메뉴 건너뛰기




Volumn 24, Issue 4, 1997, Pages 272-283

Neurotrophin regulation of gene expression

Author keywords

[No Author keywords available]

Indexed keywords

NEUROTROPHIN;

EID: 0031424306     PISSN: 03171671     EISSN: None     Source Type: Journal    
DOI: 10.1017/S0317167100032935     Document Type: Review
Times cited : (31)

References (131)
  • 1
    • 0023236055 scopus 로고
    • The nerve growth factor 35 years later
    • Levi-Montalcini R. The nerve growth factor 35 years later. Science 1987; 237: 1154-1162.
    • (1987) Science , vol.237 , pp. 1154-1162
    • Levi-Montalcini, R.1
  • 3
    • 0029812881 scopus 로고    scopus 로고
    • Therapeutic potential of neurotrophic factors for neurological disorders
    • Yuen EC, Mobley WC. Therapeutic potential of neurotrophic factors for neurological disorders. Ann Neurol 1996; 40: 346-354.
    • (1996) Ann Neurol , vol.40 , pp. 346-354
    • Yuen, E.C.1    Mobley, W.C.2
  • 4
    • 0029940555 scopus 로고    scopus 로고
    • The neurotrophins and CNTF: Two families of collaborative neurotrophic factors
    • Ip NY, Yancopoulos GD. The neurotrophins and CNTF: two families of collaborative neurotrophic factors. Ann Rev Neurosci 1996; 19: 491-515.
    • (1996) Ann Rev Neurosci , vol.19 , pp. 491-515
    • Ip, N.Y.1    Yancopoulos, G.D.2
  • 5
    • 0029892470 scopus 로고    scopus 로고
    • Physiology of the neurotrophins
    • Lewin GR, Barde Y-A. Physiology of the neurotrophins. Ann Rev Neurosci 1996: 19: 289-317.
    • (1996) Ann Rev Neurosci , vol.19 , pp. 289-317
    • Lewin, G.R.1    Barde, Y.-A.2
  • 6
    • 0028238769 scopus 로고
    • Functions of the neurotrophins during nervous system development: What the knockouts are teaching us
    • Snider WD. Functions of the neurotrophins during nervous system development: what the knockouts are teaching us. Cell 1994; 77: 627-638.
    • (1994) Cell , vol.77 , pp. 627-638
    • Snider, W.D.1
  • 7
    • 0026570535 scopus 로고
    • Neurotrophin 3 is a mitogen for cultured neural crest cells
    • Kalcheim C, Carmeli C, Rosenthal A. Neurotrophin 3 is a mitogen for cultured neural crest cells. Proc Natl Acad USA 1992; 89: 1661-1665.
    • (1992) Proc Natl Acad USA , vol.89 , pp. 1661-1665
    • Kalcheim, C.1    Carmeli, C.2    Rosenthal, A.3
  • 8
    • 0027729949 scopus 로고
    • NT-3 stimulates sympathetic neuroblast proliferation by promoting precursor survival
    • Dicicco-Bloom E, Friedman WJ, Black IB. NT-3 stimulates sympathetic neuroblast proliferation by promoting precursor survival. Neuron 1993; 11: 1101-1111.
    • (1993) Neuron , vol.11 , pp. 1101-1111
    • Dicicco-Bloom, E.1    Friedman, W.J.2    Black, I.B.3
  • 9
    • 0001716865 scopus 로고
    • Destruction of the sympathetic ganglia in mammals by an antiserum to a nerve growth factor protein
    • Levi-Montalcinin R, Booker B. Destruction of the sympathetic ganglia in mammals by an antiserum to a nerve growth factor protein. Proc Natl Acad Sci USA 1960; 46: 384-391.
    • (1960) Proc Natl Acad Sci USA , vol.46 , pp. 384-391
    • Levi-Montalcinin, R.1    Booker, B.2
  • 10
    • 0028297308 scopus 로고
    • Mice lacking nerve growth factor display perinatal loss of sensory and sympathetic neurons yet develop basal forebrain cholinergic neurons
    • Crowley C, Spencer SD, Nishimura MC, et al. Mice lacking nerve growth factor display perinatal loss of sensory and sympathetic neurons yet develop basal forebrain cholinergic neurons. Cell 1994; 76: 1001-1012.
    • (1994) Cell , vol.76 , pp. 1001-1012
    • Crowley, C.1    Spencer, S.D.2    Nishimura, M.C.3
  • 11
    • 0028331599 scopus 로고
    • Severe sensory and sympathetic neuropathies in mice carrying a disrupted trk/NGF receptor gene
    • Smeyne RJ, Klein R, Schnapp A, et al. Severe sensory and sympathetic neuropathies in mice carrying a disrupted trk/NGF receptor gene. Nature 1994; 368: 246-249.
    • (1994) Nature , vol.368 , pp. 246-249
    • Smeyne, R.J.1    Klein, R.2    Schnapp, A.3
  • 12
    • 0027410119 scopus 로고
    • Neurotrophin 3 supports the survival of developing muscle sensory neurons in culture
    • Hory-Lee F, Russell M, Lindsay RM, Frank E. Neurotrophin 3 supports the survival of developing muscle sensory neurons in culture. Proc Natl Acad Sci USA 1993; 90: 2613-2617.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2613-2617
    • Hory-Lee, F.1    Russell, M.2    Lindsay, R.M.3    Frank, E.4
  • 13
    • 0028291238 scopus 로고
    • Lack of neurotropin-3 leads to deficiencies in the peripheral nervous system and loss of limb proprioceptive afferents
    • Ernfors P, Lee K-F, Kucera J, Jaenisch R. Lack of neurotropin-3 leads to deficiencies in the peripheral nervous system and loss of limb proprioceptive afferents. Cell 1994; 77: 503-512.
    • (1994) Cell , vol.77 , pp. 503-512
    • Ernfors, P.1    Lee, K.-F.2    Kucera, J.3    Jaenisch, R.4
  • 14
    • 0028329355 scopus 로고
    • Disruption of the neurotrophin-3 receptor gene trkC eliminates Ia muscle afferents and results in abnormal movements
    • Klein R, Silos-Santiago I, Smeyne RJ, et al. Disruption of the neurotrophin-3 receptor gene trkC eliminates Ia muscle afferents and results in abnormal movements. Nature 1994; 368: 249-251.
    • (1994) Nature , vol.368 , pp. 249-251
    • Klein, R.1    Silos-Santiago, I.2    Smeyne, R.J.3
  • 15
    • 0028351190 scopus 로고
    • Targeted disruption of the brain-derived neurotrophic factor gene perturbs brain and sensory neuron but not motor neuron development
    • Jones KR, Farinas I, Backus C, Reichardt LF. Targeted disruption of the brain-derived neurotrophic factor gene perturbs brain and sensory neuron but not motor neuron development. Cell 1994; 76: 989-1000.
    • (1994) Cell , vol.76 , pp. 989-1000
    • Jones, K.R.1    Farinas, I.2    Backus, C.3    Reichardt, L.F.4
  • 16
    • 0022486717 scopus 로고
    • Nerve growth factor promotes survival of septal cholinergic neurons after fimbrial transections
    • Hefti F. Nerve growth factor promotes survival of septal cholinergic neurons after fimbrial transections. J Neurosci 1986; 6: 2155-2162.
    • (1986) J Neurosci , vol.6 , pp. 2155-2162
    • Hefti, F.1
  • 17
    • 0023643241 scopus 로고
    • Amelioration of cholinergic neuron atrophy and spatial memory impairment in aged rats by nerve growth factor
    • Fischer W, Wictorin K, Bjorklund A. Amelioration of cholinergic neuron atrophy and spatial memory impairment in aged rats by nerve growth factor. Nature 1987; 326: 65-68.
    • (1987) Nature , vol.326 , pp. 65-68
    • Fischer, W.1    Wictorin, K.2    Bjorklund, A.3
  • 18
    • 0029116695 scopus 로고
    • Distinct roles for bFGF and NT-3 in the regulation of cortical neurosenesis
    • Ghosh A, Greenberg ME, Distinct roles for bFGF and NT-3 in the regulation of cortical neurosenesis. Neuron 1995; 15: 1-20.
    • (1995) Neuron , vol.15 , pp. 1-20
    • Ghosh, A.1    Greenberg, M.E.2
  • 19
    • 0029150839 scopus 로고
    • Functions of basic fibroblast growth factor and neurotrophins in the differentiation of hippocampal neurons
    • Vicario-Abejon C, Johe KK, Hazel TG, Collazo D, McKay RDG. Functions of basic fibroblast growth factor and neurotrophins in the differentiation of hippocampal neurons. Neuron 1995; 15: 105-114.
    • (1995) Neuron , vol.15 , pp. 105-114
    • Vicario-Abejon, C.1    Johe, K.K.2    Hazel, T.G.3    Collazo, D.4    McKay, R.D.G.5
  • 20
    • 0027070473 scopus 로고
    • Brain-derived neurotrophic factor prevents the death of motoneurons in newborn rats after nerve section
    • Sendtner M, Holtmann B, Kolbeck R, Thoenen H, Barde Y-A. Brain-derived neurotrophic factor prevents the death of motoneurons in newborn rats after nerve section. Nature 1992; 360: 757-759.
    • (1992) Nature , vol.360 , pp. 757-759
    • Sendtner, M.1    Holtmann, B.2    Kolbeck, R.3    Thoenen, H.4    Barde, Y.-A.5
  • 21
    • 0027067035 scopus 로고
    • Brain-derived neurotrophic factor rescues spinal motor neurons from axotomy-induced cell death
    • Yan Q, Elliot J, Snider WD. Brain-derived neurotrophic factor rescues spinal motor neurons from axotomy-induced cell death. Nature 1992; 360: 753-755.
    • (1992) Nature , vol.360 , pp. 753-755
    • Yan, Q.1    Elliot, J.2    Snider, W.D.3
  • 22
    • 0027318116 scopus 로고
    • Neurotrophins promote motor neuron survival and are present in embryonic limb bud
    • Henderson CE, Camu W, Mettling C, et al. Neurotrophins promote motor neuron survival and are present in embryonic limb bud. Nature 1993; 363: 266-270.
    • (1993) Nature , vol.363 , pp. 266-270
    • Henderson, C.E.1    Camu, W.2    Mettling, C.3
  • 23
    • 0018584222 scopus 로고
    • Nerve growth factor receptors. Characterization of two distinct classes of binding sites on chick embryo sensory ganglia cells
    • Sutter A, Riopelle RJ, Harris-Warrick RM, Shooter EM. Nerve growth factor receptors. Characterization of two distinct classes of binding sites on chick embryo sensory ganglia cells. J Biol Chem 1978; 82: 5972-5982.
    • (1978) J Biol Chem , vol.82 , pp. 5972-5982
    • Sutter, A.1    Riopelle, R.J.2    Harris-Warrick, R.M.3    Shooter, E.M.4
  • 24
    • 0022451914 scopus 로고
    • Gene transfer and molecular cloning of the human NGF receptor
    • Chao MV, Bothwell MA, Ross AH, et al. Gene transfer and molecular cloning of the human NGF receptor. Science 1986; 232: 518-521.
    • (1986) Science , vol.232 , pp. 518-521
    • Chao, M.V.1    Bothwell, M.A.2    Ross, A.H.3
  • 25
    • 0023002713 scopus 로고
    • Expression and structure of the human NGF receptor
    • Johnson D, Lanahan A, Buck CR, et al. Expression and structure of the human NGF receptor. Cell 1986; 47: 545-554.
    • (1986) Cell , vol.47 , pp. 545-554
    • Johnson, D.1    Lanahan, A.2    Buck, C.R.3
  • 26
    • 0023133256 scopus 로고
    • Gene transfer and molecular cloning of the rat nerve growth factor receptor
    • Radeke MJ, Misko TP, Hsu C, Herzenberg LA, Shooter EM. Gene transfer and molecular cloning of the rat nerve growth factor receptor. Nature 1987; 325: 593-597.
    • (1987) Nature , vol.325 , pp. 593-597
    • Radeke, M.J.1    Misko, T.P.2    Hsu, C.3    Herzenberg, L.A.4    Shooter, E.M.5
  • 27
    • 0026730310 scopus 로고
    • Neurotrophin receptors: A window into neuronal differentiation
    • Chao MV. Neurotrophin receptors: a window into neuronal differentiation. Neuron 1992b; 9: 583-593.
    • (1992) Neuron , vol.9 , pp. 583-593
    • Chao, M.V.1
  • 28
    • 0028916394 scopus 로고
    • Functional interactions of neurotrophins and neurotrophin receptors
    • Bothwell M. Functional interactions of neurotrophins and neurotrophin receptors. Ann Rev Neurosci 1995; 18: 223-253.
    • (1995) Ann Rev Neurosci , vol.18 , pp. 223-253
    • Bothwell, M.1
  • 29
    • 0025735392 scopus 로고
    • The trk proto-oncogene product: A signal transducing receptor for nerve growth factor
    • Kaplan DR, Hempstead B, Martin-Zanca D, Chao MV, Parada LF. The trk proto-oncogene product: a signal transducing receptor for nerve growth factor. Science 1991a; 242: 554-558.
    • (1991) Science , vol.242 , pp. 554-558
    • Kaplan, D.R.1    Hempstead, B.2    Martin-Zanca, D.3    Chao, M.V.4    Parada, L.F.5
  • 30
    • 0025797396 scopus 로고
    • Tyrosine phosphorylation and tyrosine kinase activity of the trk proto-oncogene product induced by NGF
    • Kaplan D, Martain-Zanca D, Parada LF. Tyrosine phosphorylation and tyrosine kinase activity of the trk proto-oncogene product induced by NGF. Nature 1991b; 350: 158-160.
    • (1991) Nature , vol.350 , pp. 158-160
    • Kaplan, D.1    Martain-Zanca, D.2    Parada, L.F.3
  • 31
    • 0025857391 scopus 로고
    • The trk proto-oncogene encodes a receptor for nerve growth factor
    • Klein R, Jing S, Nanduri V, O'Rourke E, Barbacid M. The trk proto-oncogene encodes a receptor for nerve growth factor. Cell 1991; 65: 189-197.
    • (1991) Cell , vol.65 , pp. 189-197
    • Klein, R.1    Jing, S.2    Nanduri, V.3    O'Rourke, E.4    Barbacid, M.5
  • 32
    • 0001419099 scopus 로고
    • PC12 pheochromocytoma cultures in neurobiological research
    • Greene LA, Tischler AS. PC12 pheochromocytoma cultures in neurobiological research. Adv Cell Neurobiol 1982; 3: 373-414.
    • (1982) Adv Cell Neurobiol , vol.3 , pp. 373-414
    • Greene, L.A.1    Tischler, A.S.2
  • 34
    • 0026091934 scopus 로고
    • The trk proto-oncogene rescues NGF responsiveness in mutant NGF-nonresponsive PC12 cell lines
    • Loeb D, Maragos J, Martin-Azanca D, Chao MV, Greene LA. The trk proto-oncogene rescues NGF responsiveness in mutant NGF-nonresponsive PC12 cell lines. Cell 1991; 66: 961-966.
    • (1991) Cell , vol.66 , pp. 961-966
    • Loeb, D.1    Maragos, J.2    Martin-Azanca, D.3    Chao, M.V.4    Greene, L.A.5
  • 35
    • 0026468503 scopus 로고
    • Overexpression of the trk tyrosine kinase rapidly accelerates nerve growth factorinduced differentiation
    • Hempstead BL, Rabin SJ, Kaplan L, et al. Overexpression of the trk tyrosine kinase rapidly accelerates nerve growth factorinduced differentiation. Neuron 1992; 9: 883-896.
    • (1992) Neuron , vol.9 , pp. 883-896
    • Hempstead, B.L.1    Rabin, S.J.2    Kaplan, L.3
  • 36
    • 0025986121 scopus 로고
    • New protein fold revealed by a 2.3 a resolution crystal structure of nerve growth factor
    • McDonald NQ, Lapatto R, Murray-Rust J, et al. New protein fold revealed by a 2.3 A resolution crystal structure of nerve growth factor. Nature 1991; 354: 411-414.
    • (1991) Nature , vol.354 , pp. 411-414
    • McDonald, N.Q.1    Lapatto, R.2    Murray-Rust, J.3
  • 37
    • 0028838012 scopus 로고
    • Dimerization of cell surface receptors in signal transduction
    • Heldin C. Dimerization of cell surface receptors in signal transduction. Cell 1995; 1995: 213-223.
    • (1995) Cell , vol.1995 , pp. 213-223
    • Heldin, C.1
  • 38
    • 0025765803 scopus 로고
    • SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins
    • Koch CA, Anderson D, Moran MF, Ellis C, Pawson T. SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins. Science 1991; 252: 668-674.
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 39
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • Cohen GB, Ren R, Baltimore D. Modular binding domains in signal transduction proteins. Cell 1995; 80: 237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • Cohen, G.B.1    Ren, R.2    Baltimore, D.3
  • 40
    • 0028888604 scopus 로고
    • The PTB domain: A new protein module implicated in signal transduction
    • van der Geer P, Pawson T. The PTB domain: a new protein module implicated in signal transduction. Trends Biochem Sci 1995; 20: 277-280.
    • (1995) Trends Biochem Sci , vol.20 , pp. 277-280
    • Van Der Geer, P.1    Pawson, T.2
  • 41
    • 0027403027 scopus 로고
    • SH2 domains recognize specific phosphopetide sequences
    • Songyang Z, Shoelson SE, Chaudhuri M, et al. SH2 domains recognize specific phosphopetide sequences. Cell 1993; 72: 767-778.
    • (1993) Cell , vol.72 , pp. 767-778
    • Songyang, Z.1    Shoelson, S.E.2    Chaudhuri, M.3
  • 42
    • 0027528508 scopus 로고
    • Tyrosine 785 is a major determinant of Trk-substrate interaction
    • Obermeier A, Halfter H, Wiesmuller KH, et al. Tyrosine 785 is a major determinant of Trk-substrate interaction. EMBO J 1993a; 12: 933-941.
    • (1993) EMBO J , vol.12 , pp. 933-941
    • Obermeier, A.1    Halfter, H.2    Wiesmuller, K.H.3
  • 43
    • 0027374486 scopus 로고
    • Identification of trk binding sites for SHC and phosphatidylinositol 3' -kinase and formation of a multimeric signaling complex
    • Obermeier A, Lammers R, Wiesmuller K, et al. Identification of trk binding sites for SHC and phosphatidylinositol 3' -kinase and formation of a multimeric signaling complex. J Biol Chem 1993b; 268: 22963-22966.
    • (1993) J Biol Chem , vol.268 , pp. 22963-22966
    • Obermeier, A.1    Lammers, R.2    Wiesmuller, K.3
  • 44
    • 0022137480 scopus 로고
    • Microinjection of the ras oncogene protein into PC12 cells induces morphologic differentiation
    • Bar-Sagi D, Feramisco JR. Microinjection of the ras oncogene protein into PC12 cells induces morphologic differentiation. Cell 1985; 42: 841-848.
    • (1985) Cell , vol.42 , pp. 841-848
    • Bar-Sagi, D.1    Feramisco, J.R.2
  • 45
    • 0022602017 scopus 로고
    • Inhibition of growth factorinduced differentiation of PC12 cells by microinjection of antibody to ras p21
    • Hagag N, Halegoua S, Viola M. Inhibition of growth factorinduced differentiation of PC12 cells by microinjection of antibody to ras p21. Cell 1986; 319: 680-682.
    • (1986) Cell , vol.319 , pp. 680-682
    • Hagag, N.1    Halegoua, S.2    Viola, M.3
  • 46
    • 0028199799 scopus 로고
    • Trk receptors use redundant signal transduction pathways involving SHC and PLC gamma 1 to mediate NGF responses
    • Stephens RD, Loeb D, Copeland T, et al. Trk receptors use redundant signal transduction pathways involving SHC and PLC gamma 1 to mediate NGF responses. Neuron 1994; 12: 691-705.
    • (1994) Neuron , vol.12 , pp. 691-705
    • Stephens, R.D.1    Loeb, D.2    Copeland, T.3
  • 47
    • 0026678172 scopus 로고
    • Association of the She and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases
    • Rozakis-Adcock M, McGlade J, Mbamulu G, et al. Association of the She and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature 1992; 360: 689-692.
    • (1992) Nature , vol.360 , pp. 689-692
    • Rozakis-Adcock, M.1    McGlade, J.2    Mbamulu, G.3
  • 48
    • 0026729382 scopus 로고
    • The SH2 and SH3 domaincontaining protein GRB2 links receptor tyrosine kinases to ras signalling
    • Lowenstein E, Daly R, Batzer A, et al. The SH2 and SH3 domaincontaining protein GRB2 links receptor tyrosine kinases to ras signalling. Cell 1992; 70: 431-442.
    • (1992) Cell , vol.70 , pp. 431-442
    • Lowenstein, E.1    Daly, R.2    Batzer, A.3
  • 49
    • 0028137615 scopus 로고
    • Activators and effectors of ras p21 proteins
    • McCormick F. Activators and effectors of ras p21 proteins. Curr Opin Genet Devel 1994; 4: 71-76.
    • (1994) Curr Opin Genet Devel , vol.4 , pp. 71-76
    • McCormick, F.1
  • 50
    • 0026534571 scopus 로고
    • Ras is essential for nerve growth factor and phorbol ester induced tyrosine phosphorylation of MAP kinases
    • Thomas SM, DeMarco M, D'Arcangelo G, Holegoua S, Brugge J. Ras is essential for nerve growth factor and phorbol ester induced tyrosine phosphorylation of MAP kinases. Cell 1992; 68: 1031-1040.
    • (1992) Cell , vol.68 , pp. 1031-1040
    • Thomas, S.M.1    DeMarco, M.2    D'Arcangelo, G.3    Holegoua, S.4    Brugge, J.5
  • 51
    • 0026523559 scopus 로고
    • Ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase, Raf-1, and RSK
    • Wood KW, Samecki C, Roberts TM, Blenis J. Ras mediates nerve growth factor receptor modulation of three signal-transducing protein kinases: MAP kinase, Raf-1, and RSK. Cell 1992; 68: 1041-1050.
    • (1992) Cell , vol.68 , pp. 1041-1050
    • Wood, K.W.1    Samecki, C.2    Roberts, T.M.3    Blenis, J.4
  • 52
    • 0028272507 scopus 로고
    • Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
    • Leevers SJ, Paterson HF, Marshall CJ. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 1994; 364: 411-414.
    • (1994) Nature , vol.364 , pp. 411-414
    • Leevers, S.J.1    Paterson, H.F.2    Marshall, C.J.3
  • 53
    • 0029006126 scopus 로고
    • Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phopshorylation
    • Marais R, Light Y, Paterson HF, Marshall CJ. Ras recruits Raf-1 to the plasma membrane for activation by tyrosine phopshorylation. 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
  • 54
    • 0028293931 scopus 로고
    • Identification of the sites in MAP kinase kinase-1 phosphorylated by p74raf-1
    • Alessi DR, Saito Y, Campbell DG, 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
  • 55
    • 0028228616 scopus 로고
    • Activation of MAP kinase kinase is necessary and sufficient for PC 12 cell differentiation and for transformation of NIH 3T3 cells
    • Cowley S, Paterson H, Kemp P, Marshall CJ. Activation of MAP kinase kinase is necessary and sufficient for PC 12 cell differentiation and for transformation of NIH 3T3 cells. Cell 1994; 77: 841-852.
    • (1994) Cell , vol.77 , pp. 841-852
    • Cowley, S.1    Paterson, H.2    Kemp, P.3    Marshall, C.J.4
  • 56
    • 0028152333 scopus 로고
    • MAP kinase kinase kinase, MAP kinase kinase, and MAP kinase
    • Marshall CJ. MAP kinase kinase kinase, MAP kinase kinase, and MAP kinase. Curr Opin Genet Devel 1994; 4: 82-89.
    • (1994) Curr Opin Genet Devel , vol.4 , pp. 82-89
    • Marshall, C.J.1
  • 57
    • 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. 1993; 90: 5889-5892.
    • (1993) Proc Natl Acad Sci. , vol.90 , pp. 5889-5892
    • Blenis, J.1
  • 58
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signaling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall CJ. Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation. Cell 1995; 80(2): 179-185.
    • (1995) Cell , vol.80 , Issue.2 , pp. 179-185
    • Marshall, C.J.1
  • 59
    • 0026608787 scopus 로고
    • Nuclear localization and regulation of erk- and rsk-encoded protein kinases
    • Chen RH, Sarnecki C, Blenis J. Nuclear localization and regulation of erk-and rsk-encoded protein kinases. Mol Cell Biol 1992; 12: 915-927.
    • (1992) Mol Cell Biol , vol.12 , pp. 915-927
    • Chen, R.H.1    Sarnecki, C.2    Blenis, J.3
  • 60
    • 0020144469 scopus 로고
    • The role of transcriptiondependent priming in nerve growth factor promoted neurite outgrowth
    • Greene LA, Burstein DE, Black MM. The role of transcriptiondependent priming in nerve growth factor promoted neurite outgrowth. Dev Biol 1982; 91: 305-316.
    • (1982) Dev Biol , vol.91 , pp. 305-316
    • Greene, L.A.1    Burstein, D.E.2    Black, M.M.3
  • 61
    • 0026578026 scopus 로고
    • Growth factor signaling: Where is the specificity?
    • Chao MV. Growth factor signaling: where is the specificity? Cell 1992a; 68: 995-997.
    • (1992) Cell , vol.68 , pp. 995-997
    • Chao, M.V.1
  • 62
    • 0022344633 scopus 로고
    • Nerve growth factor and epidermal growth factor induce rapid transient changes in protooncogene transcription in PC 12 cells
    • Greenberg ME, Greene LA, Ziff EB. Nerve growth factor and epidermal growth factor induce rapid transient changes in protooncogene transcription in PC 12 cells. J Biol Chem 1985; 260: 14101-14110.
    • (1985) J Biol Chem , vol.260 , pp. 14101-14110
    • Greenberg, M.E.1    Greene, L.A.2    Ziff, E.B.3
  • 63
    • 0025267015 scopus 로고
    • The regulation and function of c-fos and other immediate early genes in the nervous system
    • Sheng M, Greenberg ME. The regulation and function of c-fos and other immediate early genes in the nervous system. Neuron 1990; 4: 477-485.
    • (1990) Neuron , vol.4 , pp. 477-485
    • Sheng, M.1    Greenberg, M.E.2
  • 64
    • 0025769412 scopus 로고
    • Primary response genes induced by growth factor and tumor promoters
    • Herschman H. Primary response genes induced by growth factor and tumor promoters. Annu Rev Biochem 1991; 60: 281-319.
    • (1991) Annu Rev Biochem , vol.60 , pp. 281-319
    • Herschman, H.1
  • 65
    • 0023798751 scopus 로고
    • Fos and Jun: The AP-1 connection
    • Curran T, Franza BRJ. Fos and Jun: the AP-1 connection. Cell 1988; 55: 395-397.
    • (1988) Cell , vol.55 , pp. 395-397
    • Curran, T.1    Franza, B.R.J.2
  • 66
    • 0026486816 scopus 로고
    • Pleitropic effects of a null mutation in the c-fos proto-oncogene
    • Johnson RS, Spiegelman BM, Papaioannou VE. Pleitropic effects of a null mutation in the c-fos proto-oncogene. Cell 1992; 74: 577-586.
    • (1992) Cell , vol.74 , pp. 577-586
    • Johnson, R.S.1    Spiegelman, B.M.2    Papaioannou, V.E.3
  • 67
    • 0025959674 scopus 로고
    • Stimulus-transcription coupling in the nervous system: Involvement of the inducible proto-oncogenes fos and jun
    • Morgan JI, Curran T. Stimulus-transcription coupling in the nervous system: involvement of the inducible proto-oncogenes fos and jun. Ann Rev Neurosci 1991; 14: 421-451.
    • (1991) Ann Rev Neurosci , vol.14 , pp. 421-451
    • Morgan, J.I.1    Curran, T.2
  • 68
    • 0022633687 scopus 로고
    • Effect of protein synthesis inhibitors on growth factor activation of c-fos, c-myc, and actin gene transcription
    • Greenberg ME, Hermanowski AL, Ziff EB. Effect of protein synthesis inhibitors on growth factor activation of c-fos, c-myc, and actin gene transcription. Mol Cell Biol 1986; 6: 1050-1057.
    • (1986) Mol Cell Biol , vol.6 , pp. 1050-1057
    • Greenberg, M.E.1    Hermanowski, A.L.2    Ziff, E.B.3
  • 69
    • 0022137059 scopus 로고
    • Transient accumulation of c-fos RNa following serum stimulation requires a conserved 5' element and c-fos 3' sequences
    • Treisman R. Transient accumulation of c-fos RNA following serum stimulation requires a conserved 5' element and c-fos 3' sequences. Cell 1985; 42: 567-574.
    • (1985) Cell , vol.42 , pp. 567-574
    • Treisman, R.1
  • 70
    • 0007877023 scopus 로고
    • Inducible binding of a factor to the c-fos regulatory region
    • Hayes TE, Kitchen AM, Cochran BH. Inducible binding of a factor to the c-fos regulatory region. Proc Natl Acad Sci USA 1987; 84: 1272-1276.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 1272-1276
    • Hayes, T.E.1    Kitchen, A.M.2    Cochran, B.H.3
  • 71
    • 0024044345 scopus 로고
    • Calcium and growth factor pathways of c-fos transcriptional activation require distinct upstream regulatory sequences
    • Sheng M, Dougan ST, McFadden G, Greenberg ME. Calcium and growth factor pathways of c-fos transcriptional activation require distinct upstream regulatory sequences. Mol Cell Biol 1988; 8: 2787-2796.
    • (1988) Mol Cell Biol , vol.8 , pp. 2787-2796
    • Sheng, M.1    Dougan, S.T.2    McFadden, G.3    Greenberg, M.E.4
  • 72
    • 0024225850 scopus 로고
    • Induction of proto-oncogene fos transcription through the adenylate cyclase pathway: Characterization of a cAMP-response element
    • Sassone-Corsi P, Visvader J, Ferland L, Mellon P, Verma IM. Induction of proto-oncogene fos transcription through the adenylate cyclase pathway: characterization of a cAMP-response element. Genes Dev 1988; 2: 1529-1538.
    • (1988) Genes Dev , vol.2 , pp. 1529-1538
    • Sassone-Corsi, P.1    Visvader, J.2    Ferland, L.3    Mellon, P.4    Verma, I.M.5
  • 73
    • 0023522286 scopus 로고
    • C-fos sequences necessary for basal expression and induction by epidermal growth factor, 12-O-tetradecanoyl phorbol-13-acetate, and the calcium ionophore
    • Fisch TM, Prywes R, Roeder RG. c-fos sequences necessary for basal expression and induction by epidermal growth factor, 12-O-tetradecanoyl phorbol-13-acetate, and the calcium ionophore. Mol Cell Biol 1987; 7: 3490-3496.
    • (1987) Mol Cell Biol , vol.7 , pp. 3490-3496
    • Fisch, T.M.1    Prywes, R.2    Roeder, R.G.3
  • 74
    • 0024431797 scopus 로고
    • Multiple sequence elements of a single functional class are required for cyclic AMP responsiveness of the mouse c-fos promoter
    • Berkowitz LA, Riabowal KT, Gilman MZ. Multiple sequence elements of a single functional class are required for cyclic AMP responsiveness of the mouse c-fos promoter. Mol Cell Biol 1989; 9: 4272-4281.
    • (1989) Mol Cell Biol , vol.9 , pp. 4272-4281
    • Berkowitz, L.A.1    Riabowal, K.T.2    Gilman, M.Z.3
  • 75
    • 0026722103 scopus 로고
    • The serum response element
    • Treisman R. The serum response element. Trends Bioch Sci 1992; 17: 423-426.
    • (1992) Trends Bioch Sci , vol.17 , pp. 423-426
    • Treisman, R.1
  • 76
    • 0022486539 scopus 로고
    • Identification of a protein binding site that mediates transcriptional response of the cfos gene to serum factors
    • Treisman R. Identification of a protein binding site that mediates transcriptional response of the cfos gene to serum factors. Cell 1986; 46: 567-574.
    • (1986) Cell , vol.46 , pp. 567-574
    • Treisman, R.1
  • 77
    • 0023009699 scopus 로고
    • Multiple protein binding sites in the 5'-flanking region regulate cfos expression
    • Gilman MZ, Wilson RN, Weinberg RA. Multiple protein binding sites in the 5'-flanking region regulate cfos expression. Mol Cell Biol 1986; 6: 4305-4315.
    • (1986) Mol Cell Biol , vol.6 , pp. 4305-4315
    • Gilman, M.Z.1    Wilson, R.N.2    Weinberg, R.A.3
  • 78
    • 0023101454 scopus 로고
    • Mutation of the c-fos gene dyad symmetry element inhibits serum inducibility of transcription in vivo and the nuclear regulatory factor binding in vitro
    • Greenberg ME, Siegfried Z, Ziff EB. Mutation of the c-fos gene dyad symmetry element inhibits serum inducibility of transcription in vivo and the nuclear regulatory factor binding in vitro. Mol Cell Biol 1987; 7: 1217-1225.
    • (1987) Mol Cell Biol , vol.7 , pp. 1217-1225
    • Greenberg, M.E.1    Siegfried, Z.2    Ziff, E.B.3
  • 79
    • 0025022697 scopus 로고
    • The inner core of the serum response element mediates both the rapid induction and subsequent repression of c-fos transcription following serum stimulation
    • Rivera VM, Sheng M, Greenberg ME. The inner core of the serum response element mediates both the rapid induction and subsequent repression of c-fos transcription following serum stimulation. Genes Dev 1990; 4: 255-268.
    • (1990) Genes Dev , vol.4 , pp. 255-268
    • Rivera, V.M.1    Sheng, M.2    Greenberg, M.E.3
  • 80
    • 0029059248 scopus 로고
    • Serine 133-phosphorylated CREB induces transcription via a cooperative mechanism that may confer specificity to neurotrophin signals
    • Bonni A, Ginty DD, Dudek H, Greenberg ME. Serine 133-phosphorylated CREB induces transcription via a cooperative mechanism that may confer specificity to neurotrophin signals. Mol Cell Neurosci 1995; 6(2): 168-183.
    • (1995) Mol Cell Neurosci , vol.6 , Issue.2 , pp. 168-183
    • Bonni, A.1    Ginty, D.D.2    Dudek, H.3    Greenberg, M.E.4
  • 81
    • 0027385031 scopus 로고
    • A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity
    • Rivera VM, Miranti CK, Misra RP, et al. A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity. Mol Cell Biol 1993; 13: 6260-6273.
    • (1993) Mol Cell Biol , vol.13 , pp. 6260-6273
    • Rivera, V.M.1    Miranti, C.K.2    Misra, R.P.3
  • 82
    • 0029054136 scopus 로고
    • Calcium activates serum response factor-dependent transcription by a Ras- and Elk-1-independent mechanism that involves a Ca2+/calmodulin-dependent kinase
    • Miranti CK, Ginty DD, Huang G, Chatila T, Greenberg ME. Calcium activates serum response factor-dependent transcription by a Ras-and Elk-1-independent mechanism that involves a Ca2+/calmodulin-dependent kinase. Mol Cell Biol 1995; 15(7): 3672-3684.
    • (1995) Mol Cell Biol , vol.15 , Issue.7 , pp. 3672-3684
    • Miranti, C.K.1    Ginty, D.D.2    Huang, G.3    Chatila, T.4    Greenberg, M.E.5
  • 83
    • 0026556859 scopus 로고
    • Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element
    • Dalton S, Treisman R. Characterization of SAP-1, a protein recruited by serum response factor to the c-fos serum response element. Cell 1992; 68: 597-612.
    • (1992) Cell , vol.68 , pp. 597-612
    • Dalton, S.1    Treisman, R.2
  • 85
    • 0026695645 scopus 로고
    • TCF by MAP kinase stimulates ternary complex formation at the c-fos promoter
    • TCF by MAP kinase stimulates ternary complex formation at the c-fos promoter. Nature 1992; 358: 414-417.
    • (1992) Nature , vol.358 , pp. 414-417
    • Gille, R.1    Sharrocks, A.D.2    Shaw, P.E.3
  • 86
    • 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
  • 87
    • 0027322153 scopus 로고
    • c-fos transcriptional activation and repression correlate temporally with the phosphorylation status of TCF
    • Zinck R, Hipskind RA, Pingoud V, Nordheim A. c-fos transcriptional activation and repression correlate temporally with the phosphorylation status of TCF. EMBO J 1993; 12: 2377-2387.
    • (1993) EMBO J , vol.12 , pp. 2377-2387
    • Zinck, R.1    Hipskind, R.A.2    Pingoud, V.3    Nordheim, A.4
  • 88
    • 0024454855 scopus 로고
    • Two distinct cellular phosphoproteins bind to the c-fos serum element
    • Ryan WA, Franza Jr. BR, Gilman MZ. Two distinct cellular phosphoproteins bind to the c-fos serum element. EMBO J 1989; 8: 1785-1792.
    • (1989) EMBO J , vol.8 , pp. 1785-1792
    • Ryan, W.A.1    Franza Jr., B.R.2    Gilman, M.Z.3
  • 89
    • 0024596936 scopus 로고
    • Cross-binding of factors to functionally different promoter elements in c-fos and skeletal actin genes
    • Walsh K. Cross-binding of factors to functionally different promoter elements in c-fos and skeletal actin genes. Mol Cell Biol 1989; 9: 2191-2201.
    • (1989) Mol Cell Biol , vol.9 , pp. 2191-2201
    • Walsh, K.1
  • 90
    • 0027714828 scopus 로고
    • DNA bending and orientation-dependent function of YY1 in the c-fos promoter
    • Natesan S, Gilman MZ. DNA bending and orientation-dependent function of YY1 in the c-fos promoter. Genes Dev 1993; 7: 2497-2509.
    • (1993) Genes Dev , vol.7 , pp. 2497-2509
    • Natesan, S.1    Gilman, M.Z.2
  • 91
    • 0026737817 scopus 로고
    • Functional antagonism between YY1 and the serum response factor
    • Gualberto AD, LePage G, Pons SL, et al. Functional antagonism between YY1 and the serum response factor. Mol Cell Biol 1992; 12: 4209-4214.
    • (1992) Mol Cell Biol , vol.12 , pp. 4209-4214
    • Gualberto, A.D.1    LePage, G.2    Pons, S.L.3
  • 92
    • 0028818259 scopus 로고
    • YY1 facilitates the association of serum response factor with the c-fos serum response element
    • Natesan S, Oilman M. YY1 facilitates the association of serum response factor with the c-fos serum response element. Mol Cell Biol 1995; 15(11): 5975-5982.
    • (1995) Mol Cell Biol , vol.15 , Issue.11 , pp. 5975-5982
    • Natesan, S.1    Oilman, M.2
  • 93
    • 0026744318 scopus 로고
    • Human and Drosophila homeodomain proteins that enhance the DNA-binding activity of serum response factor
    • Gruenberg DA, Natesan S, Alexandre C, Oilman MZ. Human and Drosophila homeodomain proteins that enhance the DNA-binding activity of serum response factor. Science 1992; 257: 1089-1094.
    • (1992) Science , vol.257 , pp. 1089-1094
    • Gruenberg, D.A.1    Natesan, S.2    Alexandre, C.3    Oilman, M.Z.4
  • 94
    • 0028338460 scopus 로고
    • NGF activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB
    • Ginty DD, Bonni A, Greenberg ME. NGF activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB. Cell 1994; 77: 713-725.
    • (1994) Cell , vol.77 , pp. 713-725
    • Ginty, D.D.1    Bonni, A.2    Greenberg, M.E.3
  • 95
    • 0024616057 scopus 로고
    • Multiple sequence elements in the c-fos promoter mediate induction by cAMP
    • Fisch TM, Prywes R, Simon MC, Roeder RG. Multiple sequence elements in the c-fos promoter mediate induction by cAMP. Genes Dev 1989; 3: 198-211.
    • (1989) Genes Dev , vol.3 , pp. 198-211
    • Fisch, T.M.1    Prywes, R.2    Simon, M.C.3    Roeder, R.G.4
  • 96
    • 0026846986 scopus 로고
    • The CREB family of transcription factors
    • Brindle PK, Montminy MR. The CREB family of transcription factors. Cur Opin Gen Dev 1992; 2: 199-204.
    • (1992) Cur Opin Gen Dev , vol.2 , pp. 199-204
    • Brindle, P.K.1    Montminy, M.R.2
  • 97
    • 0027195403 scopus 로고
    • Cyclic adenosine 3' ,5' -monophosphate response element binding protein (CREB) and related transcription-activating deoxyribonucleic acid-binding proteins
    • Meyer TE, Habener JF. Cyclic adenosine 3' ,5' -monophosphate response element binding protein (CREB) and related transcription-activating deoxyribonucleic acid-binding proteins. Endocrine Rev 1993; 14: 269-290.
    • (1993) Endocrine Rev , vol.14 , pp. 269-290
    • Meyer, T.E.1    Habener, J.F.2
  • 98
    • 0025807509 scopus 로고
    • +2-regulated transcription factor phosphorylated by CaM kinases
    • +2-regulated transcription factor phosphorylated by CaM kinases. Science 1991; 252: 1427-1430.
    • (1991) Science , vol.252 , pp. 1427-1430
    • Sheng, M.E.1    Thompson, M.A.2    Greenberg, M.E.3
  • 99
    • 0024445798 scopus 로고
    • Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at Serine 133
    • Gonzalez GA, Montminy MR. Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at Serine 133. Cell 1989; 59: 675-680.
    • (1989) Cell , vol.59 , pp. 675-680
    • Gonzalez, G.A.1    Montminy, M.R.2
  • 100
    • 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
  • 101
    • 0027433708 scopus 로고
    • Phosphorylated CREB binds specifically to the nuclear protein CBP
    • Chrivia JC, Kwok RPS, Lamb N, et al. Phosphorylated CREB binds specifically to the nuclear protein CBP. Nature 1993; 365: 855-859.
    • (1993) Nature , vol.365 , pp. 855-859
    • Chrivia, J.C.1    Kwok, R.P.S.2    Lamb, N.3
  • 102
    • 0028060029 scopus 로고
    • Nuclear protein CBP is a coactivator for the transcription factor CREB
    • Kwok RPS, Lundblad JR, Chrivia JC, et al. Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature 1994; 370: 223-226.
    • (1994) Nature , vol.370 , pp. 223-226
    • Kwok, R.P.S.1    Lundblad, J.R.2    Chrivia, J.C.3
  • 103
    • 0028483678 scopus 로고
    • EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor
    • Traverse S, Seedorf K, Paterson H, et al. EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor. Curr Biol 1994; 4: 694-701.
    • (1994) Curr Biol , vol.4 , pp. 694-701
    • Traverse, S.1    Seedorf, K.2    Paterson, H.3
  • 104
    • 0028918408 scopus 로고
    • Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Hu Q, Klippel A, Muslin AJ, Fantl WJ, Williams LT. Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase. Science 1995; 268: 100-102.
    • (1995) Science , vol.268 , pp. 100-102
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3    Fantl, W.J.4    Williams, L.T.5
  • 105
    • 0028963084 scopus 로고
    • Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor
    • Yao R, Cooper GM. Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor. Science 1995; 267: 2003-2006.
    • (1995) Science , vol.267 , pp. 2003-2006
    • Yao, R.1    Cooper, G.M.2
  • 106
    • 0028883178 scopus 로고
    • Phospholipid signaling
    • Divecha N, Irvine RF. Phospholipid signaling. Cell 1995; 80: 269-278.
    • (1995) Cell , vol.80 , pp. 269-278
    • Divecha, N.1    Irvine, R.F.2
  • 107
    • 0030907987 scopus 로고    scopus 로고
    • PI3K: Downstream AK Tion blocks apoptosis
    • Franke TF, Kaplan DR, Cantley LC. PI3K: downstream AK Tion blocks apoptosis. Cell 1997; 88: 435-437.
    • (1997) Cell , vol.88 , pp. 435-437
    • Franke, T.F.1    Kaplan, D.R.2    Cantley, L.C.3
  • 108
    • 0029160069 scopus 로고
    • Protein kinase B (Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering B, Coffer P. Protein kinase B (Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 1995; 376: 599-602.
    • (1995) Nature , vol.376 , pp. 599-602
    • Burgering, B.1    Coffer, P.2
  • 109
    • 0029079275 scopus 로고
    • The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase
    • Franke TF, Yang SI, Chan TO, et al. The protein kinase encoded by the Akt proto-oncogene is a target of the PDGF-activated phosphatidylinositol 3-kinase. Cell 1995; 81: 727-736.
    • (1995) Cell , vol.81 , pp. 727-736
    • Franke, T.F.1    Yang, S.I.2    Chan, T.O.3
  • 110
    • 0031053586 scopus 로고    scopus 로고
    • Regulation of neuronal survival by the serine-threonine protein kinase Akt
    • Dudek H, Datta SR, Franke TF, et al. Regulation of neuronal survival by the serine-threonine protein kinase Akt. Science 1997; 275: 661-665.
    • (1997) Science , vol.275 , pp. 661-665
    • Dudek, H.1    Datta, S.R.2    Franke, T.F.3
  • 112
    • 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 RP, 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
    • Groot, R.P.1    Ballou, L.M.2    Sassone-Corsi, P.3
  • 113
    • 0027395119 scopus 로고
    • SNT, a differentiation-specific target of neurotrophic factor-induced tyrosine kinase activity in neurons and PC12 cells
    • Rabin S, Cleghorn V, Kaplan DR. SNT, a differentiation-specific target of neurotrophic factor-induced tyrosine kinase activity in neurons and PC12 cells. Mol Cell Biol 1993; 13: 2203-2213.
    • (1993) Mol Cell Biol , vol.13 , pp. 2203-2213
    • Rabin, S.1    Cleghorn, V.2    Kaplan, D.R.3
  • 114
    • 0029082202 scopus 로고
    • Deletion of a conserved juxtamembrane sequence in Trk abolishes NGF-promoted neuritogenesis
    • Peng X, Greene L, Kaplan DR, Stephens R. Deletion of a conserved juxtamembrane sequence in Trk abolishes NGF-promoted neuritogenesis. Neuron 1995; 15: 395-406.
    • (1995) Neuron , vol.15 , pp. 395-406
    • Peng, X.1    Greene, L.2    Kaplan, D.R.3    Stephens, R.4
  • 115
    • 0028897113 scopus 로고
    • Transcriptional regulation by extracellular signals: Mechanisms and specificity
    • Hill CS, Treisman R. Transcriptional regulation by extracellular signals: mechanisms and specificity. Cell 1995; 80: 199-211.
    • (1995) Cell , vol.80 , pp. 199-211
    • Hill, C.S.1    Treisman, R.2
  • 116
    • 0028905076 scopus 로고
    • Transcription factor ATF2 regulation by the JNK signal transduction pathway
    • Gupta S, Campbell D, Derijard B, Davis RJ. Transcription factor ATF2 regulation by the JNK signal transduction pathway. Science 1995; 267: 389-393.
    • (1995) Science , vol.267 , pp. 389-393
    • Gupta, S.1    Campbell, D.2    Derijard, B.3    Davis, R.J.4
  • 117
    • 0029125757 scopus 로고
    • Integration of MAP kinase signal transduction pathways at the serum response element
    • Whitmarsh AJ, Shore P, Sharrocks AD, Davis RJ. Integration of MAP kinase signal transduction pathways 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
  • 118
    • 0029145073 scopus 로고
    • Rho family members: Activators of MAP kinase cascades
    • Vojtek A, Cooper JA. Rho family members: activators of MAP kinase cascades. Cell 1995; 82: 527-529.
    • (1995) Cell , vol.82 , pp. 527-529
    • Vojtek, A.1    Cooper, J.A.2
  • 119
  • 120
    • 0347537940 scopus 로고    scopus 로고
    • Requirement for ceramide-initiated SAPK/JNK signalling in stress-induced apoptosis
    • Verheij M, Bose R, Lin XH, et al. Requirement for ceramide-initiated SAPK/JNK signalling in stress-induced apoptosis. Nature 1996; 380: 75-79.
    • (1996) Nature , vol.380 , pp. 75-79
    • Verheij, M.1    Bose, R.2    Lin, X.H.3
  • 121
    • 0027197994 scopus 로고
    • Substrate recognition by ceramide-activated protein kinase
    • Joseph C, Byun H, Bittman R, Kolesnick R. Substrate recognition by ceramide-activated protein kinase. J Biol Chem 1994; 268: 20002-20006.
    • (1994) J Biol Chem , vol.268 , pp. 20002-20006
    • Joseph, C.1    Byun, H.2    Bittman, R.3    Kolesnick, R.4
  • 122
    • 0028838235 scopus 로고
    • Phosphorylation of Raf by ceramide-activated protein kinase
    • Yao B, Zhang Y, Delikat S, et al. Phosphorylation of Raf by ceramide-activated protein kinase. Nature 1995; 378: 307-310.
    • (1995) Nature , vol.378 , pp. 307-310
    • Yao, B.1    Zhang, Y.2    Delikat, S.3
  • 123
    • 0028108788 scopus 로고
    • Activation of the sphingomyelinase cycle through the lowaffinity neurotrophin receptor
    • Dobrowsky RT, Werner MH, Castellino AM, Chao MV, Hannun YA. Activation of the sphingomyelinase cycle through the lowaffinity neurotrophin receptor. Science 1994; 265: 1596-1599.
    • (1994) Science , vol.265 , pp. 1596-1599
    • Dobrowsky, R.T.1    Werner, M.H.2    Castellino, A.M.3    Chao, M.V.4    Hannun, Y.A.5
  • 124
    • 0027966170 scopus 로고
    • Disruption of NGF binding to the low affinity neurotrophin receptor p75-LNTR reduces NGF binding to TrKA on PC12 cells
    • Barker PA, Shooter EP. Disruption of NGF binding to the low affinity neurotrophin receptor p75-LNTR reduces NGF binding to TrKA on PC12 cells. Neuron 1994; 13: 203-215.
    • (1994) Neuron , vol.13 , pp. 203-215
    • Barker, P.A.1    Shooter, E.P.2
  • 125
    • 0027330994 scopus 로고
    • p75-deficient trigeminal sensory neurons have an altered response to NGF but not to other neurotrophins
    • Davies AM, Lee K-F, Jaenisch R. p75-deficient trigeminal sensory neurons have an altered response to NGF but not to other neurotrophins. Neuron 1993; 11: 565-574.
    • (1993) Neuron , vol.11 , pp. 565-574
    • Davies, A.M.1    Lee, K.-F.2    Jaenisch, R.3
  • 126
    • 0027324122 scopus 로고
    • Induction of apoptosis by the low-affinity NGF receptor
    • Rabizadeh S, Oh J, Zhong LT, et al. Induction of apoptosis by the low-affinity NGF receptor. Science 1993; 261: 345-348.
    • (1993) Science , vol.261 , pp. 345-348
    • Rabizadeh, S.1    Oh, J.2    Zhong, L.T.3
  • 130
    • 0029022770 scopus 로고
    • Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP
    • Petrij F, Giles RH, Dauwerse HG, et al. Rubinstein-Taybi syndrome caused by mutations in the transcriptional co-activator CBP. Nature 1995; 376(6538): 348-351.
    • (1995) Nature , vol.376 , Issue.6538 , pp. 348-351
    • Petrij, F.1    Giles, R.H.2    Dauwerse, H.G.3
  • 131
    • 0029832136 scopus 로고    scopus 로고
    • Mutations in the kinse Rsk-2 associated with Coffin-Lowry syndrome
    • Trivier E, De Cesare D, Jacquot S, et al. Mutations in the kinse Rsk-2 associated with Coffin-Lowry syndrome. Nature 1996; 384: 567-570.
    • (1996) Nature , vol.384 , pp. 567-570
    • Trivier, E.1    De Cesare, D.2    Jacquot, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.