메뉴 건너뛰기




Volumn 30, Issue 7-8, 2009, Pages 267-279

Proteomic profiling of x-linked muscular dystrophy

Author keywords

Duchenne muscular dystrophy; Exon skipping; Mass spectrometry; Mdx; Muscle degeneration; Proteomics

Indexed keywords

ADENYLATE KINASE; CALCIUM; CALSEQUESTRIN; DYSTROGLYCAN; DYSTROPHIN; ISOPROTEIN; MUSCLE PROTEIN; NEURONAL NITRIC OXIDE SYNTHASE; NOS1 PROTEIN, HUMAN;

EID: 77951023119     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-009-9197-6     Document Type: Review
Times cited : (34)

References (93)
  • 1
    • 0027470203 scopus 로고
    • The structural and functional diversity of dystrophin
    • Ahn AH, Kunkel LM (1993) The structural and functional diversity of dystrophin. Nat Genet 3:283-291
    • (1993) Nat Genet , vol.3 , pp. 283-291
    • Ahn, A.H.1    Kunkel, L.M.2
  • 3
    • 0034737602 scopus 로고    scopus 로고
    • Calcium influx through calcium leak channels is responsible for the elevated levels of calciumdependent proteolysis in dystrophic myotubes
    • Alderton JM, Steinhardt RA (2000) Calcium influx through calcium leak channels is responsible for the elevated levels of calciumdependent proteolysis in dystrophic myotubes. J Biol Chem 275:9452-9460
    • (2000) J Biol Chem , vol.275 , pp. 9452-9460
    • Alderton, J.M.1    Steinhardt, R.A.2
  • 4
    • 0033758449 scopus 로고    scopus 로고
    • Animal models for muscular dystrophy: Valuable tools for the development of therapies
    • Allamand V, Campbell KP (2000) Animal models for muscular dystrophy: valuable tools for the development of therapies. Hum Mol Genet 9:2459-2467
    • (2000) Hum Mol Genet , vol.9 , pp. 2459-2467
    • Allamand, V.1    Campbell, K.P.2
  • 5
    • 32244443828 scopus 로고    scopus 로고
    • Systemic delivery of morpholino oligonucleotide restores dystrophin expression bodywide and improves dystrophic pathology
    • Alter J, Lou F, Rabinowitz A, Yin H, Rosenfeld J, Wilton SD, Partridge TA, Lu QL (2006) Systemic delivery of morpholino oligonucleotide restores dystrophin expression bodywide and improves dystrophic pathology. Nat Med 12:175-177
    • (2006) Nat Med , vol.12 , pp. 175-177
    • Alter, J.1    Lou, F.2    Rabinowitz, A.3    Yin, H.4    Rosenfeld, J.5    Wilton, S.D.6    Partridge, T.A.7    Lu, Q.L.8
  • 6
    • 0001644020 scopus 로고    scopus 로고
    • The human plasma proteome: History, character, and diagnostic prospects
    • Anderson NL, Anderson NG (2002) The human plasma proteome: history, character, and diagnostic prospects. Mol Cell Proteomics 1:845-867
    • (2002) Mol Cell Proteomics , vol.1 , pp. 845-867
    • Anderson, N.L.1    Anderson, N.G.2
  • 7
    • 33646430861 scopus 로고    scopus 로고
    • Analysis of gene expression differences between utrophin/dystrophin- deficient vs mdx skeletal muscles reveals a specific upregulation of slow muscle genes in limb muscles
    • Baker PE, Kearney JA, Gong B, Merriam AP, Kuhn DE, Porter JD, Rafael-Fortney JA (2006) Analysis of gene expression differences between utrophin/dystrophin-deficient vs mdx skeletal muscles reveals a specific upregulation of slow muscle genes in limb muscles. Neurogenetics 7:81-91
    • (2006) Neurogenetics , vol.7 , pp. 81-91
    • Baker, P.E.1    Kearney, J.A.2    Gong, B.3    Merriam, A.P.4    Kuhn, D.E.5    Porter, J.D.6    Rafael-Fortney, J.A.7
  • 9
    • 0028813406 scopus 로고
    • Expression of heat shock/stress proteins in Duchenne muscular dystrophy
    • Borman L, Polla BS, Lotz BP, Gericke GS (1995) Expression of heat shock/stress proteins in Duchenne muscular dystrophy. Muscle Nerve 18:23-31
    • (1995) Muscle Nerve , vol.18 , pp. 23-31
    • Borman, L.1    Polla, B.S.2    Lotz, B.P.3    Gericke, G.S.4
  • 10
    • 2442672776 scopus 로고    scopus 로고
    • Myoblast survival enhancement and transplantation success improvement by heat-shock treatment in mdx mice
    • Bouchentouf M, Benabdallah BF, Tremblay JP (2004) Myoblast survival enhancement and transplantation success improvement by heat-shock treatment in mdx mice. Transplantation 77:1349-1356
    • (2004) Transplantation , vol.77 , pp. 1349-1356
    • Bouchentouf, M.1    Benabdallah, B.F.2    Tremblay, J.P.3
  • 11
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton- extracellular matrix linkage
    • Campbell KP (1995) Three muscular dystrophies: loss of cytoskeleton- extracellular matrix linkage. Cell 80:675-679
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 13
  • 14
    • 0034638834 scopus 로고    scopus 로고
    • Expression profiling in the muscular dystrophies: Identification of novel aspects of molecular pathophysiology
    • Chen YW, Zhao P, Borup R, Hoffman EP (2000) Expression profiling in the muscular dystrophies: identification of novel aspects of molecular pathophysiology. J Cell Biol 151:1321-1336
    • (2000) J Cell Biol , vol.151 , pp. 1321-1336
    • Chen, Y.W.1    Zhao, P.2    Borup, R.3    Hoffman, E.P.4
  • 15
    • 0030981051 scopus 로고    scopus 로고
    • Dystrophies and heart disease
    • Cox GF, Kunkel LM (1997) Dystrophies and heart disease. Curr Opin Cardiol 12:329-343
    • (1997) Curr Opin Cardiol , vol.12 , pp. 329-343
    • Cox, G.F.1    Kunkel, L.M.2
  • 16
    • 34547572949 scopus 로고    scopus 로고
    • Is proteomics the new genomics?
    • Cox J, Mann M (2007) Is proteomics the new genomics? Cell 130:395-398
    • (2007) Cell , vol.130 , pp. 395-398
    • Cox, J.1    Mann, M.2
  • 17
    • 0025353923 scopus 로고
    • Ultrastructural localization of dystrophin in human muscle by using gold immunolabelling
    • Cullen MJ, Walsh J, Nicholson LV, Harris JB (1990) Ultrastructural localization of dystrophin in human muscle by using gold immunolabelling. Proc R Soc Lond B Biol Sci 240:197-210
    • (1990) Proc R Soc Lond B Biol Sci , vol.240 , pp. 197-210
    • Cullen, M.J.1    Walsh, J.2    Nicholson, L.V.3    Harris, J.B.4
  • 18
    • 0036092560 scopus 로고    scopus 로고
    • Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle
    • Culligan K, Banville N, Dowling P, Ohlendieck K (2002) Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle. J Appl Physiol 92:435-445
    • (2002) J Appl Physiol , vol.92 , pp. 435-445
    • Culligan, K.1    Banville, N.2    Dowling, P.3    Ohlendieck, K.4
  • 20
    • 0027472047 scopus 로고
    • Evolution of the alpha-crystallin/small heat shock protein family
    • de Jong WW, Leunissen JA, Voorter CE (1993) Evolution of the alpha-crystallin/small heat shock protein family. Mol Biol Evol 10:103-126
    • (1993) Mol Biol Evol , vol.10 , pp. 103-126
    • De Jong, W.W.1    Leunissen, J.A.2    Voorter, C.E.3
  • 21
    • 55749087180 scopus 로고    scopus 로고
    • Dystrophic skeletal muscle fibers display alterations at the level of calcium microdomains
    • DiFranco M, Woods CE, Capote J, Vergara JL (2008) Dystrophic skeletal muscle fibers display alterations at the level of calcium microdomains. Proc Natl Acad Sci USA 105:14698-14703
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14698-14703
    • Difranco, M.1    Woods, C.E.2    Capote, J.3    Vergara, J.L.4
  • 22
    • 0036452835 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum function in slow- and fast-twitch skeletal muscles from mdx mice
    • Divet A, Huchet-Cadiou C (2002) Sarcoplasmic reticulum function in slow- and fast-twitch skeletal muscles from mdx mice. Pflugers Arch 444:634-643
    • (2002) Pflugers Arch , vol.444 , pp. 634-643
    • Divet, A.1    Huchet-Cadiou, C.2
  • 23
    • 33645813378 scopus 로고    scopus 로고
    • Mass spectrometry and protein analysis
    • Domon B, Aebersold R (2006) Mass spectrometry and protein analysis. Science 312:212-217
    • (2006) Science , vol.312 , pp. 212-217
    • Domon, B.1    Aebersold, R.2
  • 24
    • 4944230808 scopus 로고    scopus 로고
    • Subproteomics analysis of Ca2+ -binding proteins demonstrates decreased calsequestrin expression in dystrophic mouse skeletal muscle
    • Doran P, Dowling P, Lohan J, McDonnell K, Poetsch S, Ohlendieck K (2004) Subproteomics analysis of Ca2+ -binding proteins demonstrates decreased calsequestrin expression in dystrophic mouse skeletal muscle. Eur J Biochem 271:3943-3952
    • (2004) Eur J Biochem , vol.271 , pp. 3943-3952
    • Doran, P.1    Dowling, P.2    Lohan, J.3    McDonnell, K.4    Poetsch, S.5    Ohlendieck, K.6
  • 25
    • 33748339008 scopus 로고    scopus 로고
    • Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHsp
    • Doran P, Martin G, Dowling P, Jockusch H, Ohlendieck K (2006a) Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHsp. Proteomics 6:4610-4621
    • (2006) Proteomics , vol.6 , pp. 4610-4621
    • Doran, P.1    Martin, G.2    Dowling, P.3    Jockusch, H.4    Ohlendieck, K.5
  • 26
    • 33646102225 scopus 로고    scopus 로고
    • Reduced expression of regucalcin in young and aged mdx diaphragm indicates abnormal cytosolic calcium handling in dystrophin-deficient muscle
    • Doran P, Dowling P, Donoghue P, Buffini M, Ohlendieck K (2006b) Reduced expression of regucalcin in young and aged mdx diaphragm indicates abnormal cytosolic calcium handling in dystrophin-deficient muscle. Biochim Biophys Acta 1764:773-785
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 773-785
    • Doran, P.1    Dowling, P.2    Donoghue, P.3    Buffini, M.4    Ohlendieck, K.5
  • 27
    • 38349131087 scopus 로고    scopus 로고
    • Proteomic profiling of animal models mimicking skeletal muscle disorders
    • Doran P, Gannon J, O'Connell K, Ohlendieck K (2007) Proteomic profiling of animal models mimicking skeletal muscle disorders. Proteomics Clin Appl 1:1169-1184
    • (2007) Proteomics Clin Appl , vol.1 , pp. 1169-1184
    • Doran, P.1    Gannon, J.2    O'Connell, K.3    Ohlendieck, K.4
  • 29
    • 60549096114 scopus 로고    scopus 로고
    • Proteomic profiling of antisense-induced exon skipping reveals reversal of pathobiochemical abnormalities in dystrophic mdx diaphragm
    • Doran P, Wilton SD, Fletcher S, Ohlendieck K (2009b) Proteomic profiling of antisense-induced exon skipping reveals reversal of pathobiochemical abnormalities in dystrophic mdx diaphragm. Proteomics 9:671-685
    • (2009) Proteomics , vol.9 , pp. 671-685
    • Doran, P.1    Wilton, S.D.2    Fletcher, S.3    Ohlendieck, K.4
  • 30
    • 0036188005 scopus 로고    scopus 로고
    • Distal mdx muscle groups exhibiting up-regulation of utrophin and rescue of dystrophin-associated glycoproteins exemplify a protected phenotype in muscular dystrophy
    • Dowling P, Culligan K, Ohlendieck K (2002) Distal mdx muscle groups exhibiting up-regulation of utrophin and rescue of dystrophin-associated glycoproteins exemplify a protected phenotype in muscular dystrophy. Naturwissenschaften 89:75-88
    • (2002) Naturwissenschaften , vol.89 , pp. 75-88
    • Dowling, P.1    Culligan, K.2    Ohlendieck, K.3
  • 31
    • 0038823857 scopus 로고    scopus 로고
    • Comparative analysis of Dp427-deficient mdx tissues shows that the milder dystrophic phenotype of extraocular and toe muscle fibres is associated with a persistent expression of beta-dystroglycan
    • Dowling P, Lohan J, Ohlendieck K (2003) Comparative analysis of Dp427-deficient mdx tissues shows that the milder dystrophic phenotype of extraocular and toe muscle fibres is associated with a persistent expression of beta-dystroglycan. Eur J Cell Biol 82:222-230
    • (2003) Eur J Cell Biol , vol.82 , pp. 222-230
    • Dowling, P.1    Lohan, J.2    Ohlendieck, K.3
  • 32
    • 2342614190 scopus 로고    scopus 로고
    • Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy
    • Dowling P, Doran P, Ohlendieck K (2004) Drastic reduction of sarcalumenin in Dp427 (dystrophin of 427 kDa)-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy. Biochem J 379:479-488
    • (2004) Biochem J , vol.379 , pp. 479-488
    • Dowling, P.1    Doran, P.2    Ohlendieck, K.3
  • 33
    • 0036591684 scopus 로고    scopus 로고
    • Muscular dystrophies involving the dystrophin-glycoprotein complex: An overview of current mouse models
    • Durbeej M, Campbell KP (2002) Muscular dystrophies involving the dystrophin-glycoprotein complex: an overview of current mouse models. Curr Opin Genet Dev 12:349-361
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 349-361
    • Durbeej, M.1    Campbell, K.P.2
  • 34
    • 0037160782 scopus 로고    scopus 로고
    • The muscular dystrophies
    • Emery AE (2002a) The muscular dystrophies. Lancet 359:687-695
    • (2002) Lancet , vol.359 , pp. 687-695
    • Emery, A.E.1
  • 35
    • 0036227796 scopus 로고    scopus 로고
    • Muscular dystrophy into the new millennium
    • Emery AE (2002b) Muscular dystrophy into the new millennium. Neuromuscul Disord 12:343-349
    • (2002) Neuromuscul Disord , vol.12 , pp. 343-349
    • Emery, A.E.1
  • 37
    • 38949130017 scopus 로고    scopus 로고
    • Biology of the striated muscle dystrophin-glycoprotein complex
    • Ervasti JM, Sonnemann KJ (2008) Biology of the striated muscle dystrophin-glycoprotein complex. Int Rev Cytol 265:191-225
    • (2008) Int Rev Cytol , vol.265 , pp. 191-225
    • Ervasti, J.M.1    Sonnemann, K.J.2
  • 38
    • 0025272250 scopus 로고
    • Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
    • 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
    • (1990) Nature , vol.345 , pp. 315-319
    • Ervasti, J.M.1    Ohlendieck, K.2    Kahl, S.D.3    Gaver, M.G.4    Campbell, K.P.5
  • 39
    • 0024438708 scopus 로고
    • Electrospray ionization for mass spectrometry of large biomolecules
    • Fenn JB, Mann M, Meng CK, Wong SF, Whitehouse CM (1989) Electrospray ionization for mass spectrometry of large biomolecules. Science 246:64-71
    • (1989) Science , vol.246 , pp. 64-71
    • Fenn, J.B.1    Mann, M.2    Meng, C.K.3    Wong, S.F.4    Whitehouse, C.M.5
  • 40
    • 65949093523 scopus 로고    scopus 로고
    • Sarcoplasmicendoplasmic- reticulum Ca2+ -ATPase and calsequestrin are overexpressed in spared intrinsic laryngeal muscles of dystrophin- deficient mdx mice
    • Ferretti R, Marques MJ, Pertille A, Neto HS (2009) Sarcoplasmicendoplasmic- reticulum Ca2+ -ATPase and calsequestrin are overexpressed in spared intrinsic laryngeal muscles of dystrophin- deficient mdx mice. Muscle Nerve 39:609-615
    • (2009) Muscle Nerve , vol.39 , pp. 609-615
    • Ferretti, R.1    Marques, M.J.2    Pertille, A.3    Neto, H.S.4
  • 41
    • 51149109591 scopus 로고    scopus 로고
    • Complementary methods to assist subcellular fractionation in organellar proteomics
    • Gauthier DJ, Lazure C (2008) Complementary methods to assist subcellular fractionation in organellar proteomics. Expert Rev Proteomics 5:603-617
    • (2008) Expert Rev Proteomics , vol.5 , pp. 603-617
    • Gauthier, D.J.1    Lazure, C.2
  • 42
    • 0142182391 scopus 로고    scopus 로고
    • Proteomic analysis of mdx skeletal muscle: Great reduction of adenylate kinase 1 expression and enzymatic activity
    • Ge Y, Molloy MP, Chamberlain JS, Andrews PC (2003) Proteomic analysis of mdx skeletal muscle: great reduction of adenylate kinase 1 expression and enzymatic activity. Proteomics 3:1895-1903
    • (2003) Proteomics , vol.3 , pp. 1895-1903
    • Ge, Y.1    Molloy, M.P.2    Chamberlain, J.S.3    Andrews, P.C.4
  • 43
    • 4444267191 scopus 로고    scopus 로고
    • Differential expression of the skeletal muscle proteome in mdx mice at different ages
    • Ge Y, Molloy MP, Chamberlain JS, Andrews PC (2004) Differential expression of the skeletal muscle proteome in mdx mice at different ages. Electrophoresis 25:2576-2585
    • (2004) Electrophoresis , vol.25 , pp. 2576-2585
    • Ge, Y.1    Molloy, M.P.2    Chamberlain, J.S.3    Andrews, P.C.4
  • 44
    • 53949118974 scopus 로고    scopus 로고
    • Insulin-like growth factor-I analogue protects muscles of dystrophic mdx mice from contraction-mediated damage
    • Gehrig SM, Ryall JG, Schertzer JD, Lynch GS (2008) Insulin-like growth factor-I analogue protects muscles of dystrophic mdx mice from contraction-mediated damage. Exp Physiol 93:1190-1198
    • (2008) Exp Physiol , vol.93 , pp. 1190-1198
    • Gehrig, S.M.1    Ryall, J.G.2    Schertzer, J.D.3    Lynch, G.S.4
  • 45
    • 48049121310 scopus 로고    scopus 로고
    • TRPC1 binds to caveolin-3 and is regulated by Src kinase-role in Duchenne muscular dystrophy
    • Gervasio OL, Whitehead NP, Yeung EW, Phillips WD, Allen DG (2008) TRPC1 binds to caveolin-3 and is regulated by Src kinase-role in Duchenne muscular dystrophy. J Cell Sci 121:2246-2255
    • (2008) J Cell Sci , vol.121 , pp. 2246-2255
    • Gervasio, O.L.1    Whitehead, N.P.2    Yeung, E.W.3    Phillips, W.D.4    Allen, D.G.5
  • 46
    • 10644230916 scopus 로고    scopus 로고
    • Current two-dimensional electrophoresis technology for proteomics
    • Goerg A, Weiss W, Dunn MJ (2004) Current two-dimensional electrophoresis technology for proteomics. Proteomics 4:3665-3685
    • (2004) Proteomics , vol.4 , pp. 3665-3685
    • Goerg, A.1    Weiss, W.2    Dunn, M.J.3
  • 47
    • 77950830178 scopus 로고    scopus 로고
    • Applications of metabolomics and proteomics to the mdx mouse model of Duchenne muscular dystrophy: Lessons from downstream of the transcriptome
    • Griffin JL, Des Rosiers C (2009) Applications of metabolomics and proteomics to the mdx mouse model of Duchenne muscular dystrophy: lessons from downstream of the transcriptome. Genome Med 1:32.1-32.11
    • (2009) Genome Med , vol.1 , pp. 321-3211
    • Griffin, J.L.1    Des Rosiers, C.2
  • 48
    • 52049098971 scopus 로고    scopus 로고
    • A combined metabolomic and proteomic investigation of the effects of a failure to express dystrophin in the mouse heart
    • Gulston MK, Rubtsov DV, Atherton HJ, Clarke K, Davies KE, Lilley KS, Griffin JL (2008) A combined metabolomic and proteomic investigation of the effects of a failure to express dystrophin in the mouse heart. J Proteome Res 7:2069-2077
    • (2008) J Proteome Res , vol.7 , pp. 2069-2077
    • Gulston, M.K.1    Rubtsov, D.V.2    Atherton, H.J.3    Clarke, K.4    Davies, K.E.5    Lilley, K.S.6    Griffin, J.L.7
  • 51
    • 0037023852 scopus 로고    scopus 로고
    • Proteomic analysis of striated muscle
    • Isfort RJ (2002) Proteomic analysis of striated muscle. J Chromatogr B 771:155-165
    • (2002) J Chromatogr B , vol.771 , pp. 155-165
    • Isfort, R.J.1
  • 53
    • 0025217703 scopus 로고
    • Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility
    • Koenig M, Kunkel LM (1990) Detailed analysis of the repeat domain of dystrophin reveals four potential hinge segments that may confer flexibility. J Biol Chem 265:4560-4566
    • (1990) J Biol Chem , vol.265 , pp. 4560-4566
    • Koenig, M.1    Kunkel, L.M.2
  • 54
    • 0023904860 scopus 로고
    • The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein
    • Koenig M, Monaco AP, Kunkel LM (1988) The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 53:219-226
    • (1988) Cell , vol.53 , pp. 219-226
    • Koenig, M.1    Monaco, A.P.2    Kunkel, L.M.3
  • 55
    • 45449104412 scopus 로고    scopus 로고
    • Transient receptor potential cation channels in normal and dystrophic mdx muscle
    • Krueger J, Kunert-Keil C, Bisping F, Brinkmeier H (2008) Transient receptor potential cation channels in normal and dystrophic mdx muscle. Neuromuscul Disord 18:501-513
    • (2008) Neuromuscul Disord , vol.18 , pp. 501-513
    • Krueger, J.1    Kunert-Keil, C.2    Bisping, F.3    Brinkmeier, H.4
  • 56
    • 70349249363 scopus 로고    scopus 로고
    • Malformed mdx myofibers have normal cytoskeletal architecture yet altered EC coupling and stress-induced Ca2+ signaling
    • Lovering RM, Michaelson L, Ward CW (2009) Malformed mdx myofibers have normal cytoskeletal architecture yet altered EC coupling and stress-induced Ca2+ signaling. Am J Physiol Cell Physiol 297:C571-C580
    • (2009) Am J Physiol Cell Physiol , vol.297
    • Lovering, R.M.1    Michaelson, L.2    Ward, C.W.3
  • 57
    • 0034712587 scopus 로고    scopus 로고
    • Elevated subsarcolemmal Ca2+ in mdx mouse skeletal muscle fibres detected with Ca2+ - Activated K+ channels
    • Mallouk N, Jacquemond V, Allard B (2000) Elevated subsarcolemmal Ca2+ in mdx mouse skeletal muscle fibres detected with Ca2+ - activated K+ channels. Proc Natl Acad Sci USA 97:4950-4955
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4950-4955
    • Mallouk, N.1    Jacquemond, V.2    Allard, B.3
  • 58
    • 67650489602 scopus 로고    scopus 로고
    • Diagnosis and new treatments in muscular dystrophies
    • Manzur AY, Muntoni F (2009) Diagnosis and new treatments in muscular dystrophies. J Neurol Neurosurg Psychiatry 80:706-714
    • (2009) J Neurol Neurosurg Psychiatry , vol.80 , pp. 706-714
    • Manzur, A.Y.1    Muntoni, F.2
  • 60
    • 21244495253 scopus 로고    scopus 로고
    • The development of the DIGE system: 2D fluorescence difference gel analysis technology
    • Marouga R, David S, Hawkins E (2005) The development of the DIGE system: 2D fluorescence difference gel analysis technology. Anal Bioanal Chem 382:669-678
    • (2005) Anal Bioanal Chem , vol.382 , pp. 669-678
    • Marouga, R.1    David, S.2    Hawkins, E.3
  • 61
    • 33847684752 scopus 로고    scopus 로고
    • Intrinsic laryngeal muscles are spared from myonecrosis in the mdx mouse model of Duchenne muscular dystrophy
    • Marques MJ, Ferretti R, Vomero VU, Minatel E, Neto HS (2007) Intrinsic laryngeal muscles are spared from myonecrosis in the mdx mouse model of Duchenne muscular dystrophy. Muscle Nerve 35:349-353
    • (2007) Muscle Nerve , vol.35 , pp. 349-353
    • Marques, M.J.1    Ferretti, R.2    Vomero, V.U.3    Minatel, E.4    Neto, H.S.5
  • 62
    • 60549115816 scopus 로고    scopus 로고
    • Diltiazem and verapamil protect dystrophin-deficient muscle fibers of MDX mice from degeneration: A potential role in calcium buffering and sarcolemmal stability
    • Matsumura CY, Pertille A, Albuquerque TC, Santo Neto H, Marques MJ (2009) Diltiazem and verapamil protect dystrophin-deficient muscle fibers of MDX mice from degeneration: a potential role in calcium buffering and sarcolemmal stability. Muscle Nerve 39:167-176
    • (2009) Muscle Nerve , vol.39 , pp. 167-176
    • Matsumura, C.Y.1    Pertille, A.2    Albuquerque, T.C.3    Santo Neto, H.4    Marques, M.J.5
  • 63
    • 33846697281 scopus 로고    scopus 로고
    • Structural and functional analysis of the sarcoglycan-sarcospan subcomplex
    • Miller G, Wang EL, Nassar KL, Peter AK, Crosbie RH (2007) Structural and functional analysis of the sarcoglycan-sarcospan subcomplex. Exp Cell Res 313:639-651
    • (2007) Exp Cell Res , vol.313 , pp. 639-651
    • Miller, G.1    Wang, E.L.2    Nassar, K.L.3    Peter, A.K.4    Crosbie, R.H.5
  • 66
    • 69149106708 scopus 로고    scopus 로고
    • Emerging strategies for cell and gene therapy of the muscular dystrophies
    • Muir LA, Chamberlain JS (2009) Emerging strategies for cell and gene therapy of the muscular dystrophies. Expert Rev Mol Med 11:e18
    • (2009) Expert Rev Mol Med , vol.11
    • Muir, L.A.1    Chamberlain, J.S.2
  • 67
    • 67651243772 scopus 로고    scopus 로고
    • Exon-skipping therapy for Duchenne muscular dystrophy
    • Nakamura A, Takeda S (2009) Exon-skipping therapy for Duchenne muscular dystrophy. Neuropathology 29:494-501
    • (2009) Neuropathology , vol.29 , pp. 494-501
    • Nakamura, A.1    Takeda, S.2
  • 68
    • 0028176579 scopus 로고
    • Chaperone activity of alphacrystallins modulates intermediate filament assembly
    • Nicholl ID, Quinlan RA (1994) Chaperone activity of alphacrystallins modulates intermediate filament assembly. EMBO J 13:945-953
    • (1994) EMBO J , vol.13 , pp. 945-953
    • Nicholl, I.D.1    Quinlan, R.A.2
  • 69
    • 0030026119 scopus 로고    scopus 로고
    • Towards an understanding of the dystrophinglycoprotein complex: Linkage between the extracellular matrix and the subsarcolemmal membrane cytoskeleton
    • Ohlendieck K (1996) Towards an understanding of the dystrophinglycoprotein complex: linkage between the extracellular matrix and the subsarcolemmal membrane cytoskeleton. Eur J Cell Biol 69:1-10
    • (1996) Eur J Cell Biol , vol.69 , pp. 1-10
    • Ohlendieck, K.1
  • 70
    • 0025881734 scopus 로고
    • Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle
    • Ohlendieck K, Campbell KP (1991) Dystrophin constitutes 5% of membrane cytoskeleton in skeletal muscle. FEBS Lett 283:230-234
    • (1991) FEBS Lett , vol.283 , pp. 230-234
    • Ohlendieck, K.1    Campbell, K.P.2
  • 72
    • 0026067790 scopus 로고
    • Dystrophin glycoprotein complex is highly enriched in skeletal muscle sarcolemma
    • Ohlendieck K, Ervasti JM, Snook JB, Campbell KP (1991b) Dystrophin glycoprotein complex is highly enriched in skeletal muscle sarcolemma. J Cell Biol 112:135-148
    • (1991) J Cell Biol , vol.112 , pp. 135-148
    • Ohlendieck, K.1    Ervasti, J.M.2    Snook, J.B.3    Campbell, K.P.4
  • 78
  • 81
    • 56149120851 scopus 로고    scopus 로고
    • Inhibitory control over Ca2+ sparks via mechanosensitive channels is disrupted in dystrophin deficient muscle but restored by mini-dystrophin expression
    • Teichmann MD, Wegner FV, Fink RH, Chamberlain JS, Launikonis BS, Martinac B, Friedrich O (2008) Inhibitory control over Ca2+ sparks via mechanosensitive channels is disrupted in dystrophin deficient muscle but restored by mini-dystrophin expression. PLoS One 3:e3644
    • (2008) PLoS One , vol.3
    • Teichmann, M.D.1    Wegner, F.V.2    Fink, R.H.3    Chamberlain, J.S.4    Launikonis, B.S.5    Martinac, B.6    Friedrich, O.7
  • 83
    • 0023091942 scopus 로고
    • The mutant mdx: Inherited myopathy in the mouse
    • Torres LFB, Duchen LW (1987) The mutant mdx: inherited myopathy in the mouse. Brain 110:269-299
    • (1987) Brain , vol.110 , pp. 269-299
    • Torres, L.F.B.1    Duchen, L.W.2
  • 85
    • 0027281140 scopus 로고
    • Proteolysis results in altered leak channel kinetics and elevated free calcium in mdx muscle
    • Turner PR, Schultz R, Ganguly B, Steinhardt RA (1993) Proteolysis results in altered leak channel kinetics and elevated free calcium in mdx muscle. J Membr Biol 133:243-251
    • (1993) J Membr Biol , vol.133 , pp. 243-251
    • Turner, P.R.1    Schultz, R.2    Ganguly, B.3    Steinhardt, R.A.4
  • 87
    • 0037119993 scopus 로고    scopus 로고
    • Involvement of TRPC in the abnormal calcium influx observed in dystrophic (mdx) mouse skeletal muscle fibers
    • 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
    • (2002) J Cell Biol , vol.158 , pp. 1089-1096
    • Vandebrouck, C.1    Martin, D.2    Colson-Van Schoor, M.3    Debaix, H.4    Gailly, P.5
  • 88
    • 34248180415 scopus 로고    scopus 로고
    • Two-dimensional difference gel electrophoresis
    • Viswanathan S, Unlu M, Minden JS (2006) Two-dimensional difference gel electrophoresis. Nat Protoc 1:1351-1358
    • (2006) Nat Protoc , vol.1 , pp. 1351-1358
    • Viswanathan, S.1    Unlu, M.2    Minden, J.S.3
  • 89
    • 56049083502 scopus 로고    scopus 로고
    • Exon skipping and Duchenne muscular dystrophy: Hope, hype and how feasible?
    • Wilton SD, Fletcher S (2008) Exon skipping and Duchenne muscular dystrophy: hope, hype and how feasible? Neurol India 56:254-262
    • (2008) Neurol India , vol.56 , pp. 254-262
    • Wilton, S.D.1    Fletcher, S.2
  • 90
    • 33748571491 scopus 로고    scopus 로고
    • Two-dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry
    • Wittmann-Liebold B, Graack HR, Pohl T (2006) Two-dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry. Proteomics 6:4688-4703
    • (2006) Proteomics , vol.6 , pp. 4688-4703
    • Wittmann-Liebold, B.1    Graack, H.R.2    Pohl, T.3
  • 91
    • 2942696374 scopus 로고    scopus 로고
    • The action potential-evoked sarcoplasmic reticulum calcium release is impaired in mdx mouse muscle fibres
    • Woods CE, Novo D, DiFranco M, Vergara JL (2004) The action potential-evoked sarcoplasmic reticulum calcium release is impaired in mdx mouse muscle fibres. J Physiol 557:59-75
    • (2004) J Physiol , vol.557 , pp. 59-75
    • Woods, C.E.1    Novo, D.2    Difranco, M.3    Vergara, J.L.4
  • 92
    • 0029278675 scopus 로고
    • Matrix-assisted laser desorption ionization mass spectrometry: Applications in peptide and protein characterization
    • Zaluzec EJ, Gage DA, Watson JT (1995) Matrix-assisted laser desorption ionization mass spectrometry: applications in peptide and protein characterization. Protein Expr Purif 6:109-123
    • (1995) Protein Expr Purif , vol.6 , pp. 109-123
    • Zaluzec, E.J.1    Gage, D.A.2    Watson, J.T.3
  • 93
    • 58249084982 scopus 로고    scopus 로고
    • Regulation of cell proliferation by fast myosin light chain 1 in myoblasts derived from extraocular muscle, diaphragm and gastrocnemius
    • Zhang SZ, Xie HQ, Xu Y, Li XQ, Wei RQ, Zhi W, Deng L, Qiu L, Yang ZM (2008) Regulation of cell proliferation by fast myosin light chain 1 in myoblasts derived from extraocular muscle, diaphragm and gastrocnemius. Exp Biol Med 233:1374-1384
    • (2008) Exp Biol Med , vol.233 , pp. 1374-1384
    • Zhang, S.Z.1    Xie, H.Q.2    Xu, Y.3    Li, X.Q.4    Wei, R.Q.5    Zhi, W.6    Deng, L.7    Qiu, L.8    Yang, Z.M.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.