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Volumn 24, Issue 22, 2015, Pages 6278-6292

Muscle weakness in TPM3-myopathy is due to reduced Ca2+-sensitivity and impaired acto-myosin cross-bridge cycling in slow fibres

(15)  Yuen, Michaela a,b   Cooper, Sandra T a,b   Marston, Steve B c   Nowak, Kristen J d   Mcnamara, Elyshia d   Mokbe, Nancy a,e   Ilkovski, Biljana a   Ravenscroft, Gianina d   Rendu, John f   Dewinter, Josine M g   Klinge, Lars h   Beggs, Alan H i   North, Kathryn N a,b,j,k   Ottenheijm, Coen A C g   Clarke, Nigel F b  


Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CALCIUM; MUTANT PROTEIN; MYOSIN; TPM3 PROTEIN; TROPOMYOSIN; TROPONIN; UNCLASSIFIED DRUG; ISOPROTEIN; TPM3 PROTEIN, HUMAN;

EID: 84949057883     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddv334     Document Type: Article
Times cited : (41)

References (75)
  • 2
    • 75149179143 scopus 로고    scopus 로고
    • Mutations of tropomyosin 3 (TPM3) are common and associated with type 1 myofiber hypotrophy in congenital fiber type disproportion
    • Lawlor, M.W., Dechene, E.T., Roumm, E., Geggel, A.S., Moghadaszadeh, B. and Beggs, A.H. (2010) Mutations of tropomyosin 3 (TPM3) are common and associated with type 1 myofiber hypotrophy in congenital fiber type disproportion. Hum. Mutat., 31, 176-183.
    • (2010) Hum. Mutat. , vol.31 , pp. 176-183
    • Lawlor, M.W.1    Dechene, E.T.2    Roumm, E.3    Geggel, A.S.4    Moghadaszadeh, B.5    Beggs, A.H.6
  • 9
    • 77951255913 scopus 로고    scopus 로고
    • Autosomal dominant nemaline myopathy caused by a novel alpha-tropomyosin 3 mutation
    • Kiphuth, I.C., Krause, S., Huttner, H.B., Dekomien, G., Struffert, T. and Schroder, R. (2010) Autosomal dominant nemaline myopathy caused by a novel alpha-tropomyosin 3 mutation. J. Neurol., 257, 658-660.
    • (2010) J. Neurol. , vol.257 , pp. 658-660
    • Kiphuth, I.C.1    Krause, S.2    Huttner, H.B.3    Dekomien, G.4    Struffert, T.5    Schroder, R.6
  • 10
    • 67650034772 scopus 로고    scopus 로고
    • TPM3 mutation in one of the original cases of cap disease
    • Ohlsson, M., Fidzianska, A., Tajsharghi, H. and Oldfors, A. (2009) TPM3 mutation in one of the original cases of cap disease. Neurology, 72, 1961-1963.
    • (2009) Neurology , vol.72 , pp. 1961-1963
    • Ohlsson, M.1    Fidzianska, A.2    Tajsharghi, H.3    Oldfors, A.4
  • 12
    • 34047133846 scopus 로고    scopus 로고
    • A second pedigree with autosomal dominant nemaline myopathy caused by TPM3 mutation: a clinical and pathological study
    • Penisson-Besnier, I., Monnier, N., Toutain, A., Dubas, F. and Laing, N. (2007) A second pedigree with autosomal dominant nemaline myopathy caused by TPM3 mutation: a clinical and pathological study. Neuromuscul. Disord., 17, 330-337.
    • (2007) Neuromuscul. Disord. , vol.17 , pp. 330-337
    • Penisson-Besnier, I.1    Monnier, N.2    Toutain, A.3    Dubas, F.4    Laing, N.5
  • 15
    • 0019782056 scopus 로고
    • Alpha-and beta-tropomyosin in typed single fibers of human skeletal muscle
    • Billeter, R., Heizmann, C.W., Reist, U., Howald, H. and Jenny, E. (1981) Alpha-and beta-tropomyosin in typed single fibers of human skeletal muscle. FEBS Lett., 132, 133-136.
    • (1981) FEBS Lett. , vol.132 , pp. 133-136
    • Billeter, R.1    Heizmann, C.W.2    Reist, U.3    Howald, H.4    Jenny, E.5
  • 16
    • 0034682640 scopus 로고    scopus 로고
    • Tropomyosin 3 increases striated muscle isoform diversity
    • Pieples, K. and Wieczorek, D.F. (2000) Tropomyosin 3 increases striated muscle isoform diversity. Biochemistry (Mosc), 39, 8291-8297.
    • (2000) Biochemistry (Mosc). , vol.39 , pp. 8291-8297
    • Pieples, K.1    Wieczorek, D.F.2
  • 17
    • 0016774265 scopus 로고
    • Tropomyosin coiledcoil interactions: evidence for an unstaggered structure
    • Mclachlan, A.D. and Stewart, M. (1975) Tropomyosin coiledcoil interactions: evidence for an unstaggered structure. J. Mol. Biol., 98, 293-304.
    • (1975) J. Mol. Biol. , vol.98 , pp. 293-304
    • Mclachlan, A.D.1    Stewart, M.2
  • 19
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the swiss-Pdbviewer: an environment for comparative protein modeling
    • Guex, N. and Peitsch, M.C. (1997) SWISS-MODEL and the swiss-Pdbviewer: an environment for comparative protein modeling. Electrophoresis, 18, 2714-2723.
    • (1997) Electrophoresis. , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 20
    • 0017136639 scopus 로고
    • The 14-fold periodicity in alpha-tropomyosin and the interaction with actin
    • Mclachlan, A.D. and Stewart, M. (1976) The 14-fold periodicity in alpha-tropomyosin and the interaction with actin. J. Mol. Biol., 103, 271-298.
    • (1976) J. Mol. Biol. , vol.103 , pp. 271-298
    • Mclachlan, A.D.1    Stewart, M.2
  • 21
    • 79955371742 scopus 로고    scopus 로고
    • Changes in cross-bridge cycling underlie muscle weakness in patients with tropomyosin 3-based myopathy
    • Ottenheijm, C.A., Lawlor, M.W., Stienen, G.J., Granzier, H. and Beggs, A.H. (2011) Changes in cross-bridge cycling underlie muscle weakness in patients with tropomyosin 3-based myopathy. Hum. Mol. Genet., 20, 2015-2025.
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 2015-2025
    • Ottenheijm, C.A.1    Lawlor, M.W.2    Stienen, G.J.3    Granzier, H.4    Beggs, A.H.5
  • 24
    • 0020477241 scopus 로고
    • Two-dimensional peptide analysis of myosin heavy chains and actin fromsingle-typed human skeletal muscle fibers
    • Billeter, R., Heizmann, C.W., Reist, U., Howald, H. and Jenny, E. (1982) Two-dimensional peptide analysis of myosin heavy chains and actin fromsingle-typed human skeletal muscle fibers. FEBS Lett., 139, 45-48.
    • (1982) FEBS Lett. , vol.139 , pp. 45-48
    • Billeter, R.1    Heizmann, C.W.2    Reist, U.3    Howald, H.4    Jenny, E.5
  • 28
    • 0017864059 scopus 로고
    • Specific phosphorylation at serine-283 of alpha tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle
    • USA
    • Mak, A., Smillie, L.B. and Barany, M. (1978) Specific phosphorylation at serine-283 of alpha tropomyosin from frog skeletal and rabbit skeletal and cardiac muscle. Proc. Natl acad. Sci. USA, 75, 3588-3592.
    • (1978) Proc. Natl Acad. Sci. , vol.75 , pp. 3588-3592
    • Mak, A.1    Smillie, L.B.2    Barany, M.3
  • 29
    • 0019798102 scopus 로고
    • Characterization of the tropomyosin present in various chick embryo muscle types and in muscle cells differentiated in vitro
    • Montarras, D., Fiszman, M.Y. and Gros, F. (1981) Characterization of the tropomyosin present in various chick embryo muscle types and in muscle cells differentiated in vitro. J. Biol. Chem., 256, 4081-4086.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4081-4086
    • Montarras, D.1    Fiszman, M.Y.2    Gros, F.3
  • 30
    • 58149340251 scopus 로고    scopus 로고
    • Phosphorylation of tropomyosin extends cooperative binding of myosin beyond a single regulatory unit
    • Rao, V.S., Marongelli, E.N. and Guilford, W.H. (2009) Phosphorylation of tropomyosin extends cooperative binding of myosin beyond a single regulatory unit. Cell Motil. Cytoskeleton, 66, 10-23.
    • (2009) Cell Motil. Cytoskeleton. , vol.66 , pp. 10-23
    • Rao, V.S.1    Marongelli, E.N.2    Guilford, W.H.3
  • 31
    • 34047208553 scopus 로고    scopus 로고
    • Stiffness and fraction of Myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas
    • Linari, M., Caremani, M., Piperio, C., Brandt, P. and Lombardi, V. (2007) Stiffness and fraction of Myosin motors responsible for active force in permeabilized muscle fibers from rabbit psoas. Biophys. J., 92, 2476-2490.
    • (2007) Biophys. J. , vol.92 , pp. 2476-2490
    • Linari, M.1    Caremani, M.2    Piperio, C.3    Brandt, P.4    Lombardi, V.5
  • 32
    • 71449111552 scopus 로고    scopus 로고
    • Nebulin alters cross-bridge cycling kinetics and increases thin filament activation: a novel mechanism for increasing tension and reducing tension cost
    • Chandra, M., Mamidi, R., Ford, S., Hidalgo, C.,Witt, C., Ottenheijm, C., Labeit, S. and Granzier, H. (2009) Nebulin alters cross-bridge cycling kinetics and increases thin filament activation: a novel mechanism for increasing tension and reducing tension cost. J. Biol. Chem., 284, 30889-30896.
    • (2009) J. Biol. Chem. , vol.284 , pp. 30889-30896
    • Chandra, M.1    Mamidi, R.2    Ford, S.3    Hidalgo, C.4    Witt, C.5    Ottenheijm, C.6    Labeit, S.7    Granzier, H.8
  • 33
    • 84861203567 scopus 로고    scopus 로고
    • Intracellular calcium movements during excitation-contraction coupling in mammalian slow-twitch and fast-twitch muscle fibers
    • Baylor, S.M. and Hollingworth, S. (2012) Intracellular calcium movements during excitation-contraction coupling in mammalian slow-twitch and fast-twitch muscle fibers. J. Gen. Physiol., 139, 261-272.
    • (2012) J. Gen. Physiol. , vol.139 , pp. 261-272
    • Baylor, S.M.1    Hollingworth, S.2
  • 34
    • 0025936935 scopus 로고
    • Changes of myoplasmic calcium concentration during fatigue in single mouse muscle fibers
    • Westerblad, H. and Allen, D.G. (1991) Changes of myoplasmic calcium concentration during fatigue in single mouse muscle fibers. J. Gen. Physiol., 98, 615-635.
    • (1991) J. Gen. Physiol. , vol.98 , pp. 615-635
    • Westerblad, H.1    Allen, D.G.2
  • 35
    • 38349048508 scopus 로고    scopus 로고
    • Skeletal muscle fatigue: cellular mechanisms
    • Allen, D.G., Lamb, G.D. and Westerblad, H. (2008) Skeletal muscle fatigue: cellular mechanisms. Physiol. Rev., 88, 287-332.
    • (2008) Physiol. Rev. , vol.88 , pp. 287-332
    • Allen, D.G.1    Lamb, G.D.2    Westerblad, H.3
  • 36
    • 65749100189 scopus 로고    scopus 로고
    • 2+ flux through the transverse tubular membrane, activated by individual action potentials in mammalian skeletal muscle
    • 2+ flux through the transverse tubular membrane, activated by individual action potentials in mammalian skeletal muscle. J. Physiol., 587, 2299-2312.
    • (2009) J. Physiol. , vol.587 , pp. 2299-2312
    • Launikonis, B.S.1    Stephenson, D.G.2    Friedrich, O.3
  • 40
  • 41
    • 84890115115 scopus 로고    scopus 로고
    • Tropomyosin dephosphorylation in the heart: what are the consequences?
    • Schulz, E.M. and Wieczorek, D.F. (2013) Tropomyosin dephosphorylation in the heart: what are the consequences? J. Muscle Res. Cell Motil., 34, 239-246.
    • (2013) J. Muscle Res. Cell Motil. , vol.34 , pp. 239-246
    • Schulz, E.M.1    Wieczorek, D.F.2
  • 42
    • 38149014016 scopus 로고    scopus 로고
    • Use of 2-D DIGE analysis reveals altered phosphorylation in a tropomyosin mutant (Glu54Lys) linked to dilated cardiomyopathy.
    • Warren, C.M., Arteaga, G.M., Rajan, S., Ahmed, R.P.,Wieczorek, D.F. and Solaro, R.J. (2008) Use of 2-D DIGE analysis reveals altered phosphorylation in a tropomyosin mutant (Glu54Lys) linked to dilated cardiomyopathy. Proteomics, 8, 100-105.
    • (2008) Proteomics , vol.8 , pp. 100-105
    • Warren, C.M.1    Arteaga, G.M.2    Rajan, S.3    Ahmed, R.P.4    Wieczorek, D.F.5    Solaro, R.J.6
  • 43
    • 84890128019 scopus 로고    scopus 로고
    • Phosphorylation of tropomyosin in striated muscle
    • Heeley, D.H. (2013) Phosphorylation of tropomyosin in striated muscle. J. Muscle Res. Cell Motil., 34, 233-237.
    • (2013) J. Muscle Res. Cell Motil. , vol.34 , pp. 233-237
    • Heeley, D.H.1
  • 45
    • 33847038271 scopus 로고    scopus 로고
    • P38-MAPK induced dephosphorylation of alpha-tropomyosin is associated with depression of myocardial sarcomeric tension and ATPase activity
    • Vahebi, S., Ota, A., Li, M.,Warren, C.M., Detombe, P.P.,Wang, Y. and Solaro, R.J. (2007) p38-MAPK induced dephosphorylation of alpha-tropomyosin is associated with depression of myocardial sarcomeric tension and ATPase activity. Circ. Res., 100, 408-415.
    • (2007) Circ. Res. , vol.100 , pp. 408-415
    • Vahebi, S.1    Ota, A.2    Li, M.3    Warren, C.M.4    Detombe, P.P.5    Wang, Y.6    Solaro, R.J.7
  • 46
    • 36248956949 scopus 로고    scopus 로고
    • DAP kinase mediates the phosphorylation of tropomyosin-1 downstream of the ERK pathway, which regulates the formation of stress fibers in response to oxidative stress
    • Houle, F., Poirier, A., Dumaresq, J. and Huot, J. (2007) DAP kinase mediates the phosphorylation of tropomyosin-1 downstream of the ERK pathway, which regulates the formation of stress fibers in response to oxidative stress. J. Cell Sci., 120, 3666-3677.
    • (2007) J. Cell Sci. , vol.120 , pp. 3666-3677
    • Houle, F.1    Poirier, A.2    Dumaresq, J.3    Huot, J.4
  • 47
    • 0038032832 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase mediates phosphorylation of tropomyosin-1 to promote cytoskeleton remodeling in response to oxidative stress: impact on membrane blebbing
    • Houle, F., Rousseau, S., Morrice, N., Luc, M., Mongrain, S., Turner, C.E., Tanaka, S., Moreau, P. and Huot, J. (2003) Extracellular signal-regulated kinase mediates phosphorylation of tropomyosin-1 to promote cytoskeleton remodeling in response to oxidative stress: impact on membrane blebbing. Mol. Biol. Cell, 14, 1418-1432.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1418-1432
    • Houle, F.1    Rousseau, S.2    Morrice, N.3    Luc, M.4    Mongrain, S.5    Turner, C.E.6    Tanaka, S.7    Moreau, P.8    Huot, J.9
  • 48
    • 0035406554 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase signal transduction in skeletal muscle: effects of exercise and muscle contraction
    • Widegren, U., Ryder, J.W. and Zierath, J.R. (2001) Mitogen-activated protein kinase signal transduction in skeletal muscle: effects of exercise and muscle contraction. Acta Physiol. Scand., 172, 227-238.
    • (2001) Acta Physiol. Scand. , vol.172 , pp. 227-238
    • Widegren, U.1    Ryder, J.W.2    Zierath, J.R.3
  • 49
    • 79951834827 scopus 로고    scopus 로고
    • Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry
    • Li, X.E., Tobacman, L.S., Mun, J.Y., Craig, R., Fischer, S. and Lehman, W. (2011) Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry. Biophys. J., 100, 1005-1013.
    • (2011) Biophys. J. , vol.100 , pp. 1005-1013
    • Li, X.E.1    Tobacman, L.S.2    Mun, J.Y.3    Craig, R.4    Fischer, S.5    Lehman, W.6
  • 51
    • 84893249974 scopus 로고    scopus 로고
    • Tropomyosin movement on F-actin during muscle activation explained by energy landscapes
    • Orzechowski, M., Moore, J.R., Fischer, S. and Lehman, W. (2014) Tropomyosin movement on F-actin during muscle activation explained by energy landscapes. Arch. Biochem. Biophys., 545, 63-68.
    • (2014) Arch. Biochem. Biophys. , vol.545 , pp. 63-68
    • Orzechowski, M.1    Moore, J.R.2    Fischer, S.3    Lehman, W.4
  • 52
    • 84864182402 scopus 로고    scopus 로고
    • Functional effects of congenital myopathy-related mutations in gamma-tropomyosin gene
    • Robaszkiewicz, K., Dudek, E., Kasprzak, A.A. and Moraczewska, J. (2012) Functional effects of congenital myopathy-related mutations in gamma-tropomyosin gene. Biochim. Biophys. Acta, 1822, 1562-1569.
    • (2012) Biochim. Biophys. Acta , vol.1822 , pp. 1562-1569
    • Robaszkiewicz, K.1    Dudek, E.2    Kasprzak, A.A.3    Moraczewska, J.4
  • 53
    • 0033638660 scopus 로고    scopus 로고
    • Alteration of tropomyosin function and folding by a nemaline myopathy-causing mutation
    • Moraczewska, J., Greenfield, N.J., Liu, Y. and Hitchcock-De-Gregori, S.E. (2000) Alteration of tropomyosin function and folding by a nemaline myopathy-causing mutation. Biophys. J., 79, 3217-3225.
    • (2000) Biophys. J. , vol.79 , pp. 3217-3225
    • Moraczewska, J.1    Greenfield, N.J.2    Liu, Y.3    Hitchcock-De-Gregori, S.E.4
  • 55
    • 0036391998 scopus 로고    scopus 로고
    • Expression and biological activity of Baculovirus generated wild-type human slow alpha tropomyosin and the Met9Arg mutant responsible for a dominant form of nemaline myopathy
    • Akkari, P.A., Song, Y., Hitchcock-DeGregori, S., Blechynden, L. and Laing, N. (2002) Expression and biological activity of Baculovirus generated wild-type human slow alpha tropomyosin and the Met9Arg mutant responsible for a dominant form of nemaline myopathy. Biochem. Biophys. Res. Commun., 296, 300-304.
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 300-304
    • Akkari, P.A.1    Song, Y.2    Hitchcock-DeGregori, S.3    Blechynden, L.4    Laing, N.5
  • 56
    • 54249099032 scopus 로고    scopus 로고
    • Thin filament proteins mutations associated with skeletalmyopathies: defective regulation of muscle contraction
    • Ochala, J. (2008) Thin filament proteins mutations associated with skeletalmyopathies: defective regulation of muscle contraction. J. Mol. Med., 86, 1197-1204.
    • (2008) J. Mol. Med. , vol.86 , pp. 1197-1204
    • Ochala, J.1
  • 57
    • 84890127123 scopus 로고    scopus 로고
    • Skeletal muscle myopathy mutations at the actin tropomyosin interface that cause gain-or loss-of-function
    • Memo, M. and Marston, S. (2013) Skeletal muscle myopathy mutations at the actin tropomyosin interface that cause gain-or loss-of-function. J. Muscle Res. Cell Motil., 34, 165-169.
    • (2013) J. Muscle Res. Cell Motil. , vol.34 , pp. 165-169
    • Memo, M.1    Marston, S.2
  • 59
    • 84922572735 scopus 로고    scopus 로고
    • Impaired tropomyosin-troponin interactions reduce activation of the actin thin filament
    • Robaszkiewicz, K., Ostrowska, Z., Cyranka-Czaja, A. and Moraczewska, J. (2015) Impaired tropomyosin-troponin interactions reduce activation of the actin thin filament. Biochim. Biophys. Acta, 1854, 381-390.
    • (2015) Biochim. Biophys. Acta. , vol.1854 , pp. 381-390
    • Robaszkiewicz, K.1    Ostrowska, Z.2    Cyranka-Czaja, A.3    Moraczewska, J.4
  • 60
    • 0342670586 scopus 로고
    • Oxidative capacity of muscle and mitochondria: correlation of physiological, biochemical, and morphometric characteristics
    • USA
    • Schwerzmann, K., Hoppeler, H., Kayar, S.R. and Weibel, E.R. (1989) Oxidative capacity of muscle and mitochondria: correlation of physiological, biochemical, and morphometric characteristics. Proc. Natl Acad. Sci. USA, 86, 1583-1587.
    • (1989) Proc. Natl Acad. Sci. , vol.86 , pp. 1583-1587
    • Schwerzmann, K.1    Hoppeler, H.2    Kayar, S.R.3    Weibel, E.R.4
  • 61
    • 0029880902 scopus 로고    scopus 로고
    • Characteristics of mitochondria isolated from type I and type IIb skeletal muscle
    • Jackman, M.R. and Willis, W.T. (1996) Characteristics of mitochondria isolated from type I and type IIb skeletal muscle. Am. J. Physiol., 270, C673-C678.
    • (1996) Am. J. Physiol. , vol.270 , pp. 673-678
    • Jackman, M.R.1    Willis, W.T.2
  • 64
    • 84874261774 scopus 로고    scopus 로고
    • Fast skeletal muscle troponin activation increases force of mouse fast skeletal muscle and ameliorates weakness due to nebulindeficiency
    • Lee, E.J., Dewinter, J.M., Buck, D., Jasper, J.R., Malik, F.I., Labeit, S., Ottenheijm, C.A. and Granzier, H. (2013) Fast skeletal muscle troponin activation increases force of mouse fast skeletal muscle and ameliorates weakness due to nebulindeficiency. PLOS One, 8, e55861.
    • (2013) PLOS One. , vol.8 , pp. e55861
    • Lee, E.J.1    Dewinter, J.M.2    Buck, D.3    Jasper, J.R.4    Malik, F.I.5    Labeit, S.6    Ottenheijm, C.A.7    Granzier, H.8
  • 67
    • 0032499881 scopus 로고    scopus 로고
    • Human skeletal muscle-specific alpha-actinin-2 and -3 isoforms form homodimers and heterodimers in vitro and in vivo
    • Chan, Y., Tong, H.Q., Beggs, A.H. and Kunkel, L.M. (1998) Human skeletal muscle-specific alpha-actinin-2 and -3 isoforms form homodimers and heterodimers in vitro and in vivo. Biochem. Biophys. Res. Commun., 248, 134-139.
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 134-139
    • Chan, Y.1    Tong, H.Q.2    Beggs, A.H.3    Kunkel, L.M.4
  • 69
    • 0014864488 scopus 로고
    • Muscle fiber types: how many and what kind?
    • Brooke, M.H. and Kaiser, K.K. (1970) Muscle fiber types: how many and what kind? Arch. Neurol., 23, 369-379.
    • (1970) Arch. Neurol. , vol.23 , pp. 369-379
    • Brooke, M.H.1    Kaiser, K.K.2
  • 70
    • 0037677436 scopus 로고    scopus 로고
    • Single section Western blot: improving the molecular diagnosis of the muscular dystrophies.
    • Cooper, S.T., Lo, H.P. and North, K.N. (2003) Single section Western blot: improving the molecular diagnosis of the muscular dystrophies. Neurology, 61, 93-97.
    • (2003) Neurology , vol.61 , pp. 93-97
    • Cooper, S.T.1    Lo, H.P.2    North, K.N.3
  • 71
    • 4444301749 scopus 로고    scopus 로고
    • Evidence for a dominant-negative effect in ACTA1 nemaline myopathy caused by abnormal folding, aggregation and altered polymerization of mutant actin isoforms
    • Ilkovski, B., Nowak, K.J., Domazetovska, A., Maxwell, A.L., Clement, S., Davies, K.E., Laing, N.G., North, K.N. and Cooper, S.T. (2004) Evidence for a dominant-negative effect in ACTA1 nemaline myopathy caused by abnormal folding, aggregation and altered polymerization of mutant actin isoforms. Hum. Mol. Genet., 13, 1727-1743.
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1727-1743
    • Ilkovski, B.1    Nowak, K.J.2    Domazetovska, A.3    Maxwell, A.L.4    Clement, S.5    Davies, K.E.6    Laing, N.G.7    North, K.N.8    Cooper, S.T.9
  • 72
    • 84856249208 scopus 로고    scopus 로고
    • Abnormal actin binding of aberrant beta-tropomyosins is a molecular cause of muscle weakness in TPM2-related nemaline and cap myopathy
    • Marttila, M., Lemola, E., Wallefeld, W., Memo, M., Donner, K., Laing, N.G.,Marston, S., Gronholm, M. andWallgren-Pettersson, C. (2012) Abnormal actin binding of aberrant beta-tropomyosins is a molecular cause of muscle weakness in TPM2-related nemaline and cap myopathy. Biochem. J., 442, 231-239.
    • (2012) Biochem. J. , vol.442 , pp. 231-239
    • Marttila, M.1    Lemola, E.2    Wallefeld, W.3    Memo, M.4    Donner, K.5    Laing, N.G.6    Marston, S.7    Gronholm, M.8    Wallgren-Pettersson, C.9
  • 73
    • 0030721473 scopus 로고    scopus 로고
    • 2+-dependent effects on actin-tropomyosin filament motility
    • 2+-dependent effects on actin-tropomyosin filament motility. Biochem. J., 327, 335-340.
    • (1997) Biochem. J. , vol.327 , pp. 335-340
    • Bing, W.1    Fraser, I.D.2    Marston, S.B.3
  • 74
    • 67249115136 scopus 로고    scopus 로고
    • Thin filament length dysregulation contributes to muscle weakness in nemaline myopathy patients with nebulin deficiency
    • Ottenheijm, C.A., Witt, C.C., Stienen, G.J., Labeit, S., Beggs, A.H. and Granzier, H. (2009) Thin filament length dysregulation contributes to muscle weakness in nemaline myopathy patients with nebulin deficiency. Hum. Mol. Genet., 18, 2359-2369.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 2359-2369
    • Ottenheijm, C.A.1    Witt, C.C.2    Stienen, G.J.3    Labeit, S.4    Beggs, A.H.5    Granzier, H.6


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