메뉴 건너뛰기




Volumn 144, Issue , 2017, Pages 92-101

Mechanical forces during muscle development

Author keywords

Biomechanics; Force; Integrin; Muscle; Myofibrillogenesis; Sarcomere; Self organization; Tension; Titin

Indexed keywords

INTEGRIN; ACTIN; CONNECTIN;

EID: 85008936622     PISSN: 09254773     EISSN: 18726356     Source Type: Journal    
DOI: 10.1016/j.mod.2016.11.003     Document Type: Review
Times cited : (95)

References (103)
  • 3
    • 0035941407 scopus 로고    scopus 로고
    • The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system
    • Bang, M.L., Centner, T., Fornoff, F., Geach, A.J., Gotthardt, M., McNabb, M., Witt, C.C., Labeit, D., Gregorio, C.C., Granzier, H., Labeit, S., The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system. Circ. Res. 89 (2001), 1065–1072, 10.1161/hh2301.100981.
    • (2001) Circ. Res. , vol.89 , pp. 1065-1072
    • Bang, M.L.1    Centner, T.2    Fornoff, F.3    Geach, A.J.4    Gotthardt, M.5    McNabb, M.6    Witt, C.C.7    Labeit, D.8    Gregorio, C.C.9    Granzier, H.10    Labeit, S.11
  • 6
    • 0035891368 scopus 로고    scopus 로고
    • Zipper nonmuscle myosin-II functions downstream of PS2 integrin during
    • Bloor, J., Kiehart, D., Zipper nonmuscle myosin-II functions downstream of PS2 integrin during. Dev. Biol. 239:2 (2001), 215–228.
    • (2001) Dev. Biol. , vol.239 , Issue.2 , pp. 215-228
    • Bloor, J.1    Kiehart, D.2
  • 7
    • 84902387938 scopus 로고    scopus 로고
    • Titin kinase is an inactive pseudokinase scaffold that supports MuRF1 recruitment to the sarcomeric M-line
    • Bogomolovas, J., Gasch, A., Simkovic, F., Rigden, D.J., Labeit, S., Mayans, O., Titin kinase is an inactive pseudokinase scaffold that supports MuRF1 recruitment to the sarcomeric M-line. Open Biol., 4, 2014, 140041, 10.1098/rsob.140041.
    • (2014) Open Biol. , vol.4 , pp. 140041
    • Bogomolovas, J.1    Gasch, A.2    Simkovic, F.3    Rigden, D.J.4    Labeit, S.5    Mayans, O.6
  • 8
    • 0242417166 scopus 로고    scopus 로고
    • A somitic compartment of tendon progenitors
    • Brent, A., Schweitzer, R., Tabin, C., A somitic compartment of tendon progenitors. Cell 113 (2003), 235–248.
    • (2003) Cell , vol.113 , pp. 235-248
    • Brent, A.1    Schweitzer, R.2    Tabin, C.3
  • 9
    • 4544261800 scopus 로고    scopus 로고
    • FGF acts directly on the somitic tendon progenitors through the Ets transcription factors Pea3 and Erm to regulate scleraxis expression
    • Brent, A., Tabin, C., FGF acts directly on the somitic tendon progenitors through the Ets transcription factors Pea3 and Erm to regulate scleraxis expression. Development, 131, 2004, 3885.
    • (2004) Development , vol.131 , pp. 3885
    • Brent, A.1    Tabin, C.2
  • 10
    • 0034233543 scopus 로고    scopus 로고
    • Cell-cell adhesion via the ECM: integrin genetics in fly and worm
    • Brown, N.H., Cell-cell adhesion via the ECM: integrin genetics in fly and worm. Matrix Biol. 19 (2000), 191–201.
    • (2000) Matrix Biol. , vol.19 , pp. 191-201
    • Brown, N.H.1
  • 13
    • 27744554880 scopus 로고    scopus 로고
    • In vivo selective cytoskeleton dynamics quantification in interphase cells induced by pulsed ultraviolet laser nanosurgery
    • Colombelli, J., Reynaud, E.G., Rietdorf, J., Pepperkok, R., Stelzer, E.H.K., In vivo selective cytoskeleton dynamics quantification in interphase cells induced by pulsed ultraviolet laser nanosurgery. Traffic 6 (2005), 1093–1102, 10.1111/j.1600-0854.2005.00334.x.
    • (2005) Traffic , vol.6 , pp. 1093-1102
    • Colombelli, J.1    Reynaud, E.G.2    Rietdorf, J.3    Pepperkok, R.4    Stelzer, E.H.K.5
  • 15
    • 2942659143 scopus 로고    scopus 로고
    • The sliding filament model: 1972-2004
    • Cooke, R., The sliding filament model: 1972-2004. J. Gen. Physiol. 123 (2004), 643–656, 10.1085/jgp.200409089.
    • (2004) J. Gen. Physiol. , vol.123 , pp. 643-656
    • Cooke, R.1
  • 16
    • 84930377695 scopus 로고    scopus 로고
    • Specification of the somatic musculature in Drosophila
    • Dobi, K.C., Schulman, V.K., Baylies, M.K., Specification of the somatic musculature in Drosophila. WIREs Dev. Biol., 2015, 10.1002/wdev.182.
    • (2015) WIREs Dev. Biol.
    • Dobi, K.C.1    Schulman, V.K.2    Baylies, M.K.3
  • 17
    • 0004002127 scopus 로고    scopus 로고
    • The Biomechanics of Insect Flight
    • Princeton University Press
    • Dudley, R., The Biomechanics of Insect Flight. 2000, Princeton University Press.
    • (2000)
    • Dudley, R.1
  • 18
    • 60549105984 scopus 로고    scopus 로고
    • The sarcomere and sarcomerogenesis
    • Ehler, E., Gautel, M., The sarcomere and sarcomerogenesis. Adv. Exp. Med. Biol. 642 (2008), 1–14.
    • (2008) Adv. Exp. Med. Biol. , vol.642 , pp. 1-14
    • Ehler, E.1    Gautel, M.2
  • 19
    • 0033013812 scopus 로고    scopus 로고
    • Myofibrillogenesis in the developing chicken heart: assembly of Z-disk, M-line and the thick filaments
    • Ehler, E., Rothen, B.M., Hämmerle, S.P., Komiyama, M., Perriard, J.C., Myofibrillogenesis in the developing chicken heart: assembly of Z-disk, M-line and the thick filaments. J. Cell Sci. 112:Pt 10 (1999), 1529–1539.
    • (1999) J. Cell Sci. , vol.112 , pp. 1529-1539
    • Ehler, E.1    Rothen, B.M.2    Hämmerle, S.P.3    Komiyama, M.4    Perriard, J.C.5
  • 20
    • 4544264684 scopus 로고    scopus 로고
    • Myotubes differentiate optimally on substrates with tissue-like stiffness: pathological implications for soft or stiff microenvironments
    • Engler, A.J., Myotubes differentiate optimally on substrates with tissue-like stiffness: pathological implications for soft or stiff microenvironments. J. Cell Biol. 166 (2004), 877–887, 10.1083/jcb.200405004.
    • (2004) J. Cell Biol. , vol.166 , pp. 877-887
    • Engler, A.J.1
  • 21
    • 0036837268 scopus 로고    scopus 로고
    • The kinase activity of the giant protein projectin of the flight muscle of Locusta migratoria
    • Fährmann, M., Fonk, I., Beinbrech, G., The kinase activity of the giant protein projectin of the flight muscle of Locusta migratoria. Insect Biochem. Mol. Biol. 32 (2002), 1401–1407.
    • (2002) Insect Biochem. Mol. Biol. , vol.32 , pp. 1401-1407
    • Fährmann, M.1    Fonk, I.2    Beinbrech, G.3
  • 22
    • 0032526950 scopus 로고    scopus 로고
    • A calcium signaling cascade essential for myosin thick filament assembly in Xenopus myocytes
    • Ferrari, M.B., Ribbeck, K., Hagler, D.J., Spitzer, N.C., A calcium signaling cascade essential for myosin thick filament assembly in Xenopus myocytes. J. Cell Biol. 141 (1998), 1349–1356.
    • (1998) J. Cell Biol. , vol.141 , pp. 1349-1356
    • Ferrari, M.B.1    Ribbeck, K.2    Hagler, D.J.3    Spitzer, N.C.4
  • 23
    • 84994882430 scopus 로고    scopus 로고
    • The piconewton force awakens: quantifying mechanics in cells
    • Freikamp, A., Cost, A.-L., Grashoff, C., The piconewton force awakens: quantifying mechanics in cells. Trends Cell Biol., 2016, 10.1016/j.tcb.2016.07.005.
    • (2016) Trends Cell Biol.
    • Freikamp, A.1    Cost, A.-L.2    Grashoff, C.3
  • 24
    • 0023924769 scopus 로고
    • The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line
    • Fürst, D.O., Osborn, M., Nave, R., Weber, K., The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line. J. Cell Biol. 106 (1988), 1563–1572.
    • (1988) J. Cell Biol. , vol.106 , pp. 1563-1572
    • Fürst, D.O.1    Osborn, M.2    Nave, R.3    Weber, K.4
  • 25
    • 79951552050 scopus 로고    scopus 로고
    • The sarcomeric cytoskeleton: who picks up the strain?
    • Gautel, M., The sarcomeric cytoskeleton: who picks up the strain?. Curr. Opin. Cell Biol. 23 (2011), 39–46, 10.1016/j.ceb.2010.12.001.
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 39-46
    • Gautel, M.1
  • 26
    • 79958862768 scopus 로고    scopus 로고
    • Cytoskeletal protein kinases: titin and its relations in mechanosensing
    • Gautel, M., Cytoskeletal protein kinases: titin and its relations in mechanosensing. Pflugers Arch. - Eur. J. Physiol. 462 (2011), 119–134, 10.1007/s00424-011-0946-1.
    • (2011) Pflugers Arch. - Eur. J. Physiol. , vol.462 , pp. 119-134
    • Gautel, M.1
  • 27
    • 0029882110 scopus 로고    scopus 로고
    • A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series
    • Gautel, M., Goulding, D., A molecular map of titin/connectin elasticity reveals two different mechanisms acting in series. FEBS Lett. 385 (1996), 11–14.
    • (1996) FEBS Lett. , vol.385 , pp. 11-14
    • Gautel, M.1    Goulding, D.2
  • 28
    • 0029801781 scopus 로고    scopus 로고
    • Assembly of the cardiac I-band region of titin/connectin: expression of the cardiac-specific regions and their structural relation to the elastic segments
    • Gautel, M., Lehtonen, E., Pietruschka, F., Assembly of the cardiac I-band region of titin/connectin: expression of the cardiac-specific regions and their structural relation to the elastic segments. J. Muscle Res. Cell Motil. 17 (1996), 449–461.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 449-461
    • Gautel, M.1    Lehtonen, E.2    Pietruschka, F.3
  • 29
    • 84872925287 scopus 로고    scopus 로고
    • A two-segment model for thin filament architecture in skeletal muscle
    • Gokhin, D.S., Fowler, V.M., A two-segment model for thin filament architecture in skeletal muscle. Nat. Rev. Mol. Cell Biol. 14 (2013), 113–119, 10.1038/nrm3510.
    • (2013) Nat. Rev. Mol. Cell Biol. , vol.14 , pp. 113-119
    • Gokhin, D.S.1    Fowler, V.M.2
  • 30
    • 0002836901 scopus 로고
    • Course-control, metabolism and wing interference during ultralong tethered flight in Drosophila melanogaster
    • Götz, K.G., Course-control, metabolism and wing interference during ultralong tethered flight in Drosophila melanogaster. J. Exp. Biol. 128 (1987), 35–46.
    • (1987) J. Exp. Biol. , vol.128 , pp. 35-46
    • Götz, K.G.1
  • 32
    • 59049094574 scopus 로고    scopus 로고
    • WNT11 acts as a directional cue to organize the elongation of early muscle fibres
    • Gros, J., Serralbo, O., Marcelle, C., WNT11 acts as a directional cue to organize the elongation of early muscle fibres. Nature 457 (2008), 589–593.
    • (2008) Nature , vol.457 , pp. 589-593
    • Gros, J.1    Serralbo, O.2    Marcelle, C.3
  • 33
    • 77951675873 scopus 로고    scopus 로고
    • Titin diversity—alternative splicing gone wild
    • Guo, W., Bharmal, S.J., Esbona, K., Greaser, M.L., Titin diversity—alternative splicing gone wild. J. Biomed. Biotechnol. 2010 (2010), 1–8, 10.1016/j.yjmcc.2009.11.013.
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 1-8
    • Guo, W.1    Bharmal, S.J.2    Esbona, K.3    Greaser, M.L.4
  • 35
    • 14644411012 scopus 로고    scopus 로고
    • Calcium transients regulate titin organization during myofibrillogenesis
    • Harris, B.N., Li, H., Terry, M., Ferrari, M.B., Calcium transients regulate titin organization during myofibrillogenesis. Cell Motil. Cytoskeleton 60 (2005), 129–139, 10.1002/cm.20054.
    • (2005) Cell Motil. Cytoskeleton , vol.60 , pp. 129-139
    • Harris, B.N.1    Li, H.2    Terry, M.3    Ferrari, M.B.4
  • 36
    • 84878324673 scopus 로고    scopus 로고
    • Forces in tissue morphogenesis and patterning
    • Heisenberg, C.-P., Bellaiche, Y., Forces in tissue morphogenesis and patterning. Cell 153 (2013), 948–962, 10.1016/j.cell.2013.05.008.
    • (2013) Cell , vol.153 , pp. 948-962
    • Heisenberg, C.-P.1    Bellaiche, Y.2
  • 37
    • 85014201888 scopus 로고    scopus 로고
    • Muscle
    • Academic Press
    • Hill, J., Olson, E., Muscle. 2012, Academic Press.
    • (2012)
    • Hill, J.1    Olson, E.2
  • 39
    • 0003594021 scopus 로고    scopus 로고
    • Mechanics of Motor Proteins & the Cytoskeleton
    • Sinauer Associates Incorporated
    • Howard, J., Mechanics of Motor Proteins & the Cytoskeleton. 2001, Sinauer Associates Incorporated.
    • (2001)
    • Howard, J.1
  • 40
    • 84979225455 scopus 로고    scopus 로고
    • The physics of pulling polyproteins: a review of single molecule force spectroscopy using the AFM to study protein unfolding
    • Hughes, M.L., Dougan, L., The physics of pulling polyproteins: a review of single molecule force spectroscopy using the AFM to study protein unfolding. Rep. Prog. Phys., 79, 2016, 076601, 10.1088/0034-4885/79/7/076601.
    • (2016) Rep. Prog. Phys. , vol.79 , pp. 076601
    • Hughes, M.L.1    Dougan, L.2
  • 41
    • 36949093311 scopus 로고
    • Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation
    • Huxley, H., Hanson, J., Changes in the cross-striations of muscle during contraction and stretch and their structural interpretation. Nature 173 (1954), 973–976.
    • (1954) Nature , vol.173 , pp. 973-976
    • Huxley, H.1    Hanson, J.2
  • 42
    • 0000219872 scopus 로고
    • Structural changes in muscle during contraction; interference microscopy of living muscle fibres
    • Huxley, A.F., Niedergerke, R., Structural changes in muscle during contraction; interference microscopy of living muscle fibres. Nature 173 (1954), 971–973.
    • (1954) Nature , vol.173 , pp. 971-973
    • Huxley, A.F.1    Niedergerke, R.2
  • 43
    • 84922390086 scopus 로고    scopus 로고
    • Liquid-liquid phase separation in Biology
    • Hyman, A.A., Weber, C.A., Jülicher, F., Liquid-liquid phase separation in Biology. Annu. Rev. Cell Dev. Biol. 30 (2014), 39–58, 10.1146/annurev-cellbio-100913-013325.
    • (2014) Annu. Rev. Cell Dev. Biol. , vol.30 , pp. 39-58
    • Hyman, A.A.1    Weber, C.A.2    Jülicher, F.3
  • 45
    • 84930944871 scopus 로고    scopus 로고
    • Mechanisms of myoblast fusion during muscle development
    • Kim, J.H., Jin, P., Duan, R., Chen, E.H., Mechanisms of myoblast fusion during muscle development. Curr. Opin. Genet. Dev. 32 (2015), 162–170, 10.1016/j.gde.2015.03.006.
    • (2015) Curr. Opin. Genet. Dev. , vol.32 , pp. 162-170
    • Kim, J.H.1    Jin, P.2    Duan, R.3    Chen, E.H.4
  • 48
    • 0028824480 scopus 로고
    • Titins: giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit, S., Kolmerer, B., Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270 (1995), 293–296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 49
    • 30444458378 scopus 로고    scopus 로고
    • From A to Z and back? Multicompartment proteins in the sarcomere
    • Lange, S., Ehler, E., Gautel, M., From A to Z and back? Multicompartment proteins in the sarcomere. Trends Cell Biol. 16 (2006), 11–18.
    • (2006) Trends Cell Biol. , vol.16 , pp. 11-18
    • Lange, S.1    Ehler, E.2    Gautel, M.3
  • 51
    • 80054019905 scopus 로고    scopus 로고
    • Force generation, transmission, and integration during cell and tissue morphogenesis
    • Lecuit, T., Lenne, P.-F., Munro, E., Force generation, transmission, and integration during cell and tissue morphogenesis. Annu. Rev. Cell Dev. Biol. 27 (2011), 157–184, 10.1146/annurev-cellbio-100109-104027.
    • (2011) Annu. Rev. Cell Dev. Biol. , vol.27 , pp. 157-184
    • Lecuit, T.1    Lenne, P.-F.2    Munro, E.3
  • 53
    • 61449220945 scopus 로고    scopus 로고
    • Genetic and cell biological analysis of integrin outside-in signaling
    • Legate, K.R., Wickström, S.A., Fässler, R., Genetic and cell biological analysis of integrin outside-in signaling. Genes Dev. 23 (2009), 397–418, 10.1101/gad.1758709.
    • (2009) Genes Dev. , vol.23 , pp. 397-418
    • Legate, K.R.1    Wickström, S.A.2    Fässler, R.3
  • 54
    • 0031128293 scopus 로고    scopus 로고
    • The changes in power requirements and muscle efficiency during elevated force production in the fruit fly Drosophila melanogaster
    • Lehmann, F.-O., Dickinson, M.H., The changes in power requirements and muscle efficiency during elevated force production in the fruit fly Drosophila melanogaster. J. Exp. Biol. 200 (1997), 1133–1143.
    • (1997) J. Exp. Biol. , vol.200 , pp. 1133-1143
    • Lehmann, F.-O.1    Dickinson, M.H.2
  • 55
    • 0024965992 scopus 로고
    • The function of PS integrins during Drosophila embryogenesis
    • Leptin, M., Bogaert, T., Lehmann, R., Wilcox, M., The function of PS integrins during Drosophila embryogenesis. Cell 56 (1989), 401–408.
    • (1989) Cell , vol.56 , pp. 401-408
    • Leptin, M.1    Bogaert, T.2    Lehmann, R.3    Wilcox, M.4
  • 57
    • 56549096503 scopus 로고    scopus 로고
    • A novel functional assessment of the differentiation of micropatterned muscle cells
    • Li, B., Lin, M., Tang, Y., Wang, B., Wang, J.H.C., A novel functional assessment of the differentiation of micropatterned muscle cells. J. Biomech. 41 (2008), 3349–3353, 10.1016/j.jbiomech.2008.09.025.
    • (2008) J. Biomech. , vol.41 , pp. 3349-3353
    • Li, B.1    Lin, M.2    Tang, Y.3    Wang, B.4    Wang, J.H.C.5
  • 59
    • 0033538859 scopus 로고    scopus 로고
    • I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure
    • Linke, W.A., Rudy, D.E., Centner, T., Gautel, M., Witt, C., Labeit, S., Gregorio, C.C., I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure. J. Cell Biol. 146 (1999), 631–644.
    • (1999) J. Cell Biol. , vol.146 , pp. 631-644
    • Linke, W.A.1    Rudy, D.E.2    Centner, T.3    Gautel, M.4    Witt, C.5    Labeit, S.6    Gregorio, C.C.7
  • 61
    • 49649100130 scopus 로고    scopus 로고
    • Minimally invasive high-speed imaging of sarcomere contractile dynamics in mice and humans
    • Llewellyn, M., Barretto, R., Delp, S., Schnitzer, M., Minimally invasive high-speed imaging of sarcomere contractile dynamics in mice and humans. Nature 454 (2008), 784–788.
    • (2008) Nature , vol.454 , pp. 784-788
    • Llewellyn, M.1    Barretto, R.2    Delp, S.3    Schnitzer, M.4
  • 62
    • 0022402720 scopus 로고
    • Myofibrils bear most of the resting tension in frog skeletal muscle
    • Magid, A., Law, D.J., Myofibrils bear most of the resting tension in frog skeletal muscle. Science 230 (1985), 1280–1282, 10.1126/science.4071053.
    • (1985) Science , vol.230 , pp. 1280-1282
    • Magid, A.1    Law, D.J.2
  • 63
    • 0023607765 scopus 로고
    • Role of contraction in the structure and growth of neonatal rat cardiocytes
    • Marino, T.A., Kuseryk, L., Lauva, I.K., Role of contraction in the structure and growth of neonatal rat cardiocytes. Am. J. Phys. 253 (1987), H1391–H1399.
    • (1987) Am. J. Phys. , vol.253 , pp. H1391-H1399
    • Marino, T.A.1    Kuseryk, L.2    Lauva, I.K.3
  • 64
    • 0036558029 scopus 로고    scopus 로고
    • β-Actinin, cap Z, connectin and titin: what's in a name?
    • Maruyama, K., β-Actinin, cap Z, connectin and titin: what's in a name?. Trends Biochem. Sci., 2002.
    • (2002) Trends Biochem. Sci.
    • Maruyama, K.1
  • 65
    • 0017185581 scopus 로고
    • New elastic protein from muscle
    • Maruyama, K., Natori, R., Nonomura, Y., New elastic protein from muscle. Nature 262 (1976), 58–60, 10.1038/262058a0.
    • (1976) Nature , vol.262 , pp. 58-60
    • Maruyama, K.1    Natori, R.2    Nonomura, Y.3
  • 67
    • 0032578901 scopus 로고    scopus 로고
    • Structural basis for activation of the titin kinase domain during myofibrillogenesis
    • Mayans, O., Van der Ven, P.F., Wilm, M., Mues, A., Young, P., Fürst, D.O., Wilmanns, M., Gautel, M., Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature 395 (1998), 863–869, 10.1038/27603.
    • (1998) Nature , vol.395 , pp. 863-869
    • Mayans, O.1    Van der Ven, P.F.2    Wilm, M.3    Mues, A.4    Young, P.5    Fürst, D.O.6    Wilmanns, M.7    Gautel, M.8
  • 68
    • 77957364208 scopus 로고    scopus 로고
    • Anisotropies in cortical tension reveal the physical basis of polarizing cortical flows
    • Mayer, M., Depken, M., Bois, J.S., JUlicher, F., Grill, S.W., Anisotropies in cortical tension reveal the physical basis of polarizing cortical flows. Nature 467 (2010), 617–621, 10.1038/nature09376.
    • (2010) Nature , vol.467 , pp. 617-621
    • Mayer, M.1    Depken, M.2    Bois, J.S.3    JUlicher, F.4    Grill, S.W.5
  • 69
    • 84884243072 scopus 로고    scopus 로고
    • Molecular tension sensors report forces generated by single integrin molecules in living cells
    • Morimatsu, M., Mekhdjian, A.H., Adhikari, A.S., Dunn, A.R., Molecular tension sensors report forces generated by single integrin molecules in living cells. Nano Lett. 13 (2013), 3985–3989, 10.1021/nl4005145.
    • (2013) Nano Lett. , vol.13 , pp. 3985-3989
    • Morimatsu, M.1    Mekhdjian, A.H.2    Adhikari, A.S.3    Dunn, A.R.4
  • 70
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser, M., Legate, K.R., Zent, R., Fassler, R., The tail of integrins, talin, and kindlins. Science 324 (2009), 895–899, 10.1126/science.1163865.
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4
  • 71
    • 0037237653 scopus 로고    scopus 로고
    • Dilated cardiomyopathy: a disease of the intercalated disc?
    • Perriard, J.-C., Hirschy, A., Ehler, E., Dilated cardiomyopathy: a disease of the intercalated disc?. Trends Cardiovasc. Med. 13 (2003), 30–38, 10.1016/S1050-1738(02)00209-8.
    • (2003) Trends Cardiovasc. Med. , vol.13 , pp. 30-38
    • Perriard, J.-C.1    Hirschy, A.2    Ehler, E.3
  • 74
    • 78650821701 scopus 로고    scopus 로고
    • Nature09566
    • Rauzi, M., Lenne, P.-F., Lecuit, T., Nature09566. Nature 468 (2010), 1110–1114, 10.1038/nature09566.
    • (2010) Nature , vol.468 , pp. 1110-1114
    • Rauzi, M.1    Lenne, P.-F.2    Lecuit, T.3
  • 75
    • 83255181634 scopus 로고    scopus 로고
    • Psoas muscle architectural design, in vivo sarcomere length range, and passive tensile properties support its role as a lumbar spine stabilizer
    • Regev, G.J., Kim, C.W., Tomiya, A., Lee, Y.P., Ghofrani, H., Garfin, S.R., Lieber, R.L., Ward, S.R., Psoas muscle architectural design, in vivo sarcomere length range, and passive tensile properties support its role as a lumbar spine stabilizer. Spine 36 (2011), E1666–E1674, 10.1097/BRS.0b013e31821847b3.
    • (2011) Spine , vol.36 , pp. E1666-E1674
    • Regev, G.J.1    Kim, C.W.2    Tomiya, A.3    Lee, Y.P.4    Ghofrani, H.5    Garfin, S.R.6    Lieber, R.L.7    Ward, S.R.8
  • 76
    • 0028278854 scopus 로고
    • The premyofibril: evidence for its role in myofibrillogenesis
    • Rhee, D., Sanger, J.M., Sanger, J.W., The premyofibril: evidence for its role in myofibrillogenesis. Cell Motil. Cytoskeleton 28 (1994), 1–24, 10.1002/cm.970280102.
    • (1994) Cell Motil. Cytoskeleton , vol.28 , pp. 1-24
    • Rhee, D.1    Sanger, J.M.2    Sanger, J.W.3
  • 77
    • 84958121725 scopus 로고    scopus 로고
    • For whom the cells pull: hydrogel and micropost devices for measuring traction forces
    • Ribeiro, A.J.S., Denisin, A.K., Wilson, R.E., Pruitt, B.L., For whom the cells pull: hydrogel and micropost devices for measuring traction forces. Methods 94 (2016), 51–64, 10.1016/j.ymeth.2015.08.005.
    • (2016) Methods , vol.94 , pp. 51-64
    • Ribeiro, A.J.S.1    Denisin, A.K.2    Wilson, R.E.3    Pruitt, B.L.4
  • 78
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief, M., Gautel, M., Oesterhelt, F., Fernandez, J.M., Gaub, H.E., Reversible unfolding of individual titin immunoglobulin domains by AFM. Science 276 (1997), 1109–1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 79
    • 77951213472 scopus 로고    scopus 로고
    • Myoblast fusion: when it takes more to make one
    • Rochlin, K., Yu, S., Roy, S., Baylies, M., Myoblast fusion: when it takes more to make one. Dev. Biol. 341 (2010), 66–83.
    • (2010) Dev. Biol. , vol.341 , pp. 66-83
    • Rochlin, K.1    Yu, S.2    Roy, S.3    Baylies, M.4
  • 80
    • 78649708350 scopus 로고    scopus 로고
    • Sarcomere formation occurs by the assembly of multiple latent protein complexes
    • Rui, Y., Bai, J., Perrimon, N., Sarcomere formation occurs by the assembly of multiple latent protein complexes. PLoS Genet., 6, 2010, e1001208, 10.1371/journal.pgen.1001208.
    • (2010) PLoS Genet. , vol.6
    • Rui, Y.1    Bai, J.2    Perrimon, N.3
  • 82
    • 80054760368 scopus 로고    scopus 로고
    • Fiber types in mammalian skeletal muscles
    • Schiaffino, S., Reggiani, C., Fiber types in mammalian skeletal muscles. Physiol. Rev. 91 (2011), 1447–1531, 10.1152/physrev.00031.2010.
    • (2011) Physiol. Rev. , vol.91 , pp. 1447-1531
    • Schiaffino, S.1    Reggiani, C.2
  • 83
    • 4344573300 scopus 로고    scopus 로고
    • Muscle building mechanisms of myotube guidance and attachment site selection
    • Schnorrer, F., Dickson, B., Muscle building mechanisms of myotube guidance and attachment site selection. Dev. Cell 7 (2004), 9–20.
    • (2004) Dev. Cell , vol.7 , pp. 9-20
    • Schnorrer, F.1    Dickson, B.2
  • 84
    • 34247605961 scopus 로고    scopus 로고
    • The transmembrane protein Kon-tiki couples to Dgrip to mediate myotube targeting in Drosophila
    • Schnorrer, F., Kalchhauser, I., Dickson, B., The transmembrane protein Kon-tiki couples to Dgrip to mediate myotube targeting in Drosophila. Dev. Cell 12 (2007), 751–766.
    • (2007) Dev. Cell , vol.12 , pp. 751-766
    • Schnorrer, F.1    Kalchhauser, I.2    Dickson, B.3
  • 86
    • 81555220111 scopus 로고    scopus 로고
    • Spalt mediates an evolutionarily conserved switch to fibrillar muscle fate in insects
    • Schönbauer, C., Distler, J., Jährling, N., Radolf, M., Dodt, H.-U., Frasch, M., Schnorrer, F., Spalt mediates an evolutionarily conserved switch to fibrillar muscle fate in insects. Nature 479 (2011), 406–409, 10.1038/nature10559.
    • (2011) Nature , vol.479 , pp. 406-409
    • Schönbauer, C.1    Distler, J.2    Jährling, N.3    Radolf, M.4    Dodt, H.-U.5    Frasch, M.6    Schnorrer, F.7
  • 89
    • 77956218581 scopus 로고    scopus 로고
    • Connecting muscles to tendons: tendons and musculoskeletal development in flies and vertebrates
    • Schweitzer, R., Zelzer, E., Volk, T., Connecting muscles to tendons: tendons and musculoskeletal development in flies and vertebrates. Development 137 (2010), 2807–2817, 10.1242/dev.047498.
    • (2010) Development , vol.137 , pp. 2807-2817
    • Schweitzer, R.1    Zelzer, E.2    Volk, T.3
  • 90
    • 79959644058 scopus 로고    scopus 로고
    • Insights into the Micromechanical Properties of the Metaphase Spindle
    • Shimamoto, Y., Maeda, Y.T., Ishiwata, S., Libchaber, A.J., Kapoor, T.M., Insights into the Micromechanical Properties of the Metaphase Spindle. Cell 145 (2011), 1062–1074, 10.1016/j.cell.2011.05.038.
    • (2011) Cell , vol.145 , pp. 1062-1074
    • Shimamoto, Y.1    Maeda, Y.T.2    Ishiwata, S.3    Libchaber, A.J.4    Kapoor, T.M.5
  • 91
    • 62849125813 scopus 로고    scopus 로고
    • The initial steps of myofibril assembly: integrins pave the way
    • Sparrow, J., Schöck, F., The initial steps of myofibril assembly: integrins pave the way. Nat. Rev. Mol. Cell Biol. 10 (2009), 293–298.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 293-298
    • Sparrow, J.1    Schöck, F.2
  • 92
    • 84892534936 scopus 로고    scopus 로고
    • Transcriptional regulation and alternative splicing cooperate in muscle fiber-type specification in flies and mammals
    • Spletter, M.L., Schnorrer, F., Transcriptional regulation and alternative splicing cooperate in muscle fiber-type specification in flies and mammals. Exp. Cell Res. 321 (2014), 90–98, 10.1016/j.yexcr.2013.10.007.
    • (2014) Exp. Cell Res. , vol.321 , pp. 90-98
    • Spletter, M.L.1    Schnorrer, F.2
  • 94
    • 2942679778 scopus 로고    scopus 로고
    • The early history of the biochemistry of muscle contraction
    • Szent-Györgyi, A.G., The early history of the biochemistry of muscle contraction. J. Gen. Physiol. 123 (2004), 631–641, 10.1085/jgp.200409091.
    • (2004) J. Gen. Physiol. , vol.123 , pp. 631-641
    • Szent-Györgyi, A.G.1
  • 95
    • 0042839620 scopus 로고    scopus 로고
    • Titin: properties and family relationships
    • Tskhovrebova, L., Trinick, J., Titin: properties and family relationships. Nat. Rev. Mol. Cell Biol. 4 (2003), 679–689, 10.1038/nrm1198.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 679-689
    • Tskhovrebova, L.1    Trinick, J.2
  • 97
    • 84959864235 scopus 로고    scopus 로고
    • IPP complex reinforces adhesion by relaying tension-dependent signals to inhibit integrin turnover
    • Vakaloglou, K.M., Chrysanthis, G., Zervas, C.G., IPP complex reinforces adhesion by relaying tension-dependent signals to inhibit integrin turnover. Cell Rep. 14 (2016), 2668–2682, 10.1016/j.celrep.2016.02.052.
    • (2016) Cell Rep. , vol.14 , pp. 2668-2682
    • Vakaloglou, K.M.1    Chrysanthis, G.2    Zervas, C.G.3
  • 99
    • 60849104490 scopus 로고    scopus 로고
    • Molecular Basis of Muscle Structure, in: Muscle Development in Drosophila, Molecular Biology Intelligence Unit
    • Springer New York, New York, NY
    • Vigoreaux, J.O., Molecular Basis of Muscle Structure, in: Muscle Development in Drosophila, Molecular Biology Intelligence Unit. 2006, Springer, New York, New York, NY, 143–156, 10.1007/0-387-32963-3_12.
    • (2006) , pp. 143-156
    • Vigoreaux, J.O.1
  • 100
    • 65949114647 scopus 로고    scopus 로고
    • Self-organization of dynein motors generates meiotic nuclear oscillations
    • Vogel, S.K., Pavin, N., Maghelli, N., JUlicher, F., Tolić-Nørrelykke, I.M., Self-organization of dynein motors generates meiotic nuclear oscillations. PLoS Biol., 7, 2009, e1000087, 10.1371/journal.pbio.1000087.
    • (2009) PLoS Biol. , vol.7
    • Vogel, S.K.1    Pavin, N.2    Maghelli, N.3    JUlicher, F.4    Tolić-Nørrelykke, I.M.5
  • 101
    • 84898059200 scopus 로고    scopus 로고
    • Tension and force-resistant attachment are essential for myofibrillogenesis in Drosophila flight muscle
    • Weitkunat, M., Kaya-Copur, A., Grill, S.W., Schnorrer, F., Tension and force-resistant attachment are essential for myofibrillogenesis in Drosophila flight muscle. Curr. Biol. 24 (2014), 705–716, 10.1016/j.cub.2014.02.032.
    • (2014) Curr. Biol. , vol.24 , pp. 705-716
    • Weitkunat, M.1    Kaya-Copur, A.2    Grill, S.W.3    Schnorrer, F.4
  • 102
    • 84906088520 scopus 로고    scopus 로고
    • Localization of sarcomeric proteins during myofibril assembly in cultured mouse primary skeletal myotubes
    • White, J., Barro, M.V., Makarenkova, H.P., Sanger, J.W., Sanger, J.M., Localization of sarcomeric proteins during myofibril assembly in cultured mouse primary skeletal myotubes. Anat. Rec. 297 (2014), 1571–1584, 10.1002/ar.22981.
    • (2014) Anat. Rec. , vol.297 , pp. 1571-1584
    • White, J.1    Barro, M.V.2    Makarenkova, H.P.3    Sanger, J.W.4    Sanger, J.M.5
  • 103
    • 0028089203 scopus 로고
    • Genes critical for muscle development and function in Caenorhabditis elegans identified through lethal mutations
    • Williams, B.D., Waterston, R.H., Genes critical for muscle development and function in Caenorhabditis elegans identified through lethal mutations. J. Cell Biol. 124 (1994), 475–490.
    • (1994) J. Cell Biol. , vol.124 , pp. 475-490
    • Williams, B.D.1    Waterston, R.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.