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Volumn 287, Issue 52, 2012, Pages 43438-43453

The F-BAR protein PACSIN2 regulates epidermal growth factor receptor internalization

Author keywords

[No Author keywords available]

Indexed keywords

CELL MIGRATION; CELL SURFACE EXPRESSION; CELL SURVIVAL; CELLULAR PROCESS; DOMAIN-CONTAINING PROTEINS; ENDOSOMES; EPIDERMAL GROWTH FACTOR RECEPTORS; EPIDERMAL GROWTH FACTORS; GROWTH FACTOR; HUMAN DISEASE; INTRACELLULAR TRAFFICKING; MEMBRANE DYNAMICS; RECEPTOR SIGNALING; RECEPTOR SURFACE; RESTING CELLS;

EID: 84871568885     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.391078     Document Type: Article
Times cited : (24)

References (47)
  • 1
    • 0028170817 scopus 로고
    • Receptor protein-tyrosine kinases and their signal transduction pathways
    • van der Geer, P., Hunter, T., and Lindberg, R. A. (1994) Receptor protein-tyrosine kinases and their signal transduction pathways. Annu. Rev. Cell Biol. 10, 251-337 (Pubitemid 24372822)
    • (1994) Annual Review of Cell Biology , vol.10 , pp. 251-337
    • Van Der, G.P.1    Hunter, T.2    Lindberg, R.A.3
  • 2
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • DOI 10.1038/35077225
    • Blume-Jensen, P., and Hunter, T. (2001) Oncogenic kinase signalling. Nature 411, 355-365 (Pubitemid 32467045)
    • (2001) Nature , vol.411 , Issue.6835 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 3
    • 33847718214 scopus 로고    scopus 로고
    • The EGF receptor family: spearheading a merger of signaling and therapeutics
    • DOI 10.1016/j.ceb.2007.02.008, PII S0955067407000221
    • Bublil, E. M., and Yarden, Y. (2007) The EGF receptor family: spearheading a merger of signaling and therapeutics. Curr. Opin. Cell Biol. 19, 124-134 (Pubitemid 46386405)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.2 , pp. 124-134
    • Bublil, E.M.1    Yarden, Y.2
  • 4
    • 77956344288 scopus 로고    scopus 로고
    • Differential roles of ERK and Akt pathways in regulation of EGFR-mediated signaling and motility in prostate cancer cells
    • Gan, Y., Shi, C., Inge, L., Hibner, M., Balducci, J., and Huang, Y. (2010) Differential roles of ERK and Akt pathways in regulation of EGFR-mediated signaling and motility in prostate cancer cells. Oncogene 29, 4947-4958
    • (2010) Oncogene , vol.29 , pp. 4947-4958
    • Gan, Y.1    Shi, C.2    Inge, L.3    Hibner, M.4    Balducci, J.5    Huang, Y.6
  • 5
    • 0028335378 scopus 로고
    • Regulation of postendocytic trafficking of the epidermal growth factor receptor through endosomal retention
    • Herbst, J. J., Opresko, L. K., Walsh, B. J., Lauffenburger, D. A., and Wiley, H. S. (1994) Regulation of postendocytic trafficking of the epidermal growth factor receptor through endosomal retention. J. Biol. Chem. 269, 12865-12873 (Pubitemid 24202085)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.17 , pp. 12865-12873
    • Herbst, J.J.1    Opresko, L.K.2    Walsh, B.J.3    Lauffenburger, D.A.4    Wiley, H.S.5
  • 6
    • 0030461226 scopus 로고    scopus 로고
    • Control of EGF receptor signaling by clathrin-mediated endocytosis
    • DOI 10.1126/science.274.5295.2086
    • Vieira, A. V., Lamaze, C., and Schmid, S. L. (1996) Control of EGF receptor signaling by clathrin-mediated endocytosis. Science 274, 2086-2089 (Pubitemid 27020702)
    • (1996) Science , vol.274 , Issue.5295 , pp. 2086-2089
    • Vieira, A.V.1    Lamaze, C.2    Schmid, S.L.3
  • 7
    • 48549088895 scopus 로고    scopus 로고
    • Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation
    • Sigismund, S., Argenzio, E., Tosoni, D., Cavallaro, E., Polo, S., and Di Fiore, P. P. (2008) Clathrin-mediated internalization is essential for sustained EGFR signaling but dispensable for degradation. Dev. Cell 15, 209-219
    • (2008) Dev. Cell , vol.15 , pp. 209-219
    • Sigismund, S.1    Argenzio, E.2    Tosoni, D.3    Cavallaro, E.4    Polo, S.5    Di Fiore, P.P.6
  • 9
    • 0037429692 scopus 로고    scopus 로고
    • Trafficking of the ErbB receptors and its influence on signaling
    • Wiley, H. S. (2003) Trafficking of the ErbB receptors and its influence on signaling. Exp. Cell Res. 284, 78-88
    • (2003) Exp. Cell Res. , vol.284 , pp. 78-88
    • Wiley, H.S.1
  • 10
    • 54849372300 scopus 로고    scopus 로고
    • Endocytosis and intracellular trafficking of ErbBs
    • Sorkin, A., and Goh, L. K. (2008) Endocytosis and intracellular trafficking of ErbBs. Exp. Cell Res. 314, 3093-3106
    • (2008) Exp. Cell Res. , vol.314 , pp. 3093-3106
    • Sorkin, A.1    Goh, L.K.2
  • 11
    • 30944435279 scopus 로고    scopus 로고
    • Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis
    • DOI 10.1083/jcb.200508091
    • Tsujita, K., Suetsugu, S., Sasaki, N., Furutani, M., Oikawa, T., and Takenawa, T. (2006) Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J. Cell Biol. 172, 269-279 (Pubitemid 43112973)
    • (2006) Journal of Cell Biology , vol.172 , Issue.2 , pp. 269-279
    • Tsujita, K.1    Suetsugu, S.2    Sasaki, N.3    Furutani, M.4    Oikawa, T.5    Takenawa, T.6
  • 12
    • 64249110493 scopus 로고    scopus 로고
    • The BAR domain superfamily: Membrane-molding macromolecules
    • Frost, A., Unger, V. M., and De Camilli, P. (2009) The BAR domain superfamily: membrane-molding macromolecules. Cell 137, 191-196
    • (2009) Cell , vol.137 , pp. 191-196
    • Frost, A.1    Unger, V.M.2    De Camilli, P.3
  • 13
    • 0037075547 scopus 로고    scopus 로고
    • Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors
    • DOI 10.1038/416183a
    • Soubeyran, P., Kowanetz, K., Szymkiewicz, I., Langdon, W. Y., and Dikic, I. (2002) Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors. Nature 416, 183-187 (Pubitemid 34246476)
    • (2002) Nature , vol.416 , Issue.6877 , pp. 183-187
    • Soubeyran, P.1    Kowanetz, K.2    Szymkiewicz, I.3    Langdon, W.Y.4    Dikic, I.5
  • 14
    • 69249244189 scopus 로고    scopus 로고
    • F-BAR-containing adaptor CIP4 localizes to early endosomes and regulates Epidermal Growth Factor Receptor trafficking and downregulation
    • Hu, J., Troglio, F., Mukhopadhyay, A., Everingham, S., Kwok, E., Scita, G., and Craig, A. W. (2009) F-BAR-containing adaptor CIP4 localizes to early endosomes and regulates Epidermal Growth Factor Receptor trafficking and downregulation. Cell Signal. 21, 1686-1697
    • (2009) Cell Signal. , vol.21 , pp. 1686-1697
    • Hu, J.1    Troglio, F.2    Mukhopadhyay, A.3    Everingham, S.4    Kwok, E.5    Scita, G.6    Craig, A.W.7
  • 15
    • 33847343505 scopus 로고    scopus 로고
    • Pombe Cdc15 homology (PCH) proteins: coordinators of membrane- cytoskeletal interactions
    • DOI 10.1016/j.tcb.2007.01.003, PII S0962892407000190
    • Chitu, V., and Stanley, E. R. (2007) Pombe Cdc15 homology (PCH) proteins: coordinators of membrane-cytoskeletal interactions. Trends Cell Biol. 17, 145-156 (Pubitemid 46341827)
    • (2007) Trends in Cell Biology , vol.17 , Issue.3 , pp. 145-156
    • Chitu, V.1    Stanley, E.R.2
  • 17
    • 4344619558 scopus 로고    scopus 로고
    • The syndapin protein family: Linking membrane trafficking with the cytoskeleton
    • DOI 10.1242/jcs.01290
    • Kessels, M. M., and Qualmann, B. (2004) The syndapin protein family: linking membrane trafficking with the cytoskeleton. J. Cell Sci. 117, 3077-3086 (Pubitemid 39144341)
    • (2004) Journal of Cell Science , vol.117 , Issue.15 , pp. 3077-3086
    • Kessels, M.M.1    Qualmann, B.2
  • 18
    • 33745000739 scopus 로고    scopus 로고
    • Syndapin oligomers interconnect the machineries for endocytic vesicle formation and actin polymerization
    • DOI 10.1074/jbc.M510226200
    • Kessels, M. M., and Qualmann, B. (2006) Syndapin oligomers interconnect the machineries for endocytic vesicle formation and actin polymerization. J. Biol. Chem. 281, 13285-13299 (Pubitemid 43862164)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.19 , pp. 13285-13299
    • Kessels, M.M.1    Qualmann, B.2
  • 20
    • 84858121800 scopus 로고    scopus 로고
    • The role of ubiquitylation in receptor endocytosis and endosomal sorting
    • Haglund, K., and Dikic, I. (2012) The role of ubiquitylation in receptor endocytosis and endosomal sorting. J. Cell Sci. 125, 265-275
    • (2012) J. Cell Sci. , vol.125 , pp. 265-275
    • Haglund, K.1    Dikic, I.2
  • 21
    • 84855275538 scopus 로고    scopus 로고
    • Endosomal accumulation of the activated epidermal growth factor receptor (EGFR) induces apoptosis
    • Rush, J. S., Quinalty, L. M., Engelman, L., Sherry, D. M., and Ceresa, B. P. (2012) Endosomal accumulation of the activated epidermal growth factor receptor (EGFR) induces apoptosis. J. Biol. Chem. 287, 712-722
    • (2012) J. Biol. Chem. , vol.287 , pp. 712-722
    • Rush, J.S.1    Quinalty, L.M.2    Engelman, L.3    Sherry, D.M.4    Ceresa, B.P.5
  • 22
    • 0033058184 scopus 로고    scopus 로고
    • Rho guanine dissociation inhibitors: Pivotal molecules in cellular signalling
    • Olofsson, B. (1999) Rho guanine dissociation inhibitors: pivotal molecules in cellular signalling. Cell Signal. 11, 545-554
    • (1999) Cell Signal. , vol.11 , pp. 545-554
    • Olofsson, B.1
  • 25
    • 0037122897 scopus 로고    scopus 로고
    • An unexpected biochemical and functional interaction between gp130 and the EGF receptor family in breast cancer cells
    • DOI 10.1038/sj/onc/1205100
    • Grant, S. L., Hammacher, A., Douglas, A. M., Goss, G. A., Mansfield, R. K., Heath, J. K., and Begley, C. G. (2002) An unexpected biochemical and functional interaction between gp130 and the EGF receptor family in breast cancer cells. Oncogene 21, 460-474 (Pubitemid 34123808)
    • (2002) Oncogene , vol.21 , Issue.3 , pp. 460-474
    • Grant, S.L.1    Hammacher, A.2    Douglas, A.M.3    Goss, G.A.4    Mansfield, R.K.5    Heath, J.K.6    Begley, C.G.7
  • 27
    • 0037155919 scopus 로고    scopus 로고
    • Hepatocyte growth factor induces ERK-dependent paxillin phosphorylation and regulates paxillin-focal adhesion kinase association
    • DOI 10.1074/jbc.M107551200
    • Liu, Z. X., Yu, C. F., Nickel, C., Thomas, S., and Cantley, L. G. (2002) Hepatocyte growth factor induces ERK-dependent paxillin phosphorylation and regulates paxillin-focal adhesion kinase association. J. Biol. Chem. 277, 10452-10458 (Pubitemid 34968166)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.12 , pp. 10452-10458
    • Liu, Z.-X.1    Yu, C.F.2    Nickel, C.3    Thomas, S.4    Cantley, L.G.5
  • 28
    • 0035174972 scopus 로고    scopus 로고
    • Specificity, diversity, and convergence in VEGF and TNF-α signaling events leading to tissue factor upregulation via EGR-1 in endothelial cells
    • DOI 10.1096/fj.00-0247com
    • Mechtcheriakova, D., Schabbauer, G., Lucerna, M., Clauss, M., De Martin, R., Binder, B. R., and Hofer, E. (2001) Specificity, diversity, and convergence in VEGF and TNF-α signaling events leading to tissue factor upregulation via EGR-1 in endothelial cells. FASEB J. 15, 230-242 (Pubitemid 32061674)
    • (2001) FASEB Journal , vol.15 , Issue.1 , pp. 230-242
    • Mechtcheriakova, D.1    Schabbauer, G.2    Lucerna, M.3    Clauss, M.4    De Martin, R.5    Binder, B.R.6    Hofer, E.7
  • 29
    • 4744365071 scopus 로고    scopus 로고
    • Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex
    • DOI 10.1128/MCB.24.20.8981-8993.2004
    • Schmidt, M. H., Hoeller, D., Yu, J., Furnari, F. B., Cavenee, W. K., Dikic, I., and Bögler, O. (2004) Alix/AIP1 antagonizes epidermal growth factor receptor downregulation by the Cbl-SETA/CIN85 complex. Mol. Cell Biol. 24, 8981-8993 (Pubitemid 39313903)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.20 , pp. 8981-8993
    • Schmidt, M.H.H.1    Hoeller, D.2    Yu, J.3    Furnari, F.B.4    Cavenee, W.K.5    Dikic, I.6    Bogler, O.7
  • 30
    • 77950595663 scopus 로고    scopus 로고
    • SNX-BAR proteins in phosphoinositide-mediated, tubular-based endosomal sorting
    • van Weering, J. R., Verkade, P., and Cullen, P. J. (2010) SNX-BAR proteins in phosphoinositide-mediated, tubular-based endosomal sorting. Semin. Cell Dev. Biol. 21, 371-380
    • (2010) Semin. Cell Dev. Biol. , vol.21 , pp. 371-380
    • Van Weering, J.R.1    Verkade, P.2    Cullen, P.J.3
  • 31
    • 0036904274 scopus 로고    scopus 로고
    • Sorting out the cellular functions of sorting nexins
    • DOI 10.1038/nrm974
    • Worby, C. A., and Dixon, J. E. (2002) Sorting out the cellular functions of sorting nexins. Nat. Rev. Mol. Cell Biol. 3, 919-931 (Pubitemid 35477370)
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , Issue.12 , pp. 919-931
    • Worby, C.A.1    Dixon, J.E.2
  • 32
    • 0029762883 scopus 로고    scopus 로고
    • Enhanced degradation of EGF receptors by a sorting nexin, SNX1
    • Kurten, R. C., Cadena, D. L., and Gill, G. N. (1996) Enhanced degradation of EGF receptors by a sorting nexin, SNX1. Science 272, 1008-1010 (Pubitemid 26259317)
    • (1996) Science , vol.272 , Issue.5264 , pp. 1008-1010
    • Kurten, R.C.1    Cadena, D.L.2    Gill, G.N.3
  • 34
    • 4344629687 scopus 로고    scopus 로고
    • Continual expression of Rab5(Q79L) causes a ligand-independent EGFR internalizaton and diminishes EGFR activity
    • DOI 10.1111/j.1398-9219.2004.00204.x
    • Dinneen, J. L., and Ceresa, B. P. (2004) Continual expression of Rab5(Q79L) causes a ligand-independent EGFR internalization and diminishes EGFR activity. Traffic 5, 606-615 (Pubitemid 39144490)
    • (2004) Traffic , vol.5 , Issue.8 , pp. 606-615
    • Dinneen, J.L.1    Ceresa, B.P.2
  • 35
    • 0037931402 scopus 로고    scopus 로고
    • Quantitative analysis of HER2-mediated effects on HER2 and epidermal growth factor receptor endocytosis. Distribution of homo- and heterodimers depends on relative HER2 levels
    • DOI 10.1074/jbc.M300477200
    • Hendriks, B. S., Opresko, L. K., Wiley, H. S., and Lauffenburger, D. (2003) Quantitative analysis of HER2-mediated effects on HER2 and epidermal growth factor receptor endocytosis: distribution of homo- and heterodimers depends on relative HER2 levels. J. Biol. Chem. 278, 23343-23351 (Pubitemid 36830149)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23343-23351
    • Hendriks, B.S.1    Opresko, L.K.2    Wiley, H.S.3    Lauffenburger, D.4
  • 36
    • 0037374022 scopus 로고    scopus 로고
    • Coregulation of epidermal growth factor receptor/human epidermal growth factor receptor 2 (HER2) levels and locations: Quantitative analysis of HER2 overexpression effects
    • Hendriks, B. S., Opresko, L. K., Wiley, H. S., and Lauffenburger, D. (2003) Coregulation of epidermal growth factor receptor/human epidermal growth factor receptor 2 (HER2) levels and locations: quantitative analysis of HER2 overexpression effects. Cancer Res. 63, 1130-1137 (Pubitemid 36278448)
    • (2003) Cancer Research , vol.63 , Issue.5 , pp. 1130-1137
    • Hendriks, B.S.1    Opresko, L.K.2    Wiley, H.S.3    Lauffenburger, D.4
  • 37
    • 33744927122 scopus 로고    scopus 로고
    • Modeling the effects of HER/ErbB1-3 coexpression on receptor dimerization and biological response
    • DOI 10.1529/biophysj.105.080580
    • Shankaran, H., Wiley, H. S., and Resat, H. (2006) Modeling the effects of HER/ErbB1-3 coexpression on receptor dimerization and biological response. Biophys. J. 90, 3993-4009 (Pubitemid 43846116)
    • (2006) Biophysical Journal , vol.90 , Issue.11 , pp. 3993-4009
    • Shankaran, H.1    Wiley, H.S.2    Resat, H.3
  • 38
    • 0034503124 scopus 로고    scopus 로고
    • All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis
    • Modregger, J., Ritter, B., Witter, B., Paulsson, M., and Plomann, M. (2000) All three PACSIN isoforms bind to endocytic proteins and inhibit endocytosis. J. Cell Sci. 113, 4511-4521 (Pubitemid 32117911)
    • (2000) Journal of Cell Science , vol.113 , Issue.24 , pp. 4511-4521
    • Modregger, J.1    Ritter, B.2    Witter, B.3    Paulsson, M.4    Plomann, M.5
  • 39
    • 0034611006 scopus 로고    scopus 로고
    • Syndapin isoforms participate in receptor-mediated endocytosis and actin organization
    • Qualmann, B., and Kelly, R. B. (2000) Syndapin isoforms participate in receptor-mediated endocytosis and actin organization. J. Cell Biol. 148, 1047-1062
    • (2000) J. Cell Biol. , vol.148 , pp. 1047-1062
    • Qualmann, B.1    Kelly, R.B.2
  • 40
    • 33745929286 scopus 로고    scopus 로고
    • Distinct roles for Tsg101 and Hrs in multivesicular body formation and inward vesiculation
    • DOI 10.1091/mbc.E05-11-1054
    • Razi, M., and Futter, C. E. (2006) Distinct roles for Tsg101 and Hrs in multivesicular body formation and inward vesiculation. Mol. Biol. Cell 17, 3469-3483 (Pubitemid 44156441)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.8 , pp. 3469-3483
    • Razi, M.1    Futter, C.E.2
  • 41
    • 0021702553 scopus 로고
    • Monensin, like methylamine, prevents degradation of 125I-epidermal growth factor, causes intracellular accumulation of receptors and blocks the mitogenic response
    • King, A. C. (1984) Monensin, like methylamine, prevents degradation of 125I-epidermal growth factor, causes intracellular accumulation of receptors and blocks the mitogenic response. Biochem. Biophys. Res. Commun. 124, 585-591
    • (1984) Biochem. Biophys. Res. Commun. , vol.124 , pp. 585-591
    • King, A.C.1
  • 42
    • 0034714277 scopus 로고    scopus 로고
    • Threonine phosphorylation diverts internalized epidermal growth factor receptors from a degradative pathway to the recycling endosome
    • Bao, J., Alroy, I., Waterman, H., Schejter, E. D., Brodie, C., Gruenberg, J., and Yarden, Y. (2000) Threonine phosphorylation diverts internalized epidermal growth factor receptors from a degradative pathway to the recycling endosome. J. Biol. Chem. 275, 26178-26186
    • (2000) J. Biol. Chem. , vol.275 , pp. 26178-26186
    • Bao, J.1    Alroy, I.2    Waterman, H.3    Schejter, E.D.4    Brodie, C.5    Gruenberg, J.6    Yarden, Y.7
  • 43
    • 33845528355 scopus 로고    scopus 로고
    • Prolactin modulates phosphorylation, signaling and trafficking of epidermal growth factor receptor in human T47D breast cancer cells
    • DOI 10.1038/sj.onc.1209740, PII 1209740
    • Huang, Y., Li, X., Jiang, J., and Frank, S. J. (2006) Prolactin modulates phosphorylation, signaling and trafficking of epidermal growth factor receptor in human T47D breast cancer cells. Oncogene 25, 7565-7576 (Pubitemid 44924470)
    • (2006) Oncogene , vol.25 , Issue.58 , pp. 7565-7576
    • Huang, Y.1    Li, X.2    Jiang, J.3    Frank, S.J.4
  • 45
    • 33748917630 scopus 로고    scopus 로고
    • Interaction of SPIN90 with syndapin is implicated in clathrin-mediated endocytic pathway in fibroblasts
    • DOI 10.1111/j.1365-2443.2006.01008.x
    • Kim, S. H., Choi, H. J., Lee, K. W., Hong, N. H., Sung, B. H., Choi, K. Y., Kim, S. M., Chang, S., Eom, S. H., and Song, W. K. (2006) Interaction of SPIN90 with syndapin is implicated in clathrin-mediated endocytic pathway in fibroblasts. Genes Cells 11, 1197-1211 (Pubitemid 44426208)
    • (2006) Genes to Cells , vol.11 , Issue.10 , pp. 1197-1211
    • Kim, S.H.1    Choi, H.J.2    Lee, K.W.3    Hong, N.H.4    Sung, B.H.5    Choi, K.Y.6    Kim, S.-M.7    Chang, S.8    Eom, S.H.9    Song, W.K.10
  • 46
    • 16844383228 scopus 로고    scopus 로고
    • SH2-containing 5′-inositol phosphatase, SHIP2, regulates cytoskeleton organization and ligand-dependent down-regulation of the epidermal growth factor receptor
    • Prasad, N. K., and Decker, S. J. (2005) SH2-containing 5′-inositol phosphatase, SHIP2, regulates cytoskeleton organization and ligand-dependent down-regulation of the epidermal growth factor receptor. J. Biol. Chem. 280, 13129-13136
    • (2005) J. Biol. Chem. , vol.280 , pp. 13129-13136
    • Prasad, N.K.1    Decker, S.J.2
  • 47
    • 38849148269 scopus 로고    scopus 로고
    • Phosphoinositol phosphatase SHIP2 promotes cancer development and metastasis coupled with alterations in EGF receptor turnover
    • DOI 10.1093/carcin/bgm213
    • Prasad, N. K., Tandon, M., Badve, S., Snyder, P. W., and Nakshatri, H. (2008) Phosphoinositol phosphatase SHIP2 promotes cancer development and metastasis coupled with alterations in EGF receptor turnover. Carcinogenesis 29, 25-34 (Pubitemid 351201738)
    • (2008) Carcinogenesis , vol.29 , Issue.1 , pp. 25-34
    • Prasad, N.K.1    Tandon, M.2    Badve, S.3    Snyder, P.W.4    Nakshatri, H.5


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