메뉴 건너뛰기




Volumn 8, Issue 1, 2008, Pages 80-89

Contribution of extracellular signal-regulated kinases to the IL-1-induced growth inhibition of human melanoma cells A375

Author keywords

CDK; Cytokines; E2F; ERK1 2; IL 1; Melanoma; p21; RB

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; CYCLIN D; CYCLIN DEPENDENT KINASE 2; CYCLIN DEPENDENT KINASE 4; INTERLEUKIN 1; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN P21; PROTEIN P27; RETINOBLASTOMA PROTEIN; TRANSCRIPTION FACTOR E2F;

EID: 36649010976     PISSN: 15675769     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.intimp.2007.10.013     Document Type: Article
Times cited : (5)

References (46)
  • 1
    • 0028926263 scopus 로고
    • Parallel signal processing among mammalian MAPKs
    • Cano E., and Mahadevan L.C. Parallel signal processing among mammalian MAPKs. Trends Biochem Sci 20 (1995) 117-122
    • (1995) Trends Biochem Sci , vol.20 , pp. 117-122
    • Cano, E.1    Mahadevan, L.C.2
  • 2
    • 0028935974 scopus 로고
    • Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms
    • Derijard B., Raingeaud J., Barrett T., Wu I.H., Han J., Ulevitch R.J., et al. Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms. Science 267 (1995) 682-685
    • (1995) Science , vol.267 , pp. 682-685
    • Derijard, B.1    Raingeaud, J.2    Barrett, T.3    Wu, I.H.4    Han, J.5    Ulevitch, R.J.6
  • 3
    • 0030044182 scopus 로고    scopus 로고
    • Characterization of the structure and function of a novel MAP kinase kinase (MKK6)
    • Han J., Lee J.D., Jiang Y., Li Z., Feng L., and Ulevitch R.J. Characterization of the structure and function of a novel MAP kinase kinase (MKK6). J Biol Chem 271 (1996) 2886-2891
    • (1996) J Biol Chem , vol.271 , pp. 2886-2891
    • Han, J.1    Lee, J.D.2    Jiang, Y.3    Li, Z.4    Feng, L.5    Ulevitch, R.J.6
  • 4
    • 0032524919 scopus 로고    scopus 로고
    • T lymphocyte activation signals for interleukin-2 production involve activation of MKK6-p38 and MKK7-SAPK/JNK signaling pathways sensitive to cyclosporin A
    • Matsuda S., Moriguchi T., Koyasu S., and Nishida E. T lymphocyte activation signals for interleukin-2 production involve activation of MKK6-p38 and MKK7-SAPK/JNK signaling pathways sensitive to cyclosporin A. J Biol Chem 273 (1998) 12378-12382
    • (1998) J Biol Chem , vol.273 , pp. 12378-12382
    • Matsuda, S.1    Moriguchi, T.2    Koyasu, S.3    Nishida, E.4
  • 5
    • 0029055761 scopus 로고
    • Components of a new human protein kinase signal transduction pathway
    • Zhou G., Bao Z.Q., and Dixon J.E. Components of a new human protein kinase signal transduction pathway. J Biol Chem 270 (1995) 12665-12669
    • (1995) J Biol Chem , vol.270 , pp. 12665-12669
    • Zhou, G.1    Bao, Z.Q.2    Dixon, J.E.3
  • 7
    • 0027410497 scopus 로고
    • The MAP kinase cascade is essential for diverse signal transduction pathways
    • Nishida E., and Gotoh Y. The MAP kinase cascade is essential for diverse signal transduction pathways. Trends Biochem Sci 18 (1993) 128-131
    • (1993) Trends Biochem Sci , vol.18 , pp. 128-131
    • Nishida, E.1    Gotoh, Y.2
  • 8
    • 0029043582 scopus 로고
    • How MAP kinases are regulated
    • Cobb M.J., and Goldsmith E.J. How MAP kinases are regulated. J Biol Chem 270 (1995) 14843-14846
    • (1995) J Biol Chem , vol.270 , pp. 14843-14846
    • Cobb, M.J.1    Goldsmith, E.J.2
  • 9
    • 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 8 (1996) 205-215
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 205-215
    • Treisman, R.1
  • 10
    • 0028935270 scopus 로고
    • Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine
    • Raingeaud J., Gupta S., Rogers J.S., Dickens M., Han J., Ulevitch R.J., et al. Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J Biol Chem 270 (1995) 7420-7426
    • (1995) J Biol Chem , vol.270 , pp. 7420-7426
    • Raingeaud, J.1    Gupta, S.2    Rogers, J.S.3    Dickens, M.4    Han, J.5    Ulevitch, R.J.6
  • 11
    • 0027994002 scopus 로고
    • An osmosensing signal transduction pathway in mammalian cells
    • Galcheva-Gargova Z., Derijard B., Wu I.H., and Davis R.J. An osmosensing signal transduction pathway in mammalian cells. Science 265 (1994) 806-808
    • (1994) Science , vol.265 , pp. 806-808
    • Galcheva-Gargova, Z.1    Derijard, B.2    Wu, I.H.3    Davis, R.J.4
  • 13
    • 0029938805 scopus 로고    scopus 로고
    • Stress-induced phosphorylation and activation of the transcription factor CHOP(GADD153) by p38MAP Kinase
    • Wang X.Z., and Ron D. Stress-induced phosphorylation and activation of the transcription factor CHOP(GADD153) by p38MAP Kinase. Science 272 (1996) 1347-1349
    • (1996) Science , vol.272 , pp. 1347-1349
    • Wang, X.Z.1    Ron, D.2
  • 14
    • 0029979369 scopus 로고    scopus 로고
    • Biological basis for interleukin-1 in disease
    • Dinarello C.A. Biological basis for interleukin-1 in disease. Blood 87 (1996) 2095-2147
    • (1996) Blood , vol.87 , pp. 2095-2147
    • Dinarello, C.A.1
  • 15
    • 0015362658 scopus 로고
    • Potentiation of the T-lymphocytes response to mitogens. I. The responding cell
    • Gery I., Gershon R.K., and Waksman B.H. Potentiation of the T-lymphocytes response to mitogens. I. The responding cell. J Exp Med 136 (1972) 128-142
    • (1972) J Exp Med , vol.136 , pp. 128-142
    • Gery, I.1    Gershon, R.K.2    Waksman, B.H.3
  • 16
    • 0023743789 scopus 로고
    • Pre-exposure of human B cells to recombinant IL-1 enhances subsequent proliferation
    • Freedman A.S., Freeman G., Whitman J., Segil J., Daley J., and Nadler J.M. Pre-exposure of human B cells to recombinant IL-1 enhances subsequent proliferation. J Immunol 141 (1988) 3398-3404
    • (1988) J Immunol , vol.141 , pp. 3398-3404
    • Freedman, A.S.1    Freeman, G.2    Whitman, J.3    Segil, J.4    Daley, J.5    Nadler, J.M.6
  • 17
    • 0019949390 scopus 로고
    • Interleukin 1, a potential regulator of fibroblast proliferation
    • Schmidt J.A., Mizel S.B., Cohen D., and Green I. Interleukin 1, a potential regulator of fibroblast proliferation. J Immunol 128 (1982) 2177-2182
    • (1982) J Immunol , vol.128 , pp. 2177-2182
    • Schmidt, J.A.1    Mizel, S.B.2    Cohen, D.3    Green, I.4
  • 18
    • 0029922662 scopus 로고    scopus 로고
    • Strain-dependent differences in sensitivity of rat beta-cells to interleukin 1 beta in vitro and in vivo: association with islet nitric oxide synthesis
    • Reimers J.I., Andersen H.U., Mauricio D., Pociot F., Karlsen A.E., Petersen J.S., et al. Strain-dependent differences in sensitivity of rat beta-cells to interleukin 1 beta in vitro and in vivo: association with islet nitric oxide synthesis. Diabetes 45 (1996) 771-778
    • (1996) Diabetes , vol.45 , pp. 771-778
    • Reimers, J.I.1    Andersen, H.U.2    Mauricio, D.3    Pociot, F.4    Karlsen, A.E.5    Petersen, J.S.6
  • 19
    • 0025186452 scopus 로고
    • Extension of the life-span of human endothelial cells by an interleukin-1 alpha antisense oligomer
    • Maier J.A., Voulalas P., Roeder D., and Maciag T. Extension of the life-span of human endothelial cells by an interleukin-1 alpha antisense oligomer. Science 249 (1990) 1570-1574
    • (1990) Science , vol.249 , pp. 1570-1574
    • Maier, J.A.1    Voulalas, P.2    Roeder, D.3    Maciag, T.4
  • 20
    • 0023230983 scopus 로고
    • Growth inhibition and augmentation of mouse myeloid leukemic cell line differentiation by interleukin 1
    • Onozaki K., Tamatani T., Hashimoto T., and Matsushima K. Growth inhibition and augmentation of mouse myeloid leukemic cell line differentiation by interleukin 1. Cancer Res 47 (1987) 2397-2402
    • (1987) Cancer Res , vol.47 , pp. 2397-2402
    • Onozaki, K.1    Tamatani, T.2    Hashimoto, T.3    Matsushima, K.4
  • 21
    • 0022237901 scopus 로고
    • Human interleukin 1 is a cytocidal factor for several tumor cell lines
    • Onozaki K., Matsushima K., Aggarwal B.B., and Oppenheim J.J. Human interleukin 1 is a cytocidal factor for several tumor cell lines. J Immunol 135 (1985) 3962-3968
    • (1985) J Immunol , vol.135 , pp. 3962-3968
    • Onozaki, K.1    Matsushima, K.2    Aggarwal, B.B.3    Oppenheim, J.J.4
  • 22
    • 0024316782 scopus 로고
    • Contribution of IL-6 to the antiproliferative effect of IL-1 and tumor necrosis factor on tumor cell lines
    • Morinaga Y., Suzuki H., Takatsuki F., Akiyama Y., Taniyama T., Matsushima K., et al. Contribution of IL-6 to the antiproliferative effect of IL-1 and tumor necrosis factor on tumor cell lines. J Immunol 143 (1989) 3538-3542
    • (1989) J Immunol , vol.143 , pp. 3538-3542
    • Morinaga, Y.1    Suzuki, H.2    Takatsuki, F.3    Akiyama, Y.4    Taniyama, T.5    Matsushima, K.6
  • 23
    • 0023778615 scopus 로고
    • Role of ornithine decarboxylase in the regulation of cell growth by IL-1 and tumor necrosis factor
    • Endo Y., Matsushima K., Onozaki K., and Oppenheim J.J. Role of ornithine decarboxylase in the regulation of cell growth by IL-1 and tumor necrosis factor. J Immunol 141 (1988) 2342-2348
    • (1988) J Immunol , vol.141 , pp. 2342-2348
    • Endo, Y.1    Matsushima, K.2    Onozaki, K.3    Oppenheim, J.J.4
  • 24
    • 0031023044 scopus 로고    scopus 로고
    • Interleukin-1-induced growth inhibition of human melanoma cells. Interleukin-1-induced antizyme expression is responsible for ornithine decarboxylase activity down-regulation
    • Yang D., Hayashi H., Takii T., Mizutani Y., Inukai Y., and Onozaki K. Interleukin-1-induced growth inhibition of human melanoma cells. Interleukin-1-induced antizyme expression is responsible for ornithine decarboxylase activity down-regulation. J Biol Chem 272 (1997) 3376-3383
    • (1997) J Biol Chem , vol.272 , pp. 3376-3383
    • Yang, D.1    Hayashi, H.2    Takii, T.3    Mizutani, Y.4    Inukai, Y.5    Onozaki, K.6
  • 25
    • 0025599872 scopus 로고
    • Antiproliferative effect of interleukin 1 (IL-1) on tumor cells: G0-G1 arrest of a human melanoma cell line by IL-1
    • Morinaga Y., Hayashi H., Takeuchi A., and Onozaki K. Antiproliferative effect of interleukin 1 (IL-1) on tumor cells: G0-G1 arrest of a human melanoma cell line by IL-1. Biochem Biophys Res Commun 173 (1990) 186-192
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 186-192
    • Morinaga, Y.1    Hayashi, H.2    Takeuchi, A.3    Onozaki, K.4
  • 26
    • 0033564934 scopus 로고    scopus 로고
    • Antiproliferative effect of IL-1 is mediated by p38 mitogen-activated protein kinase in human melanoma cell A375
    • Itoh S., Hattori T., Hayashi H., Mizutani Y., Todo M., Takii T., et al. Antiproliferative effect of IL-1 is mediated by p38 mitogen-activated protein kinase in human melanoma cell A375. J Immunol 162 (1999) 7434-7440
    • (1999) J Immunol , vol.162 , pp. 7434-7440
    • Itoh, S.1    Hattori, T.2    Hayashi, H.3    Mizutani, Y.4    Todo, M.5    Takii, T.6
  • 27
    • 0032544550 scopus 로고    scopus 로고
    • Requirement of p38 mitogen-activated protein kinase for neuronal differentiation in PC12 cells
    • Morooka T., and Nishida E. Requirement of p38 mitogen-activated protein kinase for neuronal differentiation in PC12 cells. J Biol Chem 273 (1998) 24285-24288
    • (1998) J Biol Chem , vol.273 , pp. 24285-24288
    • Morooka, T.1    Nishida, E.2
  • 28
    • 0034663903 scopus 로고    scopus 로고
    • The differetial role of extracellular-regulated kinases and p38 mitogen-activated protein kinase in eosinophil function
    • Adachi T., Choudhury B.K., Stafford S., Sur S., and Alam R. The differetial role of extracellular-regulated kinases and p38 mitogen-activated protein kinase in eosinophil function. J Immunol 165 (2000) 2198-2204
    • (2000) J Immunol , vol.165 , pp. 2198-2204
    • Adachi, T.1    Choudhury, B.K.2    Stafford, S.3    Sur, S.4    Alam, R.5
  • 29
    • 0034685876 scopus 로고    scopus 로고
    • Microtuble-interfering agents atimulate the transcription of cyclooxygenase-2. Evidence for involvement of ERK1/2 and p38 mitogen-activated protein kinase pathways
    • Subbaramaiah K., Hart J.C., Norton L., and Dannenberg A.J. Microtuble-interfering agents atimulate the transcription of cyclooxygenase-2. Evidence for involvement of ERK1/2 and p38 mitogen-activated protein kinase pathways. J Biol Chem 275 (2000) 14838-14845
    • (2000) J Biol Chem , vol.275 , pp. 14838-14845
    • Subbaramaiah, K.1    Hart, J.C.2    Norton, L.3    Dannenberg, A.J.4
  • 30
    • 0034646717 scopus 로고    scopus 로고
    • Induction of the antiogenic modulator fibroblast growth factor-binding protein by epidermal growth factor is mediated through both MEK/ERK and p38 transduction pathways
    • Harris V.K., Coticchia C.M., Kagan B.L., Ahmad S., Wellstein A., and Riegel A.T. Induction of the antiogenic modulator fibroblast growth factor-binding protein by epidermal growth factor is mediated through both MEK/ERK and p38 transduction pathways. J Biol Chem 275 (2000) 10802-10811
    • (2000) J Biol Chem , vol.275 , pp. 10802-10811
    • Harris, V.K.1    Coticchia, C.M.2    Kagan, B.L.3    Ahmad, S.4    Wellstein, A.5    Riegel, A.T.6
  • 31
    • 17644437502 scopus 로고    scopus 로고
    • Regulation of stress-induced cytokine production by pyridinylimidazoles inhibition of CSBP kinase
    • Gallagher T.F., Seibel G.L., Kassis S., Laydon J.T., Blumenthal M.J., Lee J.C., et al. Regulation of stress-induced cytokine production by pyridinylimidazoles inhibition of CSBP kinase. Bioorg Med Chem 5 (1997) 49-64
    • (1997) Bioorg Med Chem , vol.5 , pp. 49-64
    • Gallagher, T.F.1    Seibel, G.L.2    Kassis, S.3    Laydon, J.T.4    Blumenthal, M.J.5    Lee, J.C.6
  • 32
    • 29244464324 scopus 로고    scopus 로고
    • Mdm2-mediated pRB downregulation is involved in carcinogenesis in a p53-independent manner
    • Miwa S., Uchida C., Kitagawa K., Hattori T., Oda T., Sugimura H., et al. Mdm2-mediated pRB downregulation is involved in carcinogenesis in a p53-independent manner. Biochem Biophys Res Commun 340 (2006) 54-61
    • (2006) Biochem Biophys Res Commun , vol.340 , pp. 54-61
    • Miwa, S.1    Uchida, C.2    Kitagawa, K.3    Hattori, T.4    Oda, T.5    Sugimura, H.6
  • 33
    • 0033543549 scopus 로고    scopus 로고
    • Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases
    • Kawamura S., Moriguchi T., and Nishida E. Activation of the protein kinase ERK5/BMK1 by receptor tyrosine kinases. J Biol Chem 274 (1999) 26563-26571
    • (1999) J Biol Chem , vol.274 , pp. 26563-26571
    • Kawamura, S.1    Moriguchi, T.2    Nishida, E.3
  • 34
    • 0032562682 scopus 로고    scopus 로고
    • The activation of p38 and apoptosis by the inhibition of Erk is antagonized by the phosphoinositide 3-kinase/Akt pathway
    • Berra E., Diaz-Meco M.T., and Moscat J. The activation of p38 and apoptosis by the inhibition of Erk is antagonized by the phosphoinositide 3-kinase/Akt pathway. J Biol Chem 273 (1998) 10792-10797
    • (1998) J Biol Chem , vol.273 , pp. 10792-10797
    • Berra, E.1    Diaz-Meco, M.T.2    Moscat, J.3
  • 35
    • 0032528172 scopus 로고    scopus 로고
    • Retinoic acid induced mitogen-activated protein (MAP)/extracellular signal-regulated kinase (ERK) kinase-dependent MAP kinase activation needed to elicit HL-60 cell differentiation and growth arrest
    • Yen A., Roberson M.S., Varvayanis S., and Lee A.T. Retinoic acid induced mitogen-activated protein (MAP)/extracellular signal-regulated kinase (ERK) kinase-dependent MAP kinase activation needed to elicit HL-60 cell differentiation and growth arrest. Cancer Res 58 (1998) 3263-3272
    • (1998) Cancer Res , vol.58 , pp. 3263-3272
    • Yen, A.1    Roberson, M.S.2    Varvayanis, S.3    Lee, A.T.4
  • 36
    • 0033729838 scopus 로고    scopus 로고
    • Control of the eukaryotic cell cycle by MAPK kinase signaling pathways
    • Wilkinson M., and Millar J. Control of the eukaryotic cell cycle by MAPK kinase signaling pathways. FASEB J 14 (2000) 2147-2157
    • (2000) FASEB J , vol.14 , pp. 2147-2157
    • Wilkinson, M.1    Millar, J.2
  • 37
    • 0033145531 scopus 로고    scopus 로고
    • Platelet-derived growth factor stimulation of mitogen-activated protein kinases and cyclin D1 promoter activity in cultured airway smooth-muscle cells
    • Page K., Li J., and Hershenson M.B. Platelet-derived growth factor stimulation of mitogen-activated protein kinases and cyclin D1 promoter activity in cultured airway smooth-muscle cells. Role Ras. Am J Respir 20 (1999) 1294-1302
    • (1999) Role Ras. Am J Respir , vol.20 , pp. 1294-1302
    • Page, K.1    Li, J.2    Hershenson, M.B.3
  • 38
    • 0032190629 scopus 로고    scopus 로고
    • Premature senescence involving p53 and p16 is activated in response to constitutive MEK/MAPK mitogen signaling
    • Lin A.W., Barradas M., Stone J.C., van Aelst L., Serrano M., and Lowe S.W. Premature senescence involving p53 and p16 is activated in response to constitutive MEK/MAPK mitogen signaling. Genes Dev 12 (1998) 3008-3019
    • (1998) Genes Dev , vol.12 , pp. 3008-3019
    • Lin, A.W.1    Barradas, M.2    Stone, J.C.3    van Aelst, L.4    Serrano, M.5    Lowe, S.W.6
  • 39
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
    • Serrano M., Lin A.W., McCurrach M.E., Beach D., and Lowe S.W. Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 88 (1997) 593-602
    • (1997) Cell , vol.88 , pp. 593-602
    • Serrano, M.1    Lin, A.W.2    McCurrach, M.E.3    Beach, D.4    Lowe, S.W.5
  • 40
    • 0030871667 scopus 로고    scopus 로고
    • High-intensity Raf signal causes cell cycle arrest mediated by p21 Clip
    • Sewing A., Wiseman B., Lloyd A.C., and Land H. High-intensity Raf signal causes cell cycle arrest mediated by p21 Clip. Mol Cell Biol 17 (1997) 5588-5597
    • (1997) Mol Cell Biol , vol.17 , pp. 5588-5597
    • Sewing, A.1    Wiseman, B.2    Lloyd, A.C.3    Land, H.4
  • 41
    • 0030835430 scopus 로고    scopus 로고
    • Raf-induced proliferation or cell cycle arrest is determined by the level of Raf activity with arrest mediated by p21Clip1
    • Woods D., Parry D., Cherwinski H., Bosch E., Lees E., and McMahon M. Raf-induced proliferation or cell cycle arrest is determined by the level of Raf activity with arrest mediated by p21Clip1. Mol Cell Biol 17 (1997) 5598-5611
    • (1997) Mol Cell Biol , vol.17 , pp. 5598-5611
    • Woods, D.1    Parry, D.2    Cherwinski, H.3    Bosch, E.4    Lees, E.5    McMahon, M.6
  • 42
    • 0032514802 scopus 로고    scopus 로고
    • 1-phase growth-arresting action of Interleukin-1 is independent of p53 and p21/WAF1 function
    • 1-phase growth-arresting action of Interleukin-1 is independent of p53 and p21/WAF1 function. J Biol Chem 273 (1998) 30517-30523
    • (1998) J Biol Chem , vol.273 , pp. 30517-30523
    • Nalca, A.1    Rangnekar, V.M.2
  • 43
    • 0035794174 scopus 로고    scopus 로고
    • Altered regulation of cell cycle machinery involved in interleukin-1-induced G(1) and G(2) phase growth arrest of A375S2 human melanoma cells
    • Murai T., Nakagawa Y., Maeda H., and Terada K. Altered regulation of cell cycle machinery involved in interleukin-1-induced G(1) and G(2) phase growth arrest of A375S2 human melanoma cells. J Biol Chem 276 (2001) 6797-6806
    • (2001) J Biol Chem , vol.276 , pp. 6797-6806
    • Murai, T.1    Nakagawa, Y.2    Maeda, H.3    Terada, K.4
  • 45
    • 0029669966 scopus 로고    scopus 로고
    • Interleukin-1 induces growth arrest by hypophosphorylation of the retinoblastoma susceptibility gene product RB
    • Muthukkumar S., Sells S.F., Crist S.A., and Rangnekar V.M. Interleukin-1 induces growth arrest by hypophosphorylation of the retinoblastoma susceptibility gene product RB. J Biol Chem 271 (1996) 5733-5740
    • (1996) J Biol Chem , vol.271 , pp. 5733-5740
    • Muthukkumar, S.1    Sells, S.F.2    Crist, S.A.3    Rangnekar, V.M.4
  • 46
    • 0033559703 scopus 로고    scopus 로고
    • Regulation of RB and E2F by signal transduction cascades: divergent effects of JNK1 and p38 kinases
    • Wang S., Nath N., Minden A., and Chellappan S. Regulation of RB and E2F by signal transduction cascades: divergent effects of JNK1 and p38 kinases. EMBO J 18 (1999) 1559-1570
    • (1999) EMBO J , vol.18 , pp. 1559-1570
    • Wang, S.1    Nath, N.2    Minden, A.3    Chellappan, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.