메뉴 건너뛰기




Volumn 125, Issue 8, 2012, Pages 1855-1864

Actin stress fibers - Assembly, dynamics and biological roles

Author keywords

Actin; Adhesion; Assembly; Mechanotransduction; Stress fibers

Indexed keywords

ACTIN; ALPHA ACTININ; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN PHOSPHATASE;

EID: 84863113109     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.098087     Document Type: Article
Times cited : (677)

References (154)
  • 1
    • 0029015719 scopus 로고
    • Formation of stable microspikes containing actin and the 55 kDa actin bundling protein, fascin, is a consequence of cell adhesion to thrombospondin-1: implications for the anti-adhesive activities of thrombospondin-1
    • Adams, J. C. (1995). Formation of stable microspikes containing actin and the 55 kDa actin bundling protein, fascin, is a consequence of cell adhesion to thrombospondin-1: implications for the anti-adhesive activities of thrombospondin-1. J. Cell Sci. 108, 1977-1990.
    • (1995) J. Cell Sci. , vol.108 , pp. 1977-1990
    • Adams, J.C.1
  • 3
    • 58149300219 scopus 로고    scopus 로고
    • Retrograde flow and myosin II activity within the leading cell edge deliver F-actin to the lamella to seed the formation of graded polarity actomyosin II filament bundles in migrating fibroblasts
    • Anderson, T. W., Vaughan, A. N. and Cramer, L. P. (2008). Retrograde flow and myosin II activity within the leading cell edge deliver F-actin to the lamella to seed the formation of graded polarity actomyosin II filament bundles in migrating fibroblasts. Mol. Biol. Cell. 19, 5006-5018
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 5006-5018
    • Anderson, T.W.1    Vaughan, A.N.2    Cramer, L.P.3
  • 6
    • 21244469821 scopus 로고    scopus 로고
    • Vertebrate nonmuscle myosin II isoforms rescue small interfering RNA-induced defects in COS-7 cell cytokinesis
    • Bao, J., Jana, S. S. and Adelstein, R. S. (2005). Vertebrate nonmuscle myosin II isoforms rescue small interfering RNA-induced defects in COS-7 cell cytokinesis. J. Biol. Chem. 280, 19594-19599.
    • (2005) J. Biol. Chem. , vol.280 , pp. 19594-19599
    • Bao, J.1    Jana, S.S.2    Adelstein, R.S.3
  • 10
    • 0025613855 scopus 로고
    • Tropomyosin prevents depolymerization of actin filaments from the pointed end
    • Broschat, K. O. (1990). Tropomyosin prevents depolymerization of actin filaments from the pointed end. J. Biol. Chem. 265, 21323-21329.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21323-21329
    • Broschat, K.O.1
  • 11
    • 0018247351 scopus 로고
    • The gelation of actin by actinbinding protein
    • Brotschi, E. A., Hartwig, J. H. and Stossel, T. P. (1978). The gelation of actin by actinbinding protein. J. Biol. Chem. 253, 8988-8993.
    • (1978) J. Biol. Chem. , vol.253 , pp. 8988-8993
    • Brotschi, E.A.1    Hartwig, J.H.2    Stossel, T.P.3
  • 12
    • 77952896939 scopus 로고    scopus 로고
    • Control of actin filament treadmilling in cell motility
    • Bugyi, B. and Carlier, M. F. (2010). Control of actin filament treadmilling in cell motility. Annu. Rev. Biophys. 39, 449-470.
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 449-470
    • Bugyi, B.1    Carlier, M.F.2
  • 14
    • 0024150623 scopus 로고
    • Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., Fath, K., Kelly, T., Nuckolls, G. and Turner, C. (1988). Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4, 487-525.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 15
    • 77952335298 scopus 로고    scopus 로고
    • A new lock-step mechanism of matrix remodelling based on subcellular contractile events
    • Castella, L. F., Buscemi, L., Godbout, C., Meister, J. J. and Hinz, B. (2010). A new lock-step mechanism of matrix remodelling based on subcellular contractile events..J. Cell Sci. 123, 1751-1760.
    • (2010) J. Cell Sci. , vol.123 , pp. 1751-1760
    • Castella, L.F.1    Buscemi, L.2    Godbout, C.3    Meister, J.J.4    Hinz, B.5
  • 16
    • 0028877070 scopus 로고
    • Essential role of caldesmon in the actin filament reorganization induced by glucocorticoids
    • Castellino, F., Ono, S., Matsumura, F. and Luini, A. (1995). Essential role of caldesmon in the actin filament reorganization induced by glucocorticoids. J. Cell Biol. 131, 1223-1230.
    • (1995) J. Cell Biol. , vol.131 , pp. 1223-1230
    • Castellino, F.1    Ono, S.2    Matsumura, F.3    Luini, A.4
  • 17
    • 0019721193 scopus 로고
    • Mechanism of retraction of the trailing edge during fibroblast movement
    • Chen, W. T. (1981). Mechanism of retraction of the trailing edge during fibroblast movement. J. Cell Biol. 90, 187-200.
    • (1981) J. Cell Biol. , vol.90 , pp. 187-200
    • Chen, W.T.1
  • 18
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M. and Burridge, K. (1996). Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133, 1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 19
    • 77957834345 scopus 로고    scopus 로고
    • Differential regulation of unconventional fission yeast myosins via the actin track
    • Clayton, J. E., Sammons, M. R., Stark, B. C., Hodges, A. R. and Lord, M. (2010). Differential regulation of unconventional fission yeast myosins via the actin track. Curr. Biol. 20, 1423-1431.
    • (2010) Curr. Biol. , vol.20 , pp. 1423-1431
    • Clayton, J.E.1    Sammons, M.R.2    Stark, B.C.3    Hodges, A.R.4    Lord, M.5
  • 21
    • 0030864069 scopus 로고    scopus 로고
    • Identification of novel graded polarity actin filament bundles in locomoting heart fibroblasts: implications for the generation of motile force
    • Cramer, L. P., Siebert, M. and Mitchison, T. J. (1997). Identification of novel graded polarity actin filament bundles in locomoting heart fibroblasts: implications for the generation of motile force. J. Cell Biol. 136, 1287-1305.
    • (1997) J. Cell Biol. , vol.136 , pp. 1287-1305
    • Cramer, L.P.1    Siebert, M.2    Mitchison, T.J.3
  • 22
    • 0033693870 scopus 로고    scopus 로고
    • Live dynamics of GFP-calponin: isoformspecific modulation of the actin cytoskeleton and autoregulation by C-terminal sequences
    • Danninger, C. and Gimona, M. (2000). Live dynamics of GFP-calponin: isoformspecific modulation of the actin cytoskeleton and autoregulation by C-terminal sequences. J. Cell Sci. 21, 3725-3736.
    • (2000) J. Cell Sci. , vol.21 , pp. 3725-3736
    • Danninger, C.1    Gimona, M.2
  • 24
    • 0036912348 scopus 로고    scopus 로고
    • Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the leading edge
    • DesMarais, V., Ichetovkin, I., Condeelis, J. and Hitchcock-DeGregori, S. E. (2002). Spatial regulation of actin dynamics: a tropomyosin-free, actin-rich compartment at the leading edge. J. Cell Sci. 115, 4649-4660.
    • (2002) J. Cell Sci. , vol.115 , pp. 4649-4660
    • DesMarais, V.1    Ichetovkin, I.2    Condeelis, J.3    Hitchcock-DeGregori, S.E.4
  • 25
    • 27944497333 scopus 로고    scopus 로고
    • Tissue cells feel and respond to the stiffness of their substrate
    • Discher, D. E., Janmey, P. and Wang, Y.-L. (2005). Tissue cells feel and respond to the stiffness of their substrate. Science 310, 1139-1143.
    • (2005) Science , vol.310 , pp. 1139-1143
    • Discher, D.E.1    Janmey, P.2    Wang, Y.-L.3
  • 26
    • 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
  • 27
    • 0025900403 scopus 로고
    • Calponin. Developmental isoforms and a low molecular weight variant
    • Draeger, A., Gimona, M., Stuckert, A., Celis, J. E. and Small, J. V. (1991). Calponin. Developmental isoforms and a low molecular weight variant. FEBS Lett. 291, 24-28.
    • (1991) FEBS Lett , vol.291 , pp. 24-28
    • Draeger, A.1    Gimona, M.2    Stuckert, A.3    Celis, J.E.4    Small, J.V.5
  • 28
    • 80054043810 scopus 로고    scopus 로고
    • Mechanical strain in actin networks regulates FilGAP and integrin binding to filamin A
    • Ehrlicher, A. J., Nakamura, F., Hartwig, J. H., Weitz, D. A. and Stossel, T. P. (2011). Mechanical strain in actin networks regulates FilGAP and integrin binding to filamin A. Nature. 478, 260-263.
    • (2011) Nature , vol.478 , pp. 260-263
    • Ehrlicher, A.J.1    Nakamura, F.2    Hartwig, J.H.3    Weitz, D.A.4    Stossel, T.P.5
  • 30
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • Engler, A. J., Sen, S., Sweeney, H. L. and Discher, D. E. (2006). Matrix elasticity directs stem cell lineage specification. Cell 126, 677-689.
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 31
    • 77951191158 scopus 로고    scopus 로고
    • The small GTPase Rif is an alternative trigger for the formation of actin stress fibers in epithelial cells
    • Fan, L., Pellegrin, S., Scott, A. and Mellor, H. (2010). The small GTPase Rif is an alternative trigger for the formation of actin stress fibers in epithelial cells. J. Cell Sci. 123, 1247-1252.
    • (2010) J. Cell Sci. , vol.123 , pp. 1247-1252
    • Fan, L.1    Pellegrin, S.2    Scott, A.3    Mellor, H.4
  • 32
    • 59549090911 scopus 로고    scopus 로고
    • Local Cortical Tension by Myosin II Guides 3D Endothelial Cell Branching
    • Fischer, R. S., Gardel, M., Ma, X., Adelstein, R. S. and Waterman, C. M. (2009). Local Cortical Tension by Myosin II Guides 3D Endothelial Cell Branching. Curr. Biol. 19, 260-265.
    • (2009) Curr. Biol. , vol.19 , pp. 260-265
    • Fischer, R.S.1    Gardel, M.2    Ma, X.3    Adelstein, R.S.4    Waterman, C.M.5
  • 33
    • 58249086114 scopus 로고    scopus 로고
    • Traction stress in focal adhesions correlates biphasically with actin retrograde flow speed
    • Gardel, M. L., Sabass, B., Ji, L., Danuser, G., Schwarz, U. S. and Waterman, C. M. (2008). Traction stress in focal adhesions correlates biphasically with actin retrograde flow speed. J. Cell Biol. 183, 999-1005.
    • (2008) J. Cell Biol. , vol.183 , pp. 999-1005
    • Gardel, M.L.1    Sabass, B.2    Ji, L.3    Danuser, G.4    Schwarz, U.S.5    Waterman, C.M.6
  • 37
    • 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
  • 38
    • 60849088625 scopus 로고    scopus 로고
    • Emerging issues for tropomyosin structure, regulation, function and pathology
    • Gunning, P. (2008). Emerging issues for tropomyosin structure, regulation, function and pathology. Adv. Exp. Med. Biol. 644, 293-298.
    • (2008) Adv. Exp. Med. Biol. , vol.644 , pp. 293-298
    • Gunning, P.1
  • 40
    • 0025974302 scopus 로고
    • Chicken cardiac myofibrillogenesis studied with antibodies specific for titin and the muscle and nonmuscle isoforms of actin and tropomyosin
    • Handel, S. E., Greaser, M. L., Schultz, E., Wang, S. M., Bulinski, J. C., Lin, J. J. and Lessard, J. L. (1991). Chicken cardiac myofibrillogenesis studied with antibodies specific for titin and the muscle and nonmuscle isoforms of actin and tropomyosin. Cell Tissue Res. 263, 419-430.
    • (1991) Cell Tissue Res , vol.263 , pp. 419-430
    • Handel, S.E.1    Greaser, M.L.2    Schultz, E.3    Wang, S.M.4    Bulinski, J.C.5    Lin, J.J.6    Lessard, J.L.7
  • 41
    • 80955177507 scopus 로고    scopus 로고
    • The roles of fascins in health and disease
    • Hashimoto, Y., Kim, D. J. and Adams, J. C. (2011). The roles of fascins in health and disease. J. Pathol. 224, 289-300.
    • (2011) J. Pathol. , vol.224 , pp. 289-300
    • Hashimoto, Y.1    Kim, D.J.2    Adams, J.C.3
  • 42
    • 40949165235 scopus 로고    scopus 로고
    • Actin stress fibers transmit and focus force to activate mechanosensitive channels
    • Hayakawa, K., Tatsumi, H. and Sokabe, M. (2008). Actin stress fibers transmit and focus force to activate mechanosensitive channels. J. Cell Sci. 121, 496-503.
    • (2008) J. Cell Sci. , vol.121 , pp. 496-503
    • Hayakawa, K.1    Tatsumi, H.2    Sokabe, M.3
  • 43
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies
    • Heasman, S. J. and Ridley, A. J. (2008). Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat. Rev. Mol. Cell Biol. 9, 690-701.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 44
    • 0020730448 scopus 로고
    • Behaviour and structure of the leading lamella in moving fibroblasts I. Occurrence and centripetal movement of arc-shaped microfilament bundles beneath the dorsal cell surface
    • Heath, J. P. (1983). Behaviour and structure of the leading lamella in moving fibroblasts. I. Occurrence and centripetal movement of arc-shaped microfilament bundles beneath the dorsal cell surface. J. Cell Sci. 60, 331-354.
    • (1983) J. Cell Sci. , vol.60 , pp. 331-354
    • Heath, J.P.1
  • 46
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF
    • Hill, C. S., Wynne, J. and Treisman, R. (1995). The Rho family GTPases RhoA, Rac1, and CDC42Hs regulate transcriptional activation by SRF. Cell. 81, 1159-1170.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 47
    • 0037070964 scopus 로고    scopus 로고
    • The NH2-terminal peptide of alpha-smooth muscle actin inhibits force generation by the myofibroblast in vitro and in vivo
    • Hinz, B., Gabbiani, G. and Chaponnier, C. (2002). The NH2-terminal peptide of alpha-smooth muscle actin inhibits force generation by the myofibroblast in vitro and in vivo. J. Cell Biol. 157, 657-663.
    • (2002) J. Cell Biol. , vol.157 , pp. 657-663
    • Hinz, B.1    Gabbiani, G.2    Chaponnier, C.3
  • 48
    • 53349090308 scopus 로고    scopus 로고
    • Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner
    • Hirata, H., Tatsumi, H. and Sokabe, M. (2008). Mechanical forces facilitate actin polymerization at focal adhesions in a zyxin-dependent manner. J. Cell Sci. 121, 2795-2804.
    • (2008) J. Cell Sci. , vol.121 , pp. 2795-2804
    • Hirata, H.1    Tatsumi, H.2    Sokabe, M.3
  • 50
    • 0037213601 scopus 로고    scopus 로고
    • Developmentally regulated expression of calponin isoforms and the effect of h2-calponin on cell proliferation
    • Hossain, M. M., Hwang, D. Y., Huang, Q. Q., Sasaki, Y. and Jin, J. P. (2003). Developmentally regulated expression of calponin isoforms and the effect of h2- calponin on cell proliferation. Am. J. Physiol Cell Physiol. 284, C156-C167.
    • (2003) Am. J. Physiol Cell Physiol. , vol.284
    • Hossain, M.M.1    Hwang, D.Y.2    Huang, Q.Q.3    Sasaki, Y.4    Jin, J.P.5
  • 51
    • 33646386142 scopus 로고    scopus 로고
    • Stress fibers are generated by two distinct actin assembly mechanisms in motile cells
    • Hotulainen, P. and Lappalainen, P. (2006). Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J. Cell Biol. 173, 383-394.
    • (2006) J. Cell Biol. , vol.173 , pp. 383-394
    • Hotulainen, P.1    Lappalainen, P.2
  • 52
    • 70849133453 scopus 로고    scopus 로고
    • Expression of chick Coactosin in cells in morphogenetic movement
    • Hou, X., Katahira, T., Kimura, J. and Nakamura, H. (2009). Expression of chick Coactosin in cells in morphogenetic movement. Dev. Growth Differ. 51, 833-840.
    • (2009) Dev. Growth Differ. , vol.51 , pp. 833-840
    • Hou, X.1    Katahira, T.2    Kimura, J.3    Nakamura, H.4
  • 53
    • 33846697554 scopus 로고    scopus 로고
    • Differential transmission of actin motion within focal adhesions
    • Hu, K., Ji, L., Applegate, K. T., Danuser, G. and Waterman-Storer, C. M. (2007). Differential transmission of actin motion within focal adhesions. Science. 315, 111-115.
    • (2007) Science , vol.315 , pp. 111-115
    • Hu, K.1    Ji, L.2    Applegate, K.T.3    Danuser, G.4    Waterman-Storer, C.M.5
  • 54
    • 0024565757 scopus 로고
    • Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin Potentiation of protective ability of tropomyosins by 83-kDa nonmuscle caldesmon
    • Ishikawa, R., Yamashiro, S. and Matsumura, F. (1989a). Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83-kDa nonmuscle caldesmon. J. Biol. Chem. 264, 7490-7497.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7490-7497
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 55
    • 0024432710 scopus 로고
    • Annealing of gelsolinsevered actin fragments by tropomyosin in the presence of Ca2+ Potentiation of the annealing process by caldesmon
    • Ishikawa, R., Yamashiro, S. and Matsumura, F. (1989b). Annealing of gelsolinsevered actin fragments by tropomyosin in the presence of Ca2+. Potentiation of the annealing process by caldesmon. J. Biol. Chem. 264, 16764-16770.
    • (1989) J. Biol. Chem. , vol.264 , pp. 16764-16770
    • Ishikawa, R.1    Yamashiro, S.2    Matsumura, F.3
  • 58
    • 35548961325 scopus 로고    scopus 로고
    • Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases
    • Joo, E., Surka, M. C. and Trimble, W. S. (2007). Mammalian SEPT2 is required for scaffolding nonmuscle myosin II and its kinases. Dev. Cell. 13, 677-690.
    • (2007) Dev. Cell. , vol.13 , pp. 677-690
    • Joo, E.1    Surka, M.C.2    Trimble, W.S.3
  • 60
    • 33745767358 scopus 로고    scopus 로고
    • Harnessing actin dynamics for clathrin-mediated endocytosis
    • Kaksonen, M., Toret, C. P. and Drubin, D. G. (2006). Harnessing actin dynamics for clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 7, 404-414.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 404-414
    • Kaksonen, M.1    Toret, C.P.2    Drubin, D.G.3
  • 62
    • 0028898501 scopus 로고
    • Effect of caldesmon on the assembly of smooth muscle myosin
    • Katayama, E., Scott-Woo, G. and Ikebe, M. (1995). Effect of caldesmon on the assembly of smooth muscle myosin. J. Biol. Chem. 270, 3919-3925.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3919-3925
    • Katayama, E.1    Scott-Woo, G.2    Ikebe, M.3
  • 64
    • 0034984503 scopus 로고    scopus 로고
    • Stress fiber organization regulated by MLCK and Rho-kinase in cultured human fibroblasts
    • Katoh, K., Kano, Y., Amano, M., Kaibuchi, K. and Fujiwara, K. (2001b). Stress fiber organization regulated by MLCK and Rho-kinase in cultured human fibroblasts. Am J. Physiol Cell Physiol. 280, C1669-C1679.
    • (2001) Am J. Physiol Cell Physiol. , vol.280
    • Katoh, K.1    Kano, Y.2    Amano, M.3    Kaibuchi, K.4    Fujiwara, K.5
  • 69
    • 14244260907 scopus 로고    scopus 로고
    • p116Rip decreases myosin II phosphorylation by activating myosin light chain phosphatase and by inactivating RhoA
    • Koga, Y. and Ikebe, M. (2005). p116Rip decreases myosin II phosphorylation by activating myosin light chain phosphatase and by inactivating RhoA. J. Biol. Chem. 280, 4983-4991.
    • (2005) J. Biol. Chem. , vol.280 , pp. 4983-4991
    • Koga, Y.1    Ikebe, M.2
  • 70
    • 28344440602 scopus 로고    scopus 로고
    • Phosphorylated lcaldesmon is involved in disassembly of actin stress fibers and postmitotic spreading
    • Kordowska, J., Hetrick, T., Adam, L. P. and Wang, C. L. (2006). Phosphorylated lcaldesmon is involved in disassembly of actin stress fibers and postmitotic spreading. Exp. Cell Res. 312, 95-110.
    • (2006) Exp. Cell Res. , vol.312 , pp. 95-110
    • Kordowska, J.1    Hetrick, T.2    Adam, L.P.3    Wang, C.L.4
  • 71
    • 76549109169 scopus 로고    scopus 로고
    • Nucleocytoplasmic functions of the PDZ-LIM protein family: new insights into organ development
    • Krcmery, J., Camarata, T., Kulisz, A. and Simon, H. G. (2010). Nucleocytoplasmic functions of the PDZ-LIM protein family: new insights into organ development. BioEssays 32, 100-108.
    • (2010) BioEssays , vol.32 , pp. 100-108
    • Krcmery, J.1    Camarata, T.2    Kulisz, A.3    Simon, H.G.4
  • 72
    • 78650457713 scopus 로고    scopus 로고
    • Reducing background fluorescence reveals adhesions in 3D matrices
    • Kubow, K. E. and Horwitz, A. R. (2011). Reducing background fluorescence reveals adhesions in 3D matrices. Nat. Cell Biol. 13, 3-5.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 3-5
    • Kubow, K.E.1    Horwitz, A.R.2
  • 74
    • 0016740549 scopus 로고
    • Tropomyosin antibody: the specific localization of tropomyosin in nonmuscle cells
    • Lazarides, E. (1975). Tropomyosin antibody: the specific localization of tropomyosin in nonmuscle cells. J. Cell Biol. 65, 549-561.
    • (1975) J. Cell Biol. , vol.65 , pp. 549-561
    • Lazarides, E.1
  • 75
    • 0016678780 scopus 로고
    • Alpha-actinin: immunofluorescent localization of a muscle structural protein in nonmuscle cells
    • Lazarides, E. and Burridge, K. (1975). Alpha-actinin: immunofluorescent localization of a muscle structural protein in nonmuscle cells. Cell. 6, 289-298.
    • (1975) Cell , vol.6 , pp. 289-298
    • Lazarides, E.1    Burridge, K.2
  • 76
    • 0033571710 scopus 로고    scopus 로고
    • Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins
    • Leinweber, B. D., Leavis, P. C., Grabarek, Z., Wang, C. L. and Morgan, K. G. (1999a) Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins. Biochem. J. 1, 117-123.
    • (1999) Biochem. J. , vol.1 , pp. 117-123
    • Leinweber, B.D.1    Leavis, P.C.2    Grabarek, Z.3    Wang, C.L.4    Morgan, K.G.5
  • 77
    • 0032786904 scopus 로고    scopus 로고
    • Calponin interaction with alpha-actinin-actin: evidence for a structural role for calponin
    • Leinweber, B., Tang, J. X., Stafford, W. F. and Chalovich, J. M. (1999b) Calponin interaction with alpha-actinin-actin: evidence for a structural role for calponin. Biophys. J. 77, 3208-3217.
    • (1999) Biophys. J. , vol.77 , pp. 3208-3217
    • Leinweber, B.1    Tang, J.X.2    Stafford, W.F.3    Chalovich, J.M.4
  • 78
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung, T., Chen, X. Q., Manser, E. and Lim, L. (1996). The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell Biol. 16, 5313-5327.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 79
    • 77955901384 scopus 로고    scopus 로고
    • Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement
    • Luxton, G. W., Gomes, E. R., Folker, E. S., Vintinner, E. and Gundersen, G. G. (2010). Linear arrays of nuclear envelope proteins harness retrograde actin flow for nuclear movement. Science 329, 956-959.
    • (2010) Science , vol.329 , pp. 956-959
    • Luxton, G.W.1    Gomes, E.R.2    Folker, E.S.3    Vintinner, E.4    Gundersen, G.G.5
  • 81
    • 0026586912 scopus 로고
    • Caldesmon binds to smooth muscle myosin and myosin rod and crosslinks thick filaments to actin filaments
    • Marston, S., Pinter, K. and Bennett, P. (1992). Caldesmon binds to smooth muscle myosin and myosin rod and crosslinks thick filaments to actin filaments. J. Muscle Res. Cell Motil. 13, 206-218.
    • (1992) J. Muscle Res. Cell Motil. , vol.13 , pp. 206-218
    • Marston, S.1    Pinter, K.2    Bennett, P.3
  • 82
    • 79952335646 scopus 로고    scopus 로고
    • Diversification of caldesmon-linked actin cytoskeleton in cell motility
    • Mayanagi, T. and Sobue, K. (2011). Diversification of caldesmon-linked actin cytoskeleton in cell motility. Cell Adh. Migr. 5, 150-159.
    • (2011) Cell Adh. Migr. , vol.5 , pp. 150-159
    • Mayanagi, T.1    Sobue, K.2
  • 83
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament
    • McKillop, D. F. and Geeves, M. A. (1993). Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys J. 65, 693-701.
    • (1993) Biophys J , vol.65 , pp. 693-701
    • McKillop, D.F.1    Geeves, M.A.2
  • 84
    • 33748143309 scopus 로고    scopus 로고
    • Tropomyosin isoforms localize to distinct microfilament populations in osteoclasts
    • McMichael, B. K., Kotadiya, P., Singh, T., Holliday, L. S. and Lee, B. S. (2006). Tropomyosin isoforms localize to distinct microfilament populations in osteoclasts. Bone 39, 694-705
    • (2006) Bone , vol.39 , pp. 694-705
    • McMichael, B.K.1    Kotadiya, P.2    Singh, T.3    Holliday, L.S.4    Lee, B.S.5
  • 85
    • 79960718426 scopus 로고    scopus 로고
    • Building distinct actin filament networks in a common cytoplasm
    • Michelot, A. and Drubin, D. G. (2011). Building distinct actin filament networks in a common cytoplasm. Curr. Biol. 21, R560-R569.
    • (2011) Curr. Biol. , vol.21
    • Michelot, A.1    Drubin, D.G.2
  • 87
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control SRF activity by regulation of its coactivator MAL
    • Miralles, F., Posern, G., Zaromytidou, A. I. and Treisman, R. (2003). Actin dynamics control SRF activity by regulation of its coactivator MAL. Cell 113, 329-342.
    • (2003) Cell , vol.113 , pp. 329-342
    • Miralles, F.1    Posern, G.2    Zaromytidou, A.I.3    Treisman, R.4
  • 88
    • 0030049170 scopus 로고    scopus 로고
    • Actin-Based Cell Motility and Cell Locomotion
    • Mitchison, T. J. and Cramer, L. P. (1996). Actin-Based Cell Motility and Cell Locomotion. Cell 84, 371-379.
    • (1996) Cell , vol.84 , pp. 371-379
    • Mitchison, T.J.1    Cramer, L.P.2
  • 91
    • 82555168182 scopus 로고    scopus 로고
    • Stress fibers stabilize the position of intranuclear DNA through mechanical connection with the nucleus in vascular smooth muscle cells
    • Nagayama, K., Yahiro, Y. and Matsumoto, T. (2011). Stress fibers stabilize the position of intranuclear DNA through mechanical connection with the nucleus in vascular smooth muscle cells. FEBS Lett. 585, 3992-3997.
    • (2011) FEBS Lett , vol.585 , pp. 3992-3997
    • Nagayama, K.1    Yahiro, Y.2    Matsumoto, T.3
  • 92
    • 50649090264 scopus 로고    scopus 로고
    • Mechanisms of actin stress fibre assembly
    • Review
    • Naumanen, P., Lappalainen, P. and Hotulainen, P. (2008). Mechanisms of actin stress fibre assembly. J. Microsc. 231, 446-454. Review.
    • (2008) J. Microsc. , vol.231 , pp. 446-454
    • Naumanen, P.1    Lappalainen, P.2    Hotulainen, P.3
  • 93
    • 41549108457 scopus 로고    scopus 로고
    • Building the actin cytoskeleton: filopodia contribute to the construction of contractile bundles in the lamella
    • Nemethova, M., Auinger, S. and Small, J. V. (2008). Building the actin cytoskeleton: filopodia contribute to the construction of contractile bundles in the lamella. J. Cell Biol. 180, 1233-1244.
    • (2008) J. Cell Biol. , vol.180 , pp. 1233-1244
    • Nemethova, M.1    Auinger, S.2    Small, J.V.3
  • 94
    • 77958521897 scopus 로고    scopus 로고
    • Dynamic regulation of sarcomeric actin filaments in striated muscle
    • (Hoboken)
    • Ono, S. (2010). Dynamic regulation of sarcomeric actin filaments in striated muscle. Cytoskeleton (Hoboken). 67, 677-692.
    • (2010) Cytoskeleton , vol.67 , pp. 677-692
    • Ono, S.1
  • 95
    • 0037128928 scopus 로고    scopus 로고
    • Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics
    • Ono, S. and Ono, K. (2002). Tropomyosin inhibits ADF/cofilin-dependent actin filament dynamics. J. Cell Biol. 156, 1065-1076.
    • (2002) J. Cell Biol. , vol.156 , pp. 1065-1076
    • Ono, S.1    Ono, K.2
  • 97
    • 0034618039 scopus 로고    scopus 로고
    • Characterization of palladin, a novel protein localized to stress fibers and cell adhesions
    • Parast, M. M. and Otey, C. A. (2000). Characterization of palladin, a novel protein localized to stress fibers and cell adhesions. J. Cell Biol. 150, 643-656.
    • (2000) J. Cell Biol. , vol.150 , pp. 643-656
    • Parast, M.M.1    Otey, C.A.2
  • 98
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: integrating cytoskeletal dynamics and cellular tension
    • Parsons, J. T., Horwitz, A. R. and Schwartz, M. A. (2010). Cell adhesion: integrating cytoskeletal dynamics and cellular tension. Nat. Rev. Mol. Cell Biol. 11, 633-643.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schwartz, M.A.3
  • 100
    • 36248969983 scopus 로고    scopus 로고
    • Actin stress fibres
    • Pellegrin, S. P. and Mellor, H. (2007). Actin stress fibres. J. Cell Sci. 120, 3491-3499.
    • (2007) J. Cell Sci. , vol.120 , pp. 3491-3499
    • Pellegrin, S.P.1    Mellor, H.2
  • 102
    • 34247644614 scopus 로고    scopus 로고
    • Regulation of actin filament assembly by Arp2/3 complex and formins
    • Pollard, T. D. (2007). Regulation of actin filament assembly by Arp2/3 complex and formins. Annu. Rev. Biophys Biomol. Struct. 36, 451-477.
    • (2007) Annu. Rev. Biophys Biomol. Struct. , vol.36 , pp. 451-477
    • Pollard, T.D.1
  • 103
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard, T. D. and Cooper, J. A. (2009). Actin, a central player in cell shape and movement. Science 326, 1208-1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 104
    • 75149124357 scopus 로고    scopus 로고
    • Understanding cytokinesis: lessons from fission yeast
    • Pollard, T. D. and Wu, J. Q. (2010). Understanding cytokinesis: lessons from fission yeast. Nat. Rev. Mol. Cell Biol. 11, 149-155.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 149-155
    • Pollard, T.D.1    Wu, J.Q.2
  • 105
    • 4544309783 scopus 로고    scopus 로고
    • Two Distinct Actin Networks Drive the Protrusion of Migrating Cells
    • Ponti, A., Machacek, M., Gupton, S. L., Waterman-Storer, C. M. and Danuser, G. (2004). Two Distinct Actin Networks Drive the Protrusion of Migrating Cells. Science 305, 1782-1786.
    • (2004) Science , vol.305 , pp. 1782-1786
    • Ponti, A.1    Machacek, M.2    Gupton, S.L.3    Waterman-Storer, C.M.4    Danuser, G.5
  • 107
    • 33750337536 scopus 로고    scopus 로고
    • How the headpiece hinge angle is opened: new insights into the dynamics of integrin activation
    • Puklin-Faucher, E., Gao, M., Schulten, K. and Vogel, V. (2006). How the headpiece hinge angle is opened: new insights into the dynamics of integrin activation. J. Cell Biol. 175, 349-360.
    • (2006) J. Cell Biol. , vol.175 , pp. 349-360
    • Puklin-Faucher, E.1    Gao, M.2    Schulten, K.3    Vogel, V.4
  • 109
    • 0035844869 scopus 로고    scopus 로고
    • Focal Contacts as Mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism
    • Riveline, D., Zamir, E., Balaban, N. Q., Schwarz, U. S., Ishizaki, T., Narumiya, S., Kam, Z., Geiger, B. and Bershadsky, A. D. (2001). Focal Contacts as Mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism. J. Cell Biol. 153, 1175-1186.
    • (2001) J. Cell Biol. , vol.153 , pp. 1175-1186
    • Riveline, D.1    Zamir, E.2    Balaban, N.Q.3    Schwarz, U.S.4    Ishizaki, T.5    Narumiya, S.6    Kam, Z.7    Geiger, B.8    Bershadsky, A.D.9
  • 110
    • 48949118319 scopus 로고    scopus 로고
    • Calponins: adaptable modular regulators of the actin cytoskeleton
    • Rozenblum, G. T. and Gimona, M. (2008). Calponins: adaptable modular regulators of the actin cytoskeleton. Int. J. Biochem Cell Biol. 40, 1990-1995.
    • (2008) Int. J. Biochem Cell Biol. , vol.40 , pp. 1990-1995
    • Rozenblum, G.T.1    Gimona, M.2
  • 111
    • 0021331350 scopus 로고
    • Location of actin, myosin, and microtubular structures during directed locomotion of Dictyostelium amebae
    • Rubino, S., Fighetti, M., Unger, E. and Cappuccinelli, P. (1984). Location of actin, myosin, and microtubular structures during directed locomotion of Dictyostelium amebae. J. Cell Biol. 98, 382-390.
    • (1984) J. Cell Biol. , vol.98 , pp. 382-390
    • Rubino, S.1    Fighetti, M.2    Unger, E.3    Cappuccinelli, P.4
  • 112
    • 80052998025 scopus 로고    scopus 로고
    • Actin cytoskeleton in myofibroblast differentiation: Ultrastructure defining form and driving function
    • Sandbo, N. and Dulin, N. (2011). Actin cytoskeleton in myofibroblast differentiation: Ultrastructure defining form and driving function. Transl. Res. 158, 181-196.
    • (2011) Transl. Res. , vol.158 , pp. 181-196
    • Sandbo, N.1    Dulin, N.2
  • 116
    • 33644615900 scopus 로고    scopus 로고
    • Biorheological views of endothelial cell responses to mechanical stimuli
    • Sato, M. and Ohashi, T. (2005). Biorheological views of endothelial cell responses to mechanical stimuli. Biorheology 42, 421-441.
    • (2005) Biorheology , vol.42 , pp. 421-441
    • Sato, M.1    Ohashi, T.2
  • 119
    • 10144257865 scopus 로고    scopus 로고
    • Functional interdependence between septin and actin cytoskeleton
    • Schmidt, K. and Nichols, B. J. (2004). Functional interdependence between septin and actin cytoskeleton. BMC Cell Biol. 5, 43-56.
    • (2004) BMC Cell Biol , vol.5 , pp. 43-56
    • Schmidt, K.1    Nichols, B.J.2
  • 120
    • 70349587472 scopus 로고    scopus 로고
    • Role of focal adhesions and mechanical stresses in the formation and progression of the lamellipodium-lamellum interface
    • Shemesh, T., Verkhovsky, A. B., Svitkina, T. M., Bershadsky, A. D. and Kozlov, M. M. (2009). Role of focal adhesions and mechanical stresses in the formation and progression of the lamellipodium-lamellum interface. Biophys. J. 97, 1254-6124.
    • (2009) Biophys. J. , vol.97 , pp. 1254-6124
    • Shemesh, T.1    Verkhovsky, A.B.2    Svitkina, T.M.3    Bershadsky, A.D.4    Kozlov, M.M.5
  • 122
    • 0032537991 scopus 로고    scopus 로고
    • Assembling an actin cytoskeleton for cell attachment and movement
    • Small, J. V., Rottner, K., Kaverina, I. and Anderson, K. I. (1998). Assembling an actin cytoskeleton for cell attachment and movement. Biochim. Biophys. Acta. 1404, 271-281.
    • (1998) Biochim. Biophys. Acta. , vol.1404 , pp. 271-281
    • Small, J.V.1    Rottner, K.2    Kaverina, I.3    Anderson, K.I.4
  • 124
    • 0034650714 scopus 로고    scopus 로고
    • Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II
    • Somlyo, A. P. and Somlyo, A. V. (2000). Signal transduction by G-proteins, rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II. J. Physiol. 2, 177-185.
    • (2000) J. Physiol. , vol.2 , pp. 177-185
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 125
    • 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
  • 126
    • 77949457529 scopus 로고    scopus 로고
    • Tropomyosin and myosin-II cellular levels promote actomyosin ring assembly in fission yeast
    • Stark, B. C., Sladewski, T. E., Pollard, L. W. and Lord, M. (2010). Tropomyosin and myosin-II cellular levels promote actomyosin ring assembly in fission yeast. Mol. Biol. Cell. 21, 989-1000.
    • (2010) Mol. Biol. Cell. , vol.21 , pp. 989-1000
    • Stark, B.C.1    Sladewski, T.E.2    Pollard, L.W.3    Lord, M.4
  • 127
    • 0027283067 scopus 로고
    • Mammalian calponin Identification and expression of genetic variants
    • Strasser, P., Gimona, M., Moessler, H., Herzog, M. and Small, J. V. (1993). Mammalian calponin. Identification and expression of genetic variants. FEBS Lett. 330, 13-18.
    • (1993) FEBS Lett , vol.330 , pp. 13-18
    • Strasser, P.1    Gimona, M.2    Moessler, H.3    Herzog, M.4    Small, J.V.5
  • 128
    • 30044451338 scopus 로고    scopus 로고
    • M-RIP targets myosin phosphatase to stress fibers to regulate myosin light chain phosphorylation in vascular smooth muscle cells
    • Surks, H. K., Riddick, N. and Ohtani, K. (2005). M-RIP targets myosin phosphatase to stress fibers to regulate myosin light chain phosphorylation in vascular smooth muscle cells. J. Biol. Chem. 280, 42543-42551.
    • (2005) J. Biol. Chem. , vol.280 , pp. 42543-42551
    • Surks, H.K.1    Riddick, N.2    Ohtani, K.3
  • 131
    • 0034698841 scopus 로고    scopus 로고
    • Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts
    • Totsukawa, G., Yamakita, Y., Yamashiro, S., Hartshorne, D. J., Sasaki, Y. and Matsumura, F. (2000). Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J. Cell Biol. 150, 797-806.
    • (2000) J. Cell Biol. , vol.150 , pp. 797-806
    • Totsukawa, G.1    Yamakita, Y.2    Yamashiro, S.3    Hartshorne, D.J.4    Sasaki, Y.5    Matsumura, F.6
  • 132
    • 28844455092 scopus 로고    scopus 로고
    • Cysteine-rich protein 1 (CRP1) regulates actin filament bundling
    • Tran, T. C., Singleton, C., Fraley, T. S. and Greenwood, J. A. (2005). Cysteine-rich protein 1 (CRP1) regulates actin filament bundling. BMC Cell Biol. 6, 45.
    • (2005) BMC Cell Biol , vol.6 , pp. 45
    • Tran, T.C.1    Singleton, C.2    Fraley, T.S.3    Greenwood, J.A.4
  • 133
    • 0019435848 scopus 로고
    • Distribution of actin-binding protein and myosin in polymorphonuclear leukocytes during locomotion and phagocytosis
    • Valerius, N. H., Stendahl, O., Hartwig, J. H. and Stossel, T. P. (1981). Distribution of actin-binding protein and myosin in polymorphonuclear leukocytes during locomotion and phagocytosis. Cell 24, 195-202.
    • (1981) Cell , vol.24 , pp. 195-202
    • Valerius, N.H.1    Stendahl, O.2    Hartwig, J.H.3    Stossel, T.P.4
  • 134
    • 0034646678 scopus 로고    scopus 로고
    • CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4
    • Vallenius, T., Luukko, K. and Mäkelä, T. P. (2000). CLP-36 PDZ-LIM protein associates with nonmuscle alpha-actinin-1 and alpha-actinin-4. J. Biol. Chem. 275, 11100-11105.
    • (2000) J. Biol. Chem. , vol.275 , pp. 11100-11105
    • Vallenius, T.1    Luukko, K.2    Mäkelä, T.P.3
  • 135
    • 0037092509 scopus 로고    scopus 로고
    • Clik1: a novel kinase targeted to actin stress fibers by the CLP-36 PDZ-LIM protein
    • Vallenius, T. and Mäkelä, T. P. (2002). Clik1: a novel kinase targeted to actin stress fibers by the CLP-36 PDZ-LIM protein. J. Cell Sci. 115, 2067-2073.
    • (2002) J. Cell Sci. , vol.115 , pp. 2067-2073
    • Vallenius, T.1    Mäkelä, T.P.2
  • 136
    • 79551564565 scopus 로고    scopus 로고
    • An association between NUAK2 and MRIP reveals a novel mechanism for regulation of actin stress fibers
    • Vallenius, T., Vaahtomeri, K., Kovac, B., Osiceanu, A. M., Viljanen, M. and Mäkelä, T. P. (2011). An association between NUAK2 and MRIP reveals a novel mechanism for regulation of actin stress fibers. J. Cell Sci. 124, 384-393.
    • (2011) J. Cell Sci. , vol.124 , pp. 384-393
    • Vallenius, T.1    Vaahtomeri, K.2    Kovac, B.3    Osiceanu, A.M.4    Viljanen, M.5    Mäkelä, T.P.6
  • 137
    • 68949189408 scopus 로고    scopus 로고
    • Shifting views on the leading role of the lamellipodium in cell migration: speckle tracking revisited
    • Vallotton, P. and Small, J. V. (2009). Shifting views on the leading role of the lamellipodium in cell migration: speckle tracking revisited. J. Cell Sci. 122, 1955-1958.
    • (2009) J. Cell Sci. , vol.122 , pp. 1955-1958
    • Vallotton, P.1    Small, J.V.2
  • 140
    • 33645780908 scopus 로고    scopus 로고
    • Mechanotransduction involving multimodular proteins: Converting Force into Biochemical Signals
    • Vogel, V. (2006). Mechanotransduction involving multimodular proteins: Converting Force into Biochemical Signals. Annu. Rev. Biophys. Biomol. Struct. 35, 459-488.
    • (2006) Annu. Rev. Biophys. Biomol. Struct. , vol.35 , pp. 459-488
    • Vogel, V.1
  • 141
    • 77952355776 scopus 로고    scopus 로고
    • A mechanical model of actin stress fiber formation and substrate elasticity sensing in adherent cells
    • Walcott, S. and Sun, S. X. (2010). A mechanical model of actin stress fiber formation and substrate elasticity sensing in adherent cells. Proc. Natl. Acad. Sci. USA 107, 7757-7762.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 7757-7762
    • Walcott, S.1    Sun, S.X.2
  • 142
    • 0039154943 scopus 로고
    • Filamin, a new high-molecular-weight protein found in smooth muscle and non-muscle cells
    • Wang, K., Ash, J. F. and Singer, S. J. (1975). Filamin, a new high-molecular-weight protein found in smooth muscle and non-muscle cells. Proc. Natl. Acad. Sci. USA 72, 4483-4486
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 4483-4486
    • Wang, K.1    Ash, J.F.2    Singer, S.J.3
  • 143
    • 0030911424 scopus 로고    scopus 로고
    • p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin
    • Watanabe, N., Madaule, P., Reid, T., Ishizaki, T., Watanabe, G., Kakizuka, A., Saito, Y., Nakao, K., Jockusch, B. M. and Narumiya, S. (1997). p140mDia, a mammalian homolog of Drosophila diaphanous, is a target protein for Rho small GTPase and is a ligand for profilin. EMBO J. 16, 3044-3056.
    • (1997) EMBO J , vol.16 , pp. 3044-3056
    • Watanabe, N.1    Madaule, P.2    Reid, T.3    Ishizaki, T.4    Watanabe, G.5    Kakizuka, A.6    Saito, Y.7    Nakao, K.8    Jockusch, B.M.9    Narumiya, S.10
  • 144
    • 0016267717 scopus 로고
    • Antibody to myosin: the specific visualization of myosin-containing filaments in nonmuscle cells
    • Weber, K. and Groeschel-Stewart, U. (1974). Antibody to myosin: the specific visualization of myosin-containing filaments in nonmuscle cells. Proc. Natl. Acad. Sci. USA 71, 4561-4564
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4561-4564
    • Weber, K.1    Groeschel-Stewart, U.2
  • 145
  • 146
    • 0020664146 scopus 로고
    • Actin filament stress fibers in vascular endothelial cells in vivo
    • Wong, A. J., Pollard, T. D. and Herman, I. M. (1983). Actin filament stress fibers in vascular endothelial cells in vivo. Science 219, 867-869.
    • (1983) Science , vol.219 , pp. 867-869
    • Wong, A.J.1    Pollard, T.D.2    Herman, I.M.3
  • 147
    • 0028961493 scopus 로고
    • Characterization of the COOH terminus of non-muscle caldesmon mutants lacking mitosis-specific phosphorylation sites
    • Yamashiro, S., Yamakita, Y., Yoshida, K., Takiguchi, K. and Matsumura, F. (1995). Characterization of the COOH terminus of non-muscle caldesmon mutants lacking mitosis-specific phosphorylation sites. J. Biol. Chem. 270, 4023-4030.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4023-4030
    • Yamashiro, S.1    Yamakita, Y.2    Yoshida, K.3    Takiguchi, K.4    Matsumura, F.5
  • 148
    • 0023767003 scopus 로고
    • Characterization of 83- kilodalton nonmuscle caldesmon from cultured rat cells: stimulation of actin binding of nonmuscle tropomyosin and periodic localization along microfilaments like tropomyosin
    • Yamashiro-Matsumura, S. and Matsumura, F. (1988). Characterization of 83- kilodalton nonmuscle caldesmon from cultured rat cells: stimulation of actin binding of nonmuscle tropomyosin and periodic localization along microfilaments like tropomyosin. J. Cell Biol. 106, 1973-1983.
    • (1988) J. Cell Biol. , vol.106 , pp. 1973-1983
    • Yamashiro-Matsumura, S.1    Matsumura, F.2
  • 149
    • 0034982994 scopus 로고    scopus 로고
    • Modulatory role of ERK MAPKcaldesmon pathway in PDGF-stimulated migration of cultured pulmonary artery SMCs
    • Yamboliev, I. A. and Gerthoffer, W. T. (2001). Modulatory role of ERK MAPKcaldesmon pathway in PDGF-stimulated migration of cultured pulmonary artery SMCs. Am J. Physiol. Cell Physiol. 280, C1680-C1688.
    • (2001) Am J. Physiol. Cell Physiol. , vol.280
    • Yamboliev, I.A.1    Gerthoffer, W.T.2
  • 150
    • 81255199170 scopus 로고    scopus 로고
    • Cease-fire at the leading edge: New perspectives on actin filament branching, debranching, and cross-linking
    • Ydenberg, C. A., Smith, B. A., Breitsprecher, D., Gelles, J. and Goode, B. L.(2011). Cease-fire at the leading edge: New perspectives on actin filament branching, debranching, and cross-linking. Cytoskeleton (Hoboken), 68, 596-602.
    • (2011) Cytoskeleton (Hoboken) , vol.68 , pp. 596-602
    • Ydenberg, C.A.1    Smith, B.A.2    Breitsprecher, D.3    Gelles, J.4    Goode, B.L.5
  • 151
    • 84863229197 scopus 로고    scopus 로고
    • Actin Retrograde Flow and Acto-Myosin II Arc Contraction Drive Receptor Cluster Dynamics at the Immunological Synapse in Jurkat T-Cells
    • Yi, J., Wu, X. S., Crites, T. and Hammer, J. A. (2012). Actin Retrograde Flow and Acto-Myosin II Arc Contraction Drive Receptor Cluster Dynamics at the Immunological Synapse in Jurkat T-Cells. Mol. Biol. Cell. 23, 834-852.
    • (2012) Mol. Biol. Cell. , vol.23 , pp. 834-852
    • Yi, J.1    Wu, X.S.2    Crites, T.3    Hammer, J.A.4
  • 153
    • 77953130411 scopus 로고    scopus 로고
    • Optimal matrix rigidity for stress-fibre polarization in stem cells
    • Zemel, A., Rehfeldt, F., Brown, A. E. X., Discher, D. E. and Safran, S. A. (2010). Optimal matrix rigidity for stress-fibre polarization in stem cells. Nat. Phys. 6, 468-473.
    • (2010) Nat. Phys. , vol.6 , pp. 468-473
    • Zemel, A.1    Rehfeldt, F.2    Brown, A.E.X.3    Discher, D.E.4    Safran, S.A.5
  • 154
    • 0345735940 scopus 로고    scopus 로고
    • Rho-Dependent Contractile Responses in the Neuronal Growth Cone Are Independent of Classical Peripheral Retrograde Actin Flow
    • Zhang, X.-F., Schaefer, A. W., Burnette, D. T., Schoonderwoert, V. T. and Forscher, P. (2003). Rho-Dependent Contractile Responses in the Neuronal Growth Cone Are Independent of Classical Peripheral Retrograde Actin Flow. Neuron 40, 931-944.
    • (2003) Neuron , vol.40 , pp. 931-944
    • Zhang, X.-F.1    Schaefer, A.W.2    Burnette, D.T.3    Schoonderwoert, V.T.4    Forscher, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.