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Volumn 287, Issue 22, 2012, Pages 18806-18819

Eps8 protein facilitates phagocytosis by increasing TLR4-MyD88 protein interaction in lipopolysaccharide-stimulated macrophages

Author keywords

[No Author keywords available]

Indexed keywords

COLOCALIZATION; COMPLEX FORMATIONS; CYTOSOLS; FOCAL ADHESION KINASE; IMMUNOCOMPLEX; INNATE IMMUNE RESPONSE; KEY REGULATORS; OVER-EXPRESSION; P38 MAPK; PLECKSTRIN HOMOLOGY; PROTEIN INTERACTION; TOLL-LIKE RECEPTORS;

EID: 84861551619     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.340935     Document Type: Article
Times cited : (43)

References (49)
  • 1
    • 0029240538 scopus 로고
    • Phagocytosis
    • Brown, E. J. (1995) Phagocytosis. BioEssays 17, 109-117
    • (1995) BioEssays , vol.17 , pp. 109-117
    • Brown, E.J.1
  • 3
    • 0036216769 scopus 로고    scopus 로고
    • Phagocytosis of microbes. Complexity in action
    • Underhill, D. M., and Ozinsky, A. (2002) Phagocytosis of microbes. Complexity in action. Annu. Rev. Immunol. 20, 825-852
    • (2002) Annu. Rev. Immunol. , vol.20 , pp. 825-852
    • Underhill, D.M.1    Ozinsky, A.2
  • 4
    • 0033046220 scopus 로고    scopus 로고
    • Mechanisms of phagocytosis in macrophages
    • DOI 10.1146/annurev.immunol.17.1.593
    • Aderem, A., and Underhill, D. M. (1999) Mechanisms of phagocytosis in macrophages. Annu. Rev. Immunol. 17, 593-623 (Pubitemid 29241135)
    • (1999) Annual Review of Immunology , vol.17 , pp. 593-623
    • Aderem, A.1    Underhill, D.M.2
  • 5
    • 0036467393 scopus 로고    scopus 로고
    • Phagocytosis and innate immunity
    • DOI 10.1016/S0952-7915(01)00309-0
    • Greenberg, S., and Grinstein, S. (2002) Phagocytosis and innate immunity. Curr. Opin. Immunol. 14, 136-145 (Pubitemid 34085118)
    • (2002) Current Opinion in Immunology , vol.14 , Issue.1 , pp. 136-145
    • Greenberg, S.1    Grinstein, S.2
  • 6
    • 63649108380 scopus 로고    scopus 로고
    • The roles of TLRs, RLRs, and NLRs in pathogen recognition
    • Kawai, T., and Akira, S. (2009) The roles of TLRs, RLRs, and NLRs in pathogen recognition. Int. Immunol. 21, 317-337
    • (2009) Int. Immunol. , vol.21 , pp. 317-337
    • Kawai, T.1    Akira, S.2
  • 7
    • 16644380633 scopus 로고    scopus 로고
    • Integration of Toll-like receptor and phagocytic signaling for tailored immunity
    • Underhill, D. M., and Gantner, B. (2004) Integration of Toll-like receptor and phagocytic signaling for tailored immunity. Microbes Infect. 6, 1368-1373
    • (2004) Microbes Infect. , vol.6 , pp. 1368-1373
    • Underhill, D.M.1    Gantner, B.2
  • 8
    • 0036134963 scopus 로고    scopus 로고
    • Toll-like receptors. How they work and what they do
    • Beutler, B. (2002) Toll-like receptors. How they work and what they do. Curr. Opin. Hematol. 9, 2-10
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 2-10
    • Beutler, B.1
  • 10
    • 46749113860 scopus 로고    scopus 로고
    • MyD88-independent activation of a novel actin-Cdc42/Rac pathway is required for Toll-like receptor-stimulated phagocytosis
    • DOI 10.1038/cr.2008.65, PII CR200865
    • Kong, L., and Ge, B. X. (2008) MyD88-independent activation of a novel actin-Cdc42/Rac pathway is required for Toll-like receptor-stimulated phagocytosis. Cell Res. 18, 745-755 (Pubitemid 351948225)
    • (2008) Cell Research , vol.18 , Issue.7 , pp. 745-755
    • Kong, L.1    Ge, B.-X.2
  • 11
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi, O., and Akira, S. (2010) Pattern recognition receptors and inflammation. Cell 140, 805-820
    • (2010) Cell , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 12
    • 0035804176 scopus 로고    scopus 로고
    • Overexpression of p97Eps8 leads to cellular transformation. Implication of pleckstrin homology domain in p97Eps8-mediated ERK activation
    • Maa, M. C., Hsieh, C. Y., and Leu, T. H. (2001) Overexpression of p97Eps8 leads to cellular transformation. Implication of pleckstrin homology domain in p97Eps8-mediated ERK activation. Oncogene 20, 106-112
    • (2001) Oncogene , vol.20 , pp. 106-112
    • Maa, M.C.1    Hsieh, C.Y.2    Leu, T.H.3
  • 15
    • 0035802118 scopus 로고    scopus 로고
    • An effector region in Eps8 is responsible for the activation of the Rac-specific GEF activity of Sos-1 and for the proper localization of the Rac-based actin-polymerizing machine
    • DOI 10.1083/jcb.200103146
    • Scita, G., Tenca, P., Areces, L. B., Tocchetti, A., Frittoli, E., Giardina, G., Ponzanelli, I., Sini, P., Innocenti, M., and Di Fiore, P. P. (2001) An effector region in Eps8 is responsible for the activation of the Rac-specific GEF activity of Sos-1 and for the proper localization of the Rac-based actin-polymerizing machine. J. Cell Biol. 154, 1031-1044 (Pubitemid 34286182)
    • (2001) Journal of Cell Biology , vol.154 , Issue.5 , pp. 1031-1044
    • Scita, G.1    Tenca, P.2    Areces, L.B.3    Tocchetti, A.4    Frittoli, E.5    Giardina, G.6    Ponzanelli, I.7    Sini, P.8    Innocenti, M.9    Di, F.P.P.10
  • 16
    • 3442898762 scopus 로고    scopus 로고
    • IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness
    • DOI 10.1158/0008-5472.CAN-04-0327
    • Funato, Y., Terabayashi, T., Suenaga, N., Seiki, M., Takenawa, T., and Miki, H. (2004) IRSp53-Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness. Cancer Res. 64, 5237-5244 (Pubitemid 39006543)
    • (2004) Cancer Research , vol.64 , Issue.15 , pp. 5237-5244
    • Funato, Y.1    Terabayashi, T.2    Suenaga, N.3    Seiki, M.4    Takenawa, T.5    Miki, H.6
  • 19
    • 0027179703 scopus 로고
    • Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals
    • Fazioli, F., Minichiello, L., Matoska, V., Castagnino, P., Miki, T., Wong, W. T., and Di Fiore, P. P. (1993) Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals. EMBO J. 12, 3799-3808 (Pubitemid 23282756)
    • (1993) EMBO Journal , vol.12 , Issue.10 , pp. 3799-3808
    • Fazioli, F.1    Minichiello, L.2    Matoska, V.3    Castagnino, P.4    Miki, T.5    Wong, W.T.6    Di, F.P.P.7
  • 20
    • 0033028804 scopus 로고    scopus 로고
    • Enhancement of tyrosyl phosphorylation and protein expression of eps8 by v-Src
    • Maa, M. C., Lai, J. R., Lin, R. W., and Leu, T. H. (1999) Enhancement of tyrosyl phosphorylation and protein expression of eps8 by v-Src. Biochim. Biophys. Acta 1450, 341-351
    • (1999) Biochim. Biophys. Acta , vol.1450 , pp. 341-351
    • Maa, M.C.1    Lai, J.R.2    Lin, R.W.3    Leu, T.H.4
  • 22
    • 34547104027 scopus 로고    scopus 로고
    • Eps8 facilitates cellular growth and motility of colon cancer cells by increasing the expression and activity of focal adhesion kinase
    • Maa, M. C., Lee, J. C., Chen, Y. J., Lee, Y. C., Wang, S. T., Huang, C. C., Chow, N. H., and Leu, T. H. (2007) Eps8 facilitates cellular growth and motility of colon cancer cells by increasing the expression and activity of focal adhesion kinase. J. Biol. Chem. 282, 19399-19409
    • (2007) J. Biol. Chem. , vol.282 , pp. 19399-19409
    • Maa, M.C.1    Lee, J.C.2    Chen, Y.J.3    Lee, Y.C.4    Wang, S.T.5    Huang, C.C.6    Chow, N.H.7    Leu, T.H.8
  • 23
    • 77954504211 scopus 로고    scopus 로고
    • The interplay between Eps8 and IRSp53 contributes to Src-mediated transformation
    • Liu, P. S., Jong, T. H., Maa, M. C., and Leu, T. H. (2010) The interplay between Eps8 and IRSp53 contributes to Src-mediated transformation. Oncogene 29, 3977-3989
    • (2010) Oncogene , vol.29 , pp. 3977-3989
    • Liu, P.S.1    Jong, T.H.2    Maa, M.C.3    Leu, T.H.4
  • 24
    • 57649128307 scopus 로고    scopus 로고
    • Requirement of inducible nitric-oxide synthase in lipopolysaccharide- mediated Src induction and macrophage migration
    • Maa, M. C., Chang, M. Y., Chen, Y. J., Lin, C. H., Yu, C. J., Yang, Y. L., Li, J., Chen, P. R., Tang, C. H., Lei, H. Y., and Leu, T. H. (2008) Requirement of inducible nitric-oxide synthase in lipopolysaccharide-mediated Src induction and macrophage migration. J. Biol. Chem. 283, 31408-31416
    • (2008) J. Biol. Chem. , vol.283 , pp. 31408-31416
    • Maa, M.C.1    Chang, M.Y.2    Chen, Y.J.3    Lin, C.H.4    Yu, C.J.5    Yang, Y.L.6    Li, J.7    Chen, P.R.8    Tang, C.H.9    Lei, H.Y.10    Leu, T.H.11
  • 25
    • 0034775153 scopus 로고    scopus 로고
    • Toll-like receptors control activation of adaptive immune responses
    • DOI 10.1038/ni712
    • Schnare, M., Barton, G. M., Holt, A. C., Takeda, K., Akira, S., and Medzhitov, R. (2001) Toll-like receptors control activation of adaptive immune responses. Nat. Immunol. 2, 947-950 (Pubitemid 32976167)
    • (2001) Nature Immunology , vol.2 , Issue.10 , pp. 947-950
    • Schnare, M.1    Barton, G.M.2    Holt, A.C.3    Takeda, K.4    Akira, S.5    Medzhitov, R.6
  • 26
    • 27944487579 scopus 로고    scopus 로고
    • Lipopolysaccharide-induced c-Src expression plays a role in nitric oxide and TNFα secretion in macrophages
    • DOI 10.1016/j.molimm.2005.03.015, PII S0161589005001252
    • Leu, T. H., Charoenfuprasert, S., Yen, C. K., Fan, C. W., and Maa, M. C. (2006) Lipopolysaccharide-induced c-Src expression plays a role in nitric oxide and TNFα secretion in macrophages. Mol. Immunol. 43, 308-316 (Pubitemid 41668840)
    • (2006) Molecular Immunology , vol.43 , Issue.4 , pp. 308-316
    • Leu, T.-H.1    Charoenfuprasert, S.2    Yen, C.-K.3    Fan, C.-W.4    Maa, M.-C.5
  • 28
    • 0032500744 scopus 로고    scopus 로고
    • Vanadate-dependent FAK activation is accomplished by the sustained FAK Tyr-576/577 phosphorylation
    • Maa, M. C., and Leu, T. H. (1998) Vanadate-dependent FAK activation is accomplished by the sustained FAK Tyr-576/577 phosphorylation. Biochem. Biophys. Res. Commun. 251, 344-349
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 344-349
    • Maa, M.C.1    Leu, T.H.2
  • 30
    • 33646557326 scopus 로고    scopus 로고
    • p130Cas: A versatile scaffold in signaling networks
    • DOI 10.1016/j.tcb.2006.03.003, PII S0962892406000833
    • Defilippi, P., Di Stefano, P., and Cabodi, S. (2006) p130Cas. A versatile scaffold in signaling networks. Trends Cell Biol. 16, 257-263 (Pubitemid 43728873)
    • (2006) Trends in Cell Biology , vol.16 , Issue.5 , pp. 257-263
    • Defilippi, P.1    Di, S.P.2    Cabodi, S.3
  • 31
    • 33846940017 scopus 로고    scopus 로고
    • The differential expression of Yersinia pseudotuberculosis adhesins determines the requirement for FAK and/or Pyk2 during bacterial phagocytosis by macrophages
    • DOI 10.1111/j.1462-5822.2006.00811.x
    • Owen, K. A., Thomas, K. S., and Bouton, A. H. (2007) The differential expression of Yersinia pseudotuberculosis adhesins determines the requirement for FAK and/or Pyk2 during bacterial phagocytosis by macrophages. Cell Microbiol. 9, 596-609 (Pubitemid 46231967)
    • (2007) Cellular Microbiology , vol.9 , Issue.3 , pp. 596-609
    • Owen, K.A.1    Thomas, K.S.2    Bouton, A.H.3
  • 32
    • 77950363453 scopus 로고    scopus 로고
    • PYK2 interacts with MyD88 and regulates MyD88-mediated NF-κB activation in macrophages
    • Xi, C. X., Xiong, F., Zhou Z, Mei, L., and Xiong, W. C. (2010) PYK2 interacts with MyD88 and regulates MyD88-mediated NF-κB activation in macrophages. J. Leukoc. Biol. 87, 415-423
    • (2010) J. Leukoc. Biol. , vol.87 , pp. 415-423
    • Xi, C.X.1    Xiong, F.2    Zhou, Z.3    Mei, L.4    Xiong, W.C.5
  • 33
    • 0035831497 scopus 로고    scopus 로고
    • Inhibition of osteoclast function by adenovirus expressing antisense protein-tyrosine kinase 2
    • Duong, L. T., Nakamura, I., Lakkakorpi, P. T., Lipfert, L., Bett, A. J., and Rodan, G. A. (2001) Inhibition of osteoclast function by adenovirus expressing antisense protein-tyrosine kinase 2. J. Biol. Chem. 276, 7484-7492
    • (2001) J. Biol. Chem. , vol.276 , pp. 7484-7492
    • Duong, L.T.1    Nakamura, I.2    Lakkakorpi, P.T.3    Lipfert, L.4    Bett, A.J.5    Rodan, G.A.6
  • 34
    • 0037838889 scopus 로고    scopus 로고
    • PYK2 autophosphorylation, but not kinase activity, is necessary for adhesion-induced association with c-Src, osteoclast spreading, and bone resorption
    • DOI 10.1074/jbc.M206579200
    • Lakkakorpi, P. T., Bett, A. J., Lipfert, L., Rodan, G. A., and Duong le T. (2003) PYK2 autophosphorylation, but not kinase activity, is necessary for adhesion-induced association with c-Src, osteoclast spreading, and bone resorption. J. Biol. Chem. 278, 11502-11512 (Pubitemid 36792711)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.13 , pp. 11502-11512
    • Lakkakorpi, P.T.1    Bett, A.J.2    Lipfert, L.3    Rodan, G.A.4    Duong, L.T.5
  • 35
    • 0033790639 scopus 로고    scopus 로고
    • Involvement of the Arp2/3 complex in phagocytosis mediated by FcγR or CR3
    • May, R. C., Caron, E., Hall, A., and Machesky, L. M. (2000) Involvement of the Arp2/3 complex in phagocytosis mediated by FcγR or CR3. Nat. Cell Biol. 2, 246-248
    • (2000) Nat. Cell Biol. , vol.2 , pp. 246-248
    • May, R.C.1    Caron, E.2    Hall, A.3    Machesky, L.M.4
  • 36
    • 0029162389 scopus 로고
    • A role for MARCKS, the α isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages
    • Allen, L. H., and Aderem, A. (1995) A role for MARCKS, the α isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages. J. Exp. Med. 182, 829-840
    • (1995) J. Exp. Med. , vol.182 , pp. 829-840
    • Allen, L.H.1    Aderem, A.2
  • 37
    • 0032476593 scopus 로고    scopus 로고
    • Fc receptor-mediated phagocytosis requires CDC42 and Rac1
    • DOI 10.1093/emboj/17.21.6219
    • Massol, P., Montcourrier, P., Guillemot, J. C., and Chavrier, P. (1998) Fc receptor-mediated phagocytosis requires CDC42 and Rac1. EMBO J. 17, 6219-6229 (Pubitemid 28497795)
    • (1998) EMBO Journal , vol.17 , Issue.21 , pp. 6219-6229
    • Massol, P.1    Montcourrier, P.2    Guillemot, J.-C.3    Chavrier, P.4
  • 38
    • 0035805104 scopus 로고    scopus 로고
    • Involvement of FAK/Src complex in the processes of Escherichia coli phagocytosis by insect hemocytes
    • DOI 10.1016/S0014-5793(01)02405-X, PII S001457930102405X
    • Metheniti, A., Paraskevopoulou, N., Lambropoulou, M., and Marmaras, V. J. (2001) Involvement of FAK-Src complex in the processes of Escherichia coli phagocytosis by insect hemocytes. FEBS Lett. 496, 55-59 (Pubitemid 32436421)
    • (2001) FEBS Letters , vol.496 , Issue.1 , pp. 55-59
    • Metheniti, A.1    Paraskevopoulou, N.2    Lambropoulou, M.3    Marmaras, V.J.4
  • 39
    • 0042466638 scopus 로고    scopus 로고
    • Focal adhesion kinase signaling promotes phagocytosis of integrin-bound photoreceptors
    • Finnemann, S. C. (2003) Focal adhesion kinase signaling promotes phagocytosis of integrin-bound photoreceptors. EMBO J. 22, 4143-4154
    • (2003) EMBO J. , vol.22 , pp. 4143-4154
    • Finnemann, S.C.1
  • 40
    • 0035478756 scopus 로고    scopus 로고
    • SRC in the signaling through FcγRII-FcγRIII in murine macrophages
    • DOI 10.1016/S0165-2478(01)00251-6, PII S0165247801002516
    • Antonieta Cote-Vélez, M. J., Ortega, E., and Ortega, A. (2001) Involvement of pp125FAK and p60SRC in the signaling through Fcγ RII-Fcγ RIII in murine macrophages. Immunol. Lett. 78, 189-194 (Pubitemid 32905392)
    • (2001) Immunology Letters , vol.78 , Issue.3 , pp. 189-194
    • Antonieta C.-Velez, M.J.1    Ortega, E.2    Ortega, A.3
  • 42
    • 49849083350 scopus 로고    scopus 로고
    • Eps8 decreases chemosensitivity and affects survival of cervical cancer patients
    • Chen, Y. J., Shen, M. R., Maa, M. C., and Leu, T. H. (2008) Eps8 decreases chemosensitivity and affects survival of cervical cancer patients. Mol. Cancer Ther. 7, 1376-1385
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 1376-1385
    • Chen, Y.J.1    Shen, M.R.2    Maa, M.C.3    Leu, T.H.4
  • 43
    • 2342525996 scopus 로고    scopus 로고
    • Regulation of Phagosome Maturation by Signals from Toll-Like Receptors
    • DOI 10.1126/science.1096158
    • Blander, J. M., and Medzhitov, R. (2004) Regulation of phagosome maturation by signals from Toll-like receptors. Science 304, 1014-1018 (Pubitemid 38638100)
    • (2004) Science , vol.304 , Issue.5673 , pp. 1014-1018
    • Blander, J.M.1    Medzhitov, R.2
  • 44
    • 34548459895 scopus 로고    scopus 로고
    • Structure, function and regulation of the Toll/IL-1 receptor adaptor proteins
    • DOI 10.1038/sj.icb.7100095, PII 7100095
    • Watters, T. M., Kenny, E. F., and O'Neill, L. A. (2007) Structure, function and regulation of the Toll/IL-1 receptor adaptor proteins. Immunol. Cell Biol. 85, 411-419 (Pubitemid 47367505)
    • (2007) Immunology and Cell Biology , vol.85 , Issue.6 , pp. 411-419
    • Watters, T.M.1    Kenny, E.F.2    O'Neill, L.A.J.3
  • 45
    • 33845729059 scopus 로고    scopus 로고
    • The WASP-WAVE protein network: Connecting the membrane to the cytoskeleton
    • DOI 10.1038/nrm2069, PII NRM2069
    • Takenawa, T., and Suetsugu, S. (2007) The WASP-WAVE protein network. Connecting the membrane to the cytoskeleton. Nat. Rev. Mol. Cell Biol. 8, 37-48 (Pubitemid 46012013)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.1 , pp. 37-48
    • Takenawa, T.1    Suetsugu, S.2
  • 46
    • 0036227207 scopus 로고    scopus 로고
    • Restoration of podosomes and chemotaxis in Wiskott-Aldrich syndrome macrophages following induced expression of WASp
    • DOI 10.1016/S1357-2725(01)00162-5, PII S1357272501001625
    • Jones, G. E., Zicha, D., Dunn, G. A., Blundell, M., and Thrasher, A. (2002) Restoration of podosomes and chemotaxis in Wiskott-Aldrich syndrome macrophages following induced expression of WASp. Int. J. Biochem. Cell Biol. 34, 806-815 (Pubitemid 34304169)
    • (2002) International Journal of Biochemistry and Cell Biology , vol.34 , Issue.7 , pp. 806-815
    • Jones, G.E.1    Zicha, D.2    Dunn, G.A.3    Blundell, M.4    Thrasher, A.5
  • 47
    • 29244432463 scopus 로고    scopus 로고
    • A WAVE2-Abi1 complex mediates CSF-1-induced F-actin-rich membrane protrusions and migration in macrophages
    • DOI 10.1242/jcs.02638
    • Kheir, W. A., Gevrey, J. C., Yamaguchi, H., Isaac, B., and Cox, D. (2005) A WAVE2-Abi1 complex mediates CSF-1-induced F-actin-rich membrane protrusions and migration in macrophages. J. Cell Sci. 118, 5369-5379 (Pubitemid 41819598)
    • (2005) Journal of Cell Science , vol.118 , Issue.22 , pp. 5369-5379
    • Kheir, W.A.1    Gevrey, J.-C.2    Yamaguchi, H.3    Isaac, B.4    Cox, D.5
  • 48
    • 0034775391 scopus 로고    scopus 로고
    • Yersinia enterocolitica invasin triggers phagocytosis via beta1 integrins, CDC42Hs and WASp in macrophages
    • DOI 10.1046/j.1462-5822.2001.00149.x
    • Wiedemann, A., Linder, S., Grassl, G., Albert, M., Autenrieth, I., and Aepfelbacher, M. (2001) Yersinia enterocolitica invasin triggers phagocytosis via beta1 integrins, CDC42Hs and WASp in macrophages. Cell Microbiol. 3, 693-702 (Pubitemid 32976340)
    • (2001) Cellular Microbiology , vol.3 , Issue.10 , pp. 693-702
    • Wiedemann, A.1    Linder, S.2    Grassl, G.3    Albert, M.4    Autenrieth, I.5    Aepfelbacher, M.6
  • 49
    • 40549084647 scopus 로고    scopus 로고
    • Membrane targeting of WAVE2 is not sufficient for WAVE2-dependent actin polymerization: A role for IRSp53 in mediating the interaction between Rac and WAVE2
    • DOI 10.1242/jcs.010272
    • Abou-Kheir, W., Isaac, B., Yamaguchi, H., and Cox, D. (2008) Membrane targeting of WAVE2 is not sufficient for WAVE2-dependent actin polymerization. A role for IRSp53 in mediating the interaction between Rac and WAVE2. J. Cell Sci. 121, 379-390 (Pubitemid 351356709)
    • (2008) Journal of Cell Science , vol.121 , Issue.3 , pp. 379-390
    • Abou-Kheir, W.1    Isaac, B.2    Yamaguchi, H.3    Cox, D.4


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