메뉴 건너뛰기




Volumn 1804, Issue 9, 2010, Pages 1713-1722

Dystrophin: More than just the sum of its parts

Author keywords

Actin; Coiled coil; Cytoskeleton; Dystrophin; Intermediate filaments; Membrane binding; Membrane phospholipids; Microtubules; Muscular dystrophy; NNOS; Spectrin like repeats

Indexed keywords

ACTIN; CYTOKERATIN 19; DESMIN; DYSTROPHIN; F ACTIN; NEURONAL NITRIC OXIDE SYNTHASE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLSERINE; SPECTRIN; UTROPHIN;

EID: 77955094457     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2010.05.001     Document Type: Review
Times cited : (89)

References (136)
  • 1
    • 0023614271 scopus 로고
    • Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals
    • Koenig M., Hoffman E.P., Bertelson C.J., Monaco A.P., Feener C., Kunkel L.M. Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals. Cell 1987, 50:509-517.
    • (1987) Cell , vol.50 , pp. 509-517
    • Koenig, M.1    Hoffman, E.P.2    Bertelson, C.J.3    Monaco, A.P.4    Feener, C.5    Kunkel, L.M.6
  • 3
    • 33846271135 scopus 로고    scopus 로고
    • Dystrophin, its interactions with other proteins, and implications for muscular dystrophy
    • Ervasti J.M. Dystrophin, its interactions with other proteins, and implications for muscular dystrophy. Biochim. Biophys. Acta 2007, 1772:108-117.
    • (2007) Biochim. Biophys. Acta , vol.1772 , pp. 108-117
    • Ervasti, J.M.1
  • 4
    • 33746766278 scopus 로고    scopus 로고
    • Entries in the Leiden Duchenne muscular dystrophy mutation database: an overview of mutation types and paradoxical cases that confirm the reading-frame rule
    • Aartsma-Rus A., Van Deutekom J.C., Fokkema I.F., Van Ommen G.J., Den Dunnen J.T. Entries in the Leiden Duchenne muscular dystrophy mutation database: an overview of mutation types and paradoxical cases that confirm the reading-frame rule. Muscle Nerve 2006, 34:135-144.
    • (2006) Muscle Nerve , vol.34 , pp. 135-144
    • Aartsma-Rus, A.1    Van Deutekom, J.C.2    Fokkema, I.F.3    Van Ommen, G.J.4    Den Dunnen, J.T.5
  • 8
    • 0023904860 scopus 로고
    • The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein
    • Koenig M., Monaco A.P., Kunkel L.M. The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 1988, 53:219-226.
    • (1988) Cell , vol.53 , pp. 219-226
    • Koenig, M.1    Monaco, A.P.2    Kunkel, L.M.3
  • 9
    • 0025217703 scopus 로고
    • Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility
    • Koenig M., Kunkel L.M. Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility. J. Biol. Chem. 1990, 265:4560-4566.
    • (1990) J. Biol. Chem. , vol.265 , pp. 4560-4566
    • Koenig, M.1    Kunkel, L.M.2
  • 10
    • 0025234309 scopus 로고
    • Structural predictions for the central domain of dystrophin
    • Cross R.A., Stewart M., Kendrick-Jones J. Structural predictions for the central domain of dystrophin. FEBS Lett. 1990, 262:87-92.
    • (1990) FEBS Lett. , vol.262 , pp. 87-92
    • Cross, R.A.1    Stewart, M.2    Kendrick-Jones, J.3
  • 11
    • 0029117231 scopus 로고
    • Dystrophin and utrophin: the missing links!
    • Winder S., Gibson T., Kendrick-Jones J. Dystrophin and utrophin: the missing links!. FEBS Lett. 1995, 369:27-33.
    • (1995) FEBS Lett. , vol.369 , pp. 27-33
    • Winder, S.1    Gibson, T.2    Kendrick-Jones, J.3
  • 12
    • 0030568868 scopus 로고    scopus 로고
    • Characterisation of the dystrophin-related protein utrophin in highly purified skeletal muscle sarcolemma vesicles
    • Ohlendieck K. Characterisation of the dystrophin-related protein utrophin in highly purified skeletal muscle sarcolemma vesicles. Biochim. Biophys. Acta 1996, 1283:215-222.
    • (1996) Biochim. Biophys. Acta , vol.1283 , pp. 215-222
    • Ohlendieck, K.1
  • 16
    • 0026446892 scopus 로고
    • Evolutionary conservation of the dystrophin central rod domain
    • Sherratt T.G., Vulliamy T., Strong P.N. Evolutionary conservation of the dystrophin central rod domain. Biochem. J. 1992, 287:755-799.
    • (1992) Biochem. J. , vol.287 , pp. 755-799
    • Sherratt, T.G.1    Vulliamy, T.2    Strong, P.N.3
  • 17
    • 0024299114 scopus 로고
    • Alpha-Actinins and the DMD protein contain spectrin-like repeats
    • Davison M.D., Critchley D.R. alpha-Actinins and the DMD protein contain spectrin-like repeats. Cell 1988, 52:159-160.
    • (1988) Cell , vol.52 , pp. 159-160
    • Davison, M.D.1    Critchley, D.R.2
  • 19
    • 0029063876 scopus 로고
    • Minimum folding unit of dystrophin rod domain
    • Kahana E., Gratzer W.B. Minimum folding unit of dystrophin rod domain. Biochemistry (Mosc.) 1995, 34:8110-8114.
    • (1995) Biochemistry (Mosc.) , vol.34 , pp. 8110-8114
    • Kahana, E.1    Gratzer, W.B.2
  • 21
    • 0029758344 scopus 로고    scopus 로고
    • Stability of the dystrophin rod domain fold: evidence for nested repeating units
    • Calvert R., Kahana E., Gratzer W.B. Stability of the dystrophin rod domain fold: evidence for nested repeating units. Biophys. J. 1996, 71:1605-1610.
    • (1996) Biophys. J. , vol.71 , pp. 1605-1610
    • Calvert, R.1    Kahana, E.2    Gratzer, W.B.3
  • 22
    • 33646524933 scopus 로고    scopus 로고
    • Structural cooperativity in spectrin type repeats motifs of dystrophin
    • Saadat L., Pittman L., Menhart N. Structural cooperativity in spectrin type repeats motifs of dystrophin. Biochim. Biophys. Acta 2006, 1764:943-954.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 943-954
    • Saadat, L.1    Pittman, L.2    Menhart, N.3
  • 24
    • 53149120329 scopus 로고    scopus 로고
    • Stability of dystrophin STR fragments in relation to junction helicity
    • Mirza A., Menhart N. Stability of dystrophin STR fragments in relation to junction helicity. Biochim. Biophys. Acta 2008, 1784:1301-1309.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1301-1309
    • Mirza, A.1    Menhart, N.2
  • 26
    • 67349085538 scopus 로고    scopus 로고
    • Differential stabilities of alternative exon-skipped rod motifs of dystrophin
    • Ruszczak C., Mirza A., Menhart N. Differential stabilities of alternative exon-skipped rod motifs of dystrophin. Biochim. Biophys. Acta 2009, 1794:921-928.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 921-928
    • Ruszczak, C.1    Mirza, A.2    Menhart, N.3
  • 27
    • 0032561199 scopus 로고    scopus 로고
    • A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction
    • Amann K.J., Renley B.A., Ervasti J.M. A cluster of basic repeats in the dystrophin rod domain binds F-actin through an electrostatic interaction. J. Biol. Chem. 1998, 273:28419-28423.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28419-28423
    • Amann, K.J.1    Renley, B.A.2    Ervasti, J.M.3
  • 28
    • 0033544850 scopus 로고    scopus 로고
    • Utrophin lacks the rod domain actin binding activity of dystrophin
    • Amann K.J., XGuo A.W., Ervasti J.M. Utrophin lacks the rod domain actin binding activity of dystrophin. J. Biol. Chem. 1999, 274:35375-35380.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35375-35380
    • Amann, K.J.1    XGuo, A.W.2    Ervasti, J.M.3
  • 29
    • 33745215797 scopus 로고    scopus 로고
    • Hybrid spectrin type repeats produced by exon-skipping in dystrophin
    • Menhart N. Hybrid spectrin type repeats produced by exon-skipping in dystrophin. Biochim. Biophys. Acta 2006, 1764:993-999.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 993-999
    • Menhart, N.1
  • 30
    • 0030772373 scopus 로고    scopus 로고
    • Site-directed mutagenesis of either the highly conserved Trp-22 or the moderately conserved Trp-95 to a large, hydrophobic residue reduces the thermodynamic stability of a spectrin repeating unit
    • Pantazatos D.P., MacDonald R.I. Site-directed mutagenesis of either the highly conserved Trp-22 or the moderately conserved Trp-95 to a large, hydrophobic residue reduces the thermodynamic stability of a spectrin repeating unit. J. Biol. Chem. 1997, 272:21052-21059.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21052-21059
    • Pantazatos, D.P.1    MacDonald, R.I.2
  • 31
    • 1242319561 scopus 로고    scopus 로고
    • Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer
    • MacDonald R., Cumming J. Stabilities of folding of clustered, two-repeat fragments of spectrin reveal a potential hinge in the human erythroid spectrin tetramer. Proc. Natl. Acad. Sci. USA 2004, 101:1502-1507.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1502-1507
    • MacDonald, R.1    Cumming, J.2
  • 32
    • 1842450320 scopus 로고    scopus 로고
    • Structural insights onto the stability and flexibility of unusual erythroid spectrin repeats
    • Kusunoki H., MacDonald R., Mondragon A. Structural insights onto the stability and flexibility of unusual erythroid spectrin repeats. Structure 2004, 12:645-656.
    • (2004) Structure , vol.12 , pp. 645-656
    • Kusunoki, H.1    MacDonald, R.2    Mondragon, A.3
  • 36
    • 41249094534 scopus 로고    scopus 로고
    • The folding pathway of a single domain in a multidomain protein is not affected by its neighbouring domain
    • Batey S., Clarke J. The folding pathway of a single domain in a multidomain protein is not affected by its neighbouring domain. J. Mol. Biol. 2008, 378:297-301.
    • (2008) J. Mol. Biol. , vol.378 , pp. 297-301
    • Batey, S.1    Clarke, J.2
  • 37
    • 0035799317 scopus 로고    scopus 로고
    • Free energies of urea and thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat
    • MacDonald R., Pozharski E. Free energies of urea and thermal unfolding show that two tandem repeats of spectrin are thermodynamically more stable than a single repeat. Biochemistry (Mosc.) 2001, 40:3974-3984.
    • (2001) Biochemistry (Mosc.) , vol.40 , pp. 3974-3984
    • MacDonald, R.1    Pozharski, E.2
  • 39
    • 0029863942 scopus 로고    scopus 로고
    • The spectrin repeat folds into a three-helix bundle in solution
    • Pascual J., Pfuhl M., Rivas G., Pastore A., Saraste M. The spectrin repeat folds into a three-helix bundle in solution. FEBS Lett. 1996, 383:201-207.
    • (1996) FEBS Lett. , vol.383 , pp. 201-207
    • Pascual, J.1    Pfuhl, M.2    Rivas, G.3    Pastore, A.4    Saraste, M.5
  • 40
    • 0031592935 scopus 로고    scopus 로고
    • Solution structure of spectrin repeat: a left-handed antiparallel triple-helical coiled-coil
    • Pascual J., Pfuhl M., Walther D., Saraste M. Solution structure of spectrin repeat: a left-handed antiparallel triple-helical coiled-coil. J. Mol. Biol. 1997, 273:740-751.
    • (1997) J. Mol. Biol. , vol.273 , pp. 740-751
    • Pascual, J.1    Pfuhl, M.2    Walther, D.3    Saraste, M.4
  • 41
    • 0033588274 scopus 로고    scopus 로고
    • Structures of two repeats of spectrin suggest models of flexibility
    • Grum V.L., Li D., MacDonald R.I., Mondragon A. Structures of two repeats of spectrin suggest models of flexibility. Cell 1999, 98:523-535.
    • (1999) Cell , vol.98 , pp. 523-535
    • Grum, V.L.1    Li, D.2    MacDonald, R.I.3    Mondragon, A.4
  • 43
    • 7444232111 scopus 로고    scopus 로고
    • Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin
    • Kusunoki H., Minasov G., MacDonald R., Mondragon A. Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin. J. Mol. Biol. 2004, 344:495-511.
    • (2004) J. Mol. Biol. , vol.344 , pp. 495-511
    • Kusunoki, H.1    Minasov, G.2    MacDonald, R.3    Mondragon, A.4
  • 45
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the a-actinin rod: molecular basis for cross linking of actin filaments
    • Djinovic-Carugo K., Young P., Gaudel M., Saraste M. Structure of the a-actinin rod: molecular basis for cross linking of actin filaments. Cell 1999, 98:537-546.
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gaudel, M.3    Saraste, M.4
  • 46
    • 0034933167 scopus 로고    scopus 로고
    • Crystal structure of the alpha-actinin rod reveals an extensive torsional twist
    • Ylanne J., Scheffzek K., Young P., Saraste M. Crystal structure of the alpha-actinin rod reveals an extensive torsional twist. Structure 2001, 9:597-604.
    • (2001) Structure , vol.9 , pp. 597-604
    • Ylanne, J.1    Scheffzek, K.2    Young, P.3    Saraste, M.4
  • 48
    • 65849498675 scopus 로고    scopus 로고
    • A two amino-acid mutation encountered in Duchenne muscular dystrophy decreases stability of the R23 spectrin-like repeat of dystrophin
    • Legardinier S., Legrand B., Raguénès-Nicol C., Bondon A., Hardy S., Tascon C., Le Rumeur E., Hubert J.F. A two amino-acid mutation encountered in Duchenne muscular dystrophy decreases stability of the R23 spectrin-like repeat of dystrophin. J. Biol. Chem. 2009, 284:8822-8832.
    • (2009) J. Biol. Chem. , vol.284 , pp. 8822-8832
    • Legardinier, S.1    Legrand, B.2    Raguénès-Nicol, C.3    Bondon, A.4    Hardy, S.5    Tascon, C.6    Le Rumeur, E.7    Hubert, J.F.8
  • 50
    • 0026578765 scopus 로고
    • Proteolytic susceptibility of the central domain in chicken gizzard and skeletal muscle dystrophins
    • Augier N., Leger J., Robert A., Pons F., Leger J.J., Mornet D. Proteolytic susceptibility of the central domain in chicken gizzard and skeletal muscle dystrophins. Biochim. Biophys. Acta 1992, 1138:297-304.
    • (1992) Biochim. Biophys. Acta , vol.1138 , pp. 297-304
    • Augier, N.1    Leger, J.2    Robert, A.3    Pons, F.4    Leger, J.J.5    Mornet, D.6
  • 51
    • 0030795572 scopus 로고    scopus 로고
    • In vitro expressed dystrophin fragments do not associate with each other
    • Chan Y.M., Kunkel L.M. In vitro expressed dystrophin fragments do not associate with each other. FEBS Lett. 1997, 410:153-159.
    • (1997) FEBS Lett. , vol.410 , pp. 153-159
    • Chan, Y.M.1    Kunkel, L.M.2
  • 52
    • 0029804981 scopus 로고    scopus 로고
    • A new model for the interaction of dystrophin with F-actin
    • Rybakova I., Amann K., Ervasti J. A new model for the interaction of dystrophin with F-actin. J. Cell Biol. 1996, 135:661-672.
    • (1996) J. Cell Biol. , vol.135 , pp. 661-672
    • Rybakova, I.1    Amann, K.2    Ervasti, J.3
  • 53
    • 0030695947 scopus 로고    scopus 로고
    • Dystrophin-glycoprotein complex is monomeric and stabilizes actin filaments in vitro through a lateral association
    • Rybakova I., Ervasti J. Dystrophin-glycoprotein complex is monomeric and stabilizes actin filaments in vitro through a lateral association. J. Biol. Chem. 1997, 272:28771-28778.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28771-28778
    • Rybakova, I.1    Ervasti, J.2
  • 54
    • 33744507184 scopus 로고    scopus 로고
    • Dystrophin and utrophin bind actin through distinct modes of contact
    • Rybakova I., Humston J., Sonneman K., Ervasti J. Dystrophin and utrophin bind actin through distinct modes of contact. J. Biol. Chem. 2006, 281:9996-10001.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9996-10001
    • Rybakova, I.1    Humston, J.2    Sonneman, K.3    Ervasti, J.4
  • 57
    • 0037458618 scopus 로고    scopus 로고
    • Interaction of dystrophin rod domain with membrane phospholipids: evidence of a close proximity between tryptophan residues and lipids
    • Le Rumeur E., Fichou Y., Pottier S., Gaboriau F., Rondeau-Mouro C., Vincent M., Gallay J., Bondon A. Interaction of dystrophin rod domain with membrane phospholipids: evidence of a close proximity between tryptophan residues and lipids. J. Biol. Chem. 2003, 278:5993-6001.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5993-6001
    • Le Rumeur, E.1    Fichou, Y.2    Pottier, S.3    Gaboriau, F.4    Rondeau-Mouro, C.5    Vincent, M.6    Gallay, J.7    Bondon, A.8
  • 59
    • 0345832247 scopus 로고    scopus 로고
    • Phosphatidylserine binding sites in erythroid spectrin: location and implications for membrane stability
    • An X., Guo X., Sum H., Morrow J., Gratzer W., Mohandas N. Phosphatidylserine binding sites in erythroid spectrin: location and implications for membrane stability. Biochemistry (Mosc.) 2004, 43:310-315.
    • (2004) Biochemistry (Mosc.) , vol.43 , pp. 310-315
    • An, X.1    Guo, X.2    Sum, H.3    Morrow, J.4    Gratzer, W.5    Mohandas, N.6
  • 60
    • 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 A.G. Duchenne dystrophy: electron microscopic findings pointing to a basic or early abnormality in the plasma membrane of the muscle fiber. Neurology 1975, 25:1111-1120.
    • (1975) Neurology , vol.25 , pp. 1111-1120
    • Mokri, B.1    Engel, A.G.2
  • 61
    • 0028907196 scopus 로고
    • Extent of shock-induced membrane leakage in human and mouse myotubes depends on dystrophin
    • Menke A., Jockusch H. Extent of shock-induced membrane leakage in human and mouse myotubes depends on dystrophin. J. Cell Sci. 1995, 108:727-733.
    • (1995) J. Cell Sci. , vol.108 , pp. 727-733
    • Menke, A.1    Jockusch, H.2
  • 62
    • 0030783172 scopus 로고    scopus 로고
    • Animal models for muscular dystrophy show different patterns of sarcolemmal disruption
    • Straub V., Rafael J.A., Chamberlain J.S., Campbell K.P. Animal models for muscular dystrophy show different patterns of sarcolemmal disruption. J. Cell Biol. 1997, 139:375-385.
    • (1997) J. Cell Biol. , vol.139 , pp. 375-385
    • Straub, V.1    Rafael, J.A.2    Chamberlain, J.S.3    Campbell, K.P.4
  • 63
    • 0026340589 scopus 로고
    • Mechanical properties of normal and mdx mouse sarcolemma: bearing on function of dystrophin
    • Hutter O., Burton F., Bovell D. Mechanical properties of normal and mdx mouse sarcolemma: bearing on function of dystrophin. J. Muscle Res. Cell Motil. 1991, 12:585-589.
    • (1991) J. Muscle Res. Cell Motil. , vol.12 , pp. 585-589
    • Hutter, O.1    Burton, F.2    Bovell, D.3
  • 65
    • 0036485777 scopus 로고    scopus 로고
    • Muscle lesions associated with dystrophin deficiency in neonatal golden retriever puppies
    • Nguyen F., Cherel Y., Guigand L., Goubault-Leroux I., Wyers M. Muscle lesions associated with dystrophin deficiency in neonatal golden retriever puppies. J. Comp. Pathol. 2002, 126:100-108.
    • (2002) J. Comp. Pathol. , vol.126 , pp. 100-108
    • Nguyen, F.1    Cherel, Y.2    Guigand, L.3    Goubault-Leroux, I.4    Wyers, M.5
  • 66
    • 0026479080 scopus 로고
    • Prevention of myonecrosis in mdx mice: effect of immobilization by the local tetanus method
    • Mizuno Y. Prevention of myonecrosis in mdx mice: effect of immobilization by the local tetanus method. Brain Dev. 1992, 14:319-322.
    • (1992) Brain Dev. , vol.14 , pp. 319-322
    • Mizuno, Y.1
  • 67
    • 0032981179 scopus 로고    scopus 로고
    • Hindlimb immobilization applied to 21-day-old mdx mice prevents the occurrence of muscle degeneration
    • Mokhtarian A., Lefaucheur J.P., Even P.C., Sebille A. Hindlimb immobilization applied to 21-day-old mdx mice prevents the occurrence of muscle degeneration. J. Appl. Physiol. 1999, 86:924-931.
    • (1999) J. Appl. Physiol. , vol.86 , pp. 924-931
    • Mokhtarian, A.1    Lefaucheur, J.P.2    Even, P.C.3    Sebille, A.4
  • 68
    • 28444431514 scopus 로고    scopus 로고
    • Mutation in the delta-subunit of the nAChR suppresses the muscle defects caused by lack of Dystrophin
    • Etard C., Behra M., Ertzer R., Fischer N., Jesuthasan S., Blader P., Geisler R., Strahle U. Mutation in the delta-subunit of the nAChR suppresses the muscle defects caused by lack of Dystrophin. Dev. Dyn. 2005, 234:1016-1025.
    • (2005) Dev. Dyn. , vol.234 , pp. 1016-1025
    • Etard, C.1    Behra, M.2    Ertzer, R.3    Fischer, N.4    Jesuthasan, S.5    Blader, P.6    Geisler, R.7    Strahle, U.8
  • 69
    • 33947258069 scopus 로고    scopus 로고
    • Pathophysiology of duchenne muscular dystrophy: current hypotheses
    • Deconinck N., Dan B. Pathophysiology of duchenne muscular dystrophy: current hypotheses. Pediatr. Neurol. 2007, 36:1-7.
    • (2007) Pediatr. Neurol. , vol.36 , pp. 1-7
    • Deconinck, N.1    Dan, B.2
  • 70
    • 0038190993 scopus 로고    scopus 로고
    • Costameres: the Achilles' heel of Herculean muscle
    • Ervasti J.M. Costameres: the Achilles' heel of Herculean muscle. J. Biol. Chem. 2003, 278:13591-13594.
    • (2003) J. Biol. Chem. , vol.278 , pp. 13591-13594
    • Ervasti, J.M.1
  • 71
    • 0035069134 scopus 로고    scopus 로고
    • Molecular basis of mechanotransduction in living cells
    • Hamill O., Martinac B. Molecular basis of mechanotransduction in living cells. Physiol. Rev. 2001, 81:685-740.
    • (2001) Physiol. Rev. , vol.81 , pp. 685-740
    • Hamill, O.1    Martinac, B.2
  • 72
    • 0035344650 scopus 로고    scopus 로고
    • Cell control by membrane-cytoskeleton adhesion
    • Sheetz M.P. Cell control by membrane-cytoskeleton adhesion. Nat. Rev. Mol. Cell Biol. 2001, 2:392-396.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 392-396
    • Sheetz, M.P.1
  • 73
    • 0029916311 scopus 로고    scopus 로고
    • Tensile strength and dilatational elasticity of giant sarcolemmal vesicles shed from rabbit muscle
    • Nichol J.A., Hutter O.F. Tensile strength and dilatational elasticity of giant sarcolemmal vesicles shed from rabbit muscle. J. Physiol. 1996, 493(Pt 1):187-198.
    • (1996) J. Physiol. , vol.493 , Issue.PART. 1 , pp. 187-198
    • Nichol, J.A.1    Hutter, O.F.2
  • 74
    • 33646555466 scopus 로고    scopus 로고
    • Protein-lipid interactions and surface activity in the pulmonary surfactant system
    • Serrano A.G., Perez-Gil J. Protein-lipid interactions and surface activity in the pulmonary surfactant system. Chem. Phys. Lipids 2006, 141:105-118.
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 105-118
    • Serrano, A.G.1    Perez-Gil, J.2
  • 75
    • 0037133206 scopus 로고    scopus 로고
    • Identification of a functional role for lipid asymmetry in biological membranes: phosphatidylserine - skeletal protein interactions modulate membrane stability
    • Manno S., Takakuwa Y., Mohandas N. Identification of a functional role for lipid asymmetry in biological membranes: phosphatidylserine - skeletal protein interactions modulate membrane stability. Proc. Natl. Acad. Sci. USA 2002, 99:1943-1948.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 1943-1948
    • Manno, S.1    Takakuwa, Y.2    Mohandas, N.3
  • 76
    • 33846383092 scopus 로고    scopus 로고
    • Force balance and membrane shedding at the red-blood-cell surface
    • Sens P., Gov N. Force balance and membrane shedding at the red-blood-cell surface. Phys. Rev. Lett. 2007, 98:018102.
    • (2007) Phys. Rev. Lett. , vol.98 , pp. 018102
    • Sens, P.1    Gov, N.2
  • 77
    • 0032876283 scopus 로고    scopus 로고
    • Characteristics of a membrane reservoir buffering membrane tension
    • Raucher D., Sheetz M.P. Characteristics of a membrane reservoir buffering membrane tension. Biophys. J. 1999, 77:1992-2002.
    • (1999) Biophys. J. , vol.77 , pp. 1992-2002
    • Raucher, D.1    Sheetz, M.P.2
  • 79
    • 0016754249 scopus 로고
    • The relative contributions of the folds and caveolae to the surface membrane of frog skeletal muscle fibres at different sarcomere lengths
    • Dulhunty A.F., Franzini-Armstrong C. The relative contributions of the folds and caveolae to the surface membrane of frog skeletal muscle fibres at different sarcomere lengths. J. Physiol. 1975, 250:513-539.
    • (1975) J. Physiol. , vol.250 , pp. 513-539
    • Dulhunty, A.F.1    Franzini-Armstrong, C.2
  • 80
    • 0018845082 scopus 로고
    • Quantitative studies on plasmalemmal folds and caveolae of rabbit ventricular myocardial cells
    • Levin K.R., Page E. Quantitative studies on plasmalemmal folds and caveolae of rabbit ventricular myocardial cells. Circ. Res. 1980, 46:244-255.
    • (1980) Circ. Res. , vol.46 , pp. 244-255
    • Levin, K.R.1    Page, E.2
  • 82
    • 57049168054 scopus 로고    scopus 로고
    • Molecular and cellular adaptations to chronic myotendinous strain injury in mdx mice expressing a truncated dystrophin
    • Banks G.B., Combs A.C., Chamberlain J.R., Chamberlain J.S. Molecular and cellular adaptations to chronic myotendinous strain injury in mdx mice expressing a truncated dystrophin. Hum. Mol. Genet. 2008, 17:3975-3986.
    • (2008) Hum. Mol. Genet. , vol.17 , pp. 3975-3986
    • Banks, G.B.1    Combs, A.C.2    Chamberlain, J.R.3    Chamberlain, J.S.4
  • 83
    • 62749156048 scopus 로고    scopus 로고
    • Truncated dystrophins can influence neuromuscular synapse structure
    • Banks G.B., Chamberlain J.S., Froehner S.C. Truncated dystrophins can influence neuromuscular synapse structure. Mol. Cell. Neurosci. 2009, 40:433-441.
    • (2009) Mol. Cell. Neurosci. , vol.40 , pp. 433-441
    • Banks, G.B.1    Chamberlain, J.S.2    Froehner, S.C.3
  • 84
    • 17444415361 scopus 로고    scopus 로고
    • Spectrin, alpha-actinin, and dystrophin
    • Broderick M.J., Winder S.J. Spectrin, alpha-actinin, and dystrophin. Adv. Protein Chem. 2005, 70:203-246.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 203-246
    • Broderick, M.J.1    Winder, S.J.2
  • 85
    • 0034605070 scopus 로고    scopus 로고
    • The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin
    • Rybakova I.N., Patel J.R., Ervasti J.M. The dystrophin complex forms a mechanically strong link between the sarcolemma and costameric actin. J. Cell Biol. 2000, 150:1209-1214.
    • (2000) J. Cell Biol. , vol.150 , pp. 1209-1214
    • Rybakova, I.N.1    Patel, J.R.2    Ervasti, J.M.3
  • 86
    • 0028347405 scopus 로고
    • Nebulin, a helical actin binding protein
    • Pfuhl M., Winder S.J., Pastore A. Nebulin, a helical actin binding protein. EMBO J. 1994, 13:1782-1789.
    • (1994) EMBO J. , vol.13 , pp. 1782-1789
    • Pfuhl, M.1    Winder, S.J.2    Pastore, A.3
  • 88
    • 0035999982 scopus 로고    scopus 로고
    • Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin- deficient muscle
    • Rybakova I.N., Patel J.R., Davies K.E., Yurchenco P.D., Ervasti J.M. Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin- deficient muscle. Mol. Biol. Cell 2002, 13:1512-1521.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 1512-1521
    • Rybakova, I.N.1    Patel, J.R.2    Davies, K.E.3    Yurchenco, P.D.4    Ervasti, J.M.5
  • 90
    • 0028990365 scopus 로고
    • NguyenthiMan, G.E. Morris, The N-terminal half of dystrophin is protected from proteolysis in situ
    • Hori S., Ohtani S. NguyenthiMan, G.E. Morris, The N-terminal half of dystrophin is protected from proteolysis in situ. Biochem. Biophys. Res. Commun. 1995, 209:1062-1067.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 1062-1067
    • Hori, S.1    Ohtani, S.2
  • 91
    • 33747854588 scopus 로고    scopus 로고
    • Cytoplasmic gamma-actin is not required for skeletal muscle development but its absence leads to a progressive myopathy
    • Sonnemann K.J., Fitzsimons D.P., Patel J.R., Liu Y., Schneider M.F., Moss R.L., Ervasti J.M. Cytoplasmic gamma-actin is not required for skeletal muscle development but its absence leads to a progressive myopathy. Dev. Cell 2006, 11:387-397.
    • (2006) Dev. Cell , vol.11 , pp. 387-397
    • Sonnemann, K.J.1    Fitzsimons, D.P.2    Patel, J.R.3    Liu, Y.4    Schneider, M.F.5    Moss, R.L.6    Ervasti, J.M.7
  • 92
    • 33645782024 scopus 로고    scopus 로고
    • Cytoplasmic gamma-actin contributes to a compensatory remodeling response in dystrophin-deficient muscle
    • Hanft L.M., Rybakova I.N., Patel J.R., Rafael-Fortney J.A., Ervasti J.M. Cytoplasmic gamma-actin contributes to a compensatory remodeling response in dystrophin-deficient muscle. Proc. Natl. Acad. Sci. USA 2006, 103:5385-5390.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 5385-5390
    • Hanft, L.M.1    Rybakova, I.N.2    Patel, J.R.3    Rafael-Fortney, J.A.4    Ervasti, J.M.5
  • 95
    • 24344453799 scopus 로고    scopus 로고
    • Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19
    • Stone M.R., O'Neill A., Catino D., Bloch R.J. Specific interaction of the actin-binding domain of dystrophin with intermediate filaments containing keratin 19. Mol. Biol. Cell 2005, 16:4280-4293.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4280-4293
    • Stone, M.R.1    O'Neill, A.2    Catino, D.3    Bloch, R.J.4
  • 97
    • 0028914964 scopus 로고
    • Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage
    • Campbell K.P. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 1995, 80:675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 98
    • 0032590188 scopus 로고    scopus 로고
    • Nitric oxide synthase in skeletal muscle fibers: a signaling component of the dystrophin-glycoprotein complex
    • Grozdanovic Z., Baumgarten H.G. Nitric oxide synthase in skeletal muscle fibers: a signaling component of the dystrophin-glycoprotein complex. Histol. Histopathol. 1999, 14:243-256.
    • (1999) Histol. Histopathol. , vol.14 , pp. 243-256
    • Grozdanovic, Z.1    Baumgarten, H.G.2
  • 101
    • 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 S.A., Iannaccone S.T., Stull J.T., Thomas G.D., Victor R.G. Functional muscle ischemia in neuronal nitric oxide synthase-deficient skeletal muscle of children with Duchenne muscular dystrophy. Proc. Natl. Acad. Sci. USA 2000, 97:13818-13823.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13818-13823
    • Sander, M.1    Chavoshan, B.2    Harris, S.A.3    Iannaccone, S.T.4    Stull, J.T.5    Thomas, G.D.6    Victor, R.G.7
  • 102
    • 58149284090 scopus 로고    scopus 로고
    • The dynamics of the nitric oxide release-transient from stretched muscle cells
    • Wozniak A.C., Anderson J.E. The dynamics of the nitric oxide release-transient from stretched muscle cells. Int. J. Biochem. Cell Biol. 2009, 41:625-631.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 625-631
    • Wozniak, A.C.1    Anderson, J.E.2
  • 104
    • 7044223308 scopus 로고    scopus 로고
    • Absence of neuronal nitric oxide synthase (nNOS) as a pathological marker for the diagnosis of Becker muscular dystrophy with rod domain deletions
    • Torelli S., Brown S.C., Jimenez-Mallebrera C., Feng L., Muntoni F., Sewry C.A. Absence of neuronal nitric oxide synthase (nNOS) as a pathological marker for the diagnosis of Becker muscular dystrophy with rod domain deletions. Neuropathol. Appl. Neurobiol. 2004, 30:540-545.
    • (2004) Neuropathol. Appl. Neurobiol. , vol.30 , pp. 540-545
    • Torelli, S.1    Brown, S.C.2    Jimenez-Mallebrera, C.3    Feng, L.4    Muntoni, F.5    Sewry, C.A.6
  • 105
    • 0030914424 scopus 로고    scopus 로고
    • Mini-dystrophin gene transfer in mdx4cv diaphragm muscle fibers increases sarcolemmal stability
    • Decrouy A., Renaud J.M., Davis H.L., Lunde J.A., Dickson G., Jasmin B.J. Mini-dystrophin gene transfer in mdx4cv diaphragm muscle fibers increases sarcolemmal stability. Gene Ther. 1997, 4:401-408.
    • (1997) Gene Ther. , vol.4 , pp. 401-408
    • Decrouy, A.1    Renaud, J.M.2    Davis, H.L.3    Lunde, J.A.4    Dickson, G.5    Jasmin, B.J.6
  • 106
    • 0035494421 scopus 로고    scopus 로고
    • In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4
    • Adams M.E., Mueller H.A., Froehner S.C. In vivo requirement of the alpha-syntrophin PDZ domain for the sarcolemmal localization of nNOS and aquaporin-4. J. Cell Biol. 2001, 155:113-122.
    • (2001) J. Cell Biol. , vol.155 , pp. 113-122
    • Adams, M.E.1    Mueller, H.A.2    Froehner, S.C.3
  • 107
    • 39449115511 scopus 로고    scopus 로고
    • Differential targeting of nNOS and AQP4 to dystrophin-deficient sarcolemma by membrane-directed alpha-dystrobrevin
    • Adams M.E., Tesch Y., Percival J.M., Albrecht D.E., Conhaim J.I., Anderson K., Froehner S.C. Differential targeting of nNOS and AQP4 to dystrophin-deficient sarcolemma by membrane-directed alpha-dystrobrevin. J. Cell Sci. 2008, 121:48-54.
    • (2008) J. Cell Sci. , vol.121 , pp. 48-54
    • Adams, M.E.1    Tesch, Y.2    Percival, J.M.3    Albrecht, D.E.4    Conhaim, J.I.5    Anderson, K.6    Froehner, S.C.7
  • 108
    • 65649111197 scopus 로고    scopus 로고
    • Dystrophins carrying spectrin-like repeats 16 and 17 anchor nNOS to the sarcolemma and enhance exercise performance in a mouse model of muscular dystrophy
    • Lai Y., Thomas G.D., Yue Y., Yang H.T., Li D., Long C., Judge L., Bostick B., Chamberlain J.S., Terjung R.L., Duan D. Dystrophins carrying spectrin-like repeats 16 and 17 anchor nNOS to the sarcolemma and enhance exercise performance in a mouse model of muscular dystrophy. J. Clin. Investig. 2009, 119:624-635.
    • (2009) J. Clin. Investig. , vol.119 , pp. 624-635
    • Lai, Y.1    Thomas, G.D.2    Yue, Y.3    Yang, H.T.4    Li, D.5    Long, C.6    Judge, L.7    Bostick, B.8    Chamberlain, J.S.9    Terjung, R.L.10    Duan, D.11
  • 110
    • 0023614188 scopus 로고
    • Dystrophin: the protein product of the Duchenne muscular dystrophy locus
    • Hoffman E.P., Brown R.H., Kunkel L.M. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 1987, 51:919-928.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown, R.H.2    Kunkel, L.M.3
  • 111
    • 0023718118 scopus 로고
    • An explanation for the phenotypic differences between patients bearing partial deletions of the DMD locus
    • Monaco A., Bertelson C., Liechti-Gallati S., Moser H., Kunkel L. An explanation for the phenotypic differences between patients bearing partial deletions of the DMD locus. Genomics 1988, 2:90-95.
    • (1988) Genomics , vol.2 , pp. 90-95
    • Monaco, A.1    Bertelson, C.2    Liechti-Gallati, S.3    Moser, H.4    Kunkel, L.5
  • 113
    • 58749101371 scopus 로고    scopus 로고
    • The value of mammalian models for duchenne muscular dystrophy in developing therapeutic strategies
    • Banks G.B., Chamberlain J.S. The value of mammalian models for duchenne muscular dystrophy in developing therapeutic strategies. Curr. Top. Dev. Biol. 2008, 84:431-453.
    • (2008) Curr. Top. Dev. Biol. , vol.84 , pp. 431-453
    • Banks, G.B.1    Chamberlain, J.S.2
  • 114
    • 33645987938 scopus 로고    scopus 로고
    • Restoration of all dystrophin protein interactions by functional domains in trans does not rescue dystrophy
    • Gardner K., Kearney J., Edwards J., Rafael-Fortney J. Restoration of all dystrophin protein interactions by functional domains in trans does not rescue dystrophy. Gene Ther. 2005, 13:744-751.
    • (2005) Gene Ther. , vol.13 , pp. 744-751
    • Gardner, K.1    Kearney, J.2    Edwards, J.3    Rafael-Fortney, J.4
  • 115
    • 0028243082 scopus 로고
    • Independent localization of dystrophin N- and C-terminal regions to the sarcolemma of mdx mouse myofibres in vivo
    • Dunckley M.G., Wells K.E., Piper T.A., Wells D.J., Dickson G. Independent localization of dystrophin N- and C-terminal regions to the sarcolemma of mdx mouse myofibres in vivo. J. Cell Sci. 1994, 107(Pt 6):1469-1475.
    • (1994) J. Cell Sci. , vol.107 , Issue.PART 6 , pp. 1469-1475
    • Dunckley, M.G.1    Wells, K.E.2    Piper, T.A.3    Wells, D.J.4    Dickson, G.5
  • 116
    • 0026587401 scopus 로고
    • A Truncated Dystrophin Lacking the C-Terminal Domains Is Localized at the Muscle Membrane
    • Helliwell T., Ellis J., Mountford R., Appleton R., Morris G. A Truncated Dystrophin Lacking the C-Terminal Domains Is Localized at the Muscle Membrane. Am. J. Hum. Genet. 1992, 50:508-514.
    • (1992) Am. J. Hum. Genet. , vol.50 , pp. 508-514
    • Helliwell, T.1    Ellis, J.2    Mountford, R.3    Appleton, R.4    Morris, G.5
  • 117
    • 0141760313 scopus 로고    scopus 로고
    • Proteasome inhibitor (MG-132) treatment of mdx mice rescues the expression and membrane localization of dystrophin and dystrophin-associated proteins
    • Bonucelli G., Sotgia F., Schubert W., Park D., Frank P., Woodman S., Insabato L., Cammer M., Minetti C., Lisanti M. Proteasome inhibitor (MG-132) treatment of mdx mice rescues the expression and membrane localization of dystrophin and dystrophin-associated proteins. Am. J. Pathol. 2003, 163:1663-1675.
    • (2003) Am. J. Pathol. , vol.163 , pp. 1663-1675
    • Bonucelli, G.1    Sotgia, F.2    Schubert, W.3    Park, D.4    Frank, P.5    Woodman, S.6    Insabato, L.7    Cammer, M.8    Minetti, C.9    Lisanti, M.10
  • 119
    • 0026049619 scopus 로고
    • Is the carboxyl-terminus of dystrophin required for membrane association? A novel, severe case of Duchenne muscular dystrophy
    • Hoffman E., Carlos P., Garcia A., Chamberlain J., Angelini P.C., Lupski J., Fenwick R. Is the carboxyl-terminus of dystrophin required for membrane association? A novel, severe case of Duchenne muscular dystrophy. Ann. Neurol. 1991, 30:605-610.
    • (1991) Ann. Neurol. , vol.30 , pp. 605-610
    • Hoffman, E.1    Carlos, P.2    Garcia, A.3    Chamberlain, J.4    Angelini, P.C.5    Lupski, J.6    Fenwick, R.7
  • 121
    • 0028833771 scopus 로고
    • Frameshift deletions of exons 3-7 and revertant fibers in Duchenne muscular dystrophy: mechanisms of dystrophin production
    • Winnard A.V., Mendell J.R., Prior T.W., Florence J., Burghes A.H. Frameshift deletions of exons 3-7 and revertant fibers in Duchenne muscular dystrophy: mechanisms of dystrophin production. Am. J. Hum. Genet. 1995, 56:158-166.
    • (1995) Am. J. Hum. Genet. , vol.56 , pp. 158-166
    • Winnard, A.V.1    Mendell, J.R.2    Prior, T.W.3    Florence, J.4    Burghes, A.H.5
  • 122
    • 0029825063 scopus 로고    scopus 로고
    • Transgenic mdx mice expressing dystrophin with a deletion in the actin- binding domain display a "mild Becker" phenotype
    • Corrado K., Rafael J.A., Mills P.L., Cole N.M., Faulkner J.A., Wang K., Chamberlain J.S. Transgenic mdx mice expressing dystrophin with a deletion in the actin- binding domain display a "mild Becker" phenotype. J. Cell Biol. 1996, 134:873-884.
    • (1996) J. Cell Biol. , vol.134 , pp. 873-884
    • Corrado, K.1    Rafael, J.A.2    Mills, P.L.3    Cole, N.M.4    Faulkner, J.A.5    Wang, K.6    Chamberlain, J.S.7
  • 123
    • 0028134623 scopus 로고
    • Dp71 can restore the dystrophin-associated glycoprotein complex in muscle but fails to prevent dystrophy
    • Cox G.A., Sunada Y., Campbell K.P., Chamberlain J.S. Dp71 can restore the dystrophin-associated glycoprotein complex in muscle but fails to prevent dystrophy. Nat. Genet. 1994, 8:333-339.
    • (1994) Nat. Genet. , vol.8 , pp. 333-339
    • Cox, G.A.1    Sunada, Y.2    Campbell, K.P.3    Chamberlain, J.S.4
  • 124
    • 0036566558 scopus 로고    scopus 로고
    • Expression of Dp260 in muscle tethers the actin cytoskeleton to the dystrophin-glycoprotein complex and partially prevents dystrophy
    • Warner L., DelloRusso C., Crawford R., Rybakova I., Patel J., Ervasti J., Chamberlain J. Expression of Dp260 in muscle tethers the actin cytoskeleton to the dystrophin-glycoprotein complex and partially prevents dystrophy. Hum. Mol. Genet. 2002, 11:1095-1105.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 1095-1105
    • Warner, L.1    DelloRusso, C.2    Crawford, R.3    Rybakova, I.4    Patel, J.5    Ervasti, J.6    Chamberlain, J.7
  • 126
    • 0034610364 scopus 로고    scopus 로고
    • Adeno-associated virus vector carrying human minidystrophin genes effectively ameliorates muscular dystrophy in mdx mouse model
    • Wang B., Li J., Xiao X. Adeno-associated virus vector carrying human minidystrophin genes effectively ameliorates muscular dystrophy in mdx mouse model. Proc. Natl. Acad. Sci. USA 2000, 97:13714-13719.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13714-13719
    • Wang, B.1    Li, J.2    Xiao, X.3
  • 127
    • 0036385643 scopus 로고    scopus 로고
    • Adeno-associated virus vector-mediated minidystrophin gene therapy improves dystrophic muscle contractile function in mdx mice
    • Watchko J., O'Day T., Wang B., Zhou L., Tang Y., Li J., Xiao X. Adeno-associated virus vector-mediated minidystrophin gene therapy improves dystrophic muscle contractile function in mdx mice. Hum. Gene Ther. 2002, 13:1451-1460.
    • (2002) Hum. Gene Ther. , vol.13 , pp. 1451-1460
    • Watchko, J.1    O'Day, T.2    Wang, B.3    Zhou, L.4    Tang, Y.5    Li, J.6    Xiao, X.7
  • 129
    • 33646675371 scopus 로고    scopus 로고
    • Dissecting the signaling and mechanical functions of the dystrophin-glycoprotein complex
    • Judge L.M., Haraguchiln M., Chamberlain J.S. Dissecting the signaling and mechanical functions of the dystrophin-glycoprotein complex. J. Cell Sci. 2006, 119:1537-1546.
    • (2006) J. Cell Sci. , vol.119 , pp. 1537-1546
    • Judge, L.M.1    Haraguchiln, M.2    Chamberlain, J.S.3
  • 130
    • 12744269885 scopus 로고    scopus 로고
    • Adeno-associated virus-mediated microdystrophin expression protects young mdx muscle from contraction-induced injury
    • Liu M., Yue Y., Harper S., Grange R., Chamberlain J., Duan D. Adeno-associated virus-mediated microdystrophin expression protects young mdx muscle from contraction-induced injury. Mol. Ther. 2005, 11:245-256.
    • (2005) Mol. Ther. , vol.11 , pp. 245-256
    • Liu, M.1    Yue, Y.2    Harper, S.3    Grange, R.4    Chamberlain, J.5    Duan, D.6
  • 132
    • 41149172666 scopus 로고    scopus 로고
    • Systemic microdystrophin gene delivery improves skeletal muscle structure and function in old dystrophic mdx mice
    • Gregorevic P., Blankinship M.J., Allen J.M., Chamberlain J.S. Systemic microdystrophin gene delivery improves skeletal muscle structure and function in old dystrophic mdx mice. Mol. Ther. 2008, 16:657-664.
    • (2008) Mol. Ther. , vol.16 , pp. 657-664
    • Gregorevic, P.1    Blankinship, M.J.2    Allen, J.M.3    Chamberlain, J.S.4
  • 133
    • 34249276065 scopus 로고    scopus 로고
    • Sustained AAV-mediated dystrophin expression in a canine model of Duchenne muscular dystrophy with a brief course of immunosuppression
    • Wang Z., Kuhr C.S., Allen J.M., Blankinship M., Gregorevic P., Chamberlain J.S., Tapscott S.J., Storb R. Sustained AAV-mediated dystrophin expression in a canine model of Duchenne muscular dystrophy with a brief course of immunosuppression. Mol. Ther. 2007, 15:1160-1166.
    • (2007) Mol. Ther. , vol.15 , pp. 1160-1166
    • Wang, Z.1    Kuhr, C.S.2    Allen, J.M.3    Blankinship, M.4    Gregorevic, P.5    Chamberlain, J.S.6    Tapscott, S.J.7    Storb, R.8
  • 134
    • 34548419653 scopus 로고    scopus 로고
    • Functional capacity of dystrophins carrying deletions in the N-terminal actin-binding domain
    • Banks G.B., Gregorevic P., Allen J.M., Finn E.E., Chamberlain J.S. Functional capacity of dystrophins carrying deletions in the N-terminal actin-binding domain. Hum. Mol. Genet. 2007, 16:2105-2113.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 2105-2113
    • Banks, G.B.1    Gregorevic, P.2    Allen, J.M.3    Finn, E.E.4    Chamberlain, J.S.5
  • 135
    • 63349112286 scopus 로고    scopus 로고
    • Systemic human minidystrophin gene transfer improves functions and life span of dystrophin and dystrophin/utrophin-deficient mice
    • Wang B., Li J., Fu F.H., Xiao X. Systemic human minidystrophin gene transfer improves functions and life span of dystrophin and dystrophin/utrophin-deficient mice. J. Orthop. Res. 2009, 27:421-426.
    • (2009) J. Orthop. Res. , vol.27 , pp. 421-426
    • Wang, B.1    Li, J.2    Fu, F.H.3    Xiao, X.4
  • 136
    • 33745012208 scopus 로고    scopus 로고
    • Mini-dystrophin efficiently incorporates into the dystrophin protein complex in living cells
    • Draviam R.A., Wang B., Li J., Xiao X., Watkins S.C. Mini-dystrophin efficiently incorporates into the dystrophin protein complex in living cells. J. Muscle Res. Cell Motil. 2006, 27:53-67.
    • (2006) J. Muscle Res. Cell Motil. , vol.27 , pp. 53-67
    • Draviam, R.A.1    Wang, B.2    Li, J.3    Xiao, X.4    Watkins, S.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.