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Volumn 128, Issue 12, 2015, Pages 2209-2217

The contractome - A systems view of actomyosin contractility in non-muscle cells

Author keywords

Contractility; Myosin II; Non muscle cells

Indexed keywords

ACTIN; CALCIUM; CELL PROTEIN; CONTRACTOME; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; REGULATOR PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; SCAFFOLD PROTEIN; STRUCTURAL PROTEIN; UNCLASSIFIED DRUG;

EID: 84932098853     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.170068     Document Type: Article
Times cited : (66)

References (132)
  • 1
    • 84892834113 scopus 로고    scopus 로고
    • Myosin II in mechanotransduction: master and commander of cell migration, morphogenesis, and cancer
    • Aguilar-Cuenca, R., Juanes-García, A. and Vicente-Manzanares, M. (2014). Myosin II in mechanotransduction: master and commander of cell migration, morphogenesis, and cancer. Cell. Mol. Life Sci. 71, 479-492.
    • (2014) Cell. Mol. Life Sci , vol.71 , pp. 479-492
    • Aguilar-Cuenca, R.1    Juanes-García, A.2    Vicente-Manzanares, M.3
  • 2
    • 82455168277 scopus 로고    scopus 로고
    • Analysis of the role of Ser1/Ser2/Thr9 phosphorylation on myosin II assembly and function in live cells
    • Beach, J. R., Licate, L. S., Crish, J. F. and Egelhoff, T. T. (2011). Analysis of the role of Ser1/Ser2/Thr9 phosphorylation on myosin II assembly and function in live cells. BMC Cell Biol. 12, 52.
    • (2011) BMC Cell Biol , vol.12 , pp. 52
    • Beach, J.R.1    Licate, L.S.2    Crish, J.F.3    Egelhoff, T.T.4
  • 3
    • 84901230786 scopus 로고    scopus 로고
    • Nonmuscle myosin II isoforms coassemble in living cells
    • Beach, J. R., Shao, L., Remmert, K., Li, D., Betzig, E. and Hammer, J. A., III. (2014). Nonmuscle myosin II isoforms coassemble in living cells. Curr. Biol. 24, 1160-1166.
    • (2014) Curr. Biol , vol.24 , pp. 1160-1166
    • Beach, J.R.1    Shao, L.2    Remmert, K.3    Li, D.4    Betzig, E.5    Hammer, J.A.6
  • 4
    • 33646410929 scopus 로고    scopus 로고
    • Distinct roles of nonmuscle myosin II isoforms in the regulation of MDA-MB-231 breast cancer cell spreading and migration
    • Betapudi, V., Licate, L. S. and Egelhoff, T. T. (2006). Distinct roles of nonmuscle myosin II isoforms in the regulation of MDA-MB-231 breast cancer cell spreading and migration. Cancer Res. 66, 4725-4733.
    • (2006) Cancer Res , vol.66 , pp. 4725-4733
    • Betapudi, V.1    Licate, L.S.2    Egelhoff, T.T.3
  • 5
    • 55949123735 scopus 로고    scopus 로고
    • Filamentous network mechanics and active contractility determine cell and tissue shape
    • Bischofs, I. B., Klein, F., Lehnert, D., Bastmeyer, M. and Schwarz, U. S. (2008). Filamentous network mechanics and active contractility determine cell and tissue shape. Biophys. J. 95, 3488-3496.
    • (2008) Biophys. J , vol.95 , pp. 3488-3496
    • Bischofs, I.B.1    Klein, F.2    Lehnert, D.3    Bastmeyer, M.4    Schwarz, U.S.5
  • 6
    • 84891788593 scopus 로고    scopus 로고
    • The Mouse Genome Database: integration of and access to knowledge about the laboratory mouse
    • Blake, J. A., Bult, C. J., Eppig, J. T., Kadin, J. A. and Richardson, J. E.; The Mouse Genome Database Group. (2014). The Mouse Genome Database: integration of and access to knowledge about the laboratory mouse. Nucleic Acids Res. 42, D810-D817.
    • (2014) Nucleic Acids Res , vol.42 , pp. D810-D817
    • Blake, J.A.1    Bult, C.J.2    Eppig, J.T.3    Kadin, J.A.4    Richardson, J.E.5
  • 7
    • 56049099030 scopus 로고    scopus 로고
    • Mapping local matrix remodeling induced by a migrating tumor cell using three-dimensional multiple-particle tracking
    • Bloom, R. J., George, J. P., Celedon, A., Sun, S. X. and Wirtz, D. (2008). Mapping local matrix remodeling induced by a migrating tumor cell using three-dimensional multiple-particle tracking. Biophys. J. 95, 4077-4088.
    • (2008) Biophys. J , vol.95 , pp. 4077-4088
    • Bloom, R.J.1    George, J.P.2    Celedon, A.3    Sun, S.X.4    Wirtz, D.5
  • 8
    • 84876580870 scopus 로고    scopus 로고
    • The mouse genome database: genotypes, phenotypes, and models of human disease
    • Bult, C. J., Eppig, J. T., Blake, J. A., Kadin, J. A. and Richardson, J. E.; The Mouse Genome Database Group. (2013). The mouse genome database: genotypes, phenotypes, and models of human disease. Nucleic Acids Res. 41, D885-D891.
    • (2013) Nucleic Acids Res , vol.41 , pp. D885-D891
    • Bult, C.J.1    Eppig, J.T.2    Blake, J.A.3    Kadin, J.A.4    Richardson, J.E.5
  • 9
    • 46049083951 scopus 로고    scopus 로고
    • Myosin II activity facilitates microtubule bundling in the neuronal growth cone neck
    • Burnette, D. T., Ji, L., Schaefer, A. W., Medeiros, N. A., Danuser, G. and Forscher, P. (2008). Myosin II activity facilitates microtubule bundling in the neuronal growth cone neck. Dev. Cell 15, 163-169.
    • (2008) Dev. Cell , vol.15 , pp. 163-169
    • Burnette, D.T.1    Ji, L.2    Schaefer, A.W.3    Medeiros, N.A.4    Danuser, G.5    Forscher, P.6
  • 11
    • 77949834455 scopus 로고    scopus 로고
    • A nucleator arms race: cellular control of actin assembly
    • Campellone, K. G. and Welch, M. D. (2010). A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell Biol. 11, 237-251.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 237-251
    • Campellone, K.G.1    Welch, M.D.2
  • 12
    • 40849113363 scopus 로고    scopus 로고
    • Moesin and its activating kinase Slik are required for cortical stability and microtubule organization in mitotic cells
    • Carreno, S., Kouranti, I., Glusman, E. S., Fuller, M. T., Echard, A. and Payre, F. (2008). Moesin and its activating kinase Slik are required for cortical stability and microtubule organization in mitotic cells. J. Cell Biol. 180, 739-746.
    • (2008) J. Cell Biol , vol.180 , pp. 739-746
    • Carreno, S.1    Kouranti, I.2    Glusman, E.S.3    Fuller, M.T.4    Echard, A.5    Payre, F.6
  • 13
    • 0016690411 scopus 로고
    • The origin of nuclei and of eukaryotic cells
    • Cavalier-Smith, T. (1975). The origin of nuclei and of eukaryotic cells. Nature 256, 463-468.
    • (1975) Nature , vol.256 , pp. 463-468
    • Cavalier-Smith, T.1
  • 14
    • 0036208071 scopus 로고    scopus 로고
    • The phagotrophic origin of eukaryotes and phylogenetic classification of Protozoa
    • Cavalier-Smith, T. (2002). The phagotrophic origin of eukaryotes and phylogenetic classification of Protozoa. Int. J. Syst. Evol. Microbiol. 52, 297-354.
    • (2002) Int. J. Syst. Evol. Microbiol , vol.52 , pp. 297-354
    • Cavalier-Smith, T.1
  • 17
    • 84890533531 scopus 로고    scopus 로고
    • Emerin organizes actin flow for nuclear movement and centrosome orientation in migrating fibroblasts
    • Chang, W., Folker, E. S., Worman, H. J. and Gundersen, G. G. (2013). Emerin organizes actin flow for nuclear movement and centrosome orientation in migrating fibroblasts. Mol. Biol. Cell 24, 3869-3880.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 3869-3880
    • Chang, W.1    Folker, E.S.2    Worman, H.J.3    Gundersen, G.G.4
  • 18
    • 60749122102 scopus 로고    scopus 로고
    • Actin nucleation and elongation factors: mechanisms and interplay
    • Chesarone, M. A. and Goode, B. L. (2009). Actin nucleation and elongation factors: mechanisms and interplay. Curr. Opin. Cell Biol. 21, 28-37.
    • (2009) Curr. Opin. Cell Biol , vol.21 , pp. 28-37
    • Chesarone, M.A.1    Goode, B.L.2
  • 19
    • 72449124116 scopus 로고    scopus 로고
    • Material properties of the cell dictate stress-induced spreading and differentiation in embryonic stem cells
    • Chowdhury, F., Na, S., Li, D., Poh, Y.-C., Tanaka, T. S., Wang, F. and Wang, N. (2010). Material properties of the cell dictate stress-induced spreading and differentiation in embryonic stem cells. Nat. Mater. 9, 82-88.
    • (2010) Nat. Mater , vol.9 , pp. 82-88
    • Chowdhury, F.1    Na, S.2    Li, D.3    Poh, Y.-C.4    Tanaka, T.S.5    Wang, F.6    Wang, N.7
  • 20
    • 4744364577 scopus 로고    scopus 로고
    • Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice
    • Conti, M. A., Even-Ram, S., Liu, C., Yamada, K. M. and Adelstein, R. S. (2004). Defects in cell adhesion and the visceral endoderm following ablation of nonmuscle myosin heavy chain II-A in mice. J. Biol. Chem. 279, 41263-41266.
    • (2004) J. Biol. Chem , vol.279 , pp. 41263-41266
    • Conti, M.A.1    Even-Ram, S.2    Liu, C.3    Yamada, K.M.4    Adelstein, R.S.5
  • 21
    • 84878982264 scopus 로고    scopus 로고
    • Tension modulates actin filament polymerization mediated by formin and profilin
    • Courtemanche, N., Lee, J. Y., Pollard, T. D. and Greene, E. C. (2013). Tension modulates actin filament polymerization mediated by formin and profilin. Proc. Natl. Acad. Sci. USA 110, 9752-9757.
    • (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
  • 22
    • 18244385740 scopus 로고    scopus 로고
    • Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation
    • Dulyaninova, N. G., Malashkevich, V. N., Almo, S. C. and Bresnick, A. R. (2005). Regulation of myosin-IIA assembly and Mts1 binding by heavy chain phosphorylation. Biochemistry 44, 6867-6876.
    • (2005) Biochemistry , vol.44 , pp. 6867-6876
    • Dulyaninova, N.G.1    Malashkevich, V.N.2    Almo, S.C.3    Bresnick, A.R.4
  • 23
    • 0033588990 scopus 로고    scopus 로고
    • Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility
    • Egile, C., Loisel, T. P., Laurent, V., Li, R., Pantaloni, D., Sansonetti, P. J. and Carlier, M.-F. (1999). Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell Biol. 146, 1319-1332.
    • (1999) J. Cell Biol , vol.146 , pp. 1319-1332
    • Egile, C.1    Loisel, T.P.2    Laurent, V.3    Li, R.4    Pantaloni, D.5    Sansonetti, P.J.6    Carlier, M.-F.7
  • 24
    • 79960277917 scopus 로고    scopus 로고
    • A hitchhiker's guide to mechanobiology
    • Eyckmans, J., Boudou, T., Yu, X. and Chen, C. S. (2011). A hitchhiker's guide to mechanobiology. Dev. Cell 21, 35-47.
    • (2011) Dev. Cell , vol.21 , pp. 35-47
    • Eyckmans, J.1    Boudou, T.2    Yu, X.3    Chen, C.S.4
  • 26
    • 79960706295 scopus 로고    scopus 로고
    • The 'invisible hand': regulation of RHO GTPases by RHOGDIs
    • Garcia-Mata, R., Boulter, E. and Burridge, K. (2011). The 'invisible hand': regulation of RHO GTPases by RHOGDIs. Nat. Rev. Mol. Cell Biol. 12, 493-504.
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 493-504
    • Garcia-Mata, R.1    Boulter, E.2    Burridge, K.3
  • 27
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix and the cytoskeleton
    • Geiger, B., Bershadsky, A., Pankov, R. and Yamada, K. M. (2001). Transmembrane crosstalk between the extracellular matrix and the cytoskeleton. Nat. Rev. Mol. Cell Biol. 2, 793-805.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 28
    • 68849100412 scopus 로고    scopus 로고
    • Substrate topography induces a crossover from 2D to 3D behavior in fibroblast migration
    • Ghibaudo, M., Trichet, L., Le Digabel, J., Richert, A., Hersen, P. and Ladoux, B. (2009). Substrate topography induces a crossover from 2D to 3D behavior in fibroblast migration. Biophys. J. 97, 357-368.
    • (2009) Biophys. J , vol.97 , pp. 357-368
    • Ghibaudo, M.1    Trichet, L.2    Le Digabel, J.3    Richert, A.4    Hersen, P.5    Ladoux, B.6
  • 29
    • 80053319997 scopus 로고    scopus 로고
    • Dynamics of actomyosin contractile activity during epithelial morphogenesis
    • Gorfinkiel, N. and Blanchard, G. B. (2011). Dynamics of actomyosin contractile activity during epithelial morphogenesis. Curr. Opin. Cell Biol. 23, 531-539.
    • (2011) Curr. Opin. Cell Biol , vol.23 , pp. 531-539
    • Gorfinkiel, N.1    Blanchard, G.B.2
  • 30
    • 34748820092 scopus 로고    scopus 로고
    • Control of nuclear centration in the C. elegans zygote by receptorindependent Galpha signaling and myosin II
    • Goulding, M. B., Canman, J. C., Senning, E. N., Marcus, A. H. and Bowerman, B. (2007). Control of nuclear centration in the C. elegans zygote by receptorindependent Galpha signaling and myosin II. J. Cell Biol. 178, 1177-1191.
    • (2007) J. Cell Biol , vol.178 , pp. 1177-1191
    • Goulding, M.B.1    Canman, J.C.2    Senning, E.N.3    Marcus, A.H.4    Bowerman, B.5
  • 31
    • 79958753913 scopus 로고    scopus 로고
    • The myosin phosphatase targeting protein (MYPT) family: a regulated mechanism for achieving substrate specificity of the catalytic subunit of protein phosphatase type 1delta
    • Grassie, M. E., Moffat, L. D., Walsh, M. P. and MacDonald, J. A. (2011). The myosin phosphatase targeting protein (MYPT) family: a regulated mechanism for achieving substrate specificity of the catalytic subunit of protein phosphatase type 1delta. Arch. Biochem. Biophys. 510, 147-159.
    • (2011) Arch. Biochem. Biophys , vol.510 , pp. 147-159
    • Grassie, M.E.1    Moffat, L.D.2    Walsh, M.P.3    MacDonald, J.A.4
  • 33
    • 38349059960 scopus 로고    scopus 로고
    • Tropomyosin-based regulation of the actin cytoskeleton in time and space
    • Gunning, P., O'Neill, G. and Hardeman, E. (2008). Tropomyosin-based regulation of the actin cytoskeleton in time and space. Physiol. Rev. 88, 1-35.
    • (2008) Physiol. Rev , vol.88 , pp. 1-35
    • Gunning, P.1    O'Neill, G.2    Hardeman, E.3
  • 34
    • 0034729916 scopus 로고    scopus 로고
    • Rho GTPases: molecular switches that control the organization and dynamics of the actin cytoskeleton
    • Hall, A. and Nobes, C. D. (2000). Rho GTPases: molecular switches that control the organization and dynamics of the actin cytoskeleton. Philos. Trans. R. Soc. Lond. B Biol. Sci. 355, 965-970.
    • (2000) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.355 , pp. 965-970
    • Hall, A.1    Nobes, C.D.2
  • 35
    • 79955063308 scopus 로고    scopus 로고
    • Activation of a RhoA/myosin II-dependent but Arp2/3 complexindependent pathway facilitates Salmonella invasion
    • Hanisch, J., Kolm, R., Wozniczka, M., Bumann, D., Rottner, K. and Stradal, T. E. B. (2011). Activation of a RhoA/myosin II-dependent but Arp2/3 complexindependent pathway facilitates Salmonella invasion. Cell Host Microbe 9, 273-285.
    • (2011) Cell Host Microbe , vol.9 , pp. 273-285
    • Hanisch, J.1    Kolm, R.2    Wozniczka, M.3    Bumann, D.4    Rottner, K.5    Stradal, T.E.B.6
  • 36
    • 80054079832 scopus 로고    scopus 로고
    • Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament
    • Hayakawa, K., Tatsumi, H. and Sokabe, M. (2011). Actin filaments function as a tension sensor by tension-dependent binding of cofilin to the filament. J. Cell Biol. 195, 721-727.
    • (2011) J. Cell Biol , vol.195 , pp. 721-727
    • Hayakawa, K.1    Tatsumi, H.2    Sokabe, M.3
  • 37
    • 84903291857 scopus 로고    scopus 로고
    • Proteomics analysis of the non-muscle myosin heavy chain IIa-enriched actin-myosin complex reveals multiple functions within the podocyte
    • Hays, T., Ma'ayan, A., Clark, N. R., Tan, C. M., Teixeira, A., Teixeira, A., Choi, J. W., Burdis, N., Jung, S. Y., Bajaj, A. O. et al. (2014). Proteomics analysis of the non-muscle myosin heavy chain IIa-enriched actin-myosin complex reveals multiple functions within the podocyte. PLoS ONE 9, e100660.
    • (2014) PLoS ONE , vol.9
    • Hays, T.1    Ma'ayan, A.2    Clark, N.R.3    Tan, C.M.4    Teixeira, A.5    Teixeira, A.6    Choi, J.W.7    Burdis, N.8    Jung, S.Y.9    Bajaj, A.O.10
  • 38
    • 84878324673 scopus 로고    scopus 로고
    • Forces in tissue morphogenesis and patterning
    • Heisenberg, C.-P. and Bellaiche, Y. (2013). Forces in tissue morphogenesis and patterning. Cell 153, 948-962.
    • (2013) Cell , vol.153 , pp. 948-962
    • Heisenberg, C.-P.1    Bellaiche, Y.2
  • 39
    • 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
  • 40
    • 62649137506 scopus 로고    scopus 로고
    • Diphosphorylation of regulatory light chain of myosin IIA is responsible for proper cell spreading
    • Hirata, N., Takahashi, M. and Yazawa, M. (2009). Diphosphorylation of regulatory light chain of myosin IIA is responsible for proper cell spreading. Biochem. Biophys. Res. Commun. 381, 682-687.
    • (2009) Biochem. Biophys. Res. Commun , vol.381 , pp. 682-687
    • Hirata, N.1    Takahashi, M.2    Yazawa, M.3
  • 41
    • 33845960287 scopus 로고    scopus 로고
    • Cytoskeletal tension regulates both expression and degradation of h2-calponin in lung alveolar cells
    • Hossain, M. M., Smith, P. G., Wu, K. and Jin, J.-P. (2006). Cytoskeletal tension regulates both expression and degradation of h2-calponin in lung alveolar cells. Biochemistry 45, 15670-15683.
    • (2006) Biochemistry , vol.45 , pp. 15670-15683
    • Hossain, M.M.1    Smith, P.G.2    Wu, K.3    Jin, J.-P.4
  • 42
    • 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
  • 43
    • 0022650773 scopus 로고
    • Identification, phosphorylation, and dephosphorylation of a second site for myosin light chain kinase on the 20, 000-dalton light chain of smooth muscle myosin
    • Ikebe, M., Hartshorne, D. J. and Elzinga, M. (1986). Identification, phosphorylation, and dephosphorylation of a second site for myosin light chain kinase on the 20, 000-dalton light chain of smooth muscle myosin. J. Biol. Chem. 261, 36-39.
    • (1986) J. Biol. Chem , vol.261 , pp. 36-39
    • Ikebe, M.1    Hartshorne, D.J.2    Elzinga, M.3
  • 44
    • 79955963564 scopus 로고    scopus 로고
    • Modeling myosin-dependent rearrangement and force generation in an actomyosin network
    • Inoue, Y., Tsuda, S., Nakagawa, K., Hojo, M. and Adachi, T. (2011). Modeling myosin-dependent rearrangement and force generation in an actomyosin network. J. Theor. Biol. 281, 65-73.
    • (2011) J. Theor. Biol , vol.281 , pp. 65-73
    • Inoue, Y.1    Tsuda, S.2    Nakagawa, K.3    Hojo, M.4    Adachi, T.5
  • 45
    • 84878722228 scopus 로고    scopus 로고
    • Formin mDia1 senses and generates mechanical forces on actin filaments
    • Jegou, A., Carlier, M.-F. and Romet-Lemonne, G. (2013). Formin mDia1 senses and generates mechanical forces on actin filaments. Nat. Commun. 4, 1883.
    • (2013) Nat. Commun , vol.4 , pp. 1883
    • Jegou, A.1    Carlier, M.-F.2    Romet-Lemonne, G.3
  • 48
    • 23344438447 scopus 로고    scopus 로고
    • Cell adhesion statusdependent histone acetylation is regulated through intracellular contractilityrelated signaling activities
    • Kim, Y.-B., Yu, J., Lee, S.-Y., Lee, M.-S., Ko, S.-G., Ye, S.-K., Jong, H.-S., Kim, T.-Y., Bang, Y.-J. and Lee, J. W. (2005). Cell adhesion statusdependent histone acetylation is regulated through intracellular contractilityrelated signaling activities. J. Biol. Chem. 280, 28357-28364.
    • (2005) J. Biol. Chem , vol.280 , pp. 28357-28364
    • Kim, Y.-B.1    Yu, J.2    Lee, S.-Y.3    Lee, M.-S.4    Ko, S.-G.5    Ye, S.-K.6    Jong, H.-S.7    Kim, T.-Y.8    Bang, Y.-J.9    Lee, J.W.10
  • 50
    • 79957646416 scopus 로고    scopus 로고
    • Interdependency of cell adhesion, force generation and extracellular proteolysis in matrix remodeling
    • Kirmse, R., Otto, H. and Ludwig, T. (2011). Interdependency of cell adhesion, force generation and extracellular proteolysis in matrix remodeling. J. Cell Sci. 124, 1857-1866.
    • (2011) J. Cell Sci , vol.124 , pp. 1857-1866
    • Kirmse, R.1    Otto, H.2    Ludwig, T.3
  • 51
    • 84898621923 scopus 로고    scopus 로고
    • Nuclear motility in glioma cells reveals a cell-line dependent role of various cytoskeletal components
    • Kiss, A., Horvath, P., Rothballer, A., Kutay, U. and Csucs, G. (2014). Nuclear motility in glioma cells reveals a cell-line dependent role of various cytoskeletal components. PLoS ONE 9, e93431.
    • (2014) PLoS ONE , vol.9
    • Kiss, A.1    Horvath, P.2    Rothballer, A.3    Kutay, U.4    Csucs, G.5
  • 52
    • 0031711721 scopus 로고    scopus 로고
    • Cytoplasmic dynamics of myosin IIA and IIB: spatial 'sorting' of isoforms in locomoting cells
    • Kolega, J. (1998). Cytoplasmic dynamics of myosin IIA and IIB: spatial 'sorting' of isoforms in locomoting cells. J. Cell Sci. 111, 2085-2095.
    • (1998) J. Cell Sci , vol.111 , pp. 2085-2095
    • Kolega, J.1
  • 53
    • 1642448472 scopus 로고    scopus 로고
    • Functional divergence of human cytoplasmic myosin II: kinetic characterization of the nonmuscle IIA isoform
    • Kovacs, M., Wang, F., Hu, A., Zhang, Y. and Sellers, J. R. (2003). Functional divergence of human cytoplasmic myosin II: kinetic characterization of the nonmuscle IIA isoform. J. Biol. Chem. 278, 38132-38140.
    • (2003) J. Biol. Chem , vol.278 , pp. 38132-38140
    • Kovacs, M.1    Wang, F.2    Hu, A.3    Zhang, Y.4    Sellers, J.R.5
  • 54
    • 0001675681 scopus 로고
    • Fluorescent actin filaments move on myosin fixed to a glass surface
    • Kron, S. J. and Spudich, J. A. (1986). Fluorescent actin filaments move on myosin fixed to a glass surface. Proc. Natl. Acad. Sci. USA 83, 6272-6276.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 6272-6276
    • Kron, S.J.1    Spudich, J.A.2
  • 55
    • 38349022141 scopus 로고    scopus 로고
    • Moesin controls cortical rigidity, cell rounding, and spindle morphogenesis during mitosis
    • Kunda, P., Pelling, A. E., Liu, T. and Baum, B. (2008). Moesin controls cortical rigidity, cell rounding, and spindle morphogenesis during mitosis. Curr. Biol. 18, 91-101.
    • (2008) Curr. Biol , vol.18 , pp. 91-101
    • Kunda, P.1    Pelling, A.E.2    Liu, T.3    Baum, B.4
  • 56
    • 80054019905 scopus 로고    scopus 로고
    • Force generation, transmission, and integration during cell and tissue morphogenesis
    • Lecuit, T., Lenne, P.-F. and Munro, E. (2011). Force generation, transmission, and integration during cell and tissue morphogenesis. Annu. Rev. Cell Dev. Biol. 27, 157-184.
    • (2011) Annu. Rev. Cell Dev. Biol , vol.27 , pp. 157-184
    • Lecuit, T.1    Lenne, P.-F.2    Munro, E.3
  • 57
    • 84861839886 scopus 로고    scopus 로고
    • PTK7 regulates myosin II activity to orient planar polarity in the mammalian auditory epithelium
    • Lee, J., Andreeva, A., Sipe, C. W., Liu, L., Cheng, A. and Lu, X. (2012). PTK7 regulates myosin II activity to orient planar polarity in the mammalian auditory epithelium. Curr. Biol. 22, 956-966.
    • (2012) Curr. Biol , vol.22 , pp. 956-966
    • Lee, J.1    Andreeva, A.2    Sipe, C.W.3    Liu, L.4    Cheng, A.5    Lu, X.6
  • 58
    • 22944446447 scopus 로고    scopus 로고
    • Actin-and myosin-driven movement of viruses along filopodia precedes their entry into cells
    • Lehmann, M. J., Sherer, N. M., Marks, C. B., Pypaert, M. and Mothes, W. (2005). Actin-and myosin-driven movement of viruses along filopodia precedes their entry into cells. J. Cell Biol. 170, 317-325.
    • (2005) J. Cell Biol , vol.170 , pp. 317-325
    • Lehmann, M.J.1    Sherer, N.M.2    Marks, C.B.3    Pypaert, M.4    Mothes, W.5
  • 59
    • 63449091349 scopus 로고    scopus 로고
    • Roles of caldesmon in cell motility and actin cytoskeleton remodeling
    • Lin, J. J.-C., Li, Y., Eppinga, R. D., Wang, Q. and Jin, J.-P. (2009). Roles of caldesmon in cell motility and actin cytoskeleton remodeling. Int. Rev. Cell Mol. Biol. 274, 1-68.
    • (2009) Int. Rev. Cell Mol. Biol , vol.274 , pp. 1-68
    • Lin, J.J.-C.1    Li, Y.2    Eppinga, R.D.3    Wang, Q.4    Jin, J.-P.5
  • 60
    • 84886286196 scopus 로고    scopus 로고
    • Molecular mechanisms of cellular mechanosensing
    • Luo, T., Mohan, K., Iglesias, P. A. and Robinson, D. N. (2013). Molecular mechanisms of cellular mechanosensing. Nat. Mater. 12, 1064-1071.
    • (2013) Nat. Mater , vol.12 , pp. 1064-1071
    • Luo, T.1    Mohan, K.2    Iglesias, P.A.3    Robinson, D.N.4
  • 61
    • 84871892885 scopus 로고    scopus 로고
    • Endoplasmic spreading requires coalescence of vimentin intermediate filaments at force-bearing adhesions
    • Lynch, C. D., Lazar, A. M., Iskratsch, T., Zhang, X. and Sheetz, M. P. (2013). Endoplasmic spreading requires coalescence of vimentin intermediate filaments at force-bearing adhesions. Mol. Biol. Cell 24, 21-30.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 21-30
    • Lynch, C.D.1    Lazar, A.M.2    Iskratsch, T.3    Zhang, X.4    Sheetz, M.P.5
  • 62
    • 84875264055 scopus 로고    scopus 로고
    • Cytoskeletal tension modulates MMP-1 gene expression fromtenocytes on micropillar substrates
    • Maeda, E., Sugimoto, M. and Ohashi, T. (2013). Cytoskeletal tension modulates MMP-1 gene expression fromtenocytes on micropillar substrates. J. Biomech. 46, 991-997.
    • (2013) J. Biomech , vol.46 , pp. 991-997
    • Maeda, E.1    Sugimoto, M.2    Ohashi, T.3
  • 65
    • 43149101492 scopus 로고    scopus 로고
    • Softening of the actin cytoskeleton by inhibition of myosin II
    • Martens, J. C. and Radmacher, M. (2008). Softening of the actin cytoskeleton by inhibition of myosin II. Pflugers Arch. 456, 95-100.
    • (2008) Pflugers Arch , vol.456 , pp. 95-100
    • Martens, J.C.1    Radmacher, M.2
  • 66
    • 84900030464 scopus 로고    scopus 로고
    • Apical constriction: themes and variations on a cellular mechanism driving morphogenesis
    • Martin, A. C. and Goldstein, B. (2014). Apical constriction: themes and variations on a cellular mechanism driving morphogenesis. Development 141, 1987-1998.
    • (2014) Development , vol.141 , pp. 1987-1998
    • Martin, A.C.1    Goldstein, B.2
  • 69
    • 0026354883 scopus 로고
    • Regulation of smooth muscle myosin light chain kinase by calmodulin
    • Means, A. R., Bagchi, I. C., Van Berkum, M. F. A. and Kemp, B. E. (1991). Regulation of smooth muscle myosin light chain kinase by calmodulin. Adv. Exp. Med. Biol. 304, 11-24.
    • (1991) Adv. Exp. Med. Biol , vol.304 , pp. 11-24
    • Means, A.R.1    Bagchi, I.C.2    Van Berkum, M.F.A.3    Kemp, B.E.4
  • 70
    • 33644775671 scopus 로고    scopus 로고
    • Myosin II functions in actin-bundle turnover in neuronal growth cones
    • Medeiros, N. A., Burnette, D. T. and Forscher, P. (2006). Myosin II functions in actin-bundle turnover in neuronal growth cones. Nat. Cell Biol. 8, 216-226.
    • (2006) Nat. Cell Biol , vol.8 , pp. 216-226
    • Medeiros, N.A.1    Burnette, D.T.2    Forscher, P.3
  • 71
    • 84881422916 scopus 로고    scopus 로고
    • Force to divide: structural and mechanical requirements for actomyosin ring contraction
    • Mendes Pinto, I., Rubinstein, B. and Li, R. (2013). Force to divide: structural and mechanical requirements for actomyosin ring contraction. Biophys. J. 105, 547-554.
    • (2013) Biophys. J , vol.105 , pp. 547-554
    • Mendes Pinto, I.1    Rubinstein, B.2    Li, R.3
  • 72
    • 66149115276 scopus 로고    scopus 로고
    • Dynamic release of nuclear RanGTP triggers TPX2-dependent microtubule assembly during the apoptotic execution phase
    • Moss, D. K., Wilde, A. and Lane, J. D. (2009). Dynamic release of nuclear RanGTP triggers TPX2-dependent microtubule assembly during the apoptotic execution phase. J. Cell Sci. 122, 644-655.
    • (2009) J. Cell Sci , vol.122 , pp. 644-655
    • Moss, D.K.1    Wilde, A.2    Lane, J.D.3
  • 73
    • 84899631548 scopus 로고    scopus 로고
    • Actomyosin networks and tissue morphogenesis
    • Munjal, A. and Lecuit, T. (2014). Actomyosin networks and tissue morphogenesis. Development 141, 1789-1793.
    • (2014) Development , vol.141 , pp. 1789-1793
    • Munjal, A.1    Lecuit, T.2
  • 75
    • 0037143448 scopus 로고    scopus 로고
    • Rho-kinase and myosin-II control phagocytic cup formation during CR, but not Fcgamma R, phagocytosis
    • Olazabal, I. M., Caron, E., May, R. C., Schilling, K., Knecht, D. A. and Machesky, L. M. (2002). Rho-kinase and myosin-II control phagocytic cup formation during CR, but not Fcgamma R, phagocytosis. Curr. Biol. 12, 1413-1418.
    • (2002) Curr. Biol , vol.12 , pp. 1413-1418
    • Olazabal, I.M.1    Caron, E.2    May, R.C.3    Schilling, K.4    Knecht, D.A.5    Machesky, L.M.6
  • 77
    • 84886422275 scopus 로고    scopus 로고
    • Substrate curvature sensing through Myosin IIa upregulates early osteogenesis
    • Ozdemir, T., Xu, L.-C., Siedlecki, C. and Brown, J. L. (2013). Substrate curvature sensing through Myosin IIa upregulates early osteogenesis. Integr. Biol. 5, 1407-1416.
    • (2013) Integr. Biol , vol.5 , pp. 1407-1416
    • Ozdemir, T.1    Xu, L.-C.2    Siedlecki, C.3    Brown, J.L.4
  • 78
    • 84921438809 scopus 로고    scopus 로고
    • Rac1-dependent phosphorylation and focal adhesion recruitment of Myosin IIA regulates migration and mechanosensing
    • Pasapera, A. M., Plotnikov, S. V., Fischer, R. S., Case, L. B., Egelhoff, T. T. and Waterman, C. M. (2015). Rac1-dependent phosphorylation and focal adhesion recruitment of Myosin IIA regulates migration and mechanosensing. Curr. Biol. 25, 175-186.
    • (2015) Curr. Biol , vol.25 , pp. 175-186
    • Pasapera, A.M.1    Plotnikov, S.V.2    Fischer, R.S.3    Case, L.B.4    Egelhoff, T.T.5    Waterman, C.M.6
  • 79
    • 38749124888 scopus 로고    scopus 로고
    • Anillin is a scaffold protein that links RhoA, actin, and myosin during cytokinesis
    • Piekny, A. J. and Glotzer, M. (2008). Anillin is a scaffold protein that links RhoA, actin, and myosin during cytokinesis. Curr. Biol. 18, 30-36.
    • (2008) Curr. Biol , vol.18 , pp. 30-36
    • Piekny, A.J.1    Glotzer, M.2
  • 80
    • 75749110614 scopus 로고    scopus 로고
    • Mechanics of cytokinesis in eukaryotes
    • Pollard, T. D. (2010). Mechanics of cytokinesis in eukaryotes. Curr. Opin. Cell Biol. 22, 50-56.
    • (2010) Curr. Opin. Cell Biol , vol.22 , pp. 50-56
    • Pollard, T.D.1
  • 81
    • 84926182303 scopus 로고    scopus 로고
    • Active tension: the role of cadherin adhesion and signaling in generating junctional contractility
    • Priya, R. and Yap, A. S. (2015). Active tension: the role of cadherin adhesion and signaling in generating junctional contractility. Curr. Top. Dev. Biol. 112, 65-102.
    • (2015) Curr. Top. Dev. Biol , vol.112 , pp. 65-102
    • Priya, R.1    Yap, A.S.2
  • 82
    • 77950629163 scopus 로고    scopus 로고
    • Alpha-actinin 1 and alpha-actinin 4: contrasting roles in the survival, motility, and RhoA signaling of astrocytoma cells
    • Quick, Q. and Skalli, O. (2010). Alpha-actinin 1 and alpha-actinin 4: contrasting roles in the survival, motility, and RhoA signaling of astrocytoma cells. Exp. Cell Res. 316, 1137-1147.
    • (2010) Exp. Cell Res , vol.316 , pp. 1137-1147
    • Quick, Q.1    Skalli, O.2
  • 83
    • 70349634308 scopus 로고    scopus 로고
    • The bacterial virulence factor InlC perturbs apical cell junctions and promotes cell-to-cell spread of Listeria
    • Rajabian, T., Gavicherla, B., Heisig, M., Müller-Altrock, S., Goebel, W., Gray-Owen, S. D. and Ireton, K. (2009). The bacterial virulence factor InlC perturbs apical cell junctions and promotes cell-to-cell spread of Listeria. Nat. Cell Biol. 11, 1212-1218.
    • (2009) Nat. Cell Biol , vol.11 , pp. 1212-1218
    • Rajabian, T.1    Gavicherla, B.2    Heisig, M.3    Müller-Altrock, S.4    Goebel, W.5    Gray-Owen, S.D.6    Ireton, K.7
  • 85
    • 84919478111 scopus 로고    scopus 로고
    • Genetic suppression of a phosphomimic myosin II identifies system-level factors that promote myosin II cleavage furrow accumulation
    • Ren, Y., West-Foyle, H., Surcel, A., Miller, C. and Robinson, D. N. (2014). Genetic suppression of a phosphomimic myosin II identifies system-level factors that promote myosin II cleavage furrow accumulation. Mol. Biol. Cell 25, 4150-4165.
    • (2014) Mol. Biol. Cell , vol.25 , pp. 4150-4165
    • Ren, Y.1    West-Foyle, H.2    Surcel, A.3    Miller, C.4    Robinson, D.N.5
  • 86
    • 84890858742 scopus 로고    scopus 로고
    • Interference with the contractile machinery of the fibroblastic chondrocyte cytoskeleton induces re-expression of the cartilage phenotype through involvement of PI3K, PKC and MAPKs
    • Rottmar, M., Mhanna, R., Guimond-Lischer, S., Vogel, V., Zenobi-Wong, M. and Maniura-Weber, K. (2014). Interference with the contractile machinery of the fibroblastic chondrocyte cytoskeleton induces re-expression of the cartilage phenotype through involvement of PI3K, PKC and MAPKs. Exp. Cell Res. 320, 175-187.
    • (2014) Exp. Cell Res , vol.320 , pp. 175-187
    • Rottmar, M.1    Mhanna, R.2    Guimond-Lischer, S.3    Vogel, V.4    Zenobi-Wong, M.5    Maniura-Weber, K.6
  • 87
    • 33646058254 scopus 로고    scopus 로고
    • Role of RhoA/ROCK-dependent actin contractility in the induction of tenascin-C by cyclic tensile strain
    • Sarasa-Renedo, A., Tunc-Civelek, V. and Chiquet, M. (2006). Role of RhoA/ROCK-dependent actin contractility in the induction of tenascin-C by cyclic tensile strain. Exp. Cell Res. 312, 1361-1370.
    • (2006) Exp. Cell Res , vol.312 , pp. 1361-1370
    • Sarasa-Renedo, A.1    Tunc-Civelek, V.2    Chiquet, M.3
  • 89
    • 33644809100 scopus 로고    scopus 로고
    • Influence of myosin II activity on stiffness of fibroblast cells
    • Schafer, A. and Radmacher, M. (2005). Influence of myosin II activity on stiffness of fibroblast cells. Acta Biomater. 1, 273-280.
    • (2005) Acta Biomater , vol.1 , pp. 273-280
    • Schafer, A.1    Radmacher, M.2
  • 90
    • 84878541453 scopus 로고    scopus 로고
    • Mechanosensitivity and compositional dynamics of cell-matrix adhesions
    • Schiller, H. B. and Fassler, R. (2013). Mechanosensitivity and compositional dynamics of cell-matrix adhesions. EMBO Rep. 14, 509-519.
    • (2013) EMBO Rep , vol.14 , pp. 509-519
    • Schiller, H.B.1    Fassler, R.2
  • 91
    • 78649727967 scopus 로고    scopus 로고
    • alpha-actinin-4 is essential for maintaining the spreading, motility and contractility of fibroblasts
    • Shao, H., Wang, J. H.-C., Pollak, M. R. and Wells, A. (2010). alpha-actinin-4 is essential for maintaining the spreading, motility and contractility of fibroblasts. PLoS ONE 5, e13921.
    • (2010) PLoS ONE , vol.5
    • Shao, H.1    Wang, J.H.-C.2    Pollak, M.R.3    Wells, A.4
  • 92
    • 84863767949 scopus 로고    scopus 로고
    • Functions of nonmuscle myosin II in assembly of the cellular contractile system
    • Shutova, M., Yang, C., Vasiliev, J. M. and Svitkina, T. (2012). Functions of nonmuscle myosin II in assembly of the cellular contractile system. PLoS ONE 7, e40814.
    • (2012) PLoS ONE , vol.7
    • Shutova, M.1    Yang, C.2    Vasiliev, J.M.3    Svitkina, T.4
  • 93
    • 84908053868 scopus 로고    scopus 로고
    • Endogenous species of mammalian nonmuscle myosin IIA and IIB include activated monomers and heteropolymers
    • Shutova, M. S., Spessott, W. A., Giraudo, C. G. and Svitkina, T. (2014). Endogenous species of mammalian nonmuscle myosin IIA and IIB include activated monomers and heteropolymers. Curr. Biol. 24, 1958-1968.
    • (2014) Curr. Biol , vol.24 , pp. 1958-1968
    • Shutova, M.S.1    Spessott, W.A.2    Giraudo, C.G.3    Svitkina, T.4
  • 94
    • 57749104129 scopus 로고    scopus 로고
    • JNK-mediated phosphorylation of paxillin in adhesion assembly and tension-induced cell death by the adenovirus death factor E4orf4
    • Smadja-Lamere, N., Boulanger, M.-C., Champagne, C., Branton, P. E. and Lavoie, J. N. (2008). JNK-mediated phosphorylation of paxillin in adhesion assembly and tension-induced cell death by the adenovirus death factor E4orf4. J. Biol. Chem. 283, 34352-34364.
    • (2008) J. Biol. Chem , vol.283 , pp. 34352-34364
    • Smadja-Lamere, N.1    Boulanger, M.-C.2    Champagne, C.3    Branton, P.E.4    Lavoie, J.N.5
  • 98
    • 46249126296 scopus 로고    scopus 로고
    • Isoform B of myosin II heavy chain mediates actomyosin contractility during TNFalpha-induced apoptosis
    • Solinet, S. and Vitale, M. L. (2008). Isoform B of myosin II heavy chain mediates actomyosin contractility during TNFalpha-induced apoptosis. J. Cell Sci. 121, 1681-1692.
    • (2008) J. Cell Sci , vol.121 , pp. 1681-1692
    • Solinet, S.1    Vitale, M.L.2
  • 99
    • 0036073008 scopus 로고    scopus 로고
    • ROCK-II-induced membrane blebbing and chromatin condensation require actin cytoskeleton
    • Song, Y., Hoang, B. Q. and Chang, D. D. (2002). ROCK-II-induced membrane blebbing and chromatin condensation require actin cytoskeleton. Exp. Cell Res. 278, 45-52.
    • (2002) Exp. Cell Res , vol.278 , pp. 45-52
    • Song, Y.1    Hoang, B.Q.2    Chang, D.D.3
  • 100
    • 0022263118 scopus 로고
    • Movement of myosin-coated beads on oriented filaments reconstituted from purified actin
    • Spudich, J. A., Kron, S. J. and Sheetz, M. P. (1985). Movement of myosin-coated beads on oriented filaments reconstituted from purified actin. Nature 315, 584-586.
    • (1985) Nature , vol.315 , pp. 584-586
    • Spudich, J.A.1    Kron, S.J.2    Sheetz, M.P.3
  • 101
    • 0023815476 scopus 로고
    • Calcium control of smooth muscle contractility
    • Stull, J. T., Kamm, K. E. and Taylor, D. A. (1988). Calcium control of smooth muscle contractility. Am. J. Med. Sci. 296, 241-245.
    • (1988) Am. J. Med. Sci , vol.296 , pp. 241-245
    • Stull, J.T.1    Kamm, K.E.2    Taylor, D.A.3
  • 102
    • 84874806418 scopus 로고    scopus 로고
    • Mechanobiology: a new frontier for human pluripotent stem cells
    • Sun, Y. and Fu, J. (2013). Mechanobiology: a new frontier for human pluripotent stem cells. Integr. Biol. 5, 450-457.
    • (2013) Integr. Biol , vol.5 , pp. 450-457
    • Sun, Y.1    Fu, J.2
  • 103
    • 0030777766 scopus 로고    scopus 로고
    • Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation
    • Svitkina, T. M., Verkhovsky, A. B., McQuade, K. M. and Borisy, G. G. (1997). Analysis of the actin-myosin II system in fish epidermal keratocytes: mechanism of cell body translocation. J. Cell Biol. 139, 397-415.
    • (1997) J. Cell Biol , vol.139 , pp. 397-415
    • Svitkina, T.M.1    Verkhovsky, A.B.2    McQuade, K.M.3    Borisy, G.G.4
  • 104
    • 84857556564 scopus 로고    scopus 로고
    • Lymphatic and interstitial flow in the tumour microenvironment: linking mechanobiology with immunity
    • Swartz, M. A. and Lund, A. W. (2012). Lymphatic and interstitial flow in the tumour microenvironment: linking mechanobiology with immunity. Nat. Rev. Cancer 12, 210-219.
    • (2012) Nat. Rev. Cancer , vol.12 , pp. 210-219
    • Swartz, M.A.1    Lund, A.W.2
  • 105
    • 79959354675 scopus 로고    scopus 로고
    • Inhibition of myosin II triggers morphological transition and increased nuclear motility
    • Szabo, B., Unnep, R., Marko, K., Kornyei, Z., Mehes, E. and Czirok, A. (2011). Inhibition of myosin II triggers morphological transition and increased nuclear motility. Cytoskeleton 68, 325-339.
    • (2011) Cytoskeleton , vol.68 , pp. 325-339
    • Szabo, B.1    Unnep, R.2    Marko, K.3    Kornyei, Z.4    Mehes, E.5    Czirok, A.6
  • 106
    • 84946069451 scopus 로고    scopus 로고
    • UniProt: a hub for protein information
    • The UniProt Consortium. (2015). UniProt: a hub for protein information. Nucleic Acids Res. 43, D204-D212.
    • (2015) Nucleic Acids Res , vol.43 , pp. D204-D212
  • 110
    • 0035938439 scopus 로고    scopus 로고
    • Structural abnormalities develop in the brain after ablation of the gene encoding nonmuscle myosin II-B heavy chain
    • Tullio, A. N., Bridgman, P. C., Tresser, N. J., Chan, C.-C., Conti, M. A., Adelstein, R. S. and Hara, Y. (2001). Structural abnormalities develop in the brain after ablation of the gene encoding nonmuscle myosin II-B heavy chain. J. Comp. Neurol. 433, 62-74.
    • (2001) J. Comp. Neurol , vol.433 , pp. 62-74
    • Tullio, A.N.1    Bridgman, P.C.2    Tresser, N.J.3    Chan, C.-C.4    Conti, M.A.5    Adelstein, R.S.6    Hara, Y.7
  • 111
    • 0024576739 scopus 로고
    • Effect of multiple phosphorylations of smooth muscle and cytoplasmic myosins on movement in an in vitro motility assay
    • Umemoto, S., Bengur, A. R. and Sellers, J. R. (1989). Effect of multiple phosphorylations of smooth muscle and cytoplasmic myosins on movement in an in vitro motility assay. J. Biol. Chem. 264, 1431-1436.
    • (1989) J. Biol. Chem , vol.264 , pp. 1431-1436
    • Umemoto, S.1    Bengur, A.R.2    Sellers, J.R.3
  • 112
    • 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 Makela, 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    Makela, T.P.6
  • 113
    • 0036124578 scopus 로고    scopus 로고
    • Evidence of a role for nonmuscle myosin II in herpes simplex virus type 1 egress
    • van Leeuwen, H., Elliott, G. and O'Hare, P. (2002). Evidence of a role for nonmuscle myosin II in herpes simplex virus type 1 egress. J. Virol. 76, 3471-3481.
    • (2002) J. Virol , vol.76 , pp. 3471-3481
    • van Leeuwen, H.1    Elliott, G.2    O'Hare, P.3
  • 115
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • Vogel, V. and Sheetz, M. (2006). Local force and geometry sensing regulate cell functions. Nat. Rev. Mol. Cell Biol. 7, 265-275.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 117
    • 33748488003 scopus 로고    scopus 로고
    • Planar polarization of the denticle field in the Drosophila embryo: roles for Myosin II (zipper) and fringe
    • Walters, J. W., Dilks, S. A. and DiNardo, S. (2006). Planar polarization of the denticle field in the Drosophila embryo: roles for Myosin II (zipper) and fringe. Dev. Biol. 297, 323-339.
    • (2006) Dev. Biol , vol.297 , pp. 323-339
    • Walters, J.W.1    Dilks, S.A.2    DiNardo, S.3
  • 118
    • 0042347443 scopus 로고    scopus 로고
    • Kinetic mechanism of non-muscle myosin IIB: functional adaptations for tension generation and maintenance
    • Wang, F., Kovacs, M., Hu, A., Limouze, J., Harvey, E. V. and Sellers, J. R. (2003). Kinetic mechanism of non-muscle myosin IIB: functional adaptations for tension generation and maintenance. J. Biol. Chem. 278, 27439-27448.
    • (2003) J. Biol. Chem , vol.278 , pp. 27439-27448
    • Wang, F.1    Kovacs, M.2    Hu, A.3    Limouze, J.4    Harvey, E.V.5    Sellers, J.R.6
  • 119
    • 80053367989 scopus 로고    scopus 로고
    • Distinct and redundant roles of the non-muscle myosin II isoforms and functional domains
    • Wang, A., Ma, X., Conti, M. A. and Adelstein, R. S. (2011). Distinct and redundant roles of the non-muscle myosin II isoforms and functional domains. Biochem. Soc. Trans. 39, 1131-1135.
    • (2011) Biochem. Soc. Trans , vol.39 , pp. 1131-1135
    • Wang, A.1    Ma, X.2    Conti, M.A.3    Adelstein, R.S.4
  • 120
    • 84867983782 scopus 로고    scopus 로고
    • Cytokinesis mechanics and mechanosensing
    • West-Foyle, H. and Robinson, D. N. (2012). Cytokinesis mechanics and mechanosensing. Cytoskeleton 69, 700-709.
    • (2012) Cytoskeleton , vol.69 , pp. 700-709
    • West-Foyle, H.1    Robinson, D.N.2
  • 121
    • 84858246364 scopus 로고    scopus 로고
    • ADF/cofilin regulates actomyosin assembly through competitive inhibition of myosin II binding to F-actin
    • Wiggan, O., Shaw, A. E., DeLuca, J. G. and Bamburg, J. R. (2012). ADF/cofilin regulates actomyosin assembly through competitive inhibition of myosin II binding to F-actin. Dev. Cell 22, 530-543.
    • (2012) Dev. Cell , vol.22 , pp. 530-543
    • Wiggan, O.1    Shaw, A.E.2    DeLuca, J.G.3    Bamburg, J.R.4
  • 123
    • 84875273788 scopus 로고    scopus 로고
    • Dynamic regulation of the structure and functions of integrin adhesions
    • Wolfenson, H., Lavelin, I. and Geiger, B. (2013). Dynamic regulation of the structure and functions of integrin adhesions. Dev. Cell 24, 447-458.
    • (2013) Dev. Cell , vol.24 , pp. 447-458
    • Wolfenson, H.1    Lavelin, I.2    Geiger, B.3
  • 124
    • 0032565769 scopus 로고    scopus 로고
    • Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization
    • Yang, N., Higuchi, O., Ohashi, K., Nagata, K., Wada, A., Kangawa, K., Nishida, E. and Mizuno, K. (1998). Cofilin phosphorylation by LIM-kinase 1 and its role in Rac-mediated actin reorganization. Nature 393, 809-812.
    • (1998) Nature , vol.393 , pp. 809-812
    • Yang, N.1    Higuchi, O.2    Ohashi, K.3    Nagata, K.4    Wada, A.5    Kangawa, K.6    Nishida, E.7    Mizuno, K.8
  • 125
    • 84863734478 scopus 로고    scopus 로고
    • Arp2/3 complexdependent actin networks constrain myosin II function in driving retrograde actin flow
    • Yang, Q., Zhang, X.-F., Pollard, T. D. and Forscher, P. (2012). Arp2/3 complexdependent actin networks constrain myosin II function in driving retrograde actin flow. J. Cell Biol. 197, 939-956.
    • (2012) J. Cell Biol , vol.197 , pp. 939-956
    • Yang, Q.1    Zhang, X.-F.2    Pollard, T.D.3    Forscher, P.4
  • 126
    • 33846099490 scopus 로고    scopus 로고
    • Fibronectin matrix assembly requires distinct contributions from Rho kinases I and-II
    • Yoneda, A., Ushakov, D., Multhaupt, H. A. B. and Couchman, J. R. (2007). Fibronectin matrix assembly requires distinct contributions from Rho kinases I and-II. Mol. Biol. Cell 18, 66-75.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 66-75
    • Yoneda, A.1    Ushakov, D.2    Multhaupt, H.A.B.3    Couchman, J.R.4
  • 128
    • 0030928057 scopus 로고    scopus 로고
    • Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction
    • Zhang, Q., Magnusson, M. K. and Mosher, D. F. (1997). Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction. Mol. Biol. Cell 8, 1415-1425.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1415-1425
    • Zhang, Q.1    Magnusson, M.K.2    Mosher, D.F.3
  • 130
    • 84875216538 scopus 로고    scopus 로고
    • PrePPI: a structure-informed database of protein-protein interactions
    • Zhang, Q. C., Petrey, D., Garzon, J. I., Deng, L. and Honig, B. (2013). PrePPI: a structure-informed database of protein-protein interactions. Nucleic Acids Res. 41, D828-D833.
    • (2013) Nucleic Acids Res , vol.41 , pp. D828-D833
    • Zhang, Q.C.1    Petrey, D.2    Garzon, J.I.3    Deng, L.4    Honig, B.5
  • 131
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong, C., Chrzanowska-Wodnicka, M., Brown, J., Shaub, A., Belkin, A. M. and Burridge, K. (1998). Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 141, 539-551.
    • (1998) J. Cell Biol , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.M.5    Burridge, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.