메뉴 건너뛰기




Volumn 159, Issue 3, 2003, Pages 283-300

Stress and radiation-induced activation of multiple intracellular signaling pathways

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM BINDING PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; GROWTH FACTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; INTERLEUKIN 6; LIGAND; MITOGEN ACTIVATED PROTEIN KINASE; NEU DIFFERENTIATION FACTOR; NITROGEN; PHOSPHATASE; PHOSPHATIDYLINOSITOL; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; RAF PROTEIN; REACTIVE OXYGEN METABOLITE; STRESS ACTIVATED PROTEIN KINASE; SYNAPTOPHYSIN; TUMOR NECROSIS FACTOR RECEPTOR; TYROSINE KINASE RECEPTOR;

EID: 0037335568     PISSN: 00337587     EISSN: None     Source Type: Journal    
DOI: 10.1667/0033-7587(2003)159[0283:SARIAO]2.0.CO;2     Document Type: Conference Paper
Times cited : (427)

References (256)
  • 1
    • 0012353162 scopus 로고
    • Crystalline muscle phosphorylase
    • A. A. Green, G. T. Cori and C. F. Cori, Crystalline muscle phosphorylase. J. Biol. Chem. 142, 447-448 (1942).
    • (1942) J. Biol. Chem. , vol.142 , pp. 447-448
    • Green, A.A.1    Cori, G.T.2    Cori, C.F.3
  • 2
    • 0001658828 scopus 로고
    • The enzymatic conversion of phosphorylase a to b
    • G. T. Cori and C. F. Cori, The enzymatic conversion of phosphorylase a to b. J. Biol. Chem. 158, 321-332 (1945).
    • (1945) J. Biol. Chem. , vol.158 , pp. 321-332
    • Cori, G.T.1    Cori, C.F.2
  • 3
    • 0014952140 scopus 로고
    • The biological role of cyclic AMP
    • E. W. Sutherland, The biological role of cyclic AMP. J. Am. Med. Assoc. 214, 1281-1288 (1970).
    • (1970) J. Am. Med. Assoc. , vol.214 , pp. 1281-1288
    • Sutherland, E.W.1
  • 4
    • 49749165001 scopus 로고
    • The phosphorylase b to a converting enzyme of rabbit skeletal muscle
    • E. G. Krebs and E. H. Fisher, The phosphorylase b to a converting enzyme of rabbit skeletal muscle. Biochim. Biophys. Acta 20, 150-157 (1956).
    • (1956) Biochim. Biophys. Acta , vol.20 , pp. 150-157
    • Krebs, E.G.1    Fisher, E.H.2
  • 5
    • 0014965901 scopus 로고
    • Amino acid sequence of the phosphorylated site in rabbit liver glycogen phosphorylase
    • D. P. Wolf, E. H. Fischer and E. G. Krebs, Amino acid sequence of the phosphorylated site in rabbit liver glycogen phosphorylase. Biochemistry 9, 1923-1929 (1970).
    • (1970) Biochemistry , vol.9 , pp. 1923-1929
    • Wolf, D.P.1    Fischer, E.H.2    Krebs, E.G.3
  • 6
    • 0014409394 scopus 로고
    • An adenosine 3′,5′-monophosphate-dependent protein kinase from rabbit skeletal muscle
    • D. A. Walsh, J. P. Perkins and E. G. Krebs, An adenosine 3′,5′-monophosphate-dependent protein kinase from rabbit skeletal muscle. J. Biol. Chem. 243, 3763-3775 (1968).
    • (1968) J. Biol. Chem. , vol.243 , pp. 3763-3775
    • Walsh, D.A.1    Perkins, J.P.2    Krebs, E.G.3
  • 7
    • 0014149639 scopus 로고
    • Regulation of glycogen metabolism
    • L. F. Leloir, Regulation of glycogen metabolism. Natl. Cancer Inst. Monogr. 27, 3-18 (1967).
    • (1967) Natl. Cancer Inst. Monogr. , vol.27 , pp. 3-18
    • Leloir, L.F.1
  • 8
    • 0015690675 scopus 로고
    • Covalent and noncovalent control of glycogen synthesis
    • J. Larner, Covalent and noncovalent control of glycogen synthesis. Ann. NY Acad. Sci. 210, 207-214 (1973).
    • (1973) Ann. NY Acad. Sci. , vol.210 , pp. 207-214
    • Larner, J.1
  • 10
    • 0018040458 scopus 로고
    • 2+-dependent protein phosphorylation system in membranes from various tissues, and its activation by "calcium-dependent regulator"
    • 2+-dependent protein phosphorylation system in membranes from various tissues, and its activation by "calcium-dependent regulator". Proc. Natl. Acad. Sci. USA 75, 5432-5436 (1978).
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5432-5436
    • Schulman, H.1    Greengard, P.2
  • 11
    • 0024319210 scopus 로고
    • G proteins control diverse pathways of transmembrane signaling
    • M. Freissmuth, P. J. Casey and A. G. Gilman, G proteins control diverse pathways of transmembrane signaling. FASEB J. 10, 2125- 2131 (1989).
    • (1989) FASEB J. , vol.10 , pp. 2125-2131
    • Freissmuth, M.1    Casey, P.J.2    Gilman, A.G.3
  • 12
    • 0021270640 scopus 로고
    • Inositol trisphosphate formation and calcium mobilization in Swiss 3T3 cells in response to platelet-derived growth factor
    • M. J. Berridge, J. P. Heslop, R. F. Irvine and K. D. Brown, Inositol trisphosphate formation and calcium mobilization in Swiss 3T3 cells in response to platelet-derived growth factor. Biochem. J. 222, 195-201 (1984).
    • (1984) Biochem. J. , vol.222 , pp. 195-201
    • Berridge, M.J.1    Heslop, J.P.2    Irvine, R.F.3    Brown, K.D.4
  • 13
    • 0344203380 scopus 로고
    • Inositol trisphosphate and diacylglycerol as intracellular second messengers in liver
    • J. R. Williamson, R. H. Cooper, S. K. Joseph and A. P. Thomas, Inositol trisphosphate and diacylglycerol as intracellular second messengers in liver. Am. J. Physiol. 248, C203-216 (1985).
    • (1985) Am. J. Physiol. , vol.248
    • Williamson, J.R.1    Cooper, R.H.2    Joseph, S.K.3    Thomas, A.P.4
  • 14
    • 0019310910 scopus 로고
    • Avian sarcoma virus-transforming protein, pp 60src shows protein kinase activity specific for tyrosine
    • M. S. Collett, A. F. Purchio and R. L. Erikson, Avian sarcoma virus-transforming protein, pp60src shows protein kinase activity specific for tyrosine. Nature 285, 167-169 (1980).
    • (1980) Nature , vol.285 , pp. 167-169
    • Collett, M.S.1    Purchio, A.F.2    Erikson, R.L.3
  • 15
    • 0020328955 scopus 로고
    • Human EJ bladder carcinoma oncogene is homologue of Harvey sarcoma virus ras gene
    • L. F. Parada, C. J. Tabin, C. Shih and R. A. Weinberg, Human EJ bladder carcinoma oncogene is homologue of Harvey sarcoma virus ras gene. Nature 297, 474-478 (1982).
    • (1982) Nature , vol.297 , pp. 474-478
    • Parada, L.F.1    Tabin, C.J.2    Shih, C.3    Weinberg, R.A.4
  • 16
    • 0022479478 scopus 로고
    • Muscle proteins related to microtubule associated protein-2 are substrates for an insulin-stimulatable kinase
    • T. W. Sturgill and L. B. Ray, Muscle proteins related to microtubule associated protein-2 are substrates for an insulin-stimulatable kinase. Biochem. Biophys. Res. Commun. 134, 565-571 (1986).
    • (1986) Biochem. Biophys. Res. Commun. , vol.134 , pp. 565-571
    • Sturgill, T.W.1    Ray, L.B.2
  • 17
    • 0026165752 scopus 로고
    • Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies
    • T. G. Boulton and M. H. Cobb, Identification of multiple extracellular signal-regulated kinases (ERKs) with antipeptide antibodies. Cell Regul. 2, 357-371 (1991).
    • (1991) Cell Regul. , vol.2 , pp. 357-371
    • Boulton, T.G.1    Cobb, M.H.2
  • 18
    • 0023766145 scopus 로고
    • Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II
    • T. W. Sturgill, L. B. Ray, E. Erikson and J. L. Maller, Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II. Nature 334, 715-718 (1988).
    • (1988) Nature , vol.334 , pp. 715-718
    • Sturgill, T.W.1    Ray, L.B.2    Erikson, E.3    Maller, J.L.4
  • 19
    • 0026670728 scopus 로고
    • Renaturation and partial peptide sequencing of mitogen-activated protein kinase (MAP kinase) activator from rabbit skeletal muscle
    • J. Wu, H. Michel, A. Rossomando, T. Haystead, J. Shabanowitz, D. F. Hunt and T. W. Sturgill, Renaturation and partial peptide sequencing of mitogen-activated protein kinase (MAP kinase) activator from rabbit skeletal muscle. Biochem. J. 285, 701-705 (1992).
    • (1992) Biochem. J. , vol.285 , pp. 701-705
    • Wu, J.1    Michel, H.2    Rossomando, A.3    Haystead, T.4    Shabanowitz, J.5    Hunt, D.F.6    Sturgill, T.W.7
  • 20
    • 0027526249 scopus 로고
    • Functional expression of a MAP kinase kinase in COS cells and recognition by an anti-STE7/byr1 antibody
    • C. M. Haystead, J. Wu, P. Gregory, T. W. Sturgill and T. A. Haystead, Functional expression of a MAP kinase kinase in COS cells and recognition by an anti-STE7/byr1 antibody. FEBS Lett. 317, 12-16 (1993).
    • (1993) FEBS Lett. , vol.317 , pp. 12-16
    • Haystead, C.M.1    Wu, J.2    Gregory, P.3    Sturgill, T.W.4    Haystead, T.A.5
  • 21
    • 0027532627 scopus 로고
    • Regulation and properties of extra-cellular signal-regulated protein kinases 1 and 2 in vitro
    • D. J. Robbins, E. Zhen, H. Owaki, C. A. Vanderbilt, D. Ebert, T. D. Geppert and M. H. Cobb, Regulation and properties of extra-cellular signal-regulated protein kinases 1 and 2 in vitro. J. Biol. Chem. 268, 5097-5106 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 5097-5106
    • Robbins, D.J.1    Zhen, E.2    Owaki, H.3    Vanderbilt, C.A.4    Ebert, D.5    Geppert, T.D.6    Cobb, M.H.7
  • 22
    • 0027202110 scopus 로고
    • Identification and characterization of a new mammalian mitogen-activated protein kinase kinase, MKK2
    • J. Wu, J. K. Harrison, P. Dent, K. R. Lynch, M. J. Weber and T. W. Sturgill, Identification and characterization of a new mammalian mitogen-activated protein kinase kinase, MKK2. Mol. Cell Biol. 13, 4539-4548 (1993).
    • (1993) Mol. Cell Biol. , vol.13 , pp. 4539-4548
    • Wu, J.1    Harrison, J.K.2    Dent, P.3    Lynch, K.R.4    Weber, M.J.5    Sturgill, T.W.6
  • 24
    • 0026641090 scopus 로고
    • Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro
    • P. Dent, W. Haser, T. A. Haystead, L. A. Vincent, T. M. Roberts and T. W. Sturgill, Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro. Science 257, 1404-1407 (1992).
    • (1992) Science , vol.257 , pp. 1404-1407
    • Dent, P.1    Haser, W.2    Haystead, T.A.3    Vincent, L.A.4    Roberts, T.M.5    Sturgill, T.W.6
  • 25
    • 0033584841 scopus 로고    scopus 로고
    • RIP2 is a Raf1-activated mitogen-activated protein kinase kinase
    • T. A. Navas, D. T. Baldwin and T. A. Stewart, RIP2 is a Raf1-activated mitogen-activated protein kinase kinase. J. Biol. Chem. 274, 33684-33690 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 33684-33690
    • Navas, T.A.1    Baldwin, D.T.2    Stewart, T.A.3
  • 26
    • 0030881165 scopus 로고    scopus 로고
    • Mutations of critical amino acids affect the biological and biochemical properties of oncogenic A-Raf and Raf-1
    • E. Bosch, H. Cherwinski, D. Peterson and M. McMahon, Mutations of critical amino acids affect the biological and biochemical properties of oncogenic A-Raf and Raf-1. Oncogene 15, 1021-1033 (1997).
    • (1997) Oncogene , vol.15 , pp. 1021-1033
    • Bosch, E.1    Cherwinski, H.2    Peterson, D.3    McMahon, M.4
  • 27
    • 0031041171 scopus 로고    scopus 로고
    • Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic ras and tyrosine kinases
    • R. Marais, Y. Light, H. F. Paterson, C. S. Mason and C. J. Marshall, Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic ras and tyrosine kinases. J. Biol. Chem. 272, 4378-4383 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 4378-4383
    • Marais, R.1    Light, Y.2    Paterson, H.F.3    Mason, C.S.4    Marshall, C.J.5
  • 29
    • 0027337519 scopus 로고
    • Complexes of Ras. GTP with Raf-1 and mitogen-activated protein kinase kinase
    • S. A. Moodie, B. M. Willumsen, M. J. Weber and A. Wolfman, Complexes of Ras. GTP with Raf-1 and mitogen-activated protein kinase kinase. Science 260, 1658-1661 (1993).
    • (1993) Science , vol.260 , pp. 1658-1661
    • Moodie, S.A.1    Willumsen, B.M.2    Weber, M.J.3    Wolfman, A.4
  • 31
    • 0028272507 scopus 로고
    • Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
    • S. J. Leevers, H. F. Paterson and C. J. Marshall, Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 369, 411-414 (1994).
    • (1994) Nature , vol.369 , pp. 411-414
    • Leevers, S.J.1    Paterson, H.F.2    Marshall, C.J.3
  • 32
    • 0028169624 scopus 로고
    • 6-Raf-1 in vitro by partially purified plasma membranes from v-Ras-transformed and serum stimulated fibroblasts
    • 6-Raf-1 in vitro by partially purified plasma membranes from v-Ras-transformed and serum stimulated fibroblasts. Proc. Natl. Acad. Sci. USA 91, 9544-9548 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9544-9548
    • Dent, P.1    Sturgill, T.W.2
  • 33
    • 0037169533 scopus 로고    scopus 로고
    • Phosphorylation of the myosin-binding subunit of myosin phosphatase by Raf-1 and inhibition of phosphatase activity
    • C. G. Broustas, N. Grammatikakis, M. Eto, P. Dent, D. L. Brautigan and U. Kasid, Phosphorylation of the myosin-binding subunit of myosin phosphatase by Raf-1 and inhibition of phosphatase activity. J. Biol. Chem. 277, 3053-3059 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 3053-3059
    • Broustas, C.G.1    Grammatikakis, N.2    Eto, M.3    Dent, P.4    Brautigan, D.L.5    Kasid, U.6
  • 34
    • 0034944380 scopus 로고    scopus 로고
    • Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating kinase 1 through a MEK-ERK independent mechanism
    • J. Chen, K. Fujii, L. Zhang, T. Roberts and H. Fu, Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating kinase 1 through a MEK-ERK independent mechanism. Proc. Natl. Acad. Sci. USA 98, 7783-7788 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 7783-7788
    • Chen, J.1    Fujii, K.2    Zhang, L.3    Roberts, T.4    Fu, H.5
  • 35
    • 0030919893 scopus 로고    scopus 로고
    • Activation of c-Raf-1 by Ras and Src through different mechanisms: Activation in vivo and in vitro
    • D. Stokoe and F. McCormick, Activation of c-Raf-1 by Ras and Src through different mechanisms: Activation in vivo and in vitro. EMBO J. 16, 2384-2396 (1997).
    • (1997) EMBO J. , vol.16 , pp. 2384-2396
    • Stokoe, D.1    McCormick, F.2
  • 36
    • 0032474838 scopus 로고    scopus 로고
    • A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
    • G. Tzivion, J. Luo and J. Avruch, A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity. Nature 394, 88-92 (1998).
    • (1998) Nature , vol.394 , pp. 88-92
    • Tzivion, G.1    Luo, J.2    Avruch, J.3
  • 38
    • 0033166740 scopus 로고    scopus 로고
    • Interactions of c-Raf-1 with phosphatidylserine and 14-3-3
    • R. A. McPherson, A. Harding, S. Roy, A. Lane and J. F. Hancock, Interactions of c-Raf-1 with phosphatidylserine and 14-3-3. Oncogene 18, 3862-3869 (1999).
    • (1999) Oncogene , vol.18 , pp. 3862-3869
    • McPherson, R.A.1    Harding, A.2    Roy, S.3    Lane, A.4    Hancock, J.F.5
  • 40
    • 0035811597 scopus 로고    scopus 로고
    • Protein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactions
    • M. Jaumot and J. F. Hancock, Protein phosphatases 1 and 2A promote Raf-1 activation by regulating 14-3-3 interactions. Oncogene 20, 3949-3958 (2001).
    • (2001) Oncogene , vol.20 , pp. 3949-3958
    • Jaumot, M.1    Hancock, J.F.2
  • 41
    • 0034624783 scopus 로고    scopus 로고
    • Regulation of the protein kinase Raf-1 by oncogenic Ras through phosphatidylinositol 3-kinase, Cdc42/Rac and Pak
    • H. Sun, A. J. King, H. B. Diaz and M. S. Marshall, Regulation of the protein kinase Raf-1 by oncogenic Ras through phosphatidylinositol 3-kinase, Cdc42/Rac and Pak. Curr. Biol. 10, 281-284 (2000).
    • (2000) Curr. Biol. , vol.10 , pp. 281-284
    • Sun, H.1    King, A.J.2    Diaz, H.B.3    Marshall, M.S.4
  • 44
    • 0027364980 scopus 로고
    • Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase
    • J. R. Fabian, I. O. Daar and D. K. Morrison, Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase. Mol. Cell Biol. 13, 7170-7179 (1993).
    • (1993) Mol. Cell Biol. , vol.13 , pp. 7170-7179
    • Fabian, J.R.1    Daar, I.O.2    Morrison, D.K.3
  • 45
    • 0029014973 scopus 로고
    • Reversal of Raf-1 activation by purified and membrane associated protein phosphatases
    • P. Dent, T. Jelinek, D. K. Morrison, M. J. Weber and T. W. Sturgill, Reversal of Raf-1 activation by purified and membrane associated protein phosphatases. Science 268, 1902-1906 (1995).
    • (1995) Science , vol.268 , pp. 1902-1906
    • Dent, P.1    Jelinek, T.2    Morrison, D.K.3    Weber, M.J.4    Sturgill, T.W.5
  • 46
    • 0029006126 scopus 로고
    • Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation
    • R. Marais, Y. Light, H. F. Paterson and C. J. Marshall, Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J. 14, 3136-3145 (1995).
    • (1995) EMBO J. , vol.14 , pp. 3136-3145
    • Marais, R.1    Light, Y.2    Paterson, H.F.3    Marshall, C.J.4
  • 47
    • 0039791449 scopus 로고    scopus 로고
    • Activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by conventional, novel, and atypical protein kinase C isotypes
    • D. C. Schonwasser, R. M. Marais, C. J. Marshall and P. J. Parker, Activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by conventional, novel, and atypical protein kinase C isotypes. Mol. Cell Biol. 18, 790-798 (1998).
    • (1998) Mol. Cell Biol. , vol.18 , pp. 790-798
    • Schonwasser, D.C.1    Marais, R.M.2    Marshall, C.J.3    Parker, P.J.4
  • 48
    • 0031038588 scopus 로고    scopus 로고
    • Role of diacylglycerol-regulated protein kinase C isotypes in growth factor activation of the Raf-1 protein kinase
    • H. Cai, U. Smola, V. Wixler, I. Eisenmann-Tappe, M. T. Diaz-Meco, J. Moscat, U. Rapp and G. M. Cooper, Role of diacylglycerol-regulated protein kinase C isotypes in growth factor activation of the Raf-1 protein kinase. Mol. Cell Biol. 17, 732-741 (1997).
    • (1997) Mol. Cell Biol. , vol.17 , pp. 732-741
    • Cai, H.1    Smola, U.2    Wixler, V.3    Eisenmann-Tappe, I.4    Diaz-Meco, M.T.5    Moscat, J.6    Rapp, U.7    Cooper, G.M.8
  • 49
    • 0033607633 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Raf by Akt (protein kinase B)
    • S. Zimmermann and K. Moelling, Phosphorylation and regulation of Raf by Akt (protein kinase B). Science 286, 1741-1744 (1999).
    • (1999) Science , vol.286 , pp. 1741-1744
    • Zimmermann, S.1    Moelling, K.2
  • 50
    • 0035823542 scopus 로고    scopus 로고
    • Regulation of Raf by Akt controls growth and differentiation in vascular smooth muscle cells
    • H. P. Reusch, S. Zimmermann, M. Schaefer, M. Paul and K. Moelling, Regulation of Raf by Akt controls growth and differentiation in vascular smooth muscle cells. J. Biol. Chem. 276, 33630-33637 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 33630-33637
    • Reusch, H.P.1    Zimmermann, S.2    Schaefer, M.3    Paul, M.4    Moelling, K.5
  • 51
  • 52
    • 0027468233 scopus 로고
    • A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos
    • J. P. Olivier, T. Raabe, M. Henkemeyer, B. Dickson, G. Mbamalu, B. Margolis, J. Schlessinger, E. Hafen and T. Pawson, A Drosophila SH2-SH3 adaptor protein implicated in coupling the sevenless tyrosine kinase to an activator of Ras guanine nucleotide exchange, Sos. Cell 73, 179-191 (1993).
    • (1993) Cell , vol.73 , pp. 179-191
    • Olivier, J.P.1    Raabe, T.2    Henkemeyer, M.3    Dickson, B.4    Mbamalu, G.5    Margolis, B.6    Schlessinger, J.7    Hafen, E.8    Pawson, T.9
  • 53
    • 0024950524 scopus 로고
    • Growth factor signaling pathways: Phosphoinositide metabolism and phosphorylation of phospholipase C
    • M. I. Wahl, S. Nishibe and G. Carpenter, Growth factor signaling pathways: Phosphoinositide metabolism and phosphorylation of phospholipase C. Cancer Cells 1, 101-107 (1989).
    • (1989) Cancer Cells , vol.1 , pp. 101-107
    • Wahl, M.I.1    Nishibe, S.2    Carpenter, G.3
  • 54
    • 0027029552 scopus 로고
    • Involvement of G proteins, cytoplasmic calcium, phospholipases, phospholipid-derived second messengers, and protein kinases in signal transduction from mitogenic cell surface receptors
    • R. A. Frye, Involvement of G proteins, cytoplasmic calcium, phospholipases, phospholipid-derived second messengers, and protein kinases in signal transduction from mitogenic cell surface receptors. Cancer Treat. Res. 63, 281-299 (1992).
    • (1992) Cancer Treat. Res. , vol.63 , pp. 281-299
    • Frye, R.A.1
  • 56
    • 0028971813 scopus 로고
    • Phosphoinositide-specific phospholipase C and mitogenic signaling
    • D. Y. Noh, S. H. Shin and S. G. Rhee, Phosphoinositide-specific phospholipase C and mitogenic signaling. Biochim. Biophys. Acta 1242, 99-113 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1242 , pp. 99-113
    • Noh, D.Y.1    Shin, S.H.2    Rhee, S.G.3
  • 57
    • 0034653608 scopus 로고    scopus 로고
    • The PI3K-PDK1 connection: More than just a road to PKB
    • B. Vanhaesebroeck and D. R. Alessi, The PI3K-PDK1 connection: More than just a road to PKB. Biochem. J. 346, 561-576 (2000).
    • (2000) Biochem. J. , vol.346 , pp. 561-576
    • Vanhaesebroeck, B.1    Alessi, D.R.2
  • 58
    • 0032497832 scopus 로고    scopus 로고
    • Structure and function of phospho-inositide 3-kinases
    • M. P. Wymann and L. Pirola, Structure and function of phospho-inositide 3-kinases. Biochim. Biophys. Acta 1436, 127-150 (1998).
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 127-150
    • Wymann, M.P.1    Pirola, L.2
  • 59
    • 0035941295 scopus 로고    scopus 로고
    • Specific binding of the C-terminal Src homology 2 domain of the p85α subunit of phosphoinositide 3-kinase to phosphatidylinositol 3,4,5-trisphosphate. Localization and engineering of the phosphoinositide-binding motif
    • T. T. Ching, H. P. Lin, C. C. Yang, M. Oliveira, P. J. Lu and C. S. Chen, Specific binding of the C-terminal Src homology 2 domain of the p85α subunit of phosphoinositide 3-kinase to phosphatidylinositol 3,4,5-trisphosphate. Localization and engineering of the phosphoinositide-binding motif. J. Biol. Chem. 276, 43932-43938 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 43932-43938
    • Ching, T.T.1    Lin, H.P.2    Yang, C.C.3    Oliveira, M.4    Lu, P.J.5    Chen, C.S.6
  • 60
    • 0035360262 scopus 로고    scopus 로고
    • A naturally occurring secreted human ErbB3 receptor isoform inhibits heregulin-stimulated activation of ErbB2, ErbB3, and ErbB4
    • H. Lee, R. W. Akita, M. X. Sliwkowski and N. J. Maihle, A naturally occurring secreted human ErbB3 receptor isoform inhibits heregulin-stimulated activation of ErbB2, ErbB3, and ErbB4. Cancer Res. 61, 4467-4473 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 4467-4473
    • Lee, H.1    Akita, R.W.2    Sliwkowski, M.X.3    Maihle, N.J.4
  • 61
    • 0035980153 scopus 로고    scopus 로고
    • Erk regulates the hepatocyte growth factor-mediated interaction of gab1 and the phosphatidylinositol 3-kinase
    • C. F. Yu, B. Roshan, Z. X. Liu and L. G. Cantley, Erk regulates the hepatocyte growth factor-mediated interaction of gab1 and the phosphatidylinositol 3-kinase. J. Biol. Chem. 276, 32552-32558 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 32552-32558
    • Yu, C.F.1    Roshan, B.2    Liu, Z.X.3    Cantley, L.G.4
  • 62
    • 0031948845 scopus 로고    scopus 로고
    • Protein kinase B activation and lamellipodium formation are independent phosphoinositide 3-kinase-mediated events differentially regulated by endogenous Ras
    • D. H. Van-Weering, J. de Rooij, B. Marte, J. Downward, J. L. Bos and B. M. Burgering, Protein kinase B activation and lamellipodium formation are independent phosphoinositide 3-kinase-mediated events differentially regulated by endogenous Ras. Mol. Cell Biol. 18, 1802-1811 (1998).
    • (1998) Mol. Cell Biol. , vol.18 , pp. 1802-1811
    • Van-Weering, D.H.1    De Rooij, J.2    Marte, B.3    Downward, J.4    Bos, J.L.5    Burgering, B.M.6
  • 63
    • 0033826512 scopus 로고    scopus 로고
    • New role for Shc in activation of the phosphatidylinositol 3-kinase/Akt pathway
    • H. Gu, H. Maeda, J. J. Moon, J. D. Lord, M. Yoakim, B. H. Nelson and B. G. Neel, New role for Shc in activation of the phosphatidylinositol 3-kinase/Akt pathway. Mol. Cell Biol. 20, 7109-7120 (2000).
    • (2000) Mol. Cell Biol. , vol.20 , pp. 7109-7120
    • Gu, H.1    Maeda, H.2    Moon, J.J.3    Lord, J.D.4    Yoakim, M.5    Nelson, B.H.6    Neel, B.G.7
  • 65
    • 0033912843 scopus 로고    scopus 로고
    • Effect of phosphoinositide-dependent kinase 1 on protein kinase B translocation and its subsequent activation
    • N. Filippa, C. L. Sable, B. A. Hemmings and E. Van Obberghen, Effect of phosphoinositide-dependent kinase 1 on protein kinase B translocation and its subsequent activation. Mol. Cell Biol. 20, 5712-5721 (2000).
    • (2000) Mol. Cell Biol. , vol.20 , pp. 5712-5721
    • Filippa, N.1    Sable, C.L.2    Hemmings, B.A.3    Van Obberghen, E.4
  • 66
    • 0035813230 scopus 로고    scopus 로고
    • Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 (PDK1) and their role in regulating kinase activity
    • J. Park, M. M. Hill, D. Hess, D. P. Brazil, J. Hofsteenge and B. A. Hemmings, Identification of tyrosine phosphorylation sites on 3-phosphoinositide-dependent protein kinase-1 (PDK1) and their role in regulating kinase activity. J. Biol. Chem. 276, 37459-37471 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 37459-37471
    • Park, J.1    Hill, M.M.2    Hess, D.3    Brazil, D.P.4    Hofsteenge, J.5    Hemmings, B.A.6
  • 67
    • 0035835824 scopus 로고    scopus 로고
    • PTEN: Life as a tumor suppressor
    • L. Simpson and R. Parsons, PTEN: Life as a tumor suppressor. Exp. Cell Res. 264, 29-41 (2001).
    • (2001) Exp. Cell Res. , vol.264 , pp. 29-41
    • Simpson, L.1    Parsons, R.2
  • 68
    • 0033852872 scopus 로고    scopus 로고
    • Mutations of the human PTEN gene
    • D. Bonneau and M. Longy, Mutations of the human PTEN gene. Hum. Mutat. 16, 109-122 (2000).
    • (2000) Hum. Mutat. , vol.16 , pp. 109-122
    • Bonneau, D.1    Longy, M.2
  • 69
    • 0034927062 scopus 로고    scopus 로고
    • The developmental biology of brain tumors
    • R. Wechsler-Reya and M. P. Scott, The developmental biology of brain tumors. Annu. Rev. Neurosci. 24, 385-428 (2001).
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 385-428
    • Wechsler-Reya, R.1    Scott, M.P.2
  • 70
    • 0032558822 scopus 로고    scopus 로고
    • Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC
    • D. Haas-Kogan, N. Shalev, M. Wong, G. Mills, G. Yount and D. Stokoe, Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC. Curr. Biol. 8, 1195-1198 (1998).
    • (1998) Curr. Biol. , vol.8 , pp. 1195-1198
    • Haas-Kogan, D.1    Shalev, N.2    Wong, M.3    Mills, G.4    Yount, G.5    Stokoe, D.6
  • 71
    • 0034634443 scopus 로고    scopus 로고
    • Further evidence that 3-phosphoinositide-dependent protein kinase-1 (PDK1) is required for the stability and phosphorylation of protein kinase C (PKC) isoforms
    • A. Balendran, G. R. Hare, A. Kieloch, M. R. Williams and D. R. Alessi, Further evidence that 3-phosphoinositide-dependent protein kinase-1 (PDK1) is required for the stability and phosphorylation of protein kinase C (PKC) isoforms. FEBS Lett. 484, 217-223 (2000).
    • (2000) FEBS Lett. , vol.484 , pp. 217-223
    • Balendran, A.1    Hare, G.R.2    Kieloch, A.3    Williams, M.R.4    Alessi, D.R.5
  • 72
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • D. A. Cross, D. R. Alessi, P. Cohen, M. Andjelkovich and B. A. Hemmings, Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 378, 785-789 (1995).
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 73
    • 0030590875 scopus 로고    scopus 로고
    • Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase
    • D. R. Alessi, F. B. Caudwell, M. Andjelkovic, B. A. Hemmings and P. Cohen, Molecular basis for the substrate specificity of protein kinase B; comparison with MAPKAP kinase-1 and p70 S6 kinase. FEBS Lett. 399, 333-338 (1996).
    • (1996) FEBS Lett. , vol.399 , pp. 333-338
    • Alessi, D.R.1    Caudwell, F.B.2    Andjelkovic, M.3    Hemmings, B.A.4    Cohen, P.5
  • 75
    • 0035877778 scopus 로고    scopus 로고
    • Differential activation of protein kinase B and p70(S6)K by glucose and insulin-like growth factor 1 in pancreatic beta-cells (INS-1)
    • L. M. Dickson, M. K. Lingohr, J. McCuaig, S. R. Hugl, L. Snow, B. B. Kahn, M. G. Myers and C. J. Rhodes, Differential activation of protein kinase B and p70(S6)K by glucose and insulin-like growth factor 1 in pancreatic beta-cells (INS-1). J. Biol. Chem. 276, 21110-21120 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 21110-21120
    • Dickson, L.M.1    Lingohr, M.K.2    McCuaig, J.3    Hugl, S.R.4    Snow, L.5    Kahn, B.B.6    Myers, M.G.7    Rhodes, C.J.8
  • 76
    • 0033043389 scopus 로고    scopus 로고
    • Domain swapping used to investigate the mechanism of protein kinase B regulation by 3-phosphoinositide-dependent protein kinase 1 and Ser473 kinase
    • M. Andjelkovic, S. M. Maira, P. Cron, P. J. Parker and B. A. Hemmings, Domain swapping used to investigate the mechanism of protein kinase B regulation by 3-phosphoinositide-dependent protein kinase 1 and Ser473 kinase. Mol. Cell. Biol. 19, 5061-5072 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5061-5072
    • Andjelkovic, M.1    Maira, S.M.2    Cron, P.3    Parker, P.J.4    Hemmings, B.A.5
  • 77
    • 0035793574 scopus 로고    scopus 로고
    • p38 kinase-dependent MAP-KAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils
    • M. J. Rane, P. Y. Coxon, D. W. Powell, R. Webster, J. B. Klein, W. Pierce, P. Ping and K. R. McLeish, p38 Kinase-dependent MAP- KAPK-2 activation functions as 3-phosphoinositide-dependent kinase-2 for Akt in human neutrophils. J. Biol. Chem. 276, 3517- 3523 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 3517-3523
    • Rane, M.J.1    Coxon, P.Y.2    Powell, D.W.3    Webster, R.4    Klein, J.B.5    Pierce, W.6    Ping, P.7    McLeish, K.R.8
  • 79
    • 0027423418 scopus 로고
    • Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain
    • M. Hibi, A. Lin, T. Smeal, A. Minden and M. Karin, Identification of an oncoprotein- and UV-responsive protein kinase that binds and potentiates the c-Jun activation domain. Genes. Dev. 7, 2135-2148 (1993).
    • (1993) Genes. Dev. , vol.7 , pp. 2135-2148
    • Hibi, M.1    Lin, A.2    Smeal, T.3    Minden, A.4    Karin, M.5
  • 80
    • 0028329953 scopus 로고
    • JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain
    • B. Derijard, M. Hibi, I. H. Wu, T. Barrett, B. Su, T. Deng, M. Karin and R. J. Davis, JNK1: A protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain. Cell 76, 1025-1037 (1994).
    • (1994) Cell , vol.76 , pp. 1025-1037
    • Derijard, B.1    Hibi, M.2    Wu, I.H.3    Barrett, T.4    Su, B.5    Deng, T.6    Karin, M.7    Davis, R.J.8
  • 81
    • 0032603404 scopus 로고    scopus 로고
    • Signal transduction by the c-Jun N-terminal kinase
    • R. J. Davis, Signal transduction by the c-Jun N-terminal kinase. Biochem. Soc. Symp. 64, 1-12 (1999).
    • (1999) Biochem. Soc. Symp. , vol.64 , pp. 1-12
    • Davis, R.J.1
  • 82
    • 0032536816 scopus 로고    scopus 로고
    • Differential targeting of MAP kinases to the ETS-domain transcription factor Elk-1
    • S. H. Yang, A. J. Whitmarsh, R. J. Davis and A. D. Sharrocks, Differential targeting of MAP kinases to the ETS-domain transcription factor Elk-1. EMBO J. 17, 1740-1749 (1998).
    • (1998) EMBO J. , vol.17 , pp. 1740-1749
    • Yang, S.H.1    Whitmarsh, A.J.2    Davis, R.J.3    Sharrocks, A.D.4
  • 83
    • 0032703216 scopus 로고    scopus 로고
    • Regulation of c-Myc through phosphorylation at Ser-62 and Ser-71 by c-Jun N-terminal kinase
    • K. Noguchi, C. Kitanaka, H. Yamana, A. Kokubu, T. Mochizuki and Y. Kuchino, Regulation of c-Myc through phosphorylation at Ser-62 and Ser-71 by c-Jun N-terminal kinase. J. Biol. Chem. 274, 32580-32587 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 32580-32587
    • Noguchi, K.1    Kitanaka, C.2    Yamana, H.3    Kokubu, A.4    Mochizuki, T.5    Kuchino, Y.6
  • 84
    • 0028935974 scopus 로고
    • Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms
    • B. Derijard, J. Raingeaud, T. Barrett, I. H. Wu, J. Han, R. J. Ulevitch and R. J. Davis, Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms. Science 267, 682-685 (1995).
    • (1995) Science , vol.267 , pp. 682-685
    • Derijard, B.1    Raingeaud, J.2    Barrett, T.3    Wu, I.H.4    Han, J.5    Ulevitch, R.J.6    Davis, R.J.7
  • 87
    • 0034598814 scopus 로고    scopus 로고
    • KFC, a Ste20-like kinase with mitogenic potential and capability to activate the SAPK/JNK pathway
    • J. T. Yustein, D. Li, D. Robinson and H. J. Kung, KFC, a Ste20-like kinase with mitogenic potential and capability to activate the SAPK/JNK pathway. Oncogene 19, 710-718 (2000).
    • (2000) Oncogene , vol.19 , pp. 710-718
    • Yustein, J.T.1    Li, D.2    Robinson, D.3    Kung, H.J.4
  • 88
    • 0032476674 scopus 로고    scopus 로고
    • Kit signaling through PI 3-kinase and Src kinase pathways: An essential role for Racl and JNK activation in mast cell proliferation
    • I. Timokhina, H. Kissel, G. Stella and P. Besmer, Kit signaling through PI 3-kinase and Src kinase pathways: An essential role for Racl and JNK activation in mast cell proliferation. EMBO J. 17, 6250-6262 (1998).
    • (1998) EMBO J. , vol.17 , pp. 6250-6262
    • Timokhina, I.1    Kissel, H.2    Stella, G.3    Besmer, P.4
  • 89
    • 0033546729 scopus 로고    scopus 로고
    • JNK/SAPK activation by platelet-derived growth factor in A431 cells requires both the phospholipase C-gamma and the phosphatidylinositol 3-kinase signaling pathways of the receptor
    • Z. Assefa, M. Valius, T. Vantus, P. Agostinis, W. Merlevede and J. R. Vandenheede, JNK/SAPK activation by platelet-derived growth factor in A431 cells requires both the phospholipase C-gamma and the phosphatidylinositol 3-kinase signaling pathways of the receptor. Biochem. Biophys. Res. Commun. 261, 641-645 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 641-645
    • Assefa, Z.1    Valius, M.2    Vantus, T.3    Agostinis, P.4    Merlevede, W.5    Vandenheede, J.R.6
  • 90
    • 0033135283 scopus 로고    scopus 로고
    • The Drosophila Pkn protein kinase is a Rho/Rac effector target required for dorsal closure during embryogenesis
    • Y. Lu and J. Settleman, The Drosophila Pkn protein kinase is a Rho/Rac effector target required for dorsal closure during embryogenesis. Genes Dev. 13, 1168-1180 (1999).
    • (1999) Genes Dev. , vol.13 , pp. 1168-1180
    • Lu, Y.1    Settleman, J.2
  • 91
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • J. Han, J. D. Lee, L. Bibbs and R. J. Ulevitch, A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265, 808-811 (1994).
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 93
    • 0029683683 scopus 로고    scopus 로고
    • Signaling events controlling the molecular response to genotoxic stress
    • N. J. Holbrook, Y. Liu and A. J. Fornace, Signaling events controlling the molecular response to genotoxic stress. EXS 77, 273-288 (1996).
    • (1996) EXS , vol.77 , pp. 273-288
    • Holbrook, N.J.1    Liu, Y.2    Fornace, A.J.3
  • 94
    • 0035816539 scopus 로고    scopus 로고
    • BetaPix-enhanced p38 activation by Cdc42/Rac/PAK/MKK3/6-mediated pathway. Implication in the regulation of membrane ruffling
    • S. H. Lee, M. Eom, S. J. Lee, S. Kim, H. J. Park and D. Park, BetaPix-enhanced p38 activation by Cdc42/Rac/PAK/MKK3/6-mediated pathway. Implication in the regulation of membrane ruffling. J. Biol. Chem. 276, 25066-25072 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 25066-25072
    • Lee, S.H.1    Eom, M.2    Lee, S.J.3    Kim, S.4    Park, H.J.5    Park, D.6
  • 95
    • 0035066383 scopus 로고    scopus 로고
    • Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation
    • J. M. Kyriakis and J. Avruch, Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation. Physiol. Rev. 81, 807-869 (2001).
    • (2001) Physiol. Rev. , vol.81 , pp. 807-869
    • Kyriakis, J.M.1    Avruch, J.2
  • 96
    • 0035002347 scopus 로고    scopus 로고
    • Developmental regulation of mitogen-activated protein kinase-activated kinases-2 and -3 (MAPKAPK-2/-3) in vivo during corpus luteum formation in the rat
    • E. T. Maizels, A. Mukherjee, A. Sithanandam, C. A. Peters, J. Cottom, K. E. Mayo and M. Hunzicker-Dunn, Developmental regulation of mitogen-activated protein kinase-activated kinases-2 and -3 (MAPKAPK-2/-3) in vivo during corpus luteum formation in the rat. Mol. Endocrinol. 15, 716-733 (2001).
    • (2001) Mol. Endocrinol. , vol.15 , pp. 716-733
    • Maizels, E.T.1    Mukherjee, A.2    Sithanandam, A.3    Peters, C.A.4    Cottom, J.5    Mayo, K.E.6    Hunzicker-Dunn, M.7
  • 97
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p 38, and may mediate activation of CREB
    • M. M. Deak, A. D. Clifton, L. M. Lucocq and D. R. Alessi, Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMBO J. 17, 4426-4441 (1998).
    • (1998) EMBO J. , vol.17 , pp. 4426-4441
    • Deak, M.M.1    Clifton, A.D.2    Lucocq, L.M.3    Alessi, D.R.4
  • 98
    • 0036193378 scopus 로고    scopus 로고
    • MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts
    • G. R Wiggin, A. Soloaga, J. M. Foster, V. Murray-Tait, P. Cohen and J. S. Arthur, MSK1 and MSK2 are required for the mitogen- and stress-induced phosphorylation of CREB and ATF1 in fibroblasts. Mol. Cell. Biol. 22, 2871-2881 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2871-2881
    • Wiggin, G.R.1    Soloaga, A.2    Foster, J.M.3    Murray-Tait, V.4    Cohen, P.5    Arthur, J.S.6
  • 99
    • 0035072677 scopus 로고    scopus 로고
    • Protein kinase inhibitors can suppress stress-induced dissociation of Hsp27
    • K. Kato, H. Ito, I. Iwamoto, K. Lida and Y. Inaguma, Protein kinase inhibitors can suppress stress-induced dissociation of Hsp27. Cell Stress Chaperones 6, 16-20 (2001).
    • (2001) Cell Stress Chaperones , vol.6 , pp. 16-20
    • Kato, K.1    Ito, H.2    Iwamoto, I.3    Lida, K.4    Inaguma, Y.5
  • 100
    • 0035207024 scopus 로고    scopus 로고
    • CTGF/Hcs24 induces chondrocyte differentiation through a p38 mitogen-activated protein kinase (p38MAPK), and proliferation through a p44/42 MAPK/extracellular-signal regulated kinase (ERK)
    • G. Yosimichi, T. Nakanishi, T. Nishida, T. Hattori, T. Takano-Yamamoto and M. Takigawa, CTGF/Hcs24 induces chondrocyte differentiation through a p38 mitogen-activated protein kinase (p38MAPK), and proliferation through a p44/42 MAPK/extracellular-signal regulated kinase (ERK). Eur. J. Biochem. 268, 6058-6065 (2001).
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6058-6065
    • Yosimichi, G.1    Nakanishi, T.2    Nishida, T.3    Hattori, T.4    Takano-Yamamoto, T.5    Takigawa, M.6
  • 101
    • 0034839130 scopus 로고    scopus 로고
    • ERK 1, 2 and p38 pathways are involved in the proliferative stimuli mediated by urokinase in osteoblastic SaOS- 2 cell line
    • N. Juretic, J. F. Santibanez, C. Hurtado and J. Martinez, ERK 1, 2 and p38 pathways are involved in the proliferative stimuli mediated by urokinase in osteoblastic SaOS-2 cell line. J. Cell. Biochem. 83, 92-98 (2001).
    • (2001) J. Cell. Biochem. , vol.83 , pp. 92-98
    • Juretic, N.1    Santibanez, J.F.2    Hurtado, C.3    Martinez, J.4
  • 102
    • 0035030360 scopus 로고    scopus 로고
    • Opposing effect of p38 and p44/42 signaling on TNF-α-induced apoptosis in bovine aortic endothelial cells
    • W. L. Liu, X. Guo, Q. Q. Chen and Z. G. Guo, Opposing effect of p38 and p44/42 signaling on TNF-α-induced apoptosis in bovine aortic endothelial cells. Acta Pharmacol. Sin. 22, 405-410 (2001).
    • (2001) Acta Pharmacol. Sin. , vol.22 , pp. 405-410
    • Liu, W.L.1    Guo, X.2    Chen, Q.Q.3    Guo, Z.G.4
  • 103
    • 0037059796 scopus 로고    scopus 로고
    • ERK-1/2 and p38 kinase oppositely regulate nitric oxide-induced apoptosis of chondrocytes in association with p53, caspase-3, and differentiation status
    • S. J. Kim, J. W. Ju, C. D. Oh, Y. M. Yoon, W. K. Song, J. H. Kim, Y. J. Yoo, O. S. Bang, S. S. Kang and J. S. Chun, ERK-1/2 and p38 kinase oppositely regulate nitric oxide-induced apoptosis of chondrocytes in association with p53, caspase-3, and differentiation status. J. Biol. Chem. 277, 1332-1339 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 1332-1339
    • Kim, S.J.1    Ju, J.W.2    Oh, C.D.3    Yoon, Y.M.4    Song, W.K.5    Kim, J.H.6    Yoo, Y.J.7    Bang, O.S.8    Kang, S.S.9    Chun, J.S.10
  • 104
    • 0034175409 scopus 로고    scopus 로고
    • Role of the p38 and MEK-1/2/p42/44 MAP kinase pathways in the differential activation of human immunodeficiency virus gene expression by ultraviolet and ionizing radiation
    • M. M. Taher, C. M. Hershey, J. D. Oakley and K. Valerie, Role of the p38 and MEK-1/2/p42/44 MAP kinase pathways in the differential activation of human immunodeficiency virus gene expression by ultraviolet and ionizing radiation. Photochem. Photobiol. 71, 455-459 (2000).
    • (2000) Photochem. Photobiol. , vol.71 , pp. 455-459
    • Taher, M.M.1    Hershey, C.M.2    Oakley, J.D.3    Valerie, K.4
  • 107
    • 0034468132 scopus 로고    scopus 로고
    • Tyrosine kinase signalling in breast cancer: ErbB family receptor tyrosine kinases
    • D. F. Stern, Tyrosine kinase signalling in breast cancer: ErbB family receptor tyrosine kinases. Breast Cancer Res. 2, 176-183 (2000).
    • (2000) Breast Cancer Res. , vol.2 , pp. 176-183
    • Stern, D.F.1
  • 108
    • 0035313702 scopus 로고    scopus 로고
    • Localization and modulation of ErbB receptor tyrosine kinases
    • K. L. Carraway and C. Sweeney, Localization and modulation of ErbB receptor tyrosine kinases. Curr. Opin. Cell Biol. 13, 125-130 (2001).
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 125-130
    • Carraway, K.L.1    Sweeney, C.2
  • 109
    • 0034693801 scopus 로고    scopus 로고
    • Ligand discrimination by ErbB receptors: Differential signaling through differential phosphorylation site usage
    • C. Sweeney and K. L. Carraway, 3rd, Ligand discrimination by ErbB receptors: Differential signaling through differential phosphorylation site usage. Oncogene 19, 5568-5573 (2000).
    • (2000) Oncogene , vol.19 , pp. 5568-5573
    • Sweeney, C.1    Carraway K.L. III2
  • 110
    • 0021336733 scopus 로고
    • C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity
    • C. Cochet, G. N. Gill, J. Meisenhelder, J. A. Cooper and T. Hunter, C-kinase phosphorylates the epidermal growth factor receptor and reduces its epidermal growth factor-stimulated tyrosine protein kinase activity. J. Biol. Chem. 259, 2553-2558 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 2553-2558
    • Cochet, C.1    Gill, G.N.2    Meisenhelder, J.3    Cooper, J.A.4    Hunter, T.5
  • 111
    • 0020988436 scopus 로고
    • The receptor for epidermal growth factor functions as a tyrosyl-specific kinase
    • S. Cohen, The receptor for epidermal growth factor functions as a tyrosyl-specific kinase. Prog. Nucleic Acid. Res. Mol. Biol. 29, 245-247 (1983).
    • (1983) Prog. Nucleic Acid. Res. Mol. Biol. , vol.29 , pp. 245-247
    • Cohen, S.1
  • 112
    • 0024385586 scopus 로고
    • Amplification and rearrangement of c-erb B proto-oncogenes in cancer of human female genital tract
    • X. Zhang, E. Silva, D. Gershenson and M. C. Hung, Amplification and rearrangement of c-erb B proto-oncogenes in cancer of human female genital tract. Oncogene 4, 985-989 (1989).
    • (1989) Oncogene , vol.4 , pp. 985-989
    • Zhang, X.1    Silva, E.2    Gershenson, D.3    Hung, M.C.4
  • 113
    • 0034782994 scopus 로고    scopus 로고
    • Expression profiles of erbb family receptors and prognosis in primary transitional cell carcinoma of the urinary bladder
    • N. H. Chow, S. H. Chan, T. S. Tzai, C. L. Ho and H. S. Liu, Expression profiles of erbb family receptors and prognosis in primary transitional cell carcinoma of the urinary bladder. Clin. Cancer Res. 7, 1957-1962 (2001).
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1957-1962
    • Chow, N.H.1    Chan, S.H.2    Tzai, T.S.3    Ho, C.L.4    Liu, H.S.5
  • 114
    • 0034214087 scopus 로고    scopus 로고
    • Epidermal growth factor receptor vIII enhances tumorigenicity in human breast cancer
    • C. K. Tang, X. Q. Gong, D. K. Moscatello, A. J. Wong and M. E Lippman, Epidermal growth factor receptor vIII enhances tumorigenicity in human breast cancer. Cancer Res. 60, 3081-3087 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 3081-3087
    • Tang, C.K.1    Gong, X.Q.2    Moscatello, D.K.3    Wong, A.J.4    Lippman, M.E.5
  • 115
    • 0032518915 scopus 로고    scopus 로고
    • Analysis of EGF receptor amplicons reveals amplification of multiple expressed sequences
    • X. Y. Wang, D. I. Smith, L. Frederick and C. D. James, Analysis of EGF receptor amplicons reveals amplification of multiple expressed sequences. Oncogene 16, 191-195 (1998).
    • (1998) Oncogene , vol.16 , pp. 191-195
    • Wang, X.Y.1    Smith, D.I.2    Frederick, L.3    James, C.D.4
  • 116
    • 0034231944 scopus 로고    scopus 로고
    • Analysis of genomic rearrangements associated with EGRFvIII expression suggests involvement of Alu repeat elements
    • L. Frederick, G. Eley, X. Y. Wang and C. D. James, Analysis of genomic rearrangements associated with EGRFvIII expression suggests involvement of Alu repeat elements. Neuro-oncol 2, 159-163 (2000).
    • (2000) Neuro-oncol. , vol.2 , pp. 159-163
    • Frederick, L.1    Eley, G.2    Wang, X.Y.3    James, C.D.4
  • 117
    • 0030064531 scopus 로고    scopus 로고
    • Transformation of NIH 3T3 cells by HER3 or HER4 receptors requires the presence of HER1 or HER2
    • K. Zhang, J. Sun, N. Liu, D. Wen, D. Chang, A. Thomason and S. K. Yoshinaga, Transformation of NIH 3T3 cells by HER3 or HER4 receptors requires the presence of HER1 or HER2. J. Biol. Chem. 271, 3884-3890 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 3884-3890
    • Zhang, K.1    Sun, J.2    Liu, N.3    Wen, D.4    Chang, D.5    Thomason, A.6    Yoshinaga, S.K.7
  • 118
  • 119
    • 0032055791 scopus 로고    scopus 로고
    • Proxy activation of protein ErbB2 by heterologous ligands implies a heterotetrameric mode of receptor tyrosine kinase interaction
    • G. C. Huang, X. Ouyang and R. J. Epstein, Proxy activation of protein ErbB2 by heterologous ligands implies a heterotetrameric mode of receptor tyrosine kinase interaction. Biochem. J. 331, 113-119 (1998).
    • (1998) Biochem. J. , vol.331 , pp. 113-119
    • Huang, G.C.1    Ouyang, X.2    Epstein, R.J.3
  • 120
    • 0028156927 scopus 로고
    • Heterodimerization of epidermal growth factor receptor and wild-type or kinase-deficient Neu: A mechanism of interreceptor kinase activation and transphosphorylation
    • X. Qian, C. M LeVea, J. K. Freeman, W. C. Dougall and M. I. Greene, Heterodimerization of epidermal growth factor receptor and wild-type or kinase-deficient Neu: A mechanism of interreceptor kinase activation and transphosphorylation. Proc. Natl. Acad. Sci. USA 91, 1500-1504 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 1500-1504
    • Qian, X.1    LeVea, C.M.2    Freeman, J.K.3    Dougall, W.C.4    Greene, M.I.5
  • 121
    • 0035939791 scopus 로고    scopus 로고
    • Expression of herstatin, an autoinhibitor of HER-2/neu, inhibits transactivation of HER-3 by HER-2 and blocks EGF activation of the EGF receptor
    • N. G. Azios, F. J. Romero, M. C. Denton, J. K. Doherty and G. M. Clinton, Expression of herstatin, an autoinhibitor of HER-2/neu, inhibits transactivation of HER-3 by HER-2 and blocks EGF activation of the EGF receptor. Oncogene 20, 5199-5209 (2001).
    • (2001) Oncogene , vol.20 , pp. 5199-5209
    • Azios, N.G.1    Romero, F.J.2    Denton, M.C.3    Doherty, J.K.4    Clinton, G.M.5
  • 122
    • 0034888719 scopus 로고    scopus 로고
    • HER-2 and choice of adjuvant chemotherapy in breast cancer
    • S. Paik and C. Park, HER-2 and choice of adjuvant chemotherapy in breast cancer. Semin. Oncol. 28, 332-335 (2001).
    • (2001) Semin. Oncol. , vol.28 , pp. 332-335
    • Paik, S.1    Park, C.2
  • 123
    • 0034992521 scopus 로고    scopus 로고
    • The epidermal growth factor receptor family as a central element for cellular signal transduction and diversification
    • N. Prenzel, O. M. Fischer, S. Streit, S. Hart and A. Ullrich, The epidermal growth factor receptor family as a central element for cellular signal transduction and diversification. Endocr. Relat. Cancer 8, 11-31 (2001).
    • (2001) Endocr. Relat. Cancer , vol.8 , pp. 11-31
    • Prenzel, N.1    Fischer, O.M.2    Streit, S.3    Hart, S.4    Ullrich, A.5
  • 124
    • 0032578782 scopus 로고    scopus 로고
    • The use of the yeast two hybrid system to evaluate ErbB-3 interactions with SH2 domain containing proteins
    • J. Y. Yoo and A. W. Hamburger, The use of the yeast two hybrid system to evaluate ErbB-3 interactions with SH2 domain containing proteins. Biochem. Biophys. Res. Commun. 251, 903-906 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 903-906
    • Yoo, J.Y.1    Hamburger, A.W.2
  • 125
    • 0027971393 scopus 로고
    • ErbB-3 and ErbB-4 function as the respective low and high affinity receptors of all Neu differentiation factor/heregulin isoforms
    • E. Tzahar, G. Levkowitz, D. Karunagaran, L. Yi, E. Peles, S. Lavi, D. Chang, N. Liu, A. Yayon and D. Wen, ErbB-3 and ErbB-4 function as the respective low and high affinity receptors of all Neu differentiation factor/heregulin isoforms. J. Biol. Chem. 269, 25226-25233 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 25226-25233
    • Tzahar, E.1    Levkowitz, G.2    Karunagaran, D.3    Yi, L.4    Peles, E.5    Lavi, S.6    Chang, D.7    Liu, N.8    Yayon, A.9    Wen, D.10
  • 126
    • 0033564877 scopus 로고    scopus 로고
    • The C-terminus of the kinase-defective neuregulin receptor ErbB-3 confers mitogenic superiority and dictates endocytic routing
    • H. Waterman, I. Alroy, S. Strano, R. Seger and Y. Yarden, The C-terminus of the kinase-defective neuregulin receptor ErbB-3 confers mitogenic superiority and dictates endocytic routing. EMBO J. 18, 3348-3358 (1999).
    • (1999) EMBO J. , vol.18 , pp. 3348-3358
    • Waterman, H.1    Alroy, I.2    Strano, S.3    Seger, R.4    Yarden, Y.5
  • 127
    • 0033583778 scopus 로고    scopus 로고
    • Expression of c-erbB-4/HER4 is regulated in T47D breast carcinoma cells by retinoids and vitamin D3
    • M. Offterdinger, S. M. Schneider, H. Huber and T. W. Grunt, Expression of c-erbB-4/HER4 is regulated in T47D breast carcinoma cells by retinoids and vitamin D3. Biochem. Biophys. Res. Commun. 258, 559-564 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.258 , pp. 559-564
    • Offterdinger, M.1    Schneider, S.M.2    Huber, H.3    Grunt, T.W.4
  • 128
    • 0030131175 scopus 로고    scopus 로고
    • Involvement of the neuregulins and their receptors in cardiac and neural development
    • K. L. Carraway, Involvement of the neuregulins and their receptors in cardiac and neural development. Bioessays 18, 263-266 (1996).
    • (1996) Bioessays , vol.18 , pp. 263-266
    • Carraway, K.L.1
  • 130
    • 0032551990 scopus 로고    scopus 로고
    • Two erbB-4 transcripts are expressed in normal breast and in most breast cancers
    • C. Sawyer, I. Hiles, M. Page, M. Crompton and C. Dean, Two erbB-4 transcripts are expressed in normal breast and in most breast cancers. Oncogene 17, 919-924 (1998).
    • (1998) Oncogene , vol.17 , pp. 919-924
    • Sawyer, C.1    Hiles, I.2    Page, M.3    Crompton, M.4    Dean, C.5
  • 131
    • 0032575135 scopus 로고    scopus 로고
    • Inhibition of mitogen activated protein kinase cascade potentiates cell killing by low dose ionizing radiation in A431 human squamous carcinoma cells
    • S. Carter, K. L. Auer, M. Birrer, P. B. Fisher, R. K. Schmidt-Ullrich, K. Valerie, R. Mikkelsen and P. Dent, Inhibition of mitogen activated protein kinase cascade potentiates cell killing by low dose ionizing radiation in A431 human squamous carcinoma cells. Oncogene 16, 2787-2796 (1998).
    • (1998) Oncogene , vol.16 , pp. 2787-2796
    • Carter, S.1    Auer, K.L.2    Birrer, M.3    Fisher, P.B.4    Schmidt-Ullrich, R.K.5    Valerie, K.6    Mikkelsen, R.7    Dent, P.8
  • 132
    • 0031806483 scopus 로고    scopus 로고
    • Calcium-dependent stimulation of mitogen-activated protein kinase activity in A431 cells by low doses of ionizing radiation
    • B. D. Kavanagh, P. Dent, R. K. Schmidt-Ullrich, P. Chen and R. B. Mikkelsen, Calcium-dependent stimulation of mitogen-activated protein kinase activity in A431 cells by low doses of ionizing radiation. Radiat. Res. 149, 579-587 (1998).
    • (1998) Radiat. Res. , vol.149 , pp. 579-587
    • Kavanagh, B.D.1    Dent, P.2    Schmidt-Ullrich, R.K.3    Chen, P.4    Mikkelsen, R.B.5
  • 133
    • 0000091450 scopus 로고    scopus 로고
    • The effect of ionizing radiation on signal transduction: Antibodies to EGF receptor sensitize A 431 cells to radiation
    • N. Balaban, J. Moni, M. Shannon, L. Dang, E. Murphy and T. Goldkorn, The effect of ionizing radiation on signal transduction: Antibodies to EGF receptor sensitize A431 cells to radiation. Biochim. Biophys. Acta 1314, 147-156 (1996).
    • (1996) Biochim. Biophys. Acta , vol.1314 , pp. 147-156
    • Balaban, N.1    Moni, J.2    Shannon, M.3    Dang, L.4    Murphy, E.5    Goldkorn, T.6
  • 134
    • 0030849058 scopus 로고    scopus 로고
    • Association of Grb2 with Sos and Ras with Raf-1 upon gamma irradiation of breast cancer cells
    • S. Suy, W. B. Anderson, P. Dent, E. Chang and U. Kasid, Association of Grb2 with Sos and Ras with Raf-1 upon gamma irradiation of breast cancer cells. Oncogene 15, 53-61 (1997).
    • (1997) Oncogene , vol.15 , pp. 53-61
    • Suy, S.1    Anderson, W.B.2    Dent, P.3    Chang, E.4    Kasid, U.5
  • 135
    • 0031779534 scopus 로고    scopus 로고
    • The estrogen-like effect of 4-hydroxytamoxifen on induction of transforming growth factor alpha mRNA in MDA-MB-231 breast cancer cells stably expressing the estrogen receptor
    • A. S. Levenson, D. A. Tonetti and V. C. Jordan, The estrogen-like effect of 4-hydroxytamoxifen on induction of transforming growth factor alpha mRNA in MDA-MB-231 breast cancer cells stably expressing the estrogen receptor. Br. J. Cancer 77, 1812-1819 (1998).
    • (1998) Br. J. Cancer , vol.77 , pp. 1812-1819
    • Levenson, A.S.1    Tonetti, D.A.2    Jordan, V.C.3
  • 136
    • 0030038201 scopus 로고    scopus 로고
    • Autocrine regulation of membrane transforming growth factor-α cleavage
    • J. Baselga, J. Mendelson, Y. M. Kim and A. Pandiella, Autocrine regulation of membrane transforming growth factor-α cleavage. J. Biol. Chem. 271, 3279-3284 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 3279-3284
    • Baselga, J.1    Mendelson, J.2    Kim, Y.M.3    Pandiella, A.4
  • 137
    • 0026529225 scopus 로고
    • Expression of oestrogen receptor and transforming growth factor-α in MCF-7 cells after exposure to fractionated irradiation
    • R. K. Schmidt-Ullrich, K. Valerie, W. Chan, D. E. Wazer and P. S. Lin, Expression of oestrogen receptor and transforming growth factor-α in MCF-7 cells after exposure to fractionated irradiation. Int. J. Radiat. Biol. 61, 405-415 (1992).
    • (1992) Int. J. Radiat. Biol. , vol.61 , pp. 405-415
    • Schmidt-Ullrich, R.K.1    Valerie, K.2    Chan, W.3    Wazer, D.E.4    Lin, P.S.5
  • 138
    • 0032894222 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF) receptor blockade inhibits the action of EGF, insulin-like growth factor 1, and a protein kinase A activator on the mitogen-activated protein kinase pathway in prostate cancer cell lines
    • T. Putz, Z. Culig, I. E. Eder, C. Nessler-Menardi, G. Bartsch, H. Grunicke, F. Uberall and H. Klocker, Epidermal growth factor (EGF) receptor blockade inhibits the action of EGF, insulin-like growth factor 1, and a protein kinase A activator on the mitogen-activated protein kinase pathway in prostate cancer cell lines. Cancer Res. 59, 227-233 (1999).
    • (1999) Cancer Res. , vol.59 , pp. 227-233
    • Putz, T.1    Culig, Z.2    Eder, I.E.3    Nessler-Menardi, C.4    Bartsch, G.5    Grunicke, H.6    Uberall, F.7    Klocker, H.8
  • 139
    • 0032815618 scopus 로고    scopus 로고
    • Radiation-induced activations of the epidermal growth factor receptor and the mitogen activated protein kinase pathway via transforming growth factor a in autocrine-regulated carcinoma cells
    • P. Dent, D. B. Reardon, J. S. Park, G. Bowers, C. Logsdon, K. Valerie and R. K. Schmidt-Ullrich, Radiation-induced activations of the epidermal growth factor receptor and the mitogen activated protein kinase pathway via transforming growth factor a in autocrine-regulated carcinoma cells. Mol. Biol. Cell 10, 2493-2506 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2493-2506
    • Dent, P.1    Reardon, D.B.2    Park, J.S.3    Bowers, G.4    Logsdon, C.5    Valerie, K.6    Schmidt-Ullrich, R.K.7
  • 140
    • 0012254332 scopus 로고    scopus 로고
    • Inhibition of the MAPK pathway radiosensitizes DU145 prostate carcinoma cells
    • M. Hagan and P. Dent, Inhibition of the MAPK pathway radiosensitizes DU145 prostate carcinoma cells. Radiat. Res. 153, 371-381 (2000).
    • (2000) Radiat. Res. , vol.153 , pp. 371-381
    • Hagan, M.1    Dent, P.2
  • 141
    • 0035871383 scopus 로고    scopus 로고
    • Analysis of the transcriptional program induced by Raf in epithelial cells
    • A. Schulze, K. Lehmann, H. B. Jefferies, M. McMahon and J. Downward, Analysis of the transcriptional program induced by Raf in epithelial cells. Genes Dev. 15, 981-994. (2001).
    • (2001) Genes Dev. , vol.15 , pp. 981-994
    • Schulze, A.1    Lehmann, K.2    Jefferies, H.B.3    McMahon, M.4    Downward, J.5
  • 142
    • 0034671497 scopus 로고    scopus 로고
    • Involvement of deregulated epiregulin expression in tumorigenesis in vivo through activated Ki-Ras signaling pathway in human colon cancer cells
    • I. Baba, S. Shirasawa, R. Iwamoto, K. Okumura, T. Tsunoda, M. Nishioka, K. Fukuyama, K. Yamamoto, E. Mekada and T. Sasazuki, Involvement of deregulated epiregulin expression in tumorigenesis in vivo through activated Ki-Ras signaling pathway in human colon cancer cells. Cancer Res. 60, 6886-6889 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 6886-6889
    • Baba, I.1    Shirasawa, S.2    Iwamoto, R.3    Okumura, K.4    Tsunoda, T.5    Nishioka, M.6    Fukuyama, K.7    Yamamoto, K.8    Mekada, E.9    Sasazuki, T.10
  • 145
    • 0036479747 scopus 로고    scopus 로고
    • Roles of ERBB family receptor tyrosine kinases, and downstream signaling pathways, in the control of cell growth and survival
    • S. Grant, L. Qiao and P. Dent, Roles of ERBB family receptor tyrosine kinases, and downstream signaling pathways, in the control of cell growth and survival. Front. Biosci. 7, 376-389 (2002).
    • (2002) Front. Biosci. , vol.7 , pp. 376-389
    • Grant, S.1    Qiao, L.2    Dent, P.3
  • 147
    • 0030013561 scopus 로고    scopus 로고
    • Growth inhibitory concentrations of EGF induce p21 (WAF1/Cip1) and alter cell cycle control in squamous carcinoma cells
    • J. Jakus and W. A. Yeudall, Growth inhibitory concentrations of EGF induce p21 (WAF1/Cip1) and alter cell cycle control in squamous carcinoma cells. Oncogene 12, 2369-2376 (1996).
    • (1996) Oncogene , vol.12 , pp. 2369-2376
    • Jakus, J.1    Yeudall, W.A.2
  • 148
    • 0035951665 scopus 로고    scopus 로고
    • Epidermal growth factor induces Gadd45 (growth arrest and DNA damage inducible protein) expression in A431 cells
    • W. F. Fong, C. H. Leung, W. Lam, N. S. Wong and S. H. Cheng, Epidermal growth factor induces Gadd45 (growth arrest and DNA damage inducible protein) expression in A431 cells. Biochim. Biophys. Acta 1517, 250-256 (2001).
    • (2001) Biochim. Biophys. Acta , vol.1517 , pp. 250-256
    • Fong, W.F.1    Leung, C.H.2    Lam, W.3    Wong, N.S.4    Cheng, S.H.5
  • 149
    • 0034988184 scopus 로고    scopus 로고
    • The epidermal growth factor receptor as a target for cancer therapy
    • J. Mendelsohn, The epidermal growth factor receptor as a target for cancer therapy. Endocr. Relat. Cancer 8, 3-9 (2001).
    • (2001) Endocr. Relat. Cancer , vol.8 , pp. 3-9
    • Mendelsohn, J.1
  • 150
    • 0031759864 scopus 로고    scopus 로고
    • The HER-2/neu oncogene in breast cancer: Prognostic factor, predictive factor, and target for therapy
    • J. S. Ross and J. A. Fletcher, The HER-2/neu oncogene in breast cancer: Prognostic factor, predictive factor, and target for therapy. Stem Cells 16, 413-428 (1998).
    • (1998) Stem Cells , vol.16 , pp. 413-428
    • Ross, J.S.1    Fletcher, J.A.2
  • 151
    • 0035878746 scopus 로고    scopus 로고
    • Growth suppression of intracranial xenografted glioblastomas overexpressing mutant epidermal growth factor receptors by systemic administration of monoclonal antibody (mAb) 806, a novel monoclonal antibody directed to the receptor
    • K. Mishima, T. G. Johns, R. B. Luwor, A. M. Scott, E. Stockert, A. A. Jungbluth, X. D. Ji, P. Suvarna, J. R. Voland and W. K. Cavenee, Growth suppression of intracranial xenografted glioblastomas overexpressing mutant epidermal growth factor receptors by systemic administration of monoclonal antibody (mAb) 806, a novel monoclonal antibody directed to the receptor. Cancer Res. 61, 5349-5354 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 5349-5354
    • Mishima, K.1    Johns, T.G.2    Luwor, R.B.3    Scott, A.M.4    Stockert, E.5    Jungbluth, A.A.6    Ji, X.D.7    Suvarna, P.8    Voland, J.R.9    Cavenee, W.K.10
  • 152
    • 0035863314 scopus 로고    scopus 로고
    • The HER tyrosine kinase inhibitor CI1033 enhances cytotoxicity of 7-ethyl-10-hydroxycamptothecin and topotecan by inhibiting breast cancer resistance protein-mediated drug efflux
    • C. Erlichman, S. A. Boerner, C. G. Hallgren, R. Spieker, X. Y. Wang, C. D. James, G. L. Scheffer, M. Maliepaard, D. D. Ross and S. H. Kaufmann, The HER tyrosine kinase inhibitor CI1033 enhances cytotoxicity of 7-ethyl-10-hydroxycamptothecin and topotecan by inhibiting breast cancer resistance protein-mediated drug efflux. Cancer Res. 61, 739-748 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 739-748
    • Erlichman, C.1    Boerner, S.A.2    Hallgren, C.G.3    Spieker, R.4    Wang, X.Y.5    James, C.D.6    Scheffer, G.L.7    Maliepaard, M.8    Ross, D.D.9    Kaufmann, S.H.10
  • 153
    • 0034212763 scopus 로고    scopus 로고
    • Blockade of the epidermal growth factor receptor signaling by a novel tyrosine kinase inhibitor leads to apoptosis of endothelial cells and therapy of human pancreatic carcinoma
    • C. J. Bruns, C. C. Solorzano, M. T. Harbison, S. Ozawa, R. Tsan, D. Fan, J. Abbruzzese, P. Traxler, E. Buchdunger and I. J. Fidler, Blockade of the epidermal growth factor receptor signaling by a novel tyrosine kinase inhibitor leads to apoptosis of endothelial cells and therapy of human pancreatic carcinoma. Cancer Res. 60, 2926-2935 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 2926-2935
    • Bruns, C.J.1    Solorzano, C.C.2    Harbison, M.T.3    Ozawa, S.4    Tsan, R.5    Fan, D.6    Abbruzzese, J.7    Traxler, P.8    Buchdunger, E.9    Fidler, I.J.10
  • 154
    • 0035879004 scopus 로고    scopus 로고
    • Extremely low-dose ionizing radiation causes activation of mitogen-activated protein kinase pathway and enhances proliferation of normal human diploid cells
    • K. Suzuki, S. Kodama and M. Watanabe, Extremely low-dose ionizing radiation causes activation of mitogen-activated protein kinase pathway and enhances proliferation of normal human diploid cells. Cancer Res. 61, 5396-5401 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 5396-5401
    • Suzuki, K.1    Kodama, S.2    Watanabe, M.3
  • 155
    • 0033601343 scopus 로고    scopus 로고
    • Activation of epidermal growth factor receptor promotes late terminal differentiation of cell-matrix interaction-disrupted keratinocytes
    • H. Wakita and M. Takigawa, Activation of epidermal growth factor receptor promotes late terminal differentiation of cell-matrix interaction-disrupted keratinocytes. J. Biol. Chem. 274, 37285-37291 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 37285-37291
    • Wakita, H.1    Takigawa, M.2
  • 159
    • 0032852374 scopus 로고    scopus 로고
    • ErbB-2 kinase is required for constitutive stat 3 activation in malignant human lung epithelial cells
    • A. Fernandes, A. W. Hamburger and B. I. Gerwin, ErbB-2 kinase is required for constitutive stat 3 activation in malignant human lung epithelial cells. Int. J. Cancer 83, 564-570 (1999).
    • (1999) Int. J. Cancer , vol.83 , pp. 564-570
    • Fernandes, A.1    Hamburger, A.W.2    Gerwin, B.I.3
  • 160
    • 0033545848 scopus 로고    scopus 로고
    • From HER2/Neu signal cascade to androgen receptor and its coactivators: A novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells
    • S. Yeh, H. K. Lin, H. Y. Kang, T. H. Thin, M. F. Lin and C. Chang, From HER2/Neu signal cascade to androgen receptor and its coactivators: A novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells. Proc. Natl. Acad. Sci. USA 96, 5458-5463 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 5458-5463
    • Yeh, S.1    Lin, H.K.2    Kang, H.Y.3    Thin, T.H.4    Lin, M.F.5    Chang, C.6
  • 161
    • 0033584391 scopus 로고    scopus 로고
    • Dominant negative EGFR-CD533 and inhibition of MAPK modify JNK1 activation and enhance radiation toxicity of human mammary carcinoma cells
    • D. B. Reardon, J. N. Contessa, R. B. Mikkelsen, K. Valerie, C. Amir, P. Dent and R. K. Schmidt-Ullrich, Dominant negative EGFR-CD533 and inhibition of MAPK modify JNK1 activation and enhance radiation toxicity of human mammary carcinoma cells. Oncogene 18, 4756-4766 (1999).
    • (1999) Oncogene , vol.18 , pp. 4756-4766
    • Reardon, D.B.1    Contessa, J.N.2    Mikkelsen, R.B.3    Valerie, K.4    Amir, C.5    Dent, P.6    Schmidt-Ullrich, R.K.7
  • 162
    • 0033542381 scopus 로고    scopus 로고
    • Expression of dominant-negative ErbB 2 in the mammary gland of transgenic mice reveals a role in lobuloalveolar development and lactation
    • F. E. Jones and D. F. Stern. Expression of dominant-negative ErbB2 in the mammary gland of transgenic mice reveals a role in lobuloalveolar development and lactation. Oncogene 18, 3481-3490 (1999).
    • (1999) Oncogene , vol.18 , pp. 3481-3490
    • Jones, F.E.1    Stern, D.F.2
  • 163
    • 0034115478 scopus 로고    scopus 로고
    • Blocking HER-2/HER-3 function with a dominant negative form of HER-3 in cells stimulated by heregulin and in breast cancer cells with HER-2 gene amplification
    • T. G. Ram, M. E. Schelling and H. L. Hosick, Blocking HER-2/ HER-3 function with a dominant negative form of HER-3 in cells stimulated by heregulin and in breast cancer cells with HER-2 gene amplification. Cell. Growth. Differ. 11, 173-183 (2000).
    • (2000) Cell Growth Differ. , vol.11 , pp. 173-183
    • Ram, T.G.1    Schelling, M.E.2    Hosick, H.L.3
  • 164
    • 0032740247 scopus 로고    scopus 로고
    • Roles for basal and stimulated p21(Cip-1/WAF1/MDA6) expression and mitogen-activated protein kinase signaling in radiation-induced cell cycle checkpoint control in carcinoma cells
    • J. S. Park, S. Carter, D. B. Reardon, R. K. Schmidt-Ullrich, P. Dent and P. B. Fisher, Roles for basal and stimulated p21(Cip-1/WAF1/MDA6) expression and mitogen-activated protein kinase signaling in radiation-induced cell cycle checkpoint control in carcinoma cells. Mol. Biol. Cell 10, 4231-4246 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 4231-4246
    • Park, J.S.1    Carter, S.2    Reardon, D.B.3    Schmidt-Ullrich, R.K.4    Dent, P.5    Fisher, P.B.6
  • 165
    • 0034722889 scopus 로고    scopus 로고
    • The EGF receptor family as targets for cancer therapy
    • J. Mendelsohn and J. Baselga, The EGF receptor family as targets for cancer therapy. Oncogene 19, 6550-6565 (2000).
    • (2000) Oncogene , vol.19 , pp. 6550-6565
    • Mendelsohn, J.1    Baselga, J.2
  • 167
    • 0036124415 scopus 로고    scopus 로고
    • Epidermal growth factor receptors as a target for cancer treatment: The emerging role of IMC-C225 in the treatment of lung and head and neck cancers
    • R. S. Herbst and C. J. Langer. Epidermal growth factor receptors as a target for cancer treatment: The emerging role of IMC-C225 in the treatment of lung and head and neck cancers. Semin. Oncol. 29, 27-36 (2002).
    • (2002) Semin. Oncol. , vol.29 , pp. 27-36
    • Herbst, R.S.1    Langer, C.J.2
  • 168
    • 0034879275 scopus 로고    scopus 로고
    • Mechanism of action of anti-HER 2 monoclonal antibodies
    • J. Baselga and J. Albanell, Mechanism of action of anti-HER2 monoclonal antibodies. Ann. Oncol. 12, 35-41 (2001).
    • (2001) Ann. Oncol. , vol.12 , pp. 35-41
    • Baselga, J.1    Albanell, J.2
  • 170
    • 0034473393 scopus 로고    scopus 로고
    • Trastuzumab and chemotherapeutics: Drug interactions and synergies
    • M. D. Pegram, A. Lopez, G. Konecny and D. J. Slamon, Trastuzumab and chemotherapeutics: Drug interactions and synergies. Semin. Oncol. 27, 21-25 (2000).
    • (2000) Semin. Oncol. , vol.27 , pp. 21-25
    • Pegram, M.D.1    Lopez, A.2    Konecny, G.3    Slamon, D.J.4
  • 171
    • 0035479052 scopus 로고    scopus 로고
    • C225 antiepidermal growth factor receptor antibody enhances tumor radiocurability
    • S. Nasu, K. K. Ang, Z. Fan and L. Milas, C225 antiepidermal growth factor receptor antibody enhances tumor radiocurability. Int. J. Radiat. Oncol. Biol. Phys. 51, 474-477 (2001).
    • (2001) Int. J. Radiat. Oncol. Biol. Phys. , vol.51 , pp. 474-477
    • Nasu, S.1    Ang, K.K.2    Fan, Z.3    Milas, L.4
  • 173
    • 0035878671 scopus 로고    scopus 로고
    • Monoclonal antibody 806 inhibits the growth of tumor xenografts expressing either the de2-7 or amplified epidermal growth factor receptor (EGFR) but not wild-type EGFR
    • R. B. Luwor, T. G. Johns, C. Murone, H. J. Huang, W. K. Cavenee, G. Ritter, L. J. Old, A. W. Burgess and A. M. Scott, Monoclonal antibody 806 inhibits the growth of tumor xenografts expressing either the de2-7 or amplified epidermal growth factor receptor (EGFR) but not wild-type EGFR. Cancer Res. 61, 5355-5361 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 5355-5361
    • Luwor, R.B.1    Johns, T.G.2    Murone, C.3    Huang, H.J.4    Cavenee, W.K.5    Ritter, G.6    Old, L.J.7    Burgess, A.W.8    Scott, A.M.9
  • 174
    • 0035272930 scopus 로고    scopus 로고
    • The 4-anilinoquinazoline class of inhibitors of the erbB family of receptor tyrosine kinases
    • W. A. Denny, The 4-anilinoquinazoline class of inhibitors of the erbB family of receptor tyrosine kinases. Farmaco 56, 51-56 (2001).
    • (2001) Farmaco , vol.56 , pp. 51-56
    • Denny, W.A.1
  • 175
    • 0032830412 scopus 로고    scopus 로고
    • The rationale and strategy used to develop a series of highly potent, irreversible, inhibitors of the epidermal growth factor receptor family of tyrosine kinases
    • A. J. Bridges, The rationale and strategy used to develop a series of highly potent, irreversible, inhibitors of the epidermal growth factor receptor family of tyrosine kinases. Curr. Med. Chem. 6, 825-843 (1999).
    • (1999) Curr. Med. Chem. , vol.6 , pp. 825-843
    • Bridges, A.J.1
  • 176
    • 0030697807 scopus 로고    scopus 로고
    • PD153035, a tyrosine kinase inhibitor, prevents epidermal growth factor receptor activation and inhibits growth of cancer cells in a receptor number-dependent manner
    • M. Bos, J. Mendelsohn, Y. M. Kim, J. Albanell, D. W. Fry and J. Baselga, PD153035, a tyrosine kinase inhibitor, prevents epidermal growth factor receptor activation and inhibits growth of cancer cells in a receptor number-dependent manner. Clin. Cancer Res. 3, 2099-2106 (1997).
    • (1997) Clin. Cancer Res. , vol.3 , pp. 2099-2106
    • Bos, M.1    Mendelsohn, J.2    Kim, Y.M.3    Albanell, J.4    Fry, D.W.5    Baselga, J.6
  • 178
    • 0030044628 scopus 로고    scopus 로고
    • Enhancement of chemosensitivity by tyrphostin AG825 in high-p185(neu) expressing non-small cell lung cancer cells
    • C. M. Tsai, A. Levitzki, L. H. Wu, K. T. Chang, C. C. Cheng, A. Gazit and R. P. Perng, Enhancement of chemosensitivity by tyrphostin AG825 in high-p185(neu) expressing non-small cell lung cancer cells. Cancer Res. 56, 1068-1074 (1996).
    • (1996) Cancer Res. , vol.56 , pp. 1068-1074
    • Tsai, C.M.1    Levitzki, A.2    Wu, L.H.3    Chang, K.T.4    Cheng, C.C.5    Gazit, A.6    Perng, R.P.7
  • 179
    • 0034565927 scopus 로고    scopus 로고
    • Radiosensitization of human breast cancer cells by a novel ErbB family receptor tyrosine kinase inhibitor
    • G. S. Rao, S. Murray and S. P. Ethier, Radiosensitization of human breast cancer cells by a novel ErbB family receptor tyrosine kinase inhibitor. Int. J. Radiat. Oncol. Biol. Phys. 48, 1519-1528 (2000).
    • (2000) Int. J. Radiat. Oncol. Biol. Phys. , vol.48 , pp. 1519-1528
    • Rao, G.S.1    Murray, S.2    Ethier, S.P.3
  • 180
    • 0035805596 scopus 로고    scopus 로고
    • Akt, MAPK (Erk1/2), and p38 act in concert to promote apoptosis in response to ErbB receptor family inhibition
    • J. M. Nelson and D. W. Fry, Akt, MAPK (Erk1/2), and p38 act in concert to promote apoptosis in response to ErbB receptor family inhibition. J. Biol. Chem. 276, 14842-14847 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 14842-14847
    • Nelson, J.M.1    Fry, D.W.2
  • 181
    • 0034489914 scopus 로고    scopus 로고
    • Efficacy of cytotoxic agents against human tumor xenografts is markedly enhanced by coadministration of ZD1839 (Iressa), an inhibitor of EGFR tyrosine kinase
    • F. M. Sirotnak, M. F. Zakowski, V. A. Miller, H. I. Scher and M. G. Kris, Efficacy of cytotoxic agents against human tumor xenografts is markedly enhanced by coadministration of ZD1839 (Iressa), an inhibitor of EGFR tyrosine kinase. Clin. Cancer Res. 6, 4885-4892 (2000).
    • (2000) Clin. Cancer Res. , vol.6 , pp. 4885-4892
    • Sirotnak, F.M.1    Zakowski, M.F.2    Miller, V.A.3    Scher, H.I.4    Kris, M.G.5
  • 182
    • 0030042135 scopus 로고    scopus 로고
    • Radiation-induced autophosphorylation of epidermal growth factor receptor in human malignant mammary and squamous epithelial cells
    • R. K. Schmidt-Ullrich, K. Valerie, P. B. Fogleman and J. Walters, Radiation-induced autophosphorylation of epidermal growth factor receptor in human malignant mammary and squamous epithelial cells. Radiat. Res. 145, 81-85 (1996).
    • (1996) Radiat. Res. , vol.145 , pp. 81-85
    • Schmidt-Ullrich, R.K.1    Valerie, K.2    Fogleman, P.B.3    Walters, J.4
  • 183
    • 0033049978 scopus 로고    scopus 로고
    • The inducible expression of dominant-negative epidermal growth factor receptor-CD533 results in radiosensitization of human mammary carcinoma cells
    • J. N. Contessa, D. B. Reardon, D. Todd, P. Dent, R. B. Mikkelsen, K. Valerie, G. D. Bowers and R. K. Schmidt-Ullrich, The inducible expression of dominant-negative epidermal growth factor receptor-CD533 results in radiosensitization of human mammary carcinoma cells. Clin. Cancer Res. 5, 405-411 (1999).
    • (1999) Clin. Cancer Res. , vol.5 , pp. 405-411
    • Contessa, J.N.1    Reardon, D.B.2    Todd, D.3    Dent, P.4    Mikkelsen, R.B.5    Valerie, K.6    Bowers, G.D.7    Schmidt-Ullrich, R.K.8
  • 186
    • 0035879822 scopus 로고    scopus 로고
    • Antisense oligonucleotides targeting the epidermal growth factor receptor inhibit proliferation, induce apoptosis, and cooperate with cytotoxic drugs in human cancer cell lines
    • F. Ciardiello, R. Caputo, T. Troiani, G. Borriello, E. R. Kandimalla, S. Agrawal, J. Mendelsohn, A. R. Bianco and G. Tortora, Antisense oligonucleotides targeting the epidermal growth factor receptor inhibit proliferation, induce apoptosis, and cooperate with cytotoxic drugs in human cancer cell lines. Int. J. Cancer 93, 172-178 (2001).
    • (2001) Int. J. Cancer , vol.93 , pp. 172-178
    • Ciardiello, F.1    Caputo, R.2    Troiani, T.3    Borriello, G.4    Kandimalla, E.R.5    Agrawal, S.6    Mendelsohn, J.7    Bianco, A.R.8    Tortora, G.9
  • 187
    • 0036012710 scopus 로고    scopus 로고
    • Altered signaling of TNFα-TNFR1 and SODD/BAG4 is responsible for radioresistance in human HT-R15 cells
    • H. Eichholtz-Wirth and D. Sagan, Altered signaling of TNFα-TNFR1 and SODD/BAG4 is responsible for radioresistance in human HT-R15 cells. Anticancer Res. 22, 235-240 (2002).
    • (2002) Anticancer Res. , vol.22 , pp. 235-240
    • Eichholtz-Wirth, H.1    Sagan, D.2
  • 188
    • 0035931045 scopus 로고    scopus 로고
    • IL-6 a key cytokine in in vitro and in vivo response of Sertoli cells to external gamma irradiation
    • F. Legue, N. Guitton, V. Brouazin-Jousseaume, S. Colleu-Durel, K. Nourgalieva and C. Chenal, IL-6 a key cytokine in in vitro and in vivo response of Sertoli cells to external gamma irradiation. Cytokine 16, 232-238 (2001).
    • (2001) Cytokine , vol.16 , pp. 232-238
    • Legue, F.1    Guitton, N.2    Brouazin-Jousseaume, V.3    Colleu-Durel, S.4    Nourgalieva, K.5    Chenal, C.6
  • 189
    • 0034782160 scopus 로고    scopus 로고
    • Endogenously produced urokinase-type plasminogen activator is a major determinant of the basal level of activated ERK/MAP kinase and prevents apoptosis in MDA-MB-231 breast cancer cells
    • Z. Ma, D. J. Webb, M. Jo and S. L. Gonias, Endogenously produced urokinase-type plasminogen activator is a major determinant of the basal level of activated ERK/MAP kinase and prevents apoptosis in MDA-MB-231 breast cancer cells. J. Cell Sci. 114, 3387-3396 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 3387-3396
    • Ma, Z.1    Webb, D.J.2    Jo, M.3    Gonias, S.L.4
  • 190
    • 0034161938 scopus 로고    scopus 로고
    • Factors underlying the cell growth-related bystander responses to alpha particles
    • R. Iyer and B. E. Lehnert, Factors underlying the cell growth-related bystander responses to alpha particles. Cancer Res. 60, 1290-1298 (2000).
    • (2000) Cancer Res. , vol.60 , pp. 1290-1298
    • Iyer, R.1    Lehnert, B.E.2
  • 191
    • 0035794225 scopus 로고    scopus 로고
    • Combinations of ERK and p38 MAPK inhibitors ablate tumor necrosis factor-alpha (TNF-α) mRNA induction. Evidence for selective destabilization of TNF-α transcripts
    • K. Rutault, C. A. Hazzalin and L. C. Mahadevan, Combinations of ERK and p38 MAPK inhibitors ablate tumor necrosis factor-alpha (TNF-α) mRNA induction. Evidence for selective destabilization of TNF-α transcripts. J. Biol. Chem. 276, 6666-6674 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 6666-6674
    • Rutault, K.1    Hazzalin, C.A.2    Mahadevan, L.C.3
  • 192
    • 0032499572 scopus 로고    scopus 로고
    • The DNA-dependent protein kinase participates in the activation of NFκB following DNA damage
    • S. Basu, K. R. Rosenzweig, M. Youmell and B. D. Price, The DNA-dependent protein kinase participates in the activation of NFκB following DNA damage. Biochem. Biophys. Res. Commun. 247, 79-83 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.247 , pp. 79-83
    • Basu, S.1    Rosenzweig, K.R.2    Youmell, M.3    Price, B.D.4
  • 194
    • 0033988528 scopus 로고    scopus 로고
    • Interleukin-6 activates phosphatidylinositol-3 kinase, which inhibits apoptosis in human prostate cancer cell lines
    • T. D. Chung, J. J. Yu, T. A. Kong, M. T. Spiotto and J. M. Lin, Interleukin-6 activates phosphatidylinositol-3 kinase, which inhibits apoptosis in human prostate cancer cell lines. Prostate 42, 1-7 (2000).
    • (2000) Prostate , vol.42 , pp. 1-7
    • Chung, T.D.1    Yu, J.J.2    Kong, T.A.3    Spiotto, M.T.4    Lin, J.M.5
  • 195
    • 0034743275 scopus 로고    scopus 로고
    • Effects of NF-κB1 (p50) targeted gene disruption on ionizing radiation-induced NF-κB activation and TNFα, IL-1α, IL-1B and IL-6 mRNA expression in vivo
    • D. Zhou, T. Yu, G. Chen, S. A. Brown, Z. Yu, M. P. Mattson and J. S. Thompson, Effects of NF-κB1 (p50) targeted gene disruption on ionizing radiation-induced NF-κB activation and TNFα, IL-1α, IL-1B and IL-6 mRNA expression in vivo. Int. J. Radiat. Biol. 77, 763-772 (2001).
    • (2001) Int. J. Radiat. Biol. , vol.77 , pp. 763-772
    • Zhou, D.1    Yu, T.2    Chen, G.3    Brown, S.A.4    Yu, Z.5    Mattson, M.P.6    Thompson, J.S.7
  • 196
    • 0035197082 scopus 로고    scopus 로고
    • Cardioprotective effects of transforming growth factor-betal during early reoxygenation or reperfusion are mediated by p42/p44 MAPK
    • G. F. Baxter, M. M. Mocanu, B. K. Brar, D. S. Latchman and D. M. Yellon, Cardioprotective effects of transforming growth factor-betal during early reoxygenation or reperfusion are mediated by p42/p44 MAPK. J. Cardiovasc. Pharmacol. 38, 930-939 (2001).
    • (2001) J. Cardiovasc. Pharmacol. , vol.38 , pp. 930-939
    • Baxter, G.F.1    Mocanu, M.M.2    Brar, B.K.3    Latchman, D.S.4    Yellon, D.M.5
  • 198
    • 0033517782 scopus 로고    scopus 로고
    • Heparin binding epidermal growth factor-like growth factor is a transforming growth factor beta-regulated gene in intestinal epithelial cells
    • N. Bulus and J. A. Barnard, Heparin binding epidermal growth factor-like growth factor is a transforming growth factor beta-regulated gene in intestinal epithelial cells. Biochem. Biophys. Res. Commun. 264, 808-812 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.264 , pp. 808-812
    • Bulus, N.1    Barnard, J.A.2
  • 199
    • 0034741661 scopus 로고    scopus 로고
    • The bcl, NFκB and p53/p21WAF1 systems are involved in spontaneous apoptosis and in the anti-apoptotic effect of TGF-β or TNF-α on activated hepatic stellate cells
    • B. Saile, N. Matthes, E. Armouche, K. Neubauer and G. Ramadori, The bcl, NFκB and p53/p21WAF1 systems are involved in spontaneous apoptosis and in the anti-apoptotic effect of TGF-β or TNF-α on activated hepatic stellate cells. Eur. J. Cell Biol. 80, 554-561 (2001).
    • (2001) Eur. J. Cell Biol. , vol.80 , pp. 554-561
    • Saile, B.1    Matthes, N.2    Armouche, E.3    Neubauer, K.4    Ramadori, G.5
  • 200
    • 0034666839 scopus 로고    scopus 로고
    • Raf induces TGFβ production while blocking its apoptotic but not invasive responses: A mechanism leading to increased malignancy in epithelial cells
    • K. Lehmann, E. Janda, C. E. Pierreux, M. Rytomaa, A. Schulze, M. McMahon, C. S. Hill, H. Beug and J. Downward, Raf induces TGFβ production while blocking its apoptotic but not invasive responses: a mechanism leading to increased malignancy in epithelial cells. Genes Dev. 14, 2610-2622 (2000).
    • (2000) Genes Dev. , vol.14 , pp. 2610-2622
    • Lehmann, K.1    Janda, E.2    Pierreux, C.E.3    Rytomaa, M.4    Schulze, A.5    McMahon, M.6    Hill, C.S.7    Beug, H.8    Downward, J.9
  • 201
    • 0032532206 scopus 로고    scopus 로고
    • Suppression of transforming growth factor-beta-induced apoptosis through a phosphatidylinositol 3-kinase/Akt-dependent pathway
    • R. H. Chen, Y. H. Su, R. L. Chuang and T. Y. Chang, Suppression of transforming growth factor-beta-induced apoptosis through a phosphatidylinositol 3-kinase/Akt-dependent pathway. Oncogene 17, 1959-1968 (1998).
    • (1998) Oncogene , vol.17 , pp. 1959-1968
    • Chen, R.H.1    Su, Y.H.2    Chuang, R.L.3    Chang, T.Y.4
  • 202
    • 0035799531 scopus 로고    scopus 로고
    • Constitutive activation of Stat3 by the Src and JAK tyrosine kinases participates in growth regulation of human breast carcinoma cells
    • R. Garcia, T. L. Bowman, G. Niu, H. Yu, S. Minton, C. A. MuroCacho, C. E. Cox, R. Falcone, R. Fairclough and R. Jove, Constitutive activation of Stat3 by the Src and JAK tyrosine kinases participates in growth regulation of human breast carcinoma cells. Oncogene 20, 2499-2513 (2001).
    • (2001) Oncogene , vol.20 , pp. 2499-2513
    • Garcia, R.1    Bowman, T.L.2    Niu, G.3    Yu, H.4    Minton, S.5    MuroCacho, C.A.6    Cox, C.E.7    Falcone, R.8    Fairclough, R.9    Jove, R.10
  • 203
    • 0034935815 scopus 로고    scopus 로고
    • Involvement of JNK-mediated pathway in EGF-mediated protection against paclitaxel-induced apoptosis in SiHa human cervical cancer cells
    • B. Liu, M. Fang, Y. Lu, Y. Lu, G. B. Mills and Z. Fan, Involvement of JNK-mediated pathway in EGF-mediated protection against paclitaxel-induced apoptosis in SiHa human cervical cancer cells. Br. J. Cancer 85, 303-311 (2001).
    • (2001) Br. J. Cancer , vol.85 , pp. 303-311
    • Liu, B.1    Fang, M.2    Lu, Y.3    Lu, Y.4    Mills, G.B.5    Fan, Z.6
  • 204
    • 0036238817 scopus 로고    scopus 로고
    • The Raf/MEK/ERK signal transduction cascade as a target for chemotherapeutic intervention in leukemia
    • J. T. Lee and J. A. McCubrey, The Raf/MEK/ERK signal transduction cascade as a target for chemotherapeutic intervention in leukemia. Leukemia 16, 486-507 (2002).
    • (2002) Leukemia , vol.16 , pp. 486-507
    • Lee, J.T.1    McCubrey, J.A.2
  • 205
    • 0032877668 scopus 로고    scopus 로고
    • Dysregulation of apoptosis in cancer
    • J. C. Reed, Dysregulation of apoptosis in cancer. J. Clin. Oncol. 17, 2941-2953 (1999).
    • (1999) J. Clin. Oncol. , vol.17 , pp. 2941-2953
    • Reed, J.C.1
  • 206
    • 0035167269 scopus 로고    scopus 로고
    • Deoxycholic acid (DCA) causes ligand-independent activation of epidermal growth factor receptor (EGFR) and FAS receptor in primary hepatocytes: Inhibition of EGFR/mitogen-activated protein kinase-signaling module enhances DCA-induced apoptosis
    • L. Qiao, E. Studer, K. Leach, R. McKinstry, S. Gupta, R. Decker, R. Kukreja, K. Valerie, P. Nagarkatti and P. Dent, Deoxycholic acid (DCA) causes ligand-independent activation of epidermal growth factor receptor (EGFR) and FAS receptor in primary hepatocytes: Inhibition of EGFR/mitogen-activated protein kinase-signaling module enhances DCA-induced apoptosis. Mol. Biol. Cell 12, 2629-2645 (2001).
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2629-2645
    • Qiao, L.1    Studer, E.2    Leach, K.3    McKinstry, R.4    Gupta, S.5    Decker, R.6    Kukreja, R.7    Valerie, K.8    Nagarkatti, P.9    Dent, P.10
  • 207
    • 0037142620 scopus 로고    scopus 로고
    • Stimulation of the mitogen-activated protein kinase pathway antagonizes TRAIL-induced apoptosis downstream of BID cleavage in human breast cancer MCF-7 cells
    • M. Sarker, C. Ruiz-Ruiz, G. Robledo and A. Lopez-Rivas, Stimulation of the mitogen-activated protein kinase pathway antagonizes TRAIL-induced apoptosis downstream of BID cleavage in human breast cancer MCF-7 cells. Oncogene 21, 4323-4327 (2002).
    • (2002) Oncogene , vol.21 , pp. 4323-4327
    • Sarker, M.1    Ruiz-Ruiz, C.2    Robledo, G.3    Lopez-Rivas, A.4
  • 208
    • 0037178881 scopus 로고    scopus 로고
    • Relief of extrinsic pathway inhibition by the bid-dependent mitochondrial release of Smac in Fas-mediated hepatocyte apoptosis
    • S. Li, Y. Zhao, X. He, T. H. Kim, D. K. Kuharsky, H. Rabinowich, J. Chen, C. Du and X. M. Yin, Relief of extrinsic pathway inhibition by the bid-dependent mitochondrial release of Smac in Fas-mediated hepatocyte apoptosis. J. Biol. Chem. 277, 26912-26920 (2002)
    • (2002) J. Biol. Chem. , vol.277 , pp. 26912-26920
    • Li, S.1    Zhao, Y.2    He, X.3    Kim, T.H.4    Kuharsky, D.K.5    Rabinowich, H.6    Chen, J.7    Du, C.8    Yin, X.M.9
  • 209
    • 0034630167 scopus 로고    scopus 로고
    • Induction of apoptosis by cancer chemotherapy
    • S. H. Kaufmann and W. C. Earnshaw, Induction of apoptosis by cancer chemotherapy. Exp. Cell Res. 256, 42-49 (2000).
    • (2000) Exp. Cell Res. , vol.256 , pp. 42-49
    • Kaufmann, S.H.1    Earnshaw, W.C.2
  • 210
    • 0036604448 scopus 로고    scopus 로고
    • Contribution of death receptor and mitochondrial pathways to Fas-mediated apoptosis in the prostatic carcinoma cell line PC3
    • N. V. Guseva, A. F. Taghiyev, O. W. Rokhlin and M. B. Cohen, Contribution of death receptor and mitochondrial pathways to Fas-mediated apoptosis in the prostatic carcinoma cell line PC3. Prostate 51, 231-240 (2002).
    • (2002) Prostate , vol.51 , pp. 231-240
    • Guseva, N.V.1    Taghiyev, A.F.2    Rokhlin, O.W.3    Cohen, M.B.4
  • 211
    • 0037071388 scopus 로고    scopus 로고
    • Dysregulation of apoptosis genes in hematopoietic malignancies
    • S. Kitada, I. M. Pedersen, A. D. Schimmer and J. C. Reed, Dysregulation of apoptosis genes in hematopoietic malignancies. Oncogene 21, 3459-3474 (2002).
    • (2002) Oncogene , vol.21 , pp. 3459-3474
    • Kitada, S.1    Pedersen, I.M.2    Schimmer, A.D.3    Reed, J.C.4
  • 212
    • 0036088471 scopus 로고    scopus 로고
    • Apoptosis: IAP proteins: Blocking the road to death's door
    • G. S. Salvesen and C. S. Duckett, Apoptosis: IAP proteins: Blocking the road to death's door. Nat. Rev. Mol. Cell Biol. 6, 401-410 (2002).
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 401-410
    • Salvesen, G.S.1    Duckett, C.S.2
  • 213
    • 0035418622 scopus 로고    scopus 로고
    • Activated extracellular signal-regulated kinases: Association with epidermal growth factor receptor/transforming growth factor alpha expression in head and neck squamous carcinoma and inhibition by anti-epidermal growth factor receptor treatments
    • J. Albanell, J. Codony-Servat, F. Rojo, J. M. Del Campo, S. Sauleda, J. Anido, G. Raspall, J. Giralt, J. Rosello and J. Baselga, Activated extracellular signal-regulated kinases: Association with epidermal growth factor receptor/transforming growth factor alpha expression in head and neck squamous carcinoma and inhibition by anti-epidermal growth factor receptor treatments. Cancer Res. 61, 6500-6510 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 6500-6510
    • Albanell, J.1    Codony-Servat, J.2    Rojo, F.3    Del Campo, J.M.4    Sauleda, S.5    Anido, J.6    Raspall, G.7    Giralt, J.8    Rosello, J.9    Baselga, J.10
  • 214
    • 0034814931 scopus 로고    scopus 로고
    • Increased in vitro activation of EGFR by membrane-bound TGF-α from gastric and colonic mucosa of aged rats
    • Z. Q. Xiao and A. P. Majumdar, Increased in vitro activation of EGFR by membrane-bound TGF-α from gastric and colonic mucosa of aged rats. Am. J. Physiol. Gastrointest. Liver Physiol. 281, G111-G116 (2001).
    • (2001) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.281
    • Xiao, Z.Q.1    Majumdar, A.P.2
  • 215
    • 0034677776 scopus 로고    scopus 로고
    • HER-2/neu blocks tumor necrosis factor-induced apoptosis via the Akt/NF-κB pathway
    • B. P. Zhou, M. C. Hu, S. A. Miller, Z. Yu, W. Xia, S. Y. Lin and M. C. Hung, HER-2/neu blocks tumor necrosis factor-induced apoptosis via the Akt/NF-κB pathway. J. Biol. Chem. 275, 8027-8031 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 8027-8031
    • Zhou, B.P.1    Hu, M.C.2    Miller, S.A.3    Yu, Z.4    Xia, W.5    Lin, S.Y.6    Hung, M.C.7
  • 216
    • 0034708598 scopus 로고    scopus 로고
    • A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis
    • V. Kainulainen, M. Sundvall, J. A. Maatta, E. Santiestevan, M. Klagsbrun and K. Elenius, A natural ErbB4 isoform that does not activate phosphoinositide 3-kinase mediates proliferation but not survival or chemotaxis. J. Biol. Chem. 27, 8641-8649 (2000).
    • (2000) J. Biol. Chem. , vol.27 , pp. 8641-8649
    • Kainulainen, V.1    Sundvall, M.2    Maatta, J.A.3    Santiestevan, E.4    Klagsbrun, M.5    Elenius, K.6
  • 217
    • 0033542379 scopus 로고    scopus 로고
    • NDF/heregulin-induced cell cycle changes and apoptosis in breast tumour cells: Role of PI3 kinase and p38 MAP kinase pathways
    • J. M. Daly, M. A. Olayioye, A. M. Wong, R. Neve, H. A. Lane, F. G. Maurer and N. E. Hynes, NDF/heregulin-induced cell cycle changes and apoptosis in breast tumour cells: Role of PI3 kinase and p38 MAP kinase pathways. Oncogene 18, 3440-3451 (1999).
    • (1999) Oncogene , vol.18 , pp. 3440-3451
    • Daly, J.M.1    Olayioye, M.A.2    Wong, A.M.3    Neve, R.4    Lane, H.A.5    Maurer, F.G.6    Hynes, N.E.7
  • 218
    • 0032970003 scopus 로고    scopus 로고
    • Role of PI3-kinase in Bcl-X induction and apoptosis inhibition mediated by IL-3 or IGF-1 in Baf-3 cells
    • Y. Leverrier, J. Thomas, A. L. Mathieu, W. Low, B. Blanquier and J. Marvel, Role of PI3-kinase in Bcl-X induction and apoptosis inhibition mediated by IL-3 or IGF-1 in Baf-3 cells. Cell Death Differ. 6, 290-296 (1999).
    • (1999) Cell Death Differ. , vol.6 , pp. 290-296
    • Leverrier, Y.1    Thomas, J.2    Mathieu, A.L.3    Low, W.4    Blanquier, B.5    Marvel, J.6
  • 219
    • 0035825596 scopus 로고    scopus 로고
    • The involvement of PI 3-K/Akt-dependent up-regulation of Mcl-1 in the prevention of apoptosis of Hep3B cells by interleukin-6
    • M. L. Kuo, S. E. Chuang, M. T. Lin and S. Y. Yang, The involvement of PI 3-K/Akt-dependent up-regulation of Mcl-1 in the prevention of apoptosis of Hep3B cells by interleukin-6. Oncogene 20, 677-685 (2001).
    • (2001) Oncogene , vol.20 , pp. 677-685
    • Kuo, M.L.1    Chuang, S.E.2    Lin, M.T.3    Yang, S.Y.4
  • 220
    • 0035831556 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase/Akt activity regulates c-FLIP expression in tumor cells
    • D. J. Panka, T. Mano, T. Suhara, K. Walsh and J. W. Mier, Phosphatidylinositol 3-kinase/Akt activity regulates c-FLIP expression in tumor cells. J. Biol. Chem. 276, 6893-6896 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 6893-6896
    • Panka, D.J.1    Mano, T.2    Suhara, T.3    Walsh, K.4    Mier, J.W.5
  • 221
    • 0035816727 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase/Akt signaling controls endothelial cell sensitivity to Fas-mediated apoptosis via regulation of FLICE-inhibitory protein (FLIP)
    • T. Suhara, T. Mano, B. E. Oliveira and K. Walsh, Phosphatidylinositol 3-kinase/Akt signaling controls endothelial cell sensitivity to Fas-mediated apoptosis via regulation of FLICE-inhibitory protein (FLIP). Circ. Res. 89, 13-19 (2001).
    • (2001) Circ. Res. , vol.89 , pp. 13-19
    • Suhara, T.1    Mano, T.2    Oliveira, B.E.3    Walsh, K.4
  • 224
    • 0035868342 scopus 로고    scopus 로고
    • Her-2/neu overexpression induces NF-κB via a PI3-kinase/Akt pathway involving calpain-mediated degradation of IκB-alpha that can be inhibited by the tumor suppressor PTEN
    • S. Pianetti, M. Arsura, R. Romieu-Mourez, R. J. Coffey and G. E. Sonenshein, Her-2/neu overexpression induces NF-κB via a PI3-kinase/Akt pathway involving calpain-mediated degradation of IκB-alpha that can be inhibited by the tumor suppressor PTEN. Oncogene 20, 1287-1299 (2001).
    • (2001) Oncogene , vol.20 , pp. 1287-1299
    • Pianetti, S.1    Arsura, M.2    Romieu-Mourez, R.3    Coffey, R.J.4    Sonenshein, G.E.5
  • 225
    • 0035874898 scopus 로고    scopus 로고
    • Down-regulation of the erbB-2 receptor by trastuzumab (herceptin) enhances tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis in breast and ovarian cancer cell lines that overexpress erbB-2
    • M. Cuello, S. A. Ettenberg, A. S. Clark, M. M. Keane, R. H. Posner, M. M. Nau, P. A. Dennis and S. Lipkowitz, Down-regulation of the erbB-2 receptor by trastuzumab (herceptin) enhances tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis in breast and ovarian cancer cell lines that overexpress erbB-2. Cancer Res. 61, 4892-4900 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 4892-4900
    • Cuello, M.1    Ettenberg, S.A.2    Clark, A.S.3    Keane, M.M.4    Posner, R.H.5    Nau, M.M.6    Dennis, P.A.7    Lipkowitz, S.8
  • 228
    • 0033932013 scopus 로고    scopus 로고
    • RAS-mediated radiation resistance is not linked to MAP kinase activation in two bladder carcinoma cell lines
    • A. K. Gupta, E. J. Bernhard, V. J. Bakanauskas, J. Wu, R. J. Muschel and W. G. McKenna, RAS-mediated radiation resistance is not linked to MAP kinase activation in two bladder carcinoma cell lines. Radiat. Res. 154, 64-72 (2000).
    • (2000) Radiat. Res. , vol.154 , pp. 64-72
    • Gupta, A.K.1    Bernhard, E.J.2    Bakanauskas, V.J.3    Wu, J.4    Muschel, R.J.5    McKenna, W.G.6
  • 229
    • 0033613944 scopus 로고    scopus 로고
    • 2/M checkpoint arrest in cells exposed to ionizing radiation
    • 2/M checkpoint arrest in cells exposed to ionizing radiation. J. Biol. Chem. 274, 2732-2742 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 2732-2742
    • Abbott, D.W.1    Holt, J.T.2
  • 231
    • 0029661835 scopus 로고    scopus 로고
    • 2 phase after 2 Gy gamma irradiation is faster in radiosensitive human cells with high expression of the RAF1 proto-oncogene
    • 2 phase after 2 Gy gamma irradiation is faster in radiosensitive human cells with high expression of the RAF1 proto-oncogene. Radiat. Res. 146, 485-493 (1996).
    • (1996) Radiat. Res. , vol.146 , pp. 485-493
    • Warenius, H.M.1    Jones, M.D.2    Thompson, C.C.3
  • 232
    • 0037023780 scopus 로고    scopus 로고
    • Fibroblast growth factor-2 induces translational regulation of Bcl-XL and Bcl-2 via a MEK-dependent pathway: Correlation with resistance to etoposide-induced apoptosis
    • O. E. Pardo, A. Arcaro, G. Salerno, S. Raguz, J. Downward and M. J. Seckl, Fibroblast growth factor-2 induces translational regulation of Bcl-XL and Bcl-2 via a MEK-dependent pathway: Correlation with resistance to etoposide-induced apoptosis. J. Biol. Chem. 277, 12040-12046 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 12040-12046
    • Pardo, O.E.1    Arcaro, A.2    Salerno, G.3    Raguz, S.4    Downward, J.5    Seckl, M.J.6
  • 233
    • 0037066686 scopus 로고    scopus 로고
    • ERK activation mediates cell cycle arrest and apoptosis after DNA damage independently of p53
    • D. Tang, D. Wu, A. Hirao, J. M. Lahti, L. Liu, B. Mazza, V. J. Kidd, T. W. Mak and A. J. Ingram, ERK activation mediates cell cycle arrest and apoptosis after DNA damage independently of p53. J. Biol. Chem. 277, 12710-12717 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 12710-12717
    • Tang, D.1    Wu, D.2    Hirao, A.3    Lahti, J.M.4    Liu, L.5    Mazza, B.6    Kidd, V.J.7    Mak, T.W.8    Ingram, A.J.9
  • 234
    • 0037016706 scopus 로고    scopus 로고
    • Activation of extracellular signal-regulated kinase by ultraviolet is mediated through Src-dependent epidermal growth factor receptor phosphorylation. Its implication in an anti-apoptotic function
    • D. Kitagawa, S. Tanemura, S. Ohata, N. Shimizu, J. Seo, G. Nishitai, T. Watanabe, K. Nakagawa, H. Kishimoto and T. Katada, Activation of extracellular signal-regulated kinase by ultraviolet is mediated through Src-dependent epidermal growth factor receptor phosphorylation. Its implication in an anti-apoptotic function. J. Biol. Chem. 277, 366-371 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 366-371
    • Kitagawa, D.1    Tanemura, S.2    Ohata, S.3    Shimizu, N.4    Seo, J.5    Nishitai, G.6    Watanabe, T.7    Nakagawa, K.8    Kishimoto, H.9    Katada, T.10
  • 235
    • 0035794191 scopus 로고    scopus 로고
    • Epidermal growth factor receptor-dependent control of keratinocyte survival and Bcl-xL expression through a MEK-dependent pathway
    • M. Jost, T. M. Huggett, C. Kari, L. H. Boise and U. Rodeck, Epidermal growth factor receptor-dependent control of keratinocyte survival and Bcl-xL expression through a MEK-dependent pathway. J. Biol. Chem. 276, 6320-6326 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 6320-6326
    • Jost, M.1    Huggett, T.M.2    Kari, C.3    Boise, L.H.4    Rodeck, U.5
  • 236
    • 0034618369 scopus 로고    scopus 로고
    • MEK/ERK signaling pathway regulates the expression of Bcl-2, Bcl-XL, and Mcl-1 and promotes survival of human pancreatic cancer cells
    • M. J. Boucher, J. Morisset, P. H. Vachon, J. C. Reed, J. Laine and N. Rivard, MEK/ERK signaling pathway regulates the expression of Bcl-2, Bcl-XL, and Mcl-1 and promotes survival of human pancreatic cancer cells. J. Cell. Biochem. 79, 355-369 (2000).
    • (2000) J. Cell. Biochem. , vol.79 , pp. 355-369
    • Boucher, M.J.1    Morisset, J.2    Vachon, P.H.3    Reed, J.C.4    Laine, J.5    Rivard, N.6
  • 237
    • 0035809182 scopus 로고    scopus 로고
    • Matrix attachment regulates Fas-induced apoptosis in endothelial cells: A role for c-flip and implications for anoikis
    • F. Aoudjit and K. Vuori, Matrix attachment regulates Fas-induced apoptosis in endothelial cells: A role for c-flip and implications for anoikis. J. Cell. Biol. 152, 633-643 (2001).
    • (2001) J. Cell. Biol. , vol.152 , pp. 633-643
    • Aoudjit, F.1    Vuori, K.2
  • 238
    • 0034769605 scopus 로고    scopus 로고
    • MAPK dependence of DNA damage repair: Ionizing radiation and the induction of expression of the DNA repair genes XRCC1 and ERCC1 in DU145 human prostate carcinoma cells in a MEK1/2 dependent fashion
    • A. Yacoub, J. S. Park, L. Qiao, P. Dent and M. P. Hagan, MAPK dependence of DNA damage repair: Ionizing radiation and the induction of expression of the DNA repair genes XRCC1 and ERCC1 in DU145 human prostate carcinoma cells in a MEK1/2 dependent fashion. Int. J. Radiat. Biol. 77, 1067-1078 (2001).
    • (2001) Int. J. Radiat. Biol. , vol.77 , pp. 1067-1078
    • Yacoub, A.1    Park, J.S.2    Qiao, L.3    Dent, P.4    Hagan, M.P.5
  • 239
    • 0033579301 scopus 로고    scopus 로고
    • Mediation by a CREB family transcription factor of NGF-dependent survival of sympathetic neurons
    • A. Riccio, S. Ahn, C. M. Davenport, J. A. Blendy and D. D. Ginty, Mediation by a CREB family transcription factor of NGF-dependent survival of sympathetic neurons. Science 286, 2358-2361 (1999).
    • (1999) Science , vol.286 , pp. 2358-2361
    • Riccio, A.1    Ahn, S.2    Davenport, C.M.3    Blendy, J.A.4    Ginty, D.D.5
  • 240
    • 0032514734 scopus 로고    scopus 로고
    • Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene
    • D. De Cesare, S. Jacquot, A. Hanauer and P. Sassone-Corsi, Rsk-2 activity is necessary for epidermal growth factor-induced phosphorylation of CREB protein and transcription of c-fos gene. Proc. Natl. Acad. Sci. USA 95, 12202-12207 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12202-12207
    • De Cesare, D.1    Jacquot, S.2    Hanauer, A.3    Sassone-Corsi, P.4
  • 241
    • 0032793067 scopus 로고    scopus 로고
    • B-Raf inhibits programmed cell death downstream of cytochrome c release from mitochondria by activating the MEK/Erk pathway
    • P. Erhardt, E. J. Schremser and G. M. Cooper, B-Raf inhibits programmed cell death downstream of cytochrome c release from mitochondria by activating the MEK/Erk pathway. Mol. Cell. Biol. 19, 5308-5315 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 5308-5315
    • Erhardt, P.1    Schremser, E.J.2    Cooper, G.M.3
  • 243
    • 0036606332 scopus 로고    scopus 로고
    • Degradation of HER2 by ansamycins induces growth arrest and apoptosis in cells with HER2 overexpression via a HER3, phosphatidylinositol 3′-kinase-AKT-dependent pathway
    • P. N. Munster, D. C. Marchion, A. D. Basso and N. Rosen, Degradation of HER2 by ansamycins induces growth arrest and apoptosis in cells with HER2 overexpression via a HER3, phosphatidylinositol 3′-kinase-AKT-dependent pathway. Cancer Res. 62, 3132-3137 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 3132-3137
    • Munster, P.N.1    Marchion, D.C.2    Basso, A.D.3    Rosen, N.4
  • 244
    • 0034788759 scopus 로고    scopus 로고
    • NF-κB signaling pathway as a target for human tumor radiosensitization
    • M. Jung and A. Dritschilo, NF-κB signaling pathway as a target for human tumor radiosensitization. Semin. Radiat. Oncol. 11, 346-351 (2001).
    • (2001) Semin. Radiat. Oncol. , vol.11 , pp. 346-351
    • Jung, M.1    Dritschilo, A.2
  • 245
    • 0037089516 scopus 로고    scopus 로고
    • Inhibition of radiation-induced nuclear factor-κB activation by an anti-Ras single-chain antibody fragment: Lack of involvement in radiosensitization
    • J. S. Russell, U. Raju, G. J. Gumin, F. F. Lang, D. R. Wilson, T. Huet and P. J. Tofilon, Inhibition of radiation-induced nuclear factor-κB activation by an anti-Ras single-chain antibody fragment: Lack of involvement in radiosensitization. Cancer Res. 62, 2318-2326 (2002).
    • (2002) Cancer Res. , vol.62 , pp. 2318-2326
    • Russell, J.S.1    Raju, U.2    Gumin, G.J.3    Lang, F.F.4    Wilson, D.R.5    Huet, T.6    Tofilon, P.J.7
  • 246
    • 85047699031 scopus 로고    scopus 로고
    • Identification of signal transduction pathways involved in constitutive NF-κB activation in breast cancer cells
    • P. Bhat-Nakshatri, C. J. Sweeney and H. Nakshatri, Identification of signal transduction pathways involved in constitutive NF-κB activation in breast cancer cells. Oncogene 21, 2066-2078 (2002).
    • (2002) Oncogene , vol.21 , pp. 2066-2078
    • Bhat-Nakshatri, P.1    Sweeney, C.J.2    Nakshatri, H.3
  • 247
    • 0032514363 scopus 로고    scopus 로고
    • Activation of NF-κB by oncogenic Raf in HEK 293 cells occurs through autocrine recruitment of the stress kinase cascade
    • J. Troppmair, J. Hartkamp and U. R. Rapp, Activation of NF-κB by oncogenic Raf in HEK 293 cells occurs through autocrine recruitment of the stress kinase cascade. Oncogene 17, 685-690 (1998).
    • (1998) Oncogene , vol.17 , pp. 685-690
    • Troppmair, J.1    Hartkamp, J.2    Rapp, U.R.3
  • 248
    • 0033561678 scopus 로고    scopus 로고
    • Extracellular-regulated kinase 1/2, Jun N-terminal kinase, and c-Jun are involved in NF-κB-dependent IL-6 expression in human monocytes
    • L. M. Tuyt, W. H. Dokter, K. Birkenkamp, S. B. Koopmans, C. Lummen, W. Kruijer and E. Vellenga, Extracellular-regulated kinase 1/2, Jun N-terminal kinase, and c-Jun are involved in NF-κB-dependent IL-6 expression in human monocytes. J. Immunol. 162, 4893-4902 (1999).
    • (1999) J. Immunol. , vol.162 , pp. 4893-4902
    • Tuyt, L.M.1    Dokter, W.H.2    Birkenkamp, K.3    Koopmans, S.B.4    Lummen, C.5    Kruijer, W.6    Vellenga, E.7
  • 249
    • 0033570912 scopus 로고    scopus 로고
    • The down regulation of the pro-apoptotic protein Par-4 is critical for Ras-induced survival and tumor progression
    • M. Barradas, A. Monjas, M. T. Diaz-Meco, M. Serrano and J. Moscat, The down regulation of the pro-apoptotic protein Par-4 is critical for Ras-induced survival and tumor progression. EMBO J. 18, 6362-6369 (1999).
    • (1999) EMBO J. , vol.18 , pp. 6362-6369
    • Barradas, M.1    Monjas, A.2    Diaz-Meco, M.T.3    Serrano, M.4    Moscat, J.5
  • 250
    • 0033604464 scopus 로고    scopus 로고
    • Negative regulation of Par-4 by oncogenic Ras is essential for cellular transformation
    • S. G. Qiu, N. El-Guendy, S. Krishnan and V. M. Rangnekar, Negative regulation of Par-4 by oncogenic Ras is essential for cellular transformation. Oncogene 18, 7115-7123 (1999).
    • (1999) Oncogene , vol.18 , pp. 7115-7123
    • Qiu, S.G.1    El-Guendy, N.2    Krishnan, S.3    Rangnekar, V.M.4
  • 251
    • 0034661739 scopus 로고    scopus 로고
    • Pro-apoptotic action of PAR-4 involves inhibition of NF-κB activity and suppression of BCL-2 expression
    • S. Camandola and M. P. Mattson, Pro-apoptotic action of PAR-4 involves inhibition of NF-κB activity and suppression of BCL-2 expression. J. Neurosci. Res. 61, 134-139 (2000).
    • (2000) J. Neurosci. Res. , vol.61 , pp. 134-139
    • Camandola, S.1    Mattson, M.P.2
  • 252
    • 0033538336 scopus 로고    scopus 로고
    • Inactivation of the inhibitory κB protein kinase/nuclear factor κB pathway by Par-4 expression potentiates tumor necrosis factor alpha-induced apoptosis
    • M. T. Diaz-Meco, M. J. Lallena, A. Monjas, S. Frutos and J. Moscat, Inactivation of the inhibitory κB protein kinase/nuclear factor κB pathway by Par-4 expression potentiates tumor necrosis factor alpha-induced apoptosis. J. Biol. Chem. 274, 19606-19612 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 19606-19612
    • Diaz-Meco, M.T.1    Lallena, M.J.2    Monjas, A.3    Frutos, S.4    Moscat, J.5
  • 253
    • 0033081893 scopus 로고    scopus 로고
    • Atypical PKC zeta is activated by ceramide, resulting in coactivation of NF-κB/JNK kinase and cell survival
    • Y. M. Wang, M. L. Seibenhener, M. L. Vandenplas and M. W. Wooten, Atypical PKC zeta is activated by ceramide, resulting in coactivation of NF-κB/JNK kinase and cell survival. J. Neurosci. Res. 55, 293-302 (1999).
    • (1999) J. Neurosci. Res. , vol.55 , pp. 293-302
    • Wang, Y.M.1    Seibenhener, M.L.2    Vandenplas, M.L.3    Wooten, M.W.4
  • 254
    • 0036491706 scopus 로고    scopus 로고
    • Par-4, A pro-apoptotic gene, inhibits radiation-induced NFkB activity and Bcl-2 expression leading to induction of radiosensitivity in human prostate cancer cells PC-3
    • D. Chendil, A. Das, S. Dey, M. Mohiuddin and M. M. Ahmed, Par-4, A pro-apoptotic gene, inhibits radiation-induced NFkB activity and Bcl-2 expression leading to induction of radiosensitivity in human prostate cancer cells PC-3. Cancer Biol. Ther. 2, 152-162 (2002).
    • (2002) Cancer Biol. Ther. , vol.2 , pp. 152-162
    • Chendil, D.1    Das, A.2    Dey, S.3    Mohiuddin, M.4    Ahmed, M.M.5
  • 255
    • 0035477544 scopus 로고    scopus 로고
    • Par-4 drives trafficking and activation of Fas and Fas1 to induce prostate cancer cell apoptosis and tumor regression
    • M. Chakraborty, S. G. Qiu, K. M. Vasudevan and V. M. Rangnekar, Par-4 drives trafficking and activation of Fas and Fas1 to induce prostate cancer cell apoptosis and tumor regression. Cancer Res. 61, 7255-7263 (2001).
    • (2001) Cancer Res. , vol.61 , pp. 7255-7263
    • Chakraborty, M.1    Qiu, S.G.2    Vasudevan, K.M.3    Rangnekar, V.M.4
  • 256
    • 0036250160 scopus 로고    scopus 로고
    • Relationship between radiation-induced low-dose hypersensitivity and the bystander effect
    • C. Mothersill, C. B. Seymour and M. C. Joiner, Relationship between radiation-induced low-dose hypersensitivity and the bystander effect. Radiat. Res. 157, 526-532 (2002).
    • (2002) Radiat. Res. , vol.157 , pp. 526-532
    • Mothersill, C.1    Seymour, C.B.2    Joiner, M.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.