메뉴 건너뛰기
Journal of Cell Biology
Volumn 210, Issue 2, 2015, Pages 225-242
ROCK 1 and 2 differentially regulate actomyosin organization to drive cell and synaptic polarity
Author keywords

[No Author keywords available]
Indexed keywords

COFILIN; ISOENZYME; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN II; RAC1 PROTEIN; RHO KINASE; ROCK1 PROTEIN; ROCK2 PROTEIN; UNCLASSIFIED DRUG; ACTIN DEPOLYMERIZING FACTOR; ROCK1 PROTEIN, RAT; ROCK2 PROTEIN, RAT;
EID: 84946074532     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201504046     Document Type: Article
Times cited : (92)
References (95)
  • 1
    • 0029149885 scopus 로고
    • Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site
    • Agnew, B.J., L.S. Minamide, and J.R. Bamburg. 1995. Reactivation of phosphorylated actin depolymerizing factor and identification of the regulatory site. J. Biol. Chem. 270:17582-17587. http://dx.doi.org/10.1074/jbc.270.29.17582.
    • (1995) J. Biol. Chem , vol.270 , pp. 17582-17587
    • Agnew, B.J.1    Minamide, L.S.2    Bamburg, J.R.3
  • 2
    • 0029786313 scopus 로고    scopus 로고
    • Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase)
    • Amano, M., M. Ito, K. Kimura, Y. Fukata, K. Chihara, T. Nakano, Y. Matsuura, and K. Kaibuchi. 1996. Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase). J. Biol. Chem. 271:20246-20249. http://dx.doi.org/10.1074/jbc.271.34.20246.
    • (1996) J. Biol. Chem , vol.271 , pp. 20246-20249
    • Amano, M.1    Ito, M.2    Kimura, K.3    Fukata, Y.4    Chihara, K.5    Nakano, T.6    Matsuura, Y.7    Kaibuchi, K.8
  • 3
    • 0031048791 scopus 로고    scopus 로고
    • Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
    • Amano, M., K. Chihara, K. Kimura, Y. Fukata, N. Nakamura, Y. Matsuura, and K. Kaibuchi. 1997. Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase. Science. 275:1308-1311. http://dx.doi.org/10.1126/science.275.5304.1308.
    • (1997) Science , vol.275 , pp. 1308-1311
    • Amano, M.1    Chihara, K.2    Kimura, K.3    Fukata, Y.4    Nakamura, N.5    Matsuura, Y.6    Kaibuchi, K.7
  • 4
    • 33845335504 scopus 로고    scopus 로고
    • Traction forces of fibroblasts are regulated by the Rho-dependent kinase but not by the myosin light chain kinase
    • Beningo, K.A., K. Hamao, M. Dembo, Y.-L. Wang, and H. Hosoya. 2006. Traction forces of fibroblasts are regulated by the Rho-dependent kinase but not by the myosin light chain kinase. Arch. Biochem. Biophys. 456:224-231. http://dx.doi.org/10.1016/j.abb.2006.09.025.
    • (2006) Arch. Biochem. Biophys , vol.456 , pp. 224-231
    • Beningo, K.A.1    Hamao, K.2    Dembo, M.3    Wang, Y.-L.4    Hosoya, H.5
  • 5
    • 84863462907 scopus 로고    scopus 로고
    • Structural plasticity of dendritic spines
    • Bosch, M., and Y. Hayashi. 2012. Structural plasticity of dendritic spines. Curr. Opin. Neurobiol. 22:383-388. http://dx.doi.org/10.1016/j.conb.2011.09.002.
    • (2012) Curr. Opin. Neurobiol , vol.22 , pp. 383-388
    • Bosch, M.1    Hayashi, Y.2
  • 6
    • 84898688394 scopus 로고    scopus 로고
    • Structural and molecular remodeling of dendritic spine substructures during long-term potentiation
    • Bosch, M., J. Castro, T. Saneyoshi, H. Matsuno, M. Sur, and Y. Hayashi. 2014. Structural and molecular remodeling of dendritic spine substructures during long-term potentiation. Neuron. 82:444-459. http://dx.doi.org/10.1016/j.neuron.2014.03.021.
    • (2014) Neuron , vol.82 , pp. 444-459
    • Bosch, M.1    Castro, J.2    Saneyoshi, T.3    Matsuno, H.4    Sur, M.5    Hayashi, Y.6
  • 7
    • 68649102300 scopus 로고    scopus 로고
    • Nonlinear elastic properties of polyacrylamide gels: implications for quantification of cellular forces
    • Boudou, T., J. Ohayon, C. Picart, R.I. Pettigrew, and P. Tracqui. 2009. Nonlinear elastic properties of polyacrylamide gels: implications for quantification of cellular forces. Biorheology. 46:191-205.
    • (2009) Biorheology , vol.46 , pp. 191-205
    • Boudou, T.1    Ohayon, J.2    Picart, C.3    Pettigrew, R.I.4    Tracqui, P.5
  • 8
    • 46049083951 scopus 로고    scopus 로고
    • Myosin II activity facilitates microtubule bundling in the neuronal growth cone neck
    • Burnette, D.T., L. Ji, A.W. Schaefer, N.A. Medeiros, G. Danuser, and P. Forscher. 2008. Myosin II activity facilitates microtubule bundling in the neuronal growth cone neck. Dev. Cell. 15:163-169. http://dx.doi.org/10.1016/j.devcel.2008.05.016.
    • (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
  • 9
    • 0036083584 scopus 로고    scopus 로고
    • Traction fields, moments, and strain energy that cells exert on their surroundings
    • Butler, J.P., I.M. Tolić-Nørrelykke, B. Fabry, and J.J. Fredberg. 2002. Traction fields, moments, and strain energy that cells exert on their surroundings. Am. J. Physiol. Cell Physiol. 282:C595-C605. http://dx.doi.org/10.1152/ajpcell.00270.2001.
    • (2002) Am. J. Physiol. Cell Physiol , vol.282 , pp. C595-C605
    • Butler, J.P.1    Tolić-Nørrelykke, I.M.2    Fabry, B.3    Fredberg, J.J.4
  • 10
    • 84899672236 scopus 로고    scopus 로고
    • Activity-dependent dendritic spine shrinkage and growth involve downregulation of cofilin via distinct mechanisms
    • Calabrese, B., J.-M. Saffin, and S. Halpain. 2014. Activity-dependent dendritic spine shrinkage and growth involve downregulation of cofilin via distinct mechanisms. PLoS ONE. 9:e94787. http://dx.doi.org/10.1371/journal.pone.0094787.
    • (2014) PLoS ONE , vol.9
    • Calabrese, B.1    Saffin, J.-M.2    Halpain, S.3
  • 11
    • 34249055892 scopus 로고    scopus 로고
    • Changes in synaptic morphology accompany actin signaling during LTP
    • Chen, L.Y., C.S. Rex, M.S. Casale, C.M. Gall, and G. Lynch. 2007. Changes in synaptic morphology accompany actin signaling during LTP. J. Neurosci. 27:5363-5372. http://dx.doi.org/10.1523/JNEUROSCI.0164-07.2007.
    • (2007) J. Neurosci , vol.27 , pp. 5363-5372
    • Chen, L.Y.1    Rex, C.S.2    Casale, M.S.3    Gall, C.M.4    Lynch, G.5
  • 12
    • 51049104617 scopus 로고    scopus 로고
    • Actin and α-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi, C.K., M. Vicente-Manzanares, J. Zareno, L.A. Whitmore, A. Mogilner, and A.R. Horwitz. 2008. Actin and α-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nat. Cell Biol. 10:1039-1050. http://dx.doi.org/10.1038/ncb1763.
    • (2008) Nat. Cell Biol , vol.10 , pp. 1039-1050
    • Choi, C.K.1    Vicente-Manzanares, M.2    Zareno, J.3    Whitmore, L.A.4    Mogilner, A.5    Horwitz, A.R.6
  • 13
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M., and K. Burridge. 1996. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133:1403-1415. http://dx.doi.org/10.1083/jcb.133.6.1403.
    • (1996) J. Cell Biol , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 15
    • 0347319161 scopus 로고    scopus 로고
    • Substrate compliance versus ligand density in cell on gel responses
    • Engler, A., L. Bacakova, C. Newman, A. Hategan, M. Griffin, and D. Discher. 2004. Substrate compliance versus ligand density in cell on gel responses. Biophys. J. 86:617-628. http://dx.doi.org/10.1016/S0006-3495(04)74140-5.
    • (2004) Biophys. J , vol.86 , pp. 617-628
    • Engler, A.1    Bacakova, L.2    Newman, C.3    Hategan, A.4    Griffin, M.5    Discher, D.6
  • 17
    • 77956247700 scopus 로고    scopus 로고
    • Long-term potentiation-dependent spine enlargement requires synaptic Ca2+-permeable AMPA receptors recruited by CaM-kinase I
    • Fortin, D.A., M.A. Davare, T. Srivastava, J.D. Brady, S. Nygaard, V.A. Derkach, and T.R. Soderling. 2010. Long-term potentiation-dependent spine enlargement requires synaptic Ca2+-permeable AMPA receptors recruited by CaM-kinase I. J. Neurosci. 30:11565-11575. http://dx.doi.org/10.1523/JNEUROSCI.1746-10.2010.
    • (2010) J. Neurosci , vol.30 , pp. 11565-11575
    • Fortin, D.A.1    Davare, M.A.2    Srivastava, T.3    Brady, J.D.4    Nygaard, S.5    Derkach, V.A.6    Soderling, T.R.7
  • 18
    • 33745232760 scopus 로고    scopus 로고
    • Actomyosin-dependent microtubule rearrangement in lysophosphatidic acid-induced neurite remodeling of young cortical neurons
    • Fukushima, N., and Y. Morita. 2006. Actomyosin-dependent microtubule rearrangement in lysophosphatidic acid-induced neurite remodeling of young cortical neurons. Brain Res. 1094:65-75. http://dx.doi.org/10.1016/j.brainres.2006.04.007.
    • (2006) Brain Res , vol.1094 , pp. 65-75
    • Fukushima, N.1    Morita, Y.2
  • 19
    • 0033593337 scopus 로고    scopus 로고
    • The Dbl-related protein, Lfc, localizes to microtubules and mediates the activation of Rac signaling pathways in cells
    • Glaven, J.A., I. Whitehead, S. Bagrodia, R. Kay, and R.A. Cerione. 1999. The Dbl-related protein, Lfc, localizes to microtubules and mediates the activation of Rac signaling pathways in cells. J. Biol. Chem. 274:2279-2285. http://dx.doi.org/10.1074/jbc.274.4.2279.
    • (1999) J. Biol. Chem , vol.274 , pp. 2279-2285
    • Glaven, J.A.1    Whitehead, I.2    Bagrodia, S.3    Kay, R.4    Cerione, R.A.5
  • 20
    • 0002329664 scopus 로고    scopus 로고
    • Rat hippocampal neurons in low-density culture
    • G. Banker, editor. MIT Press, Cambridge, MA
    • Goslin, K., and G. Banker. 1998. Rat hippocampal neurons in low-density culture. In Culturing Nerve Cells. G. Banker, editor. MIT Press, Cambridge, MA. 339-370.
    • (1998) Culturing Nerve Cells , pp. 339-370
    • Goslin, K.1    Banker, G.2
  • 21
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies
    • Heasman, S.J., and A.J. Ridley. 2008. Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat. Rev. Mol. Cell Biol. 9:690-701. http://dx.doi.org/10.1038/nrm2476.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 22
    • 14444288533 scopus 로고    scopus 로고
    • Molecular dissection of the Rho-associated protein kinase (p160ROCK)-regulated neurite remodeling in neuroblastoma N1E-115 cells
    • Hirose, M., T. Ishizaki, N. Watanabe, M. Uehata, O. Kranenburg, W.H. Moolenaar, F. Matsumura, M. Maekawa, H. Bito, and S. Narumiya. 1998. Molecular dissection of the Rho-associated protein kinase (p160ROCK)-regulated neurite remodeling in neuroblastoma N1E-115 cells. J. Cell Biol. 141:1625-1636. http://dx.doi.org/10.1083/jcb.141.7.1625.
    • (1998) J. Cell Biol , vol.141 , pp. 1625-1636
    • Hirose, M.1    Ishizaki, T.2    Watanabe, N.3    Uehata, M.4    Kranenburg, O.5    Moolenaar, W.H.6    Matsumura, F.7    Maekawa, M.8    Bito, H.9    Narumiya, S.10
  • 23
    • 80052063518 scopus 로고    scopus 로고
    • Myosin IIb activity and phosphorylation status determines dendritic spine and post-synaptic density morphology
    • Hodges, J.L., K. Newell-Litwa, H. Asmussen, M. Vicente-Manzanares, and A.R. Horwitz. 2011. Myosin IIb activity and phosphorylation status determines dendritic spine and post-synaptic density morphology. PLoS ONE. 6:e24149. http://dx.doi.org/10.1371/journal.pone.0024149.
    • (2011) PLoS ONE , vol.6
    • Hodges, J.L.1    Newell-Litwa, K.2    Asmussen, H.3    Vicente-Manzanares, M.4    Horwitz, A.R.5
  • 24
    • 84904052300 scopus 로고    scopus 로고
    • a-Actinin-2 mediates spine morphology and assembly of the post-synaptic density in hippocampal neurons
    • Hodges, J.L., S.M. Vilchez, H. Asmussen, L.A. Whitmore, and A.R. Horwitz. 2014. a-Actinin-2 mediates spine morphology and assembly of the post-synaptic density in hippocampal neurons. PLoS ONE. 9:e101770. http://dx.doi.org/10.1371/journal.pone.0101770.
    • (2014) PLoS ONE , vol.9
    • Hodges, J.L.1    Vilchez, S.M.2    Asmussen, H.3    Whitmore, L.A.4    Horwitz, A.R.5
  • 26
    • 0036724188 scopus 로고    scopus 로고
    • Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells
    • Itoh, R.E., K. Kurokawa, Y. Ohba, H. Yoshizaki, N. Mochizuki, and M. Matsuda. 2002. Activation of rac and cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells. Mol. Cell. Biol. 22:6582-6591. http://dx.doi.org/10.1128/MCB.22.18.6582-6591.2002.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 6582-6591
    • Itoh, R.E.1    Kurokawa, K.2    Ohba, Y.3    Yoshizaki, H.4    Mochizuki, N.5    Matsuda, M.6
  • 28
    • 84922235747 scopus 로고    scopus 로고
    • Rho-associated coiled-coil containing kinases (ROCK): structure, regulation, and functions
    • Julian, L., and M.F. Olson. 2014. Rho-associated coiled-coil containing kinases (ROCK): structure, regulation, and functions. Small GTPases. 5:e29846. http://dx.doi.org/10.4161/sgtp.29846.
    • (2014) Small GTPases , vol.5
    • Julian, L.1    Olson, M.F.2
  • 29
    • 0035972212 scopus 로고    scopus 로고
    • Rho-kinase-mediated contraction of isolated stress fibers
    • Katoh, K., Y. Kano, M. Amano, H. Onishi, K. Kaibuchi, and K. Fujiwara. 2001. Rho-kinase-mediated contraction of isolated stress fibers. J. Cell Biol. 153:569-584. http://dx.doi.org/10.1083/jcb.153.3.569.
    • (2001) J. Cell Biol , vol.153 , pp. 569-584
    • Katoh, K.1    Kano, Y.2    Amano, M.3    Onishi, H.4    Kaibuchi, K.5    Fujiwara, K.6
  • 33
    • 0344012487 scopus 로고    scopus 로고
    • Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction
    • Kolega, J. 2003. Asymmetric distribution of myosin IIB in migrating endothelial cells is regulated by a rho-dependent kinase and contributes to tail retraction. Mol. Biol. Cell. 14:4745-4757. http://dx.doi.org/10.1091/mbc. E03-04-0205.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4745-4757
    • Kolega, J.1
  • 34
    • 84873097224 scopus 로고    scopus 로고
    • Timothy syndrome is associated with activity-dependent dendritic retraction in rodent and human neurons
    • Krey, J.F., S.P. Pasca, A. Shcheglovitov, M. Yazawa, R. Schwemberger, R. Rasmusson, and R.E. Dolmetsch. 2013. Timothy syndrome is associated with activity-dependent dendritic retraction in rodent and human neurons. Nat. Neurosci. 16:201-209. http://dx.doi.org/10.1038/nn.3307.
    • (2013) Nat. Neurosci , vol.16 , pp. 201-209
    • Krey, J.F.1    Pasca, S.P.2    Shcheglovitov, A.3    Yazawa, M.4    Schwemberger, R.5    Rasmusson, R.6    Dolmetsch, R.E.7
  • 35
    • 79953303384 scopus 로고    scopus 로고
    • Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation
    • Kuo, J.-C., X. Han, C.-T. Hsiao, J.R. Yates III, and C.M. Waterman. 2011. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13:383-393. http://dx.doi.org/10.1038/ncb2216.
    • (2011) Nat. Cell Biol , vol.13 , pp. 383-393
    • Kuo, J.-C.1    Han, X.2    Hsiao, C.-T.3    Yates, J.R.4    Waterman, C.M.5
  • 36
    • 0035954424 scopus 로고    scopus 로고
    • Differential dynamics of α5 integrin, paxillin, and α-actinin during formation and disassembly of adhesions in migrating cells
    • Laukaitis, C.M., D.J. Webb, K. Donais, and A.F. Horwitz. 2001. Differential dynamics of α5 integrin, paxillin, and α-actinin during formation and disassembly of adhesions in migrating cells. J. Cell Biol. 153:1427-1440. http://dx.doi.org/10.1083/jcb.153.7.1427.
    • (2001) J. Cell Biol , vol.153 , pp. 1427-1440
    • Laukaitis, C.M.1    Webb, D.J.2    Donais, K.3    Horwitz, A.F.4
  • 37
    • 0030658939 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor Tiam1 affects neuronal morphology; opposing roles for the small GTPases Rac and Rho
    • Leeuwen, F.N., H.E. Kain, R.A. Kammen, F. Michiels, O.W. Kranenburg, and J.G. Collard. 1997. The guanine nucleotide exchange factor Tiam1 affects neuronal morphology; opposing roles for the small GTPases Rac and Rho. J. Cell Biol. 139:797-807. http://dx.doi.org/10.1083/jcb.139.3.797.
    • (1997) J. Cell Biol , vol.139 , pp. 797-807
    • Leeuwen, F.N.1    Kain, H.E.2    Kammen, R.A.3    Michiels, F.4    Kranenburg, O.W.5    Collard, J.G.6
  • 38
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes
    • Leung, T., E. Manser, L. Tan, and L. Lim. 1995. A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J. Biol. Chem. 270:29051-29054. http://dx.doi.org/10.1074/jbc.270.49.29051.
    • (1995) J. Biol. Chem , vol.270 , pp. 29051-29054
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 39
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung, T., X.Q. Chen, E. Manser, and L. Lim. 1996. The p160 RhoA-binding kinase ROK alpha is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16:5313-5327.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.Q.2    Manser, E.3    Lim, L.4
  • 40
    • 33845863898 scopus 로고    scopus 로고
    • LTP consolidation: substrates, explanatory power, and functional significance
    • Lynch, G., C.S. Rex, and C.M. Gall. 2007. LTP consolidation: substrates, explanatory power, and functional significance. Neuropharmacology. 52:12-23. http://dx.doi.org/10.1016/j.neuropharm.2006.07.027.
    • (2007) Neuropharmacology , vol.52 , pp. 12-23
    • Lynch, G.1    Rex, C.S.2    Gall, C.M.3
  • 43
    • 84868111953 scopus 로고    scopus 로고
    • Mechanosensitive mechanisms in transcriptional regulation
    • Mammoto, A., T. Mammoto, and D.E. Ingber. 2012. Mechanosensitive mechanisms in transcriptional regulation. J. Cell Sci. 125:3061-3073. http://dx.doi.org/10.1242/jcs.093005.
    • (2012) J. Cell Sci , vol.125 , pp. 3061-3073
    • Mammoto, A.1    Mammoto, T.2    Ingber, D.E.3
  • 45
    • 0007292851 scopus 로고
    • High actin concentrations in brain dendritic spines and postsynaptic densities
    • Matus, A., M. Ackermann, G. Pehling, H.R. Byers, and K. Fujiwara. 1982. High actin concentrations in brain dendritic spines and postsynaptic densities. Proc. Natl. Acad. Sci. USA. 79:7590-7594. http://dx.doi.org/10.1073/pnas.79.23.7590.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 7590-7594
    • Matus, A.1    Ackermann, M.2    Pehling, G.3    Byers, H.R.4    Fujiwara, K.5
  • 48
    • 0024557848 scopus 로고
    • In situ localization of myosin and actin in dendritic spines with the immunogold technique
    • Morales, M., and E. Fifková. 1989. In situ localization of myosin and actin in dendritic spines with the immunogold technique. J. Comp. Neurol. 279:666-674. http://dx.doi.org/10.1002/cne.902790412.
    • (1989) J. Comp. Neurol , vol.279 , pp. 666-674
    • Morales, M.1    Fifková, E.2
  • 49
    • 0029678546 scopus 로고    scopus 로고
    • Phosphorylation of Ser-3 of cofilin regulates its essential function on actin
    • Moriyama, K., K. Iida, and I. Yahara. 1996. Phosphorylation of Ser-3 of cofilin regulates its essential function on actin. Genes Cells. 1:73-86. http://dx.doi.org/10.1046/j.1365-2443.1996.05005.x.
    • (1996) Genes Cells , vol.1 , pp. 73-86
    • Moriyama, K.1    Iida, K.2    Yahara, I.3
  • 50
    • 0030603119 scopus 로고    scopus 로고
    • ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice
    • Nakagawa, O., K. Fujisawa, T. Ishizaki, Y. Saito, K. Nakao, and S. Narumiya. 1996. ROCK-I and ROCK-II, two isoforms of Rho-associated coiled-coil forming protein serine/threonine kinase in mice. FEBS Lett. 392:189-193. http://dx.doi.org/10.1016/0014-5793(96)00811-3.
    • (1996) FEBS Lett , vol.392 , pp. 189-193
    • Nakagawa, O.1    Fujisawa, K.2    Ishizaki, T.3    Saito, Y.4    Nakao, K.5    Narumiya, S.6
  • 52
    • 0037341905 scopus 로고    scopus 로고
    • Redox-dependent downregulation of Rho by Rac
    • Nimnual, A.S., L.J. Taylor, and D. Bar-Sagi. 2003. Redox-dependent downregulation of Rho by Rac. Nat. Cell Biol. 5:236-241. http://dx.doi.org/10.1038/ncb938.
    • (2003) Nat. Cell Biol , vol.5 , pp. 236-241
    • Nimnual, A.S.1    Taylor, L.J.2    Bar-Sagi, D.3
  • 53
    • 0025884056 scopus 로고
    • Efficient selection for high-expression transfectants with a novel eukaryotic vector
    • Niwa, H., K. Yamamura, and J. Miyazaki. 1991. Efficient selection for high-expression transfectants with a novel eukaryotic vector. Gene. 108:193-199. http://dx.doi.org/10.1016/0378-1119(91)90434-D.
    • (1991) Gene , vol.108 , pp. 193-199
    • Niwa, H.1    Yamamura, K.2    Miyazaki, J.3
  • 54
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes, C.D., and A. Hall. 1999. Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. Cell Biol. 144:1235-1244. http://dx.doi.org/10.1083/jcb.144.6.1235.
    • (1999) J. Cell Biol , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 55
    • 4644287672 scopus 로고    scopus 로고
    • Recycling endosomes supply AMPA receptors for LTP
    • Park, M., E.C. Penick, J.G. Edwards, J.A. Kauer, and M.D. Ehlers. 2004. Recycling endosomes supply AMPA receptors for LTP. Science. 305:1972-1975. http://dx.doi.org/10.1126/science.1102026.
    • (2004) Science , vol.305 , pp. 1972-1975
    • Park, M.1    Penick, E.C.2    Edwards, J.G.3    Kauer, J.A.4    Ehlers, M.D.5
  • 56
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: integrating cytoskeletal dynamics and cellular tension
    • Parsons, J.T., A.R. Horwitz, and M.A. Schwartz. 2010. Cell adhesion: integrating cytoskeletal dynamics and cellular tension. Nat. Rev. Mol. Cell Biol. 11:633-643. http://dx.doi.org/10.1038/nrm2957.
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schwartz, M.A.3
  • 59
    • 84857137299 scopus 로고    scopus 로고
    • Cofilin under control of β-arrestin-2 in NMDA-dependent dendritic spine plasticity, long-term depression (LTD), and learning
    • Pontrello, C.G., M.-Y. Sun, A. Lin, T.A. Fiacco, K.A. DeFea, and I.M. Ethell. 2012. Cofilin under control of β-arrestin-2 in NMDA-dependent dendritic spine plasticity, long-term depression (LTD), and learning. Proc. Natl. Acad. Sci. USA. 109:E442-E451. http://dx.doi.org/10.1073/pnas.1118803109.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. E442-E451
    • Pontrello, C.G.1    Sun, M.-Y.2    Lin, A.3    Fiacco, T.A.4    DeFea, K.A.5    Ethell, I.M.6
  • 60
    • 67650490390 scopus 로고    scopus 로고
    • Different Rho GTPase-dependent signaling pathways initiate sequential steps in the consolidation of long-term potentiation
    • Rex, C.S., L.Y. Chen, A. Sharma, J. Liu, A.H. Babayan, C.M. Gall, and G. Lynch. 2009. Different Rho GTPase-dependent signaling pathways initiate sequential steps in the consolidation of long-term potentiation. J. Cell Biol. 186:85-97. http://dx.doi.org/10.1083/jcb.200901084.
    • (2009) J. Cell Biol , vol.186 , pp. 85-97
    • Rex, C.S.1    Chen, L.Y.2    Sharma, A.3    Liu, J.4    Babayan, A.H.5    Gall, C.M.6    Lynch, G.7
  • 61
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J., H.F. Paterson, C.L. Johnston, D. Diekmann, and A. Hall. 1992. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell. 70:401-410. http://dx.doi.org/10.1016/0092-8674(92)90164-8.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 62
    • 35148842992 scopus 로고    scopus 로고
    • Attenuation of actinomyosinII contractile activity in growth cones accelerates filopodia-guided and microtubule-based neurite elongation
    • Rösner, H., W. Möller, T. Wassermann, J. Mihatsch, and M. Blum. 2007. Attenuation of actinomyosinII contractile activity in growth cones accelerates filopodia-guided and microtubule-based neurite elongation. Brain Res. 1176:1-10. http://dx.doi.org/10.1016/j.brainres.2007.07.081.
    • (2007) Brain Res , vol.1176 , pp. 1-10
    • Rösner, H.1    Möller, W.2    Wassermann, T.3    Mihatsch, J.4    Blum, M.5
  • 63
    • 30644456796 scopus 로고    scopus 로고
    • A critical role for myosin IIb in dendritic spine morphology and synaptic function
    • Ryu, J., L. Liu, T.P. Wong, D.C. Wu, A. Burette, R. Weinberg, Y.T. Wang, and M. Sheng. 2006. A critical role for myosin IIb in dendritic spine morphology and synaptic function. Neuron. 49:175-182. http://dx.doi.org/10.1016/j.neuron.2005.12.017.
    • (2006) Neuron , vol.49 , pp. 175-182
    • Ryu, J.1    Liu, L.2    Wong, T.P.3    Wu, D.C.4    Burette, A.5    Weinberg, R.6    Wang, Y.T.7    Sheng, M.8
  • 64
    • 37749000819 scopus 로고    scopus 로고
    • High resolution traction force microscopy based on experimental and computational advances
    • Sabass, B., M.L. Gardel, C.M. Waterman, and U.S. Schwarz. 2008. High resolution traction force microscopy based on experimental and computational advances. Biophys. J. 94:207-220. http://dx.doi.org/10.1529/biophysj.107.113670.
    • (2008) Biophys. J , vol.94 , pp. 207-220
    • Sabass, B.1    Gardel, M.L.2    Waterman, C.M.3    Schwarz, U.S.4
  • 65
    • 0033615966 scopus 로고    scopus 로고
    • Rac downregulates Rho activity: reciprocal balance between both GTPases determines cellular morphology and migratory behavior
    • Sander, E.E., J.P. ten Klooster, S. van Delft, R.A. van der Kammen, and J.G. Collard. 1999. Rac downregulates Rho activity: reciprocal balance between both GTPases determines cellular morphology and migratory behavior. J. Cell Biol. 147:1009-1022. http://dx.doi.org/10.1083/jcb.147.5.1009.
    • (1999) J. Cell Biol , vol.147 , pp. 1009-1022
    • Sander, E.E.1    ten Klooster, J.P.2    van Delft, S.3    van der Kammen, R.A.4    Collard, J.G.5
  • 66
    • 54549088877 scopus 로고    scopus 로고
    • Rac activation and inactivation control plasticity of tumor cell movement
    • Sanz-Moreno, V., G. Gadea, J. Ahn, H. Paterson, P. Marra, S. Pinner, E. Sahai, and C.J. Marshall. 2008. Rac activation and inactivation control plasticity of tumor cell movement. Cell. 135:510-523. http://dx.doi.org/10.1016/j.cell.2008.09.043.
    • (2008) Cell , vol.135 , pp. 510-523
    • Sanz-Moreno, V.1    Gadea, G.2    Ahn, J.3    Paterson, H.4    Marra, P.5    Pinner, S.6    Sahai, E.7    Marshall, C.J.8
  • 67
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner, N.C., R.E. Campbell, P.A. Steinbach, B.N.G. Giepmans, A.E. Palmer, and R.Y. Tsien. 2004. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat. Biotechnol. 22:1567-1572. http://dx.doi.org/10.1038/nbt1037.
    • (2004) Nat. Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.G.4    Palmer, A.E.5    Tsien, R.Y.6
  • 68
    • 67649321881 scopus 로고    scopus 로고
    • Focal adhesion kinase acts downstream of EphB receptors to maintain mature dendritic spines by regulating cofilin activity
    • Shi, Y., C.G. Pontrello, K.A. DeFea, L.F. Reichardt, and I.M. Ethell. 2009. Focal adhesion kinase acts downstream of EphB receptors to maintain mature dendritic spines by regulating cofilin activity. J. Neurosci. 29:8129-8142. http://dx.doi.org/10.1523/JNEUROSCI.4681-08.2009.
    • (2009) J. Neurosci , vol.29 , pp. 8129-8142
    • Shi, Y.1    Pontrello, C.G.2    DeFea, K.A.3    Reichardt, L.F.4    Ethell, I.M.5
  • 69
    • 33751171327 scopus 로고    scopus 로고
    • Tight junctions and cell polarity
    • Shin, K., V.C. Fogg, and B. Margolis. 2006. Tight junctions and cell polarity. Annu. Rev. Cell Dev. Biol. 22:207-235. http://dx.doi.org/10.1146/annurev.cellbio.22.010305.104219.
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 207-235
    • Shin, K.1    Fogg, V.C.2    Margolis, B.3
  • 70
    • 84899687377 scopus 로고    scopus 로고
    • Non-muscle myosin II regulates neuronal actin dynamics by interacting with guanine nucleotide exchange factors
    • Shin, E.-Y., C.-S. Lee, C.-Y. Yun, S.-Y. Won, H.-K. Kim, Y.H. Lee, S.-J. Kwak, and E.-G. Kim. 2014. Non-muscle myosin II regulates neuronal actin dynamics by interacting with guanine nucleotide exchange factors. PLoS ONE. 9:e95212. http://dx.doi.org/10.1371/journal.pone.0095212.
    • (2014) PLoS ONE , vol.9
    • Shin, E.-Y.1    Lee, C.-S.2    Yun, C.-Y.3    Won, S.-Y.4    Kim, H.-K.5    Lee, Y.H.6    Kwak, S.-J.7    Kim, E.-G.8
  • 71
    • 84880786274 scopus 로고    scopus 로고
    • Myosin IImediated focal adhesion maturation is tension insensitive
    • Stricker, J., Y. Beckham, M.W. Davidson, and M.L. Gardel. 2013. Myosin IImediated focal adhesion maturation is tension insensitive. PLoS ONE. 8:e70652. http://dx.doi.org/10.1371/journal.pone.0070652.
    • (2013) PLoS ONE , vol.8
    • Stricker, J.1    Beckham, Y.2    Davidson, M.W.3    Gardel, M.L.4
  • 72
    • 3242789407 scopus 로고    scopus 로고
    • Regulation of dendritic spine motility and stability by Rac1 and Rho kinase: evidence for two forms of spine motility
    • Tashiro, A., and R. Yuste. 2004. Regulation of dendritic spine motility and stability by Rac1 and Rho kinase: evidence for two forms of spine motility. Mol. Cell. Neurosci. 26:429-440. http://dx.doi.org/10.1016/j.mcn.2004.04.001.
    • (2004) Mol. Cell. Neurosci , vol.26 , pp. 429-440
    • Tashiro, A.1    Yuste, R.2
  • 73
    • 0033807686 scopus 로고    scopus 로고
    • Regulation of dendritic spine morphology by the rho family of small GTPases: antagonistic roles of Rac and Rho
    • Tashiro, A., A. Minden, and R. Yuste. 2000. Regulation of dendritic spine morphology by the rho family of small GTPases: antagonistic roles of Rac and Rho. Cereb. Cortex. 10:927-938. http://dx.doi.org/10.1093/cercor/10.10.927.
    • (2000) Cereb. Cortex , vol.10 , pp. 927-938
    • Tashiro, A.1    Minden, A.2    Yuste, R.3
  • 74
    • 0034698841 scopus 로고    scopus 로고
    • Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts
    • Totsukawa, G., Y. Yamakita, S. Yamashiro, D.J. Hartshorne, Y. Sasaki, and F. Matsumura. 2000. Distinct roles of ROCK (Rho-kinase) and MLCK in spatial regulation of MLC phosphorylation for assembly of stress fibers and focal adhesions in 3T3 fibroblasts. J. Cell Biol. 150:797-806. http://dx.doi.org/10.1083/jcb.150.4.797.
    • (2000) J. Cell Biol , vol.150 , pp. 797-806
    • Totsukawa, G.1    Yamakita, Y.2    Yamashiro, S.3    Hartshorne, D.J.4    Sasaki, Y.5    Matsumura, F.6
  • 78
    • 0024576739 scopus 로고
    • Effect of multiple phosphorylations of smooth muscle and cytoplasmic myosins on movement in an in vitro motility assay
    • Umemoto, S., A.R. Bengur, and J.R. Sellers. 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
  • 79
    • 80755168331 scopus 로고    scopus 로고
    • Genetic and epigenetic networks in intellectual disabilities
    • van Bokhoven, H. 2011. Genetic and epigenetic networks in intellectual disabilities. Annu. Rev. Genet. 45:81-104. http://dx.doi.org/10.1146/annurevgenet-110410-132512.
    • (2011) Annu. Rev. Genet , vol.45 , pp. 81-104
    • van Bokhoven, H.1
  • 80
    • 79958232399 scopus 로고    scopus 로고
    • RhoA and RhoC have distinct roles in migration and invasion by acting through different targets
    • Vega, F.M., G. Fruhwirth, T. Ng, and A.J. Ridley. 2011. RhoA and RhoC have distinct roles in migration and invasion by acting through different targets. J. Cell Biol. 193:655-665. http://dx.doi.org/10.1083/jcb.201011038.
    • (2011) J. Cell Biol , vol.193 , pp. 655-665
    • Vega, F.M.1    Fruhwirth, G.2    Ng, T.3    Ridley, A.J.4
  • 81
    • 78549241917 scopus 로고    scopus 로고
    • Myosin light chain monoand di-phosphorylation differentially regulate adhesion and polarity in migrating cells
    • Vicente-Manzanares, M., and A.R. Horwitz. 2010. Myosin light chain monoand di-phosphorylation differentially regulate adhesion and polarity in migrating cells. Biochem. Biophys. Res. Commun. 402:537-542. http://dx.doi.org/10.1016/j.bbrc.2010.10.071.
    • (2010) Biochem. Biophys. Res. Commun , vol.402 , pp. 537-542
    • Vicente-Manzanares, M.1    Horwitz, A.R.2
  • 82
    • 33847354235 scopus 로고    scopus 로고
    • Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells
    • Vicente-Manzanares, M., J. Zareno, L. Whitmore, C.K. Choi, and A.F. Horwitz. 2007. Regulation of protrusion, adhesion dynamics, and polarity by myosins IIA and IIB in migrating cells. J. Cell Biol. 176:573-580. http://dx.doi.org/10.1083/jcb.200612043.
    • (2007) J. Cell Biol , vol.176 , pp. 573-580
    • Vicente-Manzanares, M.1    Zareno, J.2    Whitmore, L.3    Choi, C.K.4    Horwitz, A.F.5
  • 83
    • 56149095489 scopus 로고    scopus 로고
    • Segregation and activation of myosin IIB creates a rear in migrating cells
    • Vicente-Manzanares, M., M.A. Koach, L. Whitmore, M.L. Lamers, and A.F. Horwitz. 2008. Segregation and activation of myosin IIB creates a rear in migrating cells. J. Cell Biol. 183:543-554. http://dx.doi.org/10.1083/jcb.200806030.
    • (2008) J. Cell Biol , vol.183 , pp. 543-554
    • Vicente-Manzanares, M.1    Koach, M.A.2    Whitmore, L.3    Lamers, M.L.4    Horwitz, A.F.5
  • 84
    • 70350454867 scopus 로고    scopus 로고
    • Nonmuscle myosin II takes centre stage in cell adhesion and migration
    • Vicente-Manzanares, M., X. Ma, R.S. Adelstein, and A.R. Horwitz. 2009. Nonmuscle myosin II takes centre stage in cell adhesion and migration. Nat. Rev. Mol. Cell Biol. 10:778-790. http://dx.doi.org/10.1038/nrm2786.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 778-790
    • Vicente-Manzanares, M.1    Ma, X.2    Adelstein, R.S.3    Horwitz, A.R.4
  • 85
    • 79955516270 scopus 로고    scopus 로고
    • Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells
    • Vicente-Manzanares, M., K. Newell-Litwa, A.I. Bachir, L.A. Whitmore, and A.R. Horwitz. 2011. Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells. J. Cell Biol. 193:381-396. http://dx.doi.org/10.1083/jcb.201012159.
    • (2011) J. Cell Biol , vol.193 , pp. 381-396
    • Vicente-Manzanares, M.1    Newell-Litwa, K.2    Bachir, A.I.3    Whitmore, L.A.4    Horwitz, A.R.5
  • 87
    • 33846815057 scopus 로고    scopus 로고
    • Regulation of myosin II dynamics by phosphorylation and dephosphorylation of its light chain in epithelial cells
    • Watanabe, T., H. Hosoya, and S. Yonemura. 2007b. Regulation of myosin II dynamics by phosphorylation and dephosphorylation of its light chain in epithelial cells. Mol. Biol. Cell. 18:605-616. http://dx.doi.org/10.1091/mbc. E06-07-0590.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 605-616
    • Watanabe, T.1    Hosoya, H.2    Yonemura, S.3
  • 88
    • 0033787392 scopus 로고    scopus 로고
    • Conditional expression of a truncated fragment of nonmuscle myosin II-A alters cell shape but not cytokinesis in HeLa cells
    • Wei, Q., and R.S. Adelstein. 2000. Conditional expression of a truncated fragment of nonmuscle myosin II-A alters cell shape but not cytokinesis in HeLa cells. Mol. Biol. Cell. 11:3617-3627. http://dx.doi.org/10.1091/mbc.11.10.3617.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3617-3627
    • Wei, Q.1    Adelstein, R.S.2
  • 89
    • 33751256003 scopus 로고    scopus 로고
    • p120-catenin and p190RhoGAP regulate cell-cell adhesion by coordinating antagonism between Rac and Rho
    • Wildenberg, G.A., M.R. Dohn, R.H. Carnahan, M.A. Davis, N.A. Lobdell, J. Settleman, and A.B. Reynolds. 2006. p120-catenin and p190RhoGAP regulate cell-cell adhesion by coordinating antagonism between Rac and Rho. Cell. 127:1027-1039. http://dx.doi.org/10.1016/j.cell.2006.09.046.
    • (2006) Cell , vol.127 , pp. 1027-1039
    • Wildenberg, G.A.1    Dohn, M.R.2    Carnahan, R.H.3    Davis, M.A.4    Lobdell, N.A.5    Settleman, J.6    Reynolds, A.B.7
  • 90
    • 0034235662 scopus 로고    scopus 로고
    • Rapid dendritic remodeling in the developing retina: dependence on neurotransmission and reciprocal regulation by Rac and Rho
    • Wong, W.T., B.E. Faulkner-Jones, J.R. Sanes, and R.O.L. Wong. 2000. Rapid dendritic remodeling in the developing retina: dependence on neurotransmission and reciprocal regulation by Rac and Rho. J. Neurosci. 20:5024-5036.
    • (2000) J. Neurosci , vol.20 , pp. 5024-5036
    • Wong, W.T.1    Faulkner-Jones, B.E.2    Sanes, J.R.3    Wong, R.O.L.4
  • 91
    • 0038037737 scopus 로고    scopus 로고
    • RhoA and ROCK promote migration by limiting membrane protrusions
    • Worthylake, R.A., and K. Burridge. 2003. RhoA and ROCK promote migration by limiting membrane protrusions. J. Biol. Chem. 278:13578-13584. http://dx.doi.org/10.1074/jbc. M211584200.
    • (2003) J. Biol. Chem , vol.278 , pp. 13578-13584
    • Worthylake, R.A.1    Burridge, K.2
  • 92
    • 0034810439 scopus 로고    scopus 로고
    • RhoA/rho-associated kinase mediates fibroblast contractile force generation
    • Yee, H.F., Jr., A.C. Melton, and B.N. Tran. 2001. RhoA/rho-associated kinase mediates fibroblast contractile force generation. Biochem. Biophys. Res. Commun. 280:1340-1345. http://dx.doi.org/10.1006/bbrc.2001.4291.
    • (2001) Biochem. Biophys. Res. Commun , vol.280 , pp. 1340-1345
    • Yee, H.F.1    Melton, A.C.2    Tran, B.N.3
  • 93
    • 23744480002 scopus 로고    scopus 로고
    • The Rho kinases I and II regulate different aspects of myosin II activity
    • Yoneda, A., H.A.B. Multhaupt, and J.R. Couchman. 2005. The Rho kinases I and II regulate different aspects of myosin II activity. J. Cell Biol. 170:443-453. http://dx.doi.org/10.1083/jcb.200412043.
    • (2005) J. Cell Biol , vol.170 , pp. 443-453
    • Yoneda, A.1    Multhaupt, H.A.B.2    Couchman, J.R.3
  • 94
    • 33644747349 scopus 로고    scopus 로고
    • The polarity protein PAR-3 and TIAM1 cooperate in dendritic spine morphogenesis
    • Zhang, H., and I.G. Macara. 2006. The polarity protein PAR-3 and TIAM1 cooperate in dendritic spine morphogenesis. Nat. Cell Biol. 8:227-237. http://dx.doi.org/10.1038/ncb1368.
    • (2006) Nat. Cell Biol , vol.8 , pp. 227-237
    • Zhang, H.1    Macara, I.G.2
  • 95
    • 0037437147 scopus 로고    scopus 로고
    • Synapse formation is regulated by the signaling adaptor GIT1
    • Zhang, H., D.J. Webb, H. Asmussen, and A.F. Horwitz. 2003. Synapse formation is regulated by the signaling adaptor GIT1. J. Cell Biol. 161:131-142. http://dx.doi.org/10.1083/jcb.200211002.
    • (2003) J. Cell Biol , vol.161 , pp. 131-142
    • Zhang, H.1    Webb, D.J.2    Asmussen, H.3    Horwitz, A.F.4

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.