메뉴 건너뛰기




Volumn 25, Issue 11, 2005, Pages 4676-4682

Graded mitogen-activated protein kinase activity precedes switch-like c-Fos induction in mammalian cells

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PROGESTERONE;

EID: 18944374155     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.25.11.4676-4682.2005     Document Type: Article
Times cited : (91)

References (20)
  • 1
    • 1242274449 scopus 로고    scopus 로고
    • Detection of multistability, bifurcations, and hysteresis in a large class of biological positive-feedback systems
    • Angeli, D., J. E. Ferrell, Jr., and E. D. Sontag. 2004. Detection of multistability, bifurcations, and hysteresis in a large class of biological positive-feedback systems. Proc. Natl. Acad. Sci. USA 101:1822-1827.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1822-1827
    • Angeli, D.1    Ferrell Jr., J.E.2    Sontag, E.D.3
  • 2
    • 0035822634 scopus 로고    scopus 로고
    • Instability in the JNK cascade
    • Bagowski, C. P., and J. E. Ferrell, Jr. 2001. Instability in the JNK cascade. Curr. Biol. 11:1176-1182.
    • (2001) Curr. Biol. , vol.11 , pp. 1176-1182
    • Bagowski, C.P.1    Ferrell Jr., J.E.2
  • 4
    • 0033081066 scopus 로고    scopus 로고
    • Nuclear translocation of p42/p44 mitogen-activated protein kinase is required for growth factor-induced gene expression and cell cycle entry
    • Brunet, A., D. Roux, P. Lenormand, S. Dowd, S. Keyse, and J. Pouyssegur. 1999. Nuclear translocation of p42/p44 mitogen-activated protein kinase is required for growth factor-induced gene expression and cell cycle entry. EMBO J. 18:664-674.
    • (1999) EMBO J. , vol.18 , pp. 664-674
    • Brunet, A.1    Roux, D.2    Lenormand, P.3    Dowd, S.4    Keyse, S.5    Pouyssegur, J.6
  • 5
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L. C. 2002. The phosphoinositide 3-kinase pathway. Science 296:1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 6
    • 0026608787 scopus 로고
    • Nuclear localization and regulation of erk- and rsk-encoded protein kinases
    • Chen, R. H., C. Sarnecki, and J. Blenis. 1992. Nuclear localization and regulation of erk- and rsk-encoded protein kinases. Mol. Cell. Biol. 12:915-927.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 915-927
    • Chen, R.H.1    Sarnecki, C.2    Blenis, J.3
  • 7
    • 0026266288 scopus 로고
    • ERKs, extracellular signal-regulated MAP-2 kinases
    • Cobb, M. H., D. J. Robbins, and T. G. Boulton. 1991. ERKs, extracellular signal-regulated MAP-2 kinases. Curr. Opin. Cell Biol. 3:1025-1032.
    • (1991) Curr. Opin. Cell Biol. , vol.3 , pp. 1025-1032
    • Cobb, M.H.1    Robbins, D.J.2    Boulton, T.G.3
  • 8
    • 0032409387 scopus 로고    scopus 로고
    • How regulated protein translocation can produce switch-like responses
    • Ferrell, J. E., Jr. 1998. How regulated protein translocation can produce switch-like responses. Trends Biochem. Sci. 23:461-465.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 461-465
    • Ferrell Jr., J.E.1
  • 9
    • 0032496358 scopus 로고    scopus 로고
    • The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes
    • Ferrell, J. E., Jr., and E. M. Machleder. 1998. The biochemical basis of an all-or-none cell fate switch in Xenopus oocytes. Science 280:895-898.
    • (1998) Science , vol.280 , pp. 895-898
    • Ferrell Jr., J.E.1    Machleder, E.M.2
  • 10
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke, T. F., S. I. Yang, T. O. Chan, K. Datta, A. Kazlauskas, D. K. Morrison, D. R. Kaplan, and P. N. Tsichlis. 1995. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 81:727-736.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.I.2    Chan, T.O.3    Datta, K.4    Kazlauskas, A.5    Morrison, D.K.6    Kaplan, D.R.7    Tsichlis, P.N.8
  • 11
    • 0142227019 scopus 로고    scopus 로고
    • Targeting the PI3K-Akt pathway in human cancer: Rationale and promise
    • Luo, J., B. D. Manning, and L. C. Cantley. 2003. Targeting the PI3K-Akt pathway in human cancer: rationale and promise. Cancer Cell 4:257-262.
    • (2003) Cancer Cell , vol.4 , pp. 257-262
    • Luo, J.1    Manning, B.D.2    Cantley, L.C.3
  • 12
    • 0345732643 scopus 로고    scopus 로고
    • A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration
    • Murphy, L. O., J. P. MacKeigan, and J. Blenis. 2004. A network of immediate early gene products propagates subtle differences in mitogen-activated protein kinase signal amplitude and duration. Mol. Cell. Biol. 24:144-153.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 144-153
    • Murphy, L.O.1    MacKeigan, J.P.2    Blenis, J.3
  • 13
    • 0036051342 scopus 로고    scopus 로고
    • Molecular interpretation of ERK signal duration by immediate early gene products
    • Murphy, L. O., S. Smith, R. H. Chen, D. C. Fingar, and J. Blenis. 2002. Molecular interpretation of ERK signal duration by immediate early gene products. Nat. Cell Biol. 4:556-554.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 556-554
    • Murphy, L.O.1    Smith, S.2    Chen, R.H.3    Fingar, D.C.4    Blenis, J.5
  • 14
    • 0345700833 scopus 로고    scopus 로고
    • Building a cell cycle oscillator: Hysteresis and bistability in the activation of Cdc2
    • Pomerening, J. R., E. D. Sontag, and J. E. Ferrell, Jr. 2003. Building a cell cycle oscillator: hysteresis and bistability in the activation of Cdc2. Nat. Cell Biol. 5:346-351.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 346-351
    • Pomerening, J.R.1    Sontag, E.D.2    Ferrell Jr., J.E.3
  • 15
    • 0038112035 scopus 로고    scopus 로고
    • Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity
    • Roux, P. P., S. A. Richards, and J. Blenis. 2003. Phosphorylation of p90 ribosomal S6 kinase (RSK) regulates extracellular signal-regulated kinase docking and RSK activity. Mol. Cell. Biol. 23:4796-4804.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4796-4804
    • Roux, P.P.1    Richards, S.A.2    Blenis, J.3
  • 17
    • 0030871667 scopus 로고    scopus 로고
    • High-intensity Raf signal causes cell cycle arrest mediated by p21Cip1
    • Sewing, A., B. Wiseman, A. C. Lloyd, and H. Land. 1997. High-intensity Raf signal causes cell cycle arrest mediated by p21Cip1. Mol. Cell. Biol. 17:5588-5597.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 5588-5597
    • Sewing, A.1    Wiseman, B.2    Lloyd, A.C.3    Land, H.4
  • 18
    • 8644266706 scopus 로고    scopus 로고
    • Stimulus-coupled spatial restriction of extracellular signal-regulated kinase 1/2 activity contributes to the specificity of signal-response pathways
    • Whitehurst, A., M. H. Cobb, and M. A. White. 2004. Stimulus-coupled spatial restriction of extracellular signal-regulated kinase 1/2 activity contributes to the specificity of signal-response pathways. Mol. Cell. Biol. 24:10145-10150.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10145-10150
    • Whitehurst, A.1    Cobb, M.H.2    White, M.A.3
  • 19
    • 0030835430 scopus 로고    scopus 로고
    • Raf-induced proliferation or cell cycle arrest is determined by the level of Raf activity with arrest mediated by p21Cip1
    • Woods, D., D. Parry, H. Cherwinski, E. Bosch, E. Lees, and M. McMahon. 1997. Raf-induced proliferation or cell cycle arrest is determined by the level of Raf activity with arrest mediated by p21Cip1. Mol. Cell. Biol. 17:5598-5611.
    • (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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.