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Volumn 35, Issue 4-6, 2006, Pages 267-281

Differential activation of extracellular signal-regulated kinase 1 and a related complex in neuronal nuclei

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; POTASSIUM; PROTEIN P90; TRANSCRIPTION FACTOR ELK 1;

EID: 44149123762     PISSN: 15597105     EISSN: 15597113     Source Type: Journal    
DOI: 10.1007/s11068-008-9018-7     Document Type: Article
Times cited : (9)

References (54)
  • 1
    • 0034610996 scopus 로고    scopus 로고
    • Nuclear export of MAP kinase (ERK) involves a MAP kinase kinase (MEK)-dependent active transport mechanism
    • Adachi, M., Fukuda, M., Nishida, E. (2000). Nuclear export of MAP kinase (ERK) involves a MAP kinase kinase (MEK)-dependent active transport mechanism. J. Cell Biol. 148, 849-856
    • (2000) J. Cell Biol. , vol.148 , pp. 849-856
    • Adachi, M.1    Fukuda, M.2    Nishida, E.3
  • 2
    • 25144433893 scopus 로고    scopus 로고
    • Late-phase long-term potentiation: Getting to the nucleus
    • Adams, J. P., Dudek, S. M. (2005). Late-phase long-term potentiation: Getting to the nucleus. Nat. Rev. Neurosci. 6, 737-743
    • (2005) Nat. Rev. Neurosci. , vol.6 , pp. 737-743
    • Adams, J.P.1    Dudek, S.M.2
  • 3
    • 0025813396 scopus 로고
    • Stimulation of protein tyrosine phosphorylation by NMDA receptor activation
    • Bading, H., Greenberg, M. E. (1991). Stimulation of protein tyrosine phosphorylation by NMDA receptor activation. Science 253, 912-914
    • (1991) Science , vol.253 , pp. 912-914
    • Bading, H.1    Greenberg, M.E.2
  • 4
    • 0030020261 scopus 로고    scopus 로고
    • Potassium chloride pulse enhances mitogen-activated protein kinase activity in rat hippocampal slices
    • Baron, C., Benes, C., Tan, H. V., Fagard, R., Roisin, M.-P. (1996). Potassium chloride pulse enhances mitogen-activated protein kinase activity in rat hippocampal slices. J. Neurochem. 66, 1005-1010
    • (1996) J. Neurochem. , vol.66 , pp. 1005-1010
    • Baron, C.1    Benes, C.2    Tan, H.V.3    Fagard, R.4    Roisin, M.-P.5
  • 5
    • 0030463470 scopus 로고    scopus 로고
    • CREB phosphorylation and dephosphorylation: A Ca2(+)- and stimulus duration-dependent switch for hippocampal gene expression
    • Bito, H., Deisseroth, K., Tsien, R. W. (1996). CREB phosphorylation and dephosphorylation: A Ca2(+)- and stimulus duration-dependent switch for hippocampal gene expression. Cell 87, 1203-1214
    • (1996) Cell , vol.87 , pp. 1203-1214
    • Bito, H.1    Deisseroth, K.2    Tsien, R.W.3
  • 6
    • 0033135345 scopus 로고    scopus 로고
    • A mitogen-activated protein kinase cascade in the CA1/CA2 subfield of the dorsal hippocampus is essential for long-term spatial memory
    • Blum, S., Moore, A. N., Adams, F., Dash, P. K. (1999). A mitogen-activated protein kinase cascade in the CA1/CA2 subfield of the dorsal hippocampus is essential for long-term spatial memory. J. Neurosci. 19, 3535-3544
    • (1999) J. Neurosci. , vol.19 , pp. 3535-3544
    • Blum, S.1    Moore, A.N.2    Adams, F.3    Dash, P.K.4
  • 7
    • 0027226219 scopus 로고
    • Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination
    • Brewer, G. J., Torricelli, J. R., Evege, E. K., Price, P. J. (1993). Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination. J. Neurosci. Res. 35, 567-576
    • (1993) J. Neurosci. Res. , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4
  • 8
    • 0041570280 scopus 로고    scopus 로고
    • Kinetic analysis of the action of tissue transglutaminase on peptide and protein substrates
    • Case, A., Stein, R. L. (2003). Kinetic analysis of the action of tissue transglutaminase on peptide and protein substrates. Biochemistry 42, 9466-9481
    • (2003) Biochemistry , vol.42 , pp. 9466-9481
    • Case, A.1    Stein, R.L.2
  • 9
    • 0026608787 scopus 로고
    • Nuclear localization and regulation of ERK- and RSK-encoded protein kinases
    • Chen, R.-H., Sarnecki, C., Blenis, J. (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
  • 11
    • 10644284616 scopus 로고    scopus 로고
    • Inhibition of calcium/calmodulin-dependent protein kinase kinase by protein 14-3-3
    • Davare, M. A., Saneyoshi, T., Guire, E. S., Nygaard, S. C., Soderling, T. R. (2004). Inhibition of calcium/calmodulin-dependent protein kinase kinase by protein 14-3-3. J. Biol. Chem. 279, 52191-52199
    • (2004) J. Biol. Chem. , vol.279 , pp. 52191-52199
    • Davare, M.A.1    Saneyoshi, T.2    Guire, E.S.3    Nygaard, S.C.4    Soderling, T.R.5
  • 12
    • 0035864132 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase/extracellular signal-regulated kinase activation in somatodendritic compartments: Roles of action potentials, frequency, and mode of calcium entry
    • Dudek, S. M., Fields, R. D. (2001). Mitogen-activated protein kinase/extracellular signal-regulated kinase activation in somatodendritic compartments: Roles of action potentials, frequency, and mode of calcium entry. J. Neurosci. 21, RC122
    • (2001) J. Neurosci. , vol.21 , pp. 122
    • Dudek, S.M.1    Fields, R.D.2
  • 13
    • 4444320809 scopus 로고    scopus 로고
    • MAP kinases as structural adaptors and enzymatic activators in transcriptional complexes
    • Edmunds, J. W., Mahadevan, L. C. (2004). MAP kinases as structural adaptors and enzymatic activators in transcriptional complexes. J. Cell Sci. 117, 3715-3723
    • (2004) J. Cell Sci. , vol.117 , pp. 3715-3723
    • Edmunds, J.W.1    Mahadevan, L.C.2
  • 14
    • 0345579566 scopus 로고    scopus 로고
    • Activation of p42 mitogen-activated protein kinase in hippocampal long term potentiation
    • English, J. D., Sweatt, J. D. (1996). Activation of p42 mitogen-activated protein kinase in hippocampal long term potentiation. J. Biol. Chem. 271, 24329-24332
    • (1996) J. Biol. Chem. , vol.271 , pp. 24329-24332
    • English, J.D.1    Sweatt, J.D.2
  • 15
    • 0034601685 scopus 로고    scopus 로고
    • What do scaffold proteins really do?
    • Ferrell, J. E. J. (2000). What do scaffold proteins really do? Sci. STKE 2000, PE1
    • (2000) Sci. STKE , vol.2000
    • Ferrell, J.E.J.1
  • 16
    • 0028073606 scopus 로고
    • Binding of 14-3-3 proteins to the protein kinase raf and effects on its activation
    • Freed, E., Symons, M., Macdonald, S. G., McCormick, F., Ruggieri, R. (1994). Binding of 14-3-3 proteins to the protein kinase raf and effects on its activation. Science 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
  • 17
    • 0029786994 scopus 로고    scopus 로고
    • Cytoplasmic localization of MAP kinase kinase directed by its N-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export sequence
    • Fukuda, M., Gotoh, I., Gotoh, Y., Nishida, E. (1996). Cytoplasmic localization of MAP kinase kinase directed by its N-terminal, leucine-rich short amino acid sequence, which acts as a nuclear export sequence. J. Biol. Chem. 271, 20024-20028
    • (1996) J. Biol. Chem. , vol.271 , pp. 20024-20028
    • Fukuda, M.1    Gotoh, I.2    Gotoh, Y.3    Nishida, E.4
  • 18
    • 0029147474 scopus 로고
    • Substrate requirements for transglutaminases. Influence of the amino acid residue preceding the amine donor lysine in a native protein
    • Grootjans, J. J., Groenen, P. J., de Jong, W. W. (1995). Substrate requirements for transglutaminases. Influence of the amino acid residue preceding the amine donor lysine in a native protein. J. Biol. Chem. 270, 22855-22858
    • (1995) J. Biol. Chem. , vol.270 , pp. 22855-22858
    • Grootjans, J.J.1    Groenen, P.J.2    De Jong, W.W.3
  • 19
    • 0033490104 scopus 로고    scopus 로고
    • Environment-specific expression of the immediate-early gene arc in hippocampal neuronal ensembles
    • Guzowski, J. F., McNaughton, B. L., Barnes, C. A., Worley, P. F. (1999). Environment-specific expression of the immediate-early gene arc in hippocampal neuronal ensembles. Nat. Neurosci. 2, 1120-1124
    • (1999) Nat. Neurosci. , vol.2 , pp. 1120-1124
    • Guzowski, J.F.1    McNaughton, B.L.2    Barnes, C.A.3    Worley, P.F.4
  • 20
    • 0035116275 scopus 로고    scopus 로고
    • Nuclear calcium signaling controls CREB-mediated gene expression triggered by synaptic activity
    • Hardingham, G. E., Arnold, F. J. L., Bading, H. (2001). Nuclear calcium signaling controls CREB-mediated gene expression triggered by synaptic activity. Nat. Neurosci. 4, 261-267
    • (2001) Nat. Neurosci. , vol.4 , pp. 261-267
    • Hardingham, G.E.1    Arnold, F.J.L.2    Bading, H.3
  • 21
    • 0037403309 scopus 로고    scopus 로고
    • Examining the mechanism of ERK nuclear translocation using green fluorescent protein
    • Horgan, A. M., Stork, P. J. (2003). Examining the mechanism of ERK nuclear translocation using green fluorescent protein. Exp. Cell Res. 285, 208-220
    • (2003) Exp. Cell Res. , vol.285 , pp. 208-220
    • Horgan, A.M.1    Stork, P.J.2
  • 23
    • 0028051904 scopus 로고
    • Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase
    • Irie, K., Gotoh, Y., Yashar, B. M., Errede, B., Nishida, E., Matsumoto, K. (1994). Stimulatory effects of yeast and mammalian 14-3-3 proteins on the Raf protein kinase. Science 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
  • 25
    • 1542375349 scopus 로고    scopus 로고
    • Immunoblot analysis reveals that isopeptide antibodies do not specifically recognize the epsilon-(gamma-glutamyl)lysine bonds formed by transglutaminase activity
    • Johnson, G. V., LeShoure, R. J. (2004). Immunoblot analysis reveals that isopeptide antibodies do not specifically recognize the epsilon-(gamma-glutamyl) lysine bonds formed by transglutaminase activity. J. Neurosci. Meth. 134, 151-158
    • (2004) J. Neurosci. Meth. , vol.134 , pp. 151-158
    • Johnson, G.V.1    Leshoure, R.J.2
  • 26
    • 4744365623 scopus 로고    scopus 로고
    • Both nuclear-cytoplasmic shuttling of the dual specificity phosphatase MKP-3 and its ability to anchor MAP kinase in the cytoplasm are mediated by a conserved nuclear export signal
    • Karlsson, M., Mathers, J., Dickinson, R. J., Mandl, M., Keyse, S. M. (2004). Both nuclear-cytoplasmic shuttling of the dual specificity phosphatase MKP-3 and its ability to anchor MAP kinase in the cytoplasm are mediated by a conserved nuclear export signal. J. Biol. Chem. 279, 41882-41891
    • (2004) J. Biol. Chem. , vol.279 , pp. 41882-41891
    • Karlsson, M.1    Mathers, J.2    Dickinson, R.J.3    Mandl, M.4    Keyse, S.M.5
  • 27
    • 27644575157 scopus 로고    scopus 로고
    • Coordinating ERK/MAPK signalling through scaffolds and inhibitors
    • Kolch, W. (2005). Coordinating ERK/MAPK signalling through scaffolds and inhibitors. Nat. Rev. Mol. Cell Biol. 6, 827-837
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 827-837
    • Kolch, W.1
  • 28
    • 0031852068 scopus 로고    scopus 로고
    • Growth factor-induced p42/p44 MAPK nuclear translocation and retention requires both MAPK activation and neosynthesis of nuclear anchoring proteins
    • Lenormand, P., Brondello, J.-M., Brunet, A., Pouyssegur, J. (1998). Growth factor-induced p42/p44 MAPK nuclear translocation and retention requires both MAPK activation and neosynthesis of nuclear anchoring proteins. J. Cell Biol. 142, 625-633
    • (1998) J. Cell Biol. , vol.142 , pp. 625-633
    • Lenormand, P.1    Brondello, J.-M.2    Brunet, A.3    Pouyssegur, J.4
  • 29
    • 0032524312 scopus 로고    scopus 로고
    • Distinct nuclear localization and activity of tissue transglutaminase
    • Lesort, M., Attanavanich, K., Zhang, J., Johnson, G. V. (1998). Distinct nuclear localization and activity of tissue transglutaminase. J. Biol. Chem. 273, 11991-11994
    • (1998) J. Biol. Chem. , vol.273 , pp. 11991-11994
    • Lesort, M.1    Attanavanich, K.2    Zhang, J.3    Johnson, G.V.4
  • 30
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand, L., Graham, R. M. (2003). Transglutaminases: Crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol. 4, 140-156
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 31
    • 0035503897 scopus 로고    scopus 로고
    • Tissue-transglutaminase in rat and human brain: Light and electron immunocytochemical analysis and in situ hybridization study
    • Maggio, N., Sellitti, S., Capano, C. P., Papa, M. (2001). Tissue-transglutaminase in rat and human brain: Light and electron immunocytochemical analysis and in situ hybridization study. Brain Res. Bull. 56, 173-182
    • (2001) Brain Res. Bull. , vol.56 , pp. 173-182
    • Maggio, N.1    Sellitti, S.2    Capano, C.P.3    Papa, M.4
  • 32
    • 26244442243 scopus 로고    scopus 로고
    • Protein phosphatases in MAPK signalling: We keep learning from yeast
    • Martin, H., Flandez, M., Nombela, C., Molina, M. (2005). Protein phosphatases in MAPK signalling: We keep learning from yeast. Mol. Microbiol. 58, 6-16
    • (2005) Mol. Microbiol. , vol.58 , pp. 6-16
    • Martin, H.1    Flandez, M.2    Nombela, C.3    Molina, M.4
  • 33
    • 1542335670 scopus 로고    scopus 로고
    • Intracellular localization and activity state of tissue transglutaminase differentially impacts cell death
    • Milakovic, T., Tucholski, J., McCoy, E., Johnson, G. V. W. (2004). Intracellular localization and activity state of tissue transglutaminase differentially impacts cell death. J. Biol. Chem. 279, 8715-8722
    • (2004) J. Biol. Chem. , vol.279 , pp. 8715-8722
    • Milakovic, T.1    Tucholski, J.2    McCoy, E.3    Johnson, G.V.W.4
  • 34
    • 0027183404 scopus 로고
    • Numerous candidate plasticity-related genes revealed by differential cDNA cloning
    • Nedivi, E., Hevroni, D., Naot, D., Israeli, D., Citri, Y. (1993). Numerous candidate plasticity-related genes revealed by differential cDNA cloning. Nature 363, 718-722
    • (1993) Nature , vol.363 , pp. 718-722
    • Nedivi, E.1    Hevroni, D.2    Naot, D.3    Israeli, D.4    Citri, Y.5
  • 35
    • 0141782254 scopus 로고    scopus 로고
    • In vivo cross-linking of nucleosomal histones catalyzed by nuclear transglutaminase in starfish sperm and its induction by egg jelly triggering the acrosome reaction
    • Nunomura, K., Kawakami, S., Shimizu, K., Hara, T., Nakamura, K., Terakawa, Y., Yamasaki, A., Ikegami, S. (2003). In vivo cross-linking of nucleosomal histones catalyzed by nuclear transglutaminase in starfish sperm and its induction by egg jelly triggering the acrosome reaction. Eur. J. Biochem. 270, 3750-3759
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3750-3759
    • Nunomura, K.1    Kawakami, S.2    Shimizu, K.3    Hara, T.4    Nakamura, K.5    Terakawa, Y.6    Yamasaki, A.7    Ikegami, S.8
  • 36
    • 0035917466 scopus 로고    scopus 로고
    • Crystal structure of the 14-3-3zeta:Serotonin N-acetyltransferase complex. a role for scaffolding in enzyme regulation
    • Obsil, T., Ghirlando, R., Klein, D. C., Ganguly, S., Dyda, F. (2001). Crystal structure of the 14-3-3zeta:Serotonin N-acetyltransferase complex. A role for scaffolding in enzyme regulation. Cell 105, 257-267
    • (2001) Cell , vol.105 , pp. 257-267
    • Obsil, T.1    Ghirlando, R.2    Klein, D.C.3    Ganguly, S.4    Dyda, F.5
  • 37
    • 0034773788 scopus 로고    scopus 로고
    • Some forms of cAMP-mediated long-lasting potentiation are associated with release of BDNF and nuclear translocation of phospho-MAP kinase
    • Patterson, S. L., Pittenger, C., Morozov, A., Martin, K. C., Scanlin, H., Drake, C., Kandel, E. R. (2001) Some forms of cAMP-mediated long-lasting potentiation are associated with release of BDNF and nuclear translocation of phospho-MAP kinase. Neuron 32, 123-140
    • (2001) Neuron , vol.32 , pp. 123-140
    • Patterson, S.L.1    Pittenger, C.2    Morozov, A.3    Martin, K.C.4    Scanlin, H.5    Drake, C.6    Kandel, E.R.7
  • 38
    • 0032988045 scopus 로고    scopus 로고
    • Interaction of tissue transglutaminase with nuclear transport protein importin-alpha3
    • Peng, X., Zhang, Y., Zhang, H., Graner, S., Williams, J. F., Levitt, M. L., Lokshin, A. (1999). Interaction of tissue transglutaminase with nuclear transport protein importin-alpha3. FEBS Lett. 446, 35-39
    • (1999) FEBS Lett. , vol.446 , pp. 35-39
    • Peng, X.1    Zhang, Y.2    Zhang, H.3    Graner, S.4    Williams, J.F.5    Levitt, M.L.6    Lokshin, A.7
  • 39
    • 30544449089 scopus 로고    scopus 로고
    • Active ERK1 is dimerized in vivo: Biphosphodimers generate peak kinase activity and monophosphodimer maintain basal ERK1 activity
    • Philipova, R., Whitaker, M. (2005). Active ERK1 is dimerized in vivo: Biphosphodimers generate peak kinase activity and monophosphodimer maintain basal ERK1 activity. J. Cell Sci. 118, 5767-5776
    • (2005) J. Cell Sci. , vol.118 , pp. 5767-5776
    • Philipova, R.1    Whitaker, M.2
  • 41
    • 0034657129 scopus 로고    scopus 로고
    • Developmentally regulated NMDA receptor-dependent dephosphorylation of cAMP response element-binding protein (CREB) in hippocampal neurons
    • Sala, C., Rudolph-Correia, S., Sheng, M. (2000). Developmentally regulated NMDA receptor-dependent dephosphorylation of cAMP response element-binding protein (CREB) in hippocampal neurons. J. Neurosci. 20, 3529-3536
    • (2000) J. Neurosci. , vol.20 , pp. 3529-3536
    • Sala, C.1    Rudolph-Correia, S.2    Sheng, M.3
  • 42
    • 2642535995 scopus 로고    scopus 로고
    • Migraine aura: New information on underlying mechanisms
    • Sanchez-del-Rio, M., Reuter, U. (2004). Migraine aura: New information on underlying mechanisms. Curr. Opin. Neurol. 17, 289-293
    • (2004) Curr. Opin. Neurol. , vol.17 , pp. 289-293
    • Sanchez-Del-Rio, M.1    Reuter, U.2
  • 43
    • 0029131043 scopus 로고
    • The activation and nuclear translocation of extracellular signal-regulated kinases (ERK-1 and -2) appear not to be required for elongation of neurites in PC12d cells
    • Sano, M., Kohno, M., Iwanaga, M. (1995). The activation and nuclear translocation of extracellular signal-regulated kinases (ERK-1 and -2) appear not to be required for elongation of neurites in PC12d cells. Brain Res. 688, 213-218
    • (1995) Brain Res. , vol.688 , pp. 213-218
    • Sano, M.1    Kohno, M.2    Iwanaga, M.3
  • 44
    • 0029925683 scopus 로고    scopus 로고
    • Intracellular signaling pathways activated by neurotrophic factors
    • Segal, R. A., Greenberg, M. E. (1996). Intracellular signaling pathways activated by neurotrophic factors. Annu. Rev. Neurosci. 19, 463-489
    • (1996) Annu. Rev. Neurosci. , vol.19 , pp. 463-489
    • Segal, R.A.1    Greenberg, M.E.2
  • 45
    • 0027964728 scopus 로고
    • Synergistic activation by Ras and 14-3-3 protein of a mitogen-activated protein kinase kinase kinase named Ras-dependent extracellular signal-regulated kinase kinase stimulator
    • Shimizu, K., Kuroda, S., Yamamori, B., Matsuda, S., Kaibuchi, K., Yamauchi, T., Isobe, T., Irie, K., Matsumoto, K., Takai, Y. (1994). Synergistic activation by Ras and 14-3-3 protein of a mitogen-activated protein kinase kinase kinase named Ras-dependent extracellular signal-regulated kinase kinase stimulator. J. Biol. Chem. 269, 22917-22920
    • (1994) J. Biol. Chem. , vol.269 , pp. 22917-22920
    • Shimizu, K.1    Kuroda, S.2    Yamamori, B.3    Matsuda, S.4    Kaibuchi, K.5    Yamauchi, T.6    Isobe, T.7    Irie, K.8    Matsumoto, K.9    Takai, Y.10
  • 46
    • 0037088902 scopus 로고    scopus 로고
    • Long-term depression in the adult hippocampus in vivo involves activation of extracellular signal-regulated kinase and phosphorylation of ELK-1
    • Thiels, E., Kanterewicz, B. I., Norman, E. D., Trzaskos, J. M., Klann, E. (2002). Long-term depression in the adult hippocampus in vivo involves activation of extracellular signal-regulated kinase and phosphorylation of ELK-1. J. Neurosci. 22, 2054-2062
    • (2002) J. Neurosci. , vol.22 , pp. 2054-2062
    • Thiels, E.1    Kanterewicz, B.I.2    Norman, E.D.3    Trzaskos, J.M.4    Klann, E.5
  • 47
    • 0026486878 scopus 로고
    • Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor
    • Traverse, S., Gomez, N., Paterson, H., Marshall, C., Cohen, P. (1992). Sustained activation of the mitogen-activated protein (MAP) kinase cascade may be required for differentiation of PC12 cells. Comparison of the effects of nerve growth factor and epidermal growth factor. Biochem. J. 288, 351-355
    • (1992) Biochem. J. , vol.288 , pp. 351-355
    • Traverse, S.1    Gomez, N.2    Paterson, H.3    Marshall, C.4    Cohen, P.5
  • 50
    • 0032422785 scopus 로고    scopus 로고
    • Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals
    • Whitmarsh, A. J., Davis, R. J. (1998). Structural organization of MAP-kinase signaling modules by scaffold proteins in yeast and mammals. Trends Biochem. Sci. 23, 481-485
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 481-485
    • Whitmarsh, A.J.1    Davis, R.J.2
  • 51
    • 0035956978 scopus 로고    scopus 로고
    • Activity-dependent CREB phosphorylation: Convergence of a fast, sensitive calmodulin kinase pathway and a slow, less sensitive mitogen-activated protein kinase pathway
    • Wu, G. Y., Deisseroth, K., Tsien, R. W. (2001). Activity-dependent CREB phosphorylation: Convergence of a fast, sensitive calmodulin kinase pathway and a slow, less sensitive mitogen-activated protein kinase pathway. Proc. Natl. Acad. Sci. USA 98, 2808-2813
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2808-2813
    • Wu, G.Y.1    Deisseroth, K.2    Tsien, R.W.3
  • 52
    • 0029058730 scopus 로고
    • Purification of a Ras-dependent mitogen-activated protein kinase kinase kinase from bovine brain cytosol and its identification as a complex of b-Raf and 14-3-3 proteins
    • Yamamori, B., Kuroda, S., Shimizu, K., Fukui, K., Ohtsuka, T., Takai, Y. (1995). Purification of a Ras-dependent mitogen-activated protein kinase kinase kinase from bovine brain cytosol and its identification as a complex of b-Raf and 14-3-3 proteins. J. Biol. Chem. 270, 11723-11726
    • (1995) J. Biol. Chem. , vol.270 , pp. 11723-11726
    • Yamamori, B.1    Kuroda, S.2    Shimizu, K.3    Fukui, K.4    Ohtsuka, T.5    Takai, Y.6
  • 53
    • 23044465671 scopus 로고    scopus 로고
    • Pattern-dependent role of NMDA receptors in action potential generation: Consequences on extracellular signal-regulated kinase activation
    • Zhao, M., Adams, J. P., Dudek, S. M. (2005). Pattern-dependent role of NMDA receptors in action potential generation: Consequences on extracellular signal-regulated kinase activation. J. Neurosci. 25, 7032-7039
    • (2005) J. Neurosci. , vol.25 , pp. 7032-7039
    • Zhao, M.1    Adams, J.P.2    Dudek, S.M.3
  • 54
    • 0029007314 scopus 로고
    • Rsk3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: Growth factor-stimulated kinase function and nuclear translocation
    • Zhao, Y., Bjorbaek, C., Weremowicz, S., Morton, C. C., Moller, D. E. (1995). Rsk3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: Growth factor-stimulated kinase function and nuclear translocation. Mol. Cell Biol. 15, 4353-4363
    • (1995) Mol. Cell Biol. , vol.15 , pp. 4353-4363
    • Zhao, Y.1    Bjorbaek, C.2    Weremowicz, S.3    Morton, C.C.4    Moller, D.E.5


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