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Volumn 94, Issue 8, 2008, Pages 2955-2964

Cytoskeletal bundle mechanics

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BIOMECHANICS; CHEMICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; CONFORMATION; CYTOSKELETON; ELASTICITY; MECHANICAL STRESS; METHODOLOGY; MICROFILAMENT; ULTRASTRUCTURE;

EID: 43149102725     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1529/biophysj.107.119743     Document Type: Article
Times cited : (141)

References (87)
  • 2
    • 0033981223 scopus 로고    scopus 로고
    • Parallel actin bundles and their multiple actin-bundling proteins
    • Bartles, J. R. 2000. Parallel actin bundles and their multiple actin-bundling proteins. Curr. Opin. Cell Biol. 12:72-78.
    • (2000) Curr. Opin. Cell Biol , vol.12 , pp. 72-78
    • Bartles, J.R.1
  • 3
    • 3543083870 scopus 로고    scopus 로고
    • The co-workers of actin filaments: From cell structures to signals
    • Revenu, C., R. Athman, S. Robine, and D. Louvard. 2004. The co-workers of actin filaments: from cell structures to signals. Nat. Rev. Mol. Cell Biol. 5:635-646.
    • (2004) Nat. Rev. Mol. Cell Biol , vol.5 , pp. 635-646
    • Revenu, C.1    Athman, R.2    Robine, S.3    Louvard, D.4
  • 4
    • 0001166495 scopus 로고
    • Sensitivity, polarity, and conductance change in response of vertebrate hair cells to controlled mechanical stimuli
    • Hudspeth, A. J., and D. P. Corey. 1977. Sensitivity, polarity, and conductance change in response of vertebrate hair cells to controlled mechanical stimuli. Proc. Natl. Acad. Sci. USA. 74:2407-2411.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 2407-2411
    • Hudspeth, A.J.1    Corey, D.P.2
  • 5
    • 0022624024 scopus 로고
    • Electrokinetic shape changes of cochlear outer hair cells
    • Kachar, B., W. E. Brownell, R. Altschuler, and J. Fex. 1986. Electrokinetic shape changes of cochlear outer hair cells. Nature. 322:365-368.
    • (1986) Nature , vol.322 , pp. 365-368
    • Kachar, B.1    Brownell, W.E.2    Altschuler, R.3    Fex, J.4
  • 7
    • 2942651287 scopus 로고    scopus 로고
    • Cell mechanics and mechanotransduction: Pathways, probes, and physiology
    • Huang, H. D., R. D. Kamm, and R. T. Lee. 2004. Cell mechanics and mechanotransduction: pathways, probes, and physiology. Am. J. Physiol. Cell Physiol. 287:C1-C11.
    • (2004) Am. J. Physiol. Cell Physiol , vol.287
    • Huang, H.D.1    Kamm, R.D.2    Lee, R.T.3
  • 8
    • 33646179573 scopus 로고    scopus 로고
    • Viscoelastic retraction of single living stress fibers and its impact on cell shape, cytoskeletal organization, and extracellular matrix mechanics
    • Kumar, S., I. Z. Maxwell, A. Heisterkamp, T. R. Polte, T. P. Lele, M. Salanga, E. Mazur, and D. E. Ingber. 2006. Viscoelastic retraction of single living stress fibers and its impact on cell shape, cytoskeletal organization, and extracellular matrix mechanics. Biophys. J. 90:3762-3773.
    • (2006) Biophys. J , vol.90 , pp. 3762-3773
    • Kumar, S.1    Maxwell, I.Z.2    Heisterkamp, A.3    Polte, T.R.4    Lele, T.P.5    Salanga, M.6    Mazur, E.7    Ingber, D.E.8
  • 9
    • 0027221483 scopus 로고
    • Cellular tensegrity: Defining new rules of biological design that govern the cytoskeleton
    • Ingber, D. E. 1993. Cellular tensegrity: defining new rules of biological design that govern the cytoskeleton. J. Cell Sci. 104:613-627.
    • (1993) J. Cell Sci , vol.104 , pp. 613-627
    • Ingber, D.E.1
  • 10
    • 33646386142 scopus 로고    scopus 로고
    • Stress fibers are generated by two distinct actin assembly mechanisms in motile cells
    • Hotulainen, P., and P. Lappalainen. 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
  • 12
    • 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., M. Siebert, and T. J. Mitchison. 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
  • 13
    • 0035997133 scopus 로고    scopus 로고
    • Buckling of actin stress fibers: A new wrinkle in the cytoskeletal tapestry
    • Costa, K. D., W. J. Hucker, and F. C. P. Yin. 2002. Buckling of actin stress fibers: a new wrinkle in the cytoskeletal tapestry. Cell Motil. Cytoskeleton. 52:266-274.
    • (2002) Cell Motil. Cytoskeleton , vol.52 , pp. 266-274
    • Costa, K.D.1    Hucker, W.J.2    Yin, F.C.P.3
  • 14
    • 0026611050 scopus 로고
    • Complementarity between sperm surface β-1,4-galactosyl-transferase and egg-coat Zp3 mediates sperm egg binding
    • Miller, D. J., M. B. Macek, and B. D. Shur. 1992. Complementarity between sperm surface β-1,4-galactosyl-transferase and egg-coat Zp3 mediates sperm egg binding. Nature. 357:589-593.
    • (1992) Nature , vol.357 , pp. 589-593
    • Miller, D.J.1    Macek, M.B.2    Shur, B.D.3
  • 16
    • 23244441861 scopus 로고    scopus 로고
    • The physics of filopodial protrusion
    • Mogilner, A., and B. Rubinstein. 2005. The physics of filopodial protrusion. Biophys. J. 89:782-795.
    • (2005) Biophys. J , vol.89 , pp. 782-795
    • Mogilner, A.1    Rubinstein, B.2
  • 17
    • 33646164411 scopus 로고    scopus 로고
    • Mechanics and dynamics of actin-driven thin membrane protrusions
    • Atilgan, E., D. Wirtz, and S. X. Sun. 2006. Mechanics and dynamics of actin-driven thin membrane protrusions. Biophys. J. 90:65-76.
    • (2006) Biophys. J , vol.90 , pp. 65-76
    • Atilgan, E.1    Wirtz, D.2    Sun, S.X.3
  • 22
    • 33644775671 scopus 로고    scopus 로고
    • Myosin II functions in actin-bundle turnover in neuronal growth cones
    • Medeiros, N. A., D. T. Burnette, and P. Forscher. 2006. Myosin II functions in actin-bundle turnover in neuronal growth cones. Nat. Cell Biol. 8:215-226.
    • (2006) Nat. Cell Biol , vol.8 , pp. 215-226
    • Medeiros, N.A.1    Burnette, D.T.2    Forscher, P.3
  • 24
    • 33749159663 scopus 로고    scopus 로고
    • Self-organization of microtubule bundles in anucleate fission yeast cells
    • Daga, R. R., K. G. Lee, S. Bratman, S. Salas-Pino, and F. Chang. 2006. Self-organization of microtubule bundles in anucleate fission yeast cells. Nat. Cell Biol. 8:1108-1113.
    • (2006) Nat. Cell Biol , vol.8 , pp. 1108-1113
    • Daga, R.R.1    Lee, K.G.2    Bratman, S.3    Salas-Pino, S.4    Chang, F.5
  • 25
    • 0030801830 scopus 로고    scopus 로고
    • Mechanics of microtubule bundles in pillar cells from the inner ear
    • Tolomeo, J. A., and M. C. Holley. 1997. Mechanics of microtubule bundles in pillar cells from the inner ear. Biophys. J. 73:2241-2247.
    • (1997) Biophys. J , vol.73 , pp. 2241-2247
    • Tolomeo, J.A.1    Holley, M.C.2
  • 29
    • 33748264168 scopus 로고    scopus 로고
    • Actin-binding proteins sensitively mediate F-actin bundle stiffness
    • Claessens, M. M. A. E., M. Bathe, E. Frey, and A. R. Bausch. 2006. Actin-binding proteins sensitively mediate F-actin bundle stiffness. Nat. Mater. 5:748-753.
    • (2006) Nat. Mater , vol.5 , pp. 748-753
    • Claessens, M.M.A.E.1    Bathe, M.2    Frey, E.3    Bausch, A.R.4
  • 32
    • 0020570679 scopus 로고
    • Actin filaments, stereocilia, and hair cells of the bird cochlea. II. Packing of actin filaments in the stereocilia and in the cuticular plate and what happens to the organization when the stereocilia are bent
    • Tilney, L. G., E. H. Egelman, D. J. DeRosier, and J. C. Saunders. 1983. Actin filaments, stereocilia, and hair cells of the bird cochlea. II. Packing of actin filaments in the stereocilia and in the cuticular plate and what happens to the organization when the stereocilia are bent. J. Cell Biol. 96:822-834.
    • (1983) J. Cell Biol , vol.96 , pp. 822-834
    • Tilney, L.G.1    Egelman, E.H.2    DeRosier, D.J.3    Saunders, J.C.4
  • 35
    • 34548238660 scopus 로고    scopus 로고
    • Chirality and equilibrium biopolymer bundles
    • Grason, G. M., and R. F. Bruinsma. 2007. Chirality and equilibrium biopolymer bundles. Phys. Rev. Lett. 99:098101.
    • (2007) Phys. Rev. Lett , vol.99 , pp. 098101
    • Grason, G.M.1    Bruinsma, R.F.2
  • 36
    • 33845542919 scopus 로고    scopus 로고
    • Elasticity of α-helical coiled coils
    • Wolgemuth, C. W., and S. X. Sun. 2006. Elasticity of α-helical coiled coils. Phys. Rev. Lett. 97:248101.
    • (2006) Phys. Rev. Lett , vol.97 , pp. 248101
    • Wolgemuth, C.W.1    Sun, S.X.2
  • 37
    • 0022517584 scopus 로고
    • Stiffness of sensory hair bundles in the sacculus of the frog
    • Howard, J., and J. F. Ashmore. 1986. Stiffness of sensory hair bundles in the sacculus of the frog. Hear. Res. 23:93-104.
    • (1986) Hear. Res , vol.23 , pp. 93-104
    • Howard, J.1    Ashmore, J.F.2
  • 38
    • 76649125304 scopus 로고
    • Fluctuations and stiffness of double-stranded polymers: Railway-track model
    • Everaers, R., R. Bundschuh, and K. Kremer. 1995. Fluctuations and stiffness of double-stranded polymers: railway-track model. Europhys. Lett. 29:263-268.
    • (1995) Europhys. Lett , vol.29 , pp. 263-268
    • Everaers, R.1    Bundschuh, R.2    Kremer, K.3
  • 40
    • 0027533269 scopus 로고
    • Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape
    • Gittes, F., B. Mickey, J. Nettleton, and J. Howard. 1993. Flexural rigidity of microtubules and actin filaments measured from thermal fluctuations in shape. J. Cell Biol. 120:923-934.
    • (1993) J. Cell Biol , vol.120 , pp. 923-934
    • Gittes, F.1    Mickey, B.2    Nettleton, J.3    Howard, J.4
  • 41
    • 0028607563 scopus 로고
    • Direct measurement of stiffness of single actin-filaments with and without tropomyosin by in-vitro nanomanipulation
    • Kojima, H., A. Ishijima, and T. Yanagida. 1994. Direct measurement of stiffness of single actin-filaments with and without tropomyosin by in-vitro nanomanipulation. Proc. Natl. Acad. Sci. USA. 91:12962-12966.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12962-12966
    • Kojima, H.1    Ishijima, A.2    Yanagida, T.3
  • 42
    • 33745893239 scopus 로고    scopus 로고
    • Thermal fluctuations of grafted microtubules provide evidence of a length-dependent persistence length
    • Pampaloni, F., G. Lattanzi, A. Jonas, T. Surrey, E. Frey, and E. L. Florin. 2006. Thermal fluctuations of grafted microtubules provide evidence of a length-dependent persistence length. Proc. Natl. Acad. Sci. USA. 103:10248-10253.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10248-10253
    • Pampaloni, F.1    Lattanzi, G.2    Jonas, A.3    Surrey, T.4    Frey, E.5    Florin, E.L.6
  • 43
    • 0035947761 scopus 로고    scopus 로고
    • An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function
    • Volkmann, N., D. DeRosier, P. Matsudaira, and D. Hanein. 2001. An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function. J. Cell Biol. 153:947-956.
    • (2001) J. Cell Biol , vol.153 , pp. 947-956
    • Volkmann, N.1    DeRosier, D.2    Matsudaira, P.3    Hanein, D.4
  • 45
    • 0027787491 scopus 로고
    • Analysis of filamin and alpha-actinin binding to actin by the stopped-flow method
    • Goldmann, W. H., and G. Isenberg. 1993. Analysis of filamin and alpha-actinin binding to actin by the stopped-flow method. FEBS Lett. 336:408-410.
    • (1993) FEBS Lett , vol.336 , pp. 408-410
    • Goldmann, W.H.1    Isenberg, G.2
  • 46
    • 0035816209 scopus 로고    scopus 로고
    • Micromechanics and ultrastructure of actin filament networks crosslinked by human fascin: A comparison with alpha-actinin
    • Tseng, Y., E. Fedorov, J. M. McCaffery, S. C. Almo, and D. Wirtz. 2001. Micromechanics and ultrastructure of actin filament networks crosslinked by human fascin: a comparison with alpha-actinin. J. Mol. Biol. 310:351-366.
    • (2001) J. Mol. Biol , vol.310 , pp. 351-366
    • Tseng, Y.1    Fedorov, E.2    McCaffery, J.M.3    Almo, S.C.4    Wirtz, D.5
  • 47
    • 0142091375 scopus 로고    scopus 로고
    • Kinks, rings, and rackets in filamentous structures
    • Cohen, A. E., and L. Mahadevan. 2003. Kinks, rings, and rackets in filamentous structures. Proc. Natl. Acad. Sci. USA. 100:12141-12146.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12141-12146
    • Cohen, A.E.1    Mahadevan, L.2
  • 48
    • 42749107973 scopus 로고    scopus 로고
    • Self-propagating patterns in active filament bundles
    • Kruse, K., S. Camalet, and F. Julicher. 2001. Self-propagating patterns in active filament bundles. Phys. Rev. Lett. 87:138191.
    • (2001) Phys. Rev. Lett , vol.87 , pp. 138191
    • Kruse, K.1    Camalet, S.2    Julicher, F.3
  • 49
    • 42749099121 scopus 로고    scopus 로고
    • Self-organization and mechanical properties of active filament bundles
    • Kruse, K., and F. Julicher. 2003. Self-organization and mechanical properties of active filament bundles. Phys. Rev. E Stat. Nonlin. Soft Matter Phys. 67:051913.
    • (2003) Phys. Rev. E Stat. Nonlin. Soft Matter Phys , vol.67 , pp. 051913
    • Kruse, K.1    Julicher, F.2
  • 51
    • 0019840118 scopus 로고
    • Organization of actin in the leading edge of cultured cells: Influence of osmium tetroxide and dehydration on the ultrastructure of actin meshworks
    • Small, J. V. 1981. Organization of actin in the leading edge of cultured cells: influence of osmium tetroxide and dehydration on the ultrastructure of actin meshworks. J. Cell Biol. 91:695-705.
    • (1981) J. Cell Biol , vol.91 , pp. 695-705
    • Small, J.V.1
  • 52
    • 0001604770 scopus 로고
    • The statistical mechanical theory of stiff chains
    • Saitô, N., K. Takahashi, and Y. Yunoki. 1967. The statistical mechanical theory of stiff chains. J. Phys. Soc. Jpn. 22:219-226.
    • (1967) J. Phys. Soc. Jpn , vol.22 , pp. 219-226
    • Saitô, N.1    Takahashi, K.2    Yunoki, Y.3
  • 53
    • 36849105157 scopus 로고
    • Statistical mechanics of wormlike chains: Path integral and diagram methods
    • Yamakawa, H. 1973. Statistical mechanics of wormlike chains: path integral and diagram methods. J. Chem. Phys. 59:3811-3815.
    • (1973) J. Chem. Phys , vol.59 , pp. 3811-3815
    • Yamakawa, H.1
  • 54
    • 34547467105 scopus 로고    scopus 로고
    • Statistical mechanics of semiflexible bundles of wormlike polymer chains
    • Heussinger, C., M. Bathe, and E. Frey. 2007. Statistical mechanics of semiflexible bundles of wormlike polymer chains. Phys. Rev. Lett. 99:048101.
    • (2007) Phys. Rev. Lett , vol.99 , pp. 048101
    • Heussinger, C.1    Bathe, M.2    Frey, E.3
  • 59
    • 0141545013 scopus 로고    scopus 로고
    • Long continuous actin bundles in Drosophila bristles are constructed by overlapping short filaments
    • Guild, G. M., P. S. Connelly, L. Ruggiero, K. A. Vranich, and L. G. Tilney. 2003. Long continuous actin bundles in Drosophila bristles are constructed by overlapping short filaments. J. Cell Biol. 162:1069-1077.
    • (2003) J. Cell Biol , vol.162 , pp. 1069-1077
    • Guild, G.M.1    Connelly, P.S.2    Ruggiero, L.3    Vranich, K.A.4    Tilney, L.G.5
  • 60
    • 0029046139 scopus 로고
    • Flexibility of actin filaments derived from thermal fluctuations: Effect of bound nucleotide, phalloidin, and muscle regulatory proteins
    • Isambert, H., P. Venier, A. C. Maggs, A. Fattoum, R. Kassab, D. Pantaloni, and M. F. Carlier. 1995. Flexibility of actin filaments derived from thermal fluctuations: effect of bound nucleotide, phalloidin, and muscle regulatory proteins. J. Biol. Chem. 270:11437-11444.
    • (1995) J. Biol. Chem , vol.270 , pp. 11437-11444
    • Isambert, H.1    Venier, P.2    Maggs, A.C.3    Fattoum, A.4    Kassab, R.5    Pantaloni, D.6    Carlier, M.F.7
  • 61
    • 0034627855 scopus 로고    scopus 로고
    • Regulation of actin filament cross-linking and bundle shape in Drosophila bristles
    • Tilney, L. G., P. S. Connelly, K. A. Vranich, M. K. Shaw, and G. M. Guild. 2000. Regulation of actin filament cross-linking and bundle shape in Drosophila bristles. J. Cell Biol. 148:87-99.
    • (2000) J. Cell Biol , vol.148 , pp. 87-99
    • Tilney, L.G.1    Connelly, P.S.2    Vranich, K.A.3    Shaw, M.K.4    Guild, G.M.5
  • 63
    • 39749171104 scopus 로고    scopus 로고
    • A finite element framework for computation of protein normal modes and mechanical response
    • Bathe, M. 2007. A finite element framework for computation of protein normal modes and mechanical response. Proteins. 70:1595-1609.
    • (2007) Proteins , vol.70 , pp. 1595-1609
    • Bathe, M.1
  • 64
    • 1442348236 scopus 로고    scopus 로고
    • Bending stiffness of a crystalline actin bundle
    • Shin, J. H., L. Mahadevan, P. T. So, and P. Matsudaira. 2004. Bending stiffness of a crystalline actin bundle. J. Mol. Biol. 337:255-261.
    • (2004) J. Mol. Biol , vol.337 , pp. 255-261
    • Shin, J.H.1    Mahadevan, L.2    So, P.T.3    Matsudaira, P.4
  • 65
    • 0016431173 scopus 로고
    • Actin filaments in acrosomal reaction of limulus sperm: Motion generated by alterations in the packing of the filaments
    • Tilney, L. G. 1975. Actin filaments in acrosomal reaction of limulus sperm: motion generated by alterations in the packing of the filaments. J. Cell Biol. 64:289-310.
    • (1975) J. Cell Biol , vol.64 , pp. 289-310
    • Tilney, L.G.1
  • 66
    • 0026677618 scopus 로고
    • Actin filaments, stereocilia, and hair cells: How cells count and measure
    • Tilney, L. G., M. S. Tilney, and D. J. Derosier. 1992. Actin filaments, stereocilia, and hair cells: how cells count and measure. Annu. Rev. Cell Biol. 8:257-274.
    • (1992) Annu. Rev. Cell Biol , vol.8 , pp. 257-274
    • Tilney, L.G.1    Tilney, M.S.2    Derosier, D.J.3
  • 67
    • 0033572941 scopus 로고    scopus 로고
    • Studies on the cellular basis of morphogenesis in the sea urchin embryo: Directed movements of primary mesenchyme cells in normal and vegetalized larvae
    • Gustafson, T., and L. Wolpert. 1999. Studies on the cellular basis of morphogenesis in the sea urchin embryo: directed movements of primary mesenchyme cells in normal and vegetalized larvae. Exp. Cell Res. 253:288-295.
    • (1999) Exp. Cell Res , vol.253 , pp. 288-295
    • Gustafson, T.1    Wolpert, L.2
  • 68
    • 0030471362 scopus 로고    scopus 로고
    • actin bundles in Drosophila bristles are assembled from modules composed of short filaments
    • Tilney, L. G., P. Connelly, S. Smith, and G. M. Guild. 1996. actin bundles in Drosophila bristles are assembled from modules composed of short filaments. J. Cell Biol. 135:1291-1308.
    • (1996) J. Cell Biol , vol.135 , pp. 1291-1308
    • Tilney, L.G.1    Connelly, P.2    Smith, S.3    Guild, G.M.4
  • 69
    • 0034979287 scopus 로고    scopus 로고
    • Probing the relation between force - lifetime - and chemistry in single molecular bonds
    • Evans E. 2001. Probing the relation between force - lifetime - and chemistry in single molecular bonds. Annu. Rev. Biophys. Biomol. Struct. 30:105-128.
    • (2001) Annu. Rev. Biophys. Biomol. Struct , vol.30 , pp. 105-128
    • Evans, E.1
  • 70
    • 0018101150 scopus 로고
    • Models for specific adhesion of cells to cells
    • Bell, G. I. 1978. Models for specific adhesion of cells to cells. Science. 200:618-627.
    • (1978) Science , vol.200 , pp. 618-627
    • Bell, G.I.1
  • 71
    • 0031001349 scopus 로고    scopus 로고
    • Dynamic strength of molecular adhesion bonds
    • Evans, E., K. Ritchie. 1997. Dynamic strength of molecular adhesion bonds. Biophys. J. 72:1541-1555.
    • (1997) Biophys. J , vol.72 , pp. 1541-1555
    • Evans, E.1    Ritchie, K.2
  • 72
    • 0029822651 scopus 로고    scopus 로고
    • Torsional rigidity of single actin filaments and actin-actin bond breaking force under torsion measured directly by in vitro micromanipulation
    • Tsuda, Y., H. Yasutake, A. Ishijima, and T. Yanagida. 1996. Torsional rigidity of single actin filaments and actin-actin bond breaking force under torsion measured directly by in vitro micromanipulation. Proc. Natl. Acad. Sci. USA. 93:12937-12942.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12937-12942
    • Tsuda, Y.1    Yasutake, H.2    Ishijima, A.3    Yanagida, T.4
  • 76
    • 8944235343 scopus 로고    scopus 로고
    • Theoretical estimates of mechanical properties of the endothelial cell cytoskeleton
    • Satcher, R. L., and C. F. Dewey. 1996. Theoretical estimates of mechanical properties of the endothelial cell cytoskeleton. Biophys. J. 71:109-118.
    • (1996) Biophys. J , vol.71 , pp. 109-118
    • Satcher, R.L.1    Dewey, C.F.2
  • 78
    • 0018898773 scopus 로고
    • The Croonian lecture, 1978: The crawling movement of metazoan cells
    • Abercrombie, M. 1980. The Croonian lecture, 1978: the crawling movement of metazoan cells. Proc. R. Soc. Lond. B. 207:129-147.
    • (1980) Proc. R. Soc. Lond. B , vol.207 , pp. 129-147
    • Abercrombie, M.1
  • 82
    • 9444287085 scopus 로고    scopus 로고
    • The role actin filaments play in providing the characteristic curved form of Drosophila bristles
    • Tilney, L. G., P. S. Connelly, L. Ruggiero, K. A. Vranich, G. M. Guild, and D. DeRosier. 2004. The role actin filaments play in providing the characteristic curved form of Drosophila bristles. Mol. Biol. Cell. 15:5481-5491.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5481-5491
    • Tilney, L.G.1    Connelly, P.S.2    Ruggiero, L.3    Vranich, K.A.4    Guild, G.M.5    DeRosier, D.6
  • 83
    • 0031037153 scopus 로고    scopus 로고
    • Identification of an actin binding region and a protein kinase C phosphorylation site on human fascin
    • Ono, S., Y. Yamakita, S. Yamashiro, P. T. Matsudaira, J. R. Gnarra, T. Obinata, and F. Matsumura. 1997. Identification of an actin binding region and a protein kinase C phosphorylation site on human fascin. J. Biol. Chem. 272:2527-2533.
    • (1997) J. Biol. Chem , vol.272 , pp. 2527-2533
    • Ono, S.1    Yamakita, Y.2    Yamashiro, S.3    Matsudaira, P.T.4    Gnarra, J.R.5    Obinata, T.6    Matsumura, F.7
  • 84
    • 15844362435 scopus 로고    scopus 로고
    • Phosphorylation of human fascin inhibits its actin binding and bundling activities
    • Yamakita, Y., S. Ono, F. Matsumura, and S. Yamashiro. 1996. Phosphorylation of human fascin inhibits its actin binding and bundling activities. J. Biol. Chem. 271:12632-12638.
    • (1996) J. Biol. Chem , vol.271 , pp. 12632-12638
    • Yamakita, Y.1    Ono, S.2    Matsumura, F.3    Yamashiro, S.4
  • 85
    • 0026472782 scopus 로고
    • Assembly of the intestinal brush-border cytoskeleton
    • Heintzelman, M. B., and M. S. Mooseker. 1992. Assembly of the intestinal brush-border cytoskeleton. Curr. Top. Dev. Biol. 26:93-122.
    • (1992) Curr. Top. Dev. Biol , vol.26 , pp. 93-122
    • Heintzelman, M.B.1    Mooseker, M.S.2


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