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Lehtokari VL, Ceuterick-de Groote C, de Jonghe P, et al. Cap disease caused by heterozygous deletion of the beta-tropomyosin gene TPM2. Neuromuscul Disord 2007; 17:433-442. This paper describes the first gene identified for cap disease as mutated β-tropomyosin (TPM2). The mutation is a single amino acid deletion, a type of mutation not previously seen in TPM2, where other types of mutations have previously been associated with nemaline myopathy or distal arthrogryposis.
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Jungbluth H, Zhou H, Sewry CA, et al. Centronuclear myopathy due to a de novo dominant mutation in the skeletal muscle ryanodine receptor (RYR1) gene. Neuromuscul Disord 2007; 17:338-345. This paper suggests that mutations in the ryanodine receptor gene RYR1 may also result in a centronuclear myopathy histopathological phenotype and therefore that RYR1 mutation has to be considered if such a phenotype is seen on histopathological examination in addition to dynamin mutations and MTM1 mutation.
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Jungbluth H, Zhou H, Sewry CA, et al. Centronuclear myopathy due to a de novo dominant mutation in the skeletal muscle ryanodine receptor (RYR1) gene. Neuromuscul Disord 2007; 17:338-345. This paper suggests that mutations in the ryanodine receptor gene RYR1 may also result in a centronuclear myopathy histopathological phenotype and therefore that RYR1 mutation has to be considered if such a phenotype is seen on histopathological examination in addition to dynamin mutations and MTM1 mutation.
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Actin mutations are one cause of congenital fibre type disproportion
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Clarke NF, Kidson W, Quijano-Roy S, et al. SEPN1: associated with congenital fiber-type disproportion and insulin resistance. Ann Neurol 2006; 59:546-552. This paper demonstrates for the first time that SEPN1 mutations may account for patients with a working diagnosis of congenital fibre type disproportion.
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Clarke NF, Kidson W, Quijano-Roy S, et al. SEPN1: associated with congenital fiber-type disproportion and insulin resistance. Ann Neurol 2006; 59:546-552. This paper demonstrates for the first time that SEPN1 mutations may account for patients with a working diagnosis of congenital fibre type disproportion.
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Agrawal PB, Greenleaf RS, Tomczak KK, et al. Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2. Am J Hum Genet 2007; 80:162-167. This paper identifies the sixth known genetic cause of nemaline myopathy as mutated muscle-specific cofilin CFL2. The authors found a homozygous mutation of CFL2 segregating with nemaline myopathy in one family of Middle Eastern origin.
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Agrawal PB, Greenleaf RS, Tomczak KK, et al. Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2. Am J Hum Genet 2007; 80:162-167. This paper identifies the sixth known genetic cause of nemaline myopathy as mutated muscle-specific cofilin CFL2. The authors found a homozygous mutation of CFL2 segregating with nemaline myopathy in one family of Middle Eastern origin.
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A mutation in the a-tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy
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A novel nemaline myopathy in the Amish caused by a mutation in troponin T1
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Nowak KJ, Sewry CA, Navarro C, et al. Nemaline myopathy caused by absence of alpha-skeletal muscle actin. Ann Neurol 2007; 61:175-184. This paper describes for the first time patients from various consanguineous ethnic groups homozygous for different null mutations in the skeletal muscle actin gene ACTA1. The patients have no skeletal actin but have increased cardiac actin in their skeletal muscles, cardiac actin being the fetal isoform of actin in skeletal muscle. The increased cardiac actin partially compensates for the absence of skeletal actin. Some of the patients have zebra bodies in their muscle, suggesting that mutations of actin may be the cause of the previously described zebra body myopathy.
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Nowak KJ, Sewry CA, Navarro C, et al. Nemaline myopathy caused by absence of alpha-skeletal muscle actin. Ann Neurol 2007; 61:175-184. This paper describes for the first time patients from various consanguineous ethnic groups homozygous for different null mutations in the skeletal muscle actin gene ACTA1. The patients have no skeletal actin but have increased cardiac actin in their skeletal muscles, cardiac actin being the fetal isoform of actin in skeletal muscle. The increased cardiac actin partially compensates for the absence of skeletal actin. Some of the patients have zebra bodies in their muscle, suggesting that mutations of actin may be the cause of the previously described zebra body myopathy.
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33847146380
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A congenital myopathy with diaphragmatic weakness not linked to the SMARD1 locus
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This paper suggests the existence of a novel congenital myopathy
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Hartley L, Kinali M, Knight R, et al. A congenital myopathy with diaphragmatic weakness not linked to the SMARD1 locus. Neuromuscul Disord 2007; 17:174-179. This paper suggests the existence of a novel congenital myopathy.
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Hartley, L.1
Kinali, M.2
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A benign congenital myopathy in an inbred Samaritan family
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This paper suggests the existence of a novel congenital myopathy
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Lev D, Sadeh M, Watemberg N, et al. A benign congenital myopathy in an inbred Samaritan family. Eur J Paediatr Neurol 2006; 10:182-185. This paper suggests the existence of a novel congenital myopathy.
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Lev, D.1
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Mutations in genes encoding fast-twitch contractile proteins cause distal arthrogryposis syndromes
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Zhou H, Brockington M, Jungbluth H, et al. Epigenetic allele silencing unveils recessive RYR1 mutations in core myopathies. Am J Hum Genet 2006; 79:859-868. This paper demonstrates remarkably that some patients with recessive RYR1-based core myopathies have the disease because in their muscles their normal RYR1-allele has been epigenetically silenced. This was the first determination of the mechanism of an epigenetic phenomenon in the congenital myopathies.
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Zhou H, Brockington M, Jungbluth H, et al. Epigenetic allele silencing unveils recessive RYR1 mutations in core myopathies. Am J Hum Genet 2006; 79:859-868. This paper demonstrates remarkably that some patients with recessive RYR1-based core myopathies have the disease because in their muscles their normal RYR1-allele has been epigenetically silenced. This was the first determination of the mechanism of an epigenetic phenomenon in the congenital myopathies.
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Zhou H, Yamaguchi N, Xu L, et al. Characterization of recessive RYR1 mutations in core myopathies. Hum Mol Genet 2006; 15:2791-2803. This paper suggests that recessive core disease caused by mutations in RYR1 is more common than previously thought.
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Zhou H, Yamaguchi N, Xu L, et al. Characterization of recessive RYR1 mutations in core myopathies. Hum Mol Genet 2006; 15:2791-2803. This paper suggests that recessive core disease caused by mutations in RYR1 is more common than previously thought.
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Kossugue PM, Paim JF, Navarro MM, et al. Central core disease due to recessive mutations in RYR1 gene: Is it more common than described? Muscle Nerve 2007; 35:670-674. This paper suggests that recessive core disease caused by mutations in RYR1 is more common than previously thought.
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Kossugue PM, Paim JF, Navarro MM, et al. Central core disease due to recessive mutations in RYR1 gene: Is it more common than described? Muscle Nerve 2007; 35:670-674. This paper suggests that recessive core disease caused by mutations in RYR1 is more common than previously thought.
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Wu S, Ibarra MC, Malicdan MC, et al. Central core disease is due to RYR1 mutations in more than 90% of patients. Brain 2006; 129:1470-1480. This is an excellent review of the current knowledge of RYR1 mutations causing central core disease in the Japanese population. It demonstrates many mutations outside the known hotspots.
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Wu S, Ibarra MC, Malicdan MC, et al. Central core disease is due to RYR1 mutations in more than 90% of patients. Brain 2006; 129:1470-1480. This is an excellent review of the current knowledge of RYR1 mutations causing central core disease in the Japanese population. It demonstrates many mutations outside the known hotspots.
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Robinson R, Carpenter D, Shaw MA, et al. Mutations in RYR1 in malignant hyperthermia and central core disease. Hum Mutat 2006; 27:977-989. This is an excellent review of RYR1 mutations. It demonstrates many mutations outside the known hotspots.
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Robinson R, Carpenter D, Shaw MA, et al. Mutations in RYR1 in malignant hyperthermia and central core disease. Hum Mutat 2006; 27:977-989. This is an excellent review of RYR1 mutations. It demonstrates many mutations outside the known hotspots.
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A single homozygous point mutation in a 3′ untranslated region motif of selenoprotein N mRNA causes SEPN1-related myopathy
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Allamand V, Richard P, Lescure A, et al. A single homozygous point mutation in a 3′ untranslated region motif of selenoprotein N mRNA causes SEPN1-related myopathy. EMBO Rep 2006; 7:450-454.
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Ducreux S, Zorzato F, Ferreiro A, et al. Functional properties of ryanodine receptors carrying three amino acid substitutions identified in patients affected by multiminicore disease and central core disease, expressed in immortalized lymphocytes. Biochem J 2006; 395:259-266.
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Chelu MG, Goonasekera SA, Durham WJ, et al. Heat- and anesthesia-induced malignant hyperthermia in an RyR1 knock-in mouse. Faseb J 2006; 20:329-330.
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Dulhunty AF, Beard NA, Pouliquin P, Kimura T. Novel regulators of RyR Ca2+ release channels: insight into molecular changes in genetically-linked myopathies. J Muscle Res Cell Motil 2006; 27:351-365. This is an excellent review of the current knowledge of the pathobiology of RYR1 gene mutations. The authors also introduce the possibility of a role for RYR1 in myotonic dystrophy myopathy.
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Dulhunty AF, Beard NA, Pouliquin P, Kimura T. Novel regulators of RyR Ca2+ release channels: insight into molecular changes in genetically-linked myopathies. J Muscle Res Cell Motil 2006; 27:351-365. This is an excellent review of the current knowledge of the pathobiology of RYR1 gene mutations. The authors also introduce the possibility of a role for RYR1 in myotonic dystrophy myopathy.
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Fischer D, Herasse M, Ferreiro A, et al. Muscle imaging in dominant core myopathies linked or unlinked to the ryanodine receptor 1 gene. Neurology 2006; 67:2217-2220. This very useful paper describes the differences in the pattern of muscles affected in RYR1 or non-RYR1 core myopathies as seen with MRI
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Fischer D, Herasse M, Ferreiro A, et al. Muscle imaging in dominant core myopathies linked or unlinked to the ryanodine receptor 1 gene. Neurology 2006; 67:2217-2220. This very useful paper describes the differences in the pattern of muscles affected in RYR1 or non-RYR1 core myopathies as seen with MRI
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Herasse M, Parain K, Marty I, et al. Abnormal distribution of calcium-handling proteins: a novel distinctive marker in core myopathies. J Neuropathol Exp Neurol 2007; 66:57-65. This paper suggests that RYR1 and non-RYR1 related myopathies may be distinguished by immunohistochemistry for RyR1, which is absent from RYR1-related cores.
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Herasse M, Parain K, Marty I, et al. Abnormal distribution of calcium-handling proteins: a novel distinctive marker in core myopathies. J Neuropathol Exp Neurol 2007; 66:57-65. This paper suggests that RYR1 and non-RYR1 related myopathies may be distinguished by immunohistochemistry for RyR1, which is absent from RYR1-related cores.
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Lujan Feliu-Pascual A, Shelton GD, Targett MP, et al. Inherited myopathy of great Danes. J Small Anim Pract 2006; 47:249-254.
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Lujan Feliu-Pascual A, Shelton GD, Targett MP, et al. Inherited myopathy of great Danes. J Small Anim Pract 2006; 47:249-254.
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Autosomal dominant nemaline myopathy: A new phenotype unlinked to previously known genetic loci
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This paper identifies further genetic heterogeneity for dominant nemaline myopathy, suggesting that there is yet another locus to find
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Jeannet PY, Mittaz L, Dunand M, et al. Autosomal dominant nemaline myopathy: a new phenotype unlinked to previously known genetic loci. Neuromuscul Disord 2007; 17:6-12. This paper identifies further genetic heterogeneity for dominant nemaline myopathy, suggesting that there is yet another locus to find.
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(2007)
Neuromuscul Disord
, vol.17
, pp. 6-12
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Jeannet, P.Y.1
Mittaz, L.2
Dunand, M.3
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48
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Dunwoodie SL, Joya JE, Arkell RM. Hardeman EC Multiple regions of the human cardiac actin gene are necessary for maturation-based expression in striated muscle. J Biol Chem 1994; 269:12212-12219.
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Dunwoodie SL, Joya JE, Arkell RM. Hardeman EC Multiple regions of the human cardiac actin gene are necessary for maturation-based expression in striated muscle. J Biol Chem 1994; 269:12212-12219.
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49
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Defining alpha-skeletal and alphacardiac actin expression in human heart and skeletal muscle explains the absence of cardiac involvement in ACTA1 nemaline myopathy
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Ilkovski B, Clement S, Sewry C, et al. Defining alpha-skeletal and alphacardiac actin expression in human heart and skeletal muscle explains the absence of cardiac involvement in ACTA1 nemaline myopathy. Neuromuscul Disord 2005; 15:829-835.
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(2005)
Neuromuscul Disord
, vol.15
, pp. 829-835
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Ilkovski, B.1
Clement, S.2
Sewry, C.3
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50
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Adult-onset nemaline myopathy and monoclonal gammopathy
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Keller CE, Hays AP, Rowland LP, et al. Adult-onset nemaline myopathy and monoclonal gammopathy. Arch Neurol 2006; 63:132-134.
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(2006)
Arch Neurol
, vol.63
, pp. 132-134
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Keller, C.E.1
Hays, A.P.2
Rowland, L.P.3
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51
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Camptocormia in a patient with Parkinson disease and a myopathy with nemaline rods
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Ozer F, Ozturk O, Meral H, et al. Camptocormia in a patient with Parkinson disease and a myopathy with nemaline rods. Am J Phys Med Rehabil 2007; 86:3-6.
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(2007)
Am J Phys Med Rehabil
, vol.86
, pp. 3-6
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Ozer, F.1
Ozturk, O.2
Meral, H.3
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52
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33846947179
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Variable presentation of nemaline myopathy: Novel mutation of alpha actin gene
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Bouldin AA, Parisi MA, Laing N, et al. Variable presentation of nemaline myopathy: novel mutation of alpha actin gene. Muscle Nerve 2007; 35:254-258.
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(2007)
Muscle Nerve
, vol.35
, pp. 254-258
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Bouldin, A.A.1
Parisi, M.A.2
Laing, N.3
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53
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Identification of 45 novel mutations in the nebulin gene associated with autosomal recessive nemaline myopathy
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Lehtokari VL, Pelin K, Sandbacka M, et al. Identification of 45 novel mutations in the nebulin gene associated with autosomal recessive nemaline myopathy. Hum Mutat 2006; 27:946-956.
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(2006)
Hum Mutat
, vol.27
, pp. 946-956
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Lehtokari, V.L.1
Pelin, K.2
Sandbacka, M.3
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54
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NG 138th ENMC Workshop: Nemaline Myopathy, 20-22 May 2005, Naarden, The Netherlands
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Wallgren-Pettersson C. Laing NG 138th ENMC Workshop: Nemaline Myopathy, 20-22 May 2005, Naarden, The Netherlands. Neuromuscul Disord 2006; 16:54-60.
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(2006)
Neuromuscul Disord
, vol.16
, pp. 54-60
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Laing, W.C.1
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55
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Autosomal dominant nemaline myopathy with intranuclear rods due to mutation of the skeletal muscle ACTA1 gene: Clinical and pathological variability within a kindred
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Hutchinson DO, Charlton A, Laing NG, et al. Autosomal dominant nemaline myopathy with intranuclear rods due to mutation of the skeletal muscle ACTA1 gene: Clinical and pathological variability within a kindred. Neuromuscul Disord 2006; 16:113-121.
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(2006)
Neuromuscul Disord
, vol.16
, pp. 113-121
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Hutchinson, D.O.1
Charlton, A.2
Laing, N.G.3
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57
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Wallefeld W, Krause S, Nowak KJ, et al. Severe nemaline myopathy caused by mutations of the stop codon of the skeletal muscle alpha actin gene (ACTA1). Neuromuscul Disord 2006; 16:541-547. This paper for the first time identifies severely affected nemaline myopathy patients with mutations of the normal ACTA1 stop codon. The muscle in these patients is extremely dystrophic.
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Wallefeld W, Krause S, Nowak KJ, et al. Severe nemaline myopathy caused by mutations of the stop codon of the skeletal muscle alpha actin gene (ACTA1). Neuromuscul Disord 2006; 16:541-547. This paper for the first time identifies severely affected nemaline myopathy patients with mutations of the normal ACTA1 stop codon. The muscle in these patients is extremely dystrophic.
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58
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Patient with actin aggregate myopathy and not formerly identified ACTA1 mutation is heterozygous for the Gly15Arg mutation of ACTA1, which has previously been associated with actinopathy
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Goebel HH, Brockman K, Bonnemann CG, et al. Patient with actin aggregate myopathy and not formerly identified ACTA1 mutation is heterozygous for the Gly15Arg mutation of ACTA1, which has previously been associated with actinopathy. J Child Neurol 2006; 21:545.
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(2006)
J Child Neurol
, vol.21
, pp. 545
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Goebel, H.H.1
Brockman, K.2
Bonnemann, C.G.3
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59
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Actin-related myopathy without any missense mutation in the ACTA1 gene
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Goebel HH, Brockmann K, Bonnemann CG, et al. Actin-related myopathy without any missense mutation in the ACTA1 gene. J Child Neurol 2004; 19:149-153.
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(2004)
J Child Neurol
, vol.19
, pp. 149-153
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Goebel, H.H.1
Brockmann, K.2
Bonnemann, C.G.3
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60
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Wallgren-Pettersson C, Lehtokari VL, Kalimo H, et al. Distal myopathy caused by homozygous missense mutations in the nebulin gene. Brain 2007; 130:1465-1476. This remarkable paper demonstrates that patients homozygous for missense mutations in the nebulin gene (NEB) develop an early-onset distal myopathy similar to the one caused by certain mutations in slow-skeletal/β-cardiac myosin (MYH7). The same NEB missense mutations had previously been shown to cause nemaline myopathy when inherited with frameshift, nonsense or splice-site mutations in the other NEB allele.
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Wallgren-Pettersson C, Lehtokari VL, Kalimo H, et al. Distal myopathy caused by homozygous missense mutations in the nebulin gene. Brain 2007; 130:1465-1476. This remarkable paper demonstrates that patients homozygous for missense mutations in the nebulin gene (NEB) develop an early-onset distal myopathy similar to the one caused by certain mutations in slow-skeletal/β-cardiac myosin (MYH7). The same NEB missense mutations had previously been shown to cause nemaline myopathy when inherited with frameshift, nonsense or splice-site mutations in the other NEB allele.
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61
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Mutations in the slow skeletal muscle fiber myosin heavy chain gene (MYH7) cause Laing early-onset distal myopathy (MPD1)
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Meredith C, Herrmann R, Parry C, et al. Mutations in the slow skeletal muscle fiber myosin heavy chain gene (MYH7) cause Laing early-onset distal myopathy (MPD1). Am J Hum Genet 2004; 75:703-708.
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(2004)
Am J Hum Genet
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, pp. 703-708
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Meredith, C.1
Herrmann, R.2
Parry, C.3
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62
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Distal arthrogryposis and muscle weakness associated with a beta-tropomyosin mutation
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Tajsharghi H, Kimber E, Holmgren D, et al. Distal arthrogryposis and muscle weakness associated with a beta-tropomyosin mutation. Neurology 2007; 68:772-775.
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(2007)
Neurology
, vol.68
, pp. 772-775
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Tajsharghi, H.1
Kimber, E.2
Holmgren, D.3
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63
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Homozygosity for a nonsense mutation in the alpha-tropomyosin gene TPM3 in a patient with severe infantile nemaline myopathy
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Tan P, Briner J, Boltshauser E, et al. Homozygosity for a nonsense mutation in the alpha-tropomyosin gene TPM3 in a patient with severe infantile nemaline myopathy. Neuromusc Disord 1999; 9:573-579.
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(1999)
Neuromusc Disord
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, pp. 573-579
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Tan, P.1
Briner, J.2
Boltshauser, E.3
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64
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Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle
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This paper demonstrates, remarkably, that knockout mice lacking any nebulin can survive after birth. Thin filaments are present in the nebulin knockout mouse muscle though of abnormal length and thus there are fall-back mechanisms that can control thin filament length in the absence of nebulin
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Bang ML, Li X, Littlefield R, et al. Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle. J Cell Biol 2006; 173:905-916. This paper demonstrates, remarkably, that knockout mice lacking any nebulin can survive after birth. Thin filaments are present in the nebulin knockout mouse muscle though of abnormal length and thus there are fall-back mechanisms that can control thin filament length in the absence of nebulin.
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(2006)
J Cell Biol
, vol.173
, pp. 905-916
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Bang, M.L.1
Li, X.2
Littlefield, R.3
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Witt CC, Burkart C, Labeit D, et al. Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo. EMBO J 2006; 25:3843-3855. This paper demonstrates, remarkably, that knockout mice lacking any nebulin can survive after birth. Thin filaments are present in the nebulin knockout mouse muscle though of abnormal length and thus there are fall-back mechanisms that can control thin filament length in the absence of nebulin.
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Witt CC, Burkart C, Labeit D, et al. Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo. EMBO J 2006; 25:3843-3855. This paper demonstrates, remarkably, that knockout mice lacking any nebulin can survive after birth. Thin filaments are present in the nebulin knockout mouse muscle though of abnormal length and thus there are fall-back mechanisms that can control thin filament length in the absence of nebulin.
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Sanoudou D, Corbett MA, Han M, et al. Skeletal muscle repair in a mouse model of nemaline myopathy. Hum Mol Genet 2006; 15:2603-2612. This paper suggests that there is ongoing repair, regeneration and immature muscle fibres in the slow α-tropomyosin Met9Arg mouse model of nemaline myopathy.
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Sanoudou D, Corbett MA, Han M, et al. Skeletal muscle repair in a mouse model of nemaline myopathy. Hum Mol Genet 2006; 15:2603-2612. This paper suggests that there is ongoing repair, regeneration and immature muscle fibres in the slow α-tropomyosin Met9Arg mouse model of nemaline myopathy.
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67
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Expression profiling reveals altered satellite cell numbers and glycolytic enzyme transcription in nemaline myopathy muscle
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Sanoudou D, Haslett JN, Kho AT, et al. Expression profiling reveals altered satellite cell numbers and glycolytic enzyme transcription in nemaline myopathy muscle. Proc Natl Acad Sci U S A 2003; 100:4666-4671.
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(2003)
Proc Natl Acad Sci U S A
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Sanoudou, D.1
Haslett, J.N.2
Kho, A.T.3
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68
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Molecular classification of nemaline myopathies: "nontyping" specimens exhibit unique patterns of gene expression
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Sanoudou D, Frieden LA, Haslett JN, et al. Molecular classification of nemaline myopathies: "nontyping" specimens exhibit unique patterns of gene expression. Neurobiol Dis 2004; 15:590-600.
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(2004)
Neurobiol Dis
, vol.15
, pp. 590-600
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Sanoudou, D.1
Frieden, L.A.2
Haslett, J.N.3
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69
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Fatal hypertrophic cardiomyopathy and nemaline myopathy associated with ACTA1 K336E mutation
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D'Amico A, Graziano C, Pacileo G, et al. Fatal hypertrophic cardiomyopathy and nemaline myopathy associated with ACTA1 K336E mutation. Neuromuscul Disord 2006; 16:548-552.
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(2006)
Neuromuscul Disord
, vol.16
, pp. 548-552
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D'Amico, A.1
Graziano, C.2
Pacileo, G.3
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Robinson P, Lipscomb S, Preston LC, et al. Mutations in fast skeletal troponin I, troponin T, and beta-tropomyosin that cause distal arthrogryposis all increase contractile function. Faseb J 2007; 21:896-905. This paper demonstrates that mutations in three different proteins that lead to distal arthrogryposis all increase muscle contractility, a remarkable pathobiological consensus.
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Robinson P, Lipscomb S, Preston LC, et al. Mutations in fast skeletal troponin I, troponin T, and beta-tropomyosin that cause distal arthrogryposis all increase contractile function. Faseb J 2007; 21:896-905. This paper demonstrates that mutations in three different proteins that lead to distal arthrogryposis all increase muscle contractility, a remarkable pathobiological consensus.
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Autophagic vacuolar myopathy
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This is an excellent review of the vacuolar myopathies
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Nishino I. Autophagic vacuolar myopathy. Semin Pediatr Neurol 2006; 13:90-95. This is an excellent review of the vacuolar myopathies.
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(2006)
Semin Pediatr Neurol
, vol.13
, pp. 90-95
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Nishino, I.1
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73
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Fischer D, Herasse M, Bitoun M, et al. Characterization of the muscle involvement in dynamin 2-related centronuclear myopathy. Brain 2006; 129:1463-1469. This paper demonstrates the characteristic pattern of muscle involvement in dynamin-2 centronuclear myopathy useful in diagnosis.
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Fischer D, Herasse M, Bitoun M, et al. Characterization of the muscle involvement in dynamin 2-related centronuclear myopathy. Brain 2006; 129:1463-1469. This paper demonstrates the characteristic pattern of muscle involvement in dynamin-2 centronuclear myopathy useful in diagnosis.
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Schessl J, Medne L, Hu Y, et al. MRI in DNM2-related centronuclear myopathy: evidence for highly selective muscle involvement. Neuromuscul Disord 2007; 17:28-32. This paper demonstrates the characteristic pattern of muscle involvement in dynamin-2 centronuclear myopathy useful in diagnosis.
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Schessl J, Medne L, Hu Y, et al. MRI in DNM2-related centronuclear myopathy: evidence for highly selective muscle involvement. Neuromuscul Disord 2007; 17:28-32. This paper demonstrates the characteristic pattern of muscle involvement in dynamin-2 centronuclear myopathy useful in diagnosis.
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75
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Myogenin (Myf4) upregulation in transdifferentiating fibroblasts from a congenital myopathy with arrest of myogenesis and defects of myotube formation
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Weise C, Dai F, Prols F, et al. Myogenin (Myf4) upregulation in transdifferentiating fibroblasts from a congenital myopathy with arrest of myogenesis and defects of myotube formation. Anat Embryol (Berl) 2006; 211:639-648.
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(2006)
Anat Embryol (Berl)
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, pp. 639-648
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Weise, C.1
Dai, F.2
Prols, F.3
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76
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Congenital myopathy with arrest of myogenesis prior to formation of myotubes
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Ketelsen UP, Brand-Saberi B, Uhlenberg B, et al. Congenital myopathy with arrest of myogenesis prior to formation of myotubes. Neuropediatrics 2005; 36:246-251.
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(2005)
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, vol.36
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Ketelsen, U.P.1
Brand-Saberi, B.2
Uhlenberg, B.3
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Tajsharghi H, Oldfors A, Macleod DP, Swash M. Homozygous mutation in MYH7 in myosin storage myopathy and cardiomyopathy. Neurology 2007; 68:962. This paper demonstrates homozygous mutation in the gene for slow-skeletal/β- cardiac myosin (MYH7) in patients with recessive myosin storage myopathy with cardiomyopathy. Previously patients with dominant myosin storage myopathy had also been shown to have different mutations in MYH7.
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Tajsharghi H, Oldfors A, Macleod DP, Swash M. Homozygous mutation in MYH7 in myosin storage myopathy and cardiomyopathy. Neurology 2007; 68:962. This paper demonstrates homozygous mutation in the gene for slow-skeletal/β- cardiac myosin (MYH7) in patients with recessive myosin storage myopathy with cardiomyopathy. Previously patients with dominant myosin storage myopathy had also been shown to have different mutations in MYH7.
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Dye DE, Azzarelli B, Goebel HH, Laing NG. Novel slow-skeletal myosin (MYH7) mutation in the original myosin storage myopathy kindred. Neuromuscul Disord 2006; 16:357-360. This paper by molecular analysis of archival material demonstrates a previously unidentified MYH7 mutation in the seminal myosin storage myopathy kindred.
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Dye DE, Azzarelli B, Goebel HH, Laing NG. Novel slow-skeletal myosin (MYH7) mutation in the original myosin storage myopathy kindred. Neuromuscul Disord 2006; 16:357-360. This paper by molecular analysis of archival material demonstrates a previously unidentified MYH7 mutation in the seminal myosin storage myopathy kindred.
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Myosin storage (hyaline body) myopathy: A case report
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Shingde MV, Spring PJ, Maxwell A, et al. Myosin storage (hyaline body) myopathy: a case report. Neuromuscul Disord 2006; 16:882-886.
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(2006)
Neuromuscul Disord
, vol.16
, pp. 882-886
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Shingde, M.V.1
Spring, P.J.2
Maxwell, A.3
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