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Volumn 582, Issue 15, 2008, Pages 2283-2290

Simulation of the regulation of EGFR endocytosis and EGFR-ERK signaling by endophilin-mediated RhoA-EGFR crosstalk

Author keywords

EGFR endocytosis; ERK activation; Pathway simulation; RhoA; ROCK

Indexed keywords

ENDOPHILIN; ENDOPHILIN A1; EPIDERMAL GROWTH FACTOR RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE KINASE 1; PHOSPHOPROTEIN PHOSPHATASE 2A; RHO KINASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 46549089054     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2008.05.026     Document Type: Article
Times cited : (31)

References (55)
  • 1
    • 0032514836 scopus 로고    scopus 로고
    • Conspiracy theory: RAS and RAF do not act alone
    • Sternberg P.W., and Alberola-Ila J. Conspiracy theory: RAS and RAF do not act alone. Cell 95 (1998) 447-450
    • (1998) Cell , vol.95 , pp. 447-450
    • Sternberg, P.W.1    Alberola-Ila, J.2
  • 2
    • 33750412872 scopus 로고    scopus 로고
    • Surviving cell death through epidermal growth factor (EGF) signal transduction pathways: implications for cancer therapy
    • Henson E.S., and Gibson S.B. Surviving cell death through epidermal growth factor (EGF) signal transduction pathways: implications for cancer therapy. Cell Signal. 18 (2006) 2089-2097
    • (2006) Cell Signal. , vol.18 , pp. 2089-2097
    • Henson, E.S.1    Gibson, S.B.2
  • 3
    • 33846207546 scopus 로고    scopus 로고
    • Deregulated Ras signaling in developmental disorders: new tricks for an old dog
    • Schubbert S., Bollag G., and Shannon K. Deregulated Ras signaling in developmental disorders: new tricks for an old dog. Curr. Opin. Genet. Dev. 17 (2007) 15-22
    • (2007) Curr. Opin. Genet. Dev. , vol.17 , pp. 15-22
    • Schubbert, S.1    Bollag, G.2    Shannon, K.3
  • 4
    • 33646847329 scopus 로고    scopus 로고
    • Cell signalling: growth factors and tyrosine kinase receptors
    • Perona R. Cell signalling: growth factors and tyrosine kinase receptors. Clin. Trans. Oncol. 8 (2006) 77-82
    • (2006) Clin. Trans. Oncol. , vol.8 , pp. 77-82
    • Perona, R.1
  • 5
    • 10844231985 scopus 로고    scopus 로고
    • Mutations of the epidermal growth factor receptor gene in lung cancer: biological and clinical implications
    • Kosaka T., Yatabe Y., Endoh H., Kuwano H., Takahashi T., and Mitsudomi T. Mutations of the epidermal growth factor receptor gene in lung cancer: biological and clinical implications. Cancer Res. 64 (2004) 8919-8923
    • (2004) Cancer Res. , vol.64 , pp. 8919-8923
    • Kosaka, T.1    Yatabe, Y.2    Endoh, H.3    Kuwano, H.4    Takahashi, T.5    Mitsudomi, T.6
  • 6
    • 28644439423 scopus 로고    scopus 로고
    • The inhibitory effect of ErbB2 on epidermal growth factor-induced formation of clathrin-coated pits correlates with retention of epidermal growth factor receptor-ErbB2 oligomeric complexes at the plasma membrane
    • Haslekas C., Breen K., Pedersen K.W., Johannessen L.E., Stang E., and Madshus I.H. The inhibitory effect of ErbB2 on epidermal growth factor-induced formation of clathrin-coated pits correlates with retention of epidermal growth factor receptor-ErbB2 oligomeric complexes at the plasma membrane. Mol. Biol. Cell 16 (2005) 5832-5842
    • (2005) Mol. Biol. Cell , vol.16 , pp. 5832-5842
    • Haslekas, C.1    Breen, K.2    Pedersen, K.W.3    Johannessen, L.E.4    Stang, E.5    Madshus, I.H.6
  • 7
    • 31644439697 scopus 로고    scopus 로고
    • Geldanamycin stimulates internalization of ErbB2 in a proteasome-dependent way
    • Lerdrup M., Hommelgaard A.M., Grandal M., and van Deurs B. Geldanamycin stimulates internalization of ErbB2 in a proteasome-dependent way. J. Cell Sci. 119 (2006) 85-95
    • (2006) J. Cell Sci. , vol.119 , pp. 85-95
    • Lerdrup, M.1    Hommelgaard, A.M.2    Grandal, M.3    van Deurs, B.4
  • 8
    • 35549013373 scopus 로고    scopus 로고
    • Defective ubiquitinylation of EGFR mutants of lung cancer confers prolonged signaling
    • Shtiegman K., et al. Defective ubiquitinylation of EGFR mutants of lung cancer confers prolonged signaling. Oncogene 26 (2007) 6968-6978
    • (2007) Oncogene , vol.26 , pp. 6968-6978
    • Shtiegman, K.1
  • 9
    • 34748860356 scopus 로고    scopus 로고
    • Epidermal growth factor receptor degradation: an alternative view of oncogenic pathways
    • Kirisits A., Pils D., and Krainer M. Epidermal growth factor receptor degradation: an alternative view of oncogenic pathways. Int. J. Biochem. Cell. Biol. 39 (2007) 2173-2182
    • (2007) Int. J. Biochem. Cell. Biol. , vol.39 , pp. 2173-2182
    • Kirisits, A.1    Pils, D.2    Krainer, M.3
  • 10
    • 33947148666 scopus 로고    scopus 로고
    • Activated Cdc42-associated kinase 1 is a component of EGF receptor signaling complex and regulates EGF receptor degradation
    • Shen F., Lin Q., Gu Y., Childress C., and Yang W. Activated Cdc42-associated kinase 1 is a component of EGF receptor signaling complex and regulates EGF receptor degradation. Mol. Biol. Cell 18 (2007) 732-742
    • (2007) Mol. Biol. Cell , vol.18 , pp. 732-742
    • Shen, F.1    Lin, Q.2    Gu, Y.3    Childress, C.4    Yang, W.5
  • 11
    • 33845950518 scopus 로고    scopus 로고
    • Abl tyrosine kinase regulates endocytosis of the epidermal growth factor receptor
    • Tanos B., and Pendergast A.M. Abl tyrosine kinase regulates endocytosis of the epidermal growth factor receptor. J. Biol. Chem. 281 (2006) 32714-32723
    • (2006) J. Biol. Chem. , vol.281 , pp. 32714-32723
    • Tanos, B.1    Pendergast, A.M.2
  • 12
    • 26044447158 scopus 로고    scopus 로고
    • Rho mediates endocytosis of epidermal growth factor receptor through phosphorylation of endophilin A1 by Rho-kinase
    • Kaneko T., et al. Rho mediates endocytosis of epidermal growth factor receptor through phosphorylation of endophilin A1 by Rho-kinase. Genes Cell 10 (2005) 973-987
    • (2005) Genes Cell , vol.10 , pp. 973-987
    • Kaneko, T.1
  • 13
    • 0032567503 scopus 로고    scopus 로고
    • Endocytosis of functional epidermal growth factor receptor-green fluorescent protein chimera
    • Carter R.E., and Sorkin A. Endocytosis of functional epidermal growth factor receptor-green fluorescent protein chimera. J. Biol. Chem. 273 (1998) 35000-35007
    • (1998) J. Biol. Chem. , vol.273 , pp. 35000-35007
    • Carter, R.E.1    Sorkin, A.2
  • 14
    • 0032498995 scopus 로고    scopus 로고
    • Signal transduction. Taking the Rap
    • Marshall C.J. Signal transduction. Taking the Rap. Nature 392 (1998) 553-554
    • (1998) Nature , vol.392 , pp. 553-554
    • Marshall, C.J.1
  • 16
    • 34248583886 scopus 로고    scopus 로고
    • MAP kinase signalling pathways in cancer
    • Dhillon A.S., Hagan S., Rath O., and Kolch W. MAP kinase signalling pathways in cancer. Oncogene 26 (2007) 3279-3290
    • (2007) Oncogene , vol.26 , pp. 3279-3290
    • Dhillon, A.S.1    Hagan, S.2    Rath, O.3    Kolch, W.4
  • 17
    • 31844450444 scopus 로고    scopus 로고
    • Targeting Rho and Rho-kinase in the treatment of cardiovascular disease
    • Budzyn K., Marley P.D., and Sobey C.G. Targeting Rho and Rho-kinase in the treatment of cardiovascular disease. Trends Pharmacol. Sci. 27 (2006) 97-104
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 97-104
    • Budzyn, K.1    Marley, P.D.2    Sobey, C.G.3
  • 18
    • 34249301303 scopus 로고    scopus 로고
    • Development of Rho-kinase inhibitors for cardiovascular medicine
    • Shimokawa H., and Rashid M. Development of Rho-kinase inhibitors for cardiovascular medicine. Trends Pharmacol. Sci. 28 (2007) 296-302
    • (2007) Trends Pharmacol. Sci. , vol.28 , pp. 296-302
    • Shimokawa, H.1    Rashid, M.2
  • 19
    • 33747175707 scopus 로고    scopus 로고
    • Rho kinase: a target for treating urinary bladder dysfunction?
    • Peters S.L., Schmidt M., and Michel M.C. Rho kinase: a target for treating urinary bladder dysfunction?. Trends Pharmacol. Sci. 27 (2006) 492-497
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 492-497
    • Peters, S.L.1    Schmidt, M.2    Michel, M.C.3
  • 21
    • 27844604200 scopus 로고    scopus 로고
    • Rho GTPases and the control of cell behaviour
    • Hall A. Rho GTPases and the control of cell behaviour. Biochem. Soc. Trans. 33 (2005) 891-895
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 891-895
    • Hall, A.1
  • 24
    • 3342893272 scopus 로고    scopus 로고
    • Rho family GTPases cooperate with p53 deletion to promote primary mouse embryonic fibroblast cell invasion
    • Guo F., and Zheng Y. Rho family GTPases cooperate with p53 deletion to promote primary mouse embryonic fibroblast cell invasion. Oncogene 23 (2004) 5577-5585
    • (2004) Oncogene , vol.23 , pp. 5577-5585
    • Guo, F.1    Zheng, Y.2
  • 25
    • 33847627873 scopus 로고    scopus 로고
    • Tumor suppressor p53 restricts Ras stimulation of RhoA and cancer cell motility
    • Xia M., and Land H. Tumor suppressor p53 restricts Ras stimulation of RhoA and cancer cell motility. Nat. Struct. Mol. Biol. 14 (2007) 215-223
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 215-223
    • Xia, M.1    Land, H.2
  • 27
    • 0036212767 scopus 로고    scopus 로고
    • Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors
    • Schoeberl B., Eichler-Jonsson C., Gilles E.D., and Muller G. Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors. Nat. Biotechnol. 20 (2002) 370-375
    • (2002) Nat. Biotechnol. , vol.20 , pp. 370-375
    • Schoeberl, B.1    Eichler-Jonsson, C.2    Gilles, E.D.3    Muller, G.4
  • 28
    • 0034613112 scopus 로고    scopus 로고
    • Differential feedback regulation of the MAPK cascade underlies the quantitative differences in EGF and NGF signalling in PC12 cells
    • Brightman F.A., and Fell D.A. Differential feedback regulation of the MAPK cascade underlies the quantitative differences in EGF and NGF signalling in PC12 cells. FEBS Lett. 482 (2000) 169-174
    • (2000) FEBS Lett. , vol.482 , pp. 169-174
    • Brightman, F.A.1    Fell, D.A.2
  • 29
    • 0033570090 scopus 로고    scopus 로고
    • Quantification of short term signaling by the epidermal growth factor receptor
    • Kholodenko B.N., Demin O.V., Moehren G., and Hoek J.B. Quantification of short term signaling by the epidermal growth factor receptor. J. Biol. Chem. 274 (1999) 30169-30181
    • (1999) J. Biol. Chem. , vol.274 , pp. 30169-30181
    • Kholodenko, B.N.1    Demin, O.V.2    Moehren, G.3    Hoek, J.B.4
  • 30
    • 33746021158 scopus 로고    scopus 로고
    • Scaffolding protein Grb2-associated binder 1 sustains epidermal growth factor-induced mitogenic and survival signaling by multiple positive feedback loops
    • Kiyatkin A., Aksamitiene E., Markevich N.I., Borisov N.M., Hoek J.B., and Kholodenko B.N. Scaffolding protein Grb2-associated binder 1 sustains epidermal growth factor-induced mitogenic and survival signaling by multiple positive feedback loops. J. Biol. Chem. 281 (2006) 19925-19938
    • (2006) J. Biol. Chem. , vol.281 , pp. 19925-19938
    • Kiyatkin, A.1    Aksamitiene, E.2    Markevich, N.I.3    Borisov, N.M.4    Hoek, J.B.5    Kholodenko, B.N.6
  • 31
    • 17344362384 scopus 로고    scopus 로고
    • Prediction and validation of the distinct dynamics of transient and sustained ERK activation
    • Sasagawa S., Ozaki Y., Fujita K., and Kuroda S. Prediction and validation of the distinct dynamics of transient and sustained ERK activation. Nat. Cell Biol. 7 (2005) 365-373
    • (2005) Nat. Cell Biol. , vol.7 , pp. 365-373
    • Sasagawa, S.1    Ozaki, Y.2    Fujita, K.3    Kuroda, S.4
  • 32
    • 0942300661 scopus 로고    scopus 로고
    • Model analysis of difference between EGF pathway and FGF pathway
    • Yamada S., Taketomi T., and Yoshimura A. Model analysis of difference between EGF pathway and FGF pathway. Biochem. Biophys. Res. Commun. 314 (2004) 1113-1120
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 1113-1120
    • Yamada, S.1    Taketomi, T.2    Yoshimura, A.3
  • 34
    • 35348997467 scopus 로고    scopus 로고
    • ROCK-II mediates colon cancer invasion via regulation of MMP-2 and MMP-13 at the site of invadopodia as revealed by multiphoton imaging
    • Vishnubhotla R., Sun S., Huq J., Bulic M., Ramesh A., Guzman G., Cho M., and Glover S.C. ROCK-II mediates colon cancer invasion via regulation of MMP-2 and MMP-13 at the site of invadopodia as revealed by multiphoton imaging. Lab. Invest. 87 (2007) 1149-1158
    • (2007) Lab. Invest. , vol.87 , pp. 1149-1158
    • Vishnubhotla, R.1    Sun, S.2    Huq, J.3    Bulic, M.4    Ramesh, A.5    Guzman, G.6    Cho, M.7    Glover, S.C.8
  • 35
    • 16344377134 scopus 로고    scopus 로고
    • MAPK cascade possesses decoupled controllability of signal amplification and duration
    • Mayawala K., Gelmi C.A., and Edwards J.S. MAPK cascade possesses decoupled controllability of signal amplification and duration. Biophys. J. 87 (2004) L01-L02
    • (2004) Biophys. J. , vol.87
    • Mayawala, K.1    Gelmi, C.A.2    Edwards, J.S.3
  • 36
    • 34250223002 scopus 로고    scopus 로고
    • Small rho GTPases mediate tumor-induced inhibition of endocytic activity of dendritic cells
    • Tourkova I.L., Shurin G.V., Wei S., and Shurin M.R. Small rho GTPases mediate tumor-induced inhibition of endocytic activity of dendritic cells. J. Immunol. 178 (2007) 7787-7793
    • (2007) J. Immunol. , vol.178 , pp. 7787-7793
    • Tourkova, I.L.1    Shurin, G.V.2    Wei, S.3    Shurin, M.R.4
  • 37
    • 0037449194 scopus 로고    scopus 로고
    • PKC is required for activation of ROCK by RhoA in human endothelial cells
    • Barandier C., Ming X.F., Rusconi S., and Yang Z. PKC is required for activation of ROCK by RhoA in human endothelial cells. Biochem. Biophys. Res. Commun. 304 (2003) 714-719
    • (2003) Biochem. Biophys. Res. Commun. , vol.304 , pp. 714-719
    • Barandier, C.1    Ming, X.F.2    Rusconi, S.3    Yang, Z.4
  • 38
    • 34548426552 scopus 로고    scopus 로고
    • Rho-ROCK inhibitors as emerging strategies to promote nerve regeneration
    • Kubo T., Hata K., Yamaguchi A., and Yamashita T. Rho-ROCK inhibitors as emerging strategies to promote nerve regeneration. Curr. Pharm. Des. 13 (2007) 2493-2499
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 2493-2499
    • Kubo, T.1    Hata, K.2    Yamaguchi, A.3    Yamashita, T.4
  • 39
    • 0034704153 scopus 로고    scopus 로고
    • MEKK1 binds raf-1 and the ERK2 cascade components
    • Karandikar M., Xu S., and Cobb M.H. MEKK1 binds raf-1 and the ERK2 cascade components. J. Biol. Chem. 275 (2000) 40120-40127
    • (2000) J. Biol. Chem. , vol.275 , pp. 40120-40127
    • Karandikar, M.1    Xu, S.2    Cobb, M.H.3
  • 40
    • 4444272353 scopus 로고    scopus 로고
    • Modelling the dynamics of the yeast pheromone pathway
    • Kofahl B., and Klipp E. Modelling the dynamics of the yeast pheromone pathway. Yeast 21 (2004) 831-850
    • (2004) Yeast , vol.21 , pp. 831-850
    • Kofahl, B.1    Klipp, E.2
  • 41
    • 0345826110 scopus 로고    scopus 로고
    • RhoA binds to the amino terminus of MEKK1 and regulates its kinase activity
    • Gallagher E.D., Gutowski S., Sternweis P.C., and Cobb M.H. RhoA binds to the amino terminus of MEKK1 and regulates its kinase activity. J. Biol. Chem. 279 (2004) 1872-1877
    • (2004) J. Biol. Chem. , vol.279 , pp. 1872-1877
    • Gallagher, E.D.1    Gutowski, S.2    Sternweis, P.C.3    Cobb, M.H.4
  • 42
    • 33746889808 scopus 로고    scopus 로고
    • A comprehensive pathway map of epidermal growth factor receptor signaling
    • Oda K., Matsuoka Y., Funahashi A., and Kitano H. A comprehensive pathway map of epidermal growth factor receptor signaling. Mol. Syst. Biol. 1 (2005) 0010
    • (2005) Mol. Syst. Biol. , vol.1 , pp. 0010
    • Oda, K.1    Matsuoka, Y.2    Funahashi, A.3    Kitano, H.4
  • 44
    • 0034011765 scopus 로고    scopus 로고
    • Regulation of signal transduction by endocytosis
    • Ceresa B.P., and Schmid S.L. Regulation of signal transduction by endocytosis. Curr. Opin. Cell. Biol. 12 (2000) 204-210
    • (2000) Curr. Opin. Cell. Biol. , vol.12 , pp. 204-210
    • Ceresa, B.P.1    Schmid, S.L.2
  • 45
    • 21644464655 scopus 로고    scopus 로고
    • Activation of EGF receptor endocytosis and ERK1/2 signaling by BPGAP1 requires direct interaction with EEN/endophilin II and a functional RhoGAP domain
    • Lua B.L., and Low B.C. Activation of EGF receptor endocytosis and ERK1/2 signaling by BPGAP1 requires direct interaction with EEN/endophilin II and a functional RhoGAP domain. J. Cell Sci. 118 (2005) 2707-2721
    • (2005) J. Cell Sci. , vol.118 , pp. 2707-2721
    • Lua, B.L.1    Low, B.C.2
  • 46
    • 33846662015 scopus 로고    scopus 로고
    • Cell type-specific functions of Rho GTPases revealed by gene targeting in mice
    • Wang L., and Zheng Y. Cell type-specific functions of Rho GTPases revealed by gene targeting in mice. Trends Cell Biol. 17 (2007) 58-64
    • (2007) Trends Cell Biol. , vol.17 , pp. 58-64
    • Wang, L.1    Zheng, Y.2
  • 47
    • 33745171133 scopus 로고    scopus 로고
    • RhoA and RhoC proteins promote both cell proliferation and cell invasion of human oesophageal squamous cell carcinoma cell lines in vitro and in vivo
    • Faried A., et al. RhoA and RhoC proteins promote both cell proliferation and cell invasion of human oesophageal squamous cell carcinoma cell lines in vitro and in vivo. Eur. J. Cancer 42 (2006) 1455-1465
    • (2006) Eur. J. Cancer , vol.42 , pp. 1455-1465
    • Faried, A.1
  • 48
    • 33750468907 scopus 로고    scopus 로고
    • Role of RhoA inactivation in reduced cell proliferation of human airway smooth muscle by simvastatin
    • Takeda N., Kondo M., Ito S., Ito Y., Shimokata K., and Kume H. Role of RhoA inactivation in reduced cell proliferation of human airway smooth muscle by simvastatin. Am. J. Respir. Cell Mol. Biol. 35 (2006) 722-729
    • (2006) Am. J. Respir. Cell Mol. Biol. , vol.35 , pp. 722-729
    • Takeda, N.1    Kondo, M.2    Ito, S.3    Ito, Y.4    Shimokata, K.5    Kume, H.6
  • 49
    • 33644524741 scopus 로고    scopus 로고
    • Cell-signalling dynamics in time and space
    • Kholodenko B.N. Cell-signalling dynamics in time and space. Nat. Rev. Mol. Cell Biol. 7 (2006) 165-176
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 165-176
    • Kholodenko, B.N.1
  • 50
    • 0032502733 scopus 로고    scopus 로고
    • Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA
    • Zhang B., Chernoff J., and Zheng Y. Interaction of Rac1 with GTPase-activating proteins and putative effectors. A comparison with Cdc42 and RhoA. J. Biol. Chem. 273 (1998) 8776-8782
    • (1998) J. Biol. Chem. , vol.273 , pp. 8776-8782
    • Zhang, B.1    Chernoff, J.2    Zheng, Y.3
  • 51
    • 46549084806 scopus 로고    scopus 로고
    • MathWorks, T. (2007) Matlabed (Eds.), The MathWorks Inc., Natick, MA.
    • MathWorks, T. (2007) Matlabed (Eds.), The MathWorks Inc., Natick, MA.
  • 52
    • 4344683428 scopus 로고    scopus 로고
    • Differential activation of epidermal growth factor (EGF) receptor downstream signaling pathways by betacellulin and EGF
    • Saito T., et al. Differential activation of epidermal growth factor (EGF) receptor downstream signaling pathways by betacellulin and EGF. Endocrinology 145 (2004) 4232-4243
    • (2004) Endocrinology , vol.145 , pp. 4232-4243
    • Saito, T.1
  • 53
    • 0029077563 scopus 로고
    • Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1)
    • Russell M., Lange-Carter C.A., and Johnson G.L. Direct interaction between Ras and the kinase domain of mitogen-activated protein kinase kinase kinase (MEKK1). J. Biol. Chem. 270 (1995) 11757-11760
    • (1995) J. Biol. Chem. , vol.270 , pp. 11757-11760
    • Russell, M.1    Lange-Carter, C.A.2    Johnson, G.L.3
  • 54
    • 0032544739 scopus 로고    scopus 로고
    • Grb2 interaction with MEK-kinase 1 is involved in regulation of Jun-kinase activities in response to epidermal growth factor
    • Pomerance M., Multon M.C., Parker F., Venot C., Blondeau J.P., Tocque B., and Schweighoffer F. Grb2 interaction with MEK-kinase 1 is involved in regulation of Jun-kinase activities in response to epidermal growth factor. J. Biol. Chem. 273 (1998) 24301-24304
    • (1998) J. Biol. Chem. , vol.273 , pp. 24301-24304
    • Pomerance, M.1    Multon, M.C.2    Parker, F.3    Venot, C.4    Blondeau, J.P.5    Tocque, B.6    Schweighoffer, F.7


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