메뉴 건너뛰기




Volumn 25, Issue 14, 2005, Pages 6090-6102

Targeted deletion of the integrin β4 signaling domain suppresses laminin-5-dependent nuclear entry of mitogen-activated protein kinases and NF-κB, causing defects in epidermal growth and migration

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA6BETA4 INTEGRIN; EPIDERMAL GROWTH FACTOR; FIBRONECTIN; I KAPPA B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; KALININ; MATRIX PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; STRESS ACTIVATED PROTEIN KINASE;

EID: 21744455891     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.14.6090-6102.2005     Document Type: Article
Times cited : (115)

References (55)
  • 1
    • 0036629349 scopus 로고    scopus 로고
    • Cell adhesion differentially regulates the nucleocytoplasmic distribution of active MAP kinases
    • Aplin, A. E., B. P. Hogan, J. Tomeu, and R. L. Juliano. 2002. Cell adhesion differentially regulates the nucleocytoplasmic distribution of active MAP kinases. J. Cell Sci. 115:2781-2790.
    • (2002) J. Cell Sci. , vol.115 , pp. 2781-2790
    • Aplin, A.E.1    Hogan, B.P.2    Tomeu, J.3    Juliano, R.L.4
  • 2
    • 0035897407 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1
    • Aplin, A. E., S. A. Stewart, R. K. Assoian, and R. L. Juliano. 2001. Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1. J. Cell Biol. 153:273-282.
    • (2001) J. Cell Biol. , vol.153 , pp. 273-282
    • Aplin, A.E.1    Stewart, S.A.2    Assoian, R.K.3    Juliano, R.L.4
  • 3
    • 0034611731 scopus 로고    scopus 로고
    • Integrin LFA-1 interacts with the transcriptional coactivator JAB1 to modulate AP-1 activity
    • Bianchi, E., S. Denti, A. Granata, G. Bossi, J. Geginat, A. Villa, L. Rogge, and R. Pardi. 2000. Integrin LFA-1 interacts with the transcriptional coactivator JAB1 to modulate AP-1 activity. Nature 404:617-621.
    • (2000) Nature , vol.404 , pp. 617-621
    • Bianchi, E.1    Denti, S.2    Granata, A.3    Bossi, G.4    Geginat, J.5    Villa, A.6    Rogge, L.7    Pardi, R.8
  • 5
    • 0037078320 scopus 로고    scopus 로고
    • Gab1 and SHP-2 promote Ras/MAPK regulation of epidermal growth and differentiation
    • Cai, T., K. Nishida, T. Hirano, and P. A. Khavari. 2002. Gab1 and SHP-2 promote Ras/MAPK regulation of epidermal growth and differentiation. J. Cell Biol. 159:103-112.
    • (2002) J. Cell Biol. , vol.159 , pp. 103-112
    • Cai, T.1    Nishida, K.2    Hirano, T.3    Khavari, P.A.4
  • 6
    • 4444361792 scopus 로고    scopus 로고
    • Integrin α3β1 directs the stabilization of a polarized lamellipodium in epithelial cells through activation of Rac1
    • Choma, D. P., K. Pumiglia, and C. M. DiPersio. 2004. Integrin α3β1 directs the stabilization of a polarized lamellipodium in epithelial cells through activation of Rac1. J. Cell Sci. 117:3947-3959.
    • (2004) J. Cell Sci. , vol.117 , pp. 3947-3959
    • Choma, D.P.1    Pumiglia, K.2    Dipersio, C.M.3
  • 7
    • 0035847016 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the β4 integrin cytoplasmic domain mediates Shc signaling to extracellular signal-regulated kinase and antagonizes formation of hemidesmosomes
    • Dans, M., L. Gagnoux-Palacios, P. Blaikie, S. Klein, A. Mariotti, and F. G. Giancotti. 2001. Tyrosine phosphorylation of the β4 integrin cytoplasmic domain mediates Shc signaling to extracellular signal-regulated kinase and antagonizes formation of hemidesmosomes. J. Biol. Chem. 276:1494-1502.
    • (2001) J. Biol. Chem. , vol.276 , pp. 1494-1502
    • Dans, M.1    Gagnoux-Palacios, L.2    Blaikie, P.3    Klein, S.4    Mariotti, A.5    Giancotti, F.G.6
  • 9
    • 0033828682 scopus 로고    scopus 로고
    • α3β1 and α6β4 integrin receptors for laminin-5 are not essential for epidermal morphogenesis and homeostasis during skin development
    • DiPersio, C. M., R. van der Neut, E. Georges-Labouesse, J. A. Kreidberg, A. Sonnenberg, and R. O. Hynes. 2000. α3β1 and α6β4 integrin receptors for laminin-5 are not essential for epidermal morphogenesis and homeostasis during skin development. J. Cell Sci. 113:3051-3062.
    • (2000) J. Cell Sci. , vol.113 , pp. 3051-3062
    • DiPersio, C.M.1    Van Der Neut, R.2    Georges-Labouesse, E.3    Kreidberg, J.A.4    Sonnenberg, A.5    Hynes, R.O.6
  • 10
    • 0029666420 scopus 로고    scopus 로고
    • β4 integrin is required for hemidesmosome formation, cell adhesion and cell survival
    • Dowling, J., Q. C. Yu, and E. Fuchs. 1996. β4 integrin is required for hemidesmosome formation, cell adhesion and cell survival. J. Cell Biol. 134:559-572.
    • (1996) J. Cell Biol. , vol.134 , pp. 559-572
    • Dowling, J.1    Yu, Q.C.2    Fuchs, E.3
  • 11
    • 0030829724 scopus 로고    scopus 로고
    • Integrators of epidermal growth and differentiation: Distinct functions for β1 and β4 integrins
    • Fuchs, E., J. Dowling, J. Segre, S. H. Lo, and Q. C. Yu. 1997. Integrators of epidermal growth and differentiation: distinct functions for β1 and β4 integrins. Curr. Opin. Genet. Dev. 7:672-682.
    • (1997) Curr. Opin. Genet. Dev. , vol.7 , pp. 672-682
    • Fuchs, E.1    Dowling, J.2    Segre, J.3    Lo, S.H.4    Yu, Q.C.5
  • 13
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F. G., and E. Ruoslahti. 1999. Integrin signaling. Science 285:1028-1032.
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 14
    • 0345687500 scopus 로고    scopus 로고
    • Positional control of cell fate through joint integrin/receptor protein kinase signaling
    • Giancotti, F. G., and G. Tarone. 2003. Positional control of cell fate through joint integrin/receptor protein kinase signaling. Annu. Rev. Cell Dev. Biol. 19:173-206.
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 173-206
    • Giancotti, F.G.1    Tarone, G.2
  • 15
    • 0036333993 scopus 로고    scopus 로고
    • A crucial role of β1 integrins for keratinocyte migration in vitro and during cutaneous wound repair
    • Grose, R., C. Hutter, W. Bloch, I. Thorey, F. M. Watt, R. Fassler, C. Brakebusch, and S. Werner. 2002. A crucial role of β1 integrins for keratinocyte migration in vitro and during cutaneous wound repair. Development 129:2303-2315.
    • (2002) Development , vol.129 , pp. 2303-2315
    • Grose, R.1    Hutter, C.2    Bloch, W.3    Thorey, I.4    Watt, F.M.5    Fassler, R.6    Brakebusch, C.7    Werner, S.8
  • 16
    • 0032588186 scopus 로고    scopus 로고
    • NF-κB controls cell growth and differentiation through transcriptional regulation of cyclin D1
    • Guttridge, D. C., C. Albanese, J. Y. Reuther, R. G. Pestell, and A. S. Baldwin, Jr. 1999. NF-κB controls cell growth and differentiation through transcriptional regulation of cyclin D1. Mol. Cell. Biol. 19:5785-5799.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5785-5799
    • Guttridge, D.C.1    Albanese, C.2    Reuther, J.Y.3    Pestell, R.G.4    Baldwin Jr., A.S.5
  • 17
  • 18
    • 0026577999 scopus 로고
    • Identification of a new hemidesmosomal protein, HD1: A major, high molecular mass component of isolated hemidesmosomes
    • Hieda, Y., Y. Nishizawa, J. Uematsu, and K. Owaribe. 1992. Identification of a new hemidesmosomal protein, HD1: a major, high molecular mass component of isolated hemidesmosomes. J. Cell Biol. 116:1497-1506.
    • (1992) J. Cell Biol. , vol.116 , pp. 1497-1506
    • Hieda, Y.1    Nishizawa, Y.2    Uematsu, J.3    Owaribe, K.4
  • 19
    • 0037417129 scopus 로고    scopus 로고
    • Divergent gene regulation and growth effects by NF-κB in epithelial and mesenchymal cells of human skin
    • Hinata, K., A. M. Gervin, Y. J. Zhang, and P. A. Khavari. 2003. Divergent gene regulation and growth effects by NF-κB in epithelial and mesenchymal cells of human skin. Oncogene 22:1955-1964.
    • (2003) Oncogene , vol.22 , pp. 1955-1964
    • Hinata, K.1    Gervin, A.M.2    Zhang, Y.J.3    Khavari, P.A.4
  • 21
    • 0032493934 scopus 로고    scopus 로고
    • Novel roles for α3β1 integrin as a regulator of cytoskeletal assembly and as a trans-dominant inhibitor of integrin receptor function in mouse keratinocytes
    • Hodivala-Dilke, K. M., C. M. DiPersio, J. A. Kreidberg, and R. O. Hynes. 1998. Novel roles for α3β1 integrin as a regulator of cytoskeletal assembly and as a trans-dominant inhibitor of integrin receptor function in mouse keratinocytes. J. Cell Biol. 142:1357-1369.
    • (1998) J. Cell Biol. , vol.142 , pp. 1357-1369
    • Hodivala-Dilke, K.M.1    Dipersio, C.M.2    Kreidberg, J.A.3    Hynes, R.O.4
  • 22
    • 0029005210 scopus 로고
    • Molecular genetic studies of a human epidermal autoantigen (the 180-kD bullous pemphigoid antigen/BP180): Identification of functionally important sequences within the BP180 molecule and evidence for an interaction between BP180 and α6 integrin
    • Hopkinson, S. B., S. E. Baker, and J. C. Jones. 1995. Molecular genetic studies of a human epidermal autoantigen (the 180-kD bullous pemphigoid antigen/BP180): identification of functionally important sequences within the BP180 molecule and evidence for an interaction between BP180 and α6 integrin. J. Cell Biol. 130:117-125.
    • (1995) J. Cell Biol. , vol.130 , pp. 117-125
    • Hopkinson, S.B.1    Baker, S.E.2    Jones, J.C.3
  • 23
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. 2002. Integrins: bidirectional, allosteric signaling machines. Cell 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 26
    • 0035971422 scopus 로고    scopus 로고
    • Drosophila AP-1: Lessons from an invertebrate
    • Kockel, L., J. G. Homsy, and D. Bohmann. 2001. Drosophila AP-1: lessons from an invertebrate. Oncogene 20:2347-2364.
    • (2001) Oncogene , vol.20 , pp. 2347-2364
    • Kockel, L.1    Homsy, J.G.2    Bohmann, D.3
  • 27
    • 1542344031 scopus 로고    scopus 로고
    • Role of binding of plectin to the integrin β4 subunit in the assembly of hemidesmosomes
    • Koster, J., S. van Wilpe, I. Kuikman, S. H. Litjens, and A. Sonnenberg. 2004. Role of binding of plectin to the integrin β4 subunit in the assembly of hemidesmosomes. Mol. Biol. Cell 15:1211-1223.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1211-1223
    • Koster, J.1    Van Wilpe, S.2    Kuikman, I.3    Litjens, S.H.4    Sonnenberg, A.5
  • 29
    • 0029762913 scopus 로고    scopus 로고
    • Improving structural integrity of cryosections for immunogold labeling
    • Liou, W., H. J. Geuze, and J. W. Slot. 1996. Improving structural integrity of cryosections for immunogold labeling. Histochem. Cell Biol. 106:41-58.
    • (1996) Histochem. Cell Biol. , vol.106 , pp. 41-58
    • Liou, W.1    Geuze, H.J.2    Slot, J.W.3
  • 31
    • 0029115343 scopus 로고
    • Signal transduction by the α6β4 integrin: Distinct β4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes
    • Mainiero, F., A. Pepe, K. K. Wary, L. Spinardi, M. Mohammadi, J. Schlessinger, and F. G. Giancotti. 1995. Signal transduction by the α6β4 integrin: distinct β4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes. EMBO J. 14:4470-4481.
    • (1995) EMBO J. , vol.14 , pp. 4470-4481
    • Mainiero, F.1    Pepe, A.2    Wary, K.K.3    Spinardi, L.4    Mohammadi, M.5    Schlessinger, J.6    Giancotti, F.G.7
  • 32
    • 0035851913 scopus 로고    scopus 로고
    • EGF-R signaling through Fyn kinase disrupts the function of integrin α6β4 at hemidesmosomes: Role in epithelial cell migration and carcinoma invasion
    • Mariotti, A., P. A. Kedeshian, M. Dans, A. M. Curatola, L. Gagnoux-Palacios, and F. G. Giancotti. 2001. EGF-R signaling through Fyn kinase disrupts the function of integrin α6β4 at hemidesmosomes: role in epithelial cell migration and carcinoma invasion. J. Cell Biol. 155:447-458.
    • (2001) J. Cell Biol. , vol.155 , pp. 447-458
    • Mariotti, A.1    Kedeshian, P.A.2    Dans, M.3    Curatola, A.M.4    Gagnoux-Palacios, L.5    Giancotti, F.G.6
  • 34
    • 0036222549 scopus 로고    scopus 로고
    • Sensing the environment: A historical perspective on integrin signal transduction
    • Miranti, C. K., and J. S. Brugge. 2002. Sensing the environment: a historical perspective on integrin signal transduction. Nat. Cell Biol. 4:E83-E90.
    • (2002) Nat. Cell Biol. , vol.4
    • Miranti, C.K.1    Brugge, J.S.2
  • 35
    • 0032528060 scopus 로고    scopus 로고
    • Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin β4 cytoplasmic domain
    • Murgia, C., P. Blaikie, N. Kim, M. Dans, H. T. Petrie, and F. G. Giancotti. 1998. Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin β4 cytoplasmic domain. EMBO J. 17:3940-3951.
    • (1998) EMBO J. , vol.17 , pp. 3940-3951
    • Murgia, C.1    Blaikie, P.2    Kim, N.3    Dans, M.4    Petrie, H.T.5    Giancotti, F.G.6
  • 36
    • 0035941357 scopus 로고    scopus 로고
    • Ligation of integrin α3β1 by laminin 5 at the wound edge activates Rho-dependent adhesion of leading keratinocytes on collagen
    • Nguyen, B. P., X. D. Ren, M. A. Schwartz, and W. G. Carter. 2001. Ligation of integrin α3β1 by laminin 5 at the wound edge activates Rho-dependent adhesion of leading keratinocytes on collagen. J. Biol. Chem. 276:43860-43870.
    • (2001) J. Biol. Chem. , vol.276 , pp. 43860-43870
    • Nguyen, B.P.1    Ren, X.D.2    Schwartz, M.A.3    Carter, W.G.4
  • 39
    • 0242708766 scopus 로고    scopus 로고
    • Leukocyte functional antigen 1 lowers T cell activation thresholds and signaling through cytohesin-1 and Jun-activating binding protein 1
    • Perez, O. D., D. Mitchell, G. C. Jager, S. South, C. Murriel, J. McBride, L. A. Herzenberg, S. Kinoshita, and G. P. Nolan. 2003. Leukocyte functional antigen 1 lowers T cell activation thresholds and signaling through cytohesin-1 and Jun-activating binding protein 1. Nat. Immunol. 4:1083-1092.
    • (2003) Nat. Immunol. , vol.4 , pp. 1083-1092
    • Perez, O.D.1    Mitchell, D.2    Jager, G.C.3    South, S.4    Murriel, C.5    McBride, J.6    Herzenberg, L.A.7    Kinoshita, S.8    Nolan, G.P.9
  • 40
    • 0034604845 scopus 로고    scopus 로고
    • Conditional ablation of β1 integrin in skin. Severe defects in epidermal proliferation, basement membrane formation, and hair follicle invagination
    • Raghavan, S., C. Bauer, G. Mundschau, Q. Li, and E. Fuchs. 2000. Conditional ablation of β1 integrin in skin. Severe defects in epidermal proliferation, basement membrane formation, and hair follicle invagination. J. Cell Biol. 150:1149-1160.
    • (2000) J. Cell Biol. , vol.150 , pp. 1149-1160
    • Raghavan, S.1    Bauer, C.2    Mundschau, G.3    Li, Q.4    Fuchs, E.5
  • 41
    • 0042196118 scopus 로고    scopus 로고
    • A role for αβ1 integrins in focal adhesion function and polarized cytoskeletal dynamics
    • Raghavan, S., A. Vaezi, and E. Fuchs. 2003. A role for αβ1 integrins in focal adhesion function and polarized cytoskeletal dynamics. Dev. Cell 5:415-427.
    • (2003) Dev. Cell , vol.5 , pp. 415-427
    • Raghavan, S.1    Vaezi, A.2    Fuchs, E.3
  • 42
    • 16844373398 scopus 로고    scopus 로고
    • Keratinocytes display normal proliferation, survival and differentiation in conditional β4-integrin knockout mice
    • Raymond, K., M. Kreft, H. Janssen, J. Calafat, and A. Sonnenberg. 2005. Keratinocytes display normal proliferation, survival and differentiation in conditional β4-integrin knockout mice. J. Cell Sci. 118:1045-1060.
    • (2005) J. Cell Sci. , vol.118 , pp. 1045-1060
    • Raymond, K.1    Kreft, M.2    Janssen, H.3    Calafat, J.4    Sonnenberg, A.5
  • 44
    • 0042679580 scopus 로고    scopus 로고
    • The MSP receptor regulates α6β4 and α3β1 integrins via 14-3-3 proteins in keratinocyte migration
    • Santoro, M. M., G. Gaudino, and P. C. Marchisio. 2003. The MSP receptor regulates α6β4 and α3β1 integrins via 14-3-3 proteins in keratinocyte migration. Dev. Cell 5:257-271.
    • (2003) Dev. Cell , vol.5 , pp. 257-271
    • Santoro, M.M.1    Gaudino, G.2    Marchisio, P.C.3
  • 45
    • 0035824882 scopus 로고    scopus 로고
    • Short arm region of laminin-5 γ2 chain: Structure, mechanism of processing and binding to heparin and proteins
    • Sasaki, T., W. Gohring, K. Mann, C. Brakebusch, Y. Yamada, R. Fassler, and R. Timpl. 2001. Short arm region of laminin-5 γ2 chain: structure, mechanism of processing and binding to heparin and proteins. J. Mol. Biol. 314:751-763.
    • (2001) J. Mol. Biol. , vol.314 , pp. 751-763
    • Sasaki, T.1    Gohring, W.2    Mann, K.3    Brakebusch, C.4    Yamada, Y.5    Fassler, R.6    Timpl, R.7
  • 46
    • 0032514156 scopus 로고    scopus 로고
    • Hemidesmosome formation is initiated by the β4 integrin subunit, requires complex formation of β4 and HD1/plectin, and involves a direct interaction between β4 and the bullous pemphigoid antigen 180
    • Schaapveld, R. Q., L. Borradori, D. Geerts, M. R. van Leusden, I. Kuikman, M. G. Nievers, C. M. Niessen, R. D. Steenbergen, P. J. Snyders, and A. Sonnenberg. 1998. Hemidesmosome formation is initiated by the β4 integrin subunit, requires complex formation of β4 and HD1/plectin, and involves a direct interaction between β4 and the bullous pemphigoid antigen 180. J. Cell Biol. 142:271-284.
    • (1998) J. Cell Biol. , vol.142 , pp. 271-284
    • Schaapveld, R.Q.1    Borradori, L.2    Geerts, D.3    Van Leusden, M.R.4    Kuikman, I.5    Nievers, M.G.6    Niessen, C.M.7    Steenbergen, R.D.8    Snyders, P.J.9    Sonnenberg, A.10
  • 47
    • 0032477945 scopus 로고    scopus 로고
    • Alterations in NF-κB function in transgenic epithelial tissue demonstrate a growth inhibitory role for NF-κB
    • Seitz, C. S., Q. Lin, H. Deng, and P. A. Khavari. 1998. Alterations in NF-κB function in transgenic epithelial tissue demonstrate a growth inhibitory role for NF-κB. Proc. Natl. Acad. Sci. USA 95:2307-2312.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2307-2312
    • Seitz, C.S.1    Lin, Q.2    Deng, H.3    Khavari, P.A.4
  • 48
    • 0034951677 scopus 로고    scopus 로고
    • Identification of insulin receptor substrate 1 (IRS-1) and IRS-2 as signaling intermediates in the α6β4 integrin-dependent activation of phosphoinositide 3-OH kinase and promotion of invasion
    • Shaw, L. M. 2001. Identification of insulin receptor substrate 1 (IRS-1) and IRS-2 as signaling intermediates in the α6β4 integrin-dependent activation of phosphoinositide 3-OH kinase and promotion of invasion. Mol. Cell. Biol. 21:5082-5093.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 5082-5093
    • Shaw, L.M.1
  • 49
    • 0031456065 scopus 로고    scopus 로고
    • Activation of phosphoinositide 3-OH kinase by the α6β4 integrin promotes carcinoma invasion
    • Shaw, L. M., I. Rabinovitz, H. H. Wang, A. Toker, and A. M. Mercurio. 1997. Activation of phosphoinositide 3-OH kinase by the α6β4 integrin promotes carcinoma invasion. Cell 91:949-960.
    • (1997) Cell , vol.91 , pp. 949-960
    • Shaw, L.M.1    Rabinovitz, I.2    Wang, H.H.3    Toker, A.4    Mercurio, A.M.5
  • 50
    • 0028944247 scopus 로고
    • A recombinant tail-less integrin β4 subunit disrupts hemidesmosomes, but does not suppress α6β4-mediated cell adhesion to laminins
    • Spinardi, L., S. Einheber, T. Cullen, T. A. Milner, and F. G. Giancotti. 1995. A recombinant tail-less integrin β4 subunit disrupts hemidesmosomes, but does not suppress α6β4-mediated cell adhesion to laminins. J. Cell Biol. 129:473-487.
    • (1995) J. Cell Biol. , vol.129 , pp. 473-487
    • Spinardi, L.1    Einheber, S.2    Cullen, T.3    Milner, T.A.4    Giancotti, F.G.5
  • 51
    • 0027369205 scopus 로고
    • The β4 subunit cytoplasmic domain mediates the interaction of α6β4 integrin with the cytoskeleton of hemidesmosomes
    • Spinardi, L., Y. L. Ren, R. Sanders, and F. G. Giancotti. 1993. The β4 subunit cytoplasmic domain mediates the interaction of α6β4 integrin with the cytoskeleton of hemidesmosomes. Mol. Biol. Cell 4:871-884.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 871-884
    • Spinardi, L.1    Ren, Y.L.2    Sanders, R.3    Giancotti, F.G.4
  • 52
    • 0032559962 scopus 로고    scopus 로고
    • Epidermal growth factor activation of NF-κB is mediated through IκBα degradation and intracellular free calcium
    • Sun, L., and G. Carpenter. 1998. Epidermal growth factor activation of NF-κB is mediated through IκBα degradation and intracellular free calcium. Oncogene 16:2095-2102.
    • (1998) Oncogene , vol.16 , pp. 2095-2102
    • Sun, L.1    Carpenter, G.2
  • 53
  • 54
    • 0036726312 scopus 로고    scopus 로고
    • β4 integrin-dependent formation of polarized three-dimensional architecture confers resistance to apoptosis in normal and malignant mammary epithelium
    • Weaver, V. M., S. Lelievre, J. N. Lakins, M. A. Chrenek, J. C. Jones, F. Giancotti, Z. Werb, and M. J. Bissell. 2002. β4 integrin-dependent formation of polarized three-dimensional architecture confers resistance to apoptosis in normal and malignant mammary epithelium. Cancer Cell 2:205-216.
    • (2002) Cancer Cell , vol.2 , pp. 205-216
    • Weaver, V.M.1    Lelievre, S.2    Lakins, J.N.3    Chrenek, M.A.4    Jones, J.C.5    Giancotti, F.6    Werb, Z.7    Bissell, M.J.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.