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Volumn 11, Issue 4, 2014, Pages 773-785

Triadopathies: An Emerging Class of Skeletal Muscle Diseases

Author keywords

congenital myopathies; Excitation contraction coupling; malignant hyperthermia; RYR1; triad

Indexed keywords

1,4 DIHYDROPYRIDINE RECEPTOR; ACETYLCYSTEINE; CALCIUM ION; CALCIUM RELEASE ACTIVATED CALCIUM CHANNEL; CALPAIN 3; DANTROLENE; DYSTROPHIN; HALOTHANE; ISOFLURANE; MYOTONIC DYSTROPHY PROTEIN KINASE; RYANODINE RECEPTOR; RYANODINE RECEPTOR 1; SARCOPLASMIC RETICULUM CALCIUM TRANSPORTING ADENOSINE TRIPHOSPHATASE; SELENOPROTEIN; SEVOFLURANE; CCDC78 PROTEIN, HUMAN; MICROTUBULE ASSOCIATED PROTEIN; MUSCLE PROTEIN; SEPN1 PROTEIN, HUMAN;

EID: 84919781500     PISSN: 19337213     EISSN: 18787479     Source Type: Journal    
DOI: 10.1007/s13311-014-0300-3     Document Type: Review
Times cited : (57)

References (111)
  • 2
    • 0028989453 scopus 로고
    • The role of Ca2+ ions in excitation-contraction coupling of skeletal muscle fibres
    • PID: 7742348
    • Melzer W, Herrmann-Frank A, Luttgau HC. The role of Ca2+ ions in excitation-contraction coupling of skeletal muscle fibres. Biochim Biophys Acta 1995;1241:59-116.
    • (1995) Biochim Biophys Acta , vol.1241 , pp. 59-116
    • Melzer, W.1    Herrmann-Frank, A.2    Luttgau, H.C.3
  • 3
    • 33744955800 scopus 로고    scopus 로고
    • Sarcoplasmic reticulum: the dynamic calcium governor of muscle
    • PID: 16477617, COI: 1:CAS:528:DC%2BD28XmtlKntbo%3D
    • Rossi AE, Dirksen RT. Sarcoplasmic reticulum: the dynamic calcium governor of muscle. Muscle Nerve 2006;33:715-731.
    • (2006) Muscle Nerve , vol.33 , pp. 715-731
    • Rossi, A.E.1    Dirksen, R.T.2
  • 7
    • 0032480548 scopus 로고    scopus 로고
    • Malignant hyperthermia
    • PID: 9798607, COI: 1:CAS:528:DyaK1cXmvFWkt7Y%3D
    • Denborough M. Malignant hyperthermia. Lancet 1998;352:1131-1136.
    • (1998) Lancet , vol.352 , pp. 1131-1136
    • Denborough, M.1
  • 8
    • 16544380350 scopus 로고    scopus 로고
    • Malignant hyperthermia: pathophysiology, clinical presentation, and treatment
    • PID: 15461040
    • McCarthy EJ. Malignant hyperthermia: pathophysiology, clinical presentation, and treatment. AACN Clin Issues 2004;15:231-237.
    • (2004) AACN Clin Issues , vol.15 , pp. 231-237
    • McCarthy, E.J.1
  • 9
    • 76249106192 scopus 로고    scopus 로고
    • Clinical presentation, treatment, and complications of malignant hyperthermia in North America from 1987 to 2006
    • PID: 20081135
    • Larach MG, Gronert GA, Allen GC, Brandom BW, Lehman EB. Clinical presentation, treatment, and complications of malignant hyperthermia in North America from 1987 to 2006. Anesth Analg 2010;110:498-507.
    • (2010) Anesth Analg , vol.110 , pp. 498-507
    • Larach, M.G.1    Gronert, G.A.2    Allen, G.C.3    Brandom, B.W.4    Lehman, E.B.5
  • 10
    • 0028376090 scopus 로고
    • Malignant hyperthermia. Epidemiology, pathophysiology, treatment
    • PID: 8147588, COI: 1:STN:280:DyaK2c7pslCitg%3D%3D
    • Donnelly AJ. Malignant hyperthermia. Epidemiology, pathophysiology, treatment. AORN J 1994;59:393-395.
    • (1994) AORN J , vol.59 , pp. 393-395
    • Donnelly, A.J.1
  • 11
    • 84888267800 scopus 로고    scopus 로고
    • Using exome data to identify malignant hyperthermia susceptibility mutations
    • PID: 24195946, COI: 1:CAS:528:DC%2BC3sXhslCmtbjE
    • Gonsalves SG, Ng D, Johnston JJ, et al. Using exome data to identify malignant hyperthermia susceptibility mutations. Anesthesiology 2013;119:1043-1053.
    • (2013) Anesthesiology , vol.119 , pp. 1043-1053
    • Gonsalves, S.G.1    Ng, D.2    Johnston, J.J.3
  • 12
    • 84893240891 scopus 로고    scopus 로고
    • DNA testing for malignant hyperthermia: the reality and the dream
    • PID: 24445638, COI: 1:CAS:528:DC%2BC2cXht12qs7Y%3D
    • Stowell KM. DNA testing for malignant hyperthermia: the reality and the dream. Anesth Analg 2014;118:397-406.
    • (2014) Anesth Analg , vol.118 , pp. 397-406
    • Stowell, K.M.1
  • 13
    • 33748997392 scopus 로고    scopus 로고
    • Mutations in RYR1 in malignant hyperthermia and central core disease
    • PID: 16917943, COI: 1:CAS:528:DC%2BD28XhtVKqsrbJ
    • Robinson R, Carpenter D, Shaw MA, Halsall J, Hopkins P. Mutations in RYR1 in malignant hyperthermia and central core disease. Hum Mutat 2006;27:977-989.
    • (2006) Hum Mutat , vol.27 , pp. 977-989
    • Robinson, R.1    Carpenter, D.2    Shaw, M.A.3    Halsall, J.4    Hopkins, P.5
  • 14
    • 70350521074 scopus 로고    scopus 로고
    • The role of CACNA1S in predisposition to malignant hyperthermia
    • PID: 19825159
    • Carpenter D, Ringrose C, Leo V, et al. The role of CACNA1S in predisposition to malignant hyperthermia. BMC Med Genet 2009;10:104.
    • (2009) BMC Med Genet , vol.10 , pp. 104
    • Carpenter, D.1    Ringrose, C.2    Leo, V.3
  • 15
    • 84956819799 scopus 로고    scopus 로고
    • Cav1.1 in malignant hyperthermia
    • Weiss N, Koschak A, (eds), Springer-Verlag, Berlin:
    • Yarotskyy V, Dirksen RT. Cav1.1 in malignant hyperthermia. In: Weiss N, Koschak A (eds) Pathologies of calcium channels. Springer-Verlag, Berlin, 2014.
    • (2014) Pathologies of calcium channels
    • Yarotskyy, V.1    Dirksen, R.T.2
  • 16
    • 84888247803 scopus 로고    scopus 로고
    • Exome sequencing reveals novel rare variants in the ryanodine receptor and calcium channel genes in malignant hyperthermia families
    • PID: 24013571, COI: 1:CAS:528:DC%2BC3sXhslCmtbnO
    • Kim JH, Jarvik GP, Browning BL, et al. Exome sequencing reveals novel rare variants in the ryanodine receptor and calcium channel genes in malignant hyperthermia families. Anesthesiology 2013;119:1054-1065.
    • (2013) Anesthesiology , vol.119 , pp. 1054-1065
    • Kim, J.H.1    Jarvik, G.P.2    Browning, B.L.3
  • 17
    • 70349568135 scopus 로고    scopus 로고
    • The relationship between exertional heat illness, exertional rhabdomyolysis, and malignant hyperthermia
    • PID: 19617585
    • Capacchione JF, Muldoon SM. The relationship between exertional heat illness, exertional rhabdomyolysis, and malignant hyperthermia. Anesth Analg 2009;109:1065-1069.
    • (2009) Anesth Analg , vol.109 , pp. 1065-1069
    • Capacchione, J.F.1    Muldoon, S.M.2
  • 18
    • 0034946063 scopus 로고    scopus 로고
    • Malignant hyperthermia and apparent heat stroke
    • PID: 11448278, COI: 1:STN:280:DC%2BD3MvgslCnug%3D%3D
    • Tobin JR, Jason DR, Challa VR, Nelson TE, Sambuughin N. Malignant hyperthermia and apparent heat stroke. JAMA 2001;286:168-169.
    • (2001) JAMA , vol.286 , pp. 168-169
    • Tobin, J.R.1    Jason, D.R.2    Challa, V.R.3    Nelson, T.E.4    Sambuughin, N.5
  • 19
    • 84878997369 scopus 로고    scopus 로고
    • Mutations in RYR1 are a common cause of exertional myalgia and rhabdomyolysis
    • PID: 23628358, COI: 1:STN:280:DC%2BC3srptlSlsw%3D%3D
    • Dlamini N, Voermans NC, Lillis S, et al. Mutations in RYR1 are a common cause of exertional myalgia and rhabdomyolysis. Neuromuscul Disord 2013;23:540-548.
    • (2013) Neuromuscul Disord , vol.23 , pp. 540-548
    • Dlamini, N.1    Voermans, N.C.2    Lillis, S.3
  • 20
    • 84859650685 scopus 로고    scopus 로고
    • 182nd ENMC International Workshop: RYR1-related myopathies, 15–17th April 2011, Naarden, The Netherlands
    • PID: 22226685
    • Jungbluth H, Dowling JJ, Ferreiro A, Muntoni F. 182nd ENMC International Workshop: RYR1-related myopathies, 15–17th April 2011, Naarden, The Netherlands. Neuromuscul Disord 2012;22:453-462.
    • (2012) Neuromuscul Disord , vol.22 , pp. 453-462
    • Jungbluth, H.1    Dowling, J.J.2    Ferreiro, A.3    Muntoni, F.4
  • 21
    • 34249879583 scopus 로고    scopus 로고
    • Central core disease
    • PID: 17504518
    • Jungbluth H. Central core disease. Orphanet J Rare Dis 2007;2:25.
    • (2007) Orphanet J Rare Dis , vol.2 , pp. 25
    • Jungbluth, H.1
  • 22
    • 34547909222 scopus 로고    scopus 로고
    • Multi-minicore disease
    • PID: 17631035
    • Jungbluth H. Multi-minicore disease. Orphanet J Rare Dis 2007;2:31.
    • (2007) Orphanet J Rare Dis , vol.2 , pp. 31
    • Jungbluth, H.1
  • 23
    • 78249290502 scopus 로고    scopus 로고
    • RYR1 mutations are a common cause of congenital myopathies with central nuclei
    • PID: 20839240, COI: 1:CAS:528:DC%2BC3cXhsFOnsrbJ
    • Wilmshurst JM, Lillis S, Zhou H, et al. RYR1 mutations are a common cause of congenital myopathies with central nuclei. Ann Neurol 2010;68:717-726.
    • (2010) Ann Neurol , vol.68 , pp. 717-726
    • Wilmshurst, J.M.1    Lillis, S.2    Zhou, H.3
  • 24
    • 77954130090 scopus 로고    scopus 로고
    • Recessive mutations in RYR1 are a common cause of congenital fiber type disproportion
    • PID: 20583297, COI: 1:CAS:528:DC%2BC3cXpslagtbs%3D
    • Clarke NF, Waddell LB, Cooper ST, et al. Recessive mutations in RYR1 are a common cause of congenital fiber type disproportion. Hum Mutat 2010;31:E1544-E1550.
    • (2010) Hum Mutat , vol.31 , pp. E1544-E1550
    • Clarke, N.F.1    Waddell, L.B.2    Cooper, S.T.3
  • 25
    • 84865166292 scopus 로고    scopus 로고
    • Clinical and genetic findings in a large cohort of patients with ryanodine receptor 1 gene-associated myopathies
    • PID: 22473935, COI: 1:CAS:528:DC%2BC38XhtVOmur7F
    • Klein A, Lillis S, Munteanu I, et al. Clinical and genetic findings in a large cohort of patients with ryanodine receptor 1 gene-associated myopathies. Hum Mutat 2012;33:981-988.
    • (2012) Hum Mutat , vol.33 , pp. 981-988
    • Klein, A.1    Lillis, S.2    Munteanu, I.3
  • 26
    • 77950517340 scopus 로고    scopus 로고
    • Multi-minicore disease and atypical periodic paralysis associated with novel mutations in the skeletal muscle ryanodine receptor (RYR1) gene
    • PID: 20080402
    • Zhou H, Lillis S, Loy RE, et al. Multi-minicore disease and atypical periodic paralysis associated with novel mutations in the skeletal muscle ryanodine receptor (RYR1) gene. Neuromuscul Disord 2010;20:166-173.
    • (2010) Neuromuscul Disord , vol.20 , pp. 166-173
    • Zhou, H.1    Lillis, S.2    Loy, R.E.3
  • 27
    • 84903892568 scopus 로고    scopus 로고
    • RYR1-related congenital myopathy with fatigable weakness, responding to pyridostigimine
    • PID: 24951453, COI: 1:STN:280:DC%2BC2cfksFaisw%3D%3D
    • Illingworth MA, Main M, Pitt M, et al. RYR1-related congenital myopathy with fatigable weakness, responding to pyridostigimine. Neuromuscul Disord 2014;24:707-712.
    • (2014) Neuromuscul Disord , vol.24 , pp. 707-712
    • Illingworth, M.A.1    Main, M.2    Pitt, M.3
  • 28
    • 79956088503 scopus 로고    scopus 로고
    • King-Denborough syndrome with and without mutations in the skeletal muscle ryanodine receptor (RYR1) gene
    • PID: 21514828
    • Dowling JJ, Lillis S, Amburgey K, et al. King-Denborough syndrome with and without mutations in the skeletal muscle ryanodine receptor (RYR1) gene. Neuromuscul Disord 2011;21:420-427.
    • (2011) Neuromuscul Disord , vol.21 , pp. 420-427
    • Dowling, J.J.1    Lillis, S.2    Amburgey, K.3
  • 29
    • 67349228165 scopus 로고    scopus 로고
    • Late-onset axial myopathy with cores due to a novel heterozygous dominant mutation in the skeletal muscle ryanodine receptor (RYR1) gene
    • PID: 19303294
    • Jungbluth H, Lillis S, Zhou H, et al. Late-onset axial myopathy with cores due to a novel heterozygous dominant mutation in the skeletal muscle ryanodine receptor (RYR1) gene. Neuromuscul Disord 2009;19:344-347.
    • (2009) Neuromuscul Disord , vol.19 , pp. 344-347
    • Jungbluth, H.1    Lillis, S.2    Zhou, H.3
  • 30
    • 84880966927 scopus 로고    scopus 로고
    • Genotype-phenotype correlations in recessive RYR1-related myopathies
    • PID: 23919265
    • Amburgey K, Bailey A, Hwang JH, et al. Genotype-phenotype correlations in recessive RYR1-related myopathies. Orphanet J Rare Dis 2013;8:117.
    • (2013) Orphanet J Rare Dis , vol.8 , pp. 117
    • Amburgey, K.1    Bailey, A.2    Hwang, J.H.3
  • 31
    • 44649184084 scopus 로고    scopus 로고
    • Congenital muscle disorders with cores: the ryanodine receptor calcium channel paradigm
    • PID: 18313359, COI: 1:CAS:528:DC%2BD1cXmvVyls70%3D
    • Treves S, Jungbluth H, Muntoni F, Zorzato F. Congenital muscle disorders with cores: the ryanodine receptor calcium channel paradigm. Curr Opin Pharmacol 2008;8:319-326.
    • (2008) Curr Opin Pharmacol , vol.8 , pp. 319-326
    • Treves, S.1    Jungbluth, H.2    Muntoni, F.3    Zorzato, F.4
  • 32
    • 8844266044 scopus 로고    scopus 로고
    • Pilot trial of salbutamol in central core and multi-minicore diseases
    • PID: 15534757, COI: 1:CAS:528:DC%2BD2cXhtFChurzL
    • Messina S, Hartley L, Main M, et al. Pilot trial of salbutamol in central core and multi-minicore diseases. Neuropediatrics 2004;35:262-266.
    • (2004) Neuropediatrics , vol.35 , pp. 262-266
    • Messina, S.1    Hartley, L.2    Main, M.3
  • 33
    • 84860156013 scopus 로고    scopus 로고
    • Oxidative stress and successful antioxidant treatment in models of RYR1-related myopathy
    • PID: 22418739
    • Dowling JJ, Arbogast S, Hur J, et al. Oxidative stress and successful antioxidant treatment in models of RYR1-related myopathy. Brain 2012;135:1115-1127.
    • (2012) Brain , vol.135 , pp. 1115-1127
    • Dowling, J.J.1    Arbogast, S.2    Hur, J.3
  • 34
    • 78649324563 scopus 로고    scopus 로고
    • Fixing ryanodine receptor Ca leak – a novel therapeutic strategy for contractile failure in heart and skeletal muscle
    • COI: 1:CAS:528:DC%2BC3MXht1ehtLo%3D
    • Andersson DC, Marks AR. Fixing ryanodine receptor Ca leak – a novel therapeutic strategy for contractile failure in heart and skeletal muscle. Drug Discov Today Dis Mechan 2010;7:e151-e157.
    • (2010) Drug Discov Today Dis Mechan , vol.7 , pp. e151-e157
    • Andersson, D.C.1    Marks, A.R.2
  • 35
    • 84869016830 scopus 로고    scopus 로고
    • Allele-specific gene silencing in two mouse models of autosomal dominant skeletal myopathy
    • PID: 23152933, COI: 1:CAS:528:DC%2BC38XhslCqu7bL
    • Loy RE, Lueck JD, Mostajo-Radji MA, Carrell EM, Dirksen RT. Allele-specific gene silencing in two mouse models of autosomal dominant skeletal myopathy. PloS One 2012;7:e49757.
    • (2012) PloS One , vol.7 , pp. e49757
    • Loy, R.E.1    Lueck, J.D.2    Mostajo-Radji, M.A.3    Carrell, E.M.4    Dirksen, R.T.5
  • 36
    • 84855404652 scopus 로고    scopus 로고
    • Prevalence of congenital myopathies in a representative pediatric united states population
    • PID: 22028225
    • Amburgey K, McNamara N, Bennett LR, McCormick ME, Acsadi G, Dowling JJ. Prevalence of congenital myopathies in a representative pediatric united states population. Ann Neurol 2011;70:662-665.
    • (2011) Ann Neurol , vol.70 , pp. 662-665
    • Amburgey, K.1    McNamara, N.2    Bennett, L.R.3    McCormick, M.E.4    Acsadi, G.5    Dowling, J.J.6
  • 37
    • 85027947938 scopus 로고    scopus 로고
    • Congenital myopathies–clinical features and frequency of individual subtypes diagnosed over a 5-year period in the United Kingdom
    • PID: 23394784, COI: 1:STN:280:DC%2BC3szmvVGnsA%3D%3D
    • Maggi L, Scoto M, Cirak S, et al. Congenital myopathies–clinical features and frequency of individual subtypes diagnosed over a 5-year period in the United Kingdom. Neuromuscul Disord 2013;23:195-205.
    • (2013) Neuromuscul Disord , vol.23 , pp. 195-205
    • Maggi, L.1    Scoto, M.2    Cirak, S.3
  • 38
    • 0028919291 scopus 로고
    • Abnormal junctions between surface membrane and sarcoplasmic reticulum in skeletal muscle with a mutation targeted to the ryanodine receptor
    • PID: 7724570, COI: 1:CAS:528:DyaK2MXltFSnurY%3D
    • Takekura H, Nishi M, Noda T, Takeshima H, Franzini-Armstrong C. Abnormal junctions between surface membrane and sarcoplasmic reticulum in skeletal muscle with a mutation targeted to the ryanodine receptor. Proc Natl Acad Sci U S A 1995;92:3381-3385.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 3381-3385
    • Takekura, H.1    Nishi, M.2    Noda, T.3    Takeshima, H.4    Franzini-Armstrong, C.5
  • 39
    • 34548148904 scopus 로고    scopus 로고
    • Zebrafish relatively relaxed mutants have a ryanodine receptor defect, show slow swimming and provide a model of multi-minicore disease
    • PID: 17596281, COI: 1:CAS:528:DC%2BD2sXhtVWnu7%2FK
    • Hirata H, Watanabe T, Hatakeyama J, et al. Zebrafish relatively relaxed mutants have a ryanodine receptor defect, show slow swimming and provide a model of multi-minicore disease. Development 2007;134:2771-2781.
    • (2007) Development , vol.134 , pp. 2771-2781
    • Hirata, H.1    Watanabe, T.2    Hatakeyama, J.3
  • 40
    • 77952670574 scopus 로고    scopus 로고
    • Ryanodine receptor studies using genetically engineered mice
    • PID: 20214899, COI: 1:CAS:528:DC%2BC3cXlvVarurs%3D
    • Kushnir A, Betzenhauser MJ, Marks AR. Ryanodine receptor studies using genetically engineered mice. FEBS Lett 2010;584:1956-1965.
    • (2010) FEBS Lett , vol.584 , pp. 1956-1965
    • Kushnir, A.1    Betzenhauser, M.J.2    Marks, A.R.3
  • 42
    • 84866538873 scopus 로고    scopus 로고
    • Clinical utility gene card for: Centronuclear and myotubular myopathies
    • Biancalana V, Beggs AH, Das S, et al. Clinical utility gene card for: Centronuclear and myotubular myopathies. Eur J Hum Genet 2012;20.
    • (2012) Eur J Hum Genet , pp. 20
    • Biancalana, V.1    Beggs, A.H.2    Das, S.3
  • 43
    • 9044222886 scopus 로고    scopus 로고
    • A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast
    • PID: 8640223, COI: 1:CAS:528:DyaK28XktlOhtbY%3D
    • Laporte J, Hu LJ, Kretz C, et al. A gene mutated in X-linked myotubular myopathy defines a new putative tyrosine phosphatase family conserved in yeast. Nat Genet 1996;13:175-182.
    • (1996) Nat Genet , vol.13 , pp. 175-182
    • Laporte, J.1    Hu, L.J.2    Kretz, C.3
  • 45
    • 27644543614 scopus 로고    scopus 로고
    • Mutations in dynamin 2 cause dominant centronuclear myopathy
    • PID: 16227997, COI: 1:CAS:528:DC%2BD2MXhtFGhsL3E
    • Bitoun M, Maugenre S, Jeannet PY, et al. Mutations in dynamin 2 cause dominant centronuclear myopathy. Nat Genet 2005;37:1207-1209.
    • (2005) Nat Genet , vol.37 , pp. 1207-1209
    • Bitoun, M.1    Maugenre, S.2    Jeannet, P.Y.3
  • 46
    • 84865240323 scopus 로고    scopus 로고
    • Mutation spectrum in the large GTPase dynamin 2, and genotype-phenotype correlation in autosomal dominant centronuclear myopathy
    • PID: 22396310, COI: 1:CAS:528:DC%2BC38XhtVOmur7J
    • Bohm J, Biancalana V, Dechene ET, et al. Mutation spectrum in the large GTPase dynamin 2, and genotype-phenotype correlation in autosomal dominant centronuclear myopathy. Hum Mutat 2012;33:949-959.
    • (2012) Hum Mutat , vol.33 , pp. 949-959
    • Bohm, J.1    Biancalana, V.2    Dechene, E.T.3
  • 47
    • 34548341774 scopus 로고    scopus 로고
    • Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy
    • PID: 17676042, COI: 1:CAS:528:DC%2BD2sXps12gtLo%3D
    • Nicot AS, Toussaint A, Tosch V, et al. Mutations in amphiphysin 2 (BIN1) disrupt interaction with dynamin 2 and cause autosomal recessive centronuclear myopathy. Nat Genet 2007;39:1134-1139.
    • (2007) Nat Genet , vol.39 , pp. 1134-1139
    • Nicot, A.S.1    Toussaint, A.2    Tosch, V.3
  • 48
    • 84886409449 scopus 로고    scopus 로고
    • Recessive truncating titin gene, TTN, mutations presenting as centronuclear myopathy
    • PID: 23975875, COI: 1:CAS:528:DC%2BC3sXhsFOks73I
    • Ceyhan-Birsoy O, Agrawal PB, Hidalgo C, et al. Recessive truncating titin gene, TTN, mutations presenting as centronuclear myopathy. Neurology 2013;81:1205-1214.
    • (2013) Neurology , vol.81 , pp. 1205-1214
    • Ceyhan-Birsoy, O.1    Agrawal, P.B.2    Hidalgo, C.3
  • 49
    • 84888356966 scopus 로고    scopus 로고
    • Titin and centronuclear myopathy: The tip of the iceberg for TTN-ic mutations?
    • PID: 23975873
    • Dowling JJ. Titin and centronuclear myopathy: The tip of the iceberg for TTN-ic mutations? Neurology 2013;81:1189-1190.
    • (2013) Neurology , vol.81 , pp. 1189-1190
    • Dowling, J.J.1
  • 51
    • 84885910544 scopus 로고    scopus 로고
    • Dynamin 2 homozygous mutation in humans with a lethal congenital syndrome
    • PID: 23092955, COI: 1:CAS:528:DC%2BC3sXnvFyhtb8%3D
    • Koutsopoulos OS, Kretz C, Weller CM, et al. Dynamin 2 homozygous mutation in humans with a lethal congenital syndrome. Eur J Hum Genet 2013;21:637-642.
    • (2013) Eur J Hum Genet , vol.21 , pp. 637-642
    • Koutsopoulos, O.S.1    Kretz, C.2    Weller, C.M.3
  • 52
    • 61449203897 scopus 로고    scopus 로고
    • Loss of myotubularin function results in T-tubule disorganization in zebrafish and human myotubular myopathy
    • PID: 19197364
    • Dowling JJ, Vreede AP, Low SE, et al. Loss of myotubularin function results in T-tubule disorganization in zebrafish and human myotubular myopathy. PLoS Genet 2009;5:e1000372.
    • (2009) PLoS Genet , vol.5 , pp. e1000372
    • Dowling, J.J.1    Vreede, A.P.2    Low, S.E.3
  • 53
    • 73249136944 scopus 로고    scopus 로고
    • T-tubule disorganization and defective excitation-contraction coupling in muscle fibers lacking myotubularin lipid phosphatase
    • PID: 19846786, COI: 1:CAS:528:DC%2BD1MXhsVKmtL3I
    • Al-Qusairi L, Weiss N, Toussaint A, et al. T-tubule disorganization and defective excitation-contraction coupling in muscle fibers lacking myotubularin lipid phosphatase. Proc Natl Acad Sci U S A 2009;106:18763-18768.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 18763-18768
    • Al-Qusairi, L.1    Weiss, N.2    Toussaint, A.3
  • 54
    • 79451471885 scopus 로고    scopus 로고
    • Defects in amphiphysin 2 (BIN1) and triads in several forms of centronuclear myopathies
    • PID: 20927630
    • Toussaint A, Cowling BS, Hnia K, et al. Defects in amphiphysin 2 (BIN1) and triads in several forms of centronuclear myopathies. Acta Neuropathol 2011;121:253-266.
    • (2011) Acta Neuropathol , vol.121 , pp. 253-266
    • Toussaint, A.1    Cowling, B.S.2    Hnia, K.3
  • 55
    • 78649471271 scopus 로고    scopus 로고
    • A centronuclear myopathy-dynamin 2 mutation impairs skeletal muscle structure and function in mice
    • PID: 20858595, COI: 1:CAS:528:DC%2BC3cXhsVyhsr%2FK
    • Durieux AC, Vignaud A, Prudhon B, et al. A centronuclear myopathy-dynamin 2 mutation impairs skeletal muscle structure and function in mice. Hum Mol Genet 2010;19:4820-4836.
    • (2010) Hum Mol Genet , vol.19 , pp. 4820-4836
    • Durieux, A.C.1    Vignaud, A.2    Prudhon, B.3
  • 56
    • 84892429399 scopus 로고    scopus 로고
    • The myopathy-causing mutation DNM2-S619L leads to defective tubulation in vitro and in developing zebrafish
    • COI: 1:CAS:528:DC%2BC2cXntVCmt74%3D
    • Gibbs EM, Davidson AE, Telfer WR, Feldman EL, Dowling JJ. The myopathy-causing mutation DNM2-S619L leads to defective tubulation in vitro and in developing zebrafish. Dis Models Mechan 2014;7:157-161.
    • (2014) Dis Models Mechan , vol.7 , pp. 157-161
    • Gibbs, E.M.1    Davidson, A.E.2    Telfer, W.R.3    Feldman, E.L.4    Dowling, J.J.5
  • 57
    • 84902343047 scopus 로고    scopus 로고
    • Bridging integrator 1 (Bin1) deficiency in zebrafish results in centronuclear myopathy
    • PID: 24549043, COI: 1:CAS:528:DC%2BC2cXpvV2rsbo%3D
    • Smith LL, Gupta VA, Beggs AH. Bridging integrator 1 (Bin1) deficiency in zebrafish results in centronuclear myopathy. Hum Mol Genet 2014;23:3566-3578.
    • (2014) Hum Mol Genet , vol.23 , pp. 3566-3578
    • Smith, L.L.1    Gupta, V.A.2    Beggs, A.H.3
  • 58
    • 0037119615 scopus 로고    scopus 로고
    • Amphiphysin 2 (Bin1) and T-tubule biogenesis in muscle
    • PID: 12183633, COI: 1:CAS:528:DC%2BD38XmsVOhtbc%3D
    • Lee E, Marcucci M, Daniell L, et al. Amphiphysin 2 (Bin1) and T-tubule biogenesis in muscle. Science 2002;297:1193-1196.
    • (2002) Science , vol.297 , pp. 1193-1196
    • Lee, E.1    Marcucci, M.2    Daniell, L.3
  • 59
    • 84881137026 scopus 로고    scopus 로고
    • Lack of myotubularin (MTM1) leads to muscle hypotrophy through unbalanced regulation of the autophagy and ubiquitin-proteasome pathways
    • PID: 23695157, COI: 1:CAS:528:DC%2BC3sXht1OgtLbJ
    • Al-Qusairi L, Prokic I, Amoasii L, et al. Lack of myotubularin (MTM1) leads to muscle hypotrophy through unbalanced regulation of the autophagy and ubiquitin-proteasome pathways. FASEB J 2013;27:3384-3394.
    • (2013) FASEB J , vol.27 , pp. 3384-3394
    • Al-Qusairi, L.1    Prokic, I.2    Amoasii, L.3
  • 60
    • 84871879503 scopus 로고    scopus 로고
    • Defective autophagy and mTORC1 signaling in myotubularin null mice
    • PID: 23109424, COI: 1:CAS:528:DC%2BC3sXlt1SktL0%3D
    • Fetalvero KM, Yu Y, Goetschkes M, et al. Defective autophagy and mTORC1 signaling in myotubularin null mice. Mol Cell Biol 2013;33:98-110.
    • (2013) Mol Cell Biol , vol.33 , pp. 98-110
    • Fetalvero, K.M.1    Yu, Y.2    Goetschkes, M.3
  • 61
    • 78650942651 scopus 로고    scopus 로고
    • Myotubularin controls desmin intermediate filament architecture and mitochondrial dynamics in human and mouse skeletal muscle
    • PID: 21135508, COI: 1:CAS:528:DC%2BC3MXis1ynsg%3D%3D
    • Hnia K, Tronchere H, Tomczak KK, et al. Myotubularin controls desmin intermediate filament architecture and mitochondrial dynamics in human and mouse skeletal muscle. J Clin Invest 2011;121:70-85.
    • (2011) J Clin Invest , vol.121 , pp. 70-85
    • Hnia, K.1    Tronchere, H.2    Tomczak, K.K.3
  • 62
    • 84870051787 scopus 로고    scopus 로고
    • Myotubular myopathy and the neuromuscular junction: a novel therapeutic approach from mouse models
    • COI: 1:CAS:528:DC%2BC3sXnt1Ojug%3D%3D
    • Dowling JJ, Joubert R, Low SE, et al. Myotubular myopathy and the neuromuscular junction: a novel therapeutic approach from mouse models. Dis Models Mechan 2012;5:852-859.
    • (2012) Dis Models Mechan , vol.5 , pp. 852-859
    • Dowling, J.J.1    Joubert, R.2    Low, S.E.3
  • 63
    • 79956125843 scopus 로고    scopus 로고
    • Impaired neuromuscular transmission and response to acetylcholinesterase inhibitors in centronuclear myopathies
    • PID: 21440438
    • Robb SA, Sewry CA, Dowling JJ, et al. Impaired neuromuscular transmission and response to acetylcholinesterase inhibitors in centronuclear myopathies. Neuromuscul Disord 2011;21:379-386.
    • (2011) Neuromuscul Disord , vol.21 , pp. 379-386
    • Robb, S.A.1    Sewry, C.A.2    Dowling, J.J.3
  • 64
    • 84893427190 scopus 로고    scopus 로고
    • Gene therapy prolongs survival and restores function in murine and canine models of myotubular myopathy
    • Childers MK, Joubert R, Poulard K, et al. Gene therapy prolongs survival and restores function in murine and canine models of myotubular myopathy. Sci Transl Med 2014;6:220–10.
    • (2014) Sci Transl Med , vol.6 , pp. 220-210
    • Childers, M.K.1    Joubert, R.2    Poulard, K.3
  • 65
    • 84875766052 scopus 로고    scopus 로고
    • Enzyme replacement therapy rescues weakness and improves muscle pathology in mice with X-linked myotubular myopathy
    • PID: 23307925, COI: 1:CAS:528:DC%2BC3sXksFWhsrk%3D
    • Lawlor MW, Armstrong D, Viola MG, et al. Enzyme replacement therapy rescues weakness and improves muscle pathology in mice with X-linked myotubular myopathy. Hum Mol Genet 2013;22:1525-1538.
    • (2013) Hum Mol Genet , vol.22 , pp. 1525-1538
    • Lawlor, M.W.1    Armstrong, D.2    Viola, M.G.3
  • 66
    • 84878526600 scopus 로고    scopus 로고
    • Neuromuscular junction abnormalities in DNM2-related centronuclear myopathy
    • PID: 23338057, COI: 1:CAS:528:DC%2BC3sXotV2nsbg%3D
    • Gibbs EM, Clarke NF, Rose K, et al. Neuromuscular junction abnormalities in DNM2-related centronuclear myopathy. J Mol Med 2013;91:727-737.
    • (2013) J Mol Med , vol.91 , pp. 727-737
    • Gibbs, E.M.1    Clarke, N.F.2    Rose, K.3
  • 67
    • 47349114975 scopus 로고    scopus 로고
    • Native American myopathy: congenital myopathy with cleft palate, skeletal anomalies, and susceptibility to malignant hyperthermia
    • PID: 18553514, COI: 1:CAS:528:DC%2BD1cXpsFOku7o%3D
    • Stamm DS, Aylsworth AS, Stajich JM, et al. Native American myopathy: congenital myopathy with cleft palate, skeletal anomalies, and susceptibility to malignant hyperthermia. Am J Med Genet A 2008;146A:1832-1841.
    • (2008) Am J Med Genet A , vol.146A , pp. 1832-1841
    • Stamm, D.S.1    Aylsworth, A.S.2    Stajich, J.M.3
  • 68
    • 84891642547 scopus 로고    scopus 로고
    • Stac3 is a component of the excitation-contraction coupling machinery and mutated in Native American myopathy
    • PID: 23736855
    • Horstick EJ, Linsley JW, Dowling JJ, et al. Stac3 is a component of the excitation-contraction coupling machinery and mutated in Native American myopathy. Nat Commun 2013;4:1952.
    • (2013) Nat Commun , vol.4 , pp. 1952
    • Horstick, E.J.1    Linsley, J.W.2    Dowling, J.J.3
  • 69
    • 84880391617 scopus 로고    scopus 로고
    • Skeletal muscle-specific T-tubule protein STAC3 mediates voltage-induced Ca2+ release and contractility
    • PID: 23818578, COI: 1:CAS:528:DC%2BC3sXht1emurjL
    • Nelson BR, Wu F, Liu Y, et al. Skeletal muscle-specific T-tubule protein STAC3 mediates voltage-induced Ca2+ release and contractility. Proc Natl Acad Sci U S A 2013;110:11881-11886.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 11881-11886
    • Nelson, B.R.1    Wu, F.2    Liu, Y.3
  • 70
    • 53349168381 scopus 로고    scopus 로고
    • Tubular aggregate myopathy: a rare form of myopathy
    • PID: 18824361, COI: 1:CAS:528:DC%2BD1cXht1ejtbzP
    • Jain D, Sharma MC, Sarkar C, et al. Tubular aggregate myopathy: a rare form of myopathy. J Clin Neurosci 2008;15:1222-1226.
    • (2008) J Clin Neurosci , vol.15 , pp. 1222-1226
    • Jain, D.1    Sharma, M.C.2    Sarkar, C.3
  • 71
    • 84898785230 scopus 로고    scopus 로고
    • A dominant STIM1 mutation causes Stormorken syndrome
    • PID: 24619930, COI: 1:CAS:528:DC%2BC2cXmvF2kt7w%3D
    • Misceo D, Holmgren A, Louch WE, et al. A dominant STIM1 mutation causes Stormorken syndrome. Hum Mutat 2014;35:556-564.
    • (2014) Hum Mutat , vol.35 , pp. 556-564
    • Misceo, D.1    Holmgren, A.2    Louch, W.E.3
  • 72
    • 84896540324 scopus 로고    scopus 로고
    • Activating mutations in STIM1 and ORAI1 cause overlapping syndromes of tubular myopathy and congenital miosis
    • PID: 24591628, COI: 1:CAS:528:DC%2BC2cXjtl2ju7o%3D
    • Nesin V, Wiley G, Kousi M, et al. Activating mutations in STIM1 and ORAI1 cause overlapping syndromes of tubular myopathy and congenital miosis. Proc Natl Acad Sci U S A 2014;111:4197-4202.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 4197-4202
    • Nesin, V.1    Wiley, G.2    Kousi, M.3
  • 73
    • 84873724303 scopus 로고    scopus 로고
    • Constitutive activation of the calcium sensor STIM1 causes tubular-aggregate myopathy
    • PID: 23332920, COI: 1:CAS:528:DC%2BC3sXht1GgurY%3D
    • Bohm J, Chevessier F, Maues De Paula A, et al. Constitutive activation of the calcium sensor STIM1 causes tubular-aggregate myopathy. Am J Hum Genet 2013;92:271-278.
    • (2013) Am J Hum Genet , vol.92 , pp. 271-278
    • Bohm, J.1    Chevessier, F.2    Maues De Paula, A.3
  • 74
    • 70349116421 scopus 로고    scopus 로고
    • ORAI1 and STIM1 deficiency in human and mice: roles of store-operated Ca2+ entry in the immune system and beyond
    • PID: 19754898, COI: 1:CAS:528:DC%2BD1MXhsFGlsL%2FN
    • Feske S. ORAI1 and STIM1 deficiency in human and mice: roles of store-operated Ca2+ entry in the immune system and beyond. Immunol Rev 2009;231:189-209.
    • (2009) Immunol Rev , vol.231 , pp. 189-209
    • Feske, S.1
  • 75
    • 67650382292 scopus 로고    scopus 로고
    • Checking your SOCCs and feet: the molecular mechanisms of Ca2+ entry in skeletal muscle
    • PID: 19406875, COI: 1:CAS:528:DC%2BD1MXosleqtb4%3D
    • Dirksen RT. Checking your SOCCs and feet: the molecular mechanisms of Ca2+ entry in skeletal muscle. J Physiol 2009;587:3139-3147.
    • (2009) J Physiol , vol.587 , pp. 3139-3147
    • Dirksen, R.T.1
  • 76
    • 84890960702 scopus 로고    scopus 로고
    • STIM1/Orai1 coiled-coil interplay in the regulation of store-operated calcium entry
    • PID: 24351972
    • Stathopulos PB, Schindl R, Fahrner M, et al. STIM1/Orai1 coiled-coil interplay in the regulation of store-operated calcium entry. Nat Commun 2013;4:2963.
    • (2013) Nat Commun , vol.4 , pp. 2963
    • Stathopulos, P.B.1    Schindl, R.2    Fahrner, M.3
  • 78
    • 84885446786 scopus 로고    scopus 로고
    • Accelerated activation of SOCE current in myotubes from two mouse models of anesthetic- and heat-induced sudden death
    • PID: 24143248, COI: 1:CAS:528:DC%2BC3sXhs1Kiu7zJ
    • Yarotskyy V, Protasi F, Dirksen RT. Accelerated activation of SOCE current in myotubes from two mouse models of anesthetic- and heat-induced sudden death. PloS One 2013;8:e77633.
    • (2013) PloS One , vol.8 , pp. e77633
    • Yarotskyy, V.1    Protasi, F.2    Dirksen, R.T.3
  • 79
    • 77955504257 scopus 로고    scopus 로고
    • Store-operated Ca2+ entry in malignant hyperthermia-susceptible human skeletal muscle
    • PID: 20566647, COI: 1:CAS:528:DC%2BC3cXpslKjtbc%3D
    • Duke AM, Hopkins PM, Calaghan SC, Halsall JP, Steele DS. Store-operated Ca2+ entry in malignant hyperthermia-susceptible human skeletal muscle. J Biol Chem 2010;285:25645-25653.
    • (2010) J Biol Chem , vol.285 , pp. 25645-25653
    • Duke, A.M.1    Hopkins, P.M.2    Calaghan, S.C.3    Halsall, J.P.4    Steele, D.S.5
  • 80
    • 0031782620 scopus 로고    scopus 로고
    • Tubular aggregates in skeletal muscle: their functional significance and mechanisms of pathogenesis
    • PID: 9847992, COI: 1:STN:280:DyaK1M%2FmsVCmug%3D%3D
    • Morgan-Hughes JA. Tubular aggregates in skeletal muscle: their functional significance and mechanisms of pathogenesis. Curr Opin Neurol 1998;11:439-442.
    • (1998) Curr Opin Neurol , vol.11 , pp. 439-442
    • Morgan-Hughes, J.A.1
  • 81
    • 84862338483 scopus 로고    scopus 로고
    • Sequential stages in the age-dependent gradual formation and accumulation of tubular aggregates in fast twitch muscle fibers: SERCA and calsequestrin involvement
    • PID: 21318331, COI: 1:CAS:528:DC%2BC38XhtFShuro%3D
    • Boncompagni S, Protasi F, Franzini-Armstrong C. Sequential stages in the age-dependent gradual formation and accumulation of tubular aggregates in fast twitch muscle fibers: SERCA and calsequestrin involvement. Age 2012;34:27-41.
    • (2012) Age , vol.34 , pp. 27-41
    • Boncompagni, S.1    Protasi, F.2    Franzini-Armstrong, C.3
  • 82
    • 84866436425 scopus 로고    scopus 로고
    • The myotonic dystrophies: molecular, clinical, and therapeutic challenges
    • PID: 22995693, COI: 1:CAS:528:DC%2BC38XhsVSns7fK
    • Udd B, Krahe R. The myotonic dystrophies: molecular, clinical, and therapeutic challenges. Lancet Neurol 2012;11:891-905.
    • (2012) Lancet Neurol , vol.11 , pp. 891-905
    • Udd, B.1    Krahe, R.2
  • 83
    • 77950529265 scopus 로고    scopus 로고
    • RNA-mediated neurodegeneration in repeat expansion disorders
    • PID: 20373340, COI: 1:CAS:528:DC%2BC3cXlsFSlt7w%3D
    • Todd PK, Paulson HL. RNA-mediated neurodegeneration in repeat expansion disorders. Ann Neurol 2010;67:291-300.
    • (2010) Ann Neurol , vol.67 , pp. 291-300
    • Todd, P.K.1    Paulson, H.L.2
  • 84
    • 61449183565 scopus 로고    scopus 로고
    • Alternative splicing of RyR1 alters the efficacy of skeletal EC coupling
    • PID: 19131108, COI: 1:CAS:528:DC%2BD1MXivVemsLo%3D
    • Kimura T, Lueck JD, Harvey PJ, et al. Alternative splicing of RyR1 alters the efficacy of skeletal EC coupling. Cell Calcium 2009;45:264-274.
    • (2009) Cell Calcium , vol.45 , pp. 264-274
    • Kimura, T.1    Lueck, J.D.2    Harvey, P.J.3
  • 85
    • 26444444738 scopus 로고    scopus 로고
    • Altered mRNA splicing of the skeletal muscle ryanodine receptor and sarcoplasmic/endoplasmic reticulum Ca2 + -ATPase in myotonic dystrophy type 1
    • PID: 15972723, COI: 1:CAS:528:DC%2BD2MXmt1ertr8%3D
    • Kimura T, Nakamori M, Lueck JD, et al. Altered mRNA splicing of the skeletal muscle ryanodine receptor and sarcoplasmic/endoplasmic reticulum Ca2 + -ATPase in myotonic dystrophy type 1. Hum Mol Genet 2005;14:2189-2200.
    • (2005) Hum Mol Genet , vol.14 , pp. 2189-2200
    • Kimura, T.1    Nakamori, M.2    Lueck, J.D.3
  • 86
    • 84857662317 scopus 로고    scopus 로고
    • Muscle weakness in myotonic dystrophy associated with misregulated splicing and altered gating of Ca(V)1.1 calcium channel
    • PID: 22140091, COI: 1:CAS:528:DC%2BC38XivVejtLc%3D
    • Tang ZZ, Yarotskyy V, Wei L, et al. Muscle weakness in myotonic dystrophy associated with misregulated splicing and altered gating of Ca(V)1.1 calcium channel. Hum Mol Genet 2012;21:1312-1324.
    • (2012) Hum Mol Genet , vol.21 , pp. 1312-1324
    • Tang, Z.Z.1    Yarotskyy, V.2    Wei, L.3
  • 87
    • 79958101846 scopus 로고    scopus 로고
    • Misregulated alternative splicing of BIN1 is associated with T tubule alterations and muscle weakness in myotonic dystrophy
    • PID: 21623381, COI: 1:CAS:528:DC%2BC3MXmslSkurY%3D
    • Fugier C, Klein AF, Hammer C, et al. Misregulated alternative splicing of BIN1 is associated with T tubule alterations and muscle weakness in myotonic dystrophy. Nat Med 2011;17:720-725.
    • (2011) Nat Med , vol.17 , pp. 720-725
    • Fugier, C.1    Klein, A.F.2    Hammer, C.3
  • 88
    • 79954467500 scopus 로고    scopus 로고
    • Dystrophinopathies
    • PID: 21496622
    • Morrison LA. Dystrophinopathies. Handb Clin Neurol 2011;101:11-39.
    • (2011) Handb Clin Neurol , vol.101 , pp. 11-39
    • Morrison, L.A.1
  • 89
    • 84878544086 scopus 로고    scopus 로고
    • The cell biology of disease: cellular and molecular mechanisms underlying muscular dystrophy
    • PID: 23671309, COI: 1:CAS:528:DC%2BC3sXnsl2jtrY%3D
    • Rahimov F, Kunkel LM. The cell biology of disease: cellular and molecular mechanisms underlying muscular dystrophy. J Cell Biol 2013;201:499-510.
    • (2013) J Cell Biol , vol.201 , pp. 499-510
    • Rahimov, F.1    Kunkel, L.M.2
  • 90
    • 0024300196 scopus 로고
    • Immunoelectron microscopic localization of dystrophin in myofibres
    • PID: 3290684, COI: 1:CAS:528:DyaL1cXkslWmsrY%3D
    • Watkins SC, Hoffman EP, Slayter HS, Kunkel LM. Immunoelectron microscopic localization of dystrophin in myofibres. Nature 1988;333:863-866.
    • (1988) Nature , vol.333 , pp. 863-866
    • Watkins, S.C.1    Hoffman, E.P.2    Slayter, H.S.3    Kunkel, L.M.4
  • 91
    • 77951446319 scopus 로고    scopus 로고
    • Excitation-contraction coupling alterations in mdx and utrophin/dystrophin double knockout mice: a comparative study
    • PID: 20130206, COI: 1:CAS:528:DC%2BC3cXmtlWjs7g%3D
    • Capote J, DiFranco M, Vergara JL. Excitation-contraction coupling alterations in mdx and utrophin/dystrophin double knockout mice: a comparative study. Am J Physiol Cell Physiol 2010;298:C1077-C1086.
    • (2010) Am J Physiol Cell Physiol , vol.298 , pp. C1077-C1086
    • Capote, J.1    DiFranco, M.2    Vergara, J.L.3
  • 92
    • 61949338001 scopus 로고    scopus 로고
    • Hypernitrosylated ryanodine receptor calcium release channels are leaky in dystrophic muscle
    • PID: 19198614, COI: 1:CAS:528:DC%2BD1MXhsFeqs7g%3D
    • Bellinger AM, Reiken S, Carlson C, et al. Hypernitrosylated ryanodine receptor calcium release channels are leaky in dystrophic muscle. Nat Med 2009;15:325-330.
    • (2009) Nat Med , vol.15 , pp. 325-330
    • Bellinger, A.M.1    Reiken, S.2    Carlson, C.3
  • 93
    • 76549098001 scopus 로고    scopus 로고
    • Leaky RyR2 trigger ventricular arrhythmias in Duchenne muscular dystrophy
    • PID: 20080623, COI: 1:CAS:528:DC%2BC3cXhslOrs7s%3D
    • Fauconnier J, Thireau J, Reiken S, et al. Leaky RyR2 trigger ventricular arrhythmias in Duchenne muscular dystrophy. Proc Natl Acad Sci U S A 2010;107:1559-1564.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 1559-1564
    • Fauconnier, J.1    Thireau, J.2    Reiken, S.3
  • 94
    • 79952209778 scopus 로고    scopus 로고
    • Mitigation of muscular dystrophy in mice by SERCA overexpression in skeletal muscle
    • PID: 21285509, COI: 1:CAS:528:DC%2BC3MXjtVWktbc%3D
    • Goonasekera SA, Lam CK, Millay DP, et al. Mitigation of muscular dystrophy in mice by SERCA overexpression in skeletal muscle. J Clin Invest 2011;121:1044-1052.
    • (2011) J Clin Invest , vol.121 , pp. 1044-1052
    • Goonasekera, S.A.1    Lam, C.K.2    Millay, D.P.3
  • 96
    • 84874753450 scopus 로고    scopus 로고
    • Leaky ryanodine receptors in beta-sarcoglycan deficient mice: a potential common defect in muscular dystrophy
    • PID: 22640601, COI: 1:CAS:528:DC%2BC3sXnvVCjtr4%3D
    • Andersson DC, Meli AC, Reiken S, et al. Leaky ryanodine receptors in beta-sarcoglycan deficient mice: a potential common defect in muscular dystrophy. Skelet Muscle 2012;2:9.
    • (2012) Skelet Muscle , vol.2 , pp. 9
    • Andersson, D.C.1    Meli, A.C.2    Reiken, S.3
  • 98
    • 84897949693 scopus 로고    scopus 로고
    • Dysferlin at transverse tubules regulates Ca homeostasis in skeletal muscle
    • PID: 24639655
    • Kerr JP, Ward CW, Bloch RJ. Dysferlin at transverse tubules regulates Ca homeostasis in skeletal muscle. Front Physiol 2014;5:89.
    • (2014) Front Physiol , vol.5 , pp. 89
    • Kerr, J.P.1    Ward, C.W.2    Bloch, R.J.3
  • 99
    • 84890831113 scopus 로고    scopus 로고
    • Dysferlin stabilizes stress-induced Ca2+ signaling in the transverse tubule membrane
    • PID: 24302765, COI: 1:CAS:528:DC%2BC2cXnsV2juw%3D%3D
    • Kerr JP, Ziman AP, Mueller AL, et al. Dysferlin stabilizes stress-induced Ca2+ signaling in the transverse tubule membrane. Proc Natl Acad Sci U S A 2013;110:20831-20836.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , pp. 20831-20836
    • Kerr, J.P.1    Ziman, A.P.2    Mueller, A.L.3
  • 100
    • 79954476376 scopus 로고    scopus 로고
    • Limb-girdle muscular dystrophy 2A
    • PID: 21496626
    • Gallardo E, Saenz A, Illa I. Limb-girdle muscular dystrophy 2A. Handb Clin Neurol 2011;101:97-110.
    • (2011) Handb Clin Neurol , vol.101 , pp. 97-110
    • Gallardo, E.1    Saenz, A.2    Illa, I.3
  • 101
    • 54449100812 scopus 로고    scopus 로고
    • Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle
    • PID: 18676612, COI: 1:CAS:528:DC%2BD1cXht1entrjI
    • Kramerova I, Kudryashova E, Wu B, Ottenheijm C, Granzier H, Spencer MJ. Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle. Hum Mol Genet 2008;17:3271-3280.
    • (2008) Hum Mol Genet , vol.17 , pp. 3271-3280
    • Kramerova, I.1    Kudryashova, E.2    Wu, B.3    Ottenheijm, C.4    Granzier, H.5    Spencer, M.J.6
  • 102
    • 84867330926 scopus 로고    scopus 로고
    • Selenoprotein N in skeletal muscle: from diseases to function
    • PID: 22527882, COI: 1:CAS:528:DC%2BC38XhtlGhsbrN
    • Castets P, Lescure A, Guicheney P, Allamand V. Selenoprotein N in skeletal muscle: from diseases to function. J Mol Med 2012;90:1095-1107.
    • (2012) J Mol Med , vol.90 , pp. 1095-1107
    • Castets, P.1    Lescure, A.2    Guicheney, P.3    Allamand, V.4
  • 103
    • 77649249653 scopus 로고    scopus 로고
    • Selenoproteins and protection against oxidative stress: selenoprotein N as a novel player at the crossroads of redox signaling and calcium homeostasis
    • PID: 19769461, COI: 1:CAS:528:DC%2BC3cXksFOjsbo%3D
    • Arbogast S, Ferreiro A. Selenoproteins and protection against oxidative stress: selenoprotein N as a novel player at the crossroads of redox signaling and calcium homeostasis. Antioxid Redox Signal 2010;12:893-904.
    • (2010) Antioxid Redox Signal , vol.12 , pp. 893-904
    • Arbogast, S.1    Ferreiro, A.2
  • 104
    • 79961179963 scopus 로고    scopus 로고
    • Increased muscle stress-sensitivity induced by selenoprotein N inactivation in mouse: a mammalian model for SEPN1-related myopathy
    • PID: 21858002, COI: 1:CAS:528:DC%2BC3MXhtFanur3O
    • Rederstorff M, Castets P, Arbogast S, et al. Increased muscle stress-sensitivity induced by selenoprotein N inactivation in mouse: a mammalian model for SEPN1-related myopathy. PloS One 2011;6:e23094.
    • (2011) PloS One , vol.6 , pp. e23094
    • Rederstorff, M.1    Castets, P.2    Arbogast, S.3
  • 105
    • 78751683606 scopus 로고    scopus 로고
    • Satellite cell loss and impaired muscle regeneration in selenoprotein N deficiency
    • PID: 21131290, COI: 1:CAS:528:DC%2BC3MXpsFyhsQ%3D%3D
    • Castets P, Bertrand AT, Beuvin M, et al. Satellite cell loss and impaired muscle regeneration in selenoprotein N deficiency. Hum Mol Genet 2011;20:694-704.
    • (2011) Hum Mol Genet , vol.20 , pp. 694-704
    • Castets, P.1    Bertrand, A.T.2    Beuvin, M.3
  • 107
    • 50449088082 scopus 로고    scopus 로고
    • Selenoprotein N is required for ryanodine receptor calcium release channel activity in human and zebrafish muscle
    • PID: 18713863, COI: 1:CAS:528:DC%2BD1cXhtVKqtr7E
    • Jurynec MJ, Xia R, Mackrill JJ, et al. Selenoprotein N is required for ryanodine receptor calcium release channel activity in human and zebrafish muscle. Proc Natl Acad Sci U S A 2008;105:12485-12490.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 12485-12490
    • Jurynec, M.J.1    Xia, R.2    Mackrill, J.J.3
  • 108
    • 67650066807 scopus 로고    scopus 로고
    • Oxidative stress in SEPN1-related myopathy: from pathophysiology to treatment
    • PID: 19557870, COI: 1:CAS:528:DC%2BD1MXpt1Onsbg%3D
    • Arbogast S, Beuvin M, Fraysse B, Zhou H, Muntoni F, Ferreiro A. Oxidative stress in SEPN1-related myopathy: from pathophysiology to treatment. Ann Neurol 2009;65:677-686.
    • (2009) Ann Neurol , vol.65 , pp. 677-686
    • Arbogast, S.1    Beuvin, M.2    Fraysse, B.3    Zhou, H.4    Muntoni, F.5    Ferreiro, A.6
  • 109
    • 69949177485 scopus 로고    scopus 로고
    • Selenoprotein N is dynamically expressed during mouse development and detected early in muscle precursors
    • Castets P, Maugenre S, Gartioux C, et al. Selenoprotein N is dynamically expressed during mouse development and detected early in muscle precursors. BMC Develop Biol 2009;9:46.
    • (2009) BMC Develop Biol , vol.9 , pp. 46
    • Castets, P.1    Maugenre, S.2    Gartioux, C.3
  • 110
    • 84864940150 scopus 로고    scopus 로고
    • Dominant mutation of CCDC78 in a unique congenital myopathy with prominent internal nuclei and atypical cores
    • PID: 22818856, COI: 1:CAS:528:DC%2BC38XhtVOltr3J
    • Majczenko K, Davidson AE, Camelo-Piragua S, et al. Dominant mutation of CCDC78 in a unique congenital myopathy with prominent internal nuclei and atypical cores. Am J Hum Genet 2012;91:365-371.
    • (2012) Am J Hum Genet , vol.91 , pp. 365-371
    • Majczenko, K.1    Davidson, A.E.2    Camelo-Piragua, S.3


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