메뉴 건너뛰기




Volumn 128, Issue 2, 2015, Pages 239-250

Leiomodin 3 and tropomodulin 4 have overlapping functions during skeletal myofibrillogenesis

Author keywords

Actin thin filament; Leiomodin; Sarcomere; Skeletal muscle; Tropomodulin

Indexed keywords

ACTIN CAPPING PROTEIN; LEIOMODIN 3; TROPOMODULIN; TROPOMODULIN 4; UNCLASSIFIED DRUG; LEIOMODIN-3 PROTEIN, HUMAN; MUSCLE PROTEIN;

EID: 84921396316     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.152702     Document Type: Article
Times cited : (31)

References (50)
  • 1
    • 0032948760 scopus 로고    scopus 로고
    • Tropomodulin assembles early in myofibrillogenesis in chick skeletal muscle: evidence that thin filaments rearrange to form striated myofibrils
    • Almenar-Queralt, A., Gregorio, C. C. and Fowler, V. M. (1999a). Tropomodulin assembles early in myofibrillogenesis in chick skeletal muscle: evidence that thin filaments rearrange to form striated myofibrils. J. Cell Sci. 112, 1111-1123.
    • (1999) J. Cell Sci , vol.112 , pp. 1111-1123
    • Almenar-queralt, A.1    Gregorio, C.C.2    Fowler, V.M.3
  • 2
    • 0033214493 scopus 로고    scopus 로고
    • Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle
    • Almenar-Queralt, A., Lee, A., Conley, C. A., Ribas de Pouplana, L. and Fowler, V. M. (1999b). Identification of a novel tropomodulin isoform, skeletal tropomodulin, that caps actin filament pointed ends in fast skeletal muscle. J. Biol. Chem. 274, 28466-28475.
    • (1999) J. Biol. Chem , vol.274 , pp. 28466-28475
    • Almenar-queralt, A.1    Lee, A.2    Conley, C.A.3    Ribas, D.L.4    Fowler, V.M.5
  • 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
  • 4
    • 84875460818 scopus 로고    scopus 로고
    • Investigating lasp-2 in cell adhesion: new binding partners and roles in motility
    • Bliss, K. T., Chu, M., Jones-Weinert, C. M. and Gregorio, C. C. (2013). Investigating lasp-2 in cell adhesion: new binding partners and roles in motility. Mol. Biol. Cell 24, 995-1006.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 995-1006
    • Bliss, K.T.1    Chu, M.2    Jones-weinert, C.M.3    Gregorio, C.C.4
  • 7
    • 0344406087 scopus 로고    scopus 로고
    • E-Tmod capping of actin filaments at the slow-growing end is required to establish mouse embryonic circulation
    • Chu, X., Chen, J., Reedy, M. C., Vera, C., Sung, K. L. P. and Sung, L. A. (2003). E-Tmod capping of actin filaments at the slow-growing end is required to establish mouse embryonic circulation. Am. J. Physiol. 284, 1827-1838.
    • (2003) Am. J. Physiol , vol.284 , pp. 1827-1838
    • Chu, X.1    Chen, J.2    Reedy, M.C.3    Vera, C.4    Sung, K.L.P.5    Sung, L.A.6
  • 8
    • 0035870762 scopus 로고    scopus 로고
    • Leiomodins: larger members of the tropomodulin (Tmod) gene family
    • Conley, C. A., Fritz-Six, K. L., Almenar-Queralt, A. and Fowler, V. M. (2001). Leiomodins: larger members of the tropomodulin (Tmod) gene family. Genomics 73, 127-139.
    • (2001) Genomics , vol.73 , pp. 127-139
    • Conley, C.A.1    Fritz-six, K.L.2    Almenar-queralt, A.3    Fowler, V.M.4
  • 9
    • 0141809370 scopus 로고    scopus 로고
    • Tropomodulin contains two actin filament pointed end-capping domains
    • Fowler, V. M., Greenfield, N. J. and Moyer, J. (2003). Tropomodulin contains two actin filament pointed end-capping domains. J. Biol. Chem. 278, 40000-40009.
    • (2003) J. Biol. Chem , vol.278 , pp. 40000-40009
    • Fowler, V.M.1    Greenfield, N.J.2    Moyer, J.3
  • 10
    • 0347480271 scopus 로고    scopus 로고
    • Aberrant myofibril assembly in tropomodulin1 null mice leads to aborted heart development and embryonic lethality
    • Fritz-Six, K. L., Cox, P. R., Fischer, R. S., Xu, B., Gregorio, C. C., Zoghbi, H. Y. and Fowler, V. M. (2003). Aberrant myofibril assembly in tropomodulin1 null mice leads to aborted heart development and embryonic lethality. J. Cell Biol. 163, 1033-1044.
    • (2003) J. Cell Biol , vol.163 , pp. 1033-1044
    • Fritz-six, K.L.1    Cox, P.R.2    Fischer, R.S.3    Xu, B.4    Gregorio, C.C.5    Zoghbi, H.Y.6    Fowler, V.M.7
  • 11
    • 79960260136 scopus 로고    scopus 로고
    • Cytoplasmic c-actin and tropomodulin isoforms link to the sarcoplasmic reticulum in skeletal muscle fibers
    • Gokhin, D. S. and Fowler, V. M. (2011). Cytoplasmic c-actin and tropomodulin isoforms link to the sarcoplasmic reticulum in skeletal muscle fibers. J. Cell Biol. 194, 105-120.
    • (2011) J. Cell Biol , vol.194 , pp. 105-120
    • Gokhin, D.S.1    Fowler, V.M.2
  • 12
    • 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, 1123-1132.
    • (2009) Am. J. Physiol , vol.296 , pp. 1123-1132
    • Gokhin, D.S.1    Bang, M.L.2    Zhang, J.3    Chen, J.4    Lieber, R.L.5
  • 14
    • 0025774399 scopus 로고
    • Effect of thin filament length on the force-sarcomere length relation of skeletal muscle
    • Granzier, H., Akster, H. A. and Ter Keurs, H. (1991). Effect of thin filament length on the force-sarcomere length relation of skeletal muscle. Am. J. Physiol. 260, 1060-1070.
    • (1991) Am. J. Physiol , vol.260 , pp. 1060-1070
    • Granzier, H.1    Akster, H.A.2    Keurs, T.H.3
  • 15
    • 11244323829 scopus 로고    scopus 로고
    • Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1
    • Greenfield, N. J., Kostyukova, A. S. and Hitchcock-DeGregori, S. E. (2005). Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1. Biophys. J. 88, 372-383.
    • (2005) Biophys. J , vol.88 , pp. 372-383
    • Greenfield, N.J.1    Kostyukova, A.S.2    Hitchcock-deGregori, S.E.3
  • 16
    • 0029166140 scopus 로고
    • Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes
    • Gregorio, C. C., Weber, A., Bondad, M., Pennise, C. R. and Fowler, V. M. (1995). Requirement of pointed-end capping by tropomodulin to maintain actin filament length in embryonic chick cardiac myocytes. Nature 377, 83-86.
    • (1995) Nature , vol.377 , pp. 83-86
    • Gregorio, C.C.1    Weber, A.2    Bondad, M.3    Pennise, C.R.4    Fowler, V.M.5
  • 17
    • 0026762834 scopus 로고
    • Isolation and characterization of cDNA clones encoding the skeletal and smooth muscle Xenopus laevis beta tropomyosin isoforms
    • Hardy, S. and Thiébaud, P. (1992). Isolation and characterization of cDNA clones encoding the skeletal and smooth muscle Xenopus laevis beta tropomyosin isoforms. Biochim. Biophys. 1131, 239-242.
    • (1992) Biochim. Biophys , vol.1131 , pp. 239-242
    • Hardy, S.1    Thiébaud, P.2
  • 18
    • 0032869409 scopus 로고    scopus 로고
    • Two skeletal a-tropomyosin transcripts with distinct 39UTR have different temporal and spatial patterns of expression in the striated muscle lineages of Xenopus laevis
    • Hardy, S., Hamon, S., Cooper, B., Mohun, T. and Thiébaud, P. (1999). Two skeletal a-tropomyosin transcripts with distinct 39UTR have different temporal and spatial patterns of expression in the striated muscle lineages of Xenopus laevis. Mech. Dev. 87, 199-202.
    • (1999) Mech. Dev , vol.87 , pp. 199-202
    • Hardy, S.1    Hamon, S.2    Cooper, B.3    Mohun, T.4    Thiébaud, P.5
  • 19
    • 0026285616 scopus 로고
    • In situ hybridization: an improved whole-mount method for Xenopus embryos
    • Harland, R. M. (1991). In situ hybridization: an improved whole-mount method for Xenopus embryos. Methods Cell Biol. 36, 685-695.
    • (1991) Methods Cell Biol , vol.36 , pp. 685-695
    • Harland, R.M.1
  • 21
    • 0024067123 scopus 로고
    • Development of myotomal cells in Xenopus laevis larvae
    • Huang, C. L. and Hockaday, A. R. (1988). Development of myotomal cells in Xenopus laevis larvae. J. Anat. 159, 129-136.
    • (1988) J. Anat , vol.159 , pp. 129-136
    • Huang, C.L.1    Hockaday, A.R.2
  • 22
    • 33646945995 scopus 로고    scopus 로고
    • Leucine 135 of tropomodulin-1 regulates its association with tropomyosin, its cellular localization, and the integrity of sarcomeres
    • Kong, K. Y. and Kedes, L. (2006). Leucine 135 of tropomodulin-1 regulates its association with tropomyosin, its cellular localization, and the integrity of sarcomeres. J. Biol. Chem. 281, 9589-9599.
    • (2006) J. Biol. Chem , vol.281 , pp. 9589-9599
    • Kong, K.Y.1    Kedes, L.2
  • 23
    • 34548017691 scopus 로고    scopus 로고
    • Leiomodin/tropomyosin interactions are isoform specific
    • Kostyukova, A. S. (2007). Leiomodin/tropomyosin interactions are isoform specific. Arch. Biochem. Biophys. 465, 227-230.
    • (2007) Arch. Biochem. Biophys , vol.465 , pp. 227-230
    • Kostyukova, A.S.1
  • 24
    • 39749176245 scopus 로고    scopus 로고
    • Tropomodulins and tropomodulin/tropomyosin interactions
    • Kostyukova, A. S. (2008). Tropomodulins and tropomodulin/tropomyosin interactions. Cell. Mol. Life Sci. 65, 563-569.
    • (2008) Cell. Mol. Life Sci , vol.65 , pp. 563-569
    • Kostyukova, A.S.1
  • 25
    • 15444377428 scopus 로고    scopus 로고
    • Structural requirements of tropomodulin for tropomyosin binding and actin filament capping
    • Kostyukova, A. S., Rapp, B. A., Choy, A., Greenfield, N. J. and Hitchcock-DeGregori, S. E. (2005). Structural requirements of tropomodulin for tropomyosin binding and actin filament capping. Biochemistry 44, 4905-4910.
    • (2005) Biochemistry , vol.44 , pp. 4905-4910
    • Kostyukova, A.S.1    Rapp, B.A.2    Choy, A.3    Greenfield, N.J.4    Hitchcock-deGregori, S.E.5
  • 26
    • 33749345764 scopus 로고    scopus 로고
    • Tropomodulin binds two tropomyosins: a novel model for actin filament capping
    • Kostyukova, A. S., Choy, A. and Rapp, B. A. (2006). Tropomodulin binds two tropomyosins: a novel model for actin filament capping. Biochemistry 45, 12068-12075.
    • (2006) Biochemistry , vol.45 , pp. 12068-12075
    • Kostyukova, A.S.1    Choy, A.2    Rapp, B.A.3
  • 27
    • 0034976418 scopus 로고    scopus 로고
    • Actin dynamics at pointed ends regulates thin filament length in striated muscle
    • Littlefield, R., Almenar-Queralt, A. and Fowler, V. M. (2001). Actin dynamics at pointed ends regulates thin filament length in striated muscle. Nat. Cell Biol. 3, 544-551.
    • (2001) Nat. Cell Biol , vol.3 , pp. 544-551
    • Littlefield, R.1    Almenar-queralt, A.2    Fowler, V.M.3
  • 28
    • 0036231585 scopus 로고    scopus 로고
    • Measurement of thin filament lengths by distributed deconvolution analysis of fluorescence images
    • Littlefield, R. and Fowler, V. M. (2002). Measurement of thin filament lengths by distributed deconvolution analysis of fluorescence images. Biophys J. 82, 2548-2564.
    • (2002) Biophys J , vol.82 , pp. 2548-2564
    • Littlefield, R.1    Fowler, V.M.2
  • 29
    • 58149326918 scopus 로고    scopus 로고
    • Tropomodulin1 is required in the heart but not the yolk sac for mouse embryonic development
    • McKeown, C. R., Nowak, R. B., Moyer, J., Sussman, M. A. and Fowler, V. M. (2008). Tropomodulin1 is required in the heart but not the yolk sac for mouse embryonic development. Circ. Res. 103, 1241-1248.
    • (2008) Circ. Res , vol.103 , pp. 1241-1248
    • McKeown, C.R.1    Nowak, R.B.2    Moyer, J.3    Sussman, M.A.4    Fowler, V.M.5
  • 30
    • 0021231377 scopus 로고
    • Cell type-specific activation of actin genes in the early amphibian embryo
    • Mohun, T. J., Brennan, S., Dathan, N., Fairman, S. and Gurdon, J. B. (1984). Cell type-specific activation of actin genes in the early amphibian embryo. Nature 311, 716-721.
    • (1984) Nature , vol.311 , pp. 716-721
    • Mohun, T.J.1    Brennan, S.2    Dathan, N.3    Fairman, S.4    Gurdon, J.B.5
  • 31
    • 0141545016 scopus 로고    scopus 로고
    • The interaction of tropomodulin with tropomyosin stabilizes thin filaments in cardiac myocytes
    • Mudry, R. E., Perry, C. N., Richards, M., Fowler, V. M. and Gregorio, C. C. (2003). The interaction of tropomodulin with tropomyosin stabilizes thin filaments in cardiac myocytes. J. Cell Biol. 162, 1057-1068.
    • (2003) J. Cell Biol , vol.162 , pp. 1057-1068
    • Mudry, R.E.1    Perry, C.N.2    Richards, M.3    Fowler, V.M.4    Gregorio, C.C.5
  • 32
    • 0016715199 scopus 로고
    • Myogenesis in the trunk and leg during development of the tadpole of Xenopus laevis (Daudin 1802)
    • Muntz, L. (1975). Myogenesis in the trunk and leg during development of the tadpole of Xenopus laevis (Daudin 1802). J. Embryol. Exp. Morphol. 33, 757-774.
    • (1975) J. Embryol. Exp. Morphol , vol.33 , pp. 757-774
    • Muntz, L.1
  • 33
    • 84856078064 scopus 로고    scopus 로고
    • Leiomodin 1, a new serum response factor-dependent target gene expressed preferentially in differentiated smooth muscle cells
    • Nanda, V. and Miano, J. M. (2012). Leiomodin 1, a new serum response factor-dependent target gene expressed preferentially in differentiated smooth muscle cells. J. Biol. Chem. 287, 2459-2467.
    • (2012) J. Biol. Chem , vol.287 , pp. 2459-2467
    • Nanda, V.1    Miano, J.M.2
  • 34
    • 84897953825 scopus 로고    scopus 로고
    • Preparation of developing Xenopus muscle for sarcomeric protein localization by high-resolution imaging
    • Nworu, C. U., Krieg, P. A. and Gregorio, C. C. (2013). Preparation of developing Xenopus muscle for sarcomeric protein localization by high-resolution imaging. Methods 66, 370-379.
    • (2013) Methods , vol.66 , pp. 370-379
    • Nworu, C.U.1    Krieg, P.A.2    Gregorio, C.C.3
  • 35
    • 77958521897 scopus 로고    scopus 로고
    • Dynamic regulation of sarcomeric actin filaments in striated muscle
    • Ono, S. (2010). Dynamic regulation of sarcomeric actin filaments in striated muscle. Cytoskeleton 67, 677-692.
    • (2010) Cytoskeleton , vol.67 , pp. 677-692
    • Ono, S.1
  • 36
    • 20444417053 scopus 로고    scopus 로고
    • Disruption in the tropomodulin1 (Tmod1) gene compromises cardiomyocyte development in murine embryonic stem cells by arresting myofibril maturation
    • Ono, Y., Schwach, C., Antin, P. B. and Gregorio, C. C. (2005). Disruption in the tropomodulin1 (Tmod1) gene compromises cardiomyocyte development in murine embryonic stem cells by arresting myofibril maturation. Dev. Biol. 282, 336-348.
    • (2005) Dev. Biol , vol.282 , pp. 336-348
    • Ono, Y.1    Schwach, C.2    Antin, P.B.3    Gregorio, C.C.4
  • 37
    • 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
  • 38
    • 0028278854 scopus 로고
    • The premyofibril: evidence for its role in myofibrillogenesis
    • Rhee, D., Sanger, J. M. and Sanger, J. W. (1994). The premyofibril: evidence for its role in myofibrillogenesis. Cell Motil. Cytoskeleton 28, 1-24.
    • (1994) Cell Motil. Cytoskeleton , vol.28 , pp. 1-24
    • Rhee, D.1    Sanger, J.M.2    Sanger, J.W.3
  • 39
    • 77949864284 scopus 로고    scopus 로고
    • Distinct roles for telethonin N-versus C-terminus in sarcomere assembly and maintenance
    • Sadikot, T., Hammond, C. R. and Ferrari, M. B. (2010). Distinct roles for telethonin N-versus C-terminus in sarcomere assembly and maintenance. Dev. Dyn. 239, 1124-1135.
    • (2010) Dev. Dyn , vol.239 , pp. 1124-1135
    • Sadikot, T.1    Hammond, C.R.2    Ferrari, M.B.3
  • 41
    • 62849125813 scopus 로고    scopus 로고
    • The initial steps of myofibril assembly: integrins pave the way
    • Sparrow, J. C. and Schöck, F. (2009). The initial steps of myofibril assembly: integrins pave the way. Nat. Rev. Mol. Cell Biol. 10, 293-298.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 293-298
    • Sparrow, J.C.1    Schöck, F.2
  • 42
    • 0031932605 scopus 로고    scopus 로고
    • Altered expression of tropomodulin in cardiomyocytes disrupts the sarcomeric structure of myofibrils
    • Sussman, M. A., Baqué, S., Uhm, C. S., Daniels, M. P., Price, R. L., Simpson, D., Terracio, L. and Kedes, L. (1998). Altered expression of tropomodulin in cardiomyocytes disrupts the sarcomeric structure of myofibrils. Circ. Res. 82, 94-105.
    • (1998) Circ. Res , vol.82 , pp. 94-105
    • Sussman, M.A.1    Baqué, S.2    Uhm, C.S.3    Daniels, M.P.4    Price, R.L.5    Simpson, D.6    Terracio, L.7    Kedes, L.8
  • 44
    • 77956930753 scopus 로고    scopus 로고
    • Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle
    • Tsukada, T., Pappas, C. T., Moroz, N., Antin, P. B., Kostyukova, A. S. and Gregorio, C. C. (2010). Leiomodin-2 is an antagonist of tropomodulin-1 at the pointed end of the thin filaments in cardiac muscle. J. Cell Sci. 123, 3136-3145.
    • (2010) J. Cell Sci , vol.123 , pp. 3136-3145
    • Tsukada, T.1    Pappas, C.T.2    Moroz, N.3    Antin, P.B.4    Kostyukova, A.S.5    Gregorio, C.C.6
  • 45
    • 78751507345 scopus 로고    scopus 로고
    • Identification of residues within tropomodulin-1 responsible for its localization at the pointed ends of the actin filaments in cardiac myocytes
    • Tsukada, T., Kotlyanskaya, L., Huynh, R., Desai, B., Novak, S. M., Kajava, A. V., Gregorio, C. C. and Kostyukova, A. S. (2011). Identification of residues within tropomodulin-1 responsible for its localization at the pointed ends of the actin filaments in cardiac myocytes. J. Biol. Chem. 286, 2194-2204.
    • (2011) J. Biol. Chem , vol.286 , pp. 2194-2204
    • Tsukada, T.1    Kotlyanskaya, L.2    Huynh, R.3    Desai, B.4    Novak, S.M.5    Kajava, A.V.6    Gregorio, C.C.7    Kostyukova, A.S.8
  • 46
    • 79951769664 scopus 로고    scopus 로고
    • Control of local Rho GTPase crosstalk by Abr
    • Vaughan, E. M., Miller, A. L., Yu, H. Y. and Bement, W. M. (2001). Control of local Rho GTPase crosstalk by Abr. Curr Biol. 21, 270-277.
    • (2001) Curr Biol , vol.21 , pp. 270-277
    • Vaughan, E.M.1    Miller, A.L.2    Yu, H.Y.3    Bement, W.M.4
  • 47
    • 0029838840 scopus 로고    scopus 로고
    • N-tropomodulin: a novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin
    • Watakabe, A., Kobayashi, R. and Helfman, D. M. (1996). N-tropomodulin: a novel isoform of tropomodulin identified as the major binding protein to brain tropomyosin. J. Cell Sci. 109, 2299-2310.
    • (1996) J. Cell Sci , vol.109 , pp. 2299-2310
    • Watakabe, A.1    Kobayashi, R.2    Helfman, D.M.3
  • 48
    • 0028099996 scopus 로고
    • Tropomodulin caps the pointed ends of actin filaments
    • Weber, A., Pennise, C. R., Babcock, G. G. and Fowler, V. M. (1994). Tropomodulin caps the pointed ends of actin filaments. J. Cell Biol. 127, 1627-1635.
    • (1994) J. Cell Biol , vol.127 , pp. 1627-1635
    • Weber, A.1    Pennise, C.R.2    Babcock, G.G.3    Fowler, V.M.4
  • 49
    • 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
  • 50
    • 85027946629 scopus 로고    scopus 로고
    • Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types
    • Yamashiro, S., Gokhin, D. S., Kimura, S., Nowak, R. B. and Fowler, V. M. (2012). Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types. Cytoskeleton. 69, 337-370.
    • (2012) Cytoskeleton , vol.69 , pp. 337-370
    • Yamashiro, S.1    Gokhin, D.S.2    Kimura, S.3    Nowak, R.B.4    Fowler, V.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.