메뉴 건너뛰기




Volumn 13, Issue 1, 2003, Pages 43-50

Computational modeling of the EGF-receptor system: A paradigm for systems biology

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR;

EID: 0037213006     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(02)00009-0     Document Type: Review
Times cited : (297)

References (66)
  • 1
    • 0033860695 scopus 로고    scopus 로고
    • The EGF receptor: A nexus for trafficking and signaling
    • Carpenter G. The EGF receptor: a nexus for trafficking and signaling. BioEssays. 22:2000;697-707.
    • (2000) BioEssays , vol.22 , pp. 697-707
    • Carpenter, G.1
  • 3
    • 0032939325 scopus 로고    scopus 로고
    • Multiple positive and negative regulators of signaling by the EGF-receptor
    • Moghal N., Sternberg P.W. Multiple positive and negative regulators of signaling by the EGF-receptor. Curr. Opin. Cell Biol. 11:1999;190-196.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 190-196
    • Moghal, N.1    Sternberg, P.W.2
  • 4
    • 0036500993 scopus 로고    scopus 로고
    • Systems biology: A brief overview
    • Kitano H. Systems biology: a brief overview. Science. 295:2002;1662-1664.
    • (2002) Science , vol.295 , pp. 1662-1664
    • Kitano, H.1
  • 5
    • 0021520019 scopus 로고
    • Receptor-mediated endocytosis: A model and its implications for experimental analysis
    • Gex-Fabry M., DeLisi C. Receptor-mediated endocytosis: a model and its implications for experimental analysis. Am. J. Physiol. 247:1984;R768-R779.
    • (1984) Am. J. Physiol. , vol.247
    • Gex-Fabry, M.1    DeLisi, C.2
  • 6
    • 0019404817 scopus 로고
    • A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands
    • Wiley H.S., Cunningham D.D. A steady state model for analyzing the cellular binding, internalization and degradation of polypeptide ligands. Cell. 25:1981;433-440.
    • (1981) Cell , vol.25 , pp. 433-440
    • Wiley, H.S.1    Cunningham, D.D.2
  • 7
    • 0019945866 scopus 로고
    • The endocytotic rate constant. A cellular parameter for quantitating receptor-mediated endocytosis
    • Wiley H.S., Cunningham D.D. The endocytotic rate constant. A cellular parameter for quantitating receptor-mediated endocytosis. J. Biol. Chem. 257:1982;4222-4229.
    • (1982) J. Biol. Chem. , vol.257 , pp. 4222-4229
    • Wiley, H.S.1    Cunningham, D.D.2
  • 8
    • 0024634393 scopus 로고
    • Receptor-mediated transport of peptide hormones and its importance in the overall hormone disposition in the body
    • Sugiyama Y., Hanano M. Receptor-mediated transport of peptide hormones and its importance in the overall hormone disposition in the body. Pharm. Res. 6:1989;192-202.
    • (1989) Pharm. Res. , vol.6 , pp. 192-202
    • Sugiyama, Y.1    Hanano, M.2
  • 10
    • 0020366345 scopus 로고
    • Epidermal growth factor stimulates fluid phase endocytosis in human fibroblasts through a signal generated at the cell surface
    • Wiley H.S., Cunningham D.D. Epidermal growth factor stimulates fluid phase endocytosis in human fibroblasts through a signal generated at the cell surface. J. Cell. Biochem. 19:1982;383-394.
    • (1982) J. Cell. Biochem. , vol.19 , pp. 383-394
    • Wiley, H.S.1    Cunningham, D.D.2
  • 11
    • 0021333875 scopus 로고
    • Relationship between epidermal growth factor receptor occupancy and mitogenic response. Quantitative analysis using a steady state model system
    • Knauer D.J., et al. Relationship between epidermal growth factor receptor occupancy and mitogenic response. Quantitative analysis using a steady state model system. J. Biol. Chem. 259:1984;5623-5631.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5623-5631
    • Knauer, D.J.1
  • 12
    • 0026833077 scopus 로고
    • Mathematical model for the effects of epidermal growth factor receptor trafficking dynamics on fibroblast proliferation responses
    • Starbuck C., Lauffenburger D.A. Mathematical model for the effects of epidermal growth factor receptor trafficking dynamics on fibroblast proliferation responses. Biotechnol. Prog. 8:1992;132-143.
    • (1992) Biotechnol. Prog. , vol.8 , pp. 132-143
    • Starbuck, C.1    Lauffenburger, D.A.2
  • 13
    • 0026691043 scopus 로고
    • Analysis of the influences of the E5 transforming protein on kinetic parameters of epidermal growth factor binding and metabolism
    • Waters C.M., et al. Analysis of the influences of the E5 transforming protein on kinetic parameters of epidermal growth factor binding and metabolism. J. Cell. Physiol. 152:1992;253-263.
    • (1992) J. Cell. Physiol. , vol.152 , pp. 253-263
    • Waters, C.M.1
  • 14
    • 0036500834 scopus 로고    scopus 로고
    • Reverse engineering of biological complexity
    • Csete M.E., Doyle J.C. Reverse engineering of biological complexity. Science. 295:2002;1664-1669.
    • (2002) Science , vol.295 , pp. 1664-1669
    • Csete, M.E.1    Doyle, J.C.2
  • 15
    • 0023677140 scopus 로고
    • Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system
    • Wiley H.S. Anomalous binding of epidermal growth factor to A431 cells is due to the effect of high receptor densities and a saturable endocytic system. J. Cell Biol. 107:1988;801-810.
    • (1988) J. Cell Biol. , vol.107 , pp. 801-810
    • Wiley, H.S.1
  • 16
    • 0025160570 scopus 로고
    • Quantitative analysis of the endocytic system involved in hormone-induced receptor internalization
    • Lund K.A., et al. Quantitative analysis of the endocytic system involved in hormone-induced receptor internalization. J. Biol. Chem. 265:1990;15713-15723.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15713-15723
    • Lund, K.A.1
  • 17
    • 0023663092 scopus 로고
    • Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing
    • Honegger A.M., et al. Point mutation at the ATP binding site of EGF receptor abolishes protein-tyrosine kinase activity and alters cellular routing. Cell. 51:1987;199-209.
    • (1987) Cell , vol.51 , pp. 199-209
    • Honegger, A.M.1
  • 18
    • 0025359062 scopus 로고
    • Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body
    • Felder S., et al. Kinase activity controls the sorting of the epidermal growth factor receptor within the multivesicular body. Cell. 61:1990;623-634.
    • (1990) Cell , vol.61 , pp. 623-634
    • Felder, S.1
  • 19
    • 0025908557 scopus 로고
    • The role of tyrosine kinase activity in endocytosis, compartmentation, and down-regulation of the epidermal growth factor receptor
    • Wiley H.S., et al. The role of tyrosine kinase activity in endocytosis, compartmentation, and down-regulation of the epidermal growth factor receptor. J. Biol. Chem. 266:1991;11083-11094.
    • (1991) J. Biol. Chem. , vol.266 , pp. 11083-11094
    • Wiley, H.S.1
  • 20
    • 0026344988 scopus 로고
    • Ligand-induced internalization and increased cell calcium are mediated via distinct structural elements in the carboxyl terminus of the epidermal growth factor receptor
    • Chang C.P., et al. Ligand-induced internalization and increased cell calcium are mediated via distinct structural elements in the carboxyl terminus of the epidermal growth factor receptor. J. Biol. Chem. 266:1991;23467-23470.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23467-23470
    • Chang, C.P.1
  • 21
    • 0027203952 scopus 로고
    • Ligand-induced internalization of the epidermal growth factor receptor is mediated by multiple endocytic codes analogous to the tyrosine motif found in constitutively internalized receptors
    • Chang C.P., et al. Ligand-induced internalization of the epidermal growth factor receptor is mediated by multiple endocytic codes analogous to the tyrosine motif found in constitutively internalized receptors. J. Biol. Chem. 268:1993;19312-19320.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19312-19320
    • Chang, C.P.1
  • 22
    • 0028916337 scopus 로고
    • Endocytosis and lysosomal targeting of epidermal growth factor receptors are mediated by distinct sequences independent of the tyrosine kinase domain
    • Opresko L.K., et al. Endocytosis and lysosomal targeting of epidermal growth factor receptors are mediated by distinct sequences independent of the tyrosine kinase domain. J. Biol. Chem. 270:1995;4325-4333.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4325-4333
    • Opresko, L.K.1
  • 23
    • 0032789613 scopus 로고    scopus 로고
    • Human mammary epithelial cells rapidly exchange empty EGFR between surface and intracellular pools
    • Burke P.M., Wiley H.S. Human mammary epithelial cells rapidly exchange empty EGFR between surface and intracellular pools. J. Cell. Physiol. 180:1999;448-460.
    • (1999) J. Cell. Physiol. , vol.180 , pp. 448-460
    • Burke, P.M.1    Wiley, H.S.2
  • 24
    • 0035105470 scopus 로고    scopus 로고
    • Regulation of receptor tyrosine kinase signaling by endocytic trafficking
    • Wiley H.S., Burke P.M. Regulation of receptor tyrosine kinase signaling by endocytic trafficking. Traffic. 2:2001;12-18.
    • (2001) Traffic , vol.2 , pp. 12-18
    • Wiley, H.S.1    Burke, P.M.2
  • 25
    • 0037018146 scopus 로고    scopus 로고
    • Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies
    • Longva K.E., et al. Ubiquitination and proteasomal activity is required for transport of the EGF receptor to inner membranes of multivesicular bodies. J. Cell Biol. 156:2002;843-854.
    • (2002) J. Cell Biol. , vol.156 , pp. 843-854
    • Longva, K.E.1
  • 26
    • 0028969961 scopus 로고
    • Intracellular trafficking of epidermal growth factor family ligands is directly influenced by the pH sensitivity of the receptor/ligand interaction
    • French A.R., et al. Intracellular trafficking of epidermal growth factor family ligands is directly influenced by the pH sensitivity of the receptor/ligand interaction. J. Biol. Chem. 270:1995;4334-4340.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4334-4340
    • French, A.R.1
  • 27
    • 0035895664 scopus 로고    scopus 로고
    • Molecular mechanisms underlying endocytosis and sorting of ErbB receptor tyrosine kinases
    • Waterman H., Yarden Y. Molecular mechanisms underlying endocytosis and sorting of ErbB receptor tyrosine kinases. FEBS Lett. 490:2001;142-152.
    • (2001) FEBS Lett. , vol.490 , pp. 142-152
    • Waterman, H.1    Yarden, Y.2
  • 28
    • 0037178805 scopus 로고    scopus 로고
    • Effect of tyrosine kinase inhibitors on clathrin-coated pit recruitment and internalization of epidermal growth factor receptor
    • Sorkina T., et al. Effect of tyrosine kinase inhibitors on clathrin-coated pit recruitment and internalization of epidermal growth factor receptor. J. Biol. Chem. 277:2002;27433-27441.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27433-27441
    • Sorkina, T.1
  • 29
    • 0034942833 scopus 로고    scopus 로고
    • Quantitative analysis of the EGF receptor autocrine system reveals cryptic regulation of cell response by ligand capture
    • DeWitt A.E., et al. Quantitative analysis of the EGF receptor autocrine system reveals cryptic regulation of cell response by ligand capture. J. Cell Sci. 114:2001;2301-2313.
    • (2001) J. Cell Sci. , vol.114 , pp. 2301-2313
    • DeWitt, A.E.1
  • 30
    • 0025139326 scopus 로고
    • Ligand-induced transformation by a noninternalizing epidermal growth factor receptor
    • Wells A., et al. Ligand-induced transformation by a noninternalizing epidermal growth factor receptor. Science. 247:1990;962-964.
    • (1990) Science , vol.247 , pp. 962-964
    • Wells, A.1
  • 31
    • 0028466187 scopus 로고
    • Proliferative response of fibroblasts expressing internalization-deficient epidermal growth factor (EGF) receptors is altered via differential EGF depletion effect
    • Reddy C.C., et al. Proliferative response of fibroblasts expressing internalization-deficient epidermal growth factor (EGF) receptors is altered via differential EGF depletion effect. Biotechnol. Prog. 10:1994;377-384.
    • (1994) Biotechnol. Prog. , vol.10 , pp. 377-384
    • Reddy, C.C.1
  • 32
    • 0029999241 scopus 로고    scopus 로고
    • Basic fibroblast growth factor binds its receptors, is internalized, and stimulates DNA synthesis in Balb/c3T3 cells in the absence of heparan sulfate
    • Fannon M., Nugent M.A. Basic fibroblast growth factor binds its receptors, is internalized, and stimulates DNA synthesis in Balb/c3T3 cells in the absence of heparan sulfate. J. Biol. Chem. 271:1996;17949-17956.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17949-17956
    • Fannon, M.1    Nugent, M.A.2
  • 33
    • 0029852598 scopus 로고    scopus 로고
    • Engineering epidermal growth factor for enhanced mitogenic potency
    • Reddy C.C., et al. Engineering epidermal growth factor for enhanced mitogenic potency. Nat. Biotechnol. 14:1996;1696-1699.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1696-1699
    • Reddy, C.C.1
  • 34
    • 0034629560 scopus 로고    scopus 로고
    • Increased endosomal sorting of ligand to recycling enhances potency of an interleukin-2 analog
    • Fallon E.M., et al. Increased endosomal sorting of ligand to recycling enhances potency of an interleukin-2 analog. J. Biol. Chem. 275:2000;6790-6797.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6790-6797
    • Fallon, E.M.1
  • 35
    • 0036713917 scopus 로고    scopus 로고
    • Rational cytokine design for increased lifetime and enhanced potency using pH-activated 'histidine switching'
    • Sarkar C.A., et al. Rational cytokine design for increased lifetime and enhanced potency using pH-activated 'histidine switching'. Nat. Biotechnol. 20:2002;908-913.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 908-913
    • Sarkar, C.A.1
  • 36
    • 0033555859 scopus 로고    scopus 로고
    • Emergent properties of networks of biological signaling pathways
    • Bhalla U.S., Iyengar R. Emergent properties of networks of biological signaling pathways. Science. 283:1999;381-387.
    • (1999) Science , vol.283 , pp. 381-387
    • Bhalla, U.S.1    Iyengar, R.2
  • 37
    • 0033570090 scopus 로고    scopus 로고
    • Quantification of short term signaling by the epidermal growth factor receptor
    • Kholodenko B.N., et al. 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
  • 38
    • 0033607542 scopus 로고    scopus 로고
    • Ras in fibroblasts
    • Ras in fibroblasts. J. Biol. Chem. 274:1999;34350-34360.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34350-34360
    • Haugh, J.M.1
  • 39
    • 0036212767 scopus 로고    scopus 로고
    • Computational modeling of the dynamics of the MAP kinase cascade activated by surface and internalized EGF receptors
    • Schoeberl B., et al. 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
  • 40
    • 0031936410 scopus 로고    scopus 로고
    • Specificity within the EGF family/ErbB receptor family signaling network
    • Riese D.J. II, Stern D.F. II. Specificity within the EGF family/ErbB receptor family signaling network. BioEssays. 20:1998;41-48.
    • (1998) BioEssays , vol.20 , pp. 41-48
    • Riese D.J. II1    Stern D.F. II2
  • 41
    • 0026708050 scopus 로고
    • Implications of epidermal growth factor (EGF) induced EGF receptor aggregation
    • Wofsy C., et al. Implications of epidermal growth factor (EGF) induced EGF receptor aggregation. Biophys. J. 63:1992;98-110.
    • (1992) Biophys. J. , vol.63 , pp. 98-110
    • Wofsy, C.1
  • 42
    • 0036225144 scopus 로고    scopus 로고
    • Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling
    • Martin-Fernandez M., et al. Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling. Biophys. J. 82:2002;2415-2427.
    • (2002) Biophys. J. , vol.82 , pp. 2415-2427
    • Martin-Fernandez, M.1
  • 43
    • 18644370411 scopus 로고    scopus 로고
    • Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha
    • Garrett T., et al. Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha. Cell. 110:2002;763-773.
    • (2002) Cell , vol.110 , pp. 763-773
    • Garrett, T.1
  • 44
    • 0033605560 scopus 로고    scopus 로고
    • ErbB-2 amplification inhibits down-regulation and induces constitutive activation of both ErbB-2 and epidermal growth factor receptors
    • Worthylake R., et al. ErbB-2 amplification inhibits down-regulation and induces constitutive activation of both ErbB-2 and epidermal growth factor receptors. J. Biol. Chem. 274:1999;8865-8874.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8865-8874
    • Worthylake, R.1
  • 45
    • 0032577487 scopus 로고    scopus 로고
    • Alternative intracellular routing of ErbB receptors may determine signaling potency
    • Waterman H., et al. Alternative intracellular routing of ErbB receptors may determine signaling potency. J. Biol. Chem. 273:1998;13819-13827.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13819-13827
    • Waterman, H.1
  • 46
    • 0032430264 scopus 로고    scopus 로고
    • Real-time quantitative measurement of autocrine ligand binding indicates that autocrine loops are spatially localized
    • Lauffenburger D.A., et al. Real-time quantitative measurement of autocrine ligand binding indicates that autocrine loops are spatially localized. Proc. Natl Acad. Sci. USA. 95:1998;15368-15373.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 15368-15373
    • Lauffenburger, D.A.1
  • 47
    • 0026638127 scopus 로고
    • Autocrine ligand binding to cell receptors. Mathematical analysis of competition by solution 'decoys'
    • Forsten K.E., Lauffenburger D.A. Autocrine ligand binding to cell receptors. Mathematical analysis of competition by solution 'decoys'. Biophys. J. 61:1992;518-529.
    • (1992) Biophys. J. , vol.61 , pp. 518-529
    • Forsten, K.E.1    Lauffenburger, D.A.2
  • 48
    • 0034805462 scopus 로고    scopus 로고
    • Spatial range of autocrine signaling: Modeling and computational analysis
    • Shvartsman S.Y., et al. Spatial range of autocrine signaling: modeling and computational analysis. Biophys. J. 81:2001;1854-1867.
    • (2001) Biophys. J. , vol.81 , pp. 1854-1867
    • Shvartsman, S.Y.1
  • 49
    • 85016540948 scopus 로고
    • Studies on engineered autocrine systems: Requirements for ligand release from cells producing an artificial growth factor
    • Will B.H., et al. Studies on engineered autocrine systems: requirements for ligand release from cells producing an artificial growth factor. Tissue Eng. 1:1995;81-96.
    • (1995) Tissue Eng. , vol.1 , pp. 81-96
    • Will, B.H.1
  • 50
    • 0036402459 scopus 로고    scopus 로고
    • Affinity regulates spatial range of EGF receptor autocrine ligand binding
    • DeWitt A.E., et al. Affinity regulates spatial range of EGF receptor autocrine ligand binding. Dev. Biol. 250:2002;305-316.
    • (2002) Dev. Biol. , vol.250 , pp. 305-316
    • DeWitt, A.E.1
  • 51
    • 0030038201 scopus 로고    scopus 로고
    • Autocrine regulation of membrane transforming growth factor-alpha cleavage
    • Baselga J., et al. Autocrine regulation of membrane transforming growth factor-alpha cleavage. J. Biol. Chem. 271:1996;3279-3284.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3279-3284
    • Baselga, J.1
  • 52
    • 0035945359 scopus 로고    scopus 로고
    • Autocrine epidermal growth factor signaling stimulates directionally persistent mammary epithelial cell migration
    • Maheshwari G., et al. Autocrine epidermal growth factor signaling stimulates directionally persistent mammary epithelial cell migration. J. Cell Biol. 155:2001;1123-1128.
    • (2001) J. Cell Biol. , vol.155 , pp. 1123-1128
    • Maheshwari, G.1
  • 53
    • 0033398711 scopus 로고    scopus 로고
    • Control of EGF receptor signalling: Lessons from fruitflies
    • Casci T., Freeman M. Control of EGF receptor signalling: lessons from fruitflies. Cancer Metastasis Rev. 18:1999;181-201.
    • (1999) Cancer Metastasis Rev. , vol.18 , pp. 181-201
    • Casci, T.1    Freeman, M.2
  • 54
    • 0036333324 scopus 로고    scopus 로고
    • Modeling and computational analysis of EGF receptor-mediated cell communication in Drosophila oogenesis
    • Shvartsman S.Y., et al. Modeling and computational analysis of EGF receptor-mediated cell communication in Drosophila oogenesis. Development. 129:2002;2577-2589.
    • (2002) Development , vol.129 , pp. 2577-2589
    • Shvartsman, S.Y.1
  • 55
    • 0033213984 scopus 로고    scopus 로고
    • The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading
    • Gechtman Z., et al. The shedding of membrane-anchored heparin-binding epidermal-like growth factor is regulated by the Raf/mitogen-activated protein kinase cascade and by cell adhesion and spreading. J. Biol. Chem. 274:1999;28828-28835.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28828-28835
    • Gechtman, Z.1
  • 56
    • 0034614622 scopus 로고    scopus 로고
    • Trafficking and proteolytic release of epidermal growth factor receptor ligands are modulated by their membrane-anchoring domains
    • Dong J., Wiley H.S. Trafficking and proteolytic release of epidermal growth factor receptor ligands are modulated by their membrane-anchoring domains. J. Biol. Chem. 275:2000;557-564.
    • (2000) J. Biol. Chem. , vol.275 , pp. 557-564
    • Dong, J.1    Wiley, H.S.2
  • 57
    • 0032815618 scopus 로고    scopus 로고
    • Radiation-induced release of transforming growth factor alpha activates the epidermal growth factor receptor and mitogen-activated protein kinase pathway in carcinoma cells, leading to increased proliferation and protection from radiation-induced cell death
    • Dent P., et al. Radiation-induced release of transforming growth factor alpha activates the epidermal growth factor receptor and mitogen-activated protein kinase pathway in carcinoma cells, leading to increased proliferation and protection from radiation-induced cell death. Mol. Biol. Cell. 10:1999;2493-2506.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2493-2506
    • Dent, P.1
  • 58
    • 0033398661 scopus 로고    scopus 로고
    • Molecular mechanisms of radiation-induced accelerated repopulation
    • Schmidt-Ullrich R.K., et al. Molecular mechanisms of radiation-induced accelerated repopulation. Radiat. Oncol. Investig. 7:1999;321-330.
    • (1999) Radiat. Oncol. Investig. , vol.7 , pp. 321-330
    • Schmidt-Ullrich, R.K.1
  • 59
    • 0034029550 scopus 로고    scopus 로고
    • Ionizing radiation-induced mitogen-activated protein (MAP) kinase activation in DU145 prostate carcinoma cells: MAP kinase inhibition enhances radiation-induced cell killing and G2/M-phase arrest
    • Hagan M., et al. Ionizing radiation-induced mitogen-activated protein (MAP) kinase activation in DU145 prostate carcinoma cells: MAP kinase inhibition enhances radiation-induced cell killing and G2/M-phase arrest. Radiat. Res. 153:2000;371-383.
    • (2000) Radiat. Res. , vol.153 , pp. 371-383
    • Hagan, M.1
  • 60
    • 0035918858 scopus 로고    scopus 로고
    • Epidermal growth factor receptor as a genetic therapy target for carcinoma cell radiosensitization
    • Lammering G., et al. Epidermal growth factor receptor as a genetic therapy target for carcinoma cell radiosensitization. J. Natl Cancer Inst. 93:2001;921-929.
    • (2001) J. Natl Cancer Inst. , vol.93 , pp. 921-929
    • Lammering, G.1
  • 61
    • 0036080555 scopus 로고    scopus 로고
    • Autocrine loops with positive feedback enable context-dependent cell signaling
    • Shvartsman S.Y., et al. Autocrine loops with positive feedback enable context-dependent cell signaling. Am. J. Physiol. Cell. Physiol. 282:2002;C545-C559.
    • (2002) Am. J. Physiol. Cell. Physiol. , vol.282
    • Shvartsman, S.Y.1
  • 62
    • 0021803670 scopus 로고
    • Intracellular processing of epidermal growth factor and its effect on ligand-receptor interactions
    • Wiley H.S., et al. Intracellular processing of epidermal growth factor and its effect on ligand-receptor interactions. J. Biol. Chem. 260:1985;5290-5295.
    • (1985) J. Biol. Chem. , vol.260 , pp. 5290-5295
    • Wiley, H.S.1
  • 63
    • 0032556454 scopus 로고    scopus 로고
    • Analysis of receptor internalization as a mechanism for modulating signal transduction
    • Haugh J.M., Lauffenburger D.A. Analysis of receptor internalization as a mechanism for modulating signal transduction. J. Theor. Biol. 195:1998;187-218.
    • (1998) J. Theor. Biol. , vol.195 , pp. 187-218
    • Haugh, J.M.1    Lauffenburger, D.A.2
  • 64
    • 0035162703 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking
    • Burke P., et al. Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking. Mol. Biol. Cell. 12:2001;1897-1910.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 1897-1910
    • Burke, P.1
  • 65
    • 0032991651 scopus 로고    scopus 로고
    • Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor
    • Dong J., et al. Metalloprotease-mediated ligand release regulates autocrine signaling through the epidermal growth factor receptor. Proc. Natl Acad. Sci. USA. 96:1999;6235-6240.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6235-6240
    • Dong, J.1
  • 66
    • 0034681203 scopus 로고    scopus 로고
    • EGF receptor transactivation mediated by the proteolytic production of EGF-like agonists
    • Carpenter G. EGF receptor transactivation mediated by the proteolytic production of EGF-like agonists. Science STKE. (15):2000;PE1.
    • (2000) Science STKE , Issue.15 , pp. 1
    • Carpenter, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.