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Volumn 71, Issue , 2009, Pages 37-57

Mechanisms of muscle degeneration, regeneration, and repair in the muscular dystrophies

Author keywords

Dysferlin; Dystrophin; Lamin A C; Nitric oxide synthase; Sarcoglycan

Indexed keywords

BIGLYCAN; CALCIUM ION; CALPAIN; CAVEOLIN 3; DYSFERLIN; DYSTROPHIN; EMERIN; FREE RADICAL; LAMIN A; LAMIN C; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; SARCOGLYCAN; TRANSFORMING GROWTH FACTOR BETA1;

EID: 67149122523     PISSN: 00664278     EISSN: 15451585     Source Type: Book Series    
DOI: 10.1146/annurev.physiol.010908.163216     Document Type: Review
Times cited : (260)

References (152)
  • 1
    • 0025272250 scopus 로고
    • Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
    • DOI 10.1038/345315a0
    • Ervasti JM, Ohlendieck K, Kahl SD, Gaver MG, Campbell KP. 1990. Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle. Nature 345:315-319 (Pubitemid 20159538)
    • (1990) Nature , vol.345 , Issue.6273 , pp. 315-319
    • Ervasti, J.M.1    Ohlendieck, K.2    Kahl, S.D.3    Gaver, M.G.4    Campbell, K.P.5
  • 2
    • 0025242185 scopus 로고
    • Glycoprotein complex anchoring dystrophin to sarcolemma
    • Yoshida M, Ozawa E. 1990. Glycoprotein complex anchoring dystrophin to sarcolemma. J. Biochem. 108:748-752
    • (1990) J. Biochem. , vol.108 , pp. 748-752
    • Yoshida, M.1    Ozawa, E.2
  • 3
    • 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. 2000. The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J. Cell Biol. 150:1209-1214
    • (2000) J. Cell Biol. , vol.150 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 4
  • 5
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and α1-syntrophin mediated by PDZ domains
    • Brenman JE, Chao DS, Gee SH, McGee AW, Craven SE, et al. 1996. Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and α1-syntrophin mediated by PDZ domains. Cell 84:757-767
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1    Chao, D.S.2    Gee, S.H.3    McGee, A.W.4    Craven, S.E.5
  • 7
    • 0036699086 scopus 로고    scopus 로고
    • Genetic diseases of muscle
    • Wagner KR. 2002. Genetic diseases of muscle. Neurol. Clin. 20:645-678
    • (2002) Neurol. Clin. , vol.20 , pp. 645-678
    • Wagner, K.R.1
  • 10
    • 33644868707 scopus 로고    scopus 로고
    • Impact of sarcoglycan complex on mechanical signal transduction in murine skeletal muscle
    • Barton ER. 2006. Impact of sarcoglycan complex on mechanical signal transduction in murine skeletal muscle. Am. J. Physiol. Cell Physiol. 290:C411-19
    • (2006) Am. J. Physiol. Cell Physiol. , vol.290
    • Barton, E.R.1
  • 11
    • 0028980027 scopus 로고
    • Mutations in the laminin α2-chain gene (LAMA2) cause merosin-deficient congenital muscular dystrophy
    • Helbling-Leclerc A, Zhang X, Topaloglu H, Cruaud C, Tesson F, et al. 1995. Mutations in the laminin α2-chain gene (LAMA2) cause merosin-deficient congenital muscular dystrophy. Nat. Genet. 11:216-218
    • (1995) Nat. Genet. , vol.11 , pp. 216-218
    • Helbling-Leclerc, A.1    Zhang, X.2    Topaloglu, H.3    Cruaud, C.4    Tesson, F.5
  • 13
    • 34250854638 scopus 로고    scopus 로고
    • Congenital muscular dystrophies Involving the O-mannose pathway
    • DOI 10.2174/156652407780831601
    • Martin PT. 2007. Congenital muscular dystrophies involving the O-mannose pathway. Curr. Mol. Med. 7:417-425 (Pubitemid 46979705)
    • (2007) Current Molecular Medicine , vol.7 , Issue.4 , pp. 417-425
    • Martin, P.T.1
  • 17
    • 4444306357 scopus 로고    scopus 로고
    • Genetic compensation for sarcoglycan loss by integrin α7β1 in muscle
    • DOI 10.1242/jcs.01234
    • Allikian MJ, Hack AA, Mewborn S, Mayer U, McNally EM. 2004. Genetic compensation for sarcoglycan loss by integrin α7β1 in muscle. J. Cell Sci. 117:3821-3830 (Pubitemid 39207320)
    • (2004) Journal of Cell Science , vol.117 , Issue.17 , pp. 3821-3830
    • Allikian, M.J.1    Hack, A.A.2    Mewborn, S.3    Mayer, U.4    McNally, E.M.5
  • 19
    • 33644778843 scopus 로고    scopus 로고
    • Absence of α7 integrin in dystrophin-deficient mice causes a myopathy similar to Duchenne muscular dystrophy
    • DOI 10.1093/hmg/ddl018
    • Guo C, Willem M, Werner A, Raivich G, Emerson M, et al. 2006. Absence of α7 integrin in dystrophindeficient mice causes a myopathy similar to Duchenne muscular dystrophy. Hum. Mol. Genet. 15:989-998 (Pubitemid 43338239)
    • (2006) Human Molecular Genetics , vol.15 , Issue.6 , pp. 989-998
    • Guo, C.1    Willem, M.2    Werner, A.3    Raivich, G.4    Emerson, M.5    Neyses, L.6    Mayer, U.7
  • 21
    • 0035911960 scopus 로고    scopus 로고
    • Enhanced expression of the α7β1 integrin reduces muscular dystrophy and restores viability in dystrophic mice
    • Burkin DJ, Wallace GQ, Nicol KJ, Kaufman DJ, Kaufman SJ. 2001. Enhanced expression of the α7β1 integrin reduces muscular dystrophy and restores viability in dystrophic mice. J. Cell Biol. 152:1207-1218
    • (2001) J. Cell Biol. , vol.152 , pp. 1207-1218
    • Burkin, D.J.1    Wallace, G.Q.2    Nicol, K.J.3    Kaufman, D.J.4    Kaufman, S.J.5
  • 22
    • 0016591825 scopus 로고
    • Duchenne dystrophy: Electron microscopic findings pointing to a basic or early abnormality in the plasma membrane of the muscle fiber
    • Mokri B, Engel AG. 1975. Duchenne dystrophy: electron microscopic findings pointing to a basic or early abnormality in the plasma membrane of the muscle fiber. Neurology 25:1111-1120
    • (1975) Neurology , vol.25 , pp. 1111-1120
    • Mokri, B.1    Engel, A.G.2
  • 23
    • 0033782272 scopus 로고    scopus 로고
    • Contrast agent-enhanced magnetic resonance imaging of skeletal muscle damage in animal models of muscular dystrophy
    • Straub V, Donahue KM, Allamand V, Davisson RL, Kim YR, Campbell KP. 2000. Contrast agentenhanced magnetic resonance imaging of skeletal muscle damage in animal models of muscular dystrophy. Magn. Reson. Med. 44:655-659 (Pubitemid 30769669)
    • (2000) Magnetic Resonance in Medicine , vol.44 , Issue.4 , pp. 655-659
    • Straub, V.1    Donahue, K.M.2    Allamand, V.3    Davisson, R.L.4    Kim, Y.R.5    Campbell, K.P.6
  • 24
    • 0020050391 scopus 로고
    • Membrane myopathy: Morphological similarities to Duchenne muscular dystrophy
    • Pestronk A, Parhad IM, Drachman DB, Price DL. 1982. Membrane myopathy: morphological similarities to Duchenne muscular dystrophy. Muscle Nerve 5:209-214
    • (1982) Muscle Nerve , vol.5 , pp. 209-214
    • Pestronk, A.1    Parhad, I.M.2    Drachman, D.B.3    Price, D.L.4
  • 25
    • 0026032731 scopus 로고
    • Decreased osmotic stability of dystrophin-less muscle cells from the mdx mouse
    • Menke A, Jockusch H. 1991. Decreased osmotic stability of dystrophin-less muscle cells from the mdx mouse. Nature 349:69-71 (Pubitemid 21912016)
    • (1991) Nature , vol.349 , Issue.6304 , pp. 69-71
    • Menke, A.1    Jockusch, H.2
  • 26
    • 0028929061 scopus 로고
    • Mechanical function of dystrophin in muscle cells
    • Pasternak C, Wong S, Elson EL. 1995. Mechanical function of dystrophin in muscle cells. J. Cell Biol. 128:355-361
    • (1995) J. Cell Biol. , vol.128 , pp. 355-361
    • Pasternak, C.1    Wong, S.2    Elson, E.L.3
  • 27
    • 0033594082 scopus 로고    scopus 로고
    • Extensive but coordinated reorganization of the membrane skeleton in myofibers of dystrophic (mdx) mice
    • Williams MW, Bloch RJ. 1999. Extensive but coordinated reorganization of the membrane skeleton in myofibers of dystrophic (mdx) mice. J. Cell Biol. 144:1259-1270
    • (1999) J. Cell Biol. , vol.144 , pp. 1259-1270
    • Williams, M.W.1    Bloch, R.J.2
  • 28
    • 0026731937 scopus 로고
    • Immunologic study of vinculin in Duchenne muscular dystrophy
    • Minetti C, Tanji K, Bonilla E. 1992. Immunologic study of vinculin in Duchenne muscular dystrophy. Neurology 42:1751-1754
    • (1992) Neurology , vol.42 , pp. 1751-1754
    • Minetti, C.1    Tanji, K.2    Bonilla, E.3
  • 31
    • 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, Karpati G, Vincent G, et al. 2001. Dystrophin-deficient cardiomyocytes are abnormally vulnerable to mechanical stress-induced contractile failure and injury. FASEB J. 15:1655-1657
    • (2001) FASEB J. , vol.15 , pp. 1655-1657
    • Danialou, G.1    Comtois, A.S.2    Dudley, R.3    Karpati, G.4    Vincent, G.5
  • 32
    • 0036686713 scopus 로고    scopus 로고
    • 2+ homeostasis and of survival in collagenase-isolated muscle fibres from normal and mdx mice
    • 2+ homeostasis and of survival in collagenase-isolated muscle fibres from normal and mdx mice. J. Physiol. 542:855-865
    • (2002) J. Physiol. , vol.542 , pp. 855-865
    • De Backer, F.1    Vandebrouck, C.2    Gailly, P.3    Gillis, J.M.4
  • 35
    • 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 AG. 1978. Intracellular calcium accumulation in Duchenne dystrophy and other myopathies: a study of 567,000 muscle fibers in 114 biopsies. Neurology 28:439-446
    • (1978) Neurology , vol.28 , pp. 439-446
    • Bodensteiner, J.B.1    Engel, A.G.2
  • 36
    • 0025317892 scopus 로고
    • Calcium entry through stretch-inactivated ion channels in mdx myotubes
    • DOI 10.1038/344670a0
    • Franco A Jr, Lansman JB. 1990. Calcium entry through stretch-inactivated ion channels in mdx myotubes. Nature 344:670-673 (Pubitemid 20108369)
    • (1990) Nature , vol.344 , Issue.6267 , pp. 670-673
    • Franco Jr., A.1    Lansman, J.B.2
  • 37
    • 0037119993 scopus 로고    scopus 로고
    • Involvement of TRPC in the abnormal calcium influx observed in dystrophic (mdx) mouse skeletal muscle fibers
    • DOI 10.1083/jcb.200203091
    • Vandebrouck C, Martin D, Colson-Van Schoor M, Debaix H, Gailly P. 2002. Involvement of TRPC in the abnormal calcium influx observed in dystrophic (mdx) mouse skeletal muscle fibers. J. Cell Biol. 158:1089-1096 (Pubitemid 35052691)
    • (2002) Journal of Cell Biology , vol.158 , Issue.6 , pp. 1089-1096
    • Vandebrouck, C.1    Martin, D.2    Schoor, M.C.-V.3    Debaix, H.4    Gailly, P.5
  • 39
    • 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
    • DOI 10.1016/S1050-1738(00)00075-X, PII S105017380000075X
    • Alderton JM, Steinhardt RA. 2000. How calcium influx through calcium leak channels is responsible for the elevated levels of calcium-dependent proteolysis in dystrophic myotubes. Trends Cardiovasc. Med. 10:268-272 (Pubitemid 32229884)
    • (2000) Trends in Cardiovascular Medicine , vol.10 , Issue.6 , pp. 268-272
    • Alderton, J.M.1    Steinhardt, R.A.2
  • 43
    • 41849118741 scopus 로고    scopus 로고
    • Genetic and pharmacologic inhibition of mitochondrial-dependent necrosis attenuates muscular dystrophy
    • Millay DP, Sargent MA, Osinska H, Baines CP, Barton ER, et al. 2008. Genetic and pharmacologic inhibition of mitochondrial-dependent necrosis attenuates muscular dystrophy. Nat. Med. 14:442-447
    • (2008) Nat. Med. , vol.14 , pp. 442-447
    • Millay, D.P.1    Sargent, M.A.2    Osinska, H.3    Baines, C.P.4    Barton, E.R.5
  • 45
    • 0036798005 scopus 로고    scopus 로고
    • Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology
    • Spencer MJ, Mellgren RL. 2002. Overexpression of a calpastatin transgene in mdx muscle reduces dystrophic pathology. Hum. Mol. Genet. 11:2645-2655 (Pubitemid 35174694)
    • (2002) Human Molecular Genetics , vol.11 , Issue.21 , pp. 2645-2655
    • Spencer, M.J.1    Mellgren, R.L.2
  • 46
    • 0032007205 scopus 로고    scopus 로고
    • Muscle cells from mdx mice have an increased susceptibility to oxidative stress
    • DOI 10.1016/S0960-8966(97)00124-7, PII S0960896697001247
    • Rando TA, Disatnik MH, Yu Y, Franco A. 1998. Muscle cells from mdx mice have an increased susceptibility to oxidative stress. Neuromuscular Disord. 8:14-21 (Pubitemid 28174930)
    • (1998) Neuromuscular Disorders , vol.8 , Issue.1 , pp. 14-21
    • Rando, T.A.1    Disatnik, M.-H.2    Yu, Y.3    Franco, A.4
  • 48
    • 0035494438 scopus 로고    scopus 로고
    • A nitric oxide synthase transgene ameliorates muscular dystrophy in mdx mice
    • DOI 10.1083/jcb.200105110
    • Wehling M, Spencer MJ, Tidball JG. 2001. A nitric oxide synthase transgene ameliorates muscular dystrophy in mdx mice. J. Cell Biol. 155:123-131 (Pubitemid 34286213)
    • (2001) Journal of Cell Biology , vol.155 , Issue.1 , pp. 123-131
    • Wehling, M.1    Spencer, M.J.2    Tidball, J.G.3
  • 51
    • 0035891532 scopus 로고    scopus 로고
    • Role of nitric oxide in the pathogenesis of muscular dystrophies: A "two hit" hypothesis of the cause of muscle necrosis
    • Rando TA. 2001. Role of nitric oxide in the pathogenesis of muscular dystrophies: a "two hit" hypothesis of the cause of muscle necrosis. Microsc. Res. Tech. 55:223-235
    • (2001) Microsc. Res. Tech. , vol.55 , pp. 223-235
    • Rando, T.A.1
  • 53
    • 33645450207 scopus 로고    scopus 로고
    • Sarcolemmal damage in dystrophin deficiency is modulated by synergistic interactions between mechanical and oxidative/ nitrosative stresses
    • Dudley RW, Danialou G, Govindaraju K, Lands L, Eidelman DE, Petrof BJ. 2006. Sarcolemmal damage in dystrophin deficiency is modulated by synergistic interactions between mechanical and oxidative/ nitrosative stresses. Am. J. Pathol. 168:1276-1287
    • (2006) Am. J. Pathol. , vol.168 , pp. 1276-1287
    • Dudley, R.W.1    Danialou, G.2    Govindaraju, K.3    Lands, L.4    Eidelman, D.E.5    Petrof, B.J.6
  • 54
    • 0018758714 scopus 로고
    • Catalase, superoxide dismutase, glutathione reductase and thiobarbituric acid-reactive products in normal and dystrophic human muscle
    • Kar NC, Pearson CM. 1979. Catalase, superoxide dismutase, glutathione reductase and thiobarbituric acid-reactive products in normal and dystrophic human muscle. Clin. Chim. Acta 94:277-280
    • (1979) Clin. Chim. Acta , vol.94 , pp. 277-280
    • Kar, N.C.1    Pearson, C.M.2
  • 55
    • 24644459876 scopus 로고    scopus 로고
    • Lipid imaging by gold cluster time-of-flight secondary ion mass spectrometry: Application to Duchenne muscular dystrophy
    • DOI 10.1194/jlr.M500058-JLR200
    • Touboul D, Brunelle A, Halgand F, De La Porte S, Laprevote O. 2005. Lipid imaging by gold cluster time-of-flight secondary ion mass spectrometry: application to Duchenne muscular dystrophy. J. Lipid. Res. 46:1388-1395 (Pubitemid 43109802)
    • (2005) Journal of Lipid Research , vol.46 , Issue.7 , pp. 1388-1395
    • Touboul, D.1    Brunelle, A.2    Halgand, F.3    De La Porte, S.4    Laprevote, O.5
  • 57
    • 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. 1997. Oxidative stress as a potential pathogenic mechanism in an animal model of Duchenne muscular dystrophy. Neuromuscular Disord. 7:379-386
    • (1997) Neuromuscular Disord. , vol.7 , pp. 379-386
    • Ragusa, R.J.1    Chow, C.K.2    Porter, J.D.3
  • 59
    • 0032531046 scopus 로고    scopus 로고
    • Effects of iron deprivation on the pathology and stress protein expression in murine X-linked muscular dystrophy
    • DOI 10.1016/S0006-2952(98)00055-0, PII S0006295298000550
    • Bornman L, Rossouw H, Gericke GS, Polla BS. 1998. Effects of iron deprivation on the pathology and stress protein expression in murine X-linked muscular dystrophy. Biochem. Pharmacol. 56:751-757 (Pubitemid 28454586)
    • (1998) Biochemical Pharmacology , vol.56 , Issue.6 , pp. 751-757
    • Bornman, L.1    Rossouw, H.2    Gericke, G.S.3    Polla, B.S.4
  • 60
    • 0024230749 scopus 로고
    • Selenium and vitamin e treatment of Duchenne muscular dystrophy: No effect on muscle function
    • Backman E, Nylander E, Johansson I, Henriksson KG, Tagesson C. 1988. Selenium and vitamin E treatment of Duchenne muscular dystrophy: no effect on muscle function. Acta Neurol. Scand. 78:429-435
    • (1988) Acta Neurol. Scand. , vol.78 , pp. 429-435
    • Backman, E.1    Nylander, E.2    Johansson, I.3    Henriksson, K.G.4    Tagesson, C.5
  • 63
    • 0037336186 scopus 로고    scopus 로고
    • Mechanical stress activates the nuclear factor-kappaB pathway in skeletal muscle fibers: A possible role in Duchenne muscular dystrophy
    • DOI 10.1096/fj.02-0542com
    • Kumar A, Boriek AM. 2003. Mechanical stress activates the nuclear factor-κB pathway in skeletal muscle fibers: a possible role in Duchenne muscular dystrophy. FASEB J. 17:386-396 (Pubitemid 36292954)
    • (2003) FASEB Journal , vol.17 , Issue.3 , pp. 386-396
    • Kumar, A.1    Boriek, A.M.2
  • 64
    • 3242776169 scopus 로고    scopus 로고
    • Impact of TNF-α blockade on TGF-β1 and type I collagen mRNA expression in dystrophic muscle
    • Gosselin LE, Martinez DA. 2004. Impact of TNF-α blockade on TGF-β1 and type I collagen mRNA expression in dystrophic muscle. Muscle Nerve 30:244-246
    • (2004) Muscle Nerve , vol.30 , pp. 244-246
    • Gosselin, L.E.1    Martinez, D.A.2
  • 65
    • 1842454966 scopus 로고    scopus 로고
    • Anti-TNFα (Remicade) therapy protects dystrophic skeletal muscle from necrosis
    • DOI 10.1096/fj.03-1024com
    • Grounds MD, Torrisi J. 2004. Anti-TNFα (Remicade) therapy protects dystrophic skeletal muscle from necrosis. FASEB J. 18:676-682 (Pubitemid 38451789)
    • (2004) FASEB Journal , vol.18 , Issue.6 , pp. 676-682
    • Grounds, M.D.1    Torrisi, J.2
  • 67
    • 32644442731 scopus 로고    scopus 로고
    • Nuclear factor kappa-B blockade reduces skeletal muscle degeneration and enhances muscle function in Mdx mice
    • DOI 10.1016/j.expneurol.2005.11.021, PII S0014488605004504
    • Messina S, Bitto A, Aguennouz M, Minutoli L, Monici MC, et al. 2006. Nuclear factor κ-B blockade reduces skeletal muscle degeneration and enhances muscle function in Mdx mice. Exp. Neurol. 198:234-241 (Pubitemid 43243761)
    • (2006) Experimental Neurology , vol.198 , Issue.1 , pp. 234-241
    • Messina, S.1    Bitto, A.2    Aguennouz, M.3    Minutoli, L.4    Monici, M.C.5    Altavilla, D.6    Squadrito, F.7    Vita, G.8
  • 71
    • 0030972880 scopus 로고    scopus 로고
    • A nematode gene required for sperm vesicle fusion
    • Achanzar WE, Ward S. 1997. A nematode gene required for sperm vesicle fusion. J. Cell Sci. 110(Pt. 9):1073-1081 (Pubitemid 27232277)
    • (1997) Journal of Cell Science , vol.110 , Issue.9 , pp. 1073-1081
    • Achanzar, W.E.1    Ward, S.2
  • 72
    • 0037151075 scopus 로고    scopus 로고
    • Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains
    • Davis DB, Doherty KR, Delmonte AJ, McNally EM. 2002. Calcium-sensitive phospholipid binding properties of normal and mutant ferlin C2 domains. J. Biol. Chem. 277:22883-22888
    • (2002) J. Biol. Chem. , vol.277 , pp. 22883-22888
    • Davis, D.B.1    Doherty, K.R.2    Delmonte, A.J.3    McNally, E.M.4
  • 76
    • 0033673056 scopus 로고    scopus 로고
    • Intracellular accumulation and reduced sarcolemmal expression of dysferlin in limb-girdle muscular dystrophies
    • Piccolo F, Moore SA, Ford GC, Campbell KP. 2000. Intracellular accumulation and reduced sarcolemmal expression of dysferlin in limb-girdle muscular dystrophies. Ann. Neurol. 48:902-912
    • (2000) Ann. Neurol. , vol.48 , pp. 902-912
    • Piccolo, F.1    Moore, S.A.2    Ford, G.C.3    Kp, C.4
  • 77
    • 0035849492 scopus 로고    scopus 로고
    • The earliest pathologic alterations in dysferlinopathy
    • Selcen D, Stilling G, Engel AG. 2001. The earliest pathologic alterations in dysferlinopathy. Neurology 56:1472-1481
    • (2001) Neurology , vol.56 , pp. 1472-1481
    • Selcen, D.1    Stilling, G.2    Engel, A.G.3
  • 78
    • 33745223285 scopus 로고    scopus 로고
    • Absence of dysferlin alters myogenin expression and delays human muscle differentiation "in vitro"
    • de Luna N, Gallardo E, Soriano M, Dominguez-Perles R, de la Torre C, et al. 2006. Absence of dysferlin alters myogenin expression and delays human muscle differentiation "in vitro". J. Biol. Chem. 281:17092-17098
    • (2006) J. Biol. Chem. , vol.281 , pp. 17092-17098
    • De Luna, N.1    Gallardo, E.2    Soriano, M.3    Dominguez-Perles, R.4    De La Torre, C.5
  • 85
    • 0028905205 scopus 로고
    • Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
    • Richard I, Broux O, Allamand V, Fougerousse F, Chiannilkulchai N, et al. 1995. Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell 81:27-40
    • (1995) Cell , vol.81 , pp. 27-40
    • Richard, I.1    Broux, O.2    Allamand, V.3    Fougerousse, F.4    Chiannilkulchai, N.5
  • 90
    • 0024583598 scopus 로고
    • Enhancement of calcium sensitivity of lipocortin I in phospholipid binding induced by limited proteolysis and phosphorylation at the amino terminus as analyzed by phospholipid affinity column chromatography
    • Ando Y, Imamura S, Hong YM, Owada MK, Kakunaga T, Kannagi R. 1989. Enhancement of calcium sensitivity of lipocortin I in phospholipid binding induced by limited proteolysis and phosphorylation at the amino terminus as analyzed by phospholipid affinity column chromatography. J. Biol. Chem. 264:6948-6955 (Pubitemid 19114809)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.12 , pp. 6948-6955
    • Ando, Y.1    Imamura, S.2    Hong, Y.-M.3    Owada, M.K.4    Kakunaga, T.5    Kannagi, R.6
  • 91
    • 33746701373 scopus 로고    scopus 로고
    • Mutation finding in patients with dysferlin deficiency and role of the dysferlin interacting proteins annexin A1 and A2 in muscular dystrophies
    • Cagliani R, Magri F, Toscano A, Merlini L, Fortunato F, et al. 2005. Mutation finding in patients with dysferlin deficiency and role of the dysferlin interacting proteins annexin A1 and A2 in muscular dystrophies. Hum. Mutat. 26:283
    • (2005) Hum. Mutat. , vol.26 , pp. 283
    • Cagliani, R.1    Magri, F.2    Toscano, A.3    Merlini, L.4    Fortunato, F.5
  • 93
    • 0035802119 scopus 로고    scopus 로고
    • Protein kinase B phosphorylates AHNAK and regulates its subcellular localization
    • DOI 10.1083/jcb.200105121
    • Sussman J, Stokoe D, Ossina N, Shtivelman E. 2001. Protein kinase B phosphorylates AHNAK and regulates its subcellular localization. J. Cell Biol. 154:1019-1030 (Pubitemid 34286181)
    • (2001) Journal of Cell Biology , vol.154 , Issue.5 , pp. 1019-1030
    • Sussman, J.1    Stokoe, D.2    Ossina, N.3    Shtivelman, E.4
  • 95
    • 0033972161 scopus 로고    scopus 로고
    • Myoferlin, a candidate gene and potential modifier of muscular dystrophy
    • Davis DB, Delmonte AJ, Ly CT, McNally EM. 2000. Myoferlin, a candidate gene and potential modifier of muscular dystrophy. Hum. Mol. Genet. 9:217-226
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 217-226
    • Davis, D.B.1    Delmonte, A.J.2    Ly, C.T.3    McNally, E.M.4
  • 98
    • 0032006325 scopus 로고    scopus 로고
    • HGF/SF is present in normal adult skeletal muscle and is capable of activating satellite cells
    • DOI 10.1006/dbio.1997.8803
    • Tatsumi R, Anderson JE, Nevoret CJ, Halevy O, Allen RE. 1998. HGF/SF is present in normal adult skeletal muscle and is capable of activating satellite cells. Dev. Biol. 194:114-128 (Pubitemid 28115263)
    • (1998) Developmental Biology , vol.194 , Issue.1 , pp. 114-128
    • Tatsumi, R.1    Anderson, J.E.2    Nevoret, C.J.3    Halevy, O.4    Allen, R.E.5
  • 99
    • 0344827208 scopus 로고    scopus 로고
    • Notch-mediated restoration of regenerative potential to aged muscle
    • Conboy IM, Conboy MJ, Smythe GM, Rando TA. 2003. Notch-mediated restoration of regenerative potential to aged muscle. Science 302:1575-1577
    • (2003) Science , vol.302 , pp. 1575-1577
    • Conboy, I.M.1    Conboy, M.J.2    Smythe, G.M.3    Rando, T.A.4
  • 100
    • 0036744815 scopus 로고    scopus 로고
    • The regulation of Notch signaling controls satellite cell activation and cell fate determination in postnatal myogenesis
    • Conboy IM, Rando TA. 2002. The regulation of Notch signaling controls satellite cell activation and cell fate determination in postnatal myogenesis. Dev. Cell 3:397-409
    • (2002) Dev. Cell , vol.3 , pp. 397-409
    • Conboy, I.M.1    Rando, T.A.2
  • 101
    • 22744438723 scopus 로고    scopus 로고
    • Stem cell function, self-renewal, and behavioral heterogeneity of cells from the adult muscle satellite cell niche
    • DOI 10.1016/j.cell.2005.05.010, PII S0092867405004551
    • Collins CA, Olsen I, Zammit PS, Heslop L, Petrie A, et al. 2005. Stem cell function, self-renewal, and behavioral heterogeneity of cells from the adult muscle satellite cell niche. Cell 122:289-301 (Pubitemid 41032991)
    • (2005) Cell , vol.122 , Issue.2 , pp. 289-301
    • Collins, C.A.1    Olsen, I.2    Zammit, P.S.3    Heslop, L.4    Petrie, A.5    Partridge, T.A.6    Morgan, J.E.7
  • 102
    • 0006462275 scopus 로고
    • Defective myoblasts identified in Duchenne muscular dystrophy
    • Blau HM, Webster C, Pavlath GK. 1983. Defective myoblasts identified in Duchenne muscular dystrophy. Proc. Natl. Acad. Sci. USA 80:4856-4860
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4856-4860
    • Blau, H.M.1    Webster, C.2    Pavlath, G.K.3
  • 103
    • 0025646136 scopus 로고
    • Accelerated age-related decline in replicative life-span of Duchenne muscular dystrophy myoblasts: Implications for cell and gene therapy
    • Webster C, Blau HM. 1990. Accelerated age-related decline in replicative life-span of Duchenne muscular dystrophy myoblasts: implications for cell and gene therapy. Somat. Cell Mol. Genet. 16:557-565
    • (1990) Somat. Cell Mol. Genet. , vol.16 , pp. 557-565
    • Webster, C.1    Blau, H.M.2
  • 104
    • 0033945869 scopus 로고    scopus 로고
    • Evidence for a myogenic stem cell that is exhausted in dystrophic muscle
    • Heslop L, Morgan JE, Partridge TA. 2000. Evidence for a myogenic stem cell that is exhausted in dystrophic muscle. J. Cell Sci. 113(Pt. 12):2299-2308 (Pubitemid 30426843)
    • (2000) Journal of Cell Science , vol.113 , Issue.12 , pp. 2299-2308
    • Heslop, L.1    Morgan, J.E.2    Partridge, T.A.3
  • 105
    • 0018424046 scopus 로고
    • Quantitative ultrastructural study of muscle satellite cells in Duchenne dystrophy
    • Wakayama Y, Schotland DL, Bonilla E, Orecchio E. 1979. Quantitative ultrastructural study of muscle satellite cells in Duchenne dystrophy. Neurology 29:401-407 (Pubitemid 9111029)
    • (1979) Neurology , vol.29 , Issue.3 , pp. 401-407
    • Wakayama, Y.1    Schotland, D.L.2    Bonilla, E.3    Orecchio, E.4
  • 106
    • 0021054274 scopus 로고
    • A quantitative study of the muscle satellite cells in various neuromuscular disorders
    • Ishimoto S, Goto I, Ohta M, Kuroiwa Y. 1983. A quantitative study of the muscle satellite cells in various neuromuscular disorders. J. Neurol. Sci. 62:303-314 (Pubitemid 14176257)
    • (1983) Journal of the Neurological Sciences , vol.62 , Issue.1-3 , pp. 303-314
    • Ishimoto, S.1    Goto, I.2    Ohta, M.3    Kuroiwa, Y.4
  • 108
    • 0033958440 scopus 로고    scopus 로고
    • Shorter telomeres in dystrophic muscle consistent with extensive regeneration in young children
    • DOI 10.1016/S0960-8966(99)00093-0, PII S0960896699000930
    • Decary S, Hamida CB, Mouly V, Barbet JP, Hentati F, Butler-Browne GS. 2000. Shorter telomeres in dystrophic muscle consistent with extensive regeneration in young children. Neuromuscular Disord. 10:113-120 (Pubitemid 30050623)
    • (2000) Neuromuscular Disorders , vol.10 , Issue.2 , pp. 113-120
    • Decary, S.1    Ben Hamida, C.2    Mouly, V.3    Barbet, J.P.4    Hentati, F.5    Butler-Browne, G.S.6
  • 109
    • 0030881301 scopus 로고    scopus 로고
    • Replicative potential and telomere length in human skeletal muscle: Implications for satellite cell-mediated gene therapy
    • Decary S, Mouly V, Hamida CB, Sautet A, Barbet JP, Butler-Browne GS. 1997. Replicative potential and telomere length in human skeletal muscle: implications for satellite cell-mediated gene therapy. Hum. Gene Ther. 8:1429-1438 (Pubitemid 27393998)
    • (1997) Human Gene Therapy , vol.8 , Issue.12 , pp. 1429-1438
    • Decary, S.1    Mouly, V.2    Ben Hamida, C.3    Sautet, A.4    Barbet, J.P.5    Butler-Browne, G.S.6
  • 111
    • 34548267241 scopus 로고    scopus 로고
    • Telomere shortening in diaphragm and tibialis anterior muscles of aged mdx mice
    • Lund TC, Grange RW, Lowe DA. 2007. Telomere shortening in diaphragm and tibialis anterior muscles of aged mdx mice. Muscle Nerve 36:387-390
    • (2007) Muscle Nerve , vol.36 , pp. 387-390
    • Lund, T.C.1    Grange, R.W.2    Lowe, D.A.3
  • 112
    • 0030839985 scopus 로고    scopus 로고
    • Examination of telomere lengths in muscle tissue casts doubt on replicative aging as cause of progression in Duchenne muscular dystrophy
    • Oexle K, Zwirner A, Freudenberg K, Kohlschutter A, Speer A. 1997. Examination of telomere lengths in muscle tissue casts doubt on replicative aging as cause of progression in Duchenne muscular dystrophy. Pediatr. Res. 42:226-231 (Pubitemid 27311345)
    • (1997) Pediatric Research , vol.42 , Issue.2 , pp. 226-231
    • Oexle, K.1    Zwirner, A.2    Freudenberg, K.3    Kohlschutter, A.4    Speer, A.5
  • 113
    • 0021260779 scopus 로고
    • Comparison between the growth pattern of cell cultures from normal and Duchenne dystrophy muscle
    • DOI 10.1016/0022-510X(84)90033-9
    • Delaporte C, Dehaupas M, Fardeau M. 1984. Comparison between the growth pattern of cell cultures from normal and Duchenne dystrophy muscle. J. Neurol. Sci. 64:149-160 (Pubitemid 14111138)
    • (1984) Journal of the Neurological Sciences , vol.64 , Issue.2 , pp. 149-160
    • Delaporte, C.1    Dehaupas, M.2    Fardeau, M.3
  • 114
    • 0021341805 scopus 로고
    • Impaired muscle differentiation in explant cultures of Duchenne muscular dystrophy
    • Jasmin G, Tautu C, Vanasse M, Brochu P, Simoneau R. 1984. Impaired muscle differentiation in explant cultures of Duchenne muscular dystrophy. Lab. Investig. 50:197-207 (Pubitemid 14199081)
    • (1984) Laboratory Investigation , vol.50 , Issue.2 , pp. 197-207
    • Jasmin, G.1    Tautu, C.2    Vanasse, M.3
  • 115
    • 0033456243 scopus 로고    scopus 로고
    • Defective growth in vitro of duchenne muscular dystrophy myoblasts: The molecular and biochemical basis
    • DOI 10.1002/(SICI)1097-4644(20000101)76:1<118::AID-JCB12>3.0.CO;2-F
    • Melone MA, Peluso G, Petillo O, Galderisi U, Cotrufo R. 1999. Defective growth in vitro of Duchenne Muscular Dystrophy myoblasts: the molecular and biochemical basis. J. Cell Biochem. 76:118-132 (Pubitemid 30010764)
    • (1999) Journal of Cellular Biochemistry , vol.76 , Issue.1 , pp. 118-132
    • Melone, M.A.B.1    Peluso, G.2    Petillo, O.3    Galderisi, U.4    Cotrufo, R.5
  • 116
    • 33846946114 scopus 로고    scopus 로고
    • Angiotensin II type 1 receptor blockade attenuates TGF-β-induced failure of muscle regeneration in multiple myopathic states
    • Cohn RD, van Erp C, Habashi JP, Soleimani AA, Klein EC, et al. 2007. Angiotensin II type 1 receptor blockade attenuates TGF-β-induced failure of muscle regeneration in multiple myopathic states. Nat. Med. 13:204-210
    • (2007) Nat. Med. , vol.13 , pp. 204-210
    • Cohn, R.D.1    Van Erp, C.2    Habashi, J.P.3    Soleimani, A.A.4    Klein, E.C.5
  • 117
    • 0036678803 scopus 로고    scopus 로고
    • Release of hepatocyte growth factor from mechanically stretched skeletal muscle satellite cells and role of pH and nitric oxide
    • DOI 10.1091/mbc.E02-01-0062
    • Tatsumi R, Hattori A, Ikeuchi Y, Anderson JE, Allen RE. 2002. Release of hepatocyte growth factor from mechanically stretched skeletal muscle satellite cells and role of pH and nitric oxide. Mol. Biol. Cell 13:2909-2918 (Pubitemid 34907112)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.8 , pp. 2909-2918
    • Tatsumi, R.1    Hattori, A.2    Ikeuchi, Y.3    Anderson, J.E.4    Allen, R.E.5
  • 118
    • 0034071559 scopus 로고    scopus 로고
    • A role for nitric oxide in muscle repair: Nitric oxide-mediated activation of muscle satellite cells
    • Anderson JE. 2000. A role for nitric oxide in muscle repair: nitric oxide-mediated activation of muscle satellite cells. Mol. Biol. Cell 11:1859-1874
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1859-1874
    • Anderson, J.E.1
  • 120
    • 0033838429 scopus 로고    scopus 로고
    • Increased expression of IGF-binding protein-5 in Duchenne muscular dystrophy (DMD) fibroblasts correlates with the fibroblast-induced downregulation of DMD myoblast growth: An in vitro analysis
    • Melone MA, Peluso G, Galderisi U, Petillo O, Cotrufo R. 2000. Increased expression of IGF-binding protein-5 in Duchenne muscular dystrophy (DMD) fibroblasts correlates with the fibroblast-induced downregulation of DMD myoblast growth: an in vitro analysis. J. Cell Physiol. 185:143-153
    • (2000) J. Cell Physiol. , vol.185 , pp. 143-153
    • Melone, M.A.1    Peluso, G.2    Galderisi, U.3    Petillo, O.4    Cotrufo, R.5
  • 122
    • 0036544519 scopus 로고    scopus 로고
    • Muscle-specific expression of insulin-like growth factor I counters muscle decline in mdx mice
    • DOI 10.1083/jcb.200108071
    • Barton ER, Morris L, Musaro A, Rosenthal N, Sweeney HL. 2002. Muscle-specific expression of insulinlike growth factor I counters muscle decline in mdx mice. J. Cell Biol. 157:137-148 (Pubitemid 34847836)
    • (2002) Journal of Cell Biology , vol.157 , Issue.1 , pp. 137-147
    • Barton, E.R.1    Morris, L.2    Musaro, A.3    Rosenthal, N.4    Lee Sweeney, H.5
  • 123
    • 0033060101 scopus 로고    scopus 로고
    • Macrophages enhance muscle satellite cell proliferation and delay their differentiation
    • DOI 10.1002/(SICI)1097-4598(199906)22:6<724::AID-MUS9>3.0.CO;2-O
    • Merly F, Lescaudron L, Rouaud T, Crossin F, Gardahaut MF. 1999. Macrophages enhance muscle satellite cell proliferation and delay their differentiation. Muscle Nerve 22:724-732 (Pubitemid 29256841)
    • (1999) Muscle and Nerve , vol.22 , Issue.6 , pp. 724-732
    • Merly, F.1    Lescaudron, L.2    Rouaud, T.3    Crossin, F.4    Gardahaut, M.F.5
  • 124
    • 0032441093 scopus 로고    scopus 로고
    • Age-associated changes in the response of skeletal muscle cells to exercise and regeneration
    • DOI 10.1111/j.1749-6632.1998.tb09894.x
    • Grounds MD. 1998. Age-associated changes in the response of skeletal muscle cells to exercise and regeneration. Ann. N. Y. Acad. Sci. 854:78-91 (Pubitemid 29022795)
    • (1998) Annals of the New York Academy of Sciences , vol.854 , pp. 78-91
    • Grounds, M.D.1
  • 126
    • 51349122205 scopus 로고    scopus 로고
    • Long-term stem survival of transplanted cells in immunocompetent mice with muscular dystrophy
    • Wallace GQ, Lapidos KA, Kenik JS, McNally EM. 2008. Long-term stem survival of transplanted cells in immunocompetent mice with muscular dystrophy. Am. J. Pathol. 173:792-802
    • (2008) Am. J. Pathol. , vol.173 , pp. 792-802
    • Wallace, G.Q.1    Lapidos, K.A.2    Kenik, J.S.3    McNally, E.M.4
  • 127
    • 0027985787 scopus 로고
    • Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy
    • DOI 10.1038/ng1294-323
    • Bione S, Maestrini E, Rivella S, Mancini M, Regis S, et al. 1994. Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy. Nat. Genet. 8:323-327 (Pubitemid 24375595)
    • (1994) Nature Genetics , vol.8 , Issue.4 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, S.3    Mancini, M.4    Regis, S.5    Romeo, G.6    Toniolo, D.7
  • 129
    • 0034702027 scopus 로고    scopus 로고
    • Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B)
    • Muchir A, Bonne G, Van Der Kooi AJ, van Meegen M, Baas F, et al. 2000. Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B). Hum. Mol. Genet. 9:1453-1459 (Pubitemid 30312494)
    • (2000) Human Molecular Genetics , vol.9 , Issue.9 , pp. 1453-1459
    • Muchir, A.1    Bonne, G.2    Van Der Kool, A.J.3    Van Meegen, M.4    Baas, F.5    Bolhuis, P.A.6    De Visser, M.7    Schwartz, K.8
  • 131
    • 0033518282 scopus 로고    scopus 로고
    • Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease
    • Fatkin D, MacRae C, Sasaki T, Wolff MR, Porcu M, et al. 1999. Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease. N. Engl. J. Med. 341:1715-1724
    • (1999) N. Engl. J. Med. , vol.341 , pp. 1715-1724
    • Fatkin, D.1    MacRae, C.2    Sasaki, T.3    Wolff, M.R.4    Porcu, M.5
  • 132
    • 0010397284 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein
    • DOI 10.1093/hmg/5.6.801
    • Manilal S, Nguyen TM, Sewry CA, Morris GE. 1996. The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein. Hum. Mol. Genet. 5:801-808 (Pubitemid 26171704)
    • (1996) Human Molecular Genetics , vol.5 , Issue.6 , pp. 801-808
    • Manilal, S.1    Nguyen, T.M.2    Sewry, C.A.3    Morris, G.E.4
  • 133
    • 16244370687 scopus 로고    scopus 로고
    • Nuclear lamins: Building blocks of nuclear structure and function
    • Goldman RD, Goldman AE, Shumaker DK. 2005. Nuclear lamins: building blocks of nuclear structure and function. Novartis Found. Symp. 264:3-16
    • (2005) Novartis Found. Symp. , vol.264 , pp. 3-16
    • Goldman, R.D.1    Goldman, A.E.2    Shumaker, D.K.3
  • 136
    • 0037225049 scopus 로고    scopus 로고
    • Expression of lamin a mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy
    • DOI 10.1006/excr.2002.5669
    • Favreau C, Dubosclard E, Ostlund C, Vigouroux C, Capeau J, et al. 2003. Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy. Exp. Cell Res. 282:14-23 (Pubitemid 36062608)
    • (2003) Experimental Cell Research , vol.282 , Issue.1 , pp. 14-23
    • Favreau, C.1    Dubosclard, E.2    Ostlund, C.3    Vigouroux, C.4    Capeau, J.5    Wehnert, M.6    Higuet, D.7    Worman, H.J.8    Courvalin, J.-C.9    Buendia, B.10
  • 138
    • 0035691915 scopus 로고    scopus 로고
    • Nuclear envelope disorganization in fibroblasts from lipodystrophic patients with heterozygous R482Q/W mutations in the lamin A/C gene
    • Vigouroux C, Auclair M, Dubosclard E, Pouchelet M, Capeau J, et al. 2001. Nuclear envelope disorganization in fibroblasts from lipodystrophic patients with heterozygous R482Q/W mutations in the lamin A/C gene. J. Cell Sci. 114:4459-4468 (Pubitemid 34082866)
    • (2001) Journal of Cell Science , vol.114 , Issue.24 , pp. 4459-4468
    • Vigouroux, C.1    Auclair, M.2    Dubosclard, E.3    Pouchelet, M.4    Capeau, J.5    Courvalin, J.-C.6    Buendia, B.7
  • 139
    • 24144481867 scopus 로고    scopus 로고
    • Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells
    • DOI 10.1083/jcb.200502148
    • Lammerding J, Hsiao J, Schulze PC, Kozlov S, Stewart CL, Lee RT. 2005. Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells. J. Cell Biol. 170:781-791 (Pubitemid 41242110)
    • (2005) Journal of Cell Biology , vol.170 , Issue.5 , pp. 781-791
    • Lammerding, J.1    Hsiao, J.2    Schulze, P.C.3    Kozlov, S.4    Stewart, C.L.5    Lee, R.T.6
  • 141
  • 144
    • 32644441628 scopus 로고    scopus 로고
    • Nuclear envelope dystrophies show a transcriptional fingerprint suggesting disruption of Rb-MyoD pathways in muscle regeneration
    • Bakay M, Wang Z, Melcon G, Schiltz L, Xuan J, et al. 2006. Nuclear envelope dystrophies show a transcriptional fingerprint suggesting disruption of Rb-MyoD pathways in muscle regeneration. Brain 129:996-1013
    • (2006) Brain , vol.129 , pp. 996-1013
    • Bakay, M.1    Wang, Z.2    Melcon, G.3    Schiltz, L.4    Xuan, J.5
  • 146
    • 0842347426 scopus 로고    scopus 로고
    • Expression of a Mutant Lamin a that Causes Emery-Dreifuss Muscular Dystrophy Inhibits in Vitro Differentiation of C2C12 Myoblasts
    • DOI 10.1128/MCB.24.4.1481-1492.2004
    • Favreau C, Higuet D, Courvalin JC, Buendia B. 2004. Expression of a mutant lamin A that causes Emery-Dreifuss muscular dystrophy inhibits in vitro differentiation of C2C12 myoblasts. Mol. Cell. Biol. 24:1481-1492 (Pubitemid 38167072)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.4 , pp. 1481-1492
    • Favreau, C.1    Higuet, D.2    Courvalin, J.-C.3    Buendia, B.4
  • 147
    • 14044265165 scopus 로고    scopus 로고
    • Remodelling of the nuclear lamina and nucleoskeleton is required for skeletal muscle differentiation in vitro
    • DOI 10.1242/jcs.01630
    • Markiewicz E, Ledran M, Hutchison CJ. 2005. Remodelling of the nuclear lamina and nucleoskeleton is required for skeletal muscle differentiation in vitro. J. Cell Sci. 118:409-420 (Pubitemid 40277352)
    • (2005) Journal of Cell Science , vol.118 , Issue.2 , pp. 409-420
    • Markiewicz, E.1    Ledran, M.2    Hutchison, C.J.3
  • 148
    • 33748773107 scopus 로고    scopus 로고
    • Laminopathies: Multiple disorders arising from defects in nuclear architecture
    • Parnaik VK, Manju K. 2006. Laminopathies: multiple disorders arising from defects in nuclear architecture. J. Biosci. 31:405-421 (Pubitemid 44411514)
    • (2006) Journal of Biosciences , vol.31 , Issue.3 , pp. 405-421
    • Parnaik, V.K.1    Manju, K.2
  • 150
    • 0033564139 scopus 로고    scopus 로고
    • The transition from proliferation to differentiation is delayed in satellite cells from mice lacking MyoD
    • DOI 10.1006/dbio.1999.9284
    • Yablonka-Reuveni Z, Rudnicki MA, Rivera AJ, Primig M, Anderson JE, Natanson P. 1999. The transition from proliferation to differentiation is delayed in satellite cells from mice lacking MyoD. Dev. Biol. 210:440-455 (Pubitemid 29283015)
    • (1999) Developmental Biology , vol.210 , Issue.2 , pp. 440-455
    • Yablonka-Reuveni, Z.1    Rudnicki, M.A.2    Rivera, A.J.3    Primig, M.4    Anderson, J.E.5    Natanson, P.6
  • 152
    • 0034663199 scopus 로고    scopus 로고
    • -/- satellite cells in single-fiber culture are differentiation defective and MRF4 deficient
    • -/- satellite cells in single-fiber culture are differentiation defective and MRF4 deficient. Dev. Biol. 224:122-137
    • (2000) Dev. Biol. , vol.224 , pp. 122-137
    • Cornelison, D.D.1    Olwin, B.B.2    Rudnicki, M.A.3    Wold, B.J.4


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