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Volumn 17, Issue 7, 2003, Pages 1263-1293

Signal transduction mediated by the Ras/Raf/MEK/ERK pathway from cytokine receptors to transcription factors: Potential targeting for therapeutic intervention

Author keywords

Cytokines; MAPK kinase cascade; Oncogenes; Signal transduction; Small molecular weight membrane permeable inhibitors; Therapeutic intervention

Indexed keywords

1,2,3,4,9,9A HEXAHYDRO 2 [2 (2 METHOXYPHENYL) 1 OXO 2 PROPENYL] 9 (4 METHYLPHENYL) 4,9 ETHANO 3AH BENZ[F]ISOINDOLE 3A CARBOXYLIC ACID; 2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 (2 CHLORO 4 IODOANILINO) N CYCLOPROPYLMETHOXY 3,4 DIFLUOROBENZAMIDE; 3 BENZYL 7 CYANO 2,3,4,5 TETRAHYDRO 1 (1H IMIDAZOL 4 YLMETHYL) 4 (2 THIENYLSULFONYL) 1H 1,4 BENZODIAZEPINE; ANTINEOPLASTIC AGENT; CELL SURFACE RECEPTOR; CYTOKINE RECEPTOR; GELDANAMYCIN; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; HERBIMYCIN A; INTERLEUKIN 3; LONAFARNIB; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; N (8 AMINO 2 BENZYL 5 ISOPROPYL 9 MERCAPTO 3,6 NONADIENOYL)METHIONINE; N [2 [2 (2 AMINO 3 MERCAPTOPROPYLAMINO) 3 METHYLPENTYLOXY] 3 PHENYLPROPIONYL]METHIONINE SULFONE METHYL ESTER; N [[5 [(2 AMINO 3 MERCAPTOPROPYL)AMINO][1,1' BIPHENYL] 2 YL]CARBONYL]METHIONINE METHYL ESTER; NOVOBIOCIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN INHIBITOR; PROTEIN KINASE B; PROTEIN TYROSINE KINASE; PROTEIN TYROSINE KINASE INHIBITOR; RAF PROTEIN; RAS PROTEIN; STAUROSPORINE; TIPIFARNIB; TRANSCRIPTION FACTOR; UNINDEXED DRUG; UO 126;

EID: 0037810249     PISSN: 08876924     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.leu.2402945     Document Type: Review
Times cited : (643)

References (569)
  • 1
    • 0037352170 scopus 로고    scopus 로고
    • Involvement of PI3K/Akt pathway in cell cycle progression, apoptosis, and neoplastic transformation: A target for cancer chemotherapy
    • Chang F, Lee JT, Navolanic PM, Steelman JG, Blalock WL, Franklin RA et al. Involvement of PI3K/Akt pathway in cell cycle progression, apoptosis, and neoplastic transformation: a target for cancer chemotherapy. Leukemia 2003; 17: 590-603.
    • (2003) Leukemia , vol.17 , pp. 590-603
    • Chang, F.1    Lee, J.T.2    Navolanic, P.M.3    Steelman, J.G.4    Blalock, W.L.5    Franklin, R.A.6
  • 2
    • 0037938663 scopus 로고    scopus 로고
    • Requirement for the PI3K/Akt pathway in MEK1-mediated growth and prevention of apoptosis: Identification of an Achilles heel in leukemia
    • (in press)
    • Blalock WL, Navolanic PM, Steelman LS, Shelton JG, Moye PW, Lee JT et al. Requirement for the PI3K/Akt pathway in MEK1-mediated growth and prevention of apoptosis: identification of an Achilles heel in leukemia. Leukemia 2003; 17 (in press).
    • (2003) Leukemia , vol.17
    • Blalock, W.L.1    Navolanic, P.M.2    Steelman, L.S.3    Shelton, J.G.4    Moye, P.W.5    Lee, J.T.6
  • 3
    • 0036238817 scopus 로고    scopus 로고
    • The Raf/MEK/ERK signal transduction cascade as a target for chemotherapeutic intervention
    • Lee Jr JT, McCubrey JA. The Raf/MEK/ERK signal transduction cascade as a target for chemotherapeutic intervention. Leukemia 2002; 16: 486-507.
    • (2002) Leukemia , vol.16 , pp. 486-507
    • Lee J.T., Jr.1    McCubrey, J.A.2
  • 4
    • 0032874677 scopus 로고    scopus 로고
    • Signal transduction, cell cycle regulatory, and anti-apoptotic pathways regulated by IL-3 in hematopoietic cells: Possible sites for intervention with anti-neoplastic drugs
    • Blalock WL, Weinstein-Oppenheimer C, Chang F, Hoyle PE, Wang X-Y, Algate PA et al. Signal transduction, cell cycle regulatory, and anti-apoptotic pathways regulated by IL-3 in hematopoietic cells: possible sites for intervention with anti-neoplastic drugs. Leukemia 1999; 13:1109-1166.
    • (1999) Leukemia , vol.13 , pp. 1109-1166
    • Blalock, W.L.1    Weinstein-Oppenheimer, C.2    Chang, F.3    Hoyle, P.E.4    Wang, X.-Y.5    Algate, P.A.6
  • 5
    • 0035070303 scopus 로고    scopus 로고
    • Specificity in cytokine signal transduction: Lessons learned from the IL-3/IL-5/GM-CSF receptor family
    • Geijsen N, Koenderman L, Coffer PJ. Specificity in cytokine signal transduction: lessons learned from the IL-3/IL-5/GM-CSF receptor family. Cytokine Growth Factor Rev 2001; 12: 19-25.
    • (2001) Cytokine Growth Factor Rev. , vol.12 , pp. 19-25
    • Geijsen, N.1    Koenderman, L.2    Coffer, P.J.3
  • 6
    • 0031761118 scopus 로고    scopus 로고
    • Differential abilities of activated Raf oncoproteins to abrogate cytokine dependency, prevent apoptosis and induce autocrine growth factor synthesis in human hematopoietic cells
    • McCubrey JA, Steelman LS, Hoyle PA, Blalock WL, Weinstein-Oppenheimer CR, Franklin RA et al. Differential abilities of activated Raf oncoproteins to abrogate cytokine dependency, prevent apoptosis and induce autocrine growth factor synthesis in human hematopoietic cells. Leukemia 1998; 12: 1903-1929.
    • (1998) Leukemia , vol.12 , pp. 1903-1929
    • McCubrey, J.A.1    Steelman, L.S.2    Hoyle, P.A.3    Blalock, W.L.4    Weinstein-Oppenheimer, C.R.5    Franklin, R.A.6
  • 7
    • 0033630308 scopus 로고    scopus 로고
    • Serine/threonine phosphorylation in cytokine signal transduction
    • McCubrey JA, May WS, Duronio V, Mufson A. Serine/threonine phosphorylation in cytokine signal transduction. Leukemia 2000; 14: 9-21.
    • (2000) Leukemia , vol.14 , pp. 9-21
    • McCubrey, J.A.1    May, W.S.2    Duronio, V.3    Mufson, A.4
  • 8
    • 0035224494 scopus 로고    scopus 로고
    • Interactions between the PI3K and Raf signaling pathways can result in the transformation of hematopoietic cells
    • McCubrey JA, Lee JT, Steelman LS, Blalock WL, Moye PW, Chang F et al. Interactions between the PI3K and Raf signaling pathways can result in the transformation of hematopoietic cells. Cancer Detect Prev 2001; 25: 375-393.
    • (2001) Cancer Detect. Prev. , vol.25 , pp. 375-393
    • McCubrey, J.A.1    Lee, J.T.2    Steelman, L.S.3    Blalock, W.L.4    Moye, P.W.5    Chang, F.6
  • 9
    • 0034076367 scopus 로고    scopus 로고
    • Differential abilities of the Raf family of protein kinases to abrogate cytokine dependency and prevent apoptosis in murine hematopoietic cells by a MEK1-dependent mechanism
    • Hoyle PE, Moye PW, Steelman LS, Blalock WL, Franklin RA, Pearce M et al. Differential abilities of the Raf family of protein kinases to abrogate cytokine dependency and prevent apoptosis in murine hematopoietic cells by a MEK1-dependent mechanism. Leukemia 2000; 14: 642-656.
    • (2000) Leukemia , vol.14 , pp. 642-656
    • Hoyle, P.E.1    Moye, P.W.2    Steelman, L.S.3    Blalock, W.L.4    Franklin, R.A.5    Pearce, M.6
  • 11
    • 17944368285 scopus 로고    scopus 로고
    • Enhanced ability of daniplestim and myelopoietin-1 to suppress apoptosis in human hematopoietic cells
    • McCubrey JA, Blalock WL, Saleh O, Pearce M, Burrows C, Steelman LS et al. Enhanced ability of daniplestim and myelopoietin-1 to suppress apoptosis in human hematopoietic cells. Leukemia 2001; 15: 1203-1216.
    • (2001) Leukemia , vol.15 , pp. 1203-1216
    • McCubrey, J.A.1    Blalock, W.L.2    Saleh, O.3    Pearce, M.4    Burrows, C.5    Steelman, L.S.6
  • 12
    • 85014133385 scopus 로고    scopus 로고
    • The enhanced in vitro hematopoietic activity of leridisim, a chimeric dual G-CSF and IL-3 receptor agonist
    • Abegg AL, Vickery LE, Bremer ME, Donnelly AM, Doshi PD, Evans ML et al. The enhanced in vitro hematopoietic activity of leridisim, a chimeric dual G-CSF and IL-3 receptor agonist. Leukemia 2002; 16: 316-326.
    • (2002) Leukemia , vol.16 , pp. 316-326
    • Abegg, A.L.1    Vickery, L.E.2    Bremer, M.E.3    Donnelly, A.M.4    Doshi, P.D.5    Evans, M.L.6
  • 13
    • 0036167084 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase and p38 mitogen-activated protein kinase pathways cooperate in mediating cytokine-induced proliferation of a leukemic cell line
    • Srinivasa SP, Doshi PD. Extracellular signal-regulated kinase and p38 mitogen-activated protein kinase pathways cooperate in mediating cytokine-induced proliferation of a leukemic cell line. Leukemia 2002; 16: 244-253.
    • (2002) Leukemia , vol.16 , pp. 244-253
    • Srinivasa, S.P.1    Doshi, P.D.2
  • 14
    • 0033759376 scopus 로고    scopus 로고
    • Effects of deregulated Raf activation on integrin, cytokine-receptor expression and the induction of apoptosis in hematopoietic cells
    • Weinstein-Oppenheimer C, Steelman LS, Algate PA, Blalock WL, Burrows C, Hoyle PE et al. Effects of deregulated Raf activation on integrin, cytokine-receptor expression and the induction of apoptosis in hematopoietic cells. Leukemia 2000; 14: 1921-1938.
    • (2000) Leukemia , vol.14 , pp. 1921-1938
    • Weinstein-Oppenheimer, C.1    Steelman, L.S.2    Algate, P.A.3    Blalock, W.L.4    Burrows, C.5    Hoyle, P.E.6
  • 16
    • 0034450953 scopus 로고    scopus 로고
    • Raf signal transcluction cascade as a target for chemotherapeutic intervention in growth factor-dependent tumors
    • Weinstein-Oppenheimer CR, Blalock WL, Steelman LS, Chang F, McCubrey JA. Raf signal transcluction cascade as a target for chemotherapeutic intervention in growth factor-dependent tumors. Pharm Ther 2000; 88: 229-279.
    • (2000) Pharm. Ther. , vol.88 , pp. 229-279
    • Weinstein-Oppenheimer, C.R.1    Blalock, W.L.2    Steelman, L.S.3    Chang, F.4    McCubrey, J.A.5
  • 17
    • 0034525423 scopus 로고    scopus 로고
    • Kinases positive and negative regulators of apoptosis
    • Franklin RA, McCubrey JA. Kinases positive and negative regulators of apoptosis. Leukemia 2000; 14: 2019-2034.
    • (2000) Leukemia , vol.14 , pp. 2019-2034
    • Franklin, R.A.1    McCubrey, J.A.2
  • 18
    • 0034899450 scopus 로고    scopus 로고
    • Suppression of apoptosis role in cell growth and neoplasia
    • White MK, McCubrey JA. Suppression of apoptosis role in cell growth and neoplasia. Leukemia 2001; 15: 1011-1021.
    • (2001) Leukemia , vol.15 , pp. 1011-1021
    • White, M.K.1    McCubrey, J.A.2
  • 19
    • 0034719381 scopus 로고    scopus 로고
    • A conditionally-active form of MEK1 results in autocrine transformation of human and mouse hematopoietic cells
    • Blalock WL, Pearce M, Steelman LS, Franklin RA, McCarthy SA, Cherwinski H et al. A conditionally-active form of MEK1 results in autocrine transformation of human and mouse hematopoietic cells. Oncogene 2000; 19: 526-536.
    • (2000) Oncogene , vol.19 , pp. 526-536
    • Blalock, W.L.1    Pearce, M.2    Steelman, L.S.3    Franklin, R.A.4    McCarthy, S.A.5    Cherwinski, H.6
  • 20
    • 0034130788 scopus 로고    scopus 로고
    • Combined effects of aberrant MEK1 activity and BCL2 overexpression on relieving the cytokine-dependency of hematopoietic cells
    • Blalock WL, Moye PW, Chang F, Pearce M, Steelman LS, McMahon M et al. Combined effects of aberrant MEK1 activity and BCL2 overexpression on relieving the cytokine-dependency of hematopoietic cells. Adv Enzyme Regul 2000; 40: 305-337.
    • (2000) Adv. Enzyme Regul. , vol.40 , pp. 305-337
    • Blalock, W.L.1    Moye, P.W.2    Chang, F.3    Pearce, M.4    Steelman, L.S.5    McMahon, M.6
  • 21
    • 0035019189 scopus 로고    scopus 로고
    • Effects of inducible MEK1 activation on the cytokine-dependency of lymphoid cells
    • Blalock WL, Pearce M, Chang F, Lee JT, Pohnert S, Burrows C et al. Effects of inducible MEK1 activation on the cytokine-dependency of lymphoid cells. Leukemia 2001; 15: 794-807.
    • (2001) Leukemia , vol.15 , pp. 794-807
    • Blalock, W.L.1    Pearce, M.2    Chang, F.3    Lee, J.T.4    Pohnert, S.5    Burrows, C.6
  • 23
    • 0027385030 scopus 로고
    • Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human Raf-1 protein kinase
    • Samuels ML, Weber MJ, Bishop JM, McMahon M. Conditional transformation of cells and rapid activation of the mitogen-activated protein kinase cascade by an estradiol-dependent human Raf-1 protein kinase. Mol Cell Biol 1993; 13: 6241-6252.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 6241-6252
    • Samuels, M.L.1    Weber, M.J.2    Bishop, J.M.3    McMahon, M.4
  • 24
    • 0028877441 scopus 로고
    • Conditionally oncogenic forms of the A-Raf and B-Raf protein kinases display different biological and biochemical properties in NIH-3T3 cells
    • Pritchard CA, Samuels ML, Bosch E, McMahon M. Conditionally oncogenic forms of the A-Raf and B-Raf protein kinases display different biological and biochemical properties in NIH-3T3 cells. Mol Cell Biol 1995; 15: 6430-6442.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 6430-6442
    • Pritchard, C.A.1    Samuels, M.L.2    Bosch, E.3    McMahon, M.4
  • 25
    • 0030133927 scopus 로고    scopus 로고
    • Post-natal lethality and neurological and gastrointestinal defects in mice with targeted disruption of the A-Raf protein kinase gene
    • Pritchard CA, Bolin L, Slattery R, Murray R, McMahon M. Post-natal lethality and neurological and gastrointestinal defects in mice with targeted disruption of the A-Raf protein kinase gene. Curr Biol 1996; 6: 614-617.
    • (1996) Curr. Biol. , vol.6 , pp. 614-617
    • Pritchard, C.A.1    Bolin, L.2    Slattery, R.3    Murray, R.4    McMahon, M.5
  • 27
    • 0030881165 scopus 로고    scopus 로고
    • Mutations of critical amino acids affect the biological and biochemical properties of oncogenic A-Raf and Raf-1
    • Bosch E, Cherwinski H, Peterson D, McMahon M. Mutations of critical amino acids affect the biological and biochemical properties of oncogenic A-Raf and Raf-1. Oncogene 1997; 11: 1021-1034.
    • (1997) Oncogene , vol.11 , pp. 1021-1034
    • Bosch, E.1    Cherwinski, H.2    Peterson, D.3    McMahon, M.4
  • 28
    • 0033029811 scopus 로고    scopus 로고
    • Ras caught in another affair the exchange factors for Ral
    • Wolthuis RMF, Bos JL. Ras caught in another affair the exchange factors for Ral. Curr Opin Genet Develop 1999; 9: 112-117.
    • (1999) Curr. Opin. Genet. Develop. , vol.9 , pp. 112-117
    • Wolthuis, R.M.F.1    Bos, J.L.2
  • 29
    • 0033835922 scopus 로고    scopus 로고
    • Induction of postmitotic neuroretina cell proliferation by distinct Ras downstream signaling pathways
    • Peyssonnaux C, Provot S, Felder-Schmittbuhl MP, Calothy G, Eychéne A. Induction of postmitotic neuroretina cell proliferation by distinct Ras downstream signaling pathways. Mol Cell Biol 2000; 20: 7068-7079.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 7068-7079
    • Peyssonnaux, C.1    Provot, S.2    Felder-Schmittbuhl, M.P.3    Calothy, G.4    Eychéne, A.5
  • 30
    • 0032746286 scopus 로고    scopus 로고
    • Ras-induced transformation and signaling pathway
    • Yamamoto T, Taya S, Kaibuchi K. Ras-induced transformation and signaling pathway. J Biochem 1999; 126: 799-803.
    • (1999) J. Biochem. , vol.126 , pp. 799-803
    • Yamamoto, T.1    Taya, S.2    Kaibuchi, K.3
  • 31
    • 0032508517 scopus 로고    scopus 로고
    • Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase
    • Yan J, Roy S, Apolloni A, Lane A, Hancock JF. Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase. J Biol Chem 1998; 273: 24052-24056.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24052-24056
    • Yan, J.1    Roy, S.2    Apolloni, A.3    Lane, A.4    Hancock, J.F.5
  • 32
    • 0035087327 scopus 로고    scopus 로고
    • Regulation of the Raf kinase by phosphorylation
    • Zhang BH, Guan KL. Regulation of the Raf kinase by phosphorylation. Exp Lung Res 2001; 2: 269-295.
    • (2001) Exp. Lung Res. , vol.2 , pp. 269-295
    • Zhang, B.H.1    Guan, K.L.2
  • 33
    • 0027200883 scopus 로고
    • Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro
    • Warne PH, Viciana PR, Downward J. Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature 1993; 364:352-355.
    • (1993) Nature , vol.364 , pp. 352-355
    • Warne, P.H.1    Viciana, P.R.2    Downward, J.3
  • 34
    • 0027337519 scopus 로고
    • Complexes of Ras. GTP with Raf-1 and mitogen-activated protein kinase kinase
    • Moodie SA, Willumsen BM, Weber MJ, Wolfman A. Complexes of Ras. GTP with Raf-1 and mitogen-activated protein kinase kinase. Science 1993; 260: 1658-1661.
    • (1993) Science , vol.260 , pp. 1658-1661
    • Moodie, S.A.1    Willumsen, B.M.2    Weber, M.J.3    Wolfman, A.4
  • 35
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine Raf
    • Vojteck AB, Hollenberg SM, Cooper JA. Mammalian Ras interacts directly with the serine/threonine Raf. Cell 1993; 74: 205-214.
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojteck, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 36
    • 0032444781 scopus 로고    scopus 로고
    • Dual function of Ras in Raf activation
    • Li W, Melnick M, Perrimon N. Dual function of Ras in Raf activation. Development 1998; 125: 4999-5008.
    • (1998) Development , vol.125 , pp. 4999-5008
    • Li, W.1    Melnick, M.2    Perrimon, N.3
  • 37
    • 0030581475 scopus 로고    scopus 로고
    • Raf gets it together
    • Marshall CJ. Raf gets it together. Nature 1996; 383: 127-128.
    • (1996) Nature , vol.383 , pp. 127-128
    • Marshall, C.J.1
  • 38
    • 0029807304 scopus 로고    scopus 로고
    • Activation of the Raf-1 kinase cascade by coumermycin induced dimerization
    • Farrar MA, Alberola-Ila J, Perlmutter RM. Activation of the Raf-1 kinase cascade by coumermycin induced dimerization. Nature 1996; 383: 178-181.
    • (1996) Nature , vol.383 , pp. 178-181
    • Farrar, M.A.1    Alberola-Ila, J.2    Perlmutter, R.M.3
  • 39
  • 40
    • 0035328521 scopus 로고    scopus 로고
    • Active Ras induces heterodimerization of c-Raf and B-Raf
    • Weber CK, Slupsky JR, Kalmes HA, Rapp UR. Active Ras induces heterodimerization of c-Raf and B-Raf. Cancer Res 2001; 61: 3595-31324.
    • (2001) Cancer Res. , vol.61 , pp. 3595-31324
    • Weber, C.K.1    Slupsky, J.R.2    Kalmes, H.A.3    Rapp, U.R.4
  • 41
    • 0034613293 scopus 로고    scopus 로고
    • Membrane localization of Raf assists engagement of downstream effectors
    • Farrar MA, Tian J, Perlmutter RM. Membrane localization of Raf assists engagement of downstream effectors. J Biol Chem 2000; 275: 31318-31324.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31318-31324
    • Farrar, M.A.1    Tian, J.2    Perlmutter, R.M.3
  • 42
    • 0023116071 scopus 로고
    • Definition of regions in human c-myc that are involved in transformation and nuclear localization
    • Stone J, deLange T, Ramsay G, Jakobvits E, Bishop JM, Varmus H et al. Definition of regions in human c-myc that are involved in transformation and nuclear localization. Mol Cell Biol 1987; 7: 1697-1709.
    • (1987) Mol. Cell Biol. , vol.7 , pp. 1697-1709
    • Stone, J.1    deLange, T.2    Ramsay, G.3    Jakobvits, E.4    Bishop, J.M.5    Varmus, H.6
  • 43
    • 0035898539 scopus 로고    scopus 로고
    • Positive and negative regulation of Raf kinase activity and function by phosphorylation
    • Chong H, Lee J, Guan KL. Positive and negative regulation of Raf kinase activity and function by phosphorylation. EMBO J 2001; 20: 3716-3727.
    • (2001) EMBO J. , vol.20 , pp. 3716-3727
    • Chong, H.1    Lee, J.2    Guan, K.L.3
  • 44
    • 0027364980 scopus 로고
    • Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase
    • Fabian JR, Daar IO, Morrison DK. Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase. Mol Cell Biol 1993; 13: 7170-7179.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 7170-7179
    • Fabian, J.R.1    Daar, I.O.2    Morrison, D.K.3
  • 45
    • 0027297647 scopus 로고
    • The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain
    • Marais R, Wynne J, Treisman R. The SRF accessory protein Elk-1 contains a growth factor-regulated transcriptional activation domain. Cell 1993; 73: 381-393.
    • (1993) Cell , vol.73 , pp. 381-393
    • Marais, R.1    Wynne, J.2    Treisman, R.3
  • 46
    • 0027168907 scopus 로고
    • Identification of the major phosphorylation sites of the Raf-1 kinase
    • Morrison DK, Heidecker G, Rapp UR, Copeland TD. Identification of the major phosphorylation sites of the Raf-1 kinase. J Biol Chem 1993; 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
  • 48
    • 0034745354 scopus 로고    scopus 로고
    • Bag1-Hsp70 mediates a physiological stress signaling pathway that regulates Raf-1/ERK and cell growth
    • Song J, Takeda M, Morimoto RI. Bag1-Hsp70 mediates a physiological stress signaling pathway that regulates Raf-1/ERK and cell growth. Nat Cell Biol 2001; 3: 276-282.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 276-282
    • Song, J.1    Takeda, M.2    Morimoto, R.I.3
  • 49
    • 0035473486 scopus 로고    scopus 로고
    • 14-3-3 proteins; bringing new definitions to scaffolding
    • Tzivion G, Shen YH, Zhu J. 14-3-3 proteins; bringing new definitions to scaffolding. Oncogene 2001; 20: 6331-6338.
    • (2001) Oncogene , vol.20 , pp. 6331-6338
    • Tzivion, G.1    Shen, Y.H.2    Zhu, J.3
  • 50
    • 85047695528 scopus 로고    scopus 로고
    • Hsp-90-associated oncoproteins: Multiple targets of geldanamycin and its analogs
    • Blagosklonney MV. Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs. Leukemia 2002; 16: 455-462.
    • (2002) Leukemia , vol.16 , pp. 455-462
    • Blagosklonney, M.V.1
  • 54
    • 0035977185 scopus 로고    scopus 로고
    • Association of c-Raf expression with survival and its targeting with antisense oligonucleotides in ovarian cancer
    • McPhillips F, Mullen P, Monia BP, Ritchie AA, Dorr FA, Smyth JF et al. Association of c-Raf expression with survival and its targeting with antisense oligonucleotides in ovarian cancer. Br J Cancer 2001; 85: 1753-1758.
    • (2001) Br. J. Cancer , vol.85 , pp. 1753-1758
    • McPhillips, F.1    Mullen, P.2    Monia, B.P.3    Ritchie, A.A.4    Dorr, F.A.5    Smyth, J.F.6
  • 55
    • 0032499288 scopus 로고    scopus 로고
    • Abrogation of c-Raf expression induces apoptosis in tumor cells
    • Lau QC, Brusselbach S, Muller R. Abrogation of c-Raf expression induces apoptosis in tumor cells. Oncogene 1998; 16: 1899-1902.
    • (1998) Oncogene , vol.16 , pp. 1899-1902
    • Lau, Q.C.1    Brusselbach, S.2    Muller, R.3
  • 57
    • 0028175091 scopus 로고
    • Raf meets Ras: Completing the framework of a signal transduction pathway
    • Avruch J, Zhang XF, Kyriakis JM. Raf meets Ras: completing the framework of a signal transduction pathway. Trends Biol Sci 1994; 19: 279-28358.
    • (1994) Trends Biol. Sci. , vol.19 , pp. 279-28358
    • Avruch, J.1    Zhang, X.F.2    Kyriakis, J.M.3
  • 58
    • 0029890896 scopus 로고    scopus 로고
    • Oncogenic Ras activation of Raf/mitogen-activated protein kinase-independent pathways is sufficient to cause tumorigenic transformation
    • Khosravi-Far R, White MA, Westwick JK, Solski PA, Chrzanowska-Wodnicka M, Aelst LV et al. Oncogenic Ras activation of Raf/mitogen-activated protein kinase-independent pathways is sufficient to cause tumorigenic transformation. Mol Cell Biol 1996; 16: 3923-3933.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 3923-3933
    • Khosravi-Far, R.1    White, M.A.2    Westwick, J.K.3    Solski, P.A.4    Chrzanowska-Wodnicka, M.5    Aelst, L.V.6
  • 59
    • 0029006126 scopus 로고
    • Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation
    • Marais R, Light Y, Paterson HF, Marshall CJ. Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phosphorylation. EMBO J 1995; 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
  • 60
    • 0037080956 scopus 로고    scopus 로고
    • Regulation of Raf-1 activation and signaling by dephosphorylation
    • Dhillon AS, Meikle S, Yazici Z, Eulitz M, Kolch W. Regulation of Raf-1 activation and signaling by dephosphorylation. EMBO J 2002; 1: 64-71.
    • (2002) EMBO J. , vol.1 , pp. 64-71
    • Dhillon, A.S.1    Meikle, S.2    Yazici, Z.3    Eulitz, M.4    Kolch, W.5
  • 61
    • 0035451062 scopus 로고    scopus 로고
    • To be or not to be: A question of B-Raf
    • Kolch W. To be or not to be: a question of B-Raf. Trends Neurosci 2001; 21: 498-500.
    • (2001) Trends Neurosci. , vol.21 , pp. 498-500
    • Kolch, W.1
  • 62
    • 0034667593 scopus 로고    scopus 로고
    • Meaningful relationships the regulation of the Ras/Raf/Mek-ERK pathway by protein interactions
    • Kolch W. Meaningful relationships the regulation of the Ras/Raf/Mek-ERK pathway by protein interactions. Biochem J 2000; 351: 289-305.
    • (2000) Biochem. J. , vol.351 , pp. 289-305
    • Kolch, W.1
  • 63
    • 0034698027 scopus 로고    scopus 로고
    • Raf-1 associated protein phosphatase 2A as a positive regulator of kinase activation
    • Abraham D, Podar K, Pacher M, Kubicek M, Welzel N, Hemmings BA et al. Raf-1 associated protein phosphatase 2A as a positive regulator of kinase activation. J Biol Chem 2000; 275: 22300-22304.
    • (2000) J. Biol. Chem. , vol.275 , pp. 22300-22304
    • Abraham, D.1    Podar, K.2    Pacher, M.3    Kubicek, M.4    Welzel, N.5    Hemmings, B.A.6
  • 64
    • 0033539167 scopus 로고    scopus 로고
    • Suppression of Raf-1 kinase activity and MAP kinase signaling by RKIP
    • Yeung K, Seitz T, Li S, Janosch P, McFerran B, Kaiser C et al. Suppression of Raf-1 kinase activity and MAP kinase signaling by RKIP. Nature 1999; 401: 173-177.
    • (1999) Nature , vol.401 , pp. 173-177
    • Yeung, K.1    Seitz, T.2    Li, S.3    Janosch, P.4    McFerran, B.5    Kaiser, C.6
  • 66
    • 0031041171 scopus 로고    scopus 로고
    • Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic ras and tyrosine kinases
    • Marais R, Light Y, Paterson HF, Mason CS, Marshall CJ. Differential regulation of Raf-1, A-Raf, and B-Raf by oncogenic ras and tyrosine kinases. J Biol Chem 1997; 272: 4378-4383.
    • (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
  • 67
    • 0030756069 scopus 로고    scopus 로고
    • Phosphorylation of Raf-1 serine 338-serine 339 is an essential regulatory event for Ras-dependent activation and biological signaling
    • Diaz B, Barnard D, Filson A, MacDonald S, King A, Marshall M. Phosphorylation of Raf-1 serine 338-serine 339 is an essential regulatory event for Ras-dependent activation and biological signaling. Mol Cell Biol 1997; 17: 4509-4516.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 4509-4516
    • Diaz, B.1    Barnard, D.2    Filson, A.3    MacDonald, S.4    King, A.5    Marshall, M.6
  • 68
    • 0032511882 scopus 로고    scopus 로고
    • The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338
    • King AJ, Sun H, Diaz B, Barnard D, Miao W, Bagrodia S et al. The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338. Nature 1998; 396: 180-183.
    • (1998) Nature , vol.396 , pp. 180-183
    • King, A.J.1    Sun, H.2    Diaz, B.3    Barnard, D.4    Miao, W.5    Bagrodia, S.6
  • 69
    • 0035907051 scopus 로고    scopus 로고
    • Phosphorylation site specificity of the Pak-mediated regulation of Raf-1 and cooperativity with Src
    • King AJ, Wireman RS, Hamilton M, Marshall MS. Phosphorylation site specificity of the Pak-mediated regulation of Raf-1 and cooperativity with Src. FEBS Lett 2001; 497: 6-14.
    • (2001) FEBS Lett. , vol.497 , pp. 6-14
    • King, A.J.1    Wireman, R.S.2    Hamilton, M.3    Marshall, M.S.4
  • 71
    • 0031038588 scopus 로고    scopus 로고
    • Role of diacylglycerol-regulated protein kinase C isotype in growth factor activation of the Raf-1 protein kinase
    • Cai H, Smola U, Wixler V, Eisenmann-Tappe I, Diaz-Meco MT, Moscat J et al. Role of diacylglycerol-regulated protein kinase C isotype in growth factor activation of the Raf-1 protein kinase. Mol Cell Biol 1997; 17: 732-741.
    • (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
  • 72
    • 0035903216 scopus 로고    scopus 로고
    • Sequential activation of protein kinase C (PKC)-alpha and PKC-epsilon contributes to sustained Raf/ERK1/2 activation in endothelial cells under mechanical strain
    • Cheng JJ, Wung BS, Chao YJ, Wang DL. Sequential activation of protein kinase C (PKC)-alpha and PKC-epsilon contributes to sustained Raf/ERK1/2 activation in endothelial cells under mechanical strain. J Biol Chem 2001; 276: 31368-31375.
    • (2001) J. Biol. Chem. , vol.276 , pp. 31368-31375
    • Cheng, J.J.1    Wung, B.S.2    Chao, Y.J.3    Wang, D.L.4
  • 73
    • 0032563961 scopus 로고    scopus 로고
    • Oncogenes, growth factors and phorbol esters regulate Raf-1 through common mechanisms
    • Barnard D, Diaz B, Clawson D, Marshall M. Oncogenes, growth factors and phorbol esters regulate Raf-1 through common mechanisms. Oncogene 1998; 17: 1539-1547.
    • (1998) Oncogene , vol.17 , pp. 1539-1547
    • Barnard, D.1    Diaz, B.2    Clawson, D.3    Marshall, M.4
  • 74
    • 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
    • Schonwasser DC, Marasis RM, Marshall CJ, Parker PJ. Activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by conventional, novel and atypical protein kinase C isotypes. Mol Cell Biol 1998; 18: 790-798.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 790-798
    • Schonwasser, D.C.1    Marasis, R.M.2    Marshall, C.J.3    Parker, P.J.4
  • 75
    • 0034776809 scopus 로고    scopus 로고
    • Protein kinase C isozymes, novel phorbol ester receptors and cancer chemotherapy
    • Barry OP, Kazanietz MG. Protein kinase C isozymes, novel phorbol ester receptors and cancer chemotherapy. Curr Pharm Des 2001; 7: 1725-1744.
    • (2001) Curr. Pharm. Des. , vol.7 , pp. 1725-1744
    • Barry, O.P.1    Kazanietz, M.G.2
  • 76
    • 0025004182 scopus 로고
    • Cytokine secretion effected by synergism of the immunomodulator AS101 and the protein kinase C inducer bryostatin
    • Sredni B, Kalechman Y, Albeck M, Gross O, Aurbach D, Sharon P et al. Cytokine secretion effected by synergism of the immunomodulator AS101 and the protein kinase C inducer bryostatin. Immunology 1990; 70: 473-477.
    • (1990) Immunology , vol.70 , pp. 473-477
    • Sredni, B.1    Kalechman, Y.2    Albeck, M.3    Gross, O.4    Aurbach, D.5    Sharon, P.6
  • 77
    • 0033607784 scopus 로고    scopus 로고
    • Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt
    • Rommel C, Clarke BA, Zimmermann S, Nuñez L, Rossman R, Reid K et al. Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt. Science 1999; 286: 1738-1741.
    • (1999) Science , vol.286 , pp. 1738-1741
    • Rommel, C.1    Clarke, B.A.2    Zimmermann, S.3    Nuñez, L.4    Rossman, R.5    Reid, K.6
  • 78
    • 0035823542 scopus 로고    scopus 로고
    • Regulation of Raf by Akt controls growth and differentiation in vascular smooth muscle cells
    • Reusch HP, Zimmermann S, Schaefer M, Paul M, Moelling K. Regulation of Raf by Akt controls growth and differentiation in vascular smooth muscle cells. J Biol Chem 2001; 276: 33630-33637.
    • (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
  • 79
    • 0036236897 scopus 로고    scopus 로고
    • Cyclic AMP-dependent kinase regulates Raf-1 kinase mainly by phosphorylation of serine 259
    • Dhillon AS, Pollock C, Steen H, Shaw PE, Mischak H, Kolch W. Cyclic AMP-dependent kinase regulates Raf-1 kinase mainly by phosphorylation of serine 259. Mol Cell Biol 2002; 22: 3237-3246.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 3237-3246
    • Dhillon, A.S.1    Pollock, C.2    Steen, H.3    Shaw, P.E.4    Mischak, H.5    Kolch, W.6
  • 82
    • 0028293931 scopus 로고
    • Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf-1
    • Alessi DR, Saito Y, Campbell DG, Cohen P, Sithanandam G, Rapp U et al. Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf-1. EMBO J 1994; 13: 1610-1619.
    • (1994) EMBO J. , vol.13 , pp. 1610-1619
    • Alessi, D.R.1    Saito, Y.2    Campbell, D.G.3    Cohen, P.4    Sithanandam, G.5    Rapp, U.6
  • 83
    • 0028916307 scopus 로고
    • Biochemical and biological analysis of Mek1 phosphorylation site mutants
    • Huang W, Kessler DS, Erikson RL. Biochemical and biological analysis of Mek1 phosphorylation site mutants. Mol Biol Cell 1995; 6: 237-245.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 237-245
    • Huang, W.1    Kessler, D.S.2    Erikson, R.L.3
  • 84
    • 0029028358 scopus 로고
    • B-Raf protein isoforms interact with and phosphorylate Mek-1 on serine residues 218 and 222
    • Papin C, Eychene A, Brunet A, Pages G, Pouyssegur J, Calothey G et al. B-Raf protein isoforms interact with and phosphorylate Mek-1 on serine residues 218 and 222. Oncogene 1995; 10: 1647-1651.
    • (1995) Oncogene , vol.10 , pp. 1647-1651
    • Papin, C.1    Eychene, A.2    Brunet, A.3    Pages, G.4    Pouyssegur, J.5    Calothey, G.6
  • 85
    • 0030062094 scopus 로고    scopus 로고
    • Selective activation of MEK1 but not MEK2 by A-Raf from epidermal growth factor-stimulated Hela cells
    • Wu X, Noh SJ, Zhou G, Dixon JE, Guan KL. Selective activation of MEK1 but not MEK2 by A-Raf from epidermal growth factor-stimulated Hela cells. J Biol Chem 1996; 271: 3265-3271.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3265-3271
    • Wu, X.1    Noh, S.J.2    Zhou, G.3    Dixon, J.E.4    Guan, K.L.5
  • 86
    • 0037025377 scopus 로고    scopus 로고
    • Associations of B- and C-Raf with cholesterol, phosphatidylserine, and lipid second messengers: Preferential binding of Raf to artificial lipid rafts
    • Hekman M, Hamm H, Villar AV, Bader B, Kuhlmann J, Nickel J et al. Associations of B- and C-Raf with cholesterol, phosphatidylserine, and lipid second messengers: preferential binding of Raf to artificial lipid rafts. J Biol Chem 2002; 277: 24090-24102.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24090-24102
    • Hekman, M.1    Hamm, H.2    Villar, A.V.3    Bader, B.4    Kuhlmann, J.5    Nickel, J.6
  • 87
    • 85047697320 scopus 로고    scopus 로고
    • ERK signalling and oncogene transformation are not impaired in cells lacking A-Raf
    • Mercer K, Chiloeches A, Huser M, Kiernan M, Marais R, Pritchard C. ERK signalling and oncogene transformation are not impaired in cells lacking A-Raf. Oncogene 2002; 21: 347-355.
    • (2002) Oncogene , vol.21 , pp. 347-355
    • Mercer, K.1    Chiloeches, A.2    Huser, M.3    Kiernan, M.4    Marais, R.5    Pritchard, C.6
  • 88
    • 0036165251 scopus 로고    scopus 로고
    • Pharmacological inhibitors of MAPK pathways
    • English JM, Cobb MH. Pharmacological inhibitors of MAPK pathways. Trends Pharmacol Sci 2002; 23: 40-45.
    • (2002) Trends Pharmacol. Sci. , vol.23 , pp. 40-45
    • English, J.M.1    Cobb, M.H.2
  • 89
    • 0034080399 scopus 로고    scopus 로고
    • Signal transduction pathway targets for anticancer drug discovery
    • Adjei AA. Signal transduction pathway targets for anticancer drug discovery. Current Pharm Des 2000; 6: 361-378.
    • (2000) Current. Pharm. Des. , vol.6 , pp. 361-378
    • Adjei, A.A.1
  • 90
    • 0029081006 scopus 로고
    • MEKK1 phosphorylates MEK1 and MEK2 but does not cause activation of mitogen-activated protein kinase
    • Xu S, Robbins D, Frost J, Dang A, Lange-Carter C, Cobb MH. MEKK1 phosphorylates MEK1 and MEK2 but does not cause activation of mitogen-activated protein kinase. Proc Natl Acad Sci USA 1995; 92: 6808-6812.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6808-6812
    • Xu, S.1    Robbins, D.2    Frost, J.3    Dang, A.4    Lange-Carter, C.5    Cobb, M.H.6
  • 91
    • 0027233448 scopus 로고
    • Signal transduction via the MAP kinases: Proceed at your own RSK
    • Blenis J. Signal transduction via the MAP kinases: proceed at your own RSK. Proc Natl Acad Sci USA 1993; 90: 5889-5892.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5889-5892
    • Blenis, J.1
  • 92
    • 0036709020 scopus 로고    scopus 로고
    • Fidelity and spatiotemporal control in MAP kinase (ERKs) signaling
    • Pouyssegur J, Volmat V, Lenormand P. Fidelity and spatiotemporal control in MAP kinase (ERKs) signaling. Biochem Pharm 2002; 64: 755-763.
    • (2002) Biochem. Pharm. , vol.64 , pp. 755-763
    • Pouyssegur, J.1    Volmat, V.2    Lenormand, P.3
  • 93
    • 0032896457 scopus 로고    scopus 로고
    • RAS mutations and clonality analysis in children with juvenile myelomonocytic leukemia (JMML)
    • Flotho C, Valcamonica S, Mach-Pascual S, Schmahl G, Corral L, Ritterbach J et al. RAS mutations and clonality analysis in children with juvenile myelomonocytic leukemia (JMML). Leukemia 1999; 13: 32-37.
    • (1999) Leukemia , vol.13 , pp. 32-37
    • Flotho, C.1    Valcamonica, S.2    Mach-Pascual, S.3    Schmahl, G.4    Corral, L.5    Ritterbach, J.6
  • 95
    • 0023749162 scopus 로고
    • Mutations in ras genes in myelocytic leukemias and myelodysplastic syndromes
    • Bartram CR. Mutations in ras genes in myelocytic leukemias and myelodysplastic syndromes. Blood Cells 1988; 14: 533-538.
    • (1988) Blood Cells , vol.14 , pp. 533-538
    • Bartram, C.R.1
  • 96
    • 0029030083 scopus 로고
    • Differential effects of viral and cellular oncogenes on the growth factor-dependency of hematopoietic cells
    • McCubrey JA, Steelman LS, Wang X-Y, Algate PA, Hoyle PE, White C et al. Differential effects of viral and cellular oncogenes on the growth factor-dependency of hematopoietic cells. Int J Oncol 1995; 7: 295-310.
    • (1995) Int. J. Oncol. , vol.7 , pp. 295-310
    • McCubrey, J.A.1    Steelman, L.S.2    Wang, X.-Y.3    Algate, P.A.4    Hoyle, P.E.5    White, C.6
  • 98
    • 0040433650 scopus 로고
    • Rescue of cells from ras oncogene-induced growth arrest by a second complementing oncogene
    • Hirakawa T, Ruley HE. Rescue of cells from ras oncogene-induced growth arrest by a second complementing oncogene. Proc Natl Acad Sci USA 1988; 85: 1519-1523.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1519-1523
    • Hirakawa, T.1    Ruley, H.E.2
  • 99
    • 0022137480 scopus 로고
    • Microinjection of the ras oncogene protein into PC12 cells induces morphological differentiation
    • Bar-Sagi D, Feramisco JR. Microinjection of the ras oncogene protein into PC12 cells induces morphological differentiation. Cell 1985; 42: 841-848.
    • (1985) Cell , vol.42 , pp. 841-848
    • Bar-Sagi, D.1    Feramisco, J.R.2
  • 100
    • 0025743893 scopus 로고
    • Differentiation of 3T3-L1 fibroblasts to adipocytes induced by transfection of ras oncogenes
    • Benito M, Porras A, Nebreda AR, Santos E. Differentiation of 3T3-L1 fibroblasts to adipocytes induced by transfection of ras oncogenes. Science 1991; 253: 565-568.
    • (1991) Science , vol.253 , pp. 565-568
    • Benito, M.1    Porras, A.2    Nebreda, A.R.3    Santos, E.4
  • 103
    • 0033991281 scopus 로고    scopus 로고
    • Alternative effects of Ras and Raf oncogenes on the proliferation and apoptosis of factor-dependent FDC-P1 cells
    • McGlynn AP, Padua RA, Burnett AK, Darley RL. Alternative effects of Ras and Raf oncogenes on the proliferation and apoptosis of factor-dependent FDC-P1 cells. Leukemia Res 2000; 24: 47-54.
    • (2000) Leukemia Res. , vol.24 , pp. 47-54
    • McGlynn, A.P.1    Padua, R.A.2    Burnett, A.K.3    Darley, R.L.4
  • 105
    • 0031832770 scopus 로고    scopus 로고
    • The Raf-1 protein mediates insulin-like growth factor-induced proliferation of erythroid progenitor cells
    • Sanders MR, Lu H, Walker F, Sorbad S, Dainiak N. The Raf-1 protein mediates insulin-like growth factor-induced proliferation of erythroid progenitor cells. Stem Cells 1998; 16: 200-207.
    • (1998) Stem Cells , vol.16 , pp. 200-207
    • Sanders, M.R.1    Lu, H.2    Walker, F.3    Sorbad, S.4    Dainiak, N.5
  • 106
    • 0030901947 scopus 로고    scopus 로고
    • Induction of cell proliferation in quiescent NIH-3T3 cells by oncogenic c-Raf-1
    • Kerkhoff E, Rapp UR. Induction of cell proliferation in quiescent NIH-3T3 cells by oncogenic c-Raf-1. Mol Cell Biol 1997; 17: 2576-2586.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2576-2586
    • Kerkhoff, E.1    Rapp, U.R.2
  • 107
    • 0030889954 scopus 로고    scopus 로고
    • Selective inhibition of A-Raf and C-Raf mRNA expression by antisense oligodeoxynucleotides in rat vascular smooth muscle cells: Role of A-Raf and C-Raf in serum-induced proliferation
    • Cioffi CL, Garay M, Johnston JF, McGraw K, Boggs RT, Hreniuk BD et al. Selective inhibition of A-Raf and C-Raf mRNA expression by antisense oligodeoxynucleotides in rat vascular smooth muscle cells: role of A-Raf and C-Raf in serum-induced proliferation. Mol Pharmacol 1997; 51: 383-389.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 383-389
    • Cioffi, C.L.1    Garay, M.2    Johnston, J.F.3    McGraw, K.4    Boggs, R.T.5    Hreniuk, B.D.6
  • 110
    • 0028037057 scopus 로고
    • Expression of activated Raf accelerates cell differentiation and RB protein down-regulation but not hypophosphorylation
    • Yen A, Williams M, Platko JD, Der C, Hisaka M. Expression of activated Raf accelerates cell differentiation and RB protein down-regulation but not hypophosphorylation. Eur J Cell Biol 1994; 65: 103-113.
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 103-113
    • Yen, A.1    Williams, M.2    Platko, J.D.3    Der, C.4    Hisaka, M.5
  • 111
    • 0036045733 scopus 로고    scopus 로고
    • Molecular targets for therapy signal, transduction inhibitors and imatinib
    • Killmann NMB, McCubrey JA. Molecular targets for therapy signal, transduction inhibitors and imatinib. Leukemia 2002; 16: 1205.
    • (2002) Leukemia , vol.16 , pp. 1205
    • Killmann, N.M.B.1    McCubrey, J.A.2
  • 112
    • 0036045733 scopus 로고    scopus 로고
    • Spotlight imatinib: A model for signal transduction inhibitors and imatinib
    • Hochhaus A, McCubrey JA, Killmann NMB. Spotlight imatinib: a model for signal transduction inhibitors and imatinib. Leukemia 2002; 16: 1205-1206.
    • (2002) Leukemia , vol.16 , pp. 1205-1206
    • Hochhaus, A.1    McCubrey, J.A.2    Killmann, N.M.B.3
  • 113
    • 0035913161 scopus 로고    scopus 로고
    • Cip1 induced by Raf is associated with increased Cdk4 activity in hematopoietic cells
    • Cip1 induced by Raf is associated with increased Cdk4 activity in hematopoietic cells. Oncogene 2001; 20: 4354-4364.
    • (2001) Oncogene , vol.20 , pp. 4354-4364
    • Chang, F.1    McCubrey, J.A.2
  • 114
    • 0036581985 scopus 로고    scopus 로고
    • Raf-induced cell cycle progression in human TF-1 hematopoietic cells
    • Chang F, Steelman LS, McCubrey JA. Raf-induced cell cycle progression in human TF-1 hematopoietic cells. Cell Cycle 2002; 1: 220-226.
    • (2002) Cell Cycle , vol.1 , pp. 220-226
    • Chang, F.1    Steelman, L.S.2    McCubrey, J.A.3
  • 115
    • 0030029343 scopus 로고    scopus 로고
    • Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation
    • Jelinek T, Dent P, Sturgill TW, Weber MJ. Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation. Mol Cell Biol 1996; 16: 1027-1034.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1027-1034
    • Jelinek, T.1    Dent, P.2    Sturgill, T.W.3    Weber, M.J.4
  • 116
    • 0029934831 scopus 로고    scopus 로고
    • Different effects of various phospholipids on Ki-Ras-, Ha-Ras-, and Rap1B-induced B-Raf activation
    • Kuroda S, Ohtsuka T, Yamamori B, Fukui K, Shimizu K, Takai Y. Different effects of various phospholipids on Ki-Ras-, Ha-Ras-, and Rap1B-induced B-Raf activation. J Biol Chem 1996; 271: 14680-14683.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14680-14683
    • Kuroda, S.1    Ohtsuka, T.2    Yamamori, B.3    Fukui, K.4    Shimizu, K.5    Takai, Y.6
  • 117
    • 0033546419 scopus 로고    scopus 로고
    • Four human ras homologs differ in their abilities to activate Raf-1, induce transformation, and stimulate cell motility
    • Voice J K, Klemke RL, Le A, Jackson JH. Four human ras homologs differ in their abilities to activate Raf-1, induce transformation, and stimulate cell motility. J Biol Chem 1999; 274: 17164-17170.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17164-17170
    • Voice, J.K.1    Klemke, R.L.2    Le, A.3    Jackson, J.H.4
  • 118
    • 0034642548 scopus 로고    scopus 로고
    • Mitogenic signaling of Ras is regulated by differential interaction with Raf isozymes
    • Weber CK, Slupsky JR, Hermann C, Schuler M, Rapp UR, Block C. Mitogenic signaling of Ras is regulated by differential interaction with Raf isozymes. Oncogene 2000; 19: 169-176.
    • (2000) Oncogene , vol.19 , pp. 169-176
    • Weber, C.K.1    Slupsky, J.R.2    Hermann, C.3    Schuler, M.4    Rapp, U.R.5    Block, C.6
  • 122
    • 0028073606 scopus 로고
    • Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation
    • Freed E, Symons M, MacDonald SG, McCormick F, Ruggieri R. Binding of 14-3-3 proteins to the protein kinase Raf and effects on its activation. Science 1994; 265: 1713-1716.
    • (1994) Science , vol.265 , pp. 1713-1716
    • Freed, E.1    Symons, M.2    MacDonald, S.G.3    McCormick, F.4    Ruggieri, R.5
  • 123
    • 0028051904 scopus 로고
    • Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase
    • Irie K, Gotoh Y, Yashar BM, Errede B, Nishida E, Matsumoto K. Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase. Science 1994; 265: 1716-1719.
    • (1994) Science , vol.265 , pp. 1716-1719
    • Irie, K.1    Gotoh, Y.2    Yashar, B.M.3    Errede, B.4    Nishida, E.5    Matsumoto, K.6
  • 124
    • 0029971008 scopus 로고    scopus 로고
    • Identification of signaling proteins interacting with B-Raf in the yeast two-hybrid system
    • Papin C, Denouel A, Calothy G, Eychene A. Identification of signaling proteins interacting with B-Raf in the yeast two-hybrid system. Oncogene 1996; 12: 2213-2221.
    • (1996) Oncogene , vol.12 , pp. 2213-2221
    • Papin, C.1    Denouel, A.2    Calothy, G.3    Eychene, A.4
  • 125
    • 0032474838 scopus 로고    scopus 로고
    • A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
    • Tzivion G, Luo Z, Avruch J. A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity. Nature 1998; 394: 88-92.
    • (1998) Nature , vol.394 , pp. 88-92
    • Tzivion, G.1    Luo, Z.2    Avruch, J.3
  • 126
    • 0025266334 scopus 로고
    • Expression of raf family proto-oncogenes in normal mouse tissues
    • Storm SM, Cleveland JL, Rapp UR. Expression of raf family proto-oncogenes in normal mouse tissues. Oncogene 1990; 5: 345-351.
    • (1990) Oncogene , vol.5 , pp. 345-351
    • Storm, S.M.1    Cleveland, J.L.2    Rapp, U.R.3
  • 127
    • 0027411995 scopus 로고
    • Developmental and cell lineage specificity of raf family gene expression in mouse
    • Wadewitz AG, Winer MA, Wolgemuth DJ. Developmental and cell lineage specificity of raf family gene expression in mouse. Oncogene 1993; 8: 1055-1062.
    • (1993) Oncogene , vol.8 , pp. 1055-1062
    • Wadewitz, A.G.1    Winer, M.A.2    Wolgemuth, D.J.3
  • 130
    • 0033604576 scopus 로고    scopus 로고
    • Isotype-specific functions of Raf kinases
    • Hagemann C, Rapp UR. Isotype-specific functions of Raf kinases. Exp Cell Res 1999; 253: 34-46.
    • (1999) Exp. Cell Res. , vol.253 , pp. 34-46
    • Hagemann, C.1    Rapp, U.R.2
  • 131
    • 0030963439 scopus 로고    scopus 로고
    • CAMP activates MAP kinase and Elk-1 through a B-Raf and Rap1-dependent pathway
    • Vossler MR, Yao H, York RD, Pan M-G, Rim CS, Stork PJS. CAMP activates MAP kinase and Elk-1 through a B-Raf and Rap1-dependent pathway. Cell 1997; 89: 73-82.
    • (1997) Cell , vol.89 , pp. 73-82
    • Vossler, M.R.1    Yao, H.2    York, R.D.3    Pan, M.-G.4    Rim, C.S.5    Stork, P.J.S.6
  • 133
    • 0345252018 scopus 로고    scopus 로고
    • Activation of the Raf/MAP kinase cascade by the Ras-related protein TC21 is required for the TC21-mediated transformation of NIH-3T3 cells
    • Rosario M, Paterson HF, Marshall CJ. Activation of the Raf/MAP kinase cascade by the Ras-related protein TC21 is required for the TC21-mediated transformation of NIH-3T3 cells. EMBO J 1999; 18: 1270-1279.
    • (1999) EMBO J. , vol.18 , pp. 1270-1279
    • Rosario, M.1    Paterson, H.F.2    Marshall, C.J.3
  • 134
    • 0032527620 scopus 로고    scopus 로고
    • Interaction between the protein kinase B-Raf and the alpha-subunit of the 11S proteasome regulator
    • Kalmes A, Hagemann C, Weber CK, Wixler L, Schuster T, Rapp UR. Interaction between the protein kinase B-Raf and the alpha-subunit of the 11S proteasome regulator. Cancer Res 1998; 58: 2986-2990.
    • (1998) Cancer Res. , vol.58 , pp. 2986-2990
    • Kalmes, A.1    Hagemann, C.2    Weber, C.K.3    Wixler, L.4    Schuster, T.5    Rapp, U.R.6
  • 135
    • 0033596121 scopus 로고    scopus 로고
    • Activators and target genes of Rel/NF-κB transcription factors
    • Pahl HL. Activators and target genes of Rel/NF-κB transcription factors. Oncogene 1999; 18: 6853-6866.
    • (1999) Oncogene , vol.18 , pp. 6853-6866
    • Pahl, H.L.1
  • 136
    • 0035139792 scopus 로고    scopus 로고
    • Therapeutic potential of inhibition of the NF-κB pathway in the treatment of inflammation and cancer
    • Yamamoto Y, Gaynor RB. Therapeutic potential of inhibition of the NF-κB pathway in the treatment of inflammation and cancer. J Clin Invest 2001; 107: 135-142.
    • (2001) J. Clin. Invest. , vol.107 , pp. 135-142
    • Yamamoto, Y.1    Gaynor, R.B.2
  • 137
    • 0033596120 scopus 로고    scopus 로고
    • Regulation of DNA binding by Rel/NF-kappaB transcription factors: Structural views
    • Chen FE, Ghosh G. Regulation of DNA binding by Rel/NF-kappaB transcription factors: structural views. Oncogene 1999; 18: 6845-6852.
    • (1999) Oncogene , vol.18 , pp. 6845-6852
    • Chen, F.E.1    Ghosh, G.2
  • 138
    • 0032508414 scopus 로고    scopus 로고
    • NE-κB antiapoptosis: Induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation
    • Wang CY, Mayo MW, Komeluk RG, Goeddel DV, Baldwin Jr AS. NE-κB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 1998; 281: 1680-1683.
    • (1998) Science , vol.281 , pp. 1680-1683
    • Wang, C.Y.1    Mayo, M.W.2    Komeluk, R.G.3    Goeddel, D.V.4    Baldwin A.S., Jr.5
  • 139
    • 0033596122 scopus 로고    scopus 로고
    • Control of development and immunity by Rel transcription factors in Drosophila
    • Govind S. Control of development and immunity by Rel transcription factors in Drosophila. Oncogene 1999; 18: 6875-6887.
    • (1999) Oncogene , vol.18 , pp. 6875-6887
    • Govind, S.1
  • 140
    • 0035137882 scopus 로고    scopus 로고
    • Control of oncogenesis and cancer therapy resistance by the transcription factor NF-κB
    • Baldwin AS. Control of oncogenesis and cancer therapy resistance by the transcription factor NF-κB. J Clin Invest 2001; 107: 241-246.
    • (2001) J. Clin. Invest. , vol.107 , pp. 241-246
    • Baldwin, A.S.1
  • 141
    • 0030882666 scopus 로고    scopus 로고
    • Oncogenic Ha-Ras-induced signaling activates NF-κB transcriptional activity, which is required for cellular transformation
    • Finco TS, Westwick JK, Norris JL, Beg AA, Der CJ, Baldwin Jr AS. Oncogenic Ha-Ras-induced signaling activates NF-κB transcriptional activity, which is required for cellular transformation. J Biol Chem 1997; 272: 24113-24116.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24113-24116
    • Finco, T.S.1    Westwick, J.K.2    Norris, J.L.3    Beg, A.A.4    Der, C.J.5    Baldwin A.S., Jr.6
  • 142
    • 0025139463 scopus 로고
    • NF-κB as inducible transcriptional activator of the granulocyte-macrophage colony-stimulating factor gene
    • Schreck R, Baeuerle PA. NF-κB as inducible transcriptional activator of the granulocyte-macrophage colony-stimulating factor gene. Mol Cell Biol 1990; 10: 1281-1286.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 1281-1286
    • Schreck, R.1    Baeuerle, P.A.2
  • 143
    • 0033595892 scopus 로고    scopus 로고
    • The Rel/NF-κB signal transduction pathway: Introduction
    • Gilmore TD. The Rel/NF-κB signal transduction pathway: introduction. Oncogene 1999; 18: 6845-6852.
    • (1999) Oncogene , vol.18 , pp. 6845-6852
    • Gilmore, T.D.1
  • 144
    • 0025943986 scopus 로고
    • The p65 subunit is responsible for the strong transcription activating potential of NF-κB
    • Schmitz ML, Baeuerle P. The p65 subunit is responsible for the strong transcription activating potential of NF-κB. EMBO J 1991; 10: 3805-3817.
    • (1991) EMBO J. , vol.10 , pp. 3805-3817
    • Schmitz, M.L.1    Baeuerle, P.2
  • 145
    • 0026570254 scopus 로고
    • Functional characterization of the NF-κB p65 transcriptional activator and an alternatively spliced derivative
    • Ruben SM, Narayanan R, Klement JF, Chen CH, Rosen CA. Functional characterization of the NF-κB p65 transcriptional activator and an alternatively spliced derivative. Mol Cell Biol 1192; 12: 444-454.
    • (1192) Mol. Cell Biol. , vol.12 , pp. 444-454
    • Ruben, S.M.1    Narayanan, R.2    Klement, J.F.3    Chen, C.H.4    Rosen, C.A.5
  • 146
    • 0031126395 scopus 로고    scopus 로고
    • I kappa B proteins: Structure, function and regulation
    • Whiteside ST, Israel A. I kappa B proteins: structure, function and regulation. Semin Cancer Biol 1999; 8: 75-82.
    • (1999) Semin. Cancer Biol. , vol.8 , pp. 75-82
    • Whiteside, S.T.1    Israel, A.2
  • 147
    • 0035282213 scopus 로고    scopus 로고
    • IκB-independent control of NF-κB activity by modulatory phosphorylations
    • Schmitz ML, Bacher S, Kracht M. IκB-independent control of NF-κB activity by modulatory phosphorylations. Trends Biochem Sci 2001; 26: 186-190.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 186-190
    • Schmitz, M.L.1    Bacher, S.2    Kracht, M.3
  • 148
    • 0034175930 scopus 로고    scopus 로고
    • The IKK complex: An integrator of all signals that activate NF-κB?
    • Israel A. The IKK complex: an integrator of all signals that activate NF-κB? Trends Cell Biol 2000; 10: 129-133.
    • (2000) Trends Cell Biol. , vol.10 , pp. 129-133
    • Israel, A.1
  • 149
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • Karin M, Ben-Neriah Y. Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu Rev Immunol 2000; 18: 621-663.
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 150
    • 0033595893 scopus 로고    scopus 로고
    • How NF-κB is activated: The role of the IκB kinase (IKK) Complex
    • Karin M. How NF-κB is activated: the role of the IκB kinase (IKK) Complex. Oncogene 1999; 18: 6867-6874.
    • (1999) Oncogene , vol.18 , pp. 6867-6874
    • Karin, M.1
  • 151
    • 0029670083 scopus 로고    scopus 로고
    • Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation
    • DiDonato J, Mercurio F, Rosette C, Wu-Li J, Suyang H, Ghosh S et al. Mapping of the inducible IκB phosphorylation sites that signal its ubiquitination and degradation. Mol Cell Biol 1996; 16: 1295-1304.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 1295-1304
    • DiDonato, J.1    Mercurio, F.2    Rosette, C.3    Wu-Li, J.4    Suyang, H.5    Ghosh, S.6
  • 152
    • 0033002197 scopus 로고    scopus 로고
    • Bridging the gap: Composition, regulation, and physiological function of the IκB kinase complex
    • Zandi E, Karin M. Bridging the gap: composition, regulation, and physiological function of the IκB kinase complex. Mol Cell Biol 1999; 19: 4547-4551.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4547-4551
    • Zandi, E.1    Karin, M.2
  • 153
    • 0034745011 scopus 로고    scopus 로고
    • Control Of IκBα proteolysis by the ubiquitin-proteasome pathway
    • Tanaka K, Kawakami T, Tateishi K, Yashiroda H, Chiba T. Control Of IκBα proteolysis by the ubiquitin-proteasome pathway. Biochimie 2001; 83: 351-356.
    • (2001) Biochimie , vol.83 , pp. 351-356
    • Tanaka, K.1    Kawakami, T.2    Tateishi, K.3    Yashiroda, H.4    Chiba, T.5
  • 154
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the licB kinase complex essential for NF-κB activation
    • Yamaoka S, Courtois G, Bessia C, Whiteside ST, Weil R, Agou F et al. Complementation cloning of NEMO, a component of the licB kinase complex essential for NF-κB activation. Cell 1998; 93: 1231-1240.
    • (1998) Cell , vol.93 , pp. 1231-1240
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3    Whiteside, S.T.4    Weil, R.5    Agou, F.6
  • 155
    • 0032583947 scopus 로고    scopus 로고
    • NF-κB-inducing kinase activates IKK-α by phosphorylation of Ser-176
    • Ling L, Zhaodan C, Goeddel DV. NF-κB-inducing kinase activates IKK-α by phosphorylation of Ser-176. Proc Natl Acad Sci USA 1998; 95: 3792-3797.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3792-3797
    • Ling, L.1    Zhaodan, C.2    Goeddel, D.V.3
  • 156
    • 0032583949 scopus 로고    scopus 로고
    • Differential regulation Of IκB kinase α and β by two upstream kinases, NF-κB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1
    • Nakano H, Shindo M, Sakon S, Nishinaka S, Mihara M, Yagita H et al. Differential regulation Of IκB kinase α and β by two upstream kinases, NF-κB-inducing kinase and mitogen-activated protein kinase/ERK kinase kinase-1. Proc Natl Acad Sci USA 1998; 95: 3537-3542.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3537-3542
    • Nakano, H.1    Shindo, M.2    Sakon, S.3    Nishinaka, S.4    Mihara, M.5    Yagita, H.6
  • 158
    • 0031597368 scopus 로고    scopus 로고
    • Coordinate regulation of IκB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-κB-inducing kinase
    • Nemoto S, DiDonato JA, Lin A. Coordinate regulation of IκB kinases by mitogen-activated protein kinase kinase kinase 1 and NF-κB-inducing kinase. Mol Cell Biol 1998; 18: 7336-7343.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 7336-7343
    • Nemoto, S.1    DiDonato, J.A.2    Lin, A.3
  • 159
    • 0034693133 scopus 로고    scopus 로고
    • TNFα-induced phosphorylation of RelA/p65 on ser529 is controlled by casein kinase II
    • Wang D, Westerheide SD, Hanson JL, Baldwin Jr AS. TNFα-induced phosphorylation of RelA/p65 on ser529 is controlled by casein kinase II. J Biol Chem 2000; 275: 32592-32597.
    • (2000) J. Biol. Chem. , vol.275 , pp. 32592-32597
    • Wang, D.1    Westerheide, S.D.2    Hanson, J.L.3    Baldwin A.S., Jr.4
  • 160
    • 0032589462 scopus 로고    scopus 로고
    • IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain
    • Sakurai H, Chiba H, Miyoshi H, Sugita T, Toriumi W. IκB kinases phosphorylate NF-κB p65 subunit on serine 536 in the transactivation domain. J Biol Chem 1999; 274: 30353-30356.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30353-30356
    • Sakurai, H.1    Chiba, H.2    Miyoshi, H.3    Sugita, T.4    Toriumi, W.5
  • 161
    • 0032491485 scopus 로고    scopus 로고
    • Activation of nuclear factor-κB-dependent transcription by tumor necrosis factor-α is mediated through phosphorylation of RelA/p65 on serine 529
    • Wang D, Baldwin Jr AS. Activation of nuclear factor-κB-dependent transcription by tumor necrosis factor-α is mediated through phosphorylation of RelA/p65 on serine 529. J Biol Chem 1998; 73: 29411-29416.
    • (1998) J. Biol. Chem. , vol.73 , pp. 29411-29416
    • Wang, D.1    Baldwin A.S., Jr.2
  • 162
    • 0032039076 scopus 로고    scopus 로고
    • Phosphorylation of NF-κB p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300
    • Zhong H, Voll RE, Ghosh S. Phosphorylation of NF-κB p65 by PKA stimulates transcriptional activity by promoting a novel bivalent interaction with the coactivator CBP/p300. Mol Cell 1998; 1: 661-671.
    • (1998) Mol. Cell , vol.1 , pp. 661-671
    • Zhong, H.1    Voll, R.E.2    Ghosh, S.3
  • 164
    • 0033553466 scopus 로고    scopus 로고
    • Oncogenic Ras enhances NF-κB transcriptional activity through Raf-dependent and Raf-independent mitogen-activated protein kinase signaling pathways
    • Norris JL, Baldwin Jr AS. Oncogenic Ras enhances NF-κB transcriptional activity through Raf-dependent and Raf-independent mitogen-activated protein kinase signaling pathways. J Biol Chem 1999; 274: 13841-13846.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13841-13846
    • Norris, J.L.1    Baldwin A.S., Jr.2
  • 166
    • 0035354187 scopus 로고    scopus 로고
    • Nuclear factor-κB is constitutively active in C-cell carcinoma and required for RET-induced transformation
    • Ludwig L, Kessler H, Wagne M, Hoang-Vu C, Dralle H, Adler G et al. Nuclear factor-κB is constitutively active in C-cell carcinoma and required for RET-induced transformation. Cancer Res 2001; 61: 4526-4535.
    • (2001) Cancer Res. , vol.61 , pp. 4526-4535
    • Ludwig, L.1    Kessler, H.2    Wagne, M.3    Hoang-Vu, C.4    Dralle, H.5    Adler, G.6
  • 167
    • 0029130410 scopus 로고
    • Rapid induction of heparin-binding epidermal growth factor/diphtheria toxin receptor expression by Raf and Ras oncogenes
    • McCarthy SA, Samuels ML, Pritchard CA, Abraham JA, McMahon M. Rapid induction of heparin-binding epidermal growth factor/diphtheria toxin receptor expression by Raf and Ras oncogenes. Genes Dev 1995; 9: 1953-1964.
    • (1995) Genes Dev. , vol.9 , pp. 1953-1964
    • McCarthy, S.A.1    Samuels, M.L.2    Pritchard, C.A.3    Abraham, J.A.4    McMahon, M.5
  • 168
    • 0030974039 scopus 로고    scopus 로고
    • Rapid phosphorylation of Ets-2 accompanies mitogen-activated protein kinase activation and the induction-of heparin-binding epidermal growth factor gene expression by oncogenic Raf-1
    • McCarthy SA, Chen D, Yang BS, Garcia Ramirez JJ, Cherwinski H, Chen XR et al. Rapid phosphorylation of Ets-2 accompanies mitogen-activated protein kinase activation and the induction-of heparin-binding epidermal growth factor gene expression by oncogenic Raf-1. Mol Cell Biol 1997; 17: 2401-2412.
    • (1997) Mol. Cell Biol. , vol.17 , pp. 2401-2412
    • McCarthy, S.A.1    Chen, D.2    Yang, B.S.3    Garcia Ramirez, J.J.4    Cherwinski, H.5    Chen, X.R.6
  • 171
    • 0030851775 scopus 로고    scopus 로고
    • The 90-kDa ribosomal S6 kinase (pp90rsk) phosphorylates the N-terminal regulatory domain of IκBα and stimulates its degradation in vitro
    • Ghoda L, Lin X, Greene WC. The 90-kDa ribosomal S6 kinase (pp90rsk) phosphorylates the N-terminal regulatory domain of IκBα and stimulates its degradation in vitro. J Biol Chem 1997; 272:21281-21288.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21281-21288
    • Ghoda, L.1    Lin, X.2    Greene, W.C.3
  • 172
    • 0034789898 scopus 로고    scopus 로고
    • A MEK inhibitor, PD98059 enhances IL-1-induced NF-κB activation by the enhanced and sustained degradation of IκBα
    • Funakoshi M, Tago K, Sonoda Y, Tominaga S, Kasahara T. A MEK inhibitor, PD98059 enhances IL-1-induced NF-κB activation by the enhanced and sustained degradation of IκBα. Biochem Biophys Res Commun 2001; 283: 248-254.
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 248-254
    • Funakoshi, M.1    Tago, K.2    Sonoda, Y.3    Tominaga, S.4    Kasahara, T.5
  • 173
    • 0031041602 scopus 로고    scopus 로고
    • CREB is activated by UVC through a p38/HOG-1-dependent protein kinase
    • Iordanov M, Bender K, Ade T, Schmid W, Sachsenmaier C, Engel K et al. CREB is activated by UVC through a p38/HOG-1-dependent protein kinase. EMBO J 1997; 16: 1009-1022.
    • (1997) EMBO J. , vol.16 , pp. 1009-1022
    • Iordanov, M.1    Bender, K.2    Ade, T.3    Schmid, W.4    Sachsenmaier, C.5    Engel, K.6
  • 174
    • 0032575574 scopus 로고    scopus 로고
    • A protein kinase C-, Ras-, and RSK2-dependent signal transduction pathway activates the cAMP-responsive element-binding protein transcription factor following T cell receptor engagement
    • Muthusamy N, Leiden JM. A protein kinase C-, Ras-, and RSK2-dependent signal transduction pathway activates the cAMP-responsive element-binding protein transcription factor following T cell receptor engagement. J Biol Chem 1998; 273: 22841-22847.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22841-22847
    • Muthusamy, N.1    Leiden, J.M.2
  • 175
    • 0033773179 scopus 로고    scopus 로고
    • Mechanisms of transcriptional activation of cAMP-responsive element-binding protein CREB
    • Haus-Seuffert P, Meisterernst M. Mechanisms of transcriptional activation of cAMP-responsive element-binding protein CREB. Mol Cell Biochem 2000; 212: 5-9.
    • (2000) Mol. Cell Biochem. , vol.212 , pp. 5-9
    • Haus-Seuffert, P.1    Meisterernst, M.2
  • 176
    • 0033995549 scopus 로고    scopus 로고
    • ATF and Jun transcription factors, acting through an Ets/CRE promoter module, mediate lipopolysaccharide inducibility of the chemokine RANTES in monocytic Mono Mac 6 cells
    • Boehlk S, Fessele S, Mojaat A, Miyamoto NG, Werner T, Nelson EL et al. ATF and Jun transcription factors, acting through an Ets/CRE promoter module, mediate lipopolysaccharide inducibility of the chemokine RANTES in monocytic Mono Mac 6 cells. Eur J Immunol 2000; 30: 1102-1112.
    • (2000) Eur. J. Immunol. , vol.30 , pp. 1102-1112
    • Boehlk, S.1    Fessele, S.2    Mojaat, A.3    Miyamoto, N.G.4    Werner, T.5    Nelson, E.L.6
  • 178
    • 0031821578 scopus 로고    scopus 로고
    • Activation of the Rat cyclin A promoter by ATF2 and Jun family members and its suppression by ATF4
    • Shimizu M, Nomura Y, Suzuki H, Ichikawa E, Takeuchi A, Suzuki M et al. Activation of the Rat cyclin A promoter by ATF2 and Jun family members and its suppression by ATF4. Exp Cell Res 1998; 239: 93-103.
    • (1998) Exp. Cell Res. , vol.239 , pp. 93-103
    • Shimizu, M.1    Nomura, Y.2    Suzuki, H.3    Ichikawa, E.4    Takeuchi, A.5    Suzuki, M.6
  • 180
    • 0035808326 scopus 로고    scopus 로고
    • 1 gene is mediated by multiple cis-elements. including SP1 sites and a cAMP-responsive element in vascular endothelial cells
    • 1 gene is mediated by multiple cis-elements. including SP1 sites and a cAMP-responsive element in vascular endothelial cells. J Biol Chem 2001; 276: 662-669.
    • (2001) J. Biol. Chem. , vol.276 , pp. 662-669
    • Nagata, D.1    Suzuki, E.2    Nishimatsu, H.3    Satonaka, H.4    Goto, A.5    Omata, M.6
  • 181
    • 0032947179 scopus 로고    scopus 로고
    • Glumate induces phosphorylation of Elk-1 and CREB, along with c-fos activation, via an extracellular signal-regulated kinase-dependent pathway in brain slices
    • Vanhoutte P, Barrier J, Gilbert B, Pages C, Besson M, Hipskind RA et al. Glumate induces phosphorylation of Elk-1 and CREB, along with c-fos activation, via an extracellular signal-regulated kinase-dependent pathway in brain slices. Mol Cell Biol 1999; 19: 136-146.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 136-146
    • Vanhoutte, P.1    Barrier, J.2    Gilbert, B.3    Pages, C.4    Besson, M.5    Hipskind, R.A.6
  • 182
    • 0034624822 scopus 로고    scopus 로고
    • Activation of the c-fos enhancer by the erk MAP kinase pathway through two sequence elements: The c-fos AP-1 and p62TCF sites
    • Wang Y, Prywes R. Activation of the c-fos enhancer by the erk MAP kinase pathway through two sequence elements: the c-fos AP-1 and p62TCF sites. Oncogene 2000; 19: 1379-1385.
    • (2000) Oncogene , vol.19 , pp. 1379-1385
    • Wang, Y.1    Prywes, R.2
  • 183
    • 0033600722 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 induces bcl-2 promoter through the transcription factor cAMP-responsive element-binding protein
    • Pugazhenthi S, Miller E, Sable C, Young P, Heidenreich KA, Boxer LM et al. Insulin-like growth factor-1 induces bcl-2 promoter through the transcription factor cAMP-responsive element-binding protein. J Biol Chem 1999; 274: 27529-27535.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27529-27535
    • Pugazhenthi, S.1    Miller, E.2    Sable, C.3    Young, P.4    Heidenreich, K.A.5    Boxer, L.M.6
  • 184
    • 0035394360 scopus 로고    scopus 로고
    • Molecular mechanisms of transcriptional control of bcl-2 and c-myc in follicular and transformed lymphoma
    • Arcinas M, Heckman CA, Mehew JW, Boxer LM. Molecular mechanisms of transcriptional control of bcl-2 and c-myc in follicular and transformed lymphoma. Cancer Res 2001; 61: 5202-5206.
    • (2001) Cancer Res. , vol.61 , pp. 5202-5206
    • Arcinas, M.1    Heckman, C.A.2    Mehew, J.W.3    Boxer, L.M.4
  • 185
    • 0029810469 scopus 로고    scopus 로고
    • Induction of bcl-2 expression by phosphorylated CREB proteins during B-cell activation and rescue from apoptosis
    • Wilson BE, Mochon E, Boxer LM. Induction of bcl-2 expression by phosphorylated CREB proteins during B-cell activation and rescue from apoptosis. Mol Cell Biol 1996; 16: 5546-5556.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 5546-5556
    • Wilson, B.E.1    Mochon, E.2    Boxer, L.M.3
  • 186
    • 0029935418 scopus 로고    scopus 로고
    • Regulation of transcription by MAP kinase cascades
    • Treisman R. Regulation of transcription by MAP kinase cascades. Curr Opin Cell Biol 1996; 8: 205-215.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 205-215
    • Treisman, R.1
  • 187
    • 0026722103 scopus 로고
    • The serum response element
    • Treisman R. The serum response element. Trends Biochem Sci 1992; 17: 423-426.
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 423-426
    • Treisman, R.1
  • 188
    • 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
    • De Cesare D, Jacquot S, Hanauer A, Sassone-Corsi P. 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 1998; 95: 12202-12207.
    • (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
  • 190
    • 0030902507 scopus 로고    scopus 로고
    • Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors
    • Nakajima T, Uchida C, Anderson SF, Parvin JD, Montminy M. Analysis of a cAMP-responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors. Genes Dev 1997; 11: 738-747.
    • (1997) Genes Dev. , vol.11 , pp. 738-747
    • Nakajima, T.1    Uchida, C.2    Anderson, S.F.3    Parvin, J.D.4    Montminy, M.5
  • 192
    • 0033000990 scopus 로고    scopus 로고
    • Histone acetylases and deacetylases in cell proliferation
    • Kouzarides T. Histone acetylases and deacetylases in cell proliferation. Curr Opin Genet Dev 1999; 9: 40-48.
    • (1999) Curr. Opin. Genet. Dev. , vol.9 , pp. 40-48
    • Kouzarides, T.1
  • 193
    • 0030463470 scopus 로고    scopus 로고
    • 2+- and stimulus duration-dependent switch for hippocampal gene expression
    • 2+- and stimulus duration-dependent switch for hippocampal gene expression. Cell 1996; 87: 1203-1214.
    • (1996) Cell , vol.87 , pp. 1203-1214
    • Bito, H.1    Deisseroth, K.2    Tsien, R.W.3
  • 194
    • 0029789643 scopus 로고    scopus 로고
    • Coupling of the RAS-MAPK-pathway to gene activation by RSK2, a growth factor-regulated CREB kinase
    • Xing J, Ginty DD, Greenberg ME. Coupling of the RAS-MAPK-pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. Science 1996; 273: 959-963.
    • (1996) Science , vol.273 , pp. 959-963
    • Xing, J.1    Ginty, D.D.2    Greenberg, M.E.3
  • 195
    • 0027981633 scopus 로고
    • Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression
    • Matthews RP, Guthrie CR, Wailes LM, Zhao X, Means AR, McKnight GS. Calcium/calmodulin-dependent protein kinase types II and IV differentially regulate CREB-dependent gene expression. Mol Cell Biol 1994; 14: 6107-6116.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 6107-6116
    • Matthews, R.P.1    Guthrie, C.R.2    Wailes, L.M.3    Zhao, X.4    Means, A.R.5    McKnight, G.S.6
  • 196
    • 0027983480 scopus 로고
    • Positive regulation of the cAMP-responsive activator CREM by the p70 S6 kinase: An alternative route to mitogen-induced gene expression
    • De Groot R, Ballou LM, Sassone-Corsi P. Positive regulation of the cAMP-responsive activator CREM by the p70 S6 kinase: an alternative route to mitogen-induced gene expression. Cell 1994; 79: 81-91.
    • (1994) Cell , vol.79 , pp. 81-91
    • De Groot, R.1    Ballou, L.M.2    Sassone-Corsi, P.3
  • 197
    • 0032479983 scopus 로고    scopus 로고
    • Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB
    • Deak M, Clifton AD, Lucocq JM, Alessi DR. Mitogen- and stress-activated protein kinase-1 (MSK1) is directly activated by MAPK and SAPK2/p38, and may mediate activation of CREB. EMB0 J 1998; 17: 4426-4441.
    • (1998) EMBO J. , vol.17 , pp. 4426-4441
    • Deak, M.1    Clifton, A.D.2    Lucocq, J.M.3    Alessi, D.R.4
  • 199
    • 0030783628 scopus 로고    scopus 로고
    • Cross-talk in signal transduction: Ras-dependent induction of cAMP-responsive transcriptional repressor ICER by nerve growth factor
    • Monaco L, Sassone-Corsi P. Cross-talk in signal transduction: Ras-dependent induction of cAMP-responsive transcriptional repressor ICER by nerve growth factor. Oncogene 1997; 15: 2493-2500.
    • (1997) Oncogene , vol.15 , pp. 2493-2500
    • Monaco, L.1    Sassone-Corsi, P.2
  • 201
    • 0032589380 scopus 로고    scopus 로고
    • Activation of p90RSK and cAMP response element binding protein in stimulated neutrophils: Novel effects of the pyridinyl imidazole SB 203580 on activation of the extracellular signal-regulated kinase cascade
    • Lian JP, Huang R, Robinson D, Badwey JA. Activation of p90RSK and cAMP response element binding protein in stimulated neutrophils: novel effects of the pyridinyl imidazole SB 203580 on activation of the extracellular signal-regulated kinase cascade. J Immunol 1999; 163: 4527-4536.
    • (1999) J. Immunol. , vol.163 , pp. 4527-4536
    • Lian, J.P.1    Huang, R.2    Robinson, D.3    Badwey, J.A.4
  • 203
    • 0029883919 scopus 로고    scopus 로고
    • ETS1 and ETS2 in p53 regulatin: Spatial separation of ETS binding sites (EBS) modulate protein: DNA interaction
    • Vananzoni MC, Robinson LR, Hodge DR, Kola I, Seth A. ETS1 and ETS2 in p53 regulatin: spatial separation of ETS binding sites (EBS) modulate protein: DNA interaction. Oncogene 1996; 12: 1199-1204.
    • (1996) Oncogene , vol.12 , pp. 1199-1204
    • Vananzoni, M.C.1    Robinson, L.R.2    Hodge, D.R.3    Kola, I.4    Seth, A.5
  • 204
    • 0027933827 scopus 로고
    • Serum response factor associated ETS proteins: Ternary complex factors and PEA3-binding factor
    • Liu SH, Ng SY. Serum response factor associated ETS proteins: ternary complex factors and PEA3-binding factor. Biochem Biophys Res Commun 1994; 201: 1406-1413.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 1406-1413
    • Liu, S.H.1    Ng, S.Y.2
  • 207
    • 0032974230 scopus 로고    scopus 로고
    • Fil-1, an Ets-related transcription factor, regulates erythropoietin-induced erythroid proliferation and differentiation evidence for direct transcriptional repression of the Rb gene during differentiation
    • Tamir A, Howard J, Higgins RR, Li YJ, Berger L, Zacksenhaus E et al. Fil-1, an Ets-related transcription factor, regulates erythropoietin-induced erythroid proliferation and differentiation evidence for direct transcriptional repression of the Rb gene during differentiation. Mol Cell Biol 1999; 19: 4452-4464.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4452-4464
    • Tamir, A.1    Howard, J.2    Higgins, R.R.3    Li, Y.J.4    Berger, L.5    Zacksenhaus, E.6
  • 209
    • 0029844212 scopus 로고    scopus 로고
    • v-Myb of E26 leukemia virus upregulates bcl-2 and suppress apoptosis in myeloid cells
    • Frampton J, Ramqvist T, Graf T. v-Myb of E26 leukemia virus upregulates bcl-2 and suppress apoptosis in myeloid cells. Genes Dev 1996; 10: 2720-2731.
    • (1996) Genes Dev. , vol.10 , pp. 2720-2731
    • Frampton, J.1    Ramqvist, T.2    Graf, T.3
  • 210
    • 0032935396 scopus 로고    scopus 로고
    • The Ets2 transcription factor inhibits apoptosis induced by colony stimulating factor 1 deprivation of macrophages through a Bcl-xL-dependent mechanism
    • Sevilla L, Aperlo C, Dulic V, Chambard JC, Boutonnet C, Pasquier O et al. The Ets2 transcription factor inhibits apoptosis induced by colony stimulating factor 1 deprivation of macrophages through a Bcl-xL-dependent mechanism. Mol Cell Biol 1999; 19: 2624-2634.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 2624-2634
    • Sevilla, L.1    Aperlo, C.2    Dulic, V.3    Chambard, J.C.4    Boutonnet, C.5    Pasquier, O.6
  • 211
    • 0033521026 scopus 로고    scopus 로고
    • Transcriptional regulation of Fas gene expression by GA-binding protein and AP-1 in T cell antigen receptor.CD3 complex-stimulated T cells
    • Li XR, Chong AS, Wu J, Roebuck KA, Kumar A, Parrillo JE et al. Transcriptional regulation of Fas gene expression by GA-binding protein and AP-1 in T cell antigen receptor.CD3 complex-stimulated T cells. J Biol Chem 1999; 274: 35203-35210.
    • (1999) J. Biol. Chem. , vol.274 , pp. 35203-35210
    • Li, X.R.1    Chong, A.S.2    Wu, J.3    Roebuck, K.A.4    Kumar, A.5    Parrillo, J.E.6
  • 212
    • 0034640284 scopus 로고    scopus 로고
    • An ordered array of cold shock domain repressor elements across tumor necrosis factor-responsive elements of the granulocyte-macrophage colony-stimulating factor promoter
    • Coles LS, Diamond P, Occhiodoro F, Vadas MA, Shannon MF. An ordered array of cold shock domain repressor elements across tumor necrosis factor-responsive elements of the granulocyte-macrophage colony-stimulating factor promoter. J Biol Chem 2000; 275: 14482-14493.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14482-14493
    • Coles, L.S.1    Diamond, P.2    Occhiodoro, F.3    Vadas, M.A.4    Shannon, M.F.5
  • 213
    • 0030013142 scopus 로고    scopus 로고
    • Transcriptional regulation of interleukin-3 expression in megakaryocytes
    • Nimer S, Zhang J, Avraham H, Miyazaki Y. Transcriptional regulation of interleukin-3 expression in megakaryocytes. Blood 1996; 88: 66-74.
    • (1996) Blood , vol.88 , pp. 66-74
    • Nimer, S.1    Zhang, J.2    Avraham, H.3    Miyazaki, Y.4
  • 214
    • 0032509413 scopus 로고    scopus 로고
    • Identification of a cell type-specific enhancer in the distal 5′-region of the platelet-derived growth factor A-chain gene
    • Maul RS, Zhang H, Reid JDT, Pedigo NG, Kaetzel DM. Identification of a cell type-specific enhancer in the distal 5′-region of the platelet-derived growth factor A-chain gene. J Biol Chem 1998; 273: 33239-33246.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33239-33246
    • Maul, R.S.1    Zhang, H.2    Reid, J.D.T.3    Pedigo, N.G.4    Kaetzel, D.M.5
  • 215
    • 0034684622 scopus 로고    scopus 로고
    • Proteins of the ETS family with transcriptional receptor activity
    • Mavrothalassitis G, Ghysdael J. Proteins of the ETS family with transcriptional receptor activity. Oncogene 2000; 19: 6524-6532.
    • (2000) Oncogene , vol.19 , pp. 6524-6532
    • Mavrothalassitis, G.1    Ghysdael, J.2
  • 216
    • 0030048767 scopus 로고    scopus 로고
    • Ras-mediated phosphorylation of a conserved threonine residue enhances the transactivation activities of c-Ets1 and c-Ets2
    • Yang B, Hauser CA, Henkel G, Colman MS, van Beveren C, Stacey KJ et al. Ras-mediated phosphorylation of a conserved threonine residue enhances the transactivation activities of c-Ets1 and c-Ets2. Mol Cell Biol 1996; 16: 538-547.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 538-547
    • Yang, B.1    Hauser, C.A.2    Henkel, G.3    Colman, M.S.4    van Beveren, C.5    Stacey, K.J.6
  • 217
    • 0031882123 scopus 로고    scopus 로고
    • The Elk-1 ETS-domain transcription factor contains a mitogen-activated protein kinase targeting motif
    • Yang SH, Yates PR, Whitmarsh AJ, Davis RJ, Sharrocks AD. The Elk-1 ETS-domain transcription factor contains a mitogen-activated protein kinase targeting motif. Mol Cell Biol 1998; 18: 710-720.
    • (1998) Mol. Cell Biol. , vol.18 , pp. 710-720
    • Yang, S.H.1    Yates, P.R.2    Whitmarsh, A.J.3    Davis, R.J.4    Sharrocks, A.D.5
  • 218
    • 0034684620 scopus 로고    scopus 로고
    • Signal transduction and the Ets family of transcription factors
    • Yordy JS, Muise-Helmericks RC. Signal transduction and the Ets family of transcription factors. Oncogene 2000; 19: 6503-6513.
    • (2000) Oncogene , vol.19 , pp. 6503-6513
    • Yordy, J.S.1    Muise-Helmericks, R.C.2
  • 219
    • 0029095176 scopus 로고
    • ERF: An ETS domain protein with strong transcriptional repressor activity, can suppress ets-associated tumorigenesis and is regulated by phosphorylation during cell cycle and mitogenic stimulation
    • Sgouras DN, Athanasiou MA, Beal Jr GJ, Fisher RJ, Blair DG, Mavrothalassitis GJ. ERF: an ETS domain protein with strong transcriptional repressor activity, can suppress ets-associated tumorigenesis and is regulated by phosphorylation during cell cycle and mitogenic stimulation. EMBO J 1995; 14: 4781-4793.
    • (1995) EMBO J. , vol.14 , pp. 4781-4793
    • Sgouras, D.N.1    Athanasiou, M.A.2    Beal G.J., Jr.3    Fisher, R.J.4    Blair, D.G.5    Mavrothalassitis, G.J.6
  • 220
    • 0033564261 scopus 로고    scopus 로고
    • Net, a negative Ras-switchable TCF, contains a second inhibition domain, the CID, that mediates repression through interactions with CtBP and de-acetylation
    • Criqui-Filipe P, Ducret C, Maira SM, Wasylyk B. Net, a negative Ras-switchable TCF, contains a second inhibition domain, the CID, that mediates repression through interactions with CtBP and de-acetylation. EMBO J 1999; 18: 3392-3403.
    • (1999) EMBO J. , vol.18 , pp. 3392-3403
    • Criqui-Filipe, P.1    Ducret, C.2    Maira, S.M.3    Wasylyk, B.4
  • 222
    • 0033050069 scopus 로고    scopus 로고
    • Transcriptional repressor ERF is a Ras/mitogen-activated protein kinase target that regulates cellular proliferation
    • Le Gallic L, Sgouras D, Beal Jr G, Mavrothalassitis G. Transcriptional repressor ERF is a Ras/mitogen-activated protein kinase target that regulates cellular proliferation. Mol Cell Biol 1999; 19: 4121-4133.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4121-4133
    • Le Gallic, L.1    Sgouras, D.2    Beal G., Jr.3    Mavrothalassitis, G.4
  • 223
    • 0031984279 scopus 로고    scopus 로고
    • In vivo expression and regulation of Elk-1, a target of the extracellular-regulated kinase signaling pathway, in the adult rat brain
    • Sgambato V, Vanhoutte P, Pages C, Rogard M, Hipskind R, Besson MJ et al. In vivo expression and regulation of Elk-1, a target of the extracellular-regulated kinase signaling pathway, in the adult rat brain. J Neurosci 1998; 18: 214-226.
    • (1998) J. Neurosci. , vol.18 , pp. 214-226
    • Sgambato, V.1    Vanhoutte, P.2    Pages, C.3    Rogard, M.4    Hipskind, R.5    Besson, M.J.6
  • 224
    • 0029125757 scopus 로고
    • Integration of MAP kinase signal transduction pathway at the serum response element
    • Whitmarsh AJ, Shore P, Sharrocks AD, Davis RJ. Integration of MAP kinase signal transduction pathway at the serum response element. Science 1995; 269: 403-407.
    • (1995) Science , vol.269 , pp. 403-407
    • Whitmarsh, A.J.1    Shore, P.2    Sharrocks, A.D.3    Davis, R.J.4
  • 225
    • 0027191808 scopus 로고
    • Functional analysis of a growth factor-responsive transcription factor complex
    • Hill CS, Marais R, John S, Wynne J, Dalton S, Treisman R. Functional analysis of a growth factor-responsive transcription factor complex. Cell 1993; 73: 395-406.
    • (1993) Cell , vol.73 , pp. 395-406
    • Hill, C.S.1    Marais, R.2    John, S.3    Wynne, J.4    Dalton, S.5    Treisman, R.6
  • 226
    • 0026695645 scopus 로고
    • Phosphorylation of transcriptioin factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter
    • Gille H, Sharrocks AD, Shaw PE. Phosphorylation of transcriptioin factor p62TCF by MAP kinase stimulates ternary complex formation at c-fos promoter. Nature 1992; 358: 414-417.
    • (1992) Nature , vol.358 , pp. 414-417
    • Gille, H.1    Sharrocks, A.D.2    Shaw, P.E.3
  • 227
    • 0028931406 scopus 로고
    • ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation
    • Gille H, Kortenjann M, Thomae O, Moomaw C, Slaughter C, Cobb M et al. ERK phosphorylation potentiates Elk-1-mediated ternary complex formation and transactivation. EMBO J 1995; 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.6
  • 228
    • 0029827366 scopus 로고    scopus 로고
    • The p38 and ERK MAP kinase pathways co-operate to activate ternary complex factors and c-fos transcription in response to activate ternary complex factors and c-fos transcription in response to UV light
    • Price MA, Cruzalegui FH, Treisman R. The p38 and ERK MAP kinase pathways co-operate to activate ternary complex factors and c-fos transcription in response to activate ternary complex factors and c-fos transcription in response to UV light. EMBO J 1996; 15: 6552-6563.
    • (1996) EMBO J. , vol.15 , pp. 6552-6563
    • Price, M.A.1    Cruzalegui, F.H.2    Treisman, R.3
  • 229
    • 0034717029 scopus 로고    scopus 로고
    • Helicobacter pylori activates mitogen-activated protein kinase cascades and induces expression of the proto-oncogenes c-fos and c-jun
    • Meyer-Vehn T, Covacci A, Kist M, Pahl HL. Helicobacter pylori activates mitogen-activated protein kinase cascades and induces expression of the proto-oncogenes c-fos and c-jun. J Biol Chem 2000; 275: 16064-16072.
    • (2000) J. Biol. Chem. , vol.275 , pp. 16064-16072
    • Meyer-Vehn, T.1    Covacci, A.2    Kist, M.3    Pahl, H.L.4
  • 234
    • 0031039206 scopus 로고    scopus 로고
    • Variations in Jun and Fos protein expression and AP-1 activity in cycling, resting and stimulated fibroblasts
    • Lallemand D, Spyrou G, Yaniv M, Pfarr CM. Variations in Jun and Fos protein expression and AP-1 activity in cycling, resting and stimulated fibroblasts. Oncogene 1997; 14: 819-830.
    • (1997) Oncogene , vol.14 , pp. 819-830
    • Lallemand, D.1    Spyrou, G.2    Yaniv, M.3    Pfarr, C.M.4
  • 235
    • 0035971433 scopus 로고    scopus 로고
    • Close encounters of many kinds: Fos-Jun interactions that mediate transcription regulatory specificity
    • Chinenov Y, Kerppola TK. Close encounters of many kinds: Fos-Jun interactions that mediate transcription regulatory specificity. Oncogene 2001; 20: 2438-2452.
    • (2001) Oncogene , vol.20 , pp. 2438-2452
    • Chinenov, Y.1    Kerppola, T.K.2
  • 236
    • 0035971432 scopus 로고    scopus 로고
    • AP-1 in mouse development and tumorigenesis
    • Jochum W, Passegué E, Wagner EF. AP-1 in mouse development and tumorigenesis. Oncogene 2001; 20: 2401-2412.
    • (2001) Oncogene , vol.20 , pp. 2401-2412
    • Jochum, W.1    Passegué, E.2    Wagner, E.F.3
  • 238
    • 0035971493 scopus 로고    scopus 로고
    • AP-1 in cell proliferation and survival
    • Shaulian E, Karin M. AP-1 in cell proliferation and survival. Oncogene 2001; 20: 2390-2400.
    • (2001) Oncogene , vol.20 , pp. 2390-2400
    • Shaulian, E.1    Karin, M.2
  • 241
    • 0033521651 scopus 로고    scopus 로고
    • C-Jun regulates cell cycle progression and apoptosis by distinct mechanisms
    • Wisdom R, Johnson RS, Moore C. C-Jun regulates cell cycle progression and apoptosis by distinct mechanisms. EMBO J 1999; 18: 188-197.
    • (1999) EMBO J. , vol.18 , pp. 188-197
    • Wisdom, R.1    Johnson, R.S.2    Moore, C.3
  • 242
    • 0028072795 scopus 로고
    • MafB, a new Maf family transcription activator that can associate with Maf and Fos but not with Jun
    • Kataoka K, Fujiwara KT, Noda M, Nishizawa M. MafB, a new Maf family transcription activator that can associate with Maf and Fos but not with Jun. Mol Cell Biol 1994; 14: 7581-7591.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 7581-7591
    • Kataoka, K.1    Fujiwara, K.T.2    Noda, M.3    Nishizawa, M.4
  • 243
    • 0028154038 scopus 로고
    • Maf and Nrl can bind to AP-1 sites and form heterodimers with Fos and Jun
    • Kerppola TK, Curran T. Maf and Nrl can bind to AP-1 sites and form heterodimers with Fos and Jun. Oncogene 1994; 9: 675-684.
    • (1994) Oncogene , vol.9 , pp. 675-684
    • Kerppola, T.K.1    Curran, T.2
  • 244
    • 0035971496 scopus 로고    scopus 로고
    • Distinct roles of Jun:Fos and Jun:ATF dimers in oncogenesis
    • Van Dam H, Castellazzi M. Distinct roles of Jun:Fos and Jun:ATF dimers in oncogenesis. Oncogene 2001; 20: 2453-2464.
    • (2001) Oncogene , vol.20 , pp. 2453-2464
    • Van Dam, H.1    Castellazzi, M.2
  • 245
  • 246
    • 0032979438 scopus 로고    scopus 로고
    • Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation
    • Behrens A, Sibilia M, Wagner EF. Amino-terminal phosphorylation of c-Jun regulates stress-induced apoptosis and cellular proliferation. Nat Genet 1999; 21: 326-329.
    • (1999) Nat. Genet. , vol.21 , pp. 326-329
    • Behrens, A.1    Sibilia, M.2    Wagner, E.F.3
  • 247
    • 0035846912 scopus 로고    scopus 로고
    • Chronic myeloid leukemia with increased granulocyte progenitors in mice lacking junB expression in the myeloid lineage
    • Passegué E, Jochum W, Schorpp-Kistner M, Möhle-teinlein U, Wagner EF. Chronic myeloid leukemia with increased granulocyte progenitors in mice lacking junB expression in the myeloid lineage. Cell 2001; 104: 21-32.
    • (2001) Cell , vol.104 , pp. 21-32
    • Passegué, E.1    Jochum, W.2    Schorpp-Kistner, M.3    Möhle-teinlein, U.4    Wagner, E.F.5
  • 248
    • 0028325891 scopus 로고
    • Mouse JunD negatively regulates fibroblast growth and antagonizes transformation by ras
    • Pfarr CM, Mechta F, Spyrou G, Lallemand D, Carillo S, Yaniv M. Mouse JunD negatively regulates fibroblast growth and antagonizes transformation by ras. Cell 1994; 76: 747-760.
    • (1994) Cell , vol.76 , pp. 747-760
    • Pfarr, C.M.1    Mechta, F.2    Spyrou, G.3    Lallemand, D.4    Carillo, S.5    Yaniv, M.6
  • 249
    • 0035971517 scopus 로고    scopus 로고
    • The mammalian Jun proteins: Redundancy and specificity
    • Mechta-Grigoriou F, Gerald D, Yaniv M. The mammalian Jun proteins: redundancy and specificity. Oncogene 2001; 20: 2378-2389.
    • (2001) Oncogene , vol.20 , pp. 2378-2389
    • Mechta-Grigoriou, F.1    Gerald, D.2    Yaniv, M.3
  • 250
    • 0024276523 scopus 로고
    • The jun proto-oncogene is positively autoregulated by its product, Jun/AP-1
    • Angel P, Hattori K, Smeal T, Karin M. The jun proto-oncogene is positively autoregulated by its product, Jun/AP-1. Cell 1988; 55: 875-885.
    • (1988) Cell , vol.55 , pp. 875-885
    • Angel, P.1    Hattori, K.2    Smeal, T.3    Karin, M.4
  • 251
    • 0029001643 scopus 로고
    • Regulatory role of MEF2D in serum induction of the c-jun promoter
    • Han TH, Prywes R. Regulatory role of MEF2D in serum induction of the c-jun promoter. Mol Cell Biol 1995; 15: 2907-2915.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 2907-2915
    • Han, T.H.1    Prywes, R.2
  • 252
    • 0034944380 scopus 로고    scopus 로고
    • Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating kinase 1 through a MEK-ERK independent mechanism
    • Chen J, Fujii K, Zhang L, Roberts T, Fu H. Raf-1 promotes cell survival by antagonizing apoptosis signal-regulating kinase 1 through a MEK-ERK independent mechanism. Proc Natl Acad Sci USA 2001; 98: 7783-7788.
    • (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
  • 253
    • 0026029808 scopus 로고
    • Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity
    • Boyle WJ, Smeal T, Defize LH, Angel P, Woodgett JR, Karin M et al. Activation of protein kinase C decreases phosphorylation of c-Jun at sites that negatively regulate its DNA-binding activity. Cell 1991; 64: 573-584.
    • (1991) Cell , vol.64 , pp. 573-584
    • Boyle, W.J.1    Smeal, T.2    Defize, L.H.3    Angel, P.4    Woodgett, J.R.5    Karin, M.6
  • 254
    • 0026705482 scopus 로고
    • Casein kinase II is a negative regulator of c-jun DNA binding and AP-1 activity
    • Lin A, Frost J, Deng T, Smeal T, al-Alawi N, Kikkawa U et al. Casein kinase II is a negative regulator of c-jun DNA binding and AP-1 activity. Cell 1992; 70: 777-789.
    • (1992) Cell , vol.70 , pp. 777-789
    • Lin, A.1    Frost, J.2    Deng, T.3    Smeal, T.4    al-Alawi, N.5    Kikkawa, U.6
  • 255
    • 0035971506 scopus 로고    scopus 로고
    • Jun, the oncoprotein
    • Vogt PK. Jun, the oncoprotein. Oncogene 2001; 20: 2365-2377.
    • (2001) Oncogene , vol.20 , pp. 2365-2377
    • Vogt, P.K.1
  • 256
  • 257
    • 0025806587 scopus 로고
    • Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domain
    • Binetruy B, Smeal T, Karin M. Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domain. Nature 1991; 351: 122-127.
    • (1991) Nature , vol.351 , pp. 122-127
    • Binetruy, B.1    Smeal, T.2    Karin, M.3
  • 258
    • 0026541143 scopus 로고
    • Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein
    • Leevers SJ, Marshall CJ. Activation of extracellular signal-regulated kinase, ERK2, by p21ras oncoprotein. EMBO J 1992; 11: 569-574.
    • (1992) EMBO J. , vol.11 , pp. 569-574
    • Leevers, S.J.1    Marshall, C.J.2
  • 259
    • 0026696344 scopus 로고
    • Oncoprotein-mediated signaling cascade stimulates c-Jun activity by phosphorylation of serine 63 and 73
    • Smeal T, Binetruy B, Mercola DA, Grover-Bardwick A, Heidecker G, Rapp UR et al. Oncoprotein-mediated signaling cascade stimulates c-Jun activity by phosphorylation of serine 63 and 73. Mol Cell Biol 1992; 12: 3507-3513.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3507-3513
    • Smeal, T.1    Binetruy, B.2    Mercola, D.A.3    Grover-Bardwick, A.4    Heidecker, G.5    Rapp, U.R.6
  • 260
    • 0025871767 scopus 로고
    • Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c-myc and c-jun proteins by an epidermal growth factor receptor threonine 669 protein kinase
    • Alvarez E, Northwood IC, Gonzalez FA, Latour DA, Seth A, Abate C et al. Pro-Leu-Ser/Thr-Pro is a consensus primary sequence for substrate protein phosphorylation. Characterization of the phosphorylation of c-myc and c-jun proteins by an epidermal growth factor receptor threonine 669 protein kinase. J Biol Chem 1991; 266: 15277-15285.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15277-15285
    • Alvarez, E.1    Northwood, I.C.2    Gonzalez, F.A.3    Latour, D.A.4    Seth, A.5    Abate, C.6
  • 261
    • 0027067934 scopus 로고
    • Inhibition of c-Jun DNA binding by mitogen-activated protein kinase
    • Chou SY, Baichwal V, Ferrell Jr JE. Inhibition of c-Jun DNA binding by mitogen-activated protein kinase. Mol Biol Cell 1992; 3: 1117-1130.
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1117-1130
    • Chou, S.Y.1    Baichwal, V.2    Ferrell J.E., Jr.3
  • 263
    • 0027392874 scopus 로고
    • Co-purification of mitogen-activated protein kinases with phorbol ester-induced c-Jun kinase activity in U937 leukaemic cells
    • Pulverer BJ, Hughes K, Franklin CC, Kraft AS, Leevers SJ, Woodgett JR. Co-purification of mitogen-activated protein kinases with phorbol ester-induced c-Jun kinase activity in U937 leukaemic cells. Oncogene 1993; 8: 407-415.
    • (1993) Oncogene , vol.8 , pp. 407-415
    • Pulverer, B.J.1    Hughes, K.2    Franklin, C.C.3    Kraft, A.S.4    Leevers, S.J.5    Woodgett, J.R.6
  • 267
    • 0033551387 scopus 로고    scopus 로고
    • Mechanisms of apoptosis by c-Myc
    • Prendergast GC. Mechanisms of apoptosis by c-Myc. Oncogene 1999; 18: 2967-2987.
    • (1999) Oncogene , vol.18 , pp. 2967-2987
    • Prendergast, G.C.1
  • 268
    • 0031806044 scopus 로고    scopus 로고
    • The molecular role of Myc in growth and transformation: Recent discoveries lead to new insights
    • Facchini LM, Penn LZ. The molecular role of Myc in growth and transformation: recent discoveries lead to new insights. FASEB J 1998; 12: 633-651.
    • (1998) FASEB J. , vol.12 , pp. 633-651
    • Facchini, L.M.1    Penn, L.Z.2
  • 269
    • 0032905924 scopus 로고    scopus 로고
    • c-Myc target genes involved in cell growth, apoptosis, and metabolism
    • Dang CV. c-Myc target genes involved in cell growth, apoptosis, and metabolism. Mol Cell Biol 1999; 19: 1-11.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 1-11
    • Dang, C.V.1
  • 270
    • 0033539555 scopus 로고    scopus 로고
    • c-Myc enhances protein synthesis and cell size during B lymphocyte development
    • Iritani BM, Eisenman RN. c-Myc enhances protein synthesis and cell size during B lymphocyte development. Proc Natl Acad Sci USA 1999; 96: 13180-13185.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 13180-13185
    • Iritani, B.M.1    Eisenman, R.N.2
  • 271
    • 0033551378 scopus 로고    scopus 로고
    • The role of c-myc in cellular growth control
    • Schmidt EV. The role of c-myc in cellular growth control. Oncogene 1999; 18: 2988-2996.
    • (1999) Oncogene , vol.18 , pp. 2988-2996
    • Schmidt, E.V.1
  • 272
    • 0034633761 scopus 로고    scopus 로고
    • Induction of ribosomal genes and hepatocyte hypertrophy by adenovirus-mediated expression of c-Myc in vivo
    • Kim S, Li Q, Dang CV, Lee LA. Induction of ribosomal genes and hepatocyte hypertrophy by adenovirus-mediated expression of c-Myc in vivo. Proc Natl Acad Sci USA 2000; 97: 11198-11202.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 11198-11202
    • Kim, S.1    Li, Q.2    Dang, C.V.3    Lee, L.A.4
  • 273
    • 0027943249 scopus 로고
    • 1 expression in the absence of de novo protein synthesis and links mitogen-stimulated signal transduction to the cell cycle
    • 1 expression in the absence of de novo protein synthesis and links mitogen-stimulated signal transduction to the cell cycle. Oncogene 1994; 9: 3635-3645.
    • (1994) Oncogene , vol.9 , pp. 3635-3645
    • Daksis, J.I.1    Lu, R.Y.2    Facchini, L.M.3    Marhin, W.W.4    Penn, L.J.5
  • 285
    • 0034724389 scopus 로고    scopus 로고
    • Expression analysis with oligonucleotide microarrays reveals that myc regulates genes involved in growth, cell cycle, signaling and adhesion
    • Coller HA, Grandori C, Tamayo P, Colbert T, Lander ES, Eisenman RN et al. Expression analysis with oligonucleotide microarrays reveals that myc regulates genes involved in growth, cell cycle, signaling and adhesion. Proc Natl Acad Sci USA 2000; 97: 3260-3265.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3260-3265
    • Coller, H.A.1    Grandori, C.2    Tamayo, P.3    Colbert, T.4    Lander, E.S.5    Eisenman, R.N.6
  • 286
    • 0033551377 scopus 로고    scopus 로고
    • Myc-mediated transformation: The repression connection
    • Claassen GF, Hann SR. Myc-mediated transformation: the repression connection. Oncogene 1999; 18: 2925-2933.
    • (1999) Oncogene , vol.18 , pp. 2925-2933
    • Claassen, G.F.1    Hann, S.R.2
  • 287
    • 0027425699 scopus 로고
    • Direct role for Myc in transcription initiation mediated by interactions with TFII-I
    • Roy AL, Carruthers C, Gutjahr T, Roeder RG. Direct role for Myc in transcription initiation mediated by interactions with TFII-I. Nature 1993; 365: 359-361.
    • (1993) Nature , vol.365 , pp. 359-361
    • Roy, A.L.1    Carruthers, C.2    Gutjahr, T.3    Roeder, R.G.4
  • 288
    • 0028169192 scopus 로고
    • c-Myc represses transcription in vivo by a novel mechanism dependent on the initiator element and Myc box II
    • Li LH, Nerlov C, Prendergast G, MacGregor D, Ziff EB. c-Myc represses transcription in vivo by a novel mechanism dependent on the initiator element and Myc box II. EMBO J 1994; 13: 4070-4079.
    • (1994) EMBO J. , vol.13 , pp. 4070-4079
    • Li, L.H.1    Nerlov, C.2    Prendergast, G.3    MacGregor, D.4    Ziff, E.B.5
  • 289
    • 0032996623 scopus 로고    scopus 로고
    • c-Myc regulates cyclin D-Cdk4 and -Cdk6 activity but affects cell cycle progression at multiple independent points
    • Mateyak MK, Obaya AJ, Sedivy JM. c-Myc regulates cyclin D-Cdk4 and -Cdk6 activity but affects cell cycle progression at multiple independent points. Mol Cell Biol 1999; 19: 4672-4683.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4672-4683
    • Mateyak, M.K.1    Obaya, A.J.2    Sedivy, J.M.3
  • 291
    • 0030614715 scopus 로고    scopus 로고
    • Kip1 coordinate their inhibitory interactions with cdk4 and cdk2
    • Kip1 coordinate their inhibitory interactions with cdk4 and cdk2. Genes Dev 1997; 11: 492-503.
    • (1997) Genes Dev. , vol.11 , pp. 492-503
    • Reynisdóttir, I.1    Massagué, J.2
  • 293
    • 0035118130 scopus 로고    scopus 로고
    • A modest reduction in c-Myc expression has minimal effects on cell growth and apoptosis but dramatically reduces susceptibility to Ras and Raf transformation
    • Bazarov AV, Adachi S, Li S, Mateyak MK, Wei S, Sedivy JM. A modest reduction in c-Myc expression has minimal effects on cell growth and apoptosis but dramatically reduces susceptibility to Ras and Raf transformation. Cancer Res 2001; 61: 1178-1186.
    • (2001) Cancer Res. , vol.61 , pp. 1178-1186
    • Bazarov, A.V.1    Adachi, S.2    Li, S.3    Mateyak, M.K.4    Wei, S.5    Sedivy, J.M.6
  • 294
    • 0035120348 scopus 로고    scopus 로고
    • Signal transduction through the Ras/Erk pathway is essential for the mycoestrogen zearalenone-induced cell-cycle progression in MCF-7 cells
    • Ahamed S, Foster JS, Bukovsky A, Wimalasena J. Signal transduction through the Ras/Erk pathway is essential for the mycoestrogen zearalenone-induced cell-cycle progression in MCF-7 cells. Mol Carcinog 2001; 30: 88-98.
    • (2001) Mol. Carcinog. , vol.30 , pp. 88-98
    • Ahamed, S.1    Foster, J.S.2    Bukovsky, A.3    Wimalasena, J.4
  • 295
    • 0033856881 scopus 로고    scopus 로고
    • Myc-enhanced expression of Cul1 promotes ubiquitin-dependent proteolysis and cell cycle progression
    • O'Hagan RC, Ohh M, David G, de Alboran IM, Alt FW, Kaelin Jr WG et al. Myc-enhanced expression of Cul1 promotes ubiquitin-dependent proteolysis and cell cycle progression. Genes Dev 2000; 14: 2185-2191.
    • (2000) Genes Dev. , vol.14 , pp. 2185-2191
    • O'Hagan, R.C.1    Ohh, M.2    David, G.3    de Alboran, I.M.4    Alt, F.W.5    Kaelin W.G., Jr.6
  • 298
    • 0025937489 scopus 로고
    • Constitutive c-myc expression in an IL-3-dependent myeloid cell line suppresses cell cycle arrest and accelerates apoptosis
    • Askew DS, Ashmun RA, Shimmons BC, Cleveland JL. Constitutive c-myc expression in an IL-3-dependent myeloid cell line suppresses cell cycle arrest and accelerates apoptosis. Oncogene 1991; 6: 1915-1922.
    • (1991) Oncogene , vol.6 , pp. 1915-1922
    • Askew, D.S.1    Ashmun, R.A.2    Shimmons, B.C.3    Cleveland, J.L.4
  • 300
    • 0028101015 scopus 로고
    • Nuclear c-Myc plays an important role in the cytotoxicity of tumor necrosis factor alpha in tumor cells
    • Janicke RU, Lee FH, Porter AG. Nuclear c-Myc plays an important role in the cytotoxicity of tumor necrosis factor alpha in tumor cells. Mol Cell Biol 1994; 14: 5661-5670.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 5661-5670
    • Janicke, R.U.1    Lee, F.H.2    Porter, A.G.3
  • 301
  • 302
    • 0030843522 scopus 로고    scopus 로고
    • c-Myc plays a role in cellular susceptibility to death receptor-mediated and chemotherapy-induced apoptosis in human monocytic leukemia U937 cells
    • Dong J, Naito M, Tsuruo T. c-Myc plays a role in cellular susceptibility to death receptor-mediated and chemotherapy-induced apoptosis in human monocytic leukemia U937 cells. Oncogene 1997; 15: 639-647.
    • (1997) Oncogene , vol.15 , pp. 639-647
    • Dong, J.1    Naito, M.2    Tsuruo, T.3
  • 304
    • 0027546614 scopus 로고
    • c-Myc transactivates the p53 promoter through a required downstream CACGTG motif
    • Reisman D, Elkind N, Roy B, Beamon J, Rotter V. c-Myc transactivates the p53 promoter through a required downstream CACGTG motif. Cell Growth Differ 1993; 4: 57-65.
    • (1993) Cell Growth Differ. , vol.4 , pp. 57-65
    • Reisman, D.1    Elkind, N.2    Roy, B.3    Beamon, J.4    Rotter, V.5
  • 305
    • 0027971626 scopus 로고
    • Transactivation of the human p53 tumor suppressor gene by c-Myc/Max contributes to elevated mutant p53 expression in some tumors
    • Roy B, Beamon J, Balint E, Reisman D. Transactivation of the human p53 tumor suppressor gene by c-Myc/Max contributes to elevated mutant p53 expression in some tumors. Mol Cell Biol 1994; 14: 7805-7815.
    • (1994) Mol. Cell Biol. , vol.14 , pp. 7805-7815
    • Roy, B.1    Beamon, J.2    Balint, E.3    Reisman, D.4
  • 306
    • 0033816632 scopus 로고    scopus 로고
    • Myc is an essential negative regulator of platelet-derived growth factor beta receptor expression
    • Oster SK, Marhin WW, Asker C, Facchini LM, Dion PA, Funa K et al. Myc is an essential negative regulator of platelet-derived growth factor beta receptor expression. Mol Cell Biol 2000; 20: 6768-6778.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 6768-6778
    • Oster, S.K.1    Marhin, W.W.2    Asker, C.3    Facchini, L.M.4    Dion, P.A.5    Funa, K.6
  • 308
    • 0027408096 scopus 로고
    • Mad: A heterodimeric partner for Max that antagonizes Myc transcriptional activity
    • Ayer DE, Kretzner L, Eisenman RN. Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 1993; 72: 211-222.
    • (1993) Cell , vol.72 , pp. 211-222
    • Ayer, D.E.1    Kretzner, L.2    Eisenman, R.N.3
  • 309
    • 0034059667 scopus 로고    scopus 로고
    • c-Myc proteolysis by the ubiquitin-proteosome pathway: Stabilization of c-Myc in Burkitt's lymphoma cells
    • Gregory MA, Hann SR. c-Myc proteolysis by the ubiquitin-proteosome pathway: stabilization of c-Myc in Burkitt's lymphoma cells. Mol Cell Biol 2000; 20: 2423-2435.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2423-2435
    • Gregory, M.A.1    Hann, S.R.2
  • 310
    • 0024446021 scopus 로고
    • Myc oncoproteins are phosphorylated by casein kinase II
    • Luscher B, Kuenzel EA, Krebs EG, Eisenman RN. Myc oncoproteins are phosphorylated by casein kinase II. EMBO J 1989; 8: 1111-1119.
    • (1989) EMBO J. , vol.8 , pp. 1111-1119
    • Luscher, B.1    Kuenzel, E.A.2    Krebs, E.G.3    Eisenman, R.N.4
  • 311
    • 0026458063 scopus 로고
    • Specific phosphorylation of the acidic central region of the N-myc protein by casein kinase II
    • Hagiwara T, Nakaya K, Nakamura Y, Nakajima H, Nishimura S, Tara Y. Specific phosphorylation of the acidic central region of the N-myc protein by casein kinase II. Eur J Biochem 1992; 209: 945-950.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 945-950
    • Hagiwara, T.1    Nakaya, K.2    Nakamura, Y.3    Nakajima, H.4    Nishimura, S.5    Tara, Y.6
  • 312
    • 0026554939 scopus 로고
    • Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers
    • Berberich SJ, Cole MD. Casein kinase II inhibits the DNA-binding activity of Max homodimers but not Myc/Max heterodimers. Genes Dev 1992; 6: 166-176.
    • (1992) Genes Dev. , vol.6 , pp. 166-176
    • Berberich, S.J.1    Cole, M.D.2
  • 313
    • 0025223697 scopus 로고
    • Mutational analysis of the carboxy-terminal casein kinase II phosphorylation site in human c-myc
    • Street AJ, Blackwood E, Luscher B, Eiseman RN. Mutational analysis of the carboxy-terminal casein kinase II phosphorylation site in human c-myc. Curr Top Microbiol Immunol 1990; 166: 251-258.
    • (1990) Curr. Top. Microbiol. Immunol. , vol.166 , pp. 251-258
    • Street, A.J.1    Blackwood, E.2    Luscher, B.3    Eiseman, R.N.4
  • 314
    • 0028143178 scopus 로고
    • MAP kinase binds to the NH2-terminal activation domain of c-Myc
    • Gupta S, Davis R. MAP kinase binds to the NH2-terminal activation domain of c-Myc. FEBS Lett 1994; 353: 281-285.
    • (1994) FEBS Lett. , vol.353 , pp. 281-285
    • Gupta, S.1    Davis, R.2
  • 315
    • 0027383378 scopus 로고
    • Phosphorylation sites mapping in the N-terminal domain of c-myc modulate its transforming potential
    • Henriksson M, Barkardjiev A, Klein G, Luscher B. Phosphorylation sites mapping in the N-terminal domain of c-myc modulate its transforming potential. Oncogene 1993; 8: 3199-3209.
    • (1993) Oncogene , vol.8 , pp. 3199-3209
    • Henriksson, M.1    Barkardjiev, A.2    Klein, G.3    Luscher, B.4
  • 316
    • 0026343730 scopus 로고
    • 2-terminal domain of c-Myc increases transactivation of gene expression
    • 2-terminal domain of c-Myc increases transactivation of gene expression. J Biol Chem 1991; 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
  • 317
    • 0026464922 scopus 로고
    • Signal transduction within the nucleus by mitogen-activated protein kinase
    • Seth A, Gonzlez FA, Gupta S, Raden DL, Davis RJ. Signal transduction within the nucleus by mitogen-activated protein kinase. J Biol Chem 1992; 267: 24796-24804.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24796-24804
    • Seth, A.1    Gonzlez, F.A.2    Gupta, S.3    Raden, D.L.4    Davis, R.J.5
  • 318
    • 0023203129 scopus 로고
    • Structure of mutant and wild-type MC29 v-myc alleles and biochemical properties of their protein products
    • Bister K, Trachmann C, Jansen HW, Schroeer B, Patschinsky T. Structure of mutant and wild-type MC29 v-myc alleles and biochemical properties of their protein products. Oncogene 1987; 1: 97-109.
    • (1987) Oncogene , vol.1 , pp. 97-109
    • Bister, K.1    Trachmann, C.2    Jansen, H.W.3    Schroeer, B.4    Patschinsky, T.5
  • 319
    • 0022543776 scopus 로고
    • Site-directed mutagenesis of the gag-myc gene of avian myelocytomatosis virus 29: Biological activity and intracellular localization of structurally altered proteins
    • Heaney ML, Pierce J, Parsons JT. Site-directed mutagenesis of the gag-myc gene of avian myelocytomatosis virus 29: biological activity and intracellular localization of structurally altered proteins. J Virol 1986; 60: 167-176.
    • (1986) J. Virol. , vol.60 , pp. 167-176
    • Heaney, M.L.1    Pierce, J.2    Parsons, J.T.3
  • 320
    • 0023116071 scopus 로고
    • Definition of regions in human c-myc that are involved in transformation and nuclear localization
    • Stone J, deLange T, Ramsay G, Jakobvits E, Bishop JM, Varmus H et al. Definition of regions in human c-myc that are involved in transformation and nuclear localization. Mol Cell Biol 1987; 7: 1697-1709.
    • (1987) Mol. Cell Biol. , vol.7 , pp. 1697-1709
    • Stone, J.1    deLange, T.2    Ramsay, G.3    Jakobvits, E.4    Bishop, J.M.5    Varmus, H.6
  • 321
    • 0028225705 scopus 로고
    • Functional divergence of the MAP kinase pathway: ERK1 and ERK2 activate specific transcription factors
    • Chuang C-F, Ng S-Y. Functional divergence of the MAP kinase pathway: ERK1 and ERK2 activate specific transcription factors. FEBS Lett 1994; 346: 229-234.
    • (1994) FEBS Lett. , vol.346 , pp. 229-234
    • Chuang, C.-F.1    Ng, S.-Y.2
  • 323
    • 0033081027 scopus 로고    scopus 로고
    • Destruction of Myc by ubiquitin-mediated proteolysis: Cancer-associated and transforming mutations stabilize Myc
    • Salghetti ES, Kim SY, Tansey WP. Destruction of Myc by ubiquitin-mediated proteolysis: cancer-associated and transforming mutations stabilize Myc. EMBO J 1999; 18: 717-726.
    • (1999) EMBO J. , vol.18 , pp. 717-726
    • Salghetti, E.S.1    Kim, S.Y.2    Tansey, W.P.3
  • 324
    • 0033935653 scopus 로고    scopus 로고
    • Disruption of Myc-tubulin interaction by hyperphosphorylation of c-Myc during mitosis or by constitutive hyperphosphorylation of mutant c-Myc in Burkitt's lymphoma
    • Niklinski J, Claassen G, Meyers C, Gregory MA, Allegra CJ, Kaye FJ et al. Disruption of Myc-tubulin interaction by hyperphosphorylation of c-Myc during mitosis or by constitutive hyperphosphorylation of mutant c-Myc in Burkitt's lymphoma. Mol Cell Biol 2000; 20: 5276-5284.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 5276-5284
    • Niklinski, J.1    Claassen, G.2    Meyers, C.3    Gregory, M.A.4    Allegra, C.J.5    Kaye, F.J.6
  • 325
    • 0029000938 scopus 로고
    • RelA is a potent transcriptional activator of the CD28 response element within the interleukin 2 promoter
    • Lai JH, Horvath G, Subleski J, Bruder J, Ghosh P, Tan TH. RelA is a potent transcriptional activator of the CD28 response element within the interleukin 2 promoter. Mol Cell Biol 1995; 15: 4260-4271.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 4260-4271
    • Lai, J.H.1    Horvath, G.2    Subleski, J.3    Bruder, J.4    Ghosh, P.5    Tan, T.H.6
  • 326
    • 0027384590 scopus 로고
    • NF-κB subunit-specific regulation of the interleukin-8 promoter
    • Kunsch C, Rosen CA. NF-κB subunit-specific regulation of the interleukin-8 promoter. Mol Cell Biol 1993; 13: 6137-6146.
    • (1993) Mol. Cell Biol. , vol.13 , pp. 6137-6146
    • Kunsch, C.1    Rosen, C.A.2
  • 327
    • 0025260779 scopus 로고
    • Regulation of tumor necrosis factor alpha transcription in macrophages: Involvement of four kappa B-like motifs and of constitutive and inducible forms of NF-kappa B
    • Collart MA, Baeuerle P, Vassalli P. Regulation of tumor necrosis factor alpha transcription in macrophages: involvement of four kappa B-like motifs and of constitutive and inducible forms of NF-kappa B. Mol Cell Biol 1990; 10: 1498-1506.
    • (1990) Mol. Cell Biol. , vol.10 , pp. 1498-1506
    • Collart, M.A.1    Baeuerle, P.2    Vassalli, P.3
  • 328
    • 0025519111 scopus 로고
    • Tumor necrosis factor beta (TNF-β) induces binding of the NF-κB transcription factor to a high-affinity kappa B element in the TNF-β promoter
    • Messer G, Weiss EH, Baeuerle PA. Tumor necrosis factor beta (TNF-β) induces binding of the NF-κB transcription factor to a high-affinity kappa B element in the TNF-β promoter. Cytokine 1990; 2: 389-397.
    • (1990) Cytokine , vol.2 , pp. 389-397
    • Messer, G.1    Weiss, E.H.2    Baeuerle, P.A.3
  • 329
    • 0028982830 scopus 로고
    • Nuclear factor-kappa B interacts functionally with the platelet-derived growth factor B-chain shear-stress response element in vascular endothelial cells exposed to fluid shear stress
    • Khachigian LM, Resnick N, Gimbrone MAJ, Collins T. Nuclear factor-kappa B interacts functionally with the platelet-derived growth factor B-chain shear-stress response element in vascular endothelial cells exposed to fluid shear stress. J Clin Invest 1995; 96: 1169-1175.
    • (1995) J. Clin. Invest. , vol.96 , pp. 1169-1175
    • Khachigian, L.M.1    Resnick, N.2    Gimbrone, M.A.J.3    Collins, T.4
  • 330
    • 0030851721 scopus 로고    scopus 로고
    • Genomic organization of human and mouse genes for vascular endothelial growth factor C
    • Chilov D, Kukk E, Taira S, Jeltsch M, Kaukonen J, Palotie A et al. Genomic organization of human and mouse genes for vascular endothelial growth factor C. J Biol Chem 1997; 272: 25176-25183.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25176-25183
    • Chilov, D.1    Kukk, E.2    Taira, S.3    Jeltsch, M.4    Kaukonen, J.5    Palotie, A.6
  • 332
    • 0027168447 scopus 로고
    • NF-κB controls expression of inhibitor I kappa B alpha: Evidence for an inducible autoregulatory pathway
    • Sun SC, Ganchi PA, Ballard DW, Greene WC. NF-κB controls expression of inhibitor I kappa B alpha: evidence for an inducible autoregulatory pathway. Science 1993; 259: 1912-1915.
    • (1993) Science , vol.259 , pp. 1912-1915
    • Sun, S.C.1    Ganchi, P.A.2    Ballard, D.W.3    Greene, W.C.4
  • 333
    • 0029621231 scopus 로고
    • An acute phase response factor/NF-kappa B site downstream of the junB gene that mediates responsiveness to interleukin-6 in a murine plasmacytoma
    • Brown RT, Ades IA, Nordan RP. An acute phase response factor/NF-kappa B site downstream of the junB gene that mediates responsiveness to interleukin-6 in a murine plasmacytoma. J Biol Chem 1995; 270: 31129-31135.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31129-31135
    • Brown, R.T.1    Ades, I.A.2    Nordan, R.P.3
  • 335
    • 0032537763 scopus 로고    scopus 로고
    • Involvement of Myc targets in c-myc and N-myc induced human tumors
    • Ben-Yosef T, Yanuka O, Halle D, Benvenisty N. Involvement of Myc targets in c-myc and N-myc induced human tumors. Oncogene 1998; 17: 165-171.
    • (1998) Oncogene , vol.17 , pp. 165-171
    • Ben-Yosef, T.1    Yanuka, O.2    Halle, D.3    Benvenisty, N.4
  • 336
    • 0032485391 scopus 로고    scopus 로고
    • Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA
    • Chen L, Glover JN, Hogan PG, Rao A, Harrison SC. Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA. Nature 1998; 392: 42-48.
    • (1998) Nature , vol.392 , pp. 42-48
    • Chen, L.1    Glover, J.N.2    Hogan, P.G.3    Rao, A.4    Harrison, S.C.5
  • 337
    • 0032194170 scopus 로고    scopus 로고
    • Identification of two NF-κB sites in mouse CD95 ligand (Fas ligand) promoter: Functional analysis in T cell hybridoma
    • Matsui K, Fine A, Zhu B, Marshak-Rothstein A, Ju ST. Identification of two NF-κB sites in mouse CD95 ligand (Fas ligand) promoter: functional analysis in T cell hybridoma. J Immunol 1998; 161: 3469-3473.
    • (1998) J. Immunol. , vol.161 , pp. 3469-3473
    • Matsui, K.1    Fine, A.2    Zhu, B.3    Marshak-Rothstein, A.4    Ju, S.T.5
  • 338
    • 0030973579 scopus 로고    scopus 로고
    • Transcription factors of the NFAT family: Regulation and function
    • Rao A, Luo C, Hogan PG. Transcription factors of the NFAT family: regulation and function. Annu Rev Immunol 1997; 15: 707-747.
    • (1997) Annu. Rev. Immunol. , vol.15 , pp. 707-747
    • Rao, A.1    Luo, C.2    Hogan, P.G.3
  • 339
    • 0029030775 scopus 로고
    • Coordinate and cooperative roles for NF-AT and AP-1 in the regulation of the murine IL-4 gene
    • Rooney JW, Hoey T, Gilmcher LH. Coordinate and cooperative roles for NF-AT and AP-1 in the regulation of the murine IL-4 gene. Immunity 1995; 2: 473-483.
    • (1995) Immunity , vol.2 , pp. 473-483
    • Rooney, J.W.1    Hoey, T.2    Gilmcher, L.H.3
  • 340
    • 0031002767 scopus 로고    scopus 로고
    • A T cell-specific enhancer in the interleukin-3 locus is activated cooperatively by Oct and NFAT elements within a DNase I-hypersensitive site
    • Duncliffe KN, Bert AG, Vadas MA, Cockerill PN. A T cell-specific enhancer in the interleukin-3 locus is activated cooperatively by Oct and NFAT elements within a DNase I-hypersensitive site. Immunity 1997; 6: 175-185.
    • (1997) Immunity , vol.6 , pp. 175-185
    • Duncliffe, K.N.1    Bert, A.G.2    Vadas, M.A.3    Cockerill, P.N.4
  • 341
    • 0030999542 scopus 로고    scopus 로고
    • Identification of transcription factor binding sites important in the regulation of the human interleukin-5 gene
    • Stranick KS, Zambas DN, Uss AS, Egan RW, Billah MM, Umland SP. Identification of transcription factor binding sites important in the regulation of the human interleukin-5 gene. J Biol Chem 1997; 272: 16453-16465.
    • (1997) J. Biol. Chem. , vol.272 , pp. 16453-16465
    • Stranick, K.S.1    Zambas, D.N.2    Uss, A.S.3    Egan, R.W.4    Billah, M.M.5    Umland, S.P.6
  • 342
    • 0030050784 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha gene regulation in activated T cells involves ATF-2/Jun and NFATp
    • Tsai EY, Jain J, Pesavento PA, Rao A, Goldfeld AE. Tumor necrosis factor alpha gene regulation in activated T cells involves ATF-2/Jun and NFATp. Mol Cell Biol 1996; 16: 459-467.
    • (1996) Mol. Cell Biol. , vol.16 , pp. 459-467
    • Tsai, E.Y.1    Jain, J.2    Pesavento, P.A.3    Rao, A.4    Goldfeld, A.E.5
  • 343
    • 0034100567 scopus 로고    scopus 로고
    • v-Jun overrides the mitogen dependence of S-phase entry by deregulating retinoblastoma protein phosphorylation and E2F-pocket protein interactions as a consequence of enhanced cyclin E-cdk2 catalytic activity
    • Clark W, Black E, MacLaren A, Kruse U, LaThangue N, Vogt P et al. v-Jun overrides the mitogen dependence of S-phase entry by deregulating retinoblastoma protein phosphorylation and E2F-pocket protein interactions as a consequence of enhanced cyclin E-cdk2 catalytic activity. Mol Cell Biol 2000; 20: 2529-2542.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 2529-2542
    • Clark, W.1    Black, E.2    MacLaren, A.3    Kruse, U.4    LaThangue, N.5    Vogt, P.6
  • 344
    • 0033961711 scopus 로고    scopus 로고
    • c-jun-dependent CD95-L expression is a rate-limiting step in the induction of apoptosis by alkylating agents
    • Kolbus A, Herr I, Schreiber M, Debatin KM, Wagner EF, Angel P. c-jun-dependent CD95-L expression is a rate-limiting step in the induction of apoptosis by alkylating agents. Mol Cell Biol 2000; 20: 575-582.
    • (2000) Mol. Cell Biol. , vol.20 , pp. 575-582
    • Kolbus, A.1    Herr, I.2    Schreiber, M.3    Debatin, K.M.4    Wagner, E.F.5    Angel, P.6
  • 346
    • 0032145569 scopus 로고    scopus 로고
    • Myc signaling via the ARF tumor suppressor regulates p53-dependent apoptosis and immortalization
    • Zindy F, Eischen CM, Randle DH, Kamijo T, Cleveland JL, Sherr CJ et al. Myc signaling via the ARF tumor suppressor regulates p53-dependent apoptosis and immortalization. Genes Dev 1998; 12: 2424-2433.
    • (1998) Genes Dev. , vol.12 , pp. 2424-2433
    • Zindy, F.1    Eischen, C.M.2    Randle, D.H.3    Kamijo, T.4    Cleveland, J.L.5    Sherr, C.J.6
  • 347
    • 0029779280 scopus 로고    scopus 로고
    • Cdc25 cell-cycle phosphatase as a target of c-myc
    • Galaktionov K, Chen D, Beach D. Cdc25 cell-cycle phosphatase as a target of c-myc. Nature 1996; 382: 511-517.
    • (1996) Nature , vol.382 , pp. 511-517
    • Galaktionov, K.1    Chen, D.2    Beach, D.3
  • 348
    • 0035822631 scopus 로고    scopus 로고
    • Time-dependent inhibition of protein farnesyltransferase by a benzodiazepine peptide mimetic
    • Roskoski Jr R, Ritchie PA. Time-dependent inhibition of protein farnesyltransferase by a benzodiazepine peptide mimetic. Biochemistry 2001; 40: 9329-9335.
    • (2001) Biochemistry , vol.40 , pp. 9329-9335
    • Roskoski R., Jr.1    Ritchie, P.A.2
  • 350
    • 0036676754 scopus 로고    scopus 로고
    • In vitro activity of hederacolchisid A1 compared with other saponins from Hedera colchica against proliferation of human carcinoma and melanoma cells
    • Barthomeuf C, Debiton E, Mshvildadze V, Kemertelidze E, Balansard G. In vitro activity of hederacolchisid A1 compared with other saponins from Hedera colchica against proliferation of human carcinoma and melanoma cells. Planta Med 2002; 68: 672-675.
    • (2002) Planta Med. , vol.68 , pp. 672-675
    • Barthomeuf, C.1    Debiton, E.2    Mshvildadze, V.3    Kemertelidze, E.4    Balansard, G.5
  • 352
    • 0035844247 scopus 로고    scopus 로고
    • The farnesyltransferase inhibitor, FTI-2153, blocks bipolar spindle formation and chromosome alignment and causes prometaphase accumulation during mitosis of human lung cancer cells
    • Crespo NC, Ohkanda J, Yen TJ, Hamilton AD, Sebti SM. The farnesyltransferase inhibitor, FTI-2153, blocks bipolar spindle formation and chromosome alignment and causes prometaphase accumulation during mitosis of human lung cancer cells. J Biol Chem 2001; 276: 16161-16167.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16161-16167
    • Crespo, N.C.1    Ohkanda, J.2    Yen, T.J.3    Hamilton, A.D.4    Sebti, S.M.5
  • 353
    • 0033214457 scopus 로고    scopus 로고
    • Antitumor efficacy of a novel class of non-thiol-containing peptidomimetic inhibitors of farnesyltransferase and geranylgeranyltransferase I: Combination therapy with the cytotoxic agents cisplatin, Taxol, and gemcitabine
    • Sun J, Blaskovich MA, Knowles D, Qian Y, Ohkanda J, Bailey RD et al. Antitumor efficacy of a novel class of non-thiol-containing peptidomimetic inhibitors of farnesyltransferase and geranylgeranyltransferase I: combination therapy with the cytotoxic agents cisplatin, Taxol, and gemcitabine. Cancer Res 1999; 59: 4919-4926.
    • (1999) Cancer Res. , vol.59 , pp. 4919-4926
    • Sun, J.1    Blaskovich, M.A.2    Knowles, D.3    Qian, Y.4    Ohkanda, J.5    Bailey, R.D.6
  • 354
    • 0030968859 scopus 로고    scopus 로고
    • Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo
    • Rowell CA, Kowalczyk JJ, Lewis MD, Garcia AM. Direct demonstration of geranylgeranylation and farnesylation of Ki-Ras in vivo. J Biol Chem 1997; 272: 14093-14097.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14093-14097
    • Rowell, C.A.1    Kowalczyk, J.J.2    Lewis, M.D.3    Garcia, A.M.4
  • 355
    • 0030820894 scopus 로고    scopus 로고
    • Anti tumor activity of farnesyl transferase inhibitor
    • Yoshimatsu K, Nagausu T. Anti tumor activity of farnesyl transferase inhibitor. Gan To Kagaku Ryoho 1997; 24: 145-155.
    • (1997) Gan To Kagaku Ryoho , vol.24 , pp. 145-155
    • Yoshimatsu, K.1    Nagausu, T.2
  • 356
    • 0028869067 scopus 로고
    • Inhibition of human tumor xenograft growth by treatment with the farnesyl transferase inhibitor B956
    • Nagasu T, Yoshimatsu K, Rowell C, Lewis MD, Garcia AM. Inhibition of human tumor xenograft growth by treatment with the farnesyl transferase inhibitor B956. Cancer Res 1995; 55: 5310-5314.
    • (1995) Cancer Res. , vol.55 , pp. 5310-5314
    • Nagasu, T.1    Yoshimatsu, K.2    Rowell, C.3    Lewis, M.D.4    Garcia, A.M.5
  • 357
    • 0033813127 scopus 로고    scopus 로고
    • Ras-mediated suppression of TGFBetaRII expression in intestinal epithelial cells involves Raf-independent signaling
    • Bulus NM, Sheng HM, Sizemore N, Oldham SM, Barnett JV, Coffey RJ et al. Ras-mediated suppression of TGFBetaRII expression in intestinal epithelial cells involves Raf-independent signaling. Neoplasia 2000; 2: 357-364.
    • (2000) Neoplasia , vol.2 , pp. 357-364
    • Bulus, N.M.1    Sheng, H.M.2    Sizemore, N.3    Oldham, S.M.4    Barnett, J.V.5    Coffey, R.J.6
  • 358
    • 0030624197 scopus 로고    scopus 로고
    • Inhibitors of farnesyl transferase in oncology: From basic research to pharmaceutical research
    • (Review)
    • Lavelle F. Inhibitors of farnesyl transferase in oncology: from basic research to pharmaceutical research. C R Seances Soc Biol Fil 1997; 191: 211-219 (Review).
    • (1997) C. R. Seances Soc. Biol. Fil. , vol.191 , pp. 211-219
    • Lavelle, F.1
  • 359
    • 0028958919 scopus 로고
    • Polylysine and CVIM sequences of K-RasB dictate specificity of prenylation and confer resistance to benzodiazepine peptidomimetic in vitro
    • James GL, Goldstein JL, Brown MS. Polylysine and CVIM sequences of K-RasB dictate specificity of prenylation and confer resistance to benzodiazepine peptidomimetic in vitro. J Biol Chem 1995; 270: 6221-6226.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6221-6226
    • James, G.L.1    Goldstein, J.L.2    Brown, M.S.3
  • 360
    • 0036655361 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors: Novel compounds in development for the treatment of myeloid malignancies
    • Cortes JE, Kurzrock R, Kantarjian HM. Farnesyltransferase inhibitors: novel compounds in development for the treatment of myeloid malignancies. Semin Hematol 2002; 39: 26-30.
    • (2002) Semin. Hematol. , vol.39 , pp. 26-30
    • Cortes, J.E.1    Kurzrock, R.2    Kantarjian, H.M.3
  • 361
    • 0036655043 scopus 로고    scopus 로고
    • Clinical trials referral resource. Current clinical trials of R115777 (Zarnestra)
    • Wright JJ, Zerivitz K, Gravell AE, Cheson BD. Clinical trials referral resource. Current clinical trials of R115777 (Zarnestra). Oncology (Huntingt) 2002; 16: 930-937.
    • (2002) Oncology (Huntingt) , vol.16 , pp. 930-937
    • Wright, J.J.1    Zerivitz, K.2    Gravell, A.E.3    Cheson, B.D.4
  • 363
    • 0035181479 scopus 로고    scopus 로고
    • Preclinical antitumor activity and pharmacodynamic studies with the farnesyl protein transferase inhibitor R115777 in human breast cancer
    • Kelland LR, Smith V, Valenti M, Patterson L, Clarke PA, Detre S et al. Preclinical antitumor activity and pharmacodynamic studies with the farnesyl protein transferase inhibitor R115777 in human breast cancer. Clin Cancer Res 2001; 7: 3544-3550.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 3544-3550
    • Kelland, L.R.1    Smith, V.2    Valenti, M.3    Patterson, L.4    Clarke, P.A.5    Detre, S.6
  • 364
    • 0034820022 scopus 로고    scopus 로고
    • Cell cycle regulation in the G1 phase: A promising target for the development of new chemotherapeutic anticancer agents
    • (Review)
    • Owa T, Yoshino H, Yoshimatsu K, Nagasu T. Cell cycle regulation in the G1 phase: a promising target for the development of new chemotherapeutic anticancer agents. Curr Med Chem 2001; 8: 1487-1503 (Review).
    • (2001) Curr. Med. Chem. , vol.8 , pp. 1487-1503
    • Owa, T.1    Yoshino, H.2    Yoshimatsu, K.3    Nagasu, T.4
  • 365
    • 18544412314 scopus 로고    scopus 로고
    • Phase I and pharmacokinetic study of farnesyl protein transferase inhibitor R115777 in advanced cancer
    • Zujewski J, Horak ID, Bol CJ, Woestenborghs R, Bowden C, End DW et al. Phase I and pharmacokinetic study of farnesyl protein transferase inhibitor R115777 in advanced cancer. J Clin Oncol 2000; 18: 927-941.
    • (2000) J. Clin. Oncol. , vol.18 , pp. 927-941
    • Zujewski, J.1    Horak, I.D.2    Bol, C.J.3    Woestenborghs, R.4    Bowden, C.5    End, D.W.6
  • 366
    • 0036683409 scopus 로고    scopus 로고
    • Overcoming STI571 resistance with the farnesyl transferase inhibitor SCH66336
    • Hoover RR, Mahon FX, Melo JV, Daley GQ. Overcoming STI571 resistance with the farnesyl transferase inhibitor SCH66336. Blood 2002; 100: 1068-1071.
    • (2002) Blood , vol.100 , pp. 1068-1071
    • Hoover, R.R.1    Mahon, F.X.2    Melo, J.V.3    Daley, G.Q.4
  • 368
    • 0035360259 scopus 로고    scopus 로고
    • Isotype-specific Ras.GTP-levels predict the efficacy of farnesyl transferase inhibitors against human astrocytomas regardless of Ras mutational status
    • Feldkamp MM, Lau N, Roncari L, Guha A. Isotype-specific Ras.GTP-levels predict the efficacy of farnesyl transferase inhibitors against human astrocytomas regardless of Ras mutational status. Cancer Res 2001; 61: 4425-4431.
    • (2001) Cancer Res. , vol.61 , pp. 4425-4431
    • Feldkamp, M.M.1    Lau, N.2    Roncari, L.3    Guha, A.4
  • 370
    • 0034857309 scopus 로고    scopus 로고
    • Blocking protein geranylgeranylation is essential for lovastatin-induced apoptosis of human acute myeloid leukemia cells
    • Xia Z, Tan MM, Wong WW, Dimitroulakos J, Minden MD, Penn LZ. Blocking protein geranylgeranylation is essential for lovastatin-induced apoptosis of human acute myeloid leukemia cells. Leukemia 2001; 15: 1398-1407.
    • (2001) Leukemia , vol.15 , pp. 1398-1407
    • Xia, Z.1    Tan, M.M.2    Wong, W.W.3    Dimitroulakos, J.4    Minden, M.D.5    Penn, L.Z.6
  • 371
    • 0035869396 scopus 로고    scopus 로고
    • Cell-cycle-dependent activation of mitogen-activated protein kinase kinase (MEK-1/2) in myeloid leukemia cell lines and induction of growth inhibition and apoptosis by inhibitors of RAS signaling
    • Morgan MA, Dolp O, Reuter CW. Cell-cycle-dependent activation of mitogen-activated protein kinase kinase (MEK-1/2) in myeloid leukemia cell lines and induction of growth inhibition and apoptosis by inhibitors of RAS signaling. Blood 2001; 979: 1823-1834.
    • (2001) Blood , vol.979 , pp. 1823-1834
    • Morgan, M.A.1    Dolp, O.2    Reuter, C.W.3
  • 372
    • 0032752610 scopus 로고    scopus 로고
    • Combination of the novel farnesyltransferase inhibitor RPR130401 and the geranylgeranyltransferase-1 inhibitor GGTI-298 disrupts MAP kinase activation and G(1)-S transition in Ki-Ras-overexpressing transformed adrenocortical cells
    • Mazet JL, Padieu M, Osman H, Maume G, Mailliet P, Dereu N et al. Combination of the novel farnesyltransferase inhibitor RPR130401 and the geranylgeranyltransferase-1 inhibitor GGTI-298 disrupts MAP kinase activation and G(1)-S transition in Ki-Ras-overexpressing transformed adrenocortical cells. FEBS Lett. 1999; 460: 235-240.
    • (1999) FEBS Lett. , vol.460 , pp. 235-240
    • Mazet, J.L.1    Padieu, M.2    Osman, H.3    Maume, G.4    Mailliet, P.5    Dereu, N.6
  • 374
    • 0034820022 scopus 로고    scopus 로고
    • Cell cycle regulation in the G1 phase: A promising target for the development of new chemotherapeutic anticancer agents
    • (Review)
    • Owa T, Yoshino H, Yoshimatsu K, Nagasu T. Cell cycle regulation in the G1 phase: a promising target for the development of new chemotherapeutic anticancer agents. Cur Med Chem 2001; 8: 1487-1503 (Review).
    • (2001) Cur. Med. Chem. , vol.8 , pp. 1487-1503
    • Owa, T.1    Yoshino, H.2    Yoshimatsu, K.3    Nagasu, T.4
  • 375
    • 0034609805 scopus 로고    scopus 로고
    • Discovery of (R)-7-cyano-2,3,4,5-tetrahydro-1-(1H-imidazol-4-ylmethyl)-3- (phenylmethyl)-4-(2-thienylsulfonyl)-1,H-14-benzodiazepine (BMS-214662) a farnesyltransferase inhibitor with potent preclinical antitumor activity
    • Hunt JT, Ding CZ, Batorsky R, Bednarz M, Bhide R, Cho Y et al. Discovery of (R)-7-cyano-2,3,4,5-tetrahydro-1-(1H-imidazol-4-ylmethyl)-3- (phenylmethyl)-4-(2-thienylsulfonyl)-1,H-14-benzodiazepine (BMS-214662) a farnesyltransferase inhibitor with potent preclinical antitumor activity. J Med Chem. 2000; 43: 3587-3595.
    • (2000) J. Med. Chem. , vol.43 , pp. 3587-3595
    • Hunt, J.T.1    Ding, C.Z.2    Batorsky, R.3    Bednarz, M.4    Bhide, R.5    Cho, Y.6
  • 381
    • 0036401105 scopus 로고    scopus 로고
    • BAY 43-9006: Preclinical data
    • Wilhelm S, Chien DS. BAY 43-9006: preclinical data. Curr Pharm Des 2002; 8: 2255-2257.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 2255-2257
    • Wilhelm, S.1    Chien, D.S.2
  • 382
    • 0036402628 scopus 로고    scopus 로고
    • BAY 43-9006: Early clinical data in patients with advanced solid malignancies
    • Hotte SJ, Hirte HW. BAY 43-9006: early clinical data in patients with advanced solid malignancies. Curr Pharm Des 2002; 8: 99-110.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 99-110
    • Hotte, S.J.1    Hirte, H.W.2
  • 383
    • 0036931949 scopus 로고    scopus 로고
    • Targeting the Raf kinase cascade in cancer therapy - Novel molecular targets and therapeutic strategies
    • Lee JT, McCubrey JA. Targeting the Raf kinase cascade in cancer therapy - novel molecular targets and therapeutic strategies. Exp Opin 2002; 6: 1-20.
    • (2002) Exp. Opin. , vol.6 , pp. 1-20
    • Lee, J.T.1    McCubrey, J.A.2
  • 384
    • 0036023413 scopus 로고    scopus 로고
    • A randomized phase II and pharmacolinetic study of the antisense oligonucleotides ISIS 3521 and ISIS 5132 in patients with hormone-refractory prostate cancer
    • Tulcher AW, Reyno L, Venner PM, Ernst SD, Moore M, Geary RS et al. A randomized phase II and pharmacolinetic study of the antisense oligonucleotides ISIS 3521 and ISIS 5132 in patients with hormone-refractory prostate cancer. Clin Cancer Res 2002; 8: 2530-2535.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 2530-2535
    • Tulcher, A.W.1    Reyno, L.2    Venner, P.M.3    Ernst, S.D.4    Moore, M.5    Geary, R.S.6
  • 385
    • 0035845318 scopus 로고    scopus 로고
    • Antisense therapy in oncology: New hope for an old idea?
    • Tamm I, Dorken B, Hartmann G. Antisense therapy in oncology: new hope for an old idea? Lancet 2001; 358: 489-497.
    • (2001) Lancet , vol.358 , pp. 489-497
    • Tamm, I.1    Dorken, B.2    Hartmann, G.3
  • 386
    • 0035977185 scopus 로고    scopus 로고
    • Association of c-Raf expression with survival and its targeting with antisense oligonucleotides in ovarian cancer
    • McPhillips F, Mullen P, Monia BP, Ritchie AA, Dorr FA, Smyth JF et al. Association of c-Raf expression with survival and its targeting with antisense oligonucleotides in ovarian cancer. Br J Cancer 2001; 85: 1753-1758.
    • (2001) Br. J. Cancer , vol.85 , pp. 1753-1758
    • McPhillips, F.1    Mullen, P.2    Monia, B.P.3    Ritchie, A.A.4    Dorr, F.A.5    Smyth, J.F.6
  • 387
    • 0032499288 scopus 로고    scopus 로고
    • Abrogation of c-Raf expression induces apoptosis in tumor cells
    • Lau QC, Brusselbach S, Muller R. Abrogation of c-Raf expression induces apoptosis in tumor cells. Oncogene 1998; 16: 1899-1902.
    • (1998) Oncogene , vol.16 , pp. 1899-1902
    • Lau, Q.C.1    Brusselbach, S.2    Muller, R.3
  • 388
    • 0036734775 scopus 로고    scopus 로고
    • The treatment of patients with disseminated malignant melanoma by vaccination with autologous cell hybrids of tumor cells and dendritic cells
    • Krause SW, Neumann C, Soruri A, Mayer S, Peters JH, Andreesen R. The treatment of patients with disseminated malignant melanoma by vaccination with autologous cell hybrids of tumor cells and dendritic cells. J Immunother 2002; 25: 421-428.
    • (2002) J. Immunother. , vol.25 , pp. 421-428
    • Krause, S.W.1    Neumann, C.2    Soruri, A.3    Mayer, S.4    Peters, J.H.5    Andreesen, R.6
  • 389
    • 0036693183 scopus 로고    scopus 로고
    • Clinical trials in childhood acute lymphoblastic leukemia: A common prognostic classification and a common induction therapy are now warranted
    • Donadieu J, Hill C. Clinical trials in childhood acute lymphoblastic leukemia: a common prognostic classification and a common induction therapy are now warranted. J Pediatr Hematol Oncol 2002; 24: 424-4255.
    • (2002) J. Pediatr. Hematol. Oncol. , vol.24 , pp. 424-4255
    • Donadieu, J.1    Hill, C.2
  • 390
    • 0036733213 scopus 로고    scopus 로고
    • Efficacy of adjuvant immunochemotherapy with OK-432 for patients with curatively resected gastric cancer: A metaanalysis of centrally randomized controlled clinical trials
    • Sakamoto J, Teramukai S, Nakazato H, Sato Y, Uchino J, Taguchi T et al. Efficacy of adjuvant immunochemotherapy with OK-432 for patients with curatively resected gastric cancer: a metaanalysis of centrally randomized controlled clinical trials. J Immunother 2002; 25: 405-412.
    • (2002) J. Immunother. , vol.25 , pp. 405-412
    • Sakamoto, J.1    Teramukai, S.2    Nakazato, H.3    Sato, Y.4    Uchino, J.5    Taguchi, T.6
  • 391
  • 392
    • 0034594644 scopus 로고    scopus 로고
    • Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins
    • Marcu MG, Schulte TW, Neckers L. Novobiocin and related coumarins and depletion of heat shock protein 90-dependent signaling proteins. J Natl Cancer Inst 2000; 92: 242-248.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 242-248
    • Marcu, M.G.1    Schulte, T.W.2    Neckers, L.3
  • 393
    • 0027200479 scopus 로고
    • The interaction between coumarin drugs and DNA gyrase
    • (Review)
    • Maxwell A. The interaction between coumarin drugs and DNA gyrase. Mol Microbiol 1993; 9: 681-686 (Review).
    • (1993) Mol. Microbiol. , vol.9 , pp. 681-686
    • Maxwell, A.1
  • 394
    • 0037062576 scopus 로고    scopus 로고
    • DNA gyrase interaction with coumarin-based inhibitors: The role of the hydroxybenzoate isopentenyl moiety and the 5′-methyl group of the noviose
    • Lafitte D, Lamour V, Tsvetkov PO, Makarov AA, Klich M, Deprez P et al. DNA gyrase interaction with coumarin-based inhibitors: the role of the hydroxybenzoate isopentenyl moiety and the 5′-methyl group of the noviose. Biochemistry 2002; 41: 71217-71223.
    • (2002) Biochemistry , vol.41 , pp. 71217-71223
    • Lafitte, D.1    Lamour, V.2    Tsvetkov, P.O.3    Makarov, A.A.4    Klich, M.5    Deprez, P.6
  • 396
    • 0034665760 scopus 로고    scopus 로고
    • Novel oxime derivatives of radicicol induce erythroid differentiation associated with preferential G(1) phase accumulation against chronic myelogenous leukemia cells through destabilization of Bcr-Abl with Hsp90 complex
    • Shiotsu Y, Neckers LM, Wortman I, An WG, Schulte TW, Soga S et al. Novel oxime derivatives of radicicol induce erythroid differentiation associated with preferential G(1) phase accumulation against chronic myelogenous leukemia cells through destabilization of Bcr-Abl with Hsp90 complex. Blood 2000; 96: 2284-2291.
    • (2000) Blood , vol.96 , pp. 2284-2291
    • Shiotsu, Y.1    Neckers, L.M.2    Wortman, I.3    An, W.G.4    Schulte, T.W.5    Soga, S.6
  • 397
    • 0033564430 scopus 로고    scopus 로고
    • KF25706, a novel oxime derivative of radicicol, exhibits in vivo antitumor activity via selective depletion of Hsp90 binding signaling molecules
    • Soga S, Neckers LM, Schulte TW, Shiotsu Y, Akasaka K, Narumi H et al. KF25706, a novel oxime derivative of radicicol, exhibits in vivo antitumor activity via selective depletion of Hsp90 binding signaling molecules. Cancer Res 1999; 59: 2931-2938.
    • (1999) Cancer Res. , vol.59 , pp. 2931-2938
    • Soga, S.1    Neckers, L.M.2    Schulte, T.W.3    Shiotsu, Y.4    Akasaka, K.5    Narumi, H.6
  • 398
    • 0033786912 scopus 로고    scopus 로고
    • Phase I and pharmacokinetic study of novobiocin in combination with VP-16 in patients with refractory malignancies
    • Murren JR, DiStasio SA, Lorico A, McKeon A, Zuhowski EG, Egorin MJ et al. Phase I and pharmacokinetic study of novobiocin in combination with VP-16 in patients with refractory malignancies. Cancer J 2000; 6: 256-265.
    • (2000) Cancer J. , vol.6 , pp. 256-265
    • Murren, J.R.1    DiStasio, S.A.2    Lorico, A.3    McKeon, A.4    Zuhowski, E.G.5    Egorin, M.J.6
  • 399
    • 0030064573 scopus 로고    scopus 로고
    • Insights into mechanisms of cisplatin resistance and potential for its clinical reversal
    • Gosland M, Lum B, Schimmelpfennig J, Baker J, Doukas M. Insights into mechanisms of cisplatin resistance and potential for its clinical reversal. Pharmacotherapy 1996; 16: 16-39.
    • (1996) Pharmacotherapy , vol.16 , pp. 16-39
    • Gosland, M.1    Lum, B.2    Schimmelpfennig, J.3    Baker, J.4    Doukas, M.5
  • 400
    • 0025819479 scopus 로고
    • Cisplatin and novobiocin in the treatment of non-small cell lung cancer
    • A Southwest Oncology Group study
    • Ellis GK, Crowley J, Livingston RB, Goodwin JW, Hutchins L, Allen A. Cisplatin and novobiocin in the treatment of non-small cell lung cancer. A Southwest Oncology Group study. Cancer 1991; 67: 2969-2973.
    • (1991) Cancer , vol.67 , pp. 2969-2973
    • Ellis, G.K.1    Crowley, J.2    Livingston, R.B.3    Goodwin, J.W.4    Hutchins, L.5    Allen, A.6
  • 401
    • 0037628516 scopus 로고
    • A phase I clinical trial of novobiocin, a modulator of alkylating agent cytotoxicity
    • Eder JP, Wheeler CA, Teicher BA, Schnipper LE. A phase I clinical trial of novobiocin, a modulator of alkylating agent cytotoxicity. Cancer Res 1989; 49: 2578-2583.
    • (1989) Cancer Res. , vol.49 , pp. 2578-2583
    • Eder, J.P.1    Wheeler, C.A.2    Teicher, B.A.3    Schnipper, L.E.4
  • 402
  • 403
    • 85047695528 scopus 로고    scopus 로고
    • Hsp-90-associated oncoproteins: Multiple targets of geldanamycin and its analogs
    • (Review)
    • Blagosklonny MV. Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs. Leukemia 2002; 16: 455-462 (Review).
    • (2002) Leukemia , vol.16 , pp. 455-462
    • Blagosklonny, M.V.1
  • 404
    • 0036219609 scopus 로고    scopus 로고
    • Hsp90 inhibitors as novel cancer chemotherapeutic agents
    • (Review)
    • Neckers L. Hsp90 inhibitors as novel cancer chemotherapeutic agents. Trends Mol Med. 2002; 8: S55-S61 (Review).
    • (2002) Trends Mol. Med. , vol.8
    • Neckers, L.1
  • 405
    • 0035989680 scopus 로고    scopus 로고
    • HSP90 as a new therapeutic target for cancer therapy: The story unfolds
    • Workman P, Maloney A. HSP90 as a new therapeutic target for cancer therapy: the story unfolds. Exp Opin Biol Ther 2002; 2: 3-24.
    • (2002) Exp. Opin. Biol. Ther. , vol.2 , pp. 3-24
    • Workman, P.1    Maloney, A.2
  • 406
    • 0035176758 scopus 로고    scopus 로고
    • The Hsp90 chaperone as a promising drug target
    • (Review)
    • Piper PW. The Hsp90 chaperone as a promising drug target. Curr Opin Invest Drugs 2001; 2: 1606-1610 (Review).
    • (2001) Curr. Opin. Invest. Drugs , vol.2 , pp. 1606-1610
    • Piper, P.W.1
  • 407
    • 0034777916 scopus 로고    scopus 로고
    • Destabilization of steroid receptors by heat shock protein 90-binding drugs: A ligand-independent approach to hormonal therapy of breast cancer
    • Bagatell R, Khan O, Paine-Murrieta G, Taylor CW, Akinaga S, Whitesell L. Destabilization of steroid receptors by heat shock protein 90-binding drugs: a ligand-independent approach to hormonal therapy of breast cancer. Clin Cancer Res 2001; 7: 2076-2084.
    • (2001) Clin. Cancer Res. , vol.7 , pp. 2076-2084
    • Bagatell, R.1    Khan, O.2    Paine-Murrieta, G.3    Taylor, C.W.4    Akinaga, S.5    Whitesell, L.6
  • 408
    • 0034626718 scopus 로고    scopus 로고
    • Chimeric VEGFRs are activated by a small-molecule dimerizer and mediate downstream signalling cascades in endothelial cells
    • Knight EL, Warner AJ, Maxwell A, Prigent SA. Chimeric VEGFRs are activated by a small-molecule dimerizer and mediate downstream signalling cascades in endothelial cells. Oncogene 2000; 19: 5398-5405.
    • (2000) Oncogene , vol.19 , pp. 5398-5405
    • Knight, E.L.1    Warner, A.J.2    Maxwell, A.3    Prigent, S.A.4
  • 410
    • 0034613293 scopus 로고    scopus 로고
    • Membrane localization of Raf assists engagement of downstream effectors
    • Farrar MA, Tian J, Perlmutter RM. Membrane localization of Raf assists engagement of downstream effectors. J Biol Chem 2000; 275: 31318-31324.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31318-31324
    • Farrar, M.A.1    Tian, J.2    Perlmutter, R.M.3
  • 411
    • 0033600167 scopus 로고    scopus 로고
    • A G-CSF receptor-gyrase B fusion gene: A new type of molecular switch for expansion of genetically modified hematopoietic cells
    • Kume A, Ito K, Ueda Y, Hasegawa M, Urabe M, Mano H et al. A G-CSF receptor-gyrase B fusion gene: a new type of molecular switch for expansion of genetically modified hematopoietic cells. Biochem Biophys Res Commun 1999; 260: 9-12.
    • (1999) Biochem. Biophys. Res. Commun. , vol.260 , pp. 9-12
    • Kume, A.1    Ito, K.2    Ueda, Y.3    Hasegawa, M.4    Urabe, M.5    Mano, H.6
  • 412
    • 0031792831 scopus 로고    scopus 로고
    • Activation and functional analysis of Janus kinase 2 in BA/F3 cells using the coumermycin/gyrase B system
    • Mohi MG, Arai K, Watanabe S. Activation and functional analysis of Janus kinase 2 in BA/F3 cells using the coumermycin/gyrase B system. Mol Biol Cell 1998; 9: 3299-3308.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3299-3308
    • Mohi, M.G.1    Arai, K.2    Watanabe, S.3
  • 413
    • 0034942219 scopus 로고    scopus 로고
    • Tyrosine kinase inhibitors in the treatment of chronic myeloid leukaemia: So far so good
    • (Review)
    • Drummond MW, Holyoake TL. Tyrosine kinase inhibitors in the treatment of chronic myeloid leukaemia: so far so good. Blood Rev 2001; 15: 85-95 (Review).
    • (2001) Blood Rev. , vol.15 , pp. 85-95
    • Drummond, M.W.1    Holyoake, T.L.2
  • 414
    • 0031875042 scopus 로고    scopus 로고
    • The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin
    • Schulte TW, Neckers LM. The benzoquinone ansamycin 17-allylamino-17-demethoxygeldanamycin binds to HSP90 and shares important biologic activities with geldanamycin. Cancer Chemother Pharmacol 1998; 42: 273-279.
    • (1998) Cancer Chemother. Pharmacol. , vol.42 , pp. 273-279
    • Schulte, T.W.1    Neckers, L.M.2
  • 416
    • 85047695528 scopus 로고    scopus 로고
    • Hsp-90-associated oncoproteins: Multiple targets of geldanamycin and its analogs
    • (Review)
    • Blagosklonny MV. Hsp-90-associated oncoproteins: multiple targets of geldanamycin and its analogs. Leukemia 2002; 16: 455-462 (Review).
    • (2002) Leukemia , vol.16 , pp. 455-462
    • Blagosklonny, M.V.1
  • 418
    • 0032761526 scopus 로고    scopus 로고
    • Anti-angiogenic activity of selected receptor tyrosine kinase inhibitors, PD166285 and PD173074: Implications for combination treatment with photodynamic therapy
    • Dimitroff CJ, Klohs W, Sharma A, Pera P, Driscoll D, Veith J et al. Anti-angiogenic activity of selected receptor tyrosine kinase inhibitors, PD166285 and PD173074: implications for combination treatment with photodynamic therapy. Invest New Drugs 1999; 17: 121-135.
    • (1999) Invest. New Drugs , vol.17 , pp. 121-135
    • Dimitroff, C.J.1    Klohs, W.2    Sharma, A.3    Pera, P.4    Driscoll, D.5    Veith, J.6
  • 419
    • 0031471249 scopus 로고    scopus 로고
    • In vitro pharmacological characterization of PD 166285, a new nanomolar potent and broadly active protein tyrosine kinase inhibitor
    • Panek RL, Lu GH, Klutchko SR, Batley BL, Dahring TK, Hamby JM et al. In vitro pharmacological characterization of PD 166285, a new nanomolar potent and broadly active protein tyrosine kinase inhibitor. J Pharmacol Exp Ther 1997; 283: 1433-1444.
    • (1997) J. Pharmacol. Exp. Ther. , vol.283 , pp. 1433-1444
    • Panek, R.L.1    Lu, G.H.2    Klutchko, S.R.3    Batley, B.L.4    Dahring, T.K.5    Hamby, J.M.6
  • 420
    • 0042237015 scopus 로고    scopus 로고
    • The role of Src-kinase in the regulation of endocytosis of EGF-receptor complexes. I. Dynamics of EGF internalization, recycling, sorting, and degradation during inhibition of Src-kinase activity
    • Zheleznova NN, Melikova MS, Nikol'skii NN, Kornilova ES. [The role of Src-kinase in the regulation of endocytosis of EGF-receptor complexes. I. Dynamics of EGF internalization, recycling, sorting, and degradation during inhibition of Src-kinase activity]. Tsitologiia 2001; 43: 1136-1145.
    • (2001) Tsitologiia , vol.43 , pp. 1136-1145
    • Zheleznova, N.N.1    Melikova, M.S.2    Nikol'skii, N.N.3    Kornilova, E.S.4
  • 421
    • 2242463133 scopus 로고    scopus 로고
    • The role of Src-kinase in the regulation of endocytosis of EGF-receptor complexes. Distribution of clathrin after stimulation of EGR endocytosis in various cell lines during inhibition of Src-kinase activity
    • Melikova MS, Zheleznova NN, Nikol'skii NN, Kornilova ES. [The role of Src-kinase in the regulation of endocytosis of EGF-receptor complexes. Distribution of clathrin after stimulation of EGR endocytosis in various cell lines during inhibition of Src-kinase activity]. Tsitologiia 2001; 43: 1146-1152.
    • (2001) Tsitologiia , vol.43 , pp. 1146-1152
    • Melikova, M.S.1    Zheleznova, N.N.2    Nikol'skii, N.N.3    Kornilova, E.S.4
  • 423
    • 0036137934 scopus 로고    scopus 로고
    • Fluoroaluminate stimulates phosphorylation of p130 Cas and Fak and increases attachment and spreading of preosteoblastic MC353-E1 cells
    • Freitas F, Jeschke M, Majstorovic I, Mueller DR, Schindler P, Voshol H et al. Fluoroaluminate stimulates phosphorylation of p130 Cas and Fak and increases attachment and spreading of preosteoblastic MC353-E1 cells. Bone 2002; 30: 99-108.
    • (2002) Bone , vol.30 , pp. 99-108
    • Freitas, F.1    Jeschke, M.2    Majstorovic, I.3    Mueller, D.R.4    Schindler, P.5    Voshol, H.6
  • 424
    • 0035399133 scopus 로고    scopus 로고
    • An essential role for Src kinase in ErbB receptor signaling through the MAPK pathway
    • Olayioye MA, Badache A, Daly JM, Hynes NE. An essential role for Src kinase in ErbB receptor signaling through the MAPK pathway. Exp Cell Res 2001; 267: 81-87.
    • (2001) Exp. Cell Res. , vol.267 , pp. 81-87
    • Olayioye, M.A.1    Badache, A.2    Daly, J.M.3    Hynes, N.E.4
  • 425
    • 0035990909 scopus 로고    scopus 로고
    • Structural studies with inhibitors of the cell cycle regulatory kinase cyclin-dependent protein kinase 2
    • Johnson L, De Moliner E, Brown N, Song H, Barford D, Endicott J et al. Structural studies with inhibitors of the cell cycle regulatory kinase cyclin-dependent protein kinase 2. Pharmacol Ther 2002; 93: 113.
    • (2002) Pharmacol. Ther. , vol.93 , pp. 113
    • Johnson, L.1    De Moliner, E.2    Brown, N.3    Song, H.4    Barford, D.5    Endicott, J.6
  • 426
    • 0036134037 scopus 로고    scopus 로고
    • Protein kinase C inhibitors
    • (Review)
    • Swannie HC, Kaye SB. Protein kinase C inhibitors. Curr Oncol Rep 2002; 4: 37-46 (Review).
    • (2002) Curr. Oncol. Rep. , vol.4 , pp. 37-46
    • Swannie, H.C.1    Kaye, S.B.2
  • 427
    • 0034280331 scopus 로고    scopus 로고
    • Protein kinase C as a drug target: Implications for drug or diet prevention and treatment of cancer
    • (Review)
    • Carter CA. Protein kinase C as a drug target: implications for drug or diet prevention and treatment of cancer. Curr Drug Targets 2000; 1: 163-183 (Review).
    • (2000) Curr. Drug Targets , vol.1 , pp. 163-183
    • Carter, C.A.1
  • 428
    • 0035826163 scopus 로고    scopus 로고
    • Staurosporine and conventional anticancer drugs induce overlapping, yet distinct pathways of apoptosis and caspase activation
    • Stepczynska A, Lauber K, Engels IH, Janssen O, Kabelitz D, Wesselborg S et al. Staurosporine and conventional anticancer drugs induce overlapping, yet distinct pathways of apoptosis and caspase activation. Oncogene 2001; 20: 1193-1202.
    • (2001) Oncogene , vol.20 , pp. 1193-1202
    • Stepczynska, A.1    Lauber, K.2    Engels, I.H.3    Janssen, O.4    Kabelitz, D.5    Wesselborg, S.6
  • 429
    • 0032693143 scopus 로고    scopus 로고
    • Apoptosis regulating proteins as targets of therapy for haematological malignancies
    • Kornblau SM, Konopleva M, Andreeff M. Apoptosis regulating proteins as targets of therapy for haematological malignancies. Exp Opin Invest Drugs 1999; 8: 2027-2057.
    • (1999) Exp. Opin. Invest. Drugs , vol.8 , pp. 2027-2057
    • Kornblau, S.M.1    Konopleva, M.2    Andreeff, M.3
  • 431
    • 0035110776 scopus 로고    scopus 로고
    • UCN-01 Kyowa Hakko Kogyo Co
    • (Review)
    • Grosios K. UCN-01 Kyowa Hakko Kogyo Co. Curr Opin Invest Drugs 2001; 2: 287-297 (Review).
    • (2001) Curr. Opin. Invest. Drugs , vol.2 , pp. 287-297
    • Grosios, K.1
  • 432
    • 0036057475 scopus 로고    scopus 로고
    • The cell cycle as a target for cancer therapy: Basic and clinical findings with the small molecule inhibitors flavopiridol and UCN-01
    • Senderowicz AM. The cell cycle as a target for cancer therapy: basic and clinical findings with the small molecule inhibitors flavopiridol and UCN-01. Oncologist 2002; 2: 12-19.
    • (2002) Oncologist , vol.2 , pp. 12-19
    • Senderowicz, A.M.1
  • 433
    • 0037034928 scopus 로고    scopus 로고
    • Interference with PDK1-Akt survival signaling pathway by UCN-01 (7-hydroxystaurosporine)
    • Sato S, Fujita N, Tsuruo T. Interference with PDK1-Akt survival signaling pathway by UCN-01 (7-hydroxystaurosporine). Oncogene 2002; 21: 1727-1738.
    • (2002) Oncogene , vol.21 , pp. 1727-1738
    • Sato, S.1    Fujita, N.2    Tsuruo, T.3
  • 434
    • 0035657643 scopus 로고    scopus 로고
    • Protein kinase C inhibitors as novel anticancer drugs
    • (Review)
    • Goekjian PG, Jirousek MR. Protein kinase C inhibitors as novel anticancer drugs. Exp Opin Invest Drugs 2001; 10: 2117-2140 (Review).
    • (2001) Exp. Opin. Invest. Drugs , vol.10 , pp. 2117-2140
    • Goekjian, P.G.1    Jirousek, M.R.2
  • 435
    • 0034986264 scopus 로고    scopus 로고
    • UCN-01 induces cytotoxicity toward human CLL cells through a p53-independent mechanism
    • Byrd JC, Shinn C, Willis CR, Flinn IW, Lehman T, Sausville E et al. UCN-01 induces cytotoxicity toward human CLL cells through a p53-independent mechanism. Exp Hematol 2001; 29: 703-708.
    • (2001) Exp. Hematol. , vol.29 , pp. 703-708
    • Byrd, J.C.1    Shinn, C.2    Willis, C.R.3    Flinn, I.W.4    Lehman, T.5    Sausville, E.6
  • 436
    • 0029971096 scopus 로고    scopus 로고
    • The antitumor drug fostriecin induces vimentin hyperphosphorylation and intermediate filament reorganization
    • Ho DT, Roberge M. The antitumor drug fostriecin induces vimentin hyperphosphorylation and intermediate filament reorganization. Carcinogenesis 1996; 17: 967-972.
    • (1996) Carcinogenesis , vol.17 , pp. 967-972
    • Ho, D.T.1    Roberge, M.2
  • 437
    • 0036729475 scopus 로고    scopus 로고
    • Mechanisms of activation of NHE by cell shrinkage and by calyculin A in Ehrlich ascites tumor cells
    • Pederson SF, Varming C, Christensen ST, Hoffmann EK. Mechanisms of activation of NHE by cell shrinkage and by calyculin A in Ehrlich ascites tumor cells. J Membrane Biol 2002; 189: 67-81.
    • (2002) J. Membrane Biol. , vol.189 , pp. 67-81
    • Pederson, S.F.1    Varming, C.2    Christensen, S.T.3    Hoffmann, E.K.4
  • 438
    • 0037175021 scopus 로고    scopus 로고
    • A role for protein phosphatase-2A in p38 mitogen-activated protein kinase-mediated regulation of the c-Jun NH2-terminal kinase pathway in human neutrophils
    • Avdi NJ, Malcolm KC, Nick JA, Worthen GS. A role for protein phosphatase-2A in p38 mitogen-activated protein kinase-mediated regulation of the c-Jun NH2-terminal kinase pathway in human neutrophils. J Biol Chem 2002; 277: 40687-40696.
    • (2002) J. Biol. Chem. , vol.277 , pp. 40687-40696
    • Avdi, N.J.1    Malcolm, K.C.2    Nick, J.A.3    Worthen, G.S.4
  • 439
    • 0037125199 scopus 로고    scopus 로고
    • PP1/PP2A phosphatases inhibitors okadaic acid and calyculin A block ERK5 activation by growth factors and oxidative stress
    • Garcia L, Garcia F, Llorens F, Unzeta M, Itarte E, Gomez N. PP1/PP2A phosphatases inhibitors okadaic acid and calyculin A block ERK5 activation by growth factors and oxidative stress. FEBS Lett 2002; 523: 90-94.
    • (2002) FEBS Lett. , vol.523 , pp. 90-94
    • Garcia, L.1    Garcia, F.2    Llorens, F.3    Unzeta, M.4    Itarte, E.5    Gomez, N.6
  • 441
    • 0037188421 scopus 로고    scopus 로고
    • Evidence that protein phosphatase 5 functions to negatively modulate the maturation of the HSP90-dependent heme-regulated elF2alpha kinase
    • Shao J, Hartson SD, Matts RL. Evidence that protein phosphatase 5 functions to negatively modulate the maturation of the HSP90-dependent heme-regulated elF2alpha kinase. Biochemistry 2002; 41: 6770-6779.
    • (2002) Biochemistry , vol.41 , pp. 6770-6779
    • Shao, J.1    Hartson, S.D.2    Matts, R.L.3
  • 442
    • 0036220682 scopus 로고    scopus 로고
    • Protective effect of melatonin against nodularin-induced oxidative stress
    • Lankoff A, Banasik A, Nowak M. Protective effect of melatonin against nodularin-induced oxidative stress. Arch Toxicol 2002; 76: 158-165.
    • (2002) Arch. Toxicol. , vol.76 , pp. 158-165
    • Lankoff, A.1    Banasik, A.2    Nowak, M.3
  • 444
    • 0035978462 scopus 로고    scopus 로고
    • Microcystin-induced down-regulation of lymphocyte functions through reduced IL-2 mRNA stability
    • Yea SS, Kim HM, Oh HM, Paik KH, Yang KH. Microcystin-induced down-regulation of lymphocyte functions through reduced IL-2 mRNA stability. Toxicol Lett 2001; 122: 21-31.
    • (2001) Toxicol. Lett. , vol.122 , pp. 21-31
    • Yea, S.S.1    Kim, H.M.2    Oh, H.M.3    Paik, K.H.4    Yang, K.H.5
  • 445
    • 0034903549 scopus 로고    scopus 로고
    • Production and specificity of monoclonal antibodies against nodularin conjugated through N-methyldehydrobutyrine
    • Mikhailov A, Harmala-Brasken AS, Polosukhina E, Hanski A, Wahlsten M, Sivonen K et al. Production and specificity of monoclonal antibodies against nodularin conjugated through N-methyldehydrobutyrine. Toxicon 2001; 39: 1453-1459.
    • (2001) Toxicon , vol.39 , pp. 1453-1459
    • Mikhailov, A.1    Harmala-Brasken, A.S.2    Polosukhina, E.3    Hanski, A.4    Wahlsten, M.5    Sivonen, K.6
  • 446
    • 0036500193 scopus 로고    scopus 로고
    • Forskolin-mediated G1 arrest in acute lymphoblastic leukaemia cells: Phosphorylated pRB sequesters E2Fs
    • Gutzkow KB, Naderi S, Blomhoff HK. Forskolin-mediated G1 arrest in acute lymphoblastic leukaemia cells: phosphorylated pRB sequesters E2Fs. J Cell Sci 2002; 115: 1073-1082.
    • (2002) J. Cell Sci. , vol.115 , pp. 1073-1082
    • Gutzkow, K.B.1    Naderi, S.2    Blomhoff, H.K.3
  • 447
    • 0035283087 scopus 로고    scopus 로고
    • Protein phosphatase 2A activates the proapoptotic function of BAD in interleukin-3-dependent lymphoid cells by a mechanism requiring 14-3-3 dissociation
    • Chiang CW, Harris G, Ellig C, Masters SC, Subramanian R, Shenolikar S et al. Protein phosphatase 2A activates the proapoptotic function of BAD in interleukin-3-dependent lymphoid cells by a mechanism requiring 14-3-3 dissociation. Blood 2001; 97: 1289-1297.
    • (2001) Blood , vol.97 , pp. 1289-1297
    • Chiang, C.W.1    Harris, G.2    Ellig, C.3    Masters, S.C.4    Subramanian, R.5    Shenolikar, S.6
  • 450
    • 0037075845 scopus 로고    scopus 로고
    • Serine-threonine protein phosphatase inhibitors: Development of potential therapeutic strategies
    • (Review)
    • McCluskey A, Sim AT, Sakoff JA. Serine-threonine protein phosphatase inhibitors: development of potential therapeutic strategies. J Med Chem 2002; 45: 1151-1175 (Review).
    • (2002) J. Med. Chem. , vol.45 , pp. 1151-1175
    • McCluskey, A.1    Sim, A.T.2    Sakoff, J.A.3
  • 451
    • 0036154215 scopus 로고    scopus 로고
    • Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes
    • Resjo S, Goransson O, Harndahl L, Zolnierowicz S, Manganiello V, Degerman E. Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes. Cell Signal 2002; 14: 231-238.
    • (2002) Cell Signal , vol.14 , pp. 231-238
    • Resjo, S.1    Goransson, O.2    Harndahl, L.3    Zolnierowicz, S.4    Manganiello, V.5    Degerman, E.6
  • 452
    • 0033209692 scopus 로고    scopus 로고
    • The apoptosis-inducing activity of the two protein phosphatase inhibitors, tautomycin and thyrsiferyl 23-acetate, is not due to the inhibition of protein phosphatases PP1 and PP2A
    • (review) (Review)
    • Kikuchi K, Shima H, Mitsuhashi S, Suzuki M, Oikawa H. The apoptosis-inducing activity of the two protein phosphatase inhibitors, tautomycin and thyrsiferyl 23-acetate, is not due to the inhibition of protein phosphatases PP1 and PP2A (review). Int J Mol Med 1999; 4: 395-401 (Review).
    • (1999) Int. J. Mol. Med. , vol.4 , pp. 395-401
    • Kikuchi, K.1    Shima, H.2    Mitsuhashi, S.3    Suzuki, M.4    Oikawa, H.5
  • 453
  • 454
    • 0027946005 scopus 로고
    • Thyrsiferyl 23-acetate is a novel specific inhibitor of protein phosphatase PP2A
    • Matsuzawa S, Suzuki T, Suzuki M, Matsuda A, Kawamura T, Mizuno Y et al. Thyrsiferyl 23-acetate is a novel specific inhibitor of protein phosphatase PP2A. FEBS Lett 1994; 356: 272-274.
    • (1994) FEBS Lett. , vol.356 , pp. 272-274
    • Matsuzawa, S.1    Suzuki, T.2    Suzuki, M.3    Matsuda, A.4    Kawamura, T.5    Mizuno, Y.6
  • 456
    • 0033229838 scopus 로고    scopus 로고
    • Effects of sesquiterpenes and triterpenes from the rhizome of Alisma orientale on nitric oxide production in lipopolysaccharide-activated macrophages: Absolute stereostructures of alismaketones-B 23-acetate and -C 23-acetate
    • Matsuda H, Kageura T, Toguchicla I, Murakami T, Kishi A, Yoshikawa M. Effects of sesquiterpenes and triterpenes from the rhizome of Alisma orientale on nitric oxide production in lipopolysaccharide-activated macrophages: absolute stereostructures of alismaketones-B 23-acetate and -C 23-acetate. Bioorg Med Chem Lett 1999; 9: 3081-3086.
    • (1999) Bioorg. Med. Chem. Lett. , vol.9 , pp. 3081-3086
    • Matsuda, H.1    Kageura, T.2    Toguchicla, I.3    Murakami, T.4    Kishi, A.5    Yoshikawa, M.6
  • 457
    • 0035998334 scopus 로고    scopus 로고
    • Comparison of protein phosphatase inhibitory activity and apparent toxicity of microcystins and related compounds
    • Ito E, Takai A, Kondo F, Masui H, Imanishi S, Harada K. Comparison of protein phosphatase inhibitory activity and apparent toxicity of microcystins and related compounds. Toxicon 2002; 40: 1017-1025.
    • (2002) Toxicon , vol.40 , pp. 1017-1025
    • Ito, E.1    Takai, A.2    Kondo, F.3    Masui, H.4    Imanishi, S.5    Harada, K.6
  • 458
    • 0036045296 scopus 로고    scopus 로고
    • Possible allelopathic effects of cyanotoxins, with reference to microcystin-LR, in aquatic ecosystems
    • Pflugmacher S. Possible allelopathic effects of cyanotoxins, with reference to microcystin-LR, in aquatic ecosystems. Environ Toxicol 2002; 17: 407-413.
    • (2002) Environ. Toxicol. , vol.17 , pp. 407-413
    • Pflugmacher, S.1
  • 459
    • 0036050059 scopus 로고    scopus 로고
    • Genotoxicity of cyanobacterial extracts containing microcystins from Polish water reservoirs as determined by SOS chromotest and comet assay
    • Mankiewicz J, Walter Z, Tarczynska M, Palyvoda O, Wojtysiak-Staniaszczyk M, Zalewski M. Genotoxicity of cyanobacterial extracts containing microcystins from Polish water reservoirs as determined by SOS chromotest and comet assay. Environ Toxicol 2002; 17: 341-350.
    • (2002) Environ. Toxicol. , vol.17 , pp. 341-350
    • Mankiewicz, J.1    Walter, Z.2    Tarczynska, M.3    Palyvoda, O.4    Wojtysiak-Staniaszczyk, M.5    Zalewski, M.6
  • 460
    • 0035993533 scopus 로고    scopus 로고
    • Toxicity of cylindrospermopsin to the brine shrimp Artemia salina: Comparisons with protein synthesis inhibitors and microcystins
    • Metcalf JS, Lindsay J, Beattie KA, Birmingham S, Saker ML, Torokne AK, Codd GA. Toxicity of cylindrospermopsin to the brine shrimp Artemia salina: comparisons with protein synthesis inhibitors and microcystins. Toxicon 2002; 40: 1115-1120.
    • (2002) Toxicon , vol.40 , pp. 1115-1120
    • Metcalf, J.S.1    Lindsay, J.2    Beattie, K.A.3    Birmingham, S.4    Saker, M.L.5    Torokne, A.K.6    Codd, G.A.7
  • 461
    • 0037144405 scopus 로고    scopus 로고
    • Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes
    • Larsen AK, Moller MT, Blankson H, Samari HR, Holden L, Seglen PO. Naringin-sensitive phosphorylation of plectin, a cytoskeletal cross-linking protein, in isolated rat hepatocytes. J Biol Chem 2002; 277: 34826-34835.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34826-34835
    • Larsen, A.K.1    Moller, M.T.2    Blankson, H.3    Samari, H.R.4    Holden, L.5    Seglen, P.O.6
  • 462
    • 0032528624 scopus 로고    scopus 로고
    • Fostriecin-mediated G2-M-phase growth arrest correlates with abnormal centrosome replication, the formation of aberrant mitotic spindles, and the inhibition of serine/threonine protein phosphatase activity
    • Cheng A, Balczon R, Zuo Z, Koons JS, Walsh AH, Honkanen RE. Fostriecin-mediated G2-M-phase growth arrest correlates with abnormal centrosome replication, the formation of aberrant mitotic spindles, and the inhibition of serine/threonine protein phosphatase activity. Cancer Res 1998; 58: 3611-3619.
    • (1998) Cancer Res. , vol.58 , pp. 3611-3619
    • Cheng, A.1    Balczon, R.2    Zuo, Z.3    Koons, J.S.4    Walsh, A.H.5    Honkanen, R.E.6
  • 463
    • 0031005019 scopus 로고    scopus 로고
    • Somatostatin acts by inhibiting the cyclic 3′,5′-adenosine monophosphate (cAMP)/protein kinase A pathway, cAMP response element-binding protein (CREB) phosphorylation, and CREB transcription potency
    • Tentler JJ, Hadcock JR, Gutierrez-Hartmann A. Somatostatin acts by inhibiting the cyclic 3′,5′-adenosine monophosphate (cAMP)/protein kinase A pathway, cAMP response element-binding protein (CREB) phosphorylation, and CREB transcription potency. Mol Endocrinol 1997; 11: 859-866.
    • (1997) Mol. Endocrinol. , vol.11 , pp. 859-866
    • Tentler, J.J.1    Hadcock, J.R.2    Gutierrez-Hartmann, A.3
  • 464
    • 0029971096 scopus 로고    scopus 로고
    • The antitumor drug fostriecin induces vimentin hyperphosphorylation and intermediate filament reorganization
    • Ho DT, Roberge M. The antitumor drug fostriecin induces vimentin hyperphosphorylation and intermediate filament reorganization. Carcinogenesis 1996; 17: 967-972.
    • (1996) Carcinogenesis , vol.17 , pp. 967-972
    • Ho, D.T.1    Roberge, M.2
  • 465
    • 0036165251 scopus 로고    scopus 로고
    • Pharmacological inhibitors of MAPK pathways
    • English JM, Cobb MH. Pharmacological inhibitors of MAPK pathways. Trends Pharmcol Sci 2002; 23: 40-45.
    • (2002) Trends Pharmcol. Sci. , vol.23 , pp. 40-45
    • English, J.M.1    Cobb, M.H.2
  • 466
    • 0036882092 scopus 로고    scopus 로고
    • Oral antibiotics with anti inflammatory/immunomodulatory effects in the treatment of various dermatoses
    • Brinkmeier T, Frosch PJ. [Oral antibiotics with anti inflammatory/immunomodulatory effects in the treatment of various dermatoses]. Hautarzt2002; 53: 456-465.
    • (2002) Hautarzt , vol.53 , pp. 456-465
    • Brinkmeier, T.1    Frosch, P.J.2
  • 467
  • 468
    • 0036738595 scopus 로고    scopus 로고
    • Clinical and pharmacokinetic study of fractionated doses of oral etoposide in pediatric patients with advanced malignancies
    • Gregianin LJ, Brunetto AL, Di Leone L, Lurito JT, Santos PP, Schwartsmann G et al. Clinical and pharmacokinetic study of fractionated doses of oral etoposide in pediatric patients with advanced malignancies. Med Sci Monit 2002; 8P: 170-177.
    • (2002) Med. Sci. Monit. , vol.8 , Issue.P , pp. 170-177
    • Gregianin, L.J.1    Brunetto, A.L.2    Di Leone, L.3    Lurito, J.T.4    Santos, P.P.5    Schwartsmann, G.6
  • 470
    • 0038303997 scopus 로고    scopus 로고
    • Protein kinase C (zeta) mediated Raf-1/extracellular-regulated kinase activation by daunorubicin
    • Mansat-De Mas V, Hernandez H, Plo I, Bezombes C, Maestre N et al. Protein kinase C (zeta) mediated Raf-1/extracellular-regulated kinase activation by daunorubicin. Blood 2002; 24: 646-653.
    • (2002) Blood , vol.24 , pp. 646-653
    • Mansat-De Mas, V.1    Hernandez, H.2    Plo, I.3    Bezombes, C.4    Maestre, N.5
  • 471
    • 0034833942 scopus 로고    scopus 로고
    • Roles of extracellular signal-regulated kinase and p38 mitogen-activated protein kinase in apoptosis of human monoblastic leukemia U937 cells by lectin-II isolated from Korean mistletoe
    • Pae HO, Oh GS, Kim NY, Shin MK, Lee HS, Yun YG et al. Roles of extracellular signal-regulated kinase and p38 mitogen-activated protein kinase in apoptosis of human monoblastic leukemia U937 cells by lectin-II isolated from Korean mistletoe. In Vitro Mol Toxicol 2001; 14: 99-106.
    • (2001) In Vitro Mol. Toxicol. , vol.14 , pp. 99-106
    • Pae, H.O.1    Oh, G.S.2    Kim, N.Y.3    Shin, M.K.4    Lee, H.S.5    Yun, Y.G.6
  • 472
    • 0034986615 scopus 로고    scopus 로고
    • TGF beta-induced SMAD2 phosphorylation predicts inhibition of thymidine incorporation in CD34+ cells from healthy donors, but not from patients with AML after MDS
    • Koschmieder S, Hofmann WK, Kunert J, Wagner S, Ballas K, Seipelt G et al. TGF beta-induced SMAD2 phosphorylation predicts inhibition of thymidine incorporation in CD34+ cells from healthy donors, but not from patients with AML after MDS. Leukemia 2001; 15: 942-949.
    • (2001) Leukemia , vol.15 , pp. 942-949
    • Koschmieder, S.1    Hofmann, W.K.2    Kunert, J.3    Wagner, S.4    Ballas, K.5    Seipelt, G.6
  • 473
    • 0035007685 scopus 로고    scopus 로고
    • Transforming growth factor-betal interferes with thrombopoietin-induced signal transduction in megakaryoblastic and erythroleukemic cells
    • Kalina U, Koschmieder S, Hofmann WK, Wagner S, Kauschat D, Hoelzer D et al. Transforming growth factor-betal interferes with thrombopoietin-induced signal transduction in megakaryoblastic and erythroleukemic cells. Exp Hematol 2001; 29: 602-608.
    • (2001) Exp. Hematol. , vol.29 , pp. 602-608
    • Kalina, U.1    Koschmieder, S.2    Hofmann, W.K.3    Wagner, S.4    Kauschat, D.5    Hoelzer, D.6
  • 474
    • 0035958901 scopus 로고    scopus 로고
    • The p38 MAPK pathway mediates the growth inhibitory effects of interferon-alpha in BCR-ABL-expressing cells
    • Mayer IA, Verma A, Grumbach IM, Uddin S, Lekmine F, Ravandi F et al. The p38 MAPK pathway mediates the growth inhibitory effects of interferon-alpha in BCR-ABL-expressing cells. J Biol Chem 2001; 276: 28570-28577.
    • (2001) J. Biol. Chem. , vol.276 , pp. 28570-28577
    • Mayer, I.A.1    Verma, A.2    Grumbach, I.M.3    Uddin, S.4    Lekmine, F.5    Ravandi, F.6
  • 475
    • 0035869396 scopus 로고    scopus 로고
    • Cell-cycle-dependent activation of mitogen-activated protein kinase kinase (MEK-1/2) in myeloid leukemia cell lines and induction of growth inhibition and apoptosis by inhibitors of RAS signaling
    • Morgan MA, Dolp O, Reuter CW. Cell-cycle-dependent activation of mitogen-activated protein kinase kinase (MEK-1/2) in myeloid leukemia cell lines and induction of growth inhibition and apoptosis by inhibitors of RAS signaling. Blood 2001; 97: 1823-1834.
    • (2001) Blood , vol.97 , pp. 1823-1834
    • Morgan, M.A.1    Dolp, O.2    Reuter, C.W.3
  • 477
    • 0037183703 scopus 로고    scopus 로고
    • Activation of Go-coupled dopamine D2 receptors inhibits ERK1/ERK2 in pituitary cells. A key step in the transcriptional suppression of the prolactin gene
    • Liu JC, Baker RE, Sun C, Sundmark VC, Elsholtz HP. Activation of Go-coupled dopamine D2 receptors inhibits ERK1/ERK2 in pituitary cells. A key step in the transcriptional suppression of the prolactin gene. J Biol Chem 2002; 277: 35819-35825.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35819-35825
    • Liu, J.C.1    Baker, R.E.2    Sun, C.3    Sundmark, V.C.4    Elsholtz, H.P.5
  • 478
    • 0036714366 scopus 로고    scopus 로고
    • Cell-cycle arrest by PD184352 requires inhibition of extracellular signal-regulated kinases (ERK) 1/2 but not ERK5/BMK1
    • Squires MS, Nixon PM, Cook SJ. Cell-cycle arrest by PD184352 requires inhibition of extracellular signal-regulated kinases (ERK) 1/2 but not ERK5/BMK1. Biochem J 2002; 366, 673-680.
    • (2002) Biochem. J. , vol.366 , pp. 673-680
    • Squires, M.S.1    Nixon, P.M.2    Cook, S.J.3
  • 479
    • 0036566242 scopus 로고    scopus 로고
    • Synergistic induction of apoptosis by simultaneous disruption of the Bcl-2 and MEK/MAPK pathways in acute myelogenous leukemia
    • Milella M, Estrov Z, Kornblau SM, Carter BZ, Konopleva M, Tari A et al. Synergistic induction of apoptosis by simultaneous disruption of the Bcl-2 and MEK/MAPK pathways in acute myelogenous leukemia. Blood 2002; 99: 3461-3464.
    • (2002) Blood , vol.99 , pp. 3461-3464
    • Milella, M.1    Estrov, Z.2    Kornblau, S.M.3    Carter, B.Z.4    Konopleva, M.5    Tari, A.6
  • 480
    • 0036284741 scopus 로고    scopus 로고
    • Establishment and characterization of acquired resistance to the farnesyl protein transferase inhibitor r115777 in a human colon cancer cell line
    • Smith V, Rowlands MG, Barrie E, Workman P, Kelland LR. Establishment and characterization of acquired resistance to the farnesyl protein transferase inhibitor r115777 in a human colon cancer cell line. Clin Cancer Res 2002; 8: 2002-2009.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 2002-2009
    • Smith, V.1    Rowlands, M.G.2    Barrie, E.3    Workman, P.4    Kelland, L.R.5
  • 481
    • 0036707484 scopus 로고    scopus 로고
    • -) channel beta subunit is required for mitogen-activated protein kinase (MAPK)-dependent modulation of alpha 1B Ca(2+) channels in COS-7 cells
    • -) channel beta subunit is required for mitogen-activated protein kinase (MAPK)-dependent modulation of alpha 1B Ca(2+) channels in COS-7 cells. J Physiol 2002; 543: 425-437.
    • (2002) J. Physiol. , vol.543 , pp. 425-437
    • Fitzgerald, E.M.1
  • 482
    • 0037184080 scopus 로고    scopus 로고
    • Anti-apoptotic signaling of pleiotrophin through its receptor, anaplastic lymphoma kinase
    • Bowden ET, Stoica GE, Wellstein A. Anti-apoptotic signaling of pleiotrophin through its receptor, anaplastic lymphoma kinase. J Biol Chem 2002; 277: 35862-35868.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35862-35868
    • Bowden, E.T.1    Stoica, G.E.2    Wellstein, A.3
  • 483
    • 0037013205 scopus 로고    scopus 로고
    • Signal pathways involved in activation of p70S6K and phosphorylation of 4E-BP1 following exposure of multiple myeloma tumor cells to interleukin-6
    • Shi Y, Hsu JH, Hu L, Gera J, Lichtenstein A. Signal pathways involved in activation of p70S6K and phosphorylation of 4E-BP1 following exposure of multiple myeloma tumor cells to interleukin-6. J Biol Chem 2002; 277: 15712-15720.
    • (2002) J. Biol. Chem. , vol.277 , pp. 15712-15720
    • Shi, Y.1    Hsu, J.H.2    Hu, L.3    Gera, J.4    Lichtenstein, A.5
  • 484
    • 0036175936 scopus 로고    scopus 로고
    • Inorganic lead activates the mitogen-activated protein kinase kinase-mitogen-activated protein kinase-p90(RSK) signaling pathway in human astrocytoma cells via a protein kinase C-dependent mechanism
    • Lu H, Guizzetti M, Costa LG. Inorganic lead activates the mitogen-activated protein kinase kinase-mitogen-activated protein kinase-p90(RSK) signaling pathway in human astrocytoma cells via a protein kinase C-dependent mechanism. J Pharmacol Exp Ther 2002; 300: 818-823.
    • (2002) J. Pharmacol. Exp. Ther. , vol.300 , pp. 818-823
    • Lu, H.1    Guizzetti, M.2    Costa, L.G.3
  • 485
    • 0035914258 scopus 로고    scopus 로고
    • Cross-talk between signalling pathways and the multidrug resistant protein MDR-1
    • Ding S, Chamberlain M, McLaren A, Goh L, Duncan I, Wolf CR. Cross-talk between signalling pathways and the multidrug resistant protein MDR-1. Br J Cancer 2001; 85: 1175-1184.
    • (2001) Br. J. Cancer , vol.85 , pp. 1175-1184
    • Ding, S.1    Chamberlain, M.2    McLaren, A.3    Goh, L.4    Duncan, I.5    Wolf, C.R.6
  • 486
    • 0036034849 scopus 로고    scopus 로고
    • Regulation of ionomycin-mediated granule release from rat basophil leukemia cells
    • Hanson D, Ziegler S. Regulation of ionomycin-mediated granule release from rat basophil leukemia cells. Mol Immunol 2002; 38: 1329.
    • (2002) Mol. Immunol. , vol.38 , pp. 1329
    • Hanson, D.1    Ziegler, S.2
  • 487
    • 0037113978 scopus 로고    scopus 로고
    • Dual regulation of phosphorylation and dephosphorylation of C/EBPbeta modulate its transcriptional activation and DNA binding in response to growth hormone
    • Piwien-Pilipuk G, MacDougald O, Schwartz J. Dual regulation of phosphorylation and dephosphorylation of C/EBPbeta modulate its transcriptional activation and DNA binding in response to growth hormone. J Biol Chem 2002; 277: 44557-44565.
    • (2002) J. Biol. Chem. , vol.277 , pp. 44557-44565
    • Piwien-Pilipuk, G.1    MacDougald, O.2    Schwartz, J.3
  • 488
    • 0037044770 scopus 로고    scopus 로고
    • Serotonin-induced MMP-13 production is mediated via phospholipase C, protein kinase C and ERK1/2 in rat uterine smooth muscle cells
    • Shum JK, Melendez JA, Jeffrey JJ. Serotonin-induced MMP-13 production is mediated via phospholipase C, protein kinase C and ERK1/2 in rat uterine smooth muscle cells. J Biol Chem 2002; 277: 42830-42840.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42830-42840
    • Shum, J.K.1    Melendez, J.A.2    Jeffrey, J.J.3
  • 489
    • 0036779370 scopus 로고    scopus 로고
    • Proliferation of IL-6-independent multiple myeloma does not require the activity of extracellular signal-regulated kinases (ERK1/2)
    • Zhang B, Fenton RG. Proliferation of IL-6-independent multiple myeloma does not require the activity of extracellular signal-regulated kinases (ERK1/2). J Cell Physiol 2002; 193: 42-54.
    • (2002) J. Cell Physiol. , vol.193 , pp. 42-54
    • Zhang, B.1    Fenton, R.G.2
  • 490
    • 0036672263 scopus 로고    scopus 로고
    • Nitric oxide inhibits endothelin-1 production through the suppression of nuclear factor kappa B
    • Ohkita M, Takaoka M, Shiota Y, Nojiri R, Matsumura Y. Nitric oxide inhibits endothelin-1 production through the suppression of nuclear factor kappa B. Clin Sci (Lond) 2002; 103: 68S-71S.
    • (2002) Clin. Sci. (Lond) , vol.103
    • Ohkita, M.1    Takaoka, M.2    Shiota, Y.3    Nojiri, R.4    Matsumura, Y.5
  • 491
    • 0036721164 scopus 로고    scopus 로고
    • Bay 11-7082 inhibits transcription factor NF-kappaB and induces apoptosis of HTLV-I-infected T-cell lines and primary adult T-cell leukemia cells
    • Mori N, Yamada Y, Ikeda S, Yamasaki Y, Tsukasaki K, Tanaka Y et al. Bay 11-7082 inhibits transcription factor NF-kappaB and induces apoptosis of HTLV-I-infected T-cell lines and primary adult T-cell leukemia cells. Blood 2002; 100: 1828-1834.
    • (2002) Blood , vol.100 , pp. 1828-1834
    • Mori, N.1    Yamada, Y.2    Ikeda, S.3    Yamasaki, Y.4    Tsukasaki, K.5    Tanaka, Y.6
  • 492
    • 0036551325 scopus 로고    scopus 로고
    • Interleukin-15 inhibits spontaneous apoptosis in human eosinophils via autocrine production of granulocyte macrophage-colony stimulating factor and nuclear factor-kappaB activation
    • Hoontrakoon R, Chu HW, Gardai SJ, Wenzel SE, McDonald P, Fadok VA et al. Interleukin-15 inhibits spontaneous apoptosis in human eosinophils via autocrine production of granulocyte macrophage-colony stimulating factor and nuclear factor-kappaB activation. Am J Respir Cell Mol Biol 2002; 26: 404-412.
    • (2002) Am. J. Respir. Cell Mol. Biol. , vol.26 , pp. 404-412
    • Hoontrakoon, R.1    Chu, H.W.2    Gardai, S.J.3    Wenzel, S.E.4    McDonald, P.5    Fadok, V.A.6
  • 493
    • 0035504081 scopus 로고    scopus 로고
    • Transcriptional regulation of bcl-2 by nuclear factor kappa B and its significance in prostate cancer
    • Catz SD, Johnson JL. Transcriptional regulation of bcl-2 by nuclear factor kappa B and its significance in prostate cancer. Oncogene 2001; 20: 7342-7351.
    • (2001) Oncogene , vol.20 , pp. 7342-7351
    • Catz, S.D.1    Johnson, J.L.2
  • 494
    • 0035824664 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha regulates the expression of inducible costimulator receptor ligand on CD34(+) progenitor cells during differentiation into antigen presenting cells
    • Richter G, Hayden-Ledbetter M, Irgang M, Ledbetter JA, Westermann J, Korner I et al. Tumor necrosis factor-alpha regulates the expression of inducible costimulator receptor ligand on CD34(+) progenitor cells during differentiation into antigen presenting cells. J Biol Chem 2001; 276: 45686-45693.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45686-45693
    • Richter, G.1    Hayden-Ledbetter, M.2    Irgang, M.3    Ledbetter, J.A.4    Westermann, J.5    Korner, I.6
  • 495
    • 0034287445 scopus 로고    scopus 로고
    • Inhibition of NF-kappaB induces apoptosis of KSHV-infected primary effusion lymphoma cells
    • Keller SA, Schattner EJ, Cesarman E. Inhibition of NF-kappaB induces apoptosis of KSHV-infected primary effusion lymphoma cells. Blood 2000; 96: 2537-2542.
    • (2000) Blood , vol.96 , pp. 2537-2542
    • Keller, S.A.1    Schattner, E.J.2    Cesarman, E.3
  • 496
    • 0034032010 scopus 로고    scopus 로고
    • Insulin-like growth factor-I protects colon cancer cells from death factor-induced apoptosis by potentiating tumor necrosis factor alpha-induced mitogen-activated protein kinase and nuclear factor kappaB signaling pathways
    • Remacle-Bonnet MM, Garrouste FL, Heller S, Andre F, Marvaldi JL, Pommier GJ. Insulin-like growth factor-I protects colon cancer cells from death factor-induced apoptosis by potentiating tumor necrosis factor alpha-induced mitogen-activated protein kinase and nuclear factor kappaB signaling pathways. Cancer Res 2000; 60: 2007-2017.
    • (2000) Cancer Res. , vol.60 , pp. 2007-2017
    • Remacle-Bonnet, M.M.1    Garrouste, F.L.2    Heller, S.3    Andre, F.4    Marvaldi, J.L.5    Pommier, G.J.6
  • 498
    • 0035824664 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha regulates the expression of inducible costimulator receptor ligand on CD34(+) progenitor cells during differentiation into antigen presenting cells
    • Richter G, Hayden-Ledbetter M, Irgang M, Ledbetter JA, Westermann J, Korner I et al. Tumor necrosis factor-alpha regulates the expression of inducible costimulator receptor ligand on CD34(+) progenitor cells during differentiation into antigen presenting cells. J Biol Chem 2001; 276: 45686-45693.
    • (2001) J. Biol. Chem. , vol.276 , pp. 45686-45693
    • Richter, G.1    Hayden-Ledbetter, M.2    Irgang, M.3    Ledbetter, J.A.4    Westermann, J.5    Korner, I.6
  • 499
    • 0035880275 scopus 로고    scopus 로고
    • An IkappaBalpha inhibitor causes leukemia cell death through a p38 MAP kinase-dependent, NF-kappaB-independent mechanism
    • Hu X, Janssen WE, Moscinski LC, Bryington M, Dangsupa A, Rezai-Zadeh N et al. An IkappaBalpha inhibitor causes leukemia cell death through a p38 MAP kinase-dependent, NF-kappaB-independent mechanism. Cancer Res 2001; 61: 6290-6296.
    • (2001) Cancer Res. , vol.61 , pp. 6290-6296
    • Hu, X.1    Janssen, W.E.2    Moscinski, L.C.3    Bryington, M.4    Dangsupa, A.5    Rezai-Zadeh, N.6
  • 500
    • 0034518556 scopus 로고    scopus 로고
    • Constitutive expression of NF-kappa B is a characteristic feature of mycosis fungoides: Implications for apoptosis resistance and pathogenesis
    • Izban KF, Ergin M, Qin JZ, Martinez RL, Pooley RJ, Saeed S et al. Constitutive expression of NF-kappa B is a characteristic feature of mycosis fungoides: implications for apoptosis resistance and pathogenesis. Hum Pathol 2000; 31: 1482-1490.
    • (2000) Hum. Pathol. , vol.31 , pp. 1482-1490
    • Izban, K.F.1    Ergin, M.2    Qin, J.Z.3    Martinez, R.L.4    Pooley, R.J.5    Saeed, S.6
  • 501
    • 0036676714 scopus 로고    scopus 로고
    • Anti-trypanosomal activity of helenalin and some structurally related sesquiterpene lactones
    • Schmidt TJ, Brun R, Willuhn G, Khalid SA. Anti-trypanosomal activity of helenalin and some structurally related sesquiterpene lactones. Planta Med 2002; 68: 750-751.
    • (2002) Planta Med. , vol.68 , pp. 750-751
    • Schmidt, T.J.1    Brun, R.2    Willuhn, G.3    Khalid, S.A.4
  • 502
    • 0035479825 scopus 로고    scopus 로고
    • Inhibitory effects of helenalin and related compounds on 5-lipoxygenase and leukotriene C(4) synthase in human blood cells
    • Tornhamre S, Schmidt TJ, Nasman-Glaser B, Ericsson I, Lindgren JA. Inhibitory effects of helenalin and related compounds on 5-lipoxygenase and leukotriene C(4) synthase in human blood cells. Biochem Pharmacol 2001; 62: 903-911.
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 903-911
    • Tornhamre, S.1    Schmidt, T.J.2    Nasman-Glaser, B.3    Ericsson, I.4    Lindgren, J.A.5
  • 503
    • 0034871746 scopus 로고    scopus 로고
    • Cytotoxic sesquiterpene lactones mediate their death-inducing effect in leukemia T cells by triggering apoptosis
    • Dirsch VM, Stuppner H, Vollmar AM. Cytotoxic sesquiterpene lactones mediate their death-inducing effect in leukemia T cells by triggering apoptosis. Planta Med 2001; 67: 557-559.
    • (2001) Planta Med. , vol.67 , pp. 557-559
    • Dirsch, V.M.1    Stuppner, H.2    Vollmar, A.M.3
  • 504
    • 0034902498 scopus 로고    scopus 로고
    • The influence of glutathione and cysteine levels on the cytotoxicity of helenanolide type sesquiterpene lactones against KB cells
    • Heilmann J, Wasescha MR, Schmidt TJ. The influence of glutathione and cysteine levels on the cytotoxicity of helenanolide type sesquiterpene lactones against KB cells. Bioorg Med Chem 2001; 9: 2189-2194.
    • (2001) Bioorg. Med. Chem. , vol.9 , pp. 2189-2194
    • Heilmann, J.1    Wasescha, M.R.2    Schmidt, T.J.3
  • 505
    • 0035422774 scopus 로고    scopus 로고
    • Helenalin triggers a CD95 death receptor-independent apoptosis that is not affected by overexpression of Bcl-x(L) or Bcl-2
    • Dirsch VM, Stuppner H, Vollmar AM. Helenalin triggers a CD95 death receptor-independent apoptosis that is not affected by overexpression of Bcl-x(L) or Bcl-2. Cancer Res 2001; 61: 5817-5823.
    • (2001) Cancer Res. , vol.61 , pp. 5817-5823
    • Dirsch, V.M.1    Stuppner, H.2    Vollmar, A.M.3
  • 507
    • 0034753652 scopus 로고    scopus 로고
    • Predictors of response to pharmacotherapy with citalopram in obsessive-compulsive disorder
    • Stein DJ, Montgomery SA, Kasper S, Tanghoj P. Predictors of response to pharmacotherapy with citalopram in obsessive-compulsive disorder. Int Clin Psychopharmacol 2001; 16: 357-361.
    • (2001) Int. Clin. Psychopharmacol. , vol.16 , pp. 357-361
    • Stein, D.J.1    Montgomery, S.A.2    Kasper, S.3    Tanghoj, P.4
  • 508
    • 0036952249 scopus 로고    scopus 로고
    • The active fraction of plasmatic plasminogen activator inhibitor type 1 as a possible indicator of increased risk for metastatic melanoma
    • Hanekom GS, Stubbings HM, Kidson SH. The active fraction of plasmatic plasminogen activator inhibitor type 1 as a possible indicator of increased risk for metastatic melanoma. Cancer Detect Prevention 2002; 26: 50-59.
    • (2002) Cancer Detect Prevention , vol.26 , pp. 50-59
    • Hanekom, G.S.1    Stubbings, H.M.2    Kidson, S.H.3
  • 509
    • 0036586721 scopus 로고    scopus 로고
    • Identification of a novel role for sphingolipid signaling in TNF alpha and ischemic preconditioning mediated cardioprotection
    • Lecour S, Smith RM, Woodward B, Opie LH, Rochette L, Sack MN. Identification of a novel role for sphingolipid signaling in TNF alpha and ischemic preconditioning mediated cardioprotection. J Mol Cell Cardiol 2002; 34: 509-518.
    • (2002) J. Mol. Cell Cardiol. , vol.34 , pp. 509-518
    • Lecour, S.1    Smith, R.M.2    Woodward, B.3    Opie, L.H.4    Rochette, L.5    Sack, M.N.6
  • 510
    • 0036290661 scopus 로고    scopus 로고
    • Nuclear factor (NF)-kappa B blockade attenuates but does not abrogate LPS-mediated interleukin (IL)-1 beta biosynthesis in alveolar epithelial cells
    • Haddad JJ. Nuclear factor (NF)-kappa B blockade attenuates but does not abrogate LPS-mediated interleukin (IL)-1 beta biosynthesis in alveolar epithelial cells. Biochem Biophys Res Commun 2002; 293: 252-257.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 252-257
    • Haddad, J.J.1
  • 511
    • 0036677151 scopus 로고    scopus 로고
    • The sesquiterpene lactone parthenolide inhibits LPS- but not TNF-alpha-induced maturation of human monocyte-derived dendritic cells by inhibition of the p38 mitogen-activated protein kinase pathway
    • Uchi H, Arrighi JF, Aubry JP, Furue M, Hauser C. The sesquiterpene lactone parthenolide inhibits LPS- but not TNF-alpha-induced maturation of human monocyte-derived dendritic cells by inhibition of the p38 mitogen-activated protein kinase pathway. J Allergy Clin Immunol 2002; 110: 269-276.
    • (2002) J. Allergy Clin. Immunol. , vol.110 , pp. 269-276
    • Uchi, H.1    Arrighi, J.F.2    Aubry, J.P.3    Furue, M.4    Hauser, C.5
  • 512
    • 0037064130 scopus 로고    scopus 로고
    • Oxidative stressmediated apoptosis. The anticancer effect of the sesquiterpene lactone parthenolide
    • Wen J, You KR, Lee SY, Song CH, Kim DG. Oxidative stressmediated apoptosis. The anticancer effect of the sesquiterpene lactone parthenolide. J Biol Chem 2002; 277: 38954-38964.
    • (2002) J Biol. Chem. , vol.277 , pp. 38954-38964
    • Wen, J.1    You, K.R.2    Lee, S.Y.3    Song, C.H.4    Kim, D.G.5
  • 513
    • 18544396176 scopus 로고    scopus 로고
    • Association of interferon regulatory factor-1, nucleophosmin, nuclear factor-kappaB, and cyclic AMP response element binding with acquired resistance to Faslodex (ICI 182,780)
    • Gu Z, Lee RY, Skaar TC, Bouker KB, Welch JN, Lu J et al. Association of interferon regulatory factor-1, nucleophosmin, nuclear factor-kappaB, and cyclic AMP response element binding with acquired resistance to Faslodex (ICI 182,780). Cancer Res 2002; 62: 3428-3487.
    • (2002) Cancer Res. , vol.62 , pp. 3428-3487
    • Gu, Z.1    Lee, R.Y.2    Skaar, T.C.3    Bouker, K.B.4    Welch, J.N.5    Lu, J.6
  • 514
    • 0035572018 scopus 로고    scopus 로고
    • Augmentation of apoptosis responses in p53-deficient L1210 cells by compounds directed at blocking NFkappaB activation
    • Cory AH, Cory JG. Augmentation of apoptosis responses in p53-deficient L1210 cells by compounds directed at blocking NFkappaB activation. Anticancer Res 2001; 21: 3807-3811.
    • (2001) Anticancer Res. , vol.21 , pp. 3807-3811
    • Cory, A.H.1    Cory, J.G.2
  • 515
    • 0036198355 scopus 로고    scopus 로고
    • Enhancement of 1 alpha,25-dihydroxyvitamin D(3)-induced differentiation of human leukaemia HL-60 cells into monocytes by parthenolide via inhibition of NF-kappa B activity
    • Kang SN, Kim SH, Chung SW, Lee MH, Kim HJ, Kim TS. Enhancement of 1 alpha,25-dihydroxyvitamin D(3)-induced differentiation of human leukaemia HL-60 cells into monocytes by parthenolide via inhibition of NF-kappa B activity. Br J Pharmacol 2002; 135: 1235-1244.
    • (2002) Br. J. Pharmacol. , vol.135 , pp. 1235-1244
    • Kang, S.N.1    Kim, S.H.2    Chung, S.W.3    Lee, M.H.4    Kim, H.J.5    Kim, T.S.6
  • 516
    • 0035889120 scopus 로고    scopus 로고
    • Transformation of interleukin-3-dependent cells without participation of Stat5/bcl-xL: Cooperation of akt with raf/erk leads to p65 nuclear factor kappaB-mediated antiapoptosis involving c-IAP2
    • Gelfanov VM, Burgess GS, Litz-Jackson S, King AJ, Marshall MS, Nakshatri H et al. Transformation of interleukin-3-dependent cells without participation of Stat5/bcl-xL: cooperation of akt with raf/erk leads to p65 nuclear factor kappaB-mediated antiapoptosis involving c-IAP2. Blood 2001; 98: 2508-2517.
    • (2001) Blood , vol.98 , pp. 2508-2517
    • Gelfanov, V.M.1    Burgess, G.S.2    Litz-Jackson, S.3    King, A.J.4    Marshall, M.S.5    Nakshatri, H.6
  • 517
    • 0034828479 scopus 로고    scopus 로고
    • Activation of NF-kB mediates ICAM-1 induction in respiratory cells exposed to an adenovirus-derived vector
    • Melotti P, Nicolis E, Tamanini A, Rolfini R, Pavirani A, Cabrini G. Activation of NF-kB mediates ICAM-1 induction in respiratory cells exposed to an adenovirus-derived vector. Gene Ther 2001; 8: 1436-1442.
    • (2001) Gene Ther. , vol.8 , pp. 1436-1442
    • Melotti, P.1    Nicolis, E.2    Tamanini, A.3    Rolfini, R.4    Pavirani, A.5    Cabrini, G.6
  • 518
    • 0037015071 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin
    • Butler LM, Zhou X, Xu WS, Scher HI, Rifkind RA, Marks PA et al. The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin. Proc Natl Acad Sci USA 2002; 99: 11700-11705.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11700-11705
    • Butler, L.M.1    Zhou, X.2    Xu, W.S.3    Scher, H.I.4    Rifkind, R.A.5    Marks, P.A.6
  • 519
    • 0035577768 scopus 로고    scopus 로고
    • The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells
    • Munster PN, Troso-Sandoval T, Rosen N, Rifkind R, Marks PA, Richon VM. The histone deacetylase inhibitor suberoylanilide hydroxamic acid induces differentiation of human breast cancer cells. Cancer Res 2001; 61: 8492-8497.
    • (2001) Cancer Res. , vol.61 , pp. 8492-8497
    • Munster, P.N.1    Troso-Sandoval, T.2    Rosen, N.3    Rifkind, R.4    Marks, P.A.5    Richon, V.M.6
  • 521
    • 0034722897 scopus 로고    scopus 로고
    • New agents in cancer clinical trials
    • (Review)
    • Adams J, Elliott PJ. New agents in cancer clinical trials. Oncogene 2000; 19: 6687-6692 (Review).
    • (2000) Oncogene , vol.19 , pp. 6687-6692
    • Adams, J.1    Elliott, P.J.2
  • 522
    • 0034730127 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation
    • Richon VM, Sandhoff TW, Rifkind RA, Marks PA. Histone deacetylase inhibitor selectively induces p21WAF1 expression and gene-associated histone acetylation. Proc Natl Acad Sci USA 2000; 97: 10014-10019.
    • (2000) Proc Natl. Acad. Sci. USA , vol.97 , pp. 10014-10019
    • Richon, V.M.1    Sandhoff, T.W.2    Rifkind, R.A.3    Marks, P.A.4
  • 523
    • 0036304760 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors: A new class of potential therapeutic agents for cancer treatment
    • Richon VM, O'Brien JP. Histone deacetylase inhibitors: a new class of potential therapeutic agents for cancer treatment. Clin Cancer Res 2002; 8: 662-664.
    • (2002) Clin. Cancer Res. , vol.8 , pp. 662-664
    • Richon, V.M.1    O'Brien, J.P.2
  • 524
    • 0037085773 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor FR901228 enhances adenovirus infection of hematopoietic cells
    • Kitazono M, Rao VK, Robey R, Aikou T, Bates S, Fojo T et al. Histone deacetylase inhibitor FR901228 enhances adenovirus infection of hematopoietic cells. Blood 2002; 99: 2248-2251.
    • (2002) Blood , vol.99 , pp. 2248-2251
    • Kitazono, M.1    Rao, V.K.2    Robey, R.3    Aikou, T.4    Bates, S.5    Fojo, T.6
  • 525
  • 526
    • 0033822112 scopus 로고    scopus 로고
    • P21-dependent g(1)arrest with downregulation of cyclin D1 and upregulation of cyclin E by the histone deacetylase inhibitor FR901228
    • Sandor V, Senderowicz A, Mertins S, Sackett D, Sausville E, Blagosklonny MV et al. P21-dependent g(1)arrest with downregulation of cyclin D1 and upregulation of cyclin E by the histone deacetylase inhibitor FR901228. Br J Cancer 2000; 83: 817-825.
    • (2000) Br. J. Cancer , vol.83 , pp. 817-825
    • Sandor, V.1    Senderowicz, A.2    Mertins, S.3    Sackett, D.4    Sausville, E.5    Blagosklonny, M.V.6
  • 527
    • 0033566643 scopus 로고    scopus 로고
    • Depsipeptide (FR901228): A novel therapeutic agent with selective, in vitro activity against human B-cell chronic lymphocytic leukemia cells
    • Byrd JC, Shinn C, Ravi R, Willis CR, Waselenko JK, Flinn IW et al. Depsipeptide (FR901228): a novel therapeutic agent with selective, in vitro activity against human B-cell chronic lymphocytic leukemia cells. Blood 1999; 94: 1401-1408.
    • (1999) Blood , vol.94 , pp. 1401-1408
    • Byrd, J.C.1    Shinn, C.2    Ravi, R.3    Willis, C.R.4    Waselenko, J.K.5    Flinn, I.W.6
  • 528
    • 0036479127 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel histone deacetylase HDAC10
    • Guardiola AR, Yao TP. Molecular cloning and characterization of a novel histone deacetylase HDAC10. J Biol Chem 2002; 277: 3350-3356.
    • (2002) J. Biol. Chem. , vol.277 , pp. 3350-3356
    • Guardiola, A.R.1    Yao, T.P.2
  • 529
    • 0033523895 scopus 로고    scopus 로고
    • Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation
    • Jung M, Brosch G, Kolle D, Scherf H, Gerhauser C, Loidl P. Amide analogues of trichostatin A as inhibitors of histone deacetylase and inducers of terminal cell differentiation. J Med Chem 1999; 42: 4669-4679.
    • (1999) J. Med. Chem. , vol.42 , pp. 4669-4679
    • Jung, M.1    Brosch, G.2    Kolle, D.3    Scherf, H.4    Gerhauser, C.5    Loidl, P.6
  • 530
    • 0025673805 scopus 로고
    • Isolation and structural elucidation of new cyclotetrapeptides trapoxins, A and B, having detransformation activities as antitumor agents
    • Itazaki H, Nagashima K, Sugita K, Yoshida H, Kawamura Y, Yasuda Y et al. Isolation and structural elucidation of new cyclotetrapeptides trapoxins, A and B, having detransformation activities as antitumor agents. J Antibiot 1990; 143: 1524-1532.
    • (1990) J. Antibiot. , vol.143 , pp. 1524-1532
    • Itazaki, H.1    Nagashima, K.2    Sugita, K.3    Yoshida, H.4    Kawamura, Y.5    Yasuda, Y.6
  • 531
    • 0037096739 scopus 로고    scopus 로고
    • Ecteinascidin-743 inhibits activated but not constitutive transcription
    • Friedman D, Hu Z, Kolb EA, Gorfajn B, Scotto KW. Ecteinascidin-743 inhibits activated but not constitutive transcription. Cancer Res 2002; 62: 3377-3381.
    • (2002) Cancer Res. , vol.62 , pp. 3377-3381
    • Friedman, D.1    Hu, Z.2    Kolb, E.A.3    Gorfajn, B.4    Scotto, K.W.5
  • 533
    • 0034612352 scopus 로고    scopus 로고
    • Ecteinascidin 743, a transcription-targeted chemotherapeutic that inhibits MDR1 activation
    • Jin S, Gorfajn B, Faircloth G, Scotto KW. Ecteinascidin 743, a transcription-targeted chemotherapeutic that inhibits MDR1 activation. Proc Natl Acad Sci USA 2000; 97: 6775-6779.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6775-6779
    • Jin, S.1    Gorfajn, B.2    Faircloth, G.3    Scotto, K.W.4
  • 534
    • 0344199996 scopus 로고    scopus 로고
    • Sensitization of tumor cells to ribotoxic stress-induced apoptotic cell death: A new therapeutic strategy
    • Ruller S, Stahl C, Kohler G, Eickhoff B, Breder J, Schlaak M et al. Sensitization of tumor cells to ribotoxic stress-induced apoptotic cell death: a new therapeutic strategy. Clin Cancer Res 1999; 5: 2714-2725.
    • (1999) Clin. Cancer Res. , vol.5 , pp. 2714-2725
    • Ruller, S.1    Stahl, C.2    Kohler, G.3    Eickhoff, B.4    Breder, J.5    Schlaak, M.6
  • 535
    • 0033564458 scopus 로고    scopus 로고
    • Carboxypeptidase A3 (CPA3): A novel gene highly induced by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells
    • Huang H, Reed CP, Zhang JS, Shridhar V, Wang L, Smith DI. Carboxypeptidase A3 (CPA3): a novel gene highly induced by histone deacetylase inhibitors during differentiation of prostate epithelial cancer cells. Cancer Res 1999; 59: 2981-2988.
    • (1999) Cancer Res. , vol.59 , pp. 2981-2988
    • Huang, H.1    Reed, C.P.2    Zhang, J.S.3    Shridhar, V.4    Wang, L.5    Smith, D.I.6
  • 536
    • 0036681989 scopus 로고    scopus 로고
    • Sulfonamide anilides, a novel class of histone deacetylase inhibitors, are antiproliferative against human tumors
    • Fournel M, Trachy-Bourget MC, Yan PT, Kalita A, Bonfils C, Beaulieu C et al. Sulfonamide anilides, a novel class of histone deacetylase inhibitors, are antiproliferative against human tumors. Cancer Res 2002; 62: 4325-4330.
    • (2002) Cancer Res. , vol.62 , pp. 4325-4330
    • Fournel, M.1    Trachy-Bourget, M.C.2    Yan, P.T.3    Kalita, A.4    Bonfils, C.5    Beaulieu, C.6
  • 537
    • 0037085474 scopus 로고    scopus 로고
    • Transcriptional regulation of the transforming growth factor beta type II receptor gene by histone acetyltransferase and deacetylase is mediated by NF-Y in human breast cancer cells
    • Park SH, Lee SR, Kim BC, Cho EA, Patel SP, Kang HB et al. Transcriptional regulation of the transforming growth factor beta type II receptor gene by histone acetyltransferase and deacetylase is mediated by NF-Y in human breast cancer cells. J Biol Chem 2002; 277: 5168-5174.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5168-5174
    • Park, S.H.1    Lee, S.R.2    Kim, B.C.3    Cho, E.A.4    Patel, S.P.5    Kang, H.B.6
  • 539
    • 0034837064 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylase as new anticancer agents
    • Jung M. Inhibitors of histone deacetylase as new anticancer agents. Curr Med Chem 2001; 8: 1505-1511.
    • (2001) Curr. Med. Chem. , vol.8 , pp. 1505-1511
    • Jung, M.1
  • 540
    • 0035113602 scopus 로고    scopus 로고
    • MS-275, a histone deacetylase inhibitor, selectively induces transforming growth factor beta type II receptor expression in human breast cancer cells
    • Lee BI, Park SH, Kim JW, Sausville EA, Kim HT, Nakanishi O et al. MS-275, a histone deacetylase inhibitor, selectively induces transforming growth factor beta type II receptor expression in human breast cancer cells. Cancer Res 2001; 61: 931-934.
    • (2001) Cancer Res. , vol.61 , pp. 931-934
    • Lee, B.I.1    Park, S.H.2    Kim, J.W.3    Sausville, E.A.4    Kim, H.T.5    Nakanishi, O.6
  • 541
    • 0033614993 scopus 로고    scopus 로고
    • Synthesis and histone deacetylase inhibitory activity of new benzamide derivatives
    • Suzuki T, Ando T, Tsuchiya K, Fukazawa N, Saito A, Mariko Y et al. Synthesis and histone deacetylase inhibitory activity of new benzamide derivatives. J Med Chem 1999; 42: 3001-3003.
    • (1999) J. Med. Chem. , vol.42 , pp. 3001-3003
    • Suzuki, T.1    Ando, T.2    Tsuchiya, K.3    Fukazawa, N.4    Saito, A.5    Mariko, Y.6
  • 542
    • 0033551152 scopus 로고    scopus 로고
    • A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors
    • Saito A, Yamashita T, Mariko Y, Nosaka Y, Tsuchiya K, Ando T et al. A synthetic inhibitor of histone deacetylase, MS-27-275, with marked in vivo antitumor activity against human tumors. Proc Natl Acad Sci USA 1999; 96: 4592-4597.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4592-4597
    • Saito, A.1    Yamashita, T.2    Mariko, Y.3    Nosaka, Y.4    Tsuchiya, K.5    Ando, T.6
  • 543
    • 0034697819 scopus 로고    scopus 로고
    • The novel anti-tumour agent oxamflatin differentially regulates urokinase and plasminogen activator inhibitor type 2 expression and inhibits urokinase-mediated proteolytic activity
    • 1492
    • Dear AE, Medcalf RL. The novel anti-tumour agent oxamflatin differentially regulates urokinase and plasminogen activator inhibitor type 2 expression and inhibits urokinase-mediated proteolytic activity. Biochim Biophys Acta 2000; 1492: 15-22.
    • (2000) Biochim. Biophys. Acta , pp. 15-22
    • Dear, A.E.1    Medcalf, R.L.2
  • 544
    • 0033452640 scopus 로고    scopus 로고
    • Trichostatins and leptomycins, new cell cycle inhibitors specific for G1 and G2 phases
    • (Review)
    • Yoshida M, Beppu T. [Trichostatins and leptomycins, new cell cycle inhibitors specific for G1 and G2 phases]. Ann NY Acad Sci 1999; 886: 23-36 (Review).
    • (1999) Ann. N.Y. Acad. Sci. , vol.886 , pp. 23-36
    • Yoshida, M.1    Beppu, T.2
  • 545
    • 0033561497 scopus 로고    scopus 로고
    • Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase
    • Kim YB, Lee KH, Sugita K, Yoshida M, Horinouchi S. Oxamflatin is a novel antitumor compound that inhibits mammalian histone deacetylase. Oncogene 1999; 18: 2461-2470.
    • (1999) Oncogene , vol.18 , pp. 2461-2470
    • Kim, Y.B.1    Lee, K.H.2    Sugita, K.3    Yoshida, M.4    Horinouchi, S.5
  • 546
    • 0029946960 scopus 로고    scopus 로고
    • Oxamflatin: A novel compound which reverses malignant phenotype to normal one via induction of JunD
    • Sonoda H, Nishida K, Yoshioka T, Ohtani M, Sugita K. Oxamflatin: a novel compound which reverses malignant phenotype to normal one via induction of JunD. Oncogene 1996; 13: 143-149.
    • (1996) Oncogene , vol.13 , pp. 143-149
    • Sonoda, H.1    Nishida, K.2    Yoshioka, T.3    Ohtani, M.4    Sugita, K.5
  • 547
    • 0033835421 scopus 로고    scopus 로고
    • The importance of being K-Ras
    • Ellis CA, Glark G. The importance of being K-Ras. Cell Signal. 2000; 12: 425-434.
    • (2000) Cell Signal , vol.12 , pp. 425-434
    • Ellis, C.A.1    Glark, G.2
  • 548
    • 18444381728 scopus 로고    scopus 로고
    • Knockout of ERK1 MAP kinase enhances synaptic plasticity in the striatum and facilitates striatal-mediated learning and memory
    • Mazzucchelli C, Vantaggiato C, Ciamei A, Fasano S, Pakhotin P, Krezel W et al. Knockout of ERK1 MAP kinase enhances synaptic plasticity in the striatum and facilitates striatal-mediated learning and memory. Neuron. 2002; 34: 807-820.
    • (2002) Neuron. , vol.34 , pp. 807-820
    • Mazzucchelli, C.1    Vantaggiato, C.2    Ciamei, A.3    Fasano, S.4    Pakhotin, P.5    Krezel, W.6
  • 549
    • 17144458301 scopus 로고    scopus 로고
    • Defective thymocyte maturation in p44 MAP kinase (Erk 1) knockout mice
    • Pages G, Guerin S, Grall D, Bonino F, Smith A, Anjuere F et al. Defective thymocyte maturation in p44 MAP kinase (Erk 1) knockout mice. Science 1999; 286: 1374-1377.
    • (1999) Science , vol.286 , pp. 1374-1377
    • Pages, G.1    Guerin, S.2    Grall, D.3    Bonino, F.4    Smith, A.5    Anjuere, F.6
  • 550
  • 551
    • 0031550257 scopus 로고    scopus 로고
    • Evidence supporting a signal transduction pathway leading to the radiation-resistant phenotype in human tumor cells
    • Pirollo KF, Hao Z, Rait A, Ho CW, Chang EH. Evidence supporting a signal transduction pathway leading to the radiation-resistant phenotype in human tumor cells. Biochem Biophys Res Commun 1997; 230: 196-201.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 196-201
    • Pirollo, K.F.1    Hao, Z.2    Rait, A.3    Ho, C.W.4    Chang, E.H.5
  • 552
    • 0030468743 scopus 로고    scopus 로고
    • Effect of PD 098059, a specific inhibitor of mitogen-activated protein kinase kinase, on urokinase expression and in vitro invasion
    • Simon C, Juarez J, Nicolson GL, Boyd D. Effect of PD 098059, a specific inhibitor of mitogen-activated protein kinase kinase, on urokinase expression and in vitro invasion. Cancer Res 1996; 56: 5369-5374.
    • (1996) Cancer Res. , vol.56 , pp. 5369-5374
    • Simon, C.1    Juarez, J.2    Nicolson, G.L.3    Boyd, D.4
  • 553
    • 0029904681 scopus 로고    scopus 로고
    • Expression of mitogen-activated protein kinase phosphatase-1 in the early phases of human epithelial carcinogenesis
    • Loda M, Capodieci P, Mishra R, Yao H, Corless C, Grigioni W et al. Expression of mitogen-activated protein kinase phosphatase-1 in the early phases of human epithelial carcinogenesis. Am J Pathol 1996; 149: 1553-1564.
    • (1996) Am. J. Pathol. , vol.149 , pp. 1553-1564
    • Loda, M.1    Capodieci, P.2    Mishra, R.3    Yao, H.4    Corless, C.5    Grigioni, W.6
  • 554
    • 0031036906 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase phosphatase 1 is overexpressed in prostate cancers and is inversely related to apoptosis
    • Magi-Galluzzi C, Mishra R, Fiorentino M, Montironi R, Yao H, Capodieci P et al. Mitogen-activated protein kinase phosphatase 1 is overexpressed in prostate cancers and is inversely related to apoptosis. Lab Invest 1997; 76: 37-51.
    • (1997) Lab. Invest. , vol.76 , pp. 37-51
    • Magi-Galluzzi, C.1    Mishra, R.2    Fiorentino, M.3    Montironi, R.4    Yao, H.5    Capodieci, P.6
  • 555
    • 0030802780 scopus 로고    scopus 로고
    • Essential role of calcium in the regulation of MAP kinase phosphatase-1 expression
    • Scimeca JC, Servant MJ, Dyer JO, Meloche S. Essential role of calcium in the regulation of MAP kinase phosphatase-1 expression. Oncogene 1997; 15: 717-725.
    • (1997) Oncogene , vol.15 , pp. 717-725
    • Scimeca, J.C.1    Servant, M.J.2    Dyer, J.O.3    Meloche, S.4
  • 556
    • 0030722189 scopus 로고    scopus 로고
    • Regulation of distinct stages of skeletal muscle differentiation by mitogen-activated protein kinases
    • Bennett AM, Tonks NK. Regulation of distinct stages of skeletal muscle differentiation by mitogen-activated protein kinases. Science 1997; 278: 1288-1291.
    • (1997) Science , vol.278 , pp. 1288-1291
    • Bennett, A.M.1    Tonks, N.K.2
  • 557
    • 0023715225 scopus 로고
    • Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP
    • Feig LA, Cooper GM. Inhibition of NIH 3T3 cell proliferation by a mutant ras protein with preferential affinity for GDP. Mol Cell Biol 1988; 8: 3235-3243.
    • (1988) Mol. Cell Biol. , vol.8 , pp. 3235-3243
    • Feig, L.A.1    Cooper, G.M.2
  • 558
    • 0037192849 scopus 로고    scopus 로고
    • A distinct class of dominant negative Ras mutants: Cytosolic GTP-bound Ras effector domain mutants that inhibit Ras signaling and transformation and enhance cell adhesion
    • Fiordalisi JJ, Holly SP, Johnson II RL, Parise LV, Cox AD. A distinct class of dominant negative Ras mutants: cytosolic GTP-bound Ras effector domain mutants that inhibit Ras signaling and transformation and enhance cell adhesion. J Biol Chem 2000; 277: 10813-10823.
    • (2000) J. Biol. Chem. , vol.277 , pp. 10813-10823
    • Fiordalisi, J.J.1    Holly, S.P.2    Johnson R.L. II3    Parise, L.V.4    Cox, A.D.5
  • 559
    • 0034967677 scopus 로고    scopus 로고
    • Oligonucleotide treatment of ras-induced tumors in nude mice
    • Wickstrom E. Oligonucleotide treatment of ras-induced tumors in nude mice. Mol Biotechnol 2001; 18:35-55.
    • (2001) Mol. Biotechnol. , vol.18 , pp. 35-55
    • Wickstrom, E.1
  • 560
    • 0035977185 scopus 로고    scopus 로고
    • Association of c-Raf expression with survival and its targeting with antisense oligonucleotides in ovarian cancer
    • McPhillips F, Mullen P, Monia BP, Ritchie AA, Dorr FA, Smyth JF et al. Association of c-Raf expression with survival and its targeting with antisense oligonucleotides in ovarian cancer. Br J Cancer 2001; 85: 1753-1758.
    • (2001) Br. J. Cancer , vol.85 , pp. 1753-1758
    • McPhillips, F.1    Mullen, P.2    Monia, B.P.3    Ritchie, A.A.4    Dorr, F.A.5    Smyth, J.F.6
  • 561
    • 0033793081 scopus 로고    scopus 로고
    • RNA interference: Genetic wand and genetic watchdog
    • Bosher JM, Labouesse M. RNA interference: genetic wand and genetic watchdog. Nat Cell Biol 2000; 2: E31-E36.
    • (2000) Nat. Cell Biol. , vol.2
    • Bosher, J.M.1    Labouesse, M.2
  • 563
    • 0037329372 scopus 로고    scopus 로고
    • RNA interference is a functional pathway with therapeutic potential in human myeloid leukemia cell lines
    • Cioca DP, Aoki Y, Kiyosawa K. RNA interference is a functional pathway with therapeutic potential in human myeloid leukemia cell lines. Cancer Gene Ther 2003; 10: 125-133.
    • (2003) Cancer Gene Ther. , vol.10 , pp. 125-133
    • Cioca, D.P.1    Aoki, Y.2    Kiyosawa, K.3
  • 567
    • 0034253196 scopus 로고    scopus 로고
    • Small G-protein networks: Their crosstalk and signal cascades
    • Matozaki T, Nakanishi H, Takai Y. Small G-protein networks: their crosstalk and signal cascades. Cell Signal 2000; 12: 515-524.
    • (2000) Cell Signal , vol.12 , pp. 515-524
    • Matozaki, T.1    Nakanishi, H.2    Takai, Y.3


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