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Volumn 126, Issue 23, 2013, Pages 5477-5489

The nebulin SH3 domain is dispensable for normal skeletal muscle structure but is required for effective active load bearing in mouse

(18)  Yamamoto, Daniel L a   Vitiello, Carmen b   Zhang, Jianlin c   Gokhin, David S d   Castaldi, Alessandra e,f   Coulis, Gerald b   Piaser, Fabio e,f   Filomena, Maria Carmela f,g   Eggenhuizen, Peter J a   Kunderfranco, Paolo e,f   Camerini, Serena h   Takano, Kazunori i   Endo, Takeshi i   Crescenzi, Marco h   Luther, Pradeep K L j   Lieber, Richard L d   Chen, Ju c   Bang, Marie Louise e,f  


Author keywords

Nebulin; Nemaline myopathy; Sarcomere; Skeletal muscle; Z line

Indexed keywords

MUSCLE PROTEIN; MYOPALLADIN; NEBULIN; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; PALLADIN; PROTEIN SH3; UNCLASSIFIED DRUG; ZYXIN;

EID: 84890244333     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.137026     Document Type: Article
Times cited : (32)

References (62)
  • 2
    • 18744397819 scopus 로고    scopus 로고
    • Molecular dissection of the interaction of desmin with the C-terminal region of nebulin
    • Bang, M. L., Gregorio, C. and Labeit, S. (2002). Molecular dissection of the interaction of desmin with the C-terminal region of nebulin. J. Struct. Biol. 137, 119-127.
    • (2002) J. Struct. Biol. , vol.137 , pp. 119-127
    • Bang, M.L.1    Gregorio, C.2    Labeit, S.3
  • 3
    • 33745243854 scopus 로고    scopus 로고
    • Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle
    • Bang, M. L., Li, X., Littlefield, R., Bremner, S., Thor, A., Knowlton, K. U., Lieber, R. L. and Chen, J. (2006). Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle. J. Cell Biol. 173, 905-916.
    • (2006) J. Cell Biol. , vol.173 , pp. 905-916
    • Bang, M.L.1    Li, X.2    Littlefield, R.3    Bremner, S.4    Thor, A.5    Knowlton, K.U.6    Lieber, R.L.7    Chen, J.8
  • 5
    • 34547094568 scopus 로고    scopus 로고
    • Structural and regulatory roles of muscle ankyrin repeat protein family in skeletal muscle
    • Barash, I. A., Bang, M. L., Mathew, L., Greaser, M. L., Chen, J. and Lieber, R. L. (2007). Structural and regulatory roles of muscle ankyrin repeat protein family in skeletal muscle. Am. J. Physiol. 293, C218-C227.
    • (2007) Am. J. Physiol. , vol.293
    • Barash, I.A.1    Bang, M.L.2    Mathew, L.3    Greaser, M.L.4    Chen, J.5    Lieber, R.L.6
  • 6
    • 0035829361 scopus 로고    scopus 로고
    • Controlling the false discovery rate in behavior genetics research
    • Benjamini, Y., Drai, D., Elmer, G., Kafkafi, N. and Golani, I. (2001). Controlling the false discovery rate in behavior genetics research. Behav. Brain Res. 125, 279-284.
    • (2001) Behav. Brain Res. , vol.125 , pp. 279-284
    • Benjamini, Y.1    Drai, D.2    Elmer, G.3    Kafkafi, N.4    Golani, I.5
  • 8
    • 0026586856 scopus 로고
    • An interaction between zyxin and alpha-actinin
    • Crawford, A. W., Michelsen, J. W. and Beckerle, M. C. (1992). An interaction between zyxin and alpha-actinin. J. Cell Biol. 116, 1381-1393.
    • (1992) J. Cell Biol. , vol.116 , pp. 1381-1393
    • Crawford, A.W.1    Michelsen, J.W.2    Beckerle, M.C.3
  • 9
    • 84866505685 scopus 로고    scopus 로고
    • A simple protocol for the subcellular fractionation of skeletal muscle cells and tissue
    • Dimauro, I., Pearson, T., Caporossi, D. and Jackson, M. J. (2012). A simple protocol for the subcellular fractionation of skeletal muscle cells and tissue. BMC Res. Notes 5, 513.
    • (2012) BMC Res. Notes , vol.5 , pp. 513
    • Dimauro, I.1    Pearson, T.2    Caporossi, D.3    Jackson, M.J.4
  • 10
    • 44449099311 scopus 로고    scopus 로고
    • Palladin is an actin cross-linking protein that uses immunoglobulin-like domains to bind filamentous actin
    • Dixon, R. D., Arneman, D. K., Rachlin, A. S., Sundaresan, N. R., Costello, M. J., Campbell, S. L. and Otey, C. A. (2008). Palladin is an actin cross-linking protein that uses immunoglobulin-like domains to bind filamentous actin. J. Biol. Chem. 283, 6222-6231.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6222-6231
    • Dixon, R.D.1    Arneman, D.K.2    Rachlin, A.S.3    Sundaresan, N.R.4    Costello, M.J.5    Campbell, S.L.6    Otey, C.A.7
  • 11
    • 46249088370 scopus 로고    scopus 로고
    • lumi: a pipeline for processing Illumina microarray
    • Du, P., Kibbe, W. A. and Lin, S. M. (2008). lumi: a pipeline for processing Illumina microarray. Bioinformatics 24, 1547-1548.
    • (2008) Bioinformatics , vol.24 , pp. 1547-1548
    • Du, P.1    Kibbe, W.A.2    Lin, S.M.3
  • 12
    • 29244442950 scopus 로고    scopus 로고
    • Simplified screening for the detection of soluble fusion constructs expressed in E.coli using a modular set of vectors
    • Dümmler, A., Lawrence, A. M. and de Marco, A. (2005). Simplified screening for the detection of soluble fusion constructs expressed in E. coli using a modular set of vectors. Microb. Cell Fact. 4, 34.
    • (2005) Microb. Cell Fact. , vol.4 , pp. 34
    • Dümmler, A.1    Lawrence, A.M.2    de Marco, A.3
  • 14
    • 33744494538 scopus 로고    scopus 로고
    • The sarcomeric Z-disc: a nodal point in signalling and disease
    • Frank, D., Kuhn, C., Katus, H. A. and Frey, N. (2006). The sarcomeric Z-disc: a nodal point in signalling and disease. J. Mol. Med. 84, 446-468.
    • (2006) J. Mol. Med. , vol.84 , pp. 446-468
    • Frank, D.1    Kuhn, C.2    Katus, H.A.3    Frey, N.4
  • 15
    • 49049097083 scopus 로고    scopus 로고
    • The role of palladin in actin organization and cell motility
    • Goicoechea, S. M., Arneman, D. and Otey, C. A. (2008). The role of palladin in actin organization and cell motility. Eur. J. Cell Biol. 87, 517-525.
    • (2008) Eur. J. Cell Biol. , vol.87 , pp. 517-525
    • Goicoechea, S.M.1    Arneman, D.2    Otey, C.A.3
  • 17
    • 84872925287 scopus 로고    scopus 로고
    • A two-segment model for thin filament architecture in skeletal muscle
    • Gokhin, D. S. and Fowler, V. M. (2013). A two-segment model for thin filament architecture in skeletal muscle. Nat. Rev. Mol. Cell Biol. 14, 113-119.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 113-119
    • Gokhin, D.S.1    Fowler, V.M.2
  • 18
    • 66149095797 scopus 로고    scopus 로고
    • Reduced thin filament length in nebulin-knockout skeletal muscle alters isometric contractile properties
    • Gokhin, D. S., Bang, M. L., Zhang, J., Chen, J. and Lieber, R. L. (2009). Reduced thin filament length in nebulin-knockout skeletal muscle alters isometric contractile properties. Am. J. Physiol. 296, C1123-C1132.
    • (2009) Am. J. Physiol. , vol.296
    • Gokhin, D.S.1    Bang, M.L.2    Zhang, J.3    Chen, J.4    Lieber, R.L.5
  • 22
    • 24044465136 scopus 로고    scopus 로고
    • Novel Src homology 3 domainbinding motifs identified from proteomic screen of a Pro-rich region
    • Jia, C. Y., Nie, J., Wu, C., Li, C. and Li, S. S. (2005). Novel Src homology 3 domainbinding motifs identified from proteomic screen of a Pro-rich region. Mol. Cell. Proteomics 4, 1155-1166.
    • (2005) Mol. Cell. Proteomics , vol.4 , pp. 1155-1166
    • Jia, C.Y.1    Nie, J.2    Wu, C.3    Li, C.4    Li, S.S.5
  • 23
    • 0037184992 scopus 로고    scopus 로고
    • The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy
    • Knöll, R., Hoshijima, M., Hoffman, H. M., Person, V., Lorenzen-Schmidt, I., Bang, M. L., Hayashi, T., Shiga, N., Yasukawa, H., Schaper, W. et al. (2002). The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy. Cell 111, 943-955.
    • (2002) Cell , vol.111 , pp. 943-955
    • Knöll, R.1    Hoshijima, M.2    Hoffman, H.M.3    Person, V.4    Lorenzen-Schmidt, I.5    Bang, M.L.6    Hayashi, T.7    Shiga, N.8    Yasukawa, H.9    Schaper, W.10
  • 25
    • 33748079591 scopus 로고    scopus 로고
    • Expression of distinct classes of titin isoforms in striated and smooth muscles by alternative splicing, and their conserved interaction with filamins
    • Labeit, S., Lahmers, S., Burkart, C., Fong, C., McNabb, M., Witt, S., Witt, C., Labeit, D. and Granzier, H. (2006). Expression of distinct classes of titin isoforms in striated and smooth muscles by alternative splicing, and their conserved interaction with filamins. J. Mol. Biol. 362, 664-681.
    • (2006) J. Mol. Biol. , vol.362 , pp. 664-681
    • Labeit, S.1    Lahmers, S.2    Burkart, C.3    Fong, C.4    McNabb, M.5    Witt, S.6    Witt, C.7    Labeit, D.8    Granzier, H.9
  • 26
    • 84860631021 scopus 로고    scopus 로고
    • Interaction network of the 14-3-3 protein in the ancient protozoan parasite Giardia duodenalis
    • Lalle, M., Camerini, S., Cecchetti, S., Sayadi, A., Crescenzi, M. and Pozio, E. (2012). Interaction network of the 14-3-3 protein in the ancient protozoan parasite Giardia duodenalis. J. Proteome Res. 11, 2666-2683.
    • (2012) J. Proteome Res. , vol.11 , pp. 2666-2683
    • Lalle, M.1    Camerini, S.2    Cecchetti, S.3    Sayadi, A.4    Crescenzi, M.5    Pozio, E.6
  • 28
    • 2442576932 scopus 로고    scopus 로고
    • Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1
    • Li, B., Zhuang, L. and Trueb, B. (2004). Zyxin interacts with the SH3 domains of the cytoskeletal proteins LIM-nebulette and Lasp-1. J. Biol. Chem. 279, 20401-20410.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20401-20410
    • Li, B.1    Zhuang, L.2    Trueb, B.3
  • 29
    • 54549121277 scopus 로고    scopus 로고
    • Thin filament length regulation in striated muscle sarcomeres: pointed-end dynamics go beyond a nebulin ruler
    • Littlefield, R. S. and Fowler, V. M. (2008). Thin filament length regulation in striated muscle sarcomeres: pointed-end dynamics go beyond a nebulin ruler. Semin. Cell Dev. Biol. 19, 511-519.
    • (2008) Semin. Cell Dev. Biol. , vol.19 , pp. 511-519
    • Littlefield, R.S.1    Fowler, V.M.2
  • 30
    • 0030871066 scopus 로고    scopus 로고
    • Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression
    • Louis, H. A., Pino, J. D., Schmeichel, K. L., Pomies, P. and Beckerle, M. C. (1997). Comparison of three members of the cysteine-rich protein family reveals functional conservation and divergent patterns of gene expression. J. Biol. Chem. 272, 27484-27491.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27484-27491
    • Louis, H.A.1    Pino, J.D.2    Schmeichel, K.L.3    Pomies, P.4    Beckerle, M.C.5
  • 31
    • 75749136013 scopus 로고    scopus 로고
    • The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling
    • Luther, P. K. (2009). The vertebrate muscle Z-disc: sarcomere anchor for structure and signalling. J. Muscle Res. Cell Motil. 30, 171-185.
    • (2009) J. Muscle Res. Cell Motil. , vol.30 , pp. 171-185
    • Luther, P.K.1
  • 32
    • 0037132502 scopus 로고    scopus 로고
    • Interaction of nebulin SH3 domain with titin PEVK and myopalladin: implications for the signaling and assembly role of titin and nebulin
    • Ma, K. and Wang, K. (2002). Interaction of nebulin SH3 domain with titin PEVK and myopalladin: implications for the signaling and assembly role of titin and nebulin. FEBS Lett. 532, 273-278.
    • (2002) FEBS Lett. , vol.532 , pp. 273-278
    • Ma, K.1    Wang, K.2
  • 33
    • 33748749629 scopus 로고    scopus 로고
    • Titin as a giant scaffold for integrating stress and Src homology domain 3-mediated signaling pathways: the clustering of novel overlap ligand motifs in the elastic PEVK segment
    • Ma, K., Forbes, J. G., Gutierrez-Cruz, G. and Wang, K. (2006). Titin as a giant scaffold for integrating stress and Src homology domain 3-mediated signaling pathways: the clustering of novel overlap ligand motifs in the elastic PEVK segment. J. Biol. Chem. 281, 27539-27556.
    • (2006) J. Biol. Chem. , vol.281 , pp. 27539-27556
    • Ma, K.1    Forbes, J.G.2    Gutierrez-Cruz, G.3    Wang, K.4
  • 34
    • 0035030510 scopus 로고    scopus 로고
    • SH3 domains: complexity in moderation
    • Mayer, B. J. (2001). SH3 domains: complexity in moderation. J. Cell Sci. 114, 1253-1263.
    • (2001) J. Cell Sci. , vol.114 , pp. 1253-1263
    • Mayer, B.J.1
  • 36
    • 36549062582 scopus 로고    scopus 로고
    • Increased efficacy and decreased systemic-effects of botulinum toxin A injection after active or passive muscle manipulation
    • Minamoto, V. B., Hulst, J. B., Lim, M., Peace, W. J., Bremner, S. N., Ward, S. R. and Lieber, R. L. (2007). Increased efficacy and decreased systemic-effects of botulinum toxin A injection after active or passive muscle manipulation. Dev. Med. Child Neurol. 49, 907-914.
    • (2007) Dev. Med. Child Neurol. , vol.49 , pp. 907-914
    • Minamoto, V.B.1    Hulst, J.B.2    Lim, M.3    Peace, W.J.4    Bremner, S.N.5    Ward, S.R.6    Lieber, R.L.7
  • 37
    • 0026749753 scopus 로고
    • SH3-an abundant protein domain in search of a function
    • Musacchio, A., Gibson, T., Lehto, V. P. and Saraste, M. (1992). SH3-an abundant protein domain in search of a function. FEBS Lett. 307, 55-61.
    • (1992) FEBS Lett. , vol.307 , pp. 55-61
    • Musacchio, A.1    Gibson, T.2    Lehto, V.P.3    Saraste, M.4
  • 38
    • 16944367068 scopus 로고    scopus 로고
    • Nemaline myopathy: current concepts
    • The ENMC International Consortium and Nemaline Myopathy
    • North, K. N., Laing, N. G., Wallgren-Pettersson, C.; The ENMC International Consortium and Nemaline Myopathy (1997). Nemaline myopathy: current concepts. J. Med. Genet. 34, 705-713.
    • (1997) J. Med. Genet. , vol.34 , pp. 705-713
    • North, K.N.1    Laing, N.G.2    Wallgren-Pettersson, C.3
  • 41
    • 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
  • 42
    • 77951974414 scopus 로고    scopus 로고
    • Altered myofilament function depresses force generation in patients with nebulin-based nemaline myopathy (NEM2)
    • Ottenheijm, C. A., Hooijman, P., DeChene, E. T., Stienen, G. J., Beggs, A. H. and Granzier, H. (2010). Altered myofilament function depresses force generation in patients with nebulin-based nemaline myopathy (NEM2). J. Struct. Biol. 170, 334-343.
    • (2010) J. Struct. Biol. , vol.170 , pp. 334-343
    • Ottenheijm, C.A.1    Hooijman, P.2    DeChene, E.T.3    Stienen, G.J.4    Beggs, A.H.5    Granzier, H.6
  • 43
    • 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
  • 44
    • 48249127189 scopus 로고    scopus 로고
    • Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc
    • Pappas, C. T., Bhattacharya, N., Cooper, J. A. and Gregorio, C. C. (2008). Nebulin interacts with CapZ and regulates thin filament architecture within the Z-disc. Mol. Biol. Cell 19, 1837-1847.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1837-1847
    • Pappas, C.T.1    Bhattacharya, N.2    Cooper, J.A.3    Gregorio, C.C.4
  • 45
    • 77953141955 scopus 로고    scopus 로고
    • Nebulin regulates actin filament lengths by a stabilization mechanism
    • Pappas, C. T., Krieg, P. A. and Gregorio, C. C. (2010). Nebulin regulates actin filament lengths by a stabilization mechanism. J. Cell Biol. 189, 859-870.
    • (2010) J. Cell Biol. , vol.189 , pp. 859-870
    • Pappas, C.T.1    Krieg, P.A.2    Gregorio, C.C.3
  • 47
    • 0032512807 scopus 로고    scopus 로고
    • SH3 in muscles: solution structure of the SH3 domain from nebulin
    • Politou, A. S., Millevoi, S., Gautel, M., Kolmerer, B. and Pastore, A. (1998). SH3 in muscles: solution structure of the SH3 domain from nebulin. J. Mol. Biol. 276, 189-202.
    • (1998) J. Mol. Biol. , vol.276 , pp. 189-202
    • Politou, A.S.1    Millevoi, S.2    Gautel, M.3    Kolmerer, B.4    Pastore, A.5
  • 49
    • 0029157584 scopus 로고
    • Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein)
    • Reinhard, M., Jouvenal, K., Tripier, D. and Walter, U. (1995). Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Proc. Natl. Acad. Sci. USA 92, 7956-7960.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7956-7960
    • Reinhard, M.1    Jouvenal, K.2    Tripier, D.3    Walter, U.4
  • 50
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi, R., Ma, L., Miki, H., Lopez, M., Kirchhausen, T., Takenawa, T. and Kirschner, M. W. (1999). The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97, 221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 51
    • 2442515432 scopus 로고    scopus 로고
    • Molecular analysis of the interaction between palladin and alpha-actinin
    • Rönty, M., Taivainen, A., Moza, M., Otey, C. A. and Carpén, O. (2004). Molecular analysis of the interaction between palladin and alpha-actinin. FEBS Lett. 566, 30-34.
    • (2004) FEBS Lett. , vol.566 , pp. 30-34
    • Rönty, M.1    Taivainen, A.2    Moza, M.3    Otey, C.A.4    Carpén, O.5
  • 52
    • 36049003590 scopus 로고    scopus 로고
    • "Z"eroing in on the role of Cypher in striated muscle function, signaling, and human disease
    • Sheikh, F., Bang, M. L., Lange, S. and Chen, J. (2007). "Z"eroing in on the role of Cypher in striated muscle function, signaling, and human disease. Trends Cardiovasc. Med. 17, 258-262.
    • (2007) Trends Cardiovasc. Med. , vol.17 , pp. 258-262
    • Sheikh, F.1    Bang, M.L.2    Lange, S.3    Chen, J.4
  • 55
    • 76649104716 scopus 로고    scopus 로고
    • Reduced myofibrillar connectivity and increased Z-disk width in nebulindeficient skeletal muscle
    • Tonino, P., Pappas, C. T., Hudson, B. D., Labeit, S., Gregorio, C. C. and Granzier, H. (2010). Reduced myofibrillar connectivity and increased Z-disk width in nebulindeficient skeletal muscle. J. Cell Sci. 123, 384-391.
    • (2010) J. Cell Sci. , vol.123 , pp. 384-391
    • Tonino, P.1    Pappas, C.T.2    Hudson, B.D.3    Labeit, S.4    Gregorio, C.C.5    Granzier, H.6
  • 56
    • 84861898895 scopus 로고    scopus 로고
    • Axial distribution of myosin binding protein-C is unaffected by mutations in human cardiac and skeletal muscle
    • Vydyanath, A., Gurnett, C. A., Marston, S. and Luther, P. K. (2012). Axial distribution of myosin binding protein-C is unaffected by mutations in human cardiac and skeletal muscle. J. Muscle Res. Cell Motil. 33, 61-74.
    • (2012) J. Muscle Res. Cell Motil. , vol.33 , pp. 61-74
    • Vydyanath, A.1    Gurnett, C.A.2    Marston, S.3    Luther, P.K.4
  • 59
    • 0024226674 scopus 로고
    • Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line
    • Wang, K. and Wright, J. (1988). Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line. J. Cell Biol. 107, 2199-2212.
    • (1988) J. Cell Biol. , vol.107 , pp. 2199-2212
    • Wang, K.1    Wright, J.2
  • 60
    • 0036021778 scopus 로고    scopus 로고
    • Functional characteristics of dystrophic skeletal muscle: insights from animal models
    • Watchko, J. F., O'Day, T. L. and Hoffman, E. P. (2002). Functional characteristics of dystrophic skeletal muscle: insights from animal models. J. Appl. Physiol. 93, 407-417.
    • (2002) J. Appl. Physiol. , vol.93 , pp. 407-417
    • Watchko, J.F.1    O'Day, T.L.2    Hoffman, E.P.3
  • 61
    • 33748058496 scopus 로고    scopus 로고
    • Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo
    • Witt, C. C., Burkart, C., Labeit, D., McNabb, M., Wu, Y., Granzier, H. and Labeit, S. (2006). Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo. EMBO J. 25, 3843-3855.
    • (2006) EMBO J. , vol.25 , pp. 3843-3855
    • Witt, C.C.1    Burkart, C.2    Labeit, D.3    McNabb, M.4    Wu, Y.5    Granzier, H.6    Labeit, S.7
  • 62
    • 48249120408 scopus 로고    scopus 로고
    • Syncoilin is required for generating maximum isometric stress in skeletal muscle but dispensable for muscle cytoarchitecture
    • Zhang, J., Bang, M. L., Gokhin, D. S., Lu, Y., Cui, L., Li, X., Gu, Y., Dalton, N. D., Scimia, M. C., Peterson, K. L. et al. (2008). Syncoilin is required for generating maximum isometric stress in skeletal muscle but dispensable for muscle cytoarchitecture. Am. J. Physiol. 294, C1175-C1182.
    • (2008) Am. J. Physiol. , vol.294
    • Zhang, J.1    Bang, M.L.2    Gokhin, D.S.3    Lu, Y.4    Cui, L.5    Li, X.6    Gu, Y.7    Dalton, N.D.8    Scimia, M.C.9    Peterson, K.L.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.