메뉴 건너뛰기




Volumn 17, Issue 4, 2015, Pages 445-457

Cellular chirality arising from the self-organization of the actin cytoskeleton

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ACTININ; ALPHA ACTININ 1; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN IIA; ACTININ; ACTN1 PROTEIN, MOUSE; SMALL INTERFERING RNA;

EID: 84925945544     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb3137     Document Type: Article
Times cited : (346)

References (70)
  • 1
    • 84898721737 scopus 로고    scopus 로고
    • The evolution and conservation of left-right patterning mechanisms
    • Blum, M., Feistel, K., Thumberger, T. & Schweickert, A. The evolution and conservation of left-right patterning mechanisms. Development 141, 1603-1613 (2014).
    • (2014) Development , vol.141 , pp. 1603-1613
    • Blum, M.1    Feistel, K.2    Thumberger, T.3    Schweickert, A.4
  • 2
    • 84906850253 scopus 로고    scopus 로고
    • Diversity and convergence in the mechanisms establishing L/R asymmetry in metazoa
    • Coutelis, J. B., Gonzalez-Morales, N., Geminard, C. & Noselli, S. Diversity and convergence in the mechanisms establishing L/R asymmetry in metazoa. EMBO Rep. 15, 926-937 (2014).
    • (2014) EMBO Rep. , vol.15 , pp. 926-937
    • Coutelis, J.B.1    Gonzalez-Morales, N.2    Geminard, C.3    Noselli, S.4
  • 3
    • 84891160941 scopus 로고    scopus 로고
    • Roles of cilia, fluid flow, and Ca2C signaling in breaking of left-right symmetry
    • Yoshiba, S. & Hamada, H. Roles of cilia, fluid flow, and Ca2C signaling in breaking of left-right symmetry. Trends Genet. 30, 10-17 (2014).
    • (2014) Trends Genet. , vol.30 , pp. 10-17
    • Yoshiba, S.1    Hamada, H.2
  • 5
    • 79961082570 scopus 로고    scopus 로고
    • Micropatterned mammalian cells exhibit phenotype-specific left-right asymmetry
    • Wan, L. Q. et al. Micropatterned mammalian cells exhibit phenotype-specific left-right asymmetry. Proc. Natl Acad. Sci. USA 108, 12295-12300 (2011).
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 12295-12300
    • Wan, L.Q.1
  • 6
    • 84857646273 scopus 로고    scopus 로고
    • Left-right symmetry breaking in tissue morphogenesis via cytoskeletal mechanics
    • Chen, T. H. et al. Left-right symmetry breaking in tissue morphogenesis via cytoskeletal mechanics. Circ. Res. 110, 551-559 (2012).
    • (2012) Circ. Res. , vol.110 , pp. 551-559
    • Chen, T.H.1
  • 7
    • 34547152147 scopus 로고    scopus 로고
    • Polarity reveals intrinsic cell chirality
    • Xu, J. et al. Polarity reveals intrinsic cell chirality. Proc. Natl Acad. Sci. USA 104, 9296-9300 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 9296-9300
    • Xu, J.1
  • 8
    • 0017758570 scopus 로고
    • Clockwise growth of neurites from retinal explants
    • Heacock, A. M. & Agranoff, B. W. Clockwise growth of neurites from retinal explants. Science 198, 64-66 (1977).
    • (1977) Science , vol.198 , pp. 64-66
    • Heacock, A.M.1    Agranoff, B.W.2
  • 9
    • 76349098916 scopus 로고    scopus 로고
    • Autonomous rightscrew rotation of growth cone filopodia drives neurite turning
    • Tamada, A., Kawase, S., Murakami, F. & Kamiguchi, H. Autonomous rightscrew rotation of growth cone filopodia drives neurite turning. J. Cell Biol. 188, 429-441 (2010).
    • (2010) J. Cell Biol. , vol.188 , pp. 429-441
    • Tamada, A.1    Kawase, S.2    Murakami, F.3    Kamiguchi, H.4
  • 10
    • 0027456713 scopus 로고
    • Pattern formation and handedness in the cytoskeleton of human platelets
    • Hagmann, J. Pattern formation and handedness in the cytoskeleton of human platelets. Proc. Natl Acad. Sci. USA 90, 3280-3283 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 3280-3283
    • Hagmann, J.1
  • 11
    • 84925943286 scopus 로고    scopus 로고
    • Rotating pigment cells exhibit an intrinsic chirality
    • Yamanaka, H. & Kondo, S. Rotating pigment cells exhibit an intrinsic chirality. Genes Cells 20, 29-35 (2015).
    • (2015) Genes Cells , vol.20 , pp. 29-35
    • Yamanaka, H.1    Kondo, S.2
  • 12
    • 84866318147 scopus 로고    scopus 로고
    • Possible origins of macroscopic left-right asymmetry in organisms
    • Henley, C. L. Possible origins of macroscopic left-right asymmetry in organisms. J. Stat. Phys. 148, 741-775 (2012).
    • (2012) J. Stat. Phys. , vol.148 , pp. 741-775
    • Henley, C.L.1
  • 13
    • 84894103782 scopus 로고    scopus 로고
    • It's never too early to get it Right: A conserved role for the cytoskeleton in left-right asymmetry
    • Vandenberg, L. N., Lemire, J. M. & Levin, M. It's never too early to get it Right: a conserved role for the cytoskeleton in left-right asymmetry. Commun. Integr. Biol. 6, e27155 (2013).
    • (2013) Commun. Integr. Biol. , vol.6 , pp. e27155
    • Vandenberg, L.N.1    Lemire, J.M.2    Levin, M.3
  • 14
    • 0021627104 scopus 로고
    • Spreading of non-Transformed and transformed cells
    • Vasiliev, J. M. Spreading of non-Transformed and transformed cells. Biochim. Biophys. Acta 780, 21-65 (1985).
    • (1985) Biochim. Biophys. Acta , vol.780 , pp. 21-65
    • Vasiliev, J.M.1
  • 15
    • 0032537991 scopus 로고    scopus 로고
    • Assembling an actin cytoskeleton for cell attachment and movement
    • Small, J. V., Rottner, K., Kaverina, I. & Anderson, K. I. Assembling an actin cytoskeleton for cell attachment and movement. Biochim. Biophys. Acta 1404, 271-281 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1404 , pp. 271-281
    • Small, J.V.1    Rottner, K.2    Kaverina, I.3    Anderson, K.I.4
  • 16
    • 84863113109 scopus 로고    scopus 로고
    • Actin stress fibers-Assembly, dynamics and biological roles
    • Tojkander, S., Gateva, G. & Lappalainen, P. Actin stress fibers-Assembly, dynamics and biological roles. J. Cell Sci. 125, 1855-1864 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 1855-1864
    • Tojkander, S.1    Gateva, G.2    Lappalainen, P.3
  • 17
    • 84872084802 scopus 로고    scopus 로고
    • The tension mounts: Stress fibers as force-generating mechanotransducers
    • Burridge, K. & Wittchen, E. S. The tension mounts: stress fibers as force-generating mechanotransducers. J. Cell Biol. 200, 9-19 (2013).
    • (2013) J. Cell Biol. , vol.200 , pp. 9-19
    • Burridge, K.1    Wittchen, E.S.2
  • 18
    • 0020577405 scopus 로고
    • Direct evidence for microfilament-mediated capping of surface receptors on crawling fibroblasts
    • Heath, J. P. Direct evidence for microfilament-mediated capping of surface receptors on crawling fibroblasts. Nature 302, 532-534 (1983).
    • (1983) Nature , vol.302 , pp. 532-534
    • Heath, J.P.1
  • 19
    • 33646386142 scopus 로고    scopus 로고
    • Stress fibers are generated by two distinct actin assembly mechanisms in motile cells
    • Hotulainen, P. & Lappalainen, P. Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J. Cell Biol. 173, 383-394 (2006).
    • (2006) J. Cell Biol. , vol.173 , pp. 383-394
    • Hotulainen, P.1    Lappalainen, P.2
  • 20
  • 21
    • 84885654506 scopus 로고    scopus 로고
    • Actin stress fibre subtypes in mesenchymal-migrating cells
    • Vallenius, T. Actin stress fibre subtypes in mesenchymal-migrating cells. Open Biol. 3, 130001 (2013).
    • (2013) Open Biol. , vol.3 , pp. 130001
    • Vallenius, T.1
  • 22
    • 84859387007 scopus 로고    scopus 로고
    • Tension is required but not sufficient for focal adhesion maturation without a stress fiber template
    • Oakes, P. W., Beckham, Y., Stricker, J. & Gardel, M. L. Tension is required but not sufficient for focal adhesion maturation without a stress fiber template. J. Cell Biol. 196, 363-374 (2012).
    • (2012) J. Cell Biol. , vol.196 , pp. 363-374
    • Oakes, P.W.1    Beckham, Y.2    Stricker, J.3    Gardel, M.L.4
  • 23
    • 79953794528 scopus 로고    scopus 로고
    • A molecular pathway for myosin II recruitment to stress fibers
    • Tojkander, S. et al. A molecular pathway for myosin II recruitment to stress fibers. Curr. Biol. 21, 539-550 (2011).
    • (2011) Curr. Biol. , vol.21 , pp. 539-550
    • Tojkander, S.1
  • 24
    • 84875633689 scopus 로고    scopus 로고
    • Assembly of non-contractile dorsal stress fibers requires-Actinin-1 and Rac1 in migrating and spreading cells
    • Kovac, B., Teo, J. L., Makela, T. P. & Vallenius, T. Assembly of non-contractile dorsal stress fibers requires-Actinin-1 and Rac1 in migrating and spreading cells. J. Cell Sci. 126, 263-273 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 263-273
    • Kovac, B.1    Teo, J.L.2    Makela, T.P.3    Vallenius, T.4
  • 25
    • 84899734615 scopus 로고    scopus 로고
    • Palladin promotes assembly of non-contractile dorsal stress fibers through VASP recruitment
    • Gateva, G., Tojkander, S., Koho, S., Carpen, O. & Lappalainen, P. Palladin promotes assembly of non-contractile dorsal stress fibers through VASP recruitment. J. Cell Sci. 127, 1887-1898 (2014).
    • (2014) J. Cell Sci. , vol.127 , pp. 1887-1898
    • Gateva, G.1    Tojkander, S.2    Koho, S.3    Carpen, O.4    Lappalainen, P.5
  • 26
    • 70349587472 scopus 로고    scopus 로고
    • Role of focal adhesions and mechanical stresses in the formation and progression of the lamellipodium-lamellum interface
    • correction 97 2115 2009
    • Shemesh, T., Verkhovsky, A. B., Svitkina, T. M., Bershadsky, A. D. & Kozlov, M. M. Role of focal adhesions and mechanical stresses in the formation and progression of the lamellipodium-lamellum interface. Biophys. J. 97, 1254-1264 (2009); correction 97, 2115 (2009).
    • (2009) Biophys. J. , vol.97 , pp. 1254-1264
    • Shemesh, T.1    Verkhovsky, A.B.2    Svitkina, T.M.3    Bershadsky, A.D.4    Kozlov, M.M.5
  • 27
    • 79953325280 scopus 로고    scopus 로고
    • A role for actin arcs in the leading-edge advance of migrating cells
    • Burnette, D. T. et al. A role for actin arcs in the leading-edge advance of migrating cells. Nat. Cell Biol. 13, 371-381 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 371-381
    • Burnette, D.T.1
  • 28
    • 84901673131 scopus 로고    scopus 로고
    • A contractile and counterbalancing adhesion system controls the 3D shape of crawling cells
    • Burnette, D. T. et al. A contractile and counterbalancing adhesion system controls the 3D shape of crawling cells. J. Cell Biol. 205, 83-96 (2014).
    • (2014) J. Cell Biol. , vol.205 , pp. 83-96
    • Burnette, D.T.1
  • 30
    • 84896515379 scopus 로고    scopus 로고
    • Myosin lever arm directs collective motion on cellular actin network
    • Hariadi, R. F., Cale, M. & Sivaramakrishnan, S. Myosin lever arm directs collective motion on cellular actin network. Proc. Natl Acad. Sci. USA 111, 4091-4096 (2014).
    • (2014) Proc. Natl Acad. Sci. USA , vol.111 , pp. 4091-4096
    • Hariadi, R.F.1    Cale, M.2    Sivaramakrishnan, S.3
  • 31
    • 44349179335 scopus 로고    scopus 로고
    • Filopodia: Molecular architecture and cellular functions
    • Mattila, P. K. & Lappalainen, P. Filopodia: molecular architecture and cellular functions. Nat. Rev. Mol. Cell Biol. 9, 446-454 (2008).
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 446-454
    • Mattila, P.K.1    Lappalainen, P.2
  • 32
    • 72049090358 scopus 로고    scopus 로고
    • Identification and characterization of a small molecule inhibitor of formin-mediated actin assembly
    • Rizvi, S. A. et al. Identification and characterization of a small molecule inhibitor of formin-mediated actin assembly. Chem. Biol. 16, 1158-1168 (2009).
    • (2009) Chem. Biol. , vol.16 , pp. 1158-1168
    • Rizvi, S.A.1
  • 33
    • 69249212192 scopus 로고    scopus 로고
    • Characterization of two classes of small molecule inhibitors of Arp2/3 complex
    • Nolen, B. J. et al. Characterization of two classes of small molecule inhibitors of Arp2/3 complex. Nature 460, 1031-1034 (2009).
    • (2009) Nature , vol.460 , pp. 1031-1034
    • Nolen, B.J.1
  • 34
    • 84861926483 scopus 로고    scopus 로고
    • The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration
    • Suraneni, P. et al. The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration. J. Cell Biol. 197, 239-251 (2012).
    • (2012) J. Cell Biol. , vol.197 , pp. 239-251
    • Suraneni, P.1
  • 35
    • 84863229890 scopus 로고    scopus 로고
    • Arp2/3 is critical for lamellipodia and response to extracellular matrix cues but is dispensable for chemotaxis
    • Wu, C. et al. Arp2/3 is critical for lamellipodia and response to extracellular matrix cues but is dispensable for chemotaxis. Cell 148, 973-987 (2012).
    • (2012) Cell , vol.148 , pp. 973-987
    • Wu, C.1
  • 36
    • 0037436506 scopus 로고    scopus 로고
    • Dissecting temporal and spatial control of cytokinesis with a myosin II inhibitor
    • Straight, A. F. et al. Dissecting temporal and spatial control of cytokinesis with a myosin II inhibitor. Science 299, 1743-1747 (2003).
    • (2003) Science , vol.299 , pp. 1743-1747
    • Straight, A.F.1
  • 37
    • 0030656619 scopus 로고    scopus 로고
    • Calcium sensitization of smooth muscle mediated by a Rhoassociated protein kinase in hypertension
    • Uehata, M. et al. Calcium sensitization of smooth muscle mediated by a Rhoassociated protein kinase in hypertension. Nature 389, 990-994 (1997).
    • (1997) Nature , vol.389 , pp. 990-994
    • Uehata, M.1
  • 38
    • 33644503878 scopus 로고    scopus 로고
    • Genetic ablation of zyxin causes Mena/VASP mislocalization, increased motility, and deficits in actin remodeling
    • Hoffman, L. M. et al. Genetic ablation of zyxin causes Mena/VASP mislocalization, increased motility, and deficits in actin remodeling. J. Cell Biol. 172, 771-782 (2006).
    • (2006) J. Cell Biol. , vol.172 , pp. 771-782
    • Hoffman, L.M.1
  • 39
    • 0033588277 scopus 로고    scopus 로고
    • Structure of the-Actinin rod: Molecular basis for cross-linking of actin filaments
    • Djinovic-Carugo, K., Young, P., Gautel, M. & Saraste, M. Structure of the-Actinin rod: molecular basis for cross-linking of actin filaments. Cell 98, 537-546 (1999).
    • (1999) Cell , vol.98 , pp. 537-546
    • Djinovic-Carugo, K.1    Young, P.2    Gautel, M.3    Saraste, M.4
  • 40
    • 51049104617 scopus 로고    scopus 로고
    • Actin and-Actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi, C. K. et al. Actin and-Actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nat. Cell Biol. 10, 1039-1050 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1039-1050
    • Choi, C.K.1
  • 41
    • 84876053270 scopus 로고    scopus 로고
    • Integrin-dependent force transmission to the extracellular matrix by-Actinin triggers adhesion maturation
    • Roca-Cusachs, P. et al. Integrin-dependent force transmission to the extracellular matrix by-Actinin triggers adhesion maturation. Proc. Natl Acad. Sci. USA 110, E1361-E1370 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. E1361-E1370
    • Roca-Cusachs, P.1
  • 42
    • 77953460317 scopus 로고    scopus 로고
    • Domain analysis of-Actinin reveals new aspects of its association with F-Actin during cytokinesis
    • Low, S. H., Mukhina, S., Srinivas, V., Ng, C. Z. & Murata-Hori, M. Domain analysis of-Actinin reveals new aspects of its association with F-Actin during cytokinesis. Exp. Cell Res. 316, 1925-1934 (2010).
    • (2010) Exp. Cell Res. , vol.316 , pp. 1925-1934
    • Low, S.H.1    Mukhina, S.2    Srinivas, V.3    Ng, C.Z.4    Murata-Hori, M.5
  • 43
    • 11244345198 scopus 로고    scopus 로고
    • Processive capping by formin suggests a force-driven mechanism of actin polymerization
    • Kozlov, M. M. & Bershadsky, A. D. Processive capping by formin suggests a force-driven mechanism of actin polymerization. J. Cell Biol. 167, 1011-1017 (2004).
    • (2004) J. Cell Biol. , vol.167 , pp. 1011-1017
    • Kozlov, M.M.1    Bershadsky, A.D.2
  • 44
    • 33847785678 scopus 로고    scopus 로고
    • Actin polymerization upon processive capping by formin: A model for slowing and acceleration
    • Shemesh, T. & Kozlov, M. M. Actin polymerization upon processive capping by formin: a model for slowing and acceleration. Biophys. J. 92, 1512-1521 (2007).
    • (2007) Biophys. J. , vol.92 , pp. 1512-1521
    • Shemesh, T.1    Kozlov, M.M.2
  • 45
    • 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. & Mitchison, T. J. 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).
    • (1997) J. Cell Biol. , vol.136 , pp. 1287-1305
    • Cramer, L.P.1    Siebert, M.2    Mitchison, T.J.3
  • 46
    • 67749135871 scopus 로고    scopus 로고
    • Review of the mechanism of processive actin filament elongation by formins
    • Paul, A. S. & Pollard, T. D. Review of the mechanism of processive actin filament elongation by formins. Cell Motil. Cytoskeleton 66, 606-617 (2009).
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 606-617
    • Paul, A.S.1    Pollard, T.D.2
  • 48
    • 1542269073 scopus 로고    scopus 로고
    • Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture
    • Xu, Y. et al. Crystal structures of a Formin Homology-2 domain reveal a tethered dimer architecture. Cell 116, 711-723 (2004).
    • (2004) Cell , vol.116 , pp. 711-723
    • Xu, Y.1
  • 49
    • 24944560068 scopus 로고    scopus 로고
    • A novel mechanism of actin filament processive capping by formin: Solution of the rotation paradox
    • Shemesh, T., Otomo, T., Rosen, M. K., Bershadsky, A. D. & Kozlov, M. M. A novel mechanism of actin filament processive capping by formin: solution of the rotation paradox. J. Cell Biol. 170, 889-893 (2005).
    • (2005) J. Cell Biol. , vol.170 , pp. 889-893
    • Shemesh, T.1    Otomo, T.2    Rosen, M.K.3    Bershadsky, A.D.4    Kozlov, M.M.5
  • 50
    • 78650988290 scopus 로고    scopus 로고
    • Rotational movement of the formin mDia1 along the double helical strand of an actin filament
    • Mizuno, H. et al. Rotational movement of the formin mDia1 along the double helical strand of an actin filament. Science 331, 80-83 (2011).
    • (2011) Science , vol.331 , pp. 80-83
    • Mizuno, H.1
  • 51
    • 84878982264 scopus 로고    scopus 로고
    • Tension modulates actin filament polymerization mediated by formin and profilin
    • Courtemanche, N., Lee, J. Y., Pollard, T. D. & Greene, E. C. Tension modulates actin filament polymerization mediated by formin and profilin. Proc. Natl Acad. Sci. USA 110, 9752-9757 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , pp. 9752-9757
    • Courtemanche, N.1    Lee, J.Y.2    Pollard, T.D.3    Greene, E.C.4
  • 52
    • 84878722228 scopus 로고    scopus 로고
    • Formin mDia1 senses and generates mechanical forces on actin filaments
    • Jegou, A., Carlier, M. F. & Romet-Lemonne, G. Formin mDia1 senses and generates mechanical forces on actin filaments. Nat. Commun. 4, 1883 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 1883
    • Jegou, A.1    Carlier, M.F.2    Romet-Lemonne, G.3
  • 53
    • 0020421078 scopus 로고
    • Cytostructural dynamics of spreading and translocating cells
    • Soranno, T. & Bell, E. Cytostructural dynamics of spreading and translocating cells. J. Cell Biol. 95, 127-136 (1982).
    • (1982) J. Cell Biol. , vol.95 , pp. 127-136
    • Soranno, T.1    Bell, E.2
  • 54
    • 33645749163 scopus 로고    scopus 로고
    • Type ID unconventional myosin controls left-right asymmetry in Drosophila
    • Speder, P., Adam, G. & Noselli, S. Type ID unconventional myosin controls left-right asymmetry in Drosophila. Nature 440, 803-807 (2006).
    • (2006) Nature , vol.440 , pp. 803-807
    • Speder, P.1    Adam, G.2    Noselli, S.3
  • 55
    • 33645748910 scopus 로고    scopus 로고
    • An unconventional myosin in Drosophila reverses the default handedness in visceral organs
    • Hozumi, S. et al. An unconventional myosin in Drosophila reverses the default handedness in visceral organs. Nature 440, 798-802 (2006).
    • (2006) Nature , vol.440 , pp. 798-802
    • Hozumi, S.1
  • 56
    • 33846270046 scopus 로고    scopus 로고
    • Left-right asymmetry: Class i myosins show the direction
    • Speder, P. & Noselli, S. Left-right asymmetry: class I myosins show the direction. Curr. Opin. Cell Biol. 19, 82-87 (2007).
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 82-87
    • Speder, P.1    Noselli, S.2
  • 57
    • 84925964136 scopus 로고    scopus 로고
    • Active torque generation by the actomyosin cell cortex drives left-right symmetry breaking
    • Naganathan, S. R., Furthauer, S., Nishikawa, M., Julicher, F. & Grill, S. W. Active torque generation by the actomyosin cell cortex drives left-right symmetry breaking. eLife 3, e04165 (2014).
    • (2014) ELife , vol.3 , pp. e04165
    • Naganathan, S.R.1    Furthauer, S.2    Nishikawa, M.3    Julicher, F.4    Grill, S.W.5
  • 59
    • 33646861953 scopus 로고    scopus 로고
    • Cell distribution of stress fibres in response to the geometry of the adhesive environment
    • Thery, M., Pepin, A., Dressaire, E., Chen, Y. & Bornens, M. Cell distribution of stress fibres in response to the geometry of the adhesive environment. Cell Motil. Cytoskeleton 63, 341-355 (2006).
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 341-355
    • Thery, M.1    Pepin, A.2    Dressaire, E.3    Chen, Y.4    Bornens, M.5
  • 60
    • 0000373736 scopus 로고
    • Techniques for the preservation of 3-dimensional structure in preparing specimens for the electron microscope
    • Anderson, T. F. Techniques for the preservation of 3-dimensional structure in preparing specimens for the electron microscope. Trans. N. Y. Acad. Sci. 13, 130-134 (1951).
    • (1951) Trans. N. Y. Acad. Sci. , vol.13 , pp. 130-134
    • Anderson, T.F.1
  • 61
    • 0016817745 scopus 로고
    • Electron-microscopy of critical-point dried whole cultured-cells
    • Buckley, I. K. & Porter, K. R. Electron-microscopy of critical-point dried whole cultured-cells. J. Microsc. 104, 107-120 (1975).
    • (1975) J. Microsc. , vol.104 , pp. 107-120
    • Buckley, I.K.1    Porter, K.R.2
  • 62
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Struct. Biol. 152, 36-51 (2005).
    • (2005) J. Struct. Biol. , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 63
    • 0029879295 scopus 로고    scopus 로고
    • Computer visualization of threedimensional image data using IMOD
    • Kremer, J. R., Mastronarde, D. N. & McIntosh, J. R. Computer visualization of threedimensional image data using IMOD. J. Struct. Biol. 116, 71-76 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 71-76
    • Kremer, J.R.1    Mastronarde, D.N.2    McIntosh, J.R.3
  • 64
    • 33846538739 scopus 로고    scopus 로고
    • The power stroke of myosin VI and the basis of reverse directionality
    • Bryant, Z., Altman, D. & Spudich, J. A. The power stroke of myosin VI and the basis of reverse directionality. Proc. Natl Acad. Sci. USA 104, 772-777 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 772-777
    • Bryant, Z.1    Altman, D.2    Spudich, J.A.3
  • 65
    • 0034431113 scopus 로고    scopus 로고
    • In vitro assays of processive myosin motors
    • Rock, R. S., Rief, M., Mehta, A. D. & Spudich, J. A. In vitro assays of processive myosin motors. Methods 22, 373-381 (2000).
    • (2000) Methods , vol.22 , pp. 373-381
    • Rock, R.S.1    Rief, M.2    Mehta, A.D.3    Spudich, J.A.4
  • 66
    • 33645028600 scopus 로고    scopus 로고
    • Folding DNA to create nanoscale shapes and patterns
    • Rothemund, P. W. K. Folding DNA to create nanoscale shapes and patterns. Nature 440, 297-302 (2006).
    • (2006) Nature , vol.440 , pp. 297-302
    • Rothemund, P.W.K.1
  • 67
    • 70449721124 scopus 로고    scopus 로고
    • Coupled myosin VI motors facilitate unidirectional movement on an F-Actin network
    • Sivaramakrishnan, S. & Spudich, J. A. Coupled myosin VI motors facilitate unidirectional movement on an F-Actin network. J. Cell Biol. 187, 53-60 (2009).
    • (2009) J. Cell Biol. , vol.187 , pp. 53-60
    • Sivaramakrishnan, S.1    Spudich, J.A.2
  • 68
    • 0026031862 scopus 로고
    • Evidence that intermediate filament reorganization is induced by Atp-dependent contraction of the actomyosin cortex in permeabilized fibroblasts
    • Tint, I. S., Hollenbeck, P. J., Verkhovsky, A. B., Surgucheva, I. G. & Bershadsky, A. D. Evidence that intermediate filament reorganization is induced by Atp-dependent contraction of the actomyosin cortex in permeabilized fibroblasts. J. Cell Sci. 98, 375-384 (1991).
    • (1991) J. Cell Sci. , vol.98 , pp. 375-384
    • Tint, I.S.1    Hollenbeck, P.J.2    Verkhovsky, A.B.3    Surgucheva, I.G.4    Bershadsky, A.D.5
  • 69
    • 33746221673 scopus 로고    scopus 로고
    • Assembly dynamics of microtubules at molecular resolution
    • Kerssemakers, J. W. et al. Assembly dynamics of microtubules at molecular resolution. Nature 442, 709-712 (2006).
    • (2006) Nature , vol.442 , pp. 709-712
    • Kerssemakers, J.W.1
  • 70
    • 0023871621 scopus 로고
    • Tracking kinesin-driven movements with nanometre-scale precision
    • Gelles, J., Schnapp, B. J. & Sheetz, M. P. Tracking kinesin-driven movements with nanometre-scale precision. Nature 331, 450-453 (1988).
    • (1988) Nature , vol.331 , pp. 450-453
    • Gelles, J.1    Schnapp, B.J.2    Sheetz, M.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.