메뉴 건너뛰기




Volumn 127, Issue 16, 2014, Pages 3440-3450

Displacement of p130Cas from focal adhesions links actomyosin contraction to cell migration

Author keywords

Actomyosin; Cell migration; Focal adhesion; Frap; P130Cas; Src

Indexed keywords

CRK ASSOCIATED SUBSTRATE PROTEIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN II; PROTEIN TYROSINE KINASE; ACTIN; BCAR1 PROTEIN, HUMAN; PROTEIN KINASE P60;

EID: 84906070139     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.143438     Document Type: Article
Times cited : (19)

References (62)
  • 2
    • 3042692979 scopus 로고    scopus 로고
    • CD44 interaction with Na+-H+ exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion
    • Bourguignon, L. Y., Singleton, P. A., Diedrich, F., Stern, R. and Gilad, E. (2004). CD44 interaction with Na+-H+ exchanger (NHE1) creates acidic microenvironments leading to hyaluronidase-2 and cathepsin B activation and breast tumor cell invasion. J. Biol. Chem. 279, 26991-27007.
    • (2004) J. Biol. Chem. , vol.279 , pp. 26991-27007
    • Bourguignon, L.Y.1    Singleton, P.A.2    Diedrich, F.3    Stern, R.4    Gilad, E.5
  • 4
    • 0022504694 scopus 로고
    • The absence of myristic acid decreases membrane binding of p60src but does not affect tyrosine protein kinase activity
    • Buss, J. E., Kamps, M. P., Gould, K. and Sefton, B. M. (1986). The absence of myristic acid decreases membrane binding of p60src but does not affect tyrosine protein kinase activity. J. Virol. 58, 468-474.
    • (1986) J. Virol. , vol.58 , pp. 468-474
    • Buss, J.E.1    Kamps, M.P.2    Gould, K.3    Sefton, B.M.4
  • 6
    • 58149230940 scopus 로고    scopus 로고
    • Traction dynamics of filopodia on compliant substrates
    • Chan, C. E. and Odde, D. J. (2008). Traction dynamics of filopodia on compliant substrates. Science 322, 1687-1691.
    • (2008) Science , vol.322 , pp. 1687-1691
    • Chan, C.E.1    Odde, D.J.2
  • 7
    • 56349169536 scopus 로고    scopus 로고
    • Mechanotransduction - a field pulling together
    • Chen, C. S. (2008). Mechanotransduction - a field pulling together? J. Cell Sci. 121, 3285-3292.
    • (2008) J Cell Sci , vol.121 , pp. 3285-3292
    • Chen, C.S.1
  • 9
    • 1642575210 scopus 로고    scopus 로고
    • Regulation and localization of CAS substrate domain tyrosine phosphorylation
    • Fonseca, P. M., Shin, N. Y., Brábek, J., Ryzhova, L., Wu, J. and Hanks, S. K. (2004). Regulation and localization of CAS substrate domain tyrosine phosphorylation. Cell. Signal. 16, 621-629.
    • (2004) Cell. Signal. , vol.16 , pp. 621-629
    • Fonseca, P.M.1    Shin, N.Y.2    Brábek, J.3    Ryzhova, L.4    Wu, J.5    Hanks, S.K.6
  • 12
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix - cytoskeleton crosstalk
    • Geiger, B., Bershadsky, A., Pankov, R. and Yamada, K. M. (2001). Transmembrane crosstalk between the extracellular matrix - cytoskeleton crosstalk. 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
  • 13
    • 35848967591 scopus 로고    scopus 로고
    • Retrograde fluxes of focal adhesion proteins in response to cell migration and mechanical signals
    • Guo,W. H. andWang, Y. L. (2007). Retrograde fluxes of focal adhesion proteins in response to cell migration and mechanical signals. Mol. Biol. Cell 18, 4519-4527.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 4519-4527
    • Guo, W.H.1    Wang, Y.L.2
  • 14
    • 33745245989 scopus 로고    scopus 로고
    • Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration
    • Gupton, S. L. and Waterman-Storer, C. M. (2006). Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration. Cell 125, 1361-1374.
    • (2006) Cell , vol.125 , pp. 1361-1374
    • Gupton, S.L.1    Waterman-Storer, C.M.2
  • 15
    • 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
  • 16
    • 33947319481 scopus 로고    scopus 로고
    • Organized migration of epithelial cells requires control of adhesion and protrusion through Rho kinase effectors
    • Hopkins, A. M., Pineda, A. A., Winfree, L. M., Brown, G. T., Laukoetter, M. G. and Nusrat, A. (2007). Organized migration of epithelial cells requires control of adhesion and protrusion through Rho kinase effectors. Am. J. Physiol. 292, G806-G817.
    • (2007) Am. J. Physiol. , vol.292
    • Hopkins, A.M.1    Pineda, A.A.2    Winfree, L.M.3    Brown, G.T.4    Laukoetter, M.G.5    Nusrat, A.6
  • 19
    • 0036241055 scopus 로고    scopus 로고
    • Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation
    • Hu, C. D., Chinenov, Y. and Kerppola, T. K. (2002). Visualization of interactions among bZIP and Rel family proteins in living cells using bimolecular fluorescence complementation. Mol. Cell 9, 789-798.
    • (2002) Mol. Cell , vol.9 , pp. 789-798
    • Hu, C.D.1    Chinenov, Y.2    Kerppola, T.K.3
  • 20
    • 33846697554 scopus 로고    scopus 로고
    • Differential transmission of actin motion within focal adhesions
    • Hu, K., Ji, L., Applegate, K. T., Danuser, G. and Waterman-Storer, C. M. (2007). Differential transmission of actin motion within focal adhesions. Science 315, 111-115.
    • (2007) Science , vol.315 , pp. 111-115
    • Hu, K.1    Ji, L.2    Applegate, K.T.3    Danuser, G.4    Waterman-Storer, C.M.5
  • 23
    • 43049139541 scopus 로고    scopus 로고
    • p53 regulates glucose metabolism through an IKK-NF-kappaB pathway and inhibits cell transformation
    • Kawauchi, K., Araki, K., Tobiume, K. and Tanaka, N. (2008). p53 regulates glucose metabolism through an IKK-NF-kappaB pathway and inhibits cell transformation. Nat. Cell Biol. 10, 611-618.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 611-618
    • Kawauchi, K.1    Araki, K.2    Tobiume, K.3    Tanaka, N.4
  • 25
    • 70349373396 scopus 로고    scopus 로고
    • Visualization of molecular interactions using bimolecular fluorescence complementation analysis: characteristics of protein fragment complementation
    • Kerppola, T. K. (2009). Visualization of molecular interactions using bimolecular fluorescence complementation analysis: characteristics of protein fragment complementation. Chem. Soc. Rev. 38, 2876-2886.
    • (2009) Chem. Soc. Rev. , vol.38 , pp. 2876-2886
    • Kerppola, T.K.1
  • 26
    • 84875714704 scopus 로고    scopus 로고
    • Focal adhesion size uniquely predicts cell migration
    • Kim, D. H. and Wirtz, D. (2013). Focal adhesion size uniquely predicts cell migration. FASEB J. 27, 1351-1361. Kimura, K., Fukata, Y., Matsuoka, Y., Bennett, V., Matsuura, Y., Okawa, K.
    • (2013) FASEB J , vol.27 , pp. 1351-1361
    • Kim, D.H.1    Wirtz, D.2
  • 28
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer, R. A., Sachsenmaier, C., Cooper, J. A. and Soriano, P. (1999). Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J. 18, 2459-2471.
    • (1999) EMBO J , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 29
    • 33744772918 scopus 로고    scopus 로고
    • Fibronectin rigidity response through Fyn and p130Cas recruitment to the leading edge
    • Kostic, A. and Sheetz, M. P. (2006). Fibronectin rigidity response through Fyn and p130Cas recruitment to the leading edge. Mol. Biol. Cell 17, 2684-2695.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2684-2695
    • Kostic, A.1    Sheetz, M.P.2
  • 31
    • 79953303384 scopus 로고    scopus 로고
    • Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for b-Pix in negative regulation of focal adhesion maturation
    • Kuo, J. C., Han, X., Hsiao, C. T., Yates, J. R., 3rd and Waterman, C. M. (2011). Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for b-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13, 383-393.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 383-393
    • Kuo, J.C.1    Han, X.2    Hsiao, C.T.3    Yates III, J.R.4    Waterman, C.M.5
  • 32
    • 77956915812 scopus 로고    scopus 로고
    • Src-dependent phosphorylation of ROCK participates in regulation of focal adhesion dynamics
    • Lee, H. H., Tien, S. C., Jou, T. S., Chang, Y. C., Jhong, J. G. and Chang, Z. F. (2010). Src-dependent phosphorylation of ROCK participates in regulation of focal adhesion dynamics. J. Cell Sci. 123, 3368-3377.
    • (2010) J. Cell Sci. , vol.123 , pp. 3368-3377
    • Lee, H.H.1    Tien, S.C.2    Jou, T.S.3    Chang, Y.C.4    Jhong, J.G.5    Chang, Z.F.6
  • 33
    • 33644901594 scopus 로고    scopus 로고
    • Mechanical forces alter zyxin unbinding kinetics within focal adhesions of living cells
    • Lele, T. P., Pendse, J., Kumar, S., Salanga, M., Karavitis, J. and Ingber, D. E. (2006). Mechanical forces alter zyxin unbinding kinetics within focal adhesions of living cells. J. Cell. Physiol. 207, 187-194.
    • (2006) J. Cell. Physiol. , vol.207 , pp. 187-194
    • Lele, T.P.1    Pendse, J.2    Kumar, S.3    Salanga, M.4    Karavitis, J.5    Ingber, D.E.6
  • 34
    • 69349095079 scopus 로고    scopus 로고
    • Structural changes in the cytoplasmic domain of the mechanosensitive channel MscS during opening
    • Machiyama, H., Tatsumi, H. and Sokabe, M. (2009). Structural changes in the cytoplasmic domain of the mechanosensitive channel MscS during opening. Biophys. J. 97, 1048-1057.
    • (2009) Biophys. J. , vol.97 , pp. 1048-1057
    • Machiyama, H.1    Tatsumi, H.2    Sokabe, M.3
  • 35
    • 78149441694 scopus 로고    scopus 로고
    • P130Cas Src-binding and substrate domains have distinct roles in sustaining focal adhesion disassembly and promoting cell migration
    • Meenderink, L. M., Ryzhova, L. M., Donato, D. M., Gochberg, D. F., Kaverina, I. and Hanks, S. K. (2010). P130Cas Src-binding and substrate domains have distinct roles in sustaining focal adhesion disassembly and promoting cell migration. PLoS ONE 5, e13412.
    • (2010) PLoS ONE , vol.5
    • Meenderink, L.M.1    Ryzhova, L.M.2    Donato, D.M.3    Gochberg, D.F.4    Kaverina, I.5    Hanks, S.K.6
  • 36
    • 0032904762 scopus 로고    scopus 로고
    • A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo
    • Missbach, M., Jeschke, M., Feyen, J., Müller, K., Glatt, M., Green, J. and Susa, M. (1999). A novel inhibitor of the tyrosine kinase Src suppresses phosphorylation of its major cellular substrates and reduces bone resorption in vitro and in rodent models in vivo. Bone 24, 437-449.
    • (1999) Bone , vol.24 , pp. 437-449
    • Missbach, M.1    Jeschke, M.2    Feyen, J.3    Müller, K.4    Glatt, M.5    Green, J.6    Susa, M.7
  • 37
    • 57049179582 scopus 로고    scopus 로고
    • Highly sensitive and quantitative FRET-FLIM imaging in single dendritic spines using improved non-radiative
    • Murakoshi, H., Lee, S. J. and Yasuda, R. (2008). Highly sensitive and quantitative FRET-FLIM imaging in single dendritic spines using improved non-radiative YFP. Brain Cell Biol. 36, 31-42.
    • (2008) YFP Brain Cell Biol , vol.36 , pp. 31-42
    • Murakoshi, H.1    Lee, S.J.2    Yasuda, R.3
  • 38
    • 0036138908 scopus 로고    scopus 로고
    • A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications
    • Nagai, T., Ibata, K., Park, E. S., Kubota, M., Mikoshiba, K. and Miyawaki, A. (2002). A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications. Nat. Biotechnol. 20, 87-90.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 87-90
    • Nagai, T.1    Ibata, K.2    Park, E.S.3    Kubota, M.4    Mikoshiba, K.5    Miyawaki, A.6
  • 40
    • 14244265617 scopus 로고    scopus 로고
    • Rho-kinase and myosin II activities are required for cell type and environment specific migration
    • Nakayama, M., Amano, M., Katsumi, A., Kaneko, T., Kawabata, S., Takefuji, M. and Kaibuchi, K. (2005). Rho-kinase and myosin II activities are required for cell type and environment specific migration. Genes Cells 10, 107-117.
    • (2005) Genes Cells , vol.10 , pp. 107-117
    • Nakayama, M.1    Amano, M.2    Katsumi, A.3    Kaneko, T.4    Kawabata, S.5    Takefuji, M.6    Kaibuchi, K.7
  • 41
    • 84859387007 scopus 로고    scopus 로고
    • Tension is required but not sufficient for focal adhesion maturation without a stress fiber template
    • Oakes, P. W., Beckham, Y., Stricker, J. and Gardel, M. L. (2012). Tension is required but not sufficient for focal adhesion maturation without a stress fiber template. J. Cell Biol. 196, 363-374.
    • (2012) J. Cell Biol. , vol.196 , pp. 363-374
    • Oakes, P.W.1    Beckham, Y.2    Stricker, J.3    Gardel, M.L.4
  • 42
    • 0027305435 scopus 로고
    • Type IV collagen, laminin, and fibronectin promote the adhesion and migration of rabbit lens epithelial cells in vitro
    • Olivero, D. K. and Furcht, L. T. (1993). Type IV collagen, laminin, and fibronectin promote the adhesion and migration of rabbit lens epithelial cells in vitro. Invest. Ophthalmol. Vis. Sci. 34, 2825-2834.
    • (1993) Invest. Ophthalmol. Vis. Sci. , vol.34 , pp. 2825-2834
    • Olivero, D.K.1    Furcht, L.T.2
  • 43
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: the first ten years
    • Parsons, J. T. (2003). Focal adhesion kinase: the first ten years. J. Cell Sci. 116, 1409-1416.
    • (2003) J. Cell Sci. , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 44
    • 77949754056 scopus 로고    scopus 로고
    • Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation
    • Pasapera, A. M., Schneider, I. C., Rericha, E., Schlaepfer, D. D. and Waterman, C. M. (2010). Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation. J. Cell Biol. 188, 877-890.
    • (2010) J. Cell Biol. , vol.188 , pp. 877-890
    • Pasapera, A.M.1    Schneider, I.C.2    Rericha, E.3    Schlaepfer, D.D.4    Waterman, C.M.5
  • 45
    • 0028889436 scopus 로고
    • Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas
    • Polte, T. R. and Hanks, S. K. (1995). Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas. Proc. Natl. Acad. Sci. USA 92, 10678-10682.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10678-10682
    • Polte, T.R.1    Hanks, S.K.2
  • 46
    • 4544309783 scopus 로고    scopus 로고
    • Two distinct actin networks drive the protrusion of migrating cells
    • Ponti, A., Machacek, M., Gupton, S. L., Waterman-Storer, C. M. and Danuser, G. (2004). Two distinct actin networks drive the protrusion of migrating cells. Science 305, 1782-1786.
    • (2004) Science , vol.305 , pp. 1782-1786
    • Ponti, A.1    Machacek, M.2    Gupton, S.L.3    Waterman-Storer, C.M.4    Danuser, G.5
  • 48
    • 0034769929 scopus 로고    scopus 로고
    • Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src
    • Ruest, P. J., Shin, N. Y., Polte, T. R., Zhang, X. and Hanks, S. K. (2001). Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src. Mol. Cell. Biol. 21, 7641-7652.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7641-7652
    • Ruest, P.J.1    Shin, N.Y.2    Polte, T.R.3    Zhang, X.4    Hanks, S.K.5
  • 49
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
    • Sakai, R., Iwamatsu, A., Hirano, N., Ogawa, S., Tanaka, T., Mano, H., Yazaki, Y. and Hirai, H. (1994). A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J. 13, 3748-3756.
    • (1994) EMBO J , vol.13 , pp. 3748-3756
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Mano, H.6    Yazaki, Y.7    Hirai, H.8
  • 50
    • 12144265571 scopus 로고    scopus 로고
    • Blebbistatin, a myosin II inhibitor, is photoinactivated by blue light
    • Sakamoto, T., Limouze, J., Combs, C. A., Straight, A. F. and Sellers, J. R. (2005). Blebbistatin, a myosin II inhibitor, is photoinactivated by blue light. Biochemistry 44, 584-588.
    • (2005) Biochemistry , vol.44 , pp. 584-588
    • Sakamoto, T.1    Limouze, J.2    Combs, C.A.3    Straight, A.F.4    Sellers, J.R.5
  • 52
    • 79952598024 scopus 로고    scopus 로고
    • Integrins and extracellular matrix in mechanotransduction
    • Schwartz, M. A. (2010). Integrins and extracellular matrix in mechanotransduction. Cold Spring Harb. Perspect. Biol. 2, a005066.
    • (2010) Cold Spring Harb. Perspect. Biol. , vol.2
    • Schwartz, M.A.1
  • 53
    • 4644305806 scopus 로고    scopus 로고
    • Subsets of the major tyrosine phosphorylation sites in Crk-associated substrate (CAS) are sufficient to promote cell migration
    • Shin, N. Y., Dise, R. S., Schneider-Mergener, J., Ritchie, M. D., Kilkenny, D. M. and Hanks, S. K. (2004). Subsets of the major tyrosine phosphorylation sites in Crk-associated substrate (CAS) are sufficient to promote cell migration. J. Biol. Chem. 279, 38331-38337.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38331-38337
    • Shin, N.Y.1    Dise, R.S.2    Schneider-Mergener, J.3    Ritchie, M.D.4    Kilkenny, D.M.5    Hanks, S.K.6
  • 54
    • 84880786274 scopus 로고    scopus 로고
    • Myosin IImediated focal adhesion maturation is tension insensitive
    • Stricker, J., Beckham, Y., Davidson, M. W. and Gardel, M. L. (2013). Myosin IImediated focal adhesion maturation is tension insensitive. PLoS ONE 8, e70652.
    • (2013) PLoS ONE , vol.8
    • Stricker, J.1    Beckham, Y.2    Davidson, M.W.3    Gardel, M.L.4
  • 55
    • 0347513188 scopus 로고    scopus 로고
    • The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress
    • Tsuruta, D. and Jones, J. C. (2003). The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress. J. Cell Sci. 116, 4977-4984.
    • (2003) J. Cell Sci. , vol.116 , pp. 4977-4984
    • Tsuruta, D.1    Jones, J.C.2
  • 57
    • 34247856103 scopus 로고    scopus 로고
    • Flux at focal adhesions: slippage clutch, mechanical gauge, or signal depot
    • Wang, Y. L. (2007). Flux at focal adhesions: slippage clutch, mechanical gauge, or signal depot. Sci. STKE 2007, pe10.
    • (2007) Sci. STKE , vol.2007
    • Wang, Y.L.1
  • 58
    • 0036222784 scopus 로고    scopus 로고
    • Adhesion assembly, disassembly and turnover in migrating cells - over and over and over again
    • Webb, D. J., Parsons, J. T. and Horwitz, A. F. (2002). Adhesion assembly, disassembly and turnover in migrating cells - over and over and over again. Nat. Cell Biol. 4, E97-E100.
    • (2002) Nat. Cell Biol. , vol.4
    • Webb, D.J.1    Parsons, J.T.2    Horwitz, A.F.3
  • 60
    • 77952361543 scopus 로고    scopus 로고
    • PAK4: a pluripotent kinase that regulates prostate cancer cell adhesion
    • Wells, C. M., Whale, A. D., Parsons, M., Masters, J. R. and Jones, G. E. (2010). PAK4: a pluripotent kinase that regulates prostate cancer cell adhesion. J. Cell Sci. 123, 1663-1673.
    • (2010) J. Cell Sci. , vol.123 , pp. 1663-1673
    • Wells, C.M.1    Whale, A.D.2    Parsons, M.3    Masters, J.R.4    Jones, G.E.5
  • 61
    • 79955538660 scopus 로고    scopus 로고
    • Actomyosingenerated tension controls the molecular kinetics of focal adhesions
    • Wolfenson, H., Bershadsky, A., Henis, Y. I. and Geiger, B. (2011). Actomyosingenerated tension controls the molecular kinetics of focal adhesions. J. Cell Sci. 124, 1425-1432.
    • (2011) J. Cell Sci. , vol.124 , pp. 1425-1432
    • Wolfenson, H.1    Bershadsky, A.2    Henis, Y.I.3    Geiger, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.