
    • (2000) Hum Mol Genet , vol.9 , pp. 1033-1040
    • Yoshida, M.1    Hama, H.2    Ishikawa-Sakurai, M.3
  • 12
    • 0030775377 scopus 로고    scopus 로고
    • Dystrobrevin and dystrophin: An interaction through coiled-coil motifs
    • Sadoulet-Puccio HM, Rajala M, Kunkel LM: Dystrobrevin and dystrophin: An interaction through coiled-coil motifs. Proc Natl Acad Sci U S A 1997;94:12413-8
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 12413-12418
    • Sadoulet-Puccio, H.M.1    Rajala, M.2    Kunkel, L.M.3
  • 13
    • 0029881574 scopus 로고    scopus 로고
    • Isoform diversity of dystrobrevin, the murine 87-kDa postsynaptic protein
    • Blake DJ, Nawrotzki R, Peters MF, et al: Isoform diversity of dystrobrevin, the murine 87-kDa postsynaptic protein. J Biol Chem 1996;271:7802-10
    • (1996) J Biol Chem , vol.271 , pp. 7802-7810
    • Blake, D.J.1    Nawrotzki, R.2    Peters, M.F.3
  • 14
    • 0028928013 scopus 로고
    • Alternate binding of actin and calmodulin to multiple sites on dystrophin
    • Jarrett HW, Foster JL: Alternate binding of actin and calmodulin to multiple sites on dystrophin. J Biol Chem 1995;270:5578-86
    • (1995) J Biol Chem , vol.270 , pp. 5578-5586
    • Jarrett, H.W.1    Foster, J.L.2
  • 15
    • 0029013870 scopus 로고
    • SH3 domain-mediated interaction of dystroglycan and Grb2
    • Yang B, Jung D, Motto D, et al: SH3 domain-mediated interaction of dystroglycan and Grb2. J Biol Chem 1995;270: 11711-4
    • (1995) J Biol Chem , vol.270 , pp. 11711-11714
    • Yang, B.1    Jung, D.2    Motto, D.3
  • 16
    • 0033617341 scopus 로고    scopus 로고
    • Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin: A mechanism for specific substrate recognition
    • Hasegawa M, Cuenda A, Spillantini MG, et al: Stress-activated protein kinase-3 interacts with the PDZ domain of alpha1-syntrophin: A mechanism for specific substrate recognition. J Biol Chem 1999;274:12626-31
    • (1999) J Biol Chem , vol.274 , pp. 12626-12631
    • Hasegawa, M.1    Cuenda, A.2    Spillantini, M.G.3
  • 17
    • 0029149471 scopus 로고
    • Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy
    • Brennan JE, Chao DS, Xia H, et al: Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell 1995;85:743-52
    • (1995) Cell , vol.85 , pp. 743-752
    • Brennan, J.E.1    Chao, D.S.2    Xia, H.3
  • 18
    • 0033758449 scopus 로고    scopus 로고
    • Animal models for muscular dystrophy: Valuable tools for the development of therapies
    • Allamand V, Campbell KP: Animal models for muscular dystrophy: Valuable tools for the development of therapies. Hum Mol Genet 2000;9:2459-67
    • (2000) Hum Mol Genet , vol.9 , pp. 2459-2467
    • Allamand, V.1    Campbell, K.P.2
  • 19
    • 0033175570 scopus 로고    scopus 로고
    • Role for alpha-dystrobrevin in the pathogenesis of dystrophin-dependent muscular dystrophies
    • Grady RM, Grange RW, Lau KS, et al: Role for alpha-dystrobrevin in the pathogenesis of dystrophin-dependent muscular dystrophies. Nat Cell Biol 1999;1:215-20
    • (1999) Nat Cell Biol , vol.1 , pp. 215-220
    • Grady, R.M.1    Grange, R.W.2    Lau, K.S.3
  • 20
    • 0033982722 scopus 로고    scopus 로고
    • Sarcospan-deficient mice maintain normal muscle function
    • Lebakken CS, Venzke DP, Hrstka RF, et al: Sarcospan-deficient mice maintain normal muscle function. Mol Cell Biol 2000;20:1669-77
    • (2000) Mol Cell Biol , vol.20 , pp. 1669-1677
    • Lebakken, C.S.1    Venzke, D.P.2    Hrstka, R.F.3
  • 21
    • 0033593119 scopus 로고    scopus 로고
    • α1-Syntrophin gene disruption results in the absence of neuronal-type nitric oxide synthase at the sarcolemma but does not induce muscle degeneration
    • Kameya S, Miyagoe Y, Nonaka I, et al: α1-Syntrophin gene disruption results in the absence of neuronal-type nitric oxide synthase at the sarcolemma but does not induce muscle degeneration. J Biol Chem 1999;274:2193-200
    • (1999) J Biol Chem , vol.274 , pp. 2193-2200
    • Kameya, S.1    Miyagoe, Y.2    Nonaka, I.3
  • 22
    • 0034683669 scopus 로고    scopus 로고
    • Absence of α-syntrophin leads to structurally aberrant neuromuscular synapses deficient in utrophin
    • Adams ME, Kramarcy N, Krall SP, et al: Absence of α-syntrophin leads to structurally aberrant neuromuscular synapses deficient in utrophin. J Cell Biol 2000;150:1385-97
    • (2000) J Cell Biol , vol.150 , pp. 1385-1397
    • Adams, M.E.1    Kramarcy, N.2    Krall, S.P.3
  • 23
    • 0030610576 scopus 로고    scopus 로고
    • Integrins (alpha7beta1) in muscle function and survival: Disrupted expression in merosin-deficient congenital muscular dystrophy
    • Vachon PH, Xu H, Liu L, et al: Integrins (alpha7beta1) in muscle function and survival: Disrupted expression in merosin-deficient congenital muscular dystrophy. J Clin Invest 1997;100:1870-81
    • (1997) J Clin Invest , vol.100 , pp. 1870-1881
    • Vachon, P.H.1    Xu, H.2    Liu, L.3
  • 24
    • 0023726325 scopus 로고
    • Decreased membrane mechanical stability and in vivo loss of surface area reflect spectrin deficiencies in hereditary spherocytosis
    • Chasis JA, Agre P, Mohandas N: Decreased membrane mechanical stability and in vivo loss of surface area reflect spectrin deficiencies in hereditary spherocytosis. J Clin Invest 1988;82:617-23
    • (1988) J Clin Invest , vol.82 , pp. 617-623
    • Chasis, J.A.1    Agre, P.2    Mohandas, N.3
  • 25
    • 0023915893 scopus 로고
    • Reductions of erythrocyte membrane viscoelastic coefficients reflect spectrin deficiencies in hereditary spherocytosis
    • Waugh RE, Agre P: Reductions of erythrocyte membrane viscoelastic coefficients reflect spectrin deficiencies in hereditary spherocytosis. J Clin Invest 1988;81:133-41
    • (1988) J Clin Invest , vol.81 , pp. 133-141
    • Waugh, R.E.1    Agre, P.2
  • 26
    • 0026711133 scopus 로고
    • Dystrophin colocalizes with beta-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle
    • Porter GA, Dmytrenko GM, Winkelmann JC, et al: Dystrophin colocalizes with beta-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle. J Cell Biol 1992;117:997-1005
    • (1992) J Cell Biol , vol.117 , pp. 997-1005
    • Porter, G.A.1    Dmytrenko, G.M.2    Winkelmann, J.C.3
  • 27
    • 0026666069 scopus 로고
    • Confocal laser microscopy of dystrophin localization in guinea pig skeletal muscle fibers
    • Masuda T, Fujimaki N, Ozawa E, et al: Confocal laser microscopy of dystrophin localization in guinea pig skeletal muscle fibers. J Cell Biol 1992;119:543-8
    • (1992) J Cell Biol , vol.119 , pp. 543-548
    • Masuda, T.1    Fujimaki, N.2    Ozawa, E.3
  • 28
    • 0019842058 scopus 로고
    • Transerve sarcomere filamentous systems: "Z- and Mcables."
    • Pierobon-Bormioli S: Transerve sarcomere filamentous systems: "Z- and Mcables." J Muscle Res Cell Motil 1981;2:401-13
    • (1981) J Muscle Res Cell Motil , vol.2 , pp. 401-413
    • Pierobon-Bormioli, S.1
  • 29
    • 0020698866 scopus 로고
    • Lateral transmission of tension in frog myofibers: A myofibrillar network and transverse cytoskeletal connections are possible transmitters
    • Street SF: Lateral transmission of tension in frog myofibers: A myofibrillar network and transverse cytoskeletal connections are possible transmitters. J Cell Physiol 1983;114:346-64
    • (1983) J Cell Physiol , vol.114 , pp. 346-364
    • Street, S.F.1
  • 30
    • 0021821147 scopus 로고
    • Vinculin in subsarcolemmal densities in chicken skeletal muscle: Localization and relationship to intracellular and extracellular structures
    • Shear CR, Bloch RJ: Vinculin in subsarcolemmal densities in chicken skeletal muscle: Localization and relationship to intracellular and extracellular structures. J Cell Biol 1985;101:240-56
    • (1985) J Cell Biol , vol.101 , pp. 240-256
    • Shear, C.R.1    Bloch, R.J.2
  • 31
    • 0010935732 scopus 로고
    • A vinculin-containing cortical lattice in skeletal muscle: Traverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma
    • Pardo JV, Siliciano JD, Craig SW: A vinculin-containing cortical lattice in skeletal muscle: Traverse lattice elements ("costameres") mark sites of attachment between myofibrils and sarcolemma. Proc Natl Acad Sci USA 1983;80:1008-12
    • (1983) Proc Natl Acad Sci USA , vol.80 , pp. 1008-1012
    • Pardo, J.V.1    Siliciano, J.D.2    Craig, S.W.3
  • 32
  • 33
    • 0034605070 scopus 로고    scopus 로고
    • The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin
    • Rybakova IN, Patel JR, Ervasti JM: The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J Cell Biol 2000;150:1209-14
    • (2000) J Cell Biol , vol.150 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 34
    • 0025368276 scopus 로고
    • Immunocytochemical study of dystrophin at the myotendinous junction
    • Samitt CE, Bonilla E: Immunocytochemical study of dystrophin at the myotendinous junction. Muscle Nerve 1990;13:493-500
    • (1990) Muscle Nerve , vol.13 , pp. 493-500
    • Samitt, C.E.1    Bonilla, E.2
  • 35
    • 0025974067 scopus 로고
    • Dystrophin is required for normal thin filament-membrane associations at myotendinous junctions
    • Tidball JG, Law DJ: Dystrophin is required for normal thin filament-membrane associations at myotendinous junctions. Am J Pathol 1991;138:17-21
    • (1991) Am J Pathol , vol.138 , pp. 17-21
    • Tidball, J.G.1    Law, D.J.2
  • 36
    • 0028929061 scopus 로고
    • Mechanical function of dystrophin in muscle cells
    • Pasternak C, Wong S, Elson EL: Mechanical function of dystrophin in muscle cells. J Cell Biol 1995;128:355-61
    • (1995) J Cell Biol , vol.128 , pp. 355-361
    • Pasternak, C.1    Wong, S.2    Elson, E.L.3
  • 37
    • 0026032731 scopus 로고
    • Decreased osmotic stability of dystrophin-less muscle cells from the mdx mouse
    • Menke A, Jockusch H: Decreased osmotic stability of dystrophin-less muscle cells from the mdx mouse. Nature 1991;349:69-71
    • (1991) Nature , vol.349 , pp. 69-71
    • Menke, A.1    Jockusch, H.2
  • 38
    • 0027460658 scopus 로고
    • Dystrophin protects the sarcolemma from stresses developed during muscle contraction
    • Petrof BJ, Shrager JB, Stedman HH, et al: Dystrophin protects the sarcolemma from stresses developed during muscle contraction. Proc Natl Acad Sci USA 1993;90:3710-4
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3710-3714
    • Petrof, B.J.1    Shrager, J.B.2    Stedman, H.H.3
  • 39
    • 0027248618 scopus 로고
    • Increased susceptibility of EDL muscles from mdx mice to damage induced by contractions with stretch
    • Moens P, Baatsen PH, Marechal G: Increased susceptibility of EDL muscles from mdx mice to damage induced by contractions with stretch. J Muscle Res Cell Motil 1993;14:446-51
    • (1993) J Muscle Res Cell Motil , vol.14 , pp. 446-451
    • Moens, P.1    Baatsen, P.H.2    Marechal, G.3
  • 40
    • 0033885496 scopus 로고    scopus 로고
    • Differential requirements for individual sarcoglycans and dystrophin in the assembly and function of the dystrophinglycoprotein complex
    • Hack AA, Lam MYJ, Cordier L, et al: Differential requirements for individual sarcoglycans and dystrophin in the assembly and function of the dystrophinglycoprotein complex. J Cell Sci 2000;113:2535-44
    • (2000) J Cell Sci , vol.113 , pp. 2535-2544
    • Hack, A.A.1    Lam, M.Y.J.2    Cordier, L.3
  • 41
    • 0032907636 scopus 로고    scopus 로고
    • Stable restoration of the sarcoglycan complex in dystrophic muscle perfused with histamine and a recombinant adenoassociated viral vector
    • Greelish JP, Su CH, Lankford EB, et al: Stable restoration of the sarcoglycan complex in dystrophic muscle perfused with histamine and a recombinant adenoassociated viral vector. Nat Med 1999;5:439-43
    • (1999) Nat Med , vol.5 , pp. 439-443
    • Greelish, J.P.1    Su, C.H.2    Lankford, E.B.3
  • 42
    • 0032849111 scopus 로고    scopus 로고
    • Muscle degeneration without mechanical injury in sarcoglycan deficiency
    • Hack AA, Cordier L, Shoturma DI, et al: Muscle degeneration without mechanical injury in sarcoglycan deficiency. Proc Natl Acad Sci USA 1999;96:10723-8
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 10723-10728
    • Hack, A.A.1    Cordier, L.2    Shoturma, D.I.3
  • 43
    • 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
  • 44
    • 0027430098 scopus 로고
    • Loss of cytoplasmic basic fibroblast growth factor from physiologically wounded myofibers of normal and dystrophic muscle
    • Clarke MFC, Khakee R, McNeil PL: Loss of cytoplasmic basic fibroblast growth factor from physiologically wounded myofibers of normal and dystrophic muscle. J Cell Sci 1993;106:121-33
    • (1993) J Cell Sci , vol.106 , pp. 121-133
    • Clarke, M.F.C.1    Khakee, R.2    McNeil, P.L.3
  • 45
    • 0031924679 scopus 로고    scopus 로고
    • Evidence of mdx mouse skeletal muscle fragility in vivo by eccentric running exercise
    • Vilquin JT, Brussee V, Asselin I, et al: Evidence of mdx mouse skeletal muscle fragility in vivo by eccentric running exercise. Muscle Nerve 1998;21:567-76
    • (1998) Muscle Nerve , vol.21 , pp. 567-576
    • Vilquin, J.T.1    Brussee, V.2    Asselin, I.3
  • 46
    • 0031442922 scopus 로고    scopus 로고
    • Muscle fibers of mdx mice are more vulnerable to exercise than those of normal mice
    • Brussee V, Tardif F, Tremblay JP: Muscle fibers of mdx mice are more vulnerable to exercise than those of normal mice. Neuromuscul Disord 1997;7:487-92
    • (1997) Neuromuscul Disord , vol.7 , pp. 487-492
    • Brussee, V.1    Tardif, F.2    Tremblay, J.P.3
  • 47
    • 0025955393 scopus 로고
    • Canine X-linked muscular dystrophy studied with in vivo phosphorus magnetic resonance spectroscopy
    • McCully K, Giger U, Argov Z, et al: Canine X-linked muscular dystrophy studied with in vivo phosphorus magnetic resonance spectroscopy. Muscle Nerve 1991;14:1091-8
    • (1991) Muscle Nerve , vol.14 , pp. 1091-1098
    • McCully, K.1    Giger, U.2    Argov, Z.3
  • 48
    • 0026546263 scopus 로고
    • Contractile properties and susceptibility to exercise-induced damage of normal and mdx mouse tibialis anterior muscle
    • Sacco P, Jones DA, Dick JR, et al: Contractile properties and susceptibility to exercise-induced damage of normal and mdx mouse tibialis anterior muscle. Clin Sci 1992;82:227-36
    • (1992) Clin Sci , vol.82 , pp. 227-236
    • Sacco, P.1    Jones, D.A.2    Dick, J.R.3
  • 49
    • 0026419948 scopus 로고
    • The mdx mouse diaphragm reproduces the degenerative changes of Duchenne muscular dystrophy
    • Stedman HH, Sweeney HL, Shrager JB, et al: The mdx mouse diaphragm reproduces the degenerative changes of Duchenne muscular dystrophy. Nature 1991;352:536-9
    • (1991) Nature , vol.352 , pp. 536-539
    • Stedman, H.H.1    Sweeney, H.L.2    Shrager, J.B.3
  • 50
    • 0001855704 scopus 로고
    • The mdx mouse and mdx diaphragm: Implications for the pathogenesis of Duchenne muscular dystrophy
    • Kelly AM, Blau HM (eds): New York, Raven Press
    • Shrager JB, Stedman HH, Sweeney HL, et al: The mdx mouse and mdx diaphragm: Implications for the pathogenesis of Duchenne muscular dystrophy, in Kelly AM, Blau HM (eds): Neuromuscular Development and Disease. New York, Raven Press, 1992, pp 317-28
    • (1992) Neuromuscular Development and Disease , pp. 317-328
    • Shrager, J.B.1    Stedman, H.H.2    Sweeney, H.L.3
  • 51
  • 52
    • 8044224015 scopus 로고    scopus 로고
    • Myocardial involvement is very frequent among patients affected with subclinical Becker's muscular dystrophy
    • Melacini P, Fanin M, Danieli GA, et al: Myocardial involvement is very frequent among patients affected with subclinical Becker's muscular dystrophy. Circulation 1996;94:3168-75
    • (1996) Circulation , vol.94 , pp. 3168-3175
    • Melacini, P.1    Fanin, M.2    Danieli, G.A.3
  • 53
    • 0027502493 scopus 로고
    • The cardiomyopathy of Duchenne's muscular dystrophy and the function of dystrophin
    • Cziner DG, Levin RI: The cardiomyopathy of Duchenne's muscular dystrophy and the function of dystrophin. Med Hypotheses 1993;40:169-73
    • (1993) Med Hypotheses , vol.40 , pp. 169-173
    • Cziner, D.G.1    Levin, R.I.2
  • 54
    • 0030848338 scopus 로고    scopus 로고
    • Skeletal and cardiac myopathies in mice lacking utrophin and dystrophin: A model for Duchenne muscular dystrophy
    • Grady RM, Teng H, Nichol MC, et al: Skeletal and cardiac myopathies in mice lacking utrophin and dystrophin: A model for Duchenne muscular dystrophy. Cell 1997;90:729-38
    • (1997) Cell , vol.90 , pp. 729-738
    • Grady, R.M.1    Teng, H.2    Nichol, M.C.3
  • 55
    • 0022625394 scopus 로고
    • The association of cardiac muscle necrosis and inflammation with the degenerative and persistent myopathy of mdx mice
    • Bridges LR: The association of cardiac muscle necrosis and -inflammation with the degenerative and persistent myopathy of mdx mice. J Neurol Sci 1986;72:147-57
    • (1986) J Neurol Sci , vol.72 , pp. 147-157
    • Bridges, L.R.1
  • 56
    • 0023091942 scopus 로고
    • The mutant mdx: Inherited myopathy in the mouse. Morphological studies of nerves, muscles and end-plates
    • Torres LFB, Duchen LW: The mutant mdx: Inherited myopathy in the mouse. Morphological studies of nerves, muscles and end-plates. Brain 1987;110:269-99
    • (1987) Brain , vol.110 , pp. 269-299
    • Torres, L.F.B.1    Duchen, L.W.2
  • 57
    • 0028069326 scopus 로고
    • The effects of hyperthyroidism on muscular dystrophy in the mdx mouse: Greater dystrophy in cardiac and soleus muscle
    • Anderson JE, Kardami E: The effects of hyperthyroidism on muscular dystrophy in the mdx mouse: Greater dystrophy in cardiac and soleus muscle. Muscle Nerve 1994;17:64-73
    • (1994) Muscle Nerve , vol.17 , pp. 64-73
    • Anderson, J.E.1    Kardami, E.2
  • 58
    • 0033524407 scopus 로고    scopus 로고
    • Severe cardiomyopathy in mice lacking dystrophin and MyoD
    • Megeney LA, Kablar B, Perry RLS, et al: Severe cardiomyopathy in mice lacking dystrophin and MyoD. Proc Natl Acad Sci USA 1999;96:220-5
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 220-225
    • Megeney, L.A.1    Kablar, B.2    Perry, R.L.S.3
  • 59
    • 0035403114 scopus 로고    scopus 로고
    • Dystrophin-deficient cardiomyocytes are abnormally vulnerable to mechanical stress-induced contractile failure and injury
    • Danialou G, Comtois AS, Dudley R, et al: Dystrophin-deficient cardiomyocytes are abnormally vulnerable to mechanical stress-induced contractile failure and injury. FASEB J 2001;15:1655-7
    • (2001) FASEB J , vol.15 , pp. 1655-1657
    • Danialou, G.1    Comtois, A.S.2    Dudley, R.3
  • 60
    • 0017797971 scopus 로고
    • Intracellular calcium accumulation in Duchenne dystrophy and other myopathies: A study of 567,000 muscle fibers in 114 biopsies
    • Bodensteiner JB, Engel AB: Intracellular calcium accumulation in Duchenne dystrophy and other myopathies: A study of 567,000 muscle fibers in 114 biopsies. Neurology 1978;28:439-46
    • (1978) Neurology , vol.28 , pp. 439-446
    • Bodensteiner, J.B.1    Engel, A.B.2
  • 61
    • 0021695155 scopus 로고
    • 2+ metabolism in Duchenne muscular dystrophy: Effects on cellular and viral growth
    • 2+ metabolism in Duchenne muscular dystrophy: Effects on cellular and viral growth. Proc Natl Acad Sci USA 1984;81:7617-21
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 7617-7621
    • Fingerman, E.1    Campisi, J.2    Pardee, A.B.3
  • 62
    • 0023830725 scopus 로고
    • ++ at rest and after cholinergic stimulus is increased in cultured muscle cells from Duchenne muscular dystrophy patients
    • ++ at rest and after cholinergic stimulus is increased in cultured muscle cells from Duchenne muscular dystrophy patients. Neurology 1988;38:476-80
    • (1988) Neurology , vol.38 , pp. 476-480
    • Mongini, T.1    Ghigo, D.2    Doriguzzi, C.3
  • 63
    • 0023739851 scopus 로고
    • Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice
    • Turner PR, Westwood T, Regen CM, et al: Increased protein degradation results from elevated free calcium levels found in muscle from mdx mice. Nature 1988;335:735-8
    • (1988) Nature , vol.335 , pp. 735-738
    • Turner, P.R.1    Westwood, T.2    Regen, C.M.3
  • 64
    • 0027234619 scopus 로고
    • Critical evaluation of cytosolic calcium determination in resting muscle fibres from normal and dystrophic (mdx) mice
    • Gailly P, Boland B, Himpens B, et al: Critical evaluation of cytosolic calcium determination in resting muscle fibres from normal and dystrophic (mdx) mice. Cell Calcium 1993;14:473-83
    • (1993) Cell Calcium , vol.14 , pp. 473-483
    • Gailly, P.1    Boland, B.2    Himpens, B.3
  • 65
    • 0027185603 scopus 로고
    • Membrane potential, resting calcium and calcium transients in isolated muscle fibres from normal and dystrophic mice
    • Head SI: Membrane potential, resting calcium and calcium transients in isolated muscle fibres from normal and dystrophic mice. J Physiol 1993;469:11-9
    • (1993) J Physiol , vol.469 , pp. 11-19
    • Head, S.I.1
  • 66
    • 0028414945 scopus 로고
    • 2+ concentrations are not elevated in resting cultured muscle from Duchenne (DMD) patients and in mdx mouse muscle fibres
    • 2+ concentrations are not elevated in resting cultured muscle from Duchenne (DMD) patients and in mdx mouse muscle fibres. Pflugers Arch 1994;426:499-505
    • (1994) Pflugers Arch , vol.426 , pp. 499-505
    • Pressmar, J.1    Brinkmeier, H.2    Seewald, M.J.3
  • 67
    • 0027183617 scopus 로고
    • Changes in cytosolic resting ionized calcium level and in calcium transients during in vitro development of normal and Duchenne muscular dystrophy cultured skeletal muscle measured by laser cytofluorimetry using indo-1
    • Rivet-Bastide M, Imbert N, Cognard C, et al: Changes in cytosolic resting ionized calcium level and in calcium transients during in vitro development of normal and Duchenne muscular dystrophy cultured skeletal muscle measured by laser cytofluorimetry using indo-1. Cell Calcium 1993;14:563-71
    • (1993) Cell Calcium , vol.14 , pp. 563-571
    • Rivet-Bastide, M.1    Imbert, N.2    Cognard, C.3
  • 68
    • 0029964897 scopus 로고    scopus 로고
    • A critical evaluation of resting intracellular free calcium regulation in dystrophic mdx muscle
    • Hopf FW, Turner PRD Jr, Reddy P, et al: A critical evaluation of resting intracellular free calcium regulation in dystrophic mdx muscle. Am J Physiol 1996;271:1325-39
    • (1996) Am J Physiol , vol.271 , pp. 1325-1339
    • Hopf, F.W.1    Turner P.R.D., Jr.2    Reddy, P.3
  • 70
    • 0034468908 scopus 로고    scopus 로고
    • How calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes
    • Alderton JM, Steinhardt RA: How calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes. Trends Cardiovasc Med 2000;10:268-72
    • (2000) Trends Cardiovasc Med , vol.10 , pp. 268-272
    • Alderton, J.M.1    Steinhardt, R.A.2
  • 71
    • 0025222219 scopus 로고
    • Increased activity of calcium leak channels in myotubes of Duchenne human and mdx mouse origin
    • Fong P, Turner PR, Denetclaw WF, et al: Increased activity of calcium leak channels in myotubes of Duchenne human and mdx mouse origin. Science 1990;250:673-766
    • (1990) Science , vol.250 , pp. 673-766
    • Fong, P.1    Turner, P.R.2    Denetclaw, W.F.3
  • 72
    • 0025317892 scopus 로고
    • Calcium entry through stretch-inactivated ion channels in mdx myotubes
    • Franco A Jr, Lansman JB: Calcium entry through stretch-inactivated ion channels in mdx myotubes. Nature 1990;344:670-3
    • (1990) Nature , vol.344 , pp. 670-673
    • Franco A., Jr.1    Lansman, J.B.2
  • 73
    • 0026347187 scopus 로고
    • Increased calcium influx in dystrophic muscle
    • Turner PR, Fong P, Denetclaw WF, et al: Increased calcium influx in dystrophic muscle. J Cell Biol 1991;115:1701-12
    • (1991) J Cell Biol , vol.115 , pp. 1701-1712
    • Turner, P.R.1    Fong, P.2    Denetclaw, W.F.3
  • 74
    • 0028564748 scopus 로고
    • Mechanosensitive ion channels in skeletal muscle from normal and dystrophic mice
    • Franco-Obregon A Jr, Lansman JB: Mechanosensitive ion channels in skeletal muscle from normal and dystrophic mice. J Physiol 1994;481:299-309
    • (1994) J Physiol , vol.481 , pp. 299-309
    • Franco-Obregon A., Jr.1    Lansman, J.B.2
  • 75
    • 0034737602 scopus 로고    scopus 로고
    • Calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes
    • Alderton JM, Steinhardt RA: Calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes. J Biol Chem 2000;275:9452-60
    • (2000) J Biol Chem , vol.275 , pp. 9452-9460
    • Alderton, J.M.1    Steinhardt, R.A.2
  • 76
    • 0033863129 scopus 로고    scopus 로고
    • Increased activity of calcium leak channels caused by proteolysis near sarcolemmal ruptures
    • McCarter GC, Steinhardt RA: Increased activity of calcium leak channels caused by proteolysis near sarcolemmal ruptures. J Membr Biol 2000;176:169-74
    • (2000) J Membr Biol , vol.176 , pp. 169-174
    • McCarter, G.C.1    Steinhardt, R.A.2
  • 77
    • 0031974345 scopus 로고    scopus 로고
    • Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins
    • Gee SH, Madhavan R, Levinson SR, et al: Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins. J Neurosci 1998;18:128-37
    • (1998) J Neurosci , vol.18 , pp. 128-137
    • Gee, S.H.1    Madhavan, R.2    Levinson, S.R.3
  • 78
    • 0031985105 scopus 로고    scopus 로고
    • Specific interactions between the syntrophin PDZ domain and voltage-gated sodium channels
    • Schultz J, Hoffmuller U, Krause G, et al: Specific interactions between the syntrophin PDZ domain and voltage-gated sodium channels. Nat Struct Biol 1998;5:19-24
    • (1998) Nat Struct Biol , vol.5 , pp. 19-24
    • Schultz, J.1    Hoffmuller, U.2    Krause, G.3
  • 80
    • 0031939073 scopus 로고    scopus 로고
    • Bidirectional signaling between sarcoglycans and the integrin adhesion system in cultured L6 myocytes
    • Yoshida T, Pan Y, Hanada H, et al: Bidirectional signaling between sarcoglycans and the integrin adhesion system in cultured L6 myocytes. J Biol Chem 1998;273:1583-90
    • (1998) J Biol Chem , vol.273 , pp. 1583-1590
    • Yoshida, T.1    Pan, Y.2    Hanada, H.3
  • 81
    • 0027621320 scopus 로고
    • Dystrophin as a mechanochemical transducer in skeletal muscle
    • Brown SC, Lucy JA: Dystrophin as a mechanochemical transducer in skeletal muscle. Bioessays 1993;15:413-9
    • (1993) Bioessays , vol.15 , pp. 413-419
    • Brown, S.C.1    Lucy, J.A.2
  • 82
    • 0029664392 scopus 로고    scopus 로고
    • 2+-calmodulin binds to the carboxyl-terminal domain of dystrophin
    • 2+-calmodulin binds to the carboxyl-terminal domain of dystrophin. J Biol Chem 1996;271:6605-10
    • (1996) J Biol Chem , vol.271 , pp. 6605-6610
    • Anderson, J.T.1    Rogers, R.P.2    Jarrett, H.W.3
  • 83
    • 0028845076 scopus 로고
    • Phosphorylation of the carboxyl terminal region of dystrophin by mitogen-activated protein (MAP) kinase
    • Shemanko CS, Sanghera JS, Milner RE, et al: Phosphorylation of the carboxyl terminal region of dystrophin by mitogen-activated protein (MAP) kinase. Mol Cell Biochem 1995;152:63-70
    • (1995) Mol Cell Biochem , vol.152 , pp. 63-70
    • Shemanko, C.S.1    Sanghera, J.S.2    Milner, R.E.3
  • 84
    • 0028283972 scopus 로고
    • Calmodulin-activated phosphorylation of dystrophin
    • Madhavan R, Jarrett HW: Calmodulin-activated phosphorylation of dystrophin. Biochemistry 1994;33:5797-804
    • (1994) Biochemistry , vol.33 , pp. 5797-5804
    • Madhavan, R.1    Jarrett, H.W.2
  • 85
    • 0030338182 scopus 로고    scopus 로고
    • Phosphorylation of the carboxyl-terminal region of dystrophin
    • Michalak M, Fu SY, Milner RE, et al: Phosphorylation of the carboxyl-terminal region of dystrophin. Biochem Cell Biol 1996;74:431-7
    • (1996) Biochem Cell Biol , vol.74 , pp. 431-437
    • Michalak, M.1    Fu, S.Y.2    Milner, R.E.3
  • 87
    • 0028814451 scopus 로고
    • Phosphorylation of dystrophin: Effects on actin binding
    • Senter L, Ceoldo S, Petrusa MM, et al: Phosphorylation of dystrophin: Effects on actin binding. Biochem Biophys Res Com 1995;206:57-63
    • (1995) Biochem Biophys Res Com , vol.206 , pp. 57-63
    • Senter, L.1    Ceoldo, S.2    Petrusa, M.M.3
  • 88
    • 0029000179 scopus 로고
    • Characterization of the recombinant C-terminal domain of dystrophin: Phosphorylation by calmodulin-dependent protein kinase II and dephosphorylation by type 2B protein phosphatase
    • Walsh MP, Busaan JL, Fraser ED, et al: Characterization of the recombinant C-terminal domain of dystrophin: Phosphorylation by calmodulin-dependent protein kinase II and dephosphorylation by type 2B protein phosphatase. Biochemistry 1995;34:5561-8
    • (1995) Biochemistry , vol.34 , pp. 5561-5568
    • Walsh, M.P.1    Busaan, J.L.2    Fraser, E.D.3
  • 89
    • 0032548498 scopus 로고    scopus 로고
    • Alphal-syntrophin has distinct binding sites for actin and calmodulin
    • Iwata Y, Pan Y, Yoshida T, et al: Alphal-syntrophin has distinct binding sites for actin and calmodulin. FEBS Lett 1998;423:173-7
    • (1998) FEBS Lett , vol.423 , pp. 173-177
    • Iwata, Y.1    Pan, Y.2    Yoshida, T.3
  • 92
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and αa1-syntrophin mediated by PDZ domains
    • Brenman JE, Chao DS, Gee SH, et al: Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and αa1-syntrophin mediated by PDZ domains. Cell 1996;84:757-67
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3
  • 93
    • 8044254229 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase and dystrophin-deficient muscular dystrophy
    • Chang WJ, Iannaccone ST, Lau KS, et al: Neuronal nitric oxide synthase and dystrophin-deficient muscular dystrophy. Proc Natl Acad Sci USA 1996;93:9142-7
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9142-9147
    • Chang, W.J.1    Iannaccone, S.T.2    Lau, K.S.3
  • 94
    • 0031755357 scopus 로고    scopus 로고
    • Muscular dystrophy in mdx mice despite lack of neuronal nitric oxide synthase
    • Chao DS, Silvagno F, Bredt DS: Muscular dystrophy in mdx mice despite lack of neuronal nitric oxide synthase. J Neurochem 1998;71:784-9
    • (1998) J Neurochem , vol.71 , pp. 784-789
    • Chao, D.S.1    Silvagno, F.2    Bredt, D.S.3
  • 95
    • 0031898432 scopus 로고    scopus 로고
    • mdx Muscle pathology is independent of nNOS perturbation
    • Crosbie RH, Straub V, Yun H-Y, et al: mdx Muscle pathology is independent of nNOS perturbation. Hum Mol Genet 1998;7:823-9
    • (1998) Hum Mol Genet , vol.7 , pp. 823-829
    • Crosbie, R.H.1    Straub, V.2    Yun, H.-Y.3
  • 96
    • 0032411144 scopus 로고    scopus 로고
    • Impaired metabolic modulation of α-adrenergic vasoconstriction in dystrophindeficient skeletal muscle
    • Thomas GD, Sander M, Lau KS, et al: Impaired metabolic modulation of α-adrenergic vasoconstriction in dystrophindeficient skeletal muscle. Proc Natl Acad Sci USA 1998;95:15090-5
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15090-15095
    • Thomas, G.D.1    Sander, M.2    Lau, K.S.3
  • 97
    • 0030927063 scopus 로고    scopus 로고
    • Dystroglycan is essential for early embryonic development: Disruption of Reichert's membrane in Dag1-null mice
    • Williamson RA, Henry MD, Daniels KJ, et al: Dystroglycan is essential for early embryonic development: Disruption of Reichert's membrane in Dag1-null mice. Hum Mol Genet 1997;6:831-41
    • (1997) Hum Mol Genet , vol.6 , pp. 831-841
    • Williamson, R.A.1    Henry, M.D.2    Daniels, K.J.3
  • 98
    • 0041710928 scopus 로고    scopus 로고
    • Chimaeric mice deficient in dystroglycans develop muscular dystrophy and have disrupted myoneural synapses
    • Cote PD, Moukhles H, Lindenbaum M, et al: Chimaeric mice deficient in dystroglycans develop muscular dystrophy and have disrupted myoneural synapses. Nat Genet 1999;23:338-42
    • (1999) Nat Genet , vol.23 , pp. 338-342
    • Cote, P.D.1    Moukhles, H.2    Lindenbaum, M.3
  • 99
    • 0028178082 scopus 로고
    • Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor
    • 6-3
    • Gee SH, Montanaro F, Lindenbaum MH, et al: Dystroglycan-alpha, a dystrophin-associated glycoprotein, is a functional agrin receptor. Cell 6-3-1994;77:675-86
    • (1994) Cell , vol.77 , pp. 675-686
    • Gee, S.H.1    Montanaro, F.2    Lindenbaum, M.H.3
  • 100
    • 0033915460 scopus 로고    scopus 로고
    • Characterization of the beta-dystroglycan-growth factor receptor 2 (Grb2) interaction
    • Russo K, Di Stasio E, Macchia G, et al: Characterization of the beta-dystroglycan-growth factor receptor 2 (Grb2) interaction. Biochem Biophys Res Commun 2000;274:93-8
    • (2000) Biochem Biophys Res Commun , vol.274 , pp. 93-98
    • Russo, K.1    Di Stasio, E.2    Macchia, G.3
  • 101
    • 15844401780 scopus 로고    scopus 로고
    • Expression of caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins
    • Song KS, Scherer PE, Tang Z, et al: Expression of caveolin-3 is a component of the sarcolemma and co-fractionates with dystrophin and dystrophin-associated glycoproteins. J Biol Chem 1996;271:15160-5
    • (1996) J Biol Chem , vol.271 , pp. 15160-15165
    • Song, K.S.1    Scherer, P.E.2    Tang, Z.3
  • 102
    • 0034532164 scopus 로고    scopus 로고
    • Caveolin-3 directly interacts with the C-terminal tail of β-dystroglycan: Identification of a central WW-like domain within caveolin family members
    • Sotgia F, Lee JK, Das K, et al: Caveolin-3 directly interacts with the C-terminal tail of β-dystroglycan: Identification of a central WW-like domain within caveolin family members. J Biol Chem 2000;275:38048-58
    • (2000) J Biol Chem , vol.275 , pp. 38048-38058
    • Sotgia, F.1    Lee, J.K.2    Das, K.3
  • 104
    • 0026729382 scopus 로고
    • The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling
    • Lowenstein EJ, Daly RJ, Batzer AG, et al: The SH2 and SH3 domain-containing protein GRB2 links receptor tyrosine kinases to ras signaling. Cell 1992;70: 431-42
    • (1992) Cell , vol.70 , pp. 431-442
    • Lowenstein, E.J.1    Daly, R.J.2    Batzer, A.G.3
  • 105
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae micro-domains
    • Song KS, Li S, Okamoto T, et al: Co-purification and direct interaction of Ras with caveolin, an integral membrane protein of caveolae micro-domains. J Biol Chem 1996;271:9690-7
    • (1996) J Biol Chem , vol.271 , pp. 9690-9697
    • Song, K.S.1    Li, S.2    Okamoto, T.3
  • 106
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing: "Preassembled signaling complexes" at the plasma membrane
    • Okamoto T, Schlegel A, Scherer PE, et al: Caveolins, a family of scaffolding proteins for organizing: "Preassembled signaling complexes" at the plasma membrane. J Biol Chem 1998;273:5419-22
    • (1998) J Biol Chem , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3
  • 107
    • 0027216855 scopus 로고
    • Heterogenicity of dystrophin-associated proteins
    • Yamamoto H, Hagiwara Y, Mizuno Y, et al: Heterogenicity of dystrophin-associated proteins. J Biochem 1993;114:132-9
    • (1993) J Biochem , vol.114 , pp. 132-139
    • Yamamoto, H.1    Hagiwara, Y.2    Mizuno, Y.3
  • 108
    • 10344249872 scopus 로고    scopus 로고
    • Mutations that disrupt the carboxylterminus of gamma-sarcoglycan cause muscular dystrophy
    • McNally EM, Duggan D, Gorospe JR, et al: Mutations that disrupt the carboxylterminus of gamma-sarcoglycan cause muscular dystrophy. Hum Mol Genet 1996;5:1841-7
    • (1996) Hum Mol Genet , vol.5 , pp. 1841-1847
    • McNally, E.M.1    Duggan, D.2    Gorospe, J.R.3
  • 109
    • 0032494165 scopus 로고    scopus 로고
    • gamma-Sarcoglycan deficiency leads to muscle membrane defects and apoptosis independent of dystrophin
    • Hack AA, Ly CT, Jiang F, et al: gamma-Sarcoglycan deficiency leads to muscle membrane defects and apoptosis independent of dystrophin. J Cell Biol 1998;142:1279-87
    • (1998) J Cell Biol , vol.142 , pp. 1279-1287
    • Hack, A.A.1    Ly, C.T.2    Jiang, F.3
  • 110
    • 0033583259 scopus 로고    scopus 로고
    • Ecto-ATPase activity of α-sarcoglycan (Adhalin)
    • Betto R, Senter L, Ceoldo S, et al: Ecto-ATPase activity of α-sarcoglycan (Adhalin). J Biol Chem 1999;274:7907-12
    • (1999) J Biol Chem , vol.274 , pp. 7907-7912
    • Betto, R.1    Senter, L.2    Ceoldo, S.3
  • 111
    • 0030783172 scopus 로고    scopus 로고
    • Animal models for muscular dystrophy show different patterns of sarcolemmal disruption
    • Straub V, Rafael JA, Chamberlain JS, et al: Animal models for muscular dystrophy show different patterns of sarcolemmal disruption. J Cell Biol 1997;139:375-85
    • (1997) J Cell Biol , vol.139 , pp. 375-385
    • Straub, V.1    Rafael, J.A.2    Chamberlain, J.S.3
  • 112
    • 0033084217 scopus 로고    scopus 로고
    • Secondary reduction of alpha7B integrin in laminin alpha2 deficient congenital muscular dystrophy supports an additional transmembrane link in skeletal muscle
    • Cohn RD, Mayer U, Saher G, et al: Secondary reduction of alpha7B integrin in laminin alpha2 deficient congenital muscular dystrophy supports an additional transmembrane link in skeletal muscle. J Neurol Sci 1999;163:140-52
    • (1999) J Neurol Sci , vol.163 , pp. 140-152
    • Cohn, R.D.1    Mayer, U.2    Saher, G.3
  • 113
    • 0033600748 scopus 로고    scopus 로고
    • Activation of c-Raf-1 kinase signal transduction pathway in alpha(7) integrin-deficient mice
    • Saher G, Hildt E: Activation of c-Raf-1 kinase signal transduction pathway in alpha(7) integrin-deficient mice. J Biol Chem 1999;274:27651-7
    • (1999) J Biol Chem , vol.274 , pp. 27651-27657
    • Saher, G.1    Hildt, E.2
  • 114
    • 0030809116 scopus 로고    scopus 로고
    • Altered expression of the alpha7beta1 integrin in human and murine muscular dystrophies
    • Hodges BL, Hayashi YK, Nonaka I, et al: Altered expression of the alpha7beta1 integrin in human and murine muscular dystrophies. J Cell Sci 1997;110(pt 22):2873-81
    • (1997) J Cell Sci , vol.110 , Issue.PART 22 , pp. 2873-2881
    • Hodges, B.L.1    Hayashi, Y.K.2    Nonaka, I.3
  • 115
    • 17344372250 scopus 로고    scopus 로고
    • Mutations in the integrin alpha7 gene cause congenital myopathy
    • Hayashi YK, Chou FL, Engvall E, et al: Mutations in the integrin alpha7 gene cause congenital myopathy. Nat Genet 1998;19:94-7
    • (1998) Nat Genet , vol.19 , pp. 94-97
    • Hayashi, Y.K.1    Chou, F.L.2    Engvall, E.3
  • 116
    • 0030724952 scopus 로고    scopus 로고
    • Absence of integrin α7 a novel from of muscular dystrophy
    • Mayer U, Saher G, Fassler R, et al: Absence of integrin α7 a novel from of muscular dystrophy. Nat Genet 1997;17:318-23
    • (1997) Nat Genet , vol.17 , pp. 318-323
    • Mayer, U.1    Saher, G.2    Fassler, R.3
  • 117
    • 0035921981 scopus 로고    scopus 로고
    • An agrin minigene rescues dystrophic symptoms in a mouse model for congenital muscular dystrophy
    • Moll J, Barzaghi P, Lin S, et al: An agrin minigene rescues dystrophic symptoms in a mouse model for congenital muscular dystrophy. Nature 2001;413:302-7
    • (2001) Nature , vol.413 , pp. 302-307
    • Moll, J.1    Barzaghi, P.2    Lin, S.3
  • 118
    • 0015219671 scopus 로고
    • Duchenne muscular dystrophy: Functional ischemia reproduces its characteristic lesions
    • Mendell JR, Engel WK, Derrer EC: Duchenne muscular dystrophy: Functional ischemia reproduces its characteristic lesions. Science 1971;172:1143-5
    • (1971) Science , vol.172 , pp. 1143-1145
    • Mendell, J.R.1    Engel, W.K.2    Derrer, E.C.3
  • 119
    • 0028865926 scopus 로고
    • Free radicals, programmed cell death and muscular dystrophy
    • Brown RH: Free radicals, programmed cell death and muscular dystrophy. Curr Opin Neurobiol 1995;8:373-8
    • (1995) Curr Opin Neurobiol , vol.8 , pp. 373-378
    • Brown, R.H.1
  • 120
    • 0026777351 scopus 로고
    • Potential oxyradical damage and energy status in individual muscle fibres from degenerating muscle diseases
    • Austin L, de Niese M, McGregor A, et al: Potential oxyradical damage and energy status in individual muscle fibres from degenerating muscle diseases. Neuromuscul Disord 1992;2:27-33
    • (1992) Neuromuscul Disord , vol.2 , pp. 27-33
    • Austin, L.1    De Niese, M.2    McGregor, A.3
  • 121
    • 0024359181 scopus 로고
    • Lipid peroxide and antioxidant enzymes in muscle and nonmuscle of dystrophic mouse
    • Asayama K, Hayashibe H, Dobashi K, et al: Lipid peroxide and antioxidant enzymes in muscle and nonmuscle of dystrophic mouse. Muscle Nerve 1989;12:742-8
    • (1989) Muscle Nerve , vol.12 , pp. 742-748
    • Asayama, K.1    Hayashibe, H.2    Dobashi, K.3
  • 122
    • 0028895065 scopus 로고
    • Oxyradical damage and mitochondrial enzyme activities in the mdx mouse
    • Hauser E, Hoger H, Bittner R, et al: Oxyradical damage and mitochondrial enzyme activities in the mdx mouse. Neuropediatrics 1995;26:260-2
    • (1995) Neuropediatrics , vol.26 , pp. 260-262
    • Hauser, E.1    Hoger, H.2    Bittner, R.3
  • 124
    • 4243999581 scopus 로고    scopus 로고
    • How the lack of dystrophin may upset calcium regulation and lead to oxidative damage
    • Kakulas BA, Mastaglia FL (eds): New York, Raven Press
    • Austin L: How the lack of dystrophin may upset calcium regulation and lead to oxidative damage, in: Kakulas BA, Mastaglia FL (eds): Pathogenesis and Therapy of Duchenne and Becker Muscular Dystrophy. New York, Raven Press, 1999, pp 69-82
    • (1999) Pathogenesis and Therapy of Duchenne and Becker Muscular Dystrophy , pp. 69-82
    • Austin, L.1
  • 125
    • 0026438910 scopus 로고
    • Reactive oxygen in skeletal muscle: I. Intracellular oxidant kinetics and fatigue in vitro
    • Reid MB, Haack KE, Franchek KM, et al: Reactive oxygen in skeletal muscle: I. Intracellular oxidant kinetics and fatigue in vitro. J Appl Physiol 1992;73:1797-804
    • (1992) J Appl Physiol , vol.73 , pp. 1797-1804
    • Reid, M.B.1    Haack, K.E.2    Franchek, K.M.3
  • 126
    • 0026448466 scopus 로고
    • Reactive oxygen in skeletal muscle: II. Extracellular release of free radicals
    • Reid MB, Shoji T, Moody MR, et al: Reactive oxygen in skeletal muscle: II. Extracellular release of free radicals. J Appl Physiol 1991;73:1805-9
    • (1991) J Appl Physiol , vol.73 , pp. 1805-1809
    • Reid, M.B.1    Shoji, T.2    Moody, M.R.3
  • 127
    • 15444353991 scopus 로고    scopus 로고
    • Differential protein oxidation in Duchenne and Becker muscular dystrophy
    • Haycock JW, Mac Neil S, Mantle D: Differential protein oxidation in Duchenne and Becker muscular dystrophy. NeuroReport 1998;9:2201-7
    • (1998) NeuroReport , vol.9 , pp. 2201-2207
    • Haycock, J.W.1    Mac Neil, S.2    Mantle, D.3
  • 128
    • 0030861564 scopus 로고    scopus 로고
    • Oxidative stress as a potential pathogenic mechanism in an animal model of Duchenne muscular dystrophy
    • Ragusa RJ, Chow CK, Porter JD: Oxidative stress as a potential pathogenic mechanism in an animal model of Duchenne muscular dystrophy. Neuromuscul Disord 1997;7:379-86
    • (1997) Neuromuscul Disord , vol.7 , pp. 379-386
    • Ragusa, R.J.1    Chow, C.K.2    Porter, J.D.3
  • 129
    • 0032569827 scopus 로고    scopus 로고
    • Evidence of oxidative stress in mdx mouse muscle: Studies of the pre-necrotic state
    • Disatnik MH, Dhawan J, Yu Y, et al: Evidence of oxidative stress in mdx mouse muscle: Studies of the pre-necrotic state. J Neurol Sci 1998;161:77-84
    • (1998) J Neurol Sci , vol.161 , pp. 77-84
    • Disatnik, M.H.1    Dhawan, J.2    Yu, Y.3
  • 130
    • 0032007205 scopus 로고    scopus 로고
    • Muscle cells from mdx mice have an increased susceptibility to oxidative stress
    • Rando TA, Disatnik MH, Yu Y, et al: Muscle cells from mdx mice have an increased susceptibility to oxidative stress. Neuromuscul Disord 1998;8:14-21
    • (1998) Neuromuscul Disord , vol.8 , pp. 14-21
    • Rando, T.A.1    Disatnik, M.H.2    Yu, Y.3
  • 131
    • 0034100628 scopus 로고    scopus 로고
    • Dystrophin mutations predict cellular susceptibility to oxidative stress
    • Disatnik MH, Chamberlain JS, Rando TA: Dystrophin mutations predict cellular susceptibility to oxidative stress. Muscle Nerve 2000;23:784-92
    • (2000) Muscle Nerve , vol.23 , pp. 784-792
    • Disatnik, M.H.1    Chamberlain, J.S.2    Rando, T.A.3
  • 132
    • 0034610326 scopus 로고    scopus 로고
    • Functional muscle ischemia in neuronal nitric oxide synthase-deficient skeletal muscle of children with Duchenne muscular dystrophy
    • Sander M, Chavoshan B, Harris SA, et al: Functional muscle ischemia in neuronal nitric oxide synthase-deficient skeletal muscle of children with Duchenne muscular dystrophy. Proc Natl Acad Sci USA 2000;97:13818-23
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 13818-13823
    • Sander, M.1    Chavoshan, B.2    Harris, S.A.3
  • 133
    • 0033588050 scopus 로고    scopus 로고
    • Disruption of the sarcoglycansarcospan complex in vascular smooth muscle: A novel mechanism for cardiomyopathy and muscular dystrophy
    • Coral-Vazquez R, Chon RD, Moore SA, et al: Disruption of the sarcoglycansarcospan complex in vascular smooth muscle: A novel mechanism for cardiomyopathy and muscular dystrophy. Cell 1998;98:465-74
    • (1998) Cell , vol.98 , pp. 465-474
    • Coral-Vazquez, R.1    Chon, R.D.2    Moore, S.A.3
  • 134
    • 0033963757 scopus 로고    scopus 로고
    • Disruption of the β-sarcoglycan gene reveals pathogenetic complexity of limbgirdle muscular dystrophy type 2E
    • Durbeej M, Cohn RD, Hrstka RF, et al: Disruption of the β-sarcoglycan gene reveals pathogenetic complexity of limbgirdle muscular dystrophy type 2E. Mol Cell 2000;5:141-51
    • (2000) Mol Cell , vol.5 , pp. 141-151
    • Durbeej, M.1    Cohn, R.D.2    Hrstka, R.F.3
  • 135
    • 0019979507 scopus 로고
    • Microvascular spasm in the cardiomyopathic Syrian Hamster: A preventable cause of focal myocardial necrosis
    • Factor SM, Minase T, Cho S, et al: Microvascular spasm in the cardiomyopathic Syrian Hamster: A preventable cause of focal myocardial necrosis. Circulation 1982:342-54
    • (1982) Circulation , pp. 342-354
    • Factor, S.M.1    Minase, T.2    Cho, S.3
  • 136
    • 0028051872 scopus 로고
    • Exogenous Dp71 restores the levels of dystrophin associated proteins but does not alleviate muscle damage in mdx mice
    • Greenberg DS, Sunada Y, Campbell KP, et al: Exogenous Dp71 restores the levels of dystrophin associated proteins but does not alleviate muscle damage in mdx mice. Nat Genet 1994;8:340-4
    • (1994) Nat Genet , vol.8 , pp. 340-344
    • Greenberg, D.S.1    Sunada, Y.2    Campbell, K.P.3
  • 137
    • 0028134623 scopus 로고
    • Dp71 can restore the dystrophin-associated glycoprotein complex in muscle but fails to prevent dystrophy
    • Cox GA, Sunada Y, Campbell KP, et al: Dp71 can restore the dystrophin-associated glycoprotein complex in muscle but fails to prevent dystrophy. Nat Genet 1994;8:333-9
    • (1994) Nat Genet , vol.8 , pp. 333-339
    • Cox, G.A.1    Sunada, Y.2    Campbell, K.P.3
  • 138
    • 0027960152 scopus 로고
    • Dystrophin associated proteins fail in filling dystrophin's shoes
    • Hoffman EP: Dystrophin associated proteins fail in filling dystrophin's shoes. Nat Genet 1994;8:311-2
    • (1994) Nat Genet , vol.8 , pp. 311-312
    • Hoffman, E.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.