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Volumn 16, Issue 10, 1996, Pages 5839-5845

Destabilization of Raf-1 by geldanamycin leads to disruption of the Raf- 1-MEK-mitogen-activated protein kinase signalling pathway

Author keywords

[No Author keywords available]

Indexed keywords

GELDANAMYCIN; HEAT SHOCK PROTEIN 90; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE C; PROTEIN SERINE THREONINE KINASE; RAF PROTEIN; RAS PROTEIN; TRANSCRIPTION FACTOR;

EID: 0029813620     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.10.5839     Document Type: Article
Times cited : (259)

References (55)
  • 2
    • 0023625090 scopus 로고
    • Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factor
    • Angel, P., M. Imagawa, R. Chiu, B. Stein, R. J. Imbra, H. J. Rahmsdorf, C. Jonat, P. Herrlich, and M. Karin. 1987. Phorbol ester-inducible genes contain a common cis element recognized by a TPA-modulated trans-acting factor. Cell 49:729-739.
    • (1987) Cell , vol.49 , pp. 729-739
    • Angel, P.1    Imagawa, M.2    Chiu, R.3    Stein, B.4    Imbra, R.J.5    Rahmsdorf, H.J.6    Jonat, C.7    Herrlich, P.8    Karin, M.9
  • 3
    • 0025720735 scopus 로고
    • The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation
    • Angel, P., and M. Karin. 1991. The role of Jun, Fos and the AP-1 complex in cell-proliferation and transformation. Biochim. Biophys. Acta 1072:129-157.
    • (1991) Biochim. Biophys. Acta , vol.1072 , pp. 129-157
    • Angel, P.1    Karin, M.2
  • 4
    • 0025804529 scopus 로고
    • Lipid activation of protein kinase C
    • Bell, R. M., and D. J. Burns. 1991. Lipid activation of protein kinase C. J. Biol. Chem. 266:4661-4664.
    • (1991) J. Biol. Chem. , vol.266 , pp. 4661-4664
    • Bell, R.M.1    Burns, D.J.2
  • 5
    • 0027092897 scopus 로고
    • Cationic lipids enhance cellular uptake and activity of phosphorothioate antisense oligonucleotides
    • Bennett, C. F., M. V. Chiang, H. Chan, J. E. Shoemaker, and C. K. Mirabelli. 1992. Cationic lipids enhance cellular uptake and activity of phosphorothioate antisense oligonucleotides. Mol. Pharmacol. 41:1023-1033.
    • (1992) Mol. Pharmacol. , vol.41 , pp. 1023-1033
    • Bennett, C.F.1    Chiang, M.V.2    Chan, H.3    Shoemaker, J.E.4    Mirabelli, C.K.5
  • 6
    • 0027233448 scopus 로고
    • Signal transduction via the MAP kinases: Proceed at your own RSK
    • Blenis, J. 1993. Signal transduction via the MAP kinases: proceed at your own RSK. Proc. Natl. Acad. Sci. USA 90:5889-5892.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5889-5892
    • Blenis, J.1
  • 7
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski, M. S., and F. McCormick. 1993. Proteins regulating Ras and its relatives. Nature (London) 366:643-654.
    • (1993) Nature (London) , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 8
    • 0026596576 scopus 로고
    • Serum-, TPA-, and Ras-induced expression from Ap-1/Ets-driven promoters requires Raf-1 kinase
    • Bruder, J. T., G. Heidecker, and U. R. Rapp. 1992. Serum-, TPA-, and Ras-induced expression from Ap-1/Ets-driven promoters requires Raf-1 kinase. Genes Dev. 6:545-556.
    • (1992) Genes Dev. , vol.6 , pp. 545-556
    • Bruder, J.T.1    Heidecker, G.2    Rapp, U.R.3
  • 9
    • 0028926263 scopus 로고
    • Parallel signal processing among mammalian MAPKs
    • Cano, E., and L. C. Mahadevan. 1995. Parallel signal processing among mammalian MAPKs. Trends Biochem. Sci. 20:117-122.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 117-122
    • Cano, E.1    Mahadevan, L.C.2
  • 10
    • 0029164688 scopus 로고
    • A proline-rich sequence unique to MEK1 and MEK2 is required for raf binding and regulates MEK function
    • Catling, A. D., H. J. Schaeffer, C. W. Reuter, G. R. Reddy, and M. J. Weber. 1995. A proline-rich sequence unique to MEK1 and MEK2 is required for raf binding and regulates MEK function. Mol. Cell. Biol. 15:5214-5225.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5214-5225
    • Catling, A.D.1    Schaeffer, H.J.2    Reuter, C.W.3    Reddy, G.R.4    Weber, M.J.5
  • 11
    • 0026052924 scopus 로고
    • Antisense oligonucleotides inhibit intercellular adhesion molecule 1 expression by two distinct mechanisms
    • Chiang, M. Y., H. Chan, M. A. Zounes, S. M. Freier, W. F. Lima, and C. F. Bennett. 1991. Antisense oligonucleotides inhibit intercellular adhesion molecule 1 expression by two distinct mechanisms. J. Biol. Chem. 266:18162-18171.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18162-18171
    • Chiang, M.Y.1    Chan, H.2    Zounes, M.A.3    Freier, S.M.4    Lima, W.F.5    Bennett, C.F.6
  • 12
    • 0023782359 scopus 로고
    • The c-Fos protein interacts with c-Jun/AP-1 to stimulate transcription of AP-1 responsive genes
    • Chiu, R., W. J. Boyle, J. Meek, T. Smeal, T. Hunter, and M. Karin. 1988. The c-Fos protein interacts with c-Jun/AP-1 to stimulate transcription of AP-1 responsive genes. Cell 54:541-552.
    • (1988) Cell , vol.54 , pp. 541-552
    • Chiu, R.1    Boyle, W.J.2    Meek, J.3    Smeal, T.4    Hunter, T.5    Karin, M.6
  • 13
    • 0025819209 scopus 로고
    • Mitogen-activated Swiss mouse 3T3 RSK kinases I and II are related to pp44mpk from sea star oocytes and participate in the regulation of pp90rsk activity
    • Chung, J., S. L. Pelech, and J. Blenis. 1991. Mitogen-activated Swiss mouse 3T3 RSK kinases I and II are related to pp44mpk from sea star oocytes and participate in the regulation of pp90rsk activity. Proc. Natl. Acad. Sci. USA 88:4981-4985.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4981-4985
    • Chung, J.1    Pelech, S.L.2    Blenis, J.3
  • 14
    • 0026641090 scopus 로고
    • Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro
    • Dent, P., W. Haser, T. A. Haystead, L. A. Vincent, T. M. Roberts, and T. W. Sturgill. 1992. Activation of mitogen-activated protein kinase kinase by v-Raf in NIH 3T3 cells and in vitro. Science 257:1404-1407.
    • (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
  • 15
    • 0029042701 scopus 로고
    • Regulation of Raf-1 and Raf-1 mutants by Ras-dependent and Ras-independent mechanisms in vitro
    • Erratum, 15:5203
    • Dent, P., D. B. Reardon, D. K. Morrison, and T. W. Sturgill. 1995. Regulation of Raf-1 and Raf-1 mutants by Ras-dependent and Ras-independent mechanisms in vitro. Mol. Cell. Biol. 15:4125-4135. (Erratum, 15:5203.)
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4125-4135
    • Dent, P.1    Reardon, D.B.2    Morrison, D.K.3    Sturgill, T.W.4
  • 16
    • 0027586171 scopus 로고
    • A conserved kinase cascade for MAP kinase activation in yeast
    • Errede, B., and D. E. Levin. 1993. A conserved kinase cascade for MAP kinase activation in yeast. Curr. Opin. Cell Biol. 5:254-260.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 254-260
    • Errede, B.1    Levin, D.E.2
  • 17
    • 0027364980 scopus 로고
    • Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase
    • Fabian, J. R., I. O. Daar, and D. K. Morrison. 1993. Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase. Mol. Cell. Biol. 13:7170-7179.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7170-7179
    • Fabian, J.R.1    Daar, I.O.2    Morrison, D.K.3
  • 18
    • 0028931406 scopus 로고
    • ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation
    • Gille, H., M. Kortenjann, O. Thomae, C. Moomaw, C. Slaughter, M. H. Cobb, and P. E. Shaw. 1995. ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. EMBO J. 14:951-962.
    • (1995) EMBO J. , vol.14 , pp. 951-962
    • Gille, H.1    Kortenjann, M.2    Thomae, O.3    Moomaw, C.4    Slaughter, C.5    Cobb, M.H.6    Shaw, P.E.7
  • 19
    • 0028900634 scopus 로고
    • Immunocytochemical localization of eight protein kinase C isozymes overexpressed in NIH 3T3 fibroblasts. Isoform-specific association with microfilaments, Golgi, endoplasmic reticulum, and nuclear and cell membranes
    • Goodnight, J. A., H. Mischak, W. Kolch, and J. F. Mushinski. 1995. Immunocytochemical localization of eight protein kinase C isozymes overexpressed in NIH 3T3 fibroblasts. Isoform-specific association with microfilaments, Golgi, endoplasmic reticulum, and nuclear and cell membranes. J. Biol. Chem. 270:9991-10001.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9991-10001
    • Goodnight, J.A.1    Mischak, H.2    Kolch, W.3    Mushinski, J.F.4
  • 20
    • 0027417593 scopus 로고
    • Transactivation of gene expression by Myc is inhibited by mutation at the phosphorylation sites Thr-58 and Ser-62
    • Gupta, S., A. Seth, and R. J. Davis. 1993. Transactivation of gene expression by Myc is inhibited by mutation at the phosphorylation sites Thr-58 and Ser-62. Proc. Natl. Acad. Sci. USA 90:3216-3220.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3216-3220
    • Gupta, S.1    Seth, A.2    Davis, R.J.3
  • 22
    • 0019366764 scopus 로고
    • Nerve growth factor-induced alteration in the response of PC12 pheochromocytoma cells to epidermal growth factor
    • Huff, K., D. End, and G. Guroff. 1981. Nerve growth factor-induced alteration in the response of PC12 pheochromocytoma cells to epidermal growth factor. J. Cell Biol. 88:189-198.
    • (1981) J. Cell Biol. , vol.88 , pp. 189-198
    • Huff, K.1    End, D.2    Guroff, G.3
  • 23
    • 0018367607 scopus 로고
    • Nerve growth factor-induced reduction in epidermal growth factor responsiveness and epidermal growth factor receptors in PC12 cells: An aspect of cell differentiation
    • Huff, K. R., and G. Guroff. 1979. Nerve growth factor-induced reduction in epidermal growth factor responsiveness and epidermal growth factor receptors in PC12 cells: an aspect of cell differentiation. Biochem. Biophys. Res. Commun. 89:175-180.
    • (1979) Biochem. Biophys. Res. Commun. , vol.89 , pp. 175-180
    • Huff, K.R.1    Guroff, G.2
  • 24
    • 0025243788 scopus 로고
    • Inhibition of IL-2 receptor induction and IL-2 production in the human leukemic cell line Jurkat by a novel peptide inhibitor of protein kinase C
    • Ioannides, C. G., R. S. Freedman, R. M. Liskamp, N. E. Ward, and C. A. O'Brian. 1990. Inhibition of IL-2 receptor induction and IL-2 production in the human leukemic cell line Jurkat by a novel peptide inhibitor of protein kinase C. Cell. Immunol. 131:242-252.
    • (1990) Cell. Immunol. , vol.131 , pp. 242-252
    • Ioannides, C.G.1    Freedman, R.S.2    Liskamp, R.M.3    Ward, N.E.4    O'Brian, C.A.5
  • 25
    • 0026539206 scopus 로고
    • The AP-1 site at -150 bp, but not the NF-kappa B site, is likely to represent the major target of protein kinase C in the interleukin 2 promoter
    • Jain, J., A. V. Valge, A. J. Sinskey, and A. Rao. 1992. The AP-1 site at -150 bp, but not the NF-kappa B site, is likely to represent the major target of protein kinase C in the interleukin 2 promoter. J. Exp. Med. 175:853-862.
    • (1992) J. Exp. Med. , vol.175 , pp. 853-862
    • Jain, J.1    Valge, A.V.2    Sinskey, A.J.3    Rao, A.4
  • 27
    • 0025979335 scopus 로고
    • Raf-1 protein kinase is required for growth of induced NIH/3T3 cells
    • Kolch, W., G. Heidecker, P. Lloyd, and U. R. Rapp. 1991. Raf-1 protein kinase is required for growth of induced NIH/3T3 cells. Nature (London) 349:426-428.
    • (1991) Nature (London) , vol.349 , pp. 426-428
    • Kolch, W.1    Heidecker, G.2    Lloyd, P.3    Rapp, U.R.4
  • 28
    • 0026681340 scopus 로고
    • Mitogen stimulation of T-cells increases c-Fos and c-Jun protein levels, AP-1 binding and AP-1 transcriptional activity
    • Kvanta, A., E. Kontny, M. Jondal, S. Okret, and B. B. Fredholm. 1992. Mitogen stimulation of T-cells increases c-Fos and c-Jun protein levels, AP-1 binding and AP-1 transcriptional activity. Cell. Signalling 4:275-286.
    • (1992) Cell. Signalling , vol.4 , pp. 275-286
    • Kvanta, A.1    Kontny, E.2    Jondal, M.3    Okret, S.4    Fredholm, B.B.5
  • 30
    • 0029006126 scopus 로고
    • Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation
    • Marais, R., Y. Light, H. F. Paterson, and C. J. Marshall. 1995. Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J. 14:3136-3145.
    • (1995) EMBO J. , vol.14 , pp. 3136-3145
    • Marais, R.1    Light, Y.2    Paterson, H.F.3    Marshall, C.J.4
  • 31
    • 0028152333 scopus 로고
    • MAP kinase kinase kinase, MAP kinase kinase and MAP kinase
    • Marshall, C. J. 1994. MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr. Opin. Genet. Dev. 4:82-89.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 82-89
    • Marshall, C.J.1
  • 32
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall, C. J. 1995. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 80:179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 33
    • 0029977448 scopus 로고    scopus 로고
    • Antitumor activity of a phosphorothioate antisense oligodeoxynucleotide targeted against c-raf kinase
    • Monia, B. P., J. F. Johnston, T. Geiger, M. Muller, and D. Fabbro. 1996. Antitumor activity of a phosphorothioate antisense oligodeoxynucleotide targeted against c-raf kinase. Nat. Med. 2:668-675.
    • (1996) Nat. Med. , vol.2 , pp. 668-675
    • Monia, B.P.1    Johnston, J.F.2    Geiger, T.3    Muller, M.4    Fabbro, D.5
  • 35
    • 0027168907 scopus 로고
    • Identification of the major phosphorylation sites of the Raf-1 kinase
    • Morrison, D. K., G. Heidecker, U. R. Rapp, and T. D. Copeland. 1993. Identification of the major phosphorylation sites of the Raf-1 kinase. J. Biol. Chem. 268:17309-17316.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17309-17316
    • Morrison, D.K.1    Heidecker, G.2    Rapp, U.R.3    Copeland, T.D.4
  • 36
    • 0028030884 scopus 로고
    • Dominant negative mutant of c-Jun inhibits NF-AT transcriptional activity and prevents IL-2 gene transcription
    • Petrak, D., S. A. Memon, M. J. Birrer, J. D. Ashwell, and C. M. Zacharchuk. 1994. Dominant negative mutant of c-Jun inhibits NF-AT transcriptional activity and prevents IL-2 gene transcription. J. Immunol. 153:2046-2051.
    • (1994) J. Immunol. , vol.153 , pp. 2046-2051
    • Petrak, D.1    Memon, S.A.2    Birrer, M.J.3    Ashwell, J.D.4    Zacharchuk, C.M.5
  • 37
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor
    • Pratt, W. B. 1993. The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptor. J. Biol. Chem. 268: 21455-21458.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 39
    • 0028965111 scopus 로고
    • Biochemical analysis of MEK activation in NIH3T3 fibroblasts. Identification of B-Raf and other activators
    • Reuter, C. W., A. D. Catling, T. Jelinek, and M. J. Weber. 1995. Biochemical analysis of MEK activation in NIH3T3 fibroblasts. Identification of B-Raf and other activators. J. Biol. Chem. 270:7644-7655.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7644-7655
    • Reuter, C.W.1    Catling, A.D.2    Jelinek, T.3    Weber, M.J.4
  • 40
    • 0028022750 scopus 로고
    • A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins
    • Rouse, J., P. Cohen, S. Trigon, M. Morange, L. A. Alonso, D. Zamanillo, T. Hunt, and A. R. Nebreda. 1994. A novel kinase cascade triggered by stress and heat shock that stimulates MAPKAP kinase-2 and phosphorylation of the small heat shock proteins. Cell 78:1027-1037.
    • (1994) Cell , vol.78 , pp. 1027-1037
    • Rouse, J.1    Cohen, P.2    Trigon, S.3    Morange, M.4    Alonso, L.A.5    Zamanillo, D.6    Hunt, T.7    Nebreda, A.R.8
  • 41
    • 0028786332 scopus 로고
    • Disruption of the Raf-1-hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association
    • Schulte, T. W., M. V. Blagosklonny, C. Ingui, and L. Neckers. 1995. Disruption of the Raf-1-hsp90 molecular complex results in destabilization of Raf-1 and loss of Raf-1-Ras association. J. Biol. Chem. 270:24585-24588.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24585-24588
    • Schulte, T.W.1    Blagosklonny, M.V.2    Ingui, C.3    Neckers, L.4
  • 43
    • 0026343730 scopus 로고
    • A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression
    • Seth, A., E. Alvarez, S. Gupta, and R. J. Davis. 1991. A phosphorylation site located in the NH2-terminal domain of c-Myc increases transactivation of gene expression. J. Biol. Chem. 266:23521-23524.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23521-23524
    • Seth, A.1    Alvarez, E.2    Gupta, S.3    Davis, R.J.4
  • 44
    • 0026464922 scopus 로고
    • Signal transduction within the nucleus by mitogen-activated protein kinase
    • Seth, A., F. A. Gonzalez, S. Gupta, D. L. Raden, and R. J. Davis. 1992. Signal transduction within the nucleus by mitogen-activated protein kinase. J. Biol. Chem. 267:24796-24804.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24796-24804
    • Seth, A.1    Gonzalez, F.A.2    Gupta, S.3    Raden, D.L.4    Davis, R.J.5
  • 45
    • 0027433644 scopus 로고
    • Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system
    • Stancato, L. F., Y. H. Chow, K. A. Hutchison, G. H. Perdew, R. Jove, and W. B. Pratt. 1993. Raf exists in a native heterocomplex with hsp90 and p50 that can be reconstituted in a cell-free system. J. Biol. Chem. 268:21711-21716.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21711-21716
    • Stancato, L.F.1    Chow, Y.H.2    Hutchison, K.A.3    Perdew, G.H.4    Jove, R.5    Pratt, W.B.6
  • 47
    • 0028241533 scopus 로고
    • Activation of Raf as a result of recruitment to the plasma membrane
    • Erratum, 266:1792-1793
    • Stokoe, D., S. G. Macdonald, K. Cadwallader, M. Symons, and J. F. Hancock. 1994. Activation of Raf as a result of recruitment to the plasma membrane. Science 264:1463-1467. (Erratum, 266:1792-1793.)
    • (1994) Science , vol.264 , pp. 1463-1467
    • Stokoe, D.1    Macdonald, S.G.2    Cadwallader, K.3    Symons, M.4    Hancock, J.F.5
  • 48
    • 0023766145 scopus 로고
    • Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II
    • Sturgill, T. W., L. B. Ray, E. Erikson, and J. L. Maller. 1988. Insulin-stimulated MAP-2 kinase phosphorylates and activates ribosomal protein S6 kinase II. Nature (London) 334:715-718.
    • (1988) Nature (London) , vol.334 , pp. 715-718
    • Sturgill, T.W.1    Ray, L.B.2    Erikson, E.3    Maller, J.L.4
  • 49
    • 0027527919 scopus 로고
    • Specific association of activated MAP kinase kinase kinase (Raf) with the plasma membranes of ras-transformed retinal cells
    • Traverse, S., P. Cohen, H. Paterson, C. Marshall, U. Rapp, and R. J. Grand. 1993. Specific association of activated MAP kinase kinase kinase (Raf) with the plasma membranes of ras-transformed retinal cells. Oncogene 8:3175-3181.
    • (1993) Oncogene , vol.8 , pp. 3175-3181
    • Traverse, S.1    Cohen, P.2    Paterson, H.3    Marshall, C.4    Rapp, U.5    Grand, R.J.6
  • 50
    • 0026486878 scopus 로고
    • Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor
    • Traverse, S., N. Gomez, H. Paterson, C. Marshall, and P. Cohen. 1992. Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor. Biochem. J. 288:351-355.
    • (1992) Biochem. J. , vol.288 , pp. 351-355
    • Traverse, S.1    Gomez, N.2    Paterson, H.3    Marshall, C.4    Cohen, P.5
  • 51
    • 0028803402 scopus 로고
    • Journey to the surface of the cell: Fos regulation and the SRE
    • Treisman, R. 1995. Journey to the surface of the cell: Fos regulation and the SRE. EMBO J. 14:4905-4913.
    • (1995) EMBO J. , vol.14 , pp. 4905-4913
    • Treisman, R.1
  • 52
    • 0023792779 scopus 로고
    • Protein kinase C is required for responses to T cell receptor ligands but not to interleukin-2 in T cells
    • Valge, V. E., J. G. Wong, B. M. Datlof, A. J. Sinskey, and A. Rao. 1988. Protein kinase C is required for responses to T cell receptor ligands but not to interleukin-2 in T cells. Cell 55:101-112.
    • (1988) Cell , vol.55 , pp. 101-112
    • Valge, V.E.1    Wong, J.G.2    Datlof, B.M.3    Sinskey, A.J.4    Rao, A.5
  • 53
    • 0028227245 scopus 로고
    • The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex
    • Wartmann, M., and R. J. Davis. 1994. The native structure of the activated Raf protein kinase is a membrane-bound multi-subunit complex. J. Biol. Chem. 269:6695-6701.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6695-6701
    • Wartmann, M.1    Davis, R.J.2
  • 54
    • 0028064940 scopus 로고
    • Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: Essential role for stress proteins in oncogenic transformation
    • Whitesell, L., E. G. Mimnaugh, C. B. De, C. E. Myers, and L. M. Neckers. 1994. Inhibition of heat shock protein HSP90-pp60v-src heteroprotein complex formation by benzoquinone ansamycins: essential role for stress proteins in oncogenic transformation. Proc. Natl. Acad. Sci. USA 91:8324-8328.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8324-8328
    • Whitesell, L.1    Mimnaugh, E.G.2    De, C.B.3    Myers, C.E.4    Neckers, L.M.5
  • 55
    • 0027164311 scopus 로고
    • The cytoplasmic raf oncogene induces a neuronal phenotype in PC12 cells: A potential role for cellular raf kinases in neuronal growth factor signal transduction
    • Wood, K. W., H. Qi, G. D'Arcangelo, R. C. Armstrong, T. M. Roberts, and S. Halegoua. 1993. The cytoplasmic raf oncogene induces a neuronal phenotype in PC12 cells: a potential role for cellular raf kinases in neuronal growth factor signal transduction. Proc. Natl. Acad. Sci. USA 90:5016-5020.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5016-5020
    • Wood, K.W.1    Qi, H.2    D'Arcangelo, G.3    Armstrong, R.C.4    Roberts, T.M.5    Halegoua, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.