메뉴 건너뛰기




Volumn 12, Issue 1, 2000, Pages 63-73

Ras protein signalling

Author keywords

Cell transformation; Ras proteins; Signalling

Indexed keywords

ISOPROTEIN; RAS PROTEIN;

EID: 0033996413     PISSN: 10445323     EISSN: None     Source Type: Journal    
DOI: 10.1006/smim.2000.0208     Document Type: Article
Times cited : (96)

References (102)
  • 2
    • 0024376173 scopus 로고
    • Ras oncogenes in human cancer
    • Bos JL. Ras oncogenes in human cancer. Cancer Res. 49:1989;4682-4689.
    • (1989) Cancer Res , vol.49 , pp. 4682-4689
    • Bos, J.L.1
  • 3
    • 0029955128 scopus 로고    scopus 로고
    • Control of Ras activation
    • Downward J. Control of Ras activation. Cancer Surv. 27:1996;87-100.
    • (1996) Cancer Surv , vol.27 , pp. 87-100
    • Downward, J.1
  • 4
    • 0030670137 scopus 로고    scopus 로고
    • Ras-like GTPases
    • Bos JL. Ras-like GTPases. Biochim Biophys Acta. 1333:1997;19-31.
    • (1997) Biochim Biophys Acta , vol.1333 , pp. 19-31
    • Bos, J.L.1
  • 6
    • 0028985017 scopus 로고
    • Involvement of p21Ras distinguishes positive and negative selection in thymocytes
    • Swan KA et al. Involvement of p21Ras distinguishes positive and negative selection in thymocytes. EMBO J. 14:1995;276-285.
    • (1995) EMBO J , vol.14 , pp. 276-285
    • Swan, K.A.1
  • 7
    • 0029991920 scopus 로고    scopus 로고
    • Blocked Ras activation in anergic CD4+ T cells
    • Fields PE, Gajewski TF, Fitch FW. Blocked Ras activation in anergic CD4+ T cells. Science. 271:1996;1276-1278.
    • (1996) Science , vol.271 , pp. 1276-1278
    • Fields, P.E.1    Gajewski, T.F.2    Fitch, F.W.3
  • 8
    • 0027399707 scopus 로고
    • Thymic T cell anergy in autoimmune nonobese diabetic mice is mediated by deficient T cell receptor regulation of the pathway of p21Ras activation
    • Rapoport MJ, Lazarus AH, Jaramillo A, Speck E, Delovitch TL. Thymic T cell anergy in autoimmune nonobese diabetic mice is mediated by deficient T cell receptor regulation of the pathway of p21Ras activation. J Exp Med. 177:1993;1221-1226.
    • (1993) J Exp Med , vol.177 , pp. 1221-1226
    • Rapoport, M.J.1    Lazarus, A.H.2    Jaramillo, A.3    Speck, E.4    Delovitch, T.L.5
  • 9
    • 0030664126 scopus 로고    scopus 로고
    • Control of B cell development by Ras-mediated activation of Raf
    • Iritani BM, Forbush KA, Farrar MA, Perlmutter RM. Control of B cell development by Ras-mediated activation of Raf. EMBO J. 16:1997;7019-7031.
    • (1997) EMBO J , vol.16 , pp. 7019-7031
    • Iritani, B.M.1    Forbush, K.A.2    Farrar, M.A.3    Perlmutter, R.M.4
  • 10
    • 0028877913 scopus 로고
    • Alterations in differentiation and behavior of monocytic phagocytes in transgenic mice that express dominant suppressors of ras signaling
    • Jin DI, Jameson SB, Reddy MA, Schenkman D, Ostrowski MC. Alterations in differentiation and behavior of monocytic phagocytes in transgenic mice that express dominant suppressors of ras signaling. Mol Cell Biol. 15:1995;693-703.
    • (1995) Mol Cell Biol , vol.15 , pp. 693-703
    • Jin, D.I.1    Jameson, S.B.2    Reddy, M.A.3    Schenkman, D.4    Ostrowski, M.C.5
  • 11
    • 0032937404 scopus 로고    scopus 로고
    • Modulation of the immune response and tumor growth by activated Ras
    • Weijzen S, Velders MP, Kast WM. Modulation of the immune response and tumor growth by activated Ras. Leukemia. 13:1999;502-513.
    • (1999) Leukemia , vol.13 , pp. 502-513
    • Weijzen, S.1    Velders, M.P.2    Kast, W.M.3
  • 12
    • 0031036777 scopus 로고    scopus 로고
    • Codon 12 Ras mutations in patients with myelodysplastic syndrome: Incidence and prognostic value
    • Constantinidou M et al. Codon 12 Ras mutations in patients with myelodysplastic syndrome: incidence and prognostic value. Ann Hematol. 74:1997;11-14.
    • (1997) Ann Hematol , vol.74 , pp. 11-14
    • Constantinidou, M.1
  • 13
    • 17344371122 scopus 로고    scopus 로고
    • RAS, FMS and p53 mutations and poor clinical outcome in myelodysplasias: A 10-year follow-up
    • Padua RA et al. RAS, FMS and p53 mutations and poor clinical outcome in myelodysplasias: a 10-year follow-up. Leukemia. 12:1998;887-892.
    • (1998) Leukemia , vol.12 , pp. 887-892
    • Padua, R.A.1
  • 14
    • 0030898417 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways
    • Robinson MJ, Cobb MH. Mitogen-activated protein kinase pathways. Curr Opin Cell Biol. 9:1997;180-186.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 180-186
    • Robinson, M.J.1    Cobb, M.H.2
  • 15
    • 0033118791 scopus 로고    scopus 로고
    • Signaling specificity: The RTK/RAS/MAP kinase pathway in metazoans
    • Tan PB, Kim SK. Signaling specificity: the RTK/RAS/MAP kinase pathway in metazoans. Trends Genet. 15:1999;145-149.
    • (1999) Trends Genet , vol.15 , pp. 145-149
    • Tan, P.B.1    Kim, S.K.2
  • 16
    • 0031767247 scopus 로고    scopus 로고
    • Genetics of RAS signaling in C. elegans
    • Sternberg PW, Han M. Genetics of RAS signaling in C. elegans. Trends Genet. 14:1998;466-472.
    • (1998) Trends Genet , vol.14 , pp. 466-472
    • Sternberg, P.W.1    Han, M.2
  • 17
    • 0032493812 scopus 로고    scopus 로고
    • Increasing complexity of the Ras signaling pathway
    • Vojtek AB, Der CJ. Increasing complexity of the Ras signaling pathway. J Biol Chem. 273:1998;19925-19928.
    • (1998) J Biol Chem , vol.273 , pp. 19925-19928
    • Vojtek, A.B.1    Der, C.J.2
  • 18
    • 0028884084 scopus 로고
    • Evidence for cell-specific differences in transformation by N-, H- And K-Ras
    • Maher J, Baker DA, Manning M, Dibb NJ, Roberts IA. Evidence for cell-specific differences in transformation by N-, H- and K-Ras. Oncogene. 11:1995;1639-1647.
    • (1995) Oncogene , vol.11 , pp. 1639-1647
    • Maher, J.1    Baker, D.A.2    Manning, M.3    Dibb, N.J.4    Roberts, I.A.5
  • 19
    • 0032533861 scopus 로고    scopus 로고
    • Harvey Ras results in a higher frequency of mammary carcinomas than Kirsten Ras after direct retroviral transfer into the rat mammary gland
    • Thompson TA, Kim K, Gould MN. Harvey Ras results in a higher frequency of mammary carcinomas than Kirsten Ras after direct retroviral transfer into the rat mammary gland. Cancer Res. 58:1998;5097-5104.
    • (1998) Cancer Res , vol.58 , pp. 5097-5104
    • Thompson, T.A.1    Kim, K.2    Gould, M.N.3
  • 21
    • 0030829782 scopus 로고    scopus 로고
    • K-Ras is essential for the development of the mouse embryo
    • Koera K et al. K-Ras is essential for the development of the mouse embryo. Oncogene. 15:1997;1151-1159.
    • (1997) Oncogene , vol.15 , pp. 1151-1159
    • Koera, K.1
  • 22
    • 0345135149 scopus 로고    scopus 로고
    • K-Ras is an essential gene in the mouse with partial functional overlap with N-Ras
    • Johnson L et al. K-Ras is an essential gene in the mouse with partial functional overlap with N-Ras. Genes Dev. 11:1997;2468-2481.
    • (1997) Genes Dev , vol.11 , pp. 2468-2481
    • Johnson, L.1
  • 23
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signalling: Transient versus sustained extracellular signal- regulated kinase activation
    • Marshall CJ. Specificity of receptor tyrosine kinase signalling: transient versus sustained extracellular signal- regulated kinase activation. Cell. 80:1995;179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 24
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic Ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
    • Serrano M, Lin AW, McCurrach ME, Beach D, Lowe SW. 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
  • 25
    • 0030871667 scopus 로고    scopus 로고
    • High-intensity Raf signal causes cell cycle arrest mediated by p21Cip1
    • A. Sewing, B. Wiseman, A. C. Lloyd, H. Land. High-intensity Raf signal causes cell cycle arrest mediated by p21Cip1. Mol Cell Biol. 17:1997;5588-5597.
    • (1997) Mol Cell Biol , vol.17 , pp. 5588-5597
    • A., S.1    B., W.2    A., C.L.3    H., L.4
  • 26
    • 0032537819 scopus 로고    scopus 로고
    • Signals from Ras and Rho GTPases interact to regulate expression of p21Waf1/Cip1
    • Olson MF, Paterson HF, Marshall CJ. Signals from Ras and Rho GTPases interact to regulate expression of p21Waf1/Cip1. Nature. 394:1998;295-299.
    • (1998) Nature , vol.394 , pp. 295-299
    • Olson, M.F.1    Paterson, H.F.2    Marshall, C.J.3
  • 27
    • 0028678043 scopus 로고
    • Tyrosine kinase signalling pathways
    • Pawson T. Tyrosine kinase signalling pathways. Princess Takamatsu Symp. 24:1994;303-322.
    • (1994) Princess Takamatsu Symp , vol.24 , pp. 303-322
    • Pawson, T.1
  • 28
    • 0030706168 scopus 로고    scopus 로고
    • A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway
    • Kouhara H et al. A lipid-anchored Grb2-binding protein that links FGF-receptor activation to the Ras/MAPK signaling pathway. Cell. 89:1997;693-702.
    • (1997) Cell , vol.89 , pp. 693-702
    • Kouhara, H.1
  • 29
    • 0031835659 scopus 로고    scopus 로고
    • Binding of Shp2 tyr osine phosphatase to FRS2 is essential for fibro- blast growth factor-induced PC12 cell differentiation
    • Hadari YR, Kouhara H, Lax I, Schlessinger J. Binding of Shp2 tyr osine phosphatase to FRS2 is essential for fibro- blast growth factor-induced PC12 cell differentiation. Mol Cell Biol. 18:1998;3966-3973.
    • (1998) Mol Cell Biol , vol.18 , pp. 3966-3973
    • Hadari, Y.R.1    Kouhara, H.2    Lax, I.3    Schlessinger, J.4
  • 31
    • 0028556728 scopus 로고
    • The torso pathway in Drosophila: Lessons on receptor tyrosine kinase signaling and pattern formation
    • Duffy JB, Perrimon N. The torso pathway in Drosophila: lessons on receptor tyrosine kinase signaling and pattern formation. Dev Biol. 166:1994;380-395.
    • (1994) Dev Biol , vol.166 , pp. 380-395
    • Duffy, J.B.1    Perrimon, N.2
  • 32
    • 0029930117 scopus 로고    scopus 로고
    • Drosophila terminal structure development is regulated by the compensatory activities of positive and negative phosphotyrosine signaling sites on the Torso RTK
    • Cleghon V et al. Drosophila terminal structure development is regulated by the compensatory activities of positive and negative phosphotyrosine signaling sites on the Torso RTK. Genes Dev. 10:1996;566-577.
    • (1996) Genes Dev , vol.10 , pp. 566-577
    • Cleghon, V.1
  • 33
    • 0032238275 scopus 로고    scopus 로고
    • Opposing actions of CSW and RasGAP modulate the strength of Torso RTK signaling in the Drosophila terminal pathway
    • Cleghon V et al. Opposing actions of CSW and RasGAP modulate the strength of Torso RTK signaling in the Drosophila terminal pathway. Mol Cell. 2:1999;719-727.
    • (1999) Mol Cell , vol.2 , pp. 719-727
    • Cleghon, V.1
  • 34
    • 0033534533 scopus 로고    scopus 로고
    • Adaptors and molecular scaffolds in immune cell signaling
    • Rudd CE. Adaptors and molecular scaffolds in immune cell signaling. Cell. 96:1999;5-8.
    • (1999) Cell , vol.96 , pp. 5-8
    • Rudd, C.E.1
  • 35
    • 0032080391 scopus 로고    scopus 로고
    • The real LAT steps forward
    • Cantrell D. The real LAT steps forward. Trends Cell Biol. 8:1998;180-182.
    • (1998) Trends Cell Biol , vol.8 , pp. 180-182
    • Cantrell, D.1
  • 36
    • 0033602224 scopus 로고    scopus 로고
    • Immune signalling: SHP-2 docks at multiple ports
    • Huyer G, Alexander DR. Immune signalling: SHP-2 docks at multiple ports. Curr Biol. 9:1999;129-132.
    • (1999) Curr Biol , vol.9 , pp. 129-132
    • Huyer, G.1    Alexander, D.R.2
  • 37
    • 0030744134 scopus 로고    scopus 로고
    • Role of phosphatases in lymphocyte activation
    • Neel BG. Role of phosphatases in lymphocyte activation. Curr Opin Immunol. 9:1997;405-420.
    • (1997) Curr Opin Immunol , vol.9 , pp. 405-420
    • Neel, B.G.1
  • 38
    • 0032238298 scopus 로고    scopus 로고
    • Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation
    • Gu H, Pratt JC, Burakoff SJ, Neel BG. Cloning of p97/Gab2, the major SHP2-binding protein in hematopoietic cells, reveals a novel pathway for cytokine-induced gene activation. Mol Cell. 2:1998;729-240.
    • (1998) Mol Cell , vol.2 , pp. 729-240
    • Gu, H.1    Pratt, J.C.2    Burakoff, S.J.3    Neel, B.G.4
  • 39
    • 0032185773 scopus 로고    scopus 로고
    • The Drosophila protein Dof is specifically required for FGF signaling
    • Vincent S, Wilson R, Coelho C, Affolter M, Leptin M. The Drosophila protein Dof is specifically required for FGF signaling. Mol Cell. 2:1998;515-525.
    • (1998) Mol Cell , vol.2 , pp. 515-525
    • Vincent, S.1    Wilson, R.2    Coelho, C.3    Affolter, M.4    Leptin, M.5
  • 40
    • 0033525895 scopus 로고    scopus 로고
    • Sprouty, an intracellular inhibitor of Ras signaling
    • Casci T, Vinós J, Freeman M. Sprouty, an intracellular inhibitor of Ras signaling. Cell. 96:1999;655-665.
    • (1999) Cell , vol.96 , pp. 655-665
    • Casci, T.1    Vinós, J.2    Freeman, M.3
  • 41
    • 0033602147 scopus 로고    scopus 로고
    • Conserved function of mSpry-2, a murine homolog of Drosophila sprouty, which negatively modulates respiratory organogenesis
    • Tefft JD et al. Conserved function of mSpry-2, a murine homolog of Drosophila sprouty, which negatively modulates respiratory organogenesis. Curr Biol. 9:1999;219-222.
    • (1999) Curr Biol , vol.9 , pp. 219-222
    • Tefft, J.D.1
  • 42
    • 0026021456 scopus 로고
    • Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B)
    • Hancock JF, Cadwallader K, Marshall CJ. Methylation and proteolysis are essential for efficient membrane binding of prenylated p21K-ras(B). EMBO J. 10:1991a;641-646.
    • (1991) EMBO J , vol.10 , pp. 641-646
    • Hancock, J.F.1    Cadwallader, K.2    Marshall, C.J.3
  • 43
    • 0026037624 scopus 로고
    • A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of Ras proteins
    • Hancock JF, Cadwaller K, Paterson H, Marshall CJ. A CAAX or a CAAL motif and a second signal are sufficient for plasma membrane targeting of Ras proteins. EMBO J. 10:1991b;4033-4039.
    • (1991) EMBO J , vol.10 , pp. 4033-4039
    • Hancock, J.F.1    Cadwaller, K.2    Paterson, H.3    Marshall, C.J.4
  • 44
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21Ras to the plasma membrane
    • Hancock JF, Paterson H, Marshall CJ. A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21Ras to the plasma membrane. Cell. 63:1990;133-139.
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 45
    • 85031638627 scopus 로고    scopus 로고
    • Jacobson, K, Dietrich, C, 1999, 87, 91
    • Jacobson, K, Dietrich, C, 1999, 87, 91.
  • 46
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol. 14:1998;111-136.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 47
    • 0033538474 scopus 로고    scopus 로고
    • New insights into the interaction of Ras with the plasma membrane
    • Magee T, Marshall C. New insights into the interaction of Ras with the plasma membrane. Cell. 98:1999;9-12.
    • (1999) Cell , vol.98 , pp. 9-12
    • Magee, T.1    Marshall, C.2
  • 48
    • 0033145517 scopus 로고    scopus 로고
    • Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains
    • Roy S et al. Dominant-negative caveolin inhibits H-Ras function by disrupting cholesterol-rich plasma membrane domains. Nat Cell Biol. 1:1999;98-105.
    • (1999) Nat Cell Biol , vol.1 , pp. 98-105
    • Roy, S.1
  • 49
    • 4244023406 scopus 로고    scopus 로고
    • Caveolin, cholesterol and Ras signalling
    • E37
    • Schmid, S, Sternberg, P, Caveolin, cholesterol and Ras signalling. Nat Cell Biol, 1, E35-, E37.
    • Nat Cell Biol , vol.1
    • Schmid, S.1    Sternberg, P.2
  • 50
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK)
    • Furuchi T, Anderson RG. Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK). J Biol Chem. 273:1998;21099-21104.
    • (1998) J Biol Chem , vol.273 , pp. 21099-21104
    • Furuchi, T.1    Anderson, R.G.2
  • 51
    • 0032545266 scopus 로고    scopus 로고
    • Expression of caveolin-1 in human T cell leukemia cell lines
    • Hatanaka M et al. Expression of caveolin-1 in human T cell leukemia cell lines. Biochem Biophys Res Commun. 253:1998;382-387.
    • (1998) Biochem Biophys Res Commun , vol.253 , pp. 382-387
    • Hatanaka, M.1
  • 52
    • 0033033321 scopus 로고    scopus 로고
    • Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: Accumulation of actin regulated by local tyrosine phosphorylation
    • Harder T, Simons K. Clusters of glycolipid and glycosylphosphatidylinositol-anchored proteins in lymphoid cells: accumulation of actin regulated by local tyrosine phosphorylation. Eur J Immunol. 29:1999;556-562.
    • (1999) Eur J Immunol , vol.29 , pp. 556-562
    • Harder, T.1    Simons, K.2
  • 53
    • 0032101348 scopus 로고    scopus 로고
    • Membrane compartmentation is required for efficient T cell activation
    • Xavier R, Brennan T, Li Q, McCormack C, Seed B. Membrane compartmentation is required for efficient T cell activation. Immunity. 8:1998;723-732.
    • (1998) Immunity , vol.8 , pp. 723-732
    • Xavier, R.1    Brennan, T.2    Li, Q.3    McCormack, C.4    Seed, B.5
  • 54
    • 0031964607 scopus 로고    scopus 로고
    • Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains
    • Schroeder RJ, Ahmed SN, Zhu Y, London E, Brown DA. Cholesterol and sphingolipid enhance the Triton X-100 insolubility of glycosylphosphatidylinositol-anchored proteins by promoting the formation of detergent-insoluble ordered membrane domains. J Biol Chem. 273:1998;1150-1157.
    • (1998) J Biol Chem , vol.273 , pp. 1150-1157
    • Schroeder, R.J.1    Ahmed, S.N.2    Zhu, Y.3    London, E.4    Brown, D.A.5
  • 55
    • 0033617415 scopus 로고    scopus 로고
    • Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe
    • Volonté D et al. Flotillins/cavatellins are differentially expressed in cells and tissues and form a hetero-oligomeric complex with caveolins in vivo. Characterization and epitope-mapping of a novel flotillin-1 monoclonal antibody probe. J Biol Chem. 274:1999;12702-12709.
    • (1999) J Biol Chem , vol.274 , pp. 12702-12709
    • Volonté, D.1
  • 56
    • 0032508517 scopus 로고    scopus 로고
    • Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase
    • Yan J, Roy S, Apolloni A, Lane A, Hancock JF. Ras isoforms vary in their ability to activate Raf-1 and phosphoinositide 3-kinase. J Biol Chem. 273:1998;24052-24056.
    • (1998) J Biol Chem , vol.273 , pp. 24052-24056
    • Yan, J.1    Roy, S.2    Apolloni, A.3    Lane, A.4    Hancock, J.F.5
  • 57
    • 0033546419 scopus 로고    scopus 로고
    • Four human ras homologs differ in their abilities to activate Raf-1, induce transformation, and stimulate cell motility
    • Voice JK, Klemke RL, Le A, Jackson JH. Four human ras homologs differ in their abilities to activate Raf-1, induce transformation, and stimulate cell motility. J Biol Chem. 274:1999;17164-17170.
    • (1999) J Biol Chem , vol.274 , pp. 17164-17170
    • Voice, J.K.1    Klemke, R.L.2    Le, A.3    Jackson, J.H.4
  • 58
    • 0032546232 scopus 로고    scopus 로고
    • Ha-Ras and N-Ras regulate MAPK activity by distinct mechanisms in vivo
    • Hamilton M, Wolfman A. Ha-Ras and N-Ras regulate MAPK activity by distinct mechanisms in vivo. Oncogene. 16:1998;1417-1428.
    • (1998) Oncogene , vol.16 , pp. 1417-1428
    • Hamilton, M.1    Wolfman, A.2
  • 60
    • 0027364980 scopus 로고
    • Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase
    • Fabian JR, Daar IO, Morrison DK. Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase. Mol Cell Biol. 13:1993;7170-7179.
    • (1993) Mol Cell Biol , vol.13 , pp. 7170-7179
    • Fabian, J.R.1    Daar, I.O.2    Morrison, D.K.3
  • 61
    • 0030756069 scopus 로고    scopus 로고
    • Phosphorylation of Raf-1 serine 338-serine 339 is an essential regulatory event for Ras-dependent activation and biolgical signalling
    • Diaz B et al. Phosphorylation of Raf-1 serine 338-serine 339 is an essential regulatory event for Ras-dependent activation and biolgical signalling. Mol Cell Biol. 17:1997;4509-4516.
    • (1997) Mol Cell Biol , vol.17 , pp. 4509-4516
    • Diaz, B.1
  • 62
    • 0033561041 scopus 로고    scopus 로고
    • Serine and tyrosine phosphorylations cooperate in Raf-1, but not B-Raf activation
    • Mason CS et al. Serine and tyrosine phosphorylations cooperate in Raf-1, but not B-Raf activation. EMBO J. 18:1999;2137-2148.
    • (1999) EMBO J , vol.18 , pp. 2137-2148
    • Mason, C.S.1
  • 63
    • 0029885617 scopus 로고    scopus 로고
    • Differential regulation of Raf isozymes by growth versus differentiation inducing factors in PC12 pheochromocytoma cells
    • Wixler V, Smola U, Schuler M, Rapp U. Differential regulation of Raf isozymes by growth versus differentiation inducing factors in PC12 pheochromocytoma cells. Febs Lett. 385:1996;131-137.
    • (1996) Febs Lett , vol.385 , pp. 131-137
    • Wixler, V.1    Smola, U.2    Schuler, M.3    Rapp, U.4
  • 64
    • 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 CJ, Cohen P. 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. 288:1992.
    • (1992) Biochem J , vol.288
    • Traverse, S.1    Gomez, N.2    Paterson, H.3    Marshall, C.J.4    Cohen, P.5
  • 65
    • 0028948382 scopus 로고
    • Multiple Ras functions can contribute to mammalian cell transformation
    • White MA et al. Multiple Ras functions can contribute to mammalian cell transformation. Cell. 80:1995;533-541.
    • (1995) Cell , vol.80 , pp. 533-541
    • White, M.A.1
  • 66
    • 0030911052 scopus 로고    scopus 로고
    • Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras
    • Rodriguez-Viciana P et al. Role of phosphoinositide 3-OH kinase in cell transformation and control of the actin cytoskeleton by Ras. Cell. 89:1997;457-467.
    • (1997) Cell , vol.89 , pp. 457-467
    • Rodriguez-Viciana, P.1
  • 67
    • 0030052368 scopus 로고    scopus 로고
    • Stimulation of membrane ruffling and MAP kinase activation by distinct effectors of Ras
    • Joneson T, White MA, Wigler MH, Bar-Sagi D. Stimulation of membrane ruffling and MAP kinase activation by distinct effectors of Ras. Science. 271:1996;810-812.
    • (1996) Science , vol.271 , pp. 810-812
    • Joneson, T.1    White, M.A.2    Wigler, M.H.3    Bar-Sagi, D.4
  • 68
    • 0029890896 scopus 로고    scopus 로고
    • Oncogenic Ras activation of Raf/mitogen-activated protein kinase-independent pathways is sufficient to cause tumorigenic transformation
    • KhosraviFar R et al. Oncogenic Ras activation of Raf/mitogen-activated protein kinase-independent pathways is sufficient to cause tumorigenic transformation. Mol Cell Biol. 16:1996;3923-3933.
    • (1996) Mol Cell Biol , vol.16 , pp. 3923-3933
    • Khosravifar, R.1
  • 69
    • 0031028730 scopus 로고    scopus 로고
    • Suppression of c-Myc-induced apoptosis by Ras signalling through PI(3)K and PKB
    • Kauffmann-Zeh A et al. Suppression of c-Myc-induced apoptosis by Ras signalling through PI(3)K and PKB. Nature. 385:1997;544-548.
    • (1997) Nature , vol.385 , pp. 544-548
    • Kauffmann-Zeh, A.1
  • 70
    • 0032190774 scopus 로고    scopus 로고
    • P21ras initiates Rac-1 but not phosphatidyl inositol 3 kinase/PKB, mediated signaling pathways in T lymphocytes
    • Genot E, Reif K, Beach S, Kramer I, Cantrell D. p21ras initiates Rac-1 but not phosphatidyl inositol 3 kinase/PKB, mediated signaling pathways in T lymphocytes. Oncogene. 17:1998;1731-1738.
    • (1998) Oncogene , vol.17 , pp. 1731-1738
    • Genot, E.1    Reif, K.2    Beach, S.3    Kramer, I.4    Cantrell, D.5
  • 71
    • 0001139669 scopus 로고    scopus 로고
    • Ras pathways to cell cycle control and cell transformation
    • Malumbres M, Pellicer A. Ras pathways to cell cycle control and cell transformation. Front Biosci. 6:1998;887-912.
    • (1998) Front Biosci , vol.6 , pp. 887-912
    • Malumbres, M.1    Pellicer, A.2
  • 72
    • 0031917171 scopus 로고    scopus 로고
    • Ras-GRF activates Ha-Ras, but not N-Ras o r K-Ras 4B, protein in vivo
    • Jones MK, Jackson JH. Ras-GRF activates Ha-Ras, but not N-Ras o r K-Ras 4B, protein in vivo. J Biol Chem. 273:1998;1782-1787.
    • (1998) J Biol Chem , vol.273 , pp. 1782-1787
    • Jones, M.K.1    Jackson, J.H.2
  • 73
    • 0027491578 scopus 로고
    • Comparison of kinetic properties between tw o mammalian ras p21 GDP/GTP exchange proteins, Ras guanine nucleotide-releasing factor and smg GDP dissociation stimulation
    • Orita S et al. Comparison of kinetic properties between tw o mammalian ras p21 GDP/GTP exchange proteins, Ras guanine nucleotide-releasing factor and smg GDP dissociation stimulation. J Biol Chem. 268:1993;25542-25546.
    • (1993) J Biol Chem , vol.268 , pp. 25542-25546
    • Orita, S.1
  • 75
    • 0025091465 scopus 로고
    • The neurofibromatosis type 1 gene encodes a protein related to GAP
    • Xu G et al. The neurofibromatosis type 1 gene encodes a protein related to GAP. Cell. 62:1990a;599-608.
    • (1990) Cell , vol.62 , pp. 599-608
    • Xu, G.1
  • 76
    • 0028108970 scopus 로고
    • A novel mammalian Ras GTPase-activating protein which has phospholipid-binding and Btk homology regions
    • Maekawa M et al. A novel mammalian Ras GTPase-activating protein which has phospholipid-binding and Btk homology regions. Mol Cell Biol. 14:1994;6879-6885.
    • (1994) Mol Cell Biol , vol.14 , pp. 6879-6885
    • Maekawa, M.1
  • 77
    • 0032055396 scopus 로고    scopus 로고
    • SynGAP: A synaptic RasGAP that associates with the PSD-95/SAP90 protein family
    • Kim JH, Liao D, Lau LF, Huganir RL. SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family. Neuron. 20:1998;683-691.
    • (1998) Neuron , vol.20 , pp. 683-691
    • Kim, J.H.1    Liao, D.2    Lau, L.F.3    Huganir, R.L.4
  • 78
    • 0025729180 scopus 로고
    • Differential regulation of RasGAP and neurofibromatosis gene product activities
    • Bollag G, McCormick F. Differential regulation of RasGAP and neurofibromatosis gene product activities. Nature. 351:1991;576-580.
    • (1991) Nature , vol.351 , pp. 576-580
    • Bollag, G.1    McCormick, F.2
  • 79
    • 0030461098 scopus 로고    scopus 로고
    • Cell cycle-dependent activation of Ras
    • Taylor S, Shalloway D. Cell cycle-dependent activation of Ras. Curr Biol. 6:1996;1621-1627.
    • (1996) Curr Biol , vol.6 , pp. 1621-1627
    • Taylor, S.1    Shalloway, D.2
  • 80
    • 0031055415 scopus 로고    scopus 로고
    • Minimal Ras-binding domain of Raf1can be used as an activation-specific probe for Ras
    • de Rooij J, Bos J. Minimal Ras-binding domain of Raf1can be used as an activation-specific probe for Ras. Oncogene. 14:1997;623-625.
    • (1997) Oncogene , vol.14 , pp. 623-625
    • De, R.J.1    Bos, J.2
  • 81
    • 0029588204 scopus 로고
    • The ksr-1 gene encodes a novel protein kinase involved in Ras-mediated signaling in C. elegans
    • Kornfeld K, Hom DB, Horvitz HR. The ksr-1 gene encodes a novel protein kinase involved in Ras-mediated signaling in C. elegans. Cell. 83:1995;903-913.
    • (1995) Cell , vol.83 , pp. 903-913
    • Kornfeld, K.1    Hom, D.B.2    Horvitz, H.R.3
  • 82
    • 0029559183 scopus 로고
    • The C. elegans KSR-1 gene encodes a novel Raf-related kinase involved in Ras-mediated signal transduction
    • Sundaram M, Han M. The C. elegans KSR-1 gene encodes a novel Raf-related kinase involved in Ras-mediated signal transduction. Cell. 83:1995;889-901.
    • (1995) Cell , vol.83 , pp. 889-901
    • Sundaram, M.1    Han, M.2
  • 83
    • 0029584327 scopus 로고
    • KSR, a novel protein kinase required for RAS signal transduction
    • Therrien M et al. KSR, a novel protein kinase required for RAS signal transduction. Cell. 83:1995;879-888.
    • (1995) Cell , vol.83 , pp. 879-888
    • Therrien, M.1
  • 84
    • 0343742670 scopus 로고    scopus 로고
    • Kinase suppressor of Ras is ceramide-activated protein kinase
    • Zhang Y et al. Kinase suppressor of Ras is ceramide-activated protein kinase. Cell. 89:1997;63-72.
    • (1997) Cell , vol.89 , pp. 63-72
    • Zhang, Y.1
  • 85
    • 0030724987 scopus 로고    scopus 로고
    • KSR stimulates Raf-1 activity in a kinase-independent manner
    • Michaud NR et al. KSR stimulates Raf-1 activity in a kinase-independent manner. Proc Natl Acad Sci USA. 94:1997;12792-12796.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12792-12796
    • Michaud, N.R.1
  • 86
    • 0032571388 scopus 로고    scopus 로고
    • Kinase suppressor of Ras inhibits the activation of extracellular ligand-regulated (ERK) mitogen-activated protein (MAP) kinase by growth factors, activated Ras, and Ras effectors
    • Joneson T et al. Kinase suppressor of Ras inhibits the activation of extracellular ligand-regulated (ERK) mitogen-activated protein (MAP) kinase by growth factors, activated Ras, and Ras effectors. J Biol Chem. 273:1998;7743-7748.
    • (1998) J Biol Chem , vol.273 , pp. 7743-7748
    • Joneson, T.1
  • 87
    • 0031974812 scopus 로고    scopus 로고
    • Regulation of the MAP kinase pathway by mammalian Ksr through direct interaction with MEK and ERK
    • Yu W, Fantl WJ, Harrowe G, Williams LT. Regulation of the MAP kinase pathway by mammalian Ksr through direct interaction with MEK and ERK. Curr Biol. 8:1998;56-64.
    • (1998) Curr Biol , vol.8 , pp. 56-64
    • Yu, W.1    Fantl, W.J.2    Harrowe, G.3    Williams, L.T.4
  • 88
    • 0031974151 scopus 로고    scopus 로고
    • Murine KSR interacts with MEK and inhibits Ras-induced transformation
    • Denouel-Galy A et al. Murine KSR interacts with MEK and inhibits Ras-induced transformation. Curr Biol. 8:1998;46-55.
    • (1998) Curr Biol , vol.8 , pp. 46-55
    • Denouel-Galy, A.1
  • 89
    • 0029850713 scopus 로고    scopus 로고
    • KSR modulates signal propagation within the MAPK cascade
    • Therrien M, Michaud NR, Rubin GM, Morrison DK. KSR modulates signal propagation within the MAPK cascade. Genes Dev. 10:1996;2684-2695.
    • (1996) Genes Dev , vol.10 , pp. 2684-2695
    • Therrien, M.1    Michaud, N.R.2    Rubin, G.M.3    Morrison, D.K.4
  • 90
    • 0032959886 scopus 로고    scopus 로고
    • Identification of constitutive and Ras-inducible phosphorylation sites of KSR: Implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression
    • Cacace AM et al. Identification of constitutive and Ras-inducible phosphorylation sites of KSR: implications for 14-3-3 binding, mitogen-activated protein kinase binding, and KSR overexpression. Mol Cell Biol. 19:1999;229-240.
    • (1999) Mol Cell Biol , vol.19 , pp. 229-240
    • Cacace, A.M.1
  • 91
    • 0032582663 scopus 로고    scopus 로고
    • CNK, a RAF-binding multidomain protein required for RAS signaling
    • Therrien M, Wong AM, Rubin GM. CNK, a RAF-binding multidomain protein required for RAS signaling. Cell. 95:1998;343-353.
    • (1998) Cell , vol.95 , pp. 343-353
    • Therrien, M.1    Wong, A.M.2    Rubin, G.M.3
  • 92
    • 0032504106 scopus 로고    scopus 로고
    • SUR-8, a conserved Ras-binding protein with leucine-rich repeats, positively regulates Ras-mediated signaling in C. elegans
    • Sieburth DS, Sun Q, Han M. SUR-8, a conserved Ras-binding protein with leucine-rich repeats, positively regulates Ras-mediated signaling in C. elegans. Cell. 94:1998;119-130.
    • (1998) Cell , vol.94 , pp. 119-130
    • Sieburth, D.S.1    Sun, Q.2    Han, M.3
  • 93
    • 0032499688 scopus 로고    scopus 로고
    • Soc-2 encodes a leucine-rich repeat protein implicated in fibroblast growth factor receptor signaling
    • Selfors LM, Schutzman JL, Borland CZ, Stern MJ. soc-2 encodes a leucine-rich repeat protein implicated in fibroblast growth factor receptor signaling. Proc Natl Acad Sci USA. 95:1998;6903-6908.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6903-6908
    • Selfors, L.M.1    Schutzman, J.L.2    Borland, C.Z.3    Stern, M.J.4
  • 94
    • 0028206113 scopus 로고
    • Mutations that abolish the ability of Ha-Ras to associate with Raf-1
    • Shirouzu M et al. Mutations that abolish the ability of Ha-Ras to associate with Raf-1. Oncogene. 9:1994;2153-2157.
    • (1994) Oncogene , vol.9 , pp. 2153-2157
    • Shirouzu, M.1
  • 95
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • Kobe B, Deisenhofer J. The leucine-rich repeat: a versatile binding motif. Trends Biochem Sci. 19:1994;415-421.
    • (1994) Trends Biochem Sci , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 96
    • 0026658729 scopus 로고
    • Isolation of rsp-1, a novel cDNA capable of suppressing v-ras
    • Culter M, Bassin R, Zanoni L, Talbot N. Isolation of rsp-1, a novel cDNA capable of suppressing v-ras. Mol Cell Biol. 12:1992;3750-3756.
    • (1992) Mol Cell Biol , vol.12 , pp. 3750-3756
    • Culter, M.1    Bassin, R.2    Zanoni, L.3    Talbot, N.4
  • 97
    • 0033515899 scopus 로고    scopus 로고
    • Characterization of a novel Ras-binding protein Ce-FLI-1 comprising leucine-rich repeats and gelsolin-like domains
    • Goshima M et al. Characterization of a novel Ras-binding protein Ce-FLI-1 comprising leucine-rich repeats and gelsolin-like domains. Biochem Biophys Res Commun. 257:1999;111-116.
    • (1999) Biochem Biophys Res Commun , vol.257 , pp. 111-116
    • Goshima, M.1
  • 98
    • 0032478691 scopus 로고    scopus 로고
    • Identification of the binding partners for flightless I, A novel protein bridging the leucine-rich repeat and the gelsolin superfamilies
    • Liu YT, Yin HL. Identification of the binding partners for flightless I, A novel protein bridging the leucine-rich repeat and the gelsolin superfamilies. J Biol Chem. 273:1998;7920-7927.
    • (1998) J Biol Chem , vol.273 , pp. 7920-7927
    • Liu, Y.T.1    Yin, H.L.2
  • 99
    • 0029813250 scopus 로고    scopus 로고
    • Increased expression of the Ras suppressor Rsu-1 enhances Erk-2 activation and inhibits Jun kinase activation
    • Masuelli L, Cutler ML. Increased expression of the Ras suppressor Rsu-1 enhances Erk-2 activation and inhibits Jun kinase activation. Mol Cell Biol. 16:1996;5466-5476.
    • (1996) Mol Cell Biol , vol.16 , pp. 5466-5476
    • Masuelli, L.1    Cutler, M.L.2
  • 100
    • 0032513127 scopus 로고    scopus 로고
    • Identification of PLC210, a Caenorhabditis elegans phospholipase C, as a putative effector of Ras
    • Shibatohge. Identification of PLC210, a Caenorhabditis elegans phospholipase C, as a putative effector of Ras. J Biol Chem. 273:1998;6218-6222.
    • (1998) J Biol Chem , vol.273 , pp. 6218-6222
    • Shibatohge1
  • 101
    • 0030816045 scopus 로고    scopus 로고
    • Regulation of cone cell formation by Canoe and Ras in the developing Drosophila eye
    • Matsuo T, Takahashi K, Kondo S, Kaibuchi K, Yamamoto D. Regulation of cone cell formation by Canoe and Ras in the developing Drosophila eye. Development. 124:1997;2671-2680.
    • (1997) Development , vol.124 , pp. 2671-2680
    • Matsuo, T.1    Takahashi, K.2    Kondo, S.3    Kaibuchi, K.4    Yamamoto, D.5
  • 102
    • 0032509189 scopus 로고    scopus 로고
    • Identification of Ce-AF-6, a novel Caenorhabditis elegans protein, as a putative Ras effector
    • Watari Y et al. Identification of Ce-AF-6, a novel Caenorhabditis elegans protein, as a putative Ras effector. Gene. 224:1998;53-58.
    • (1998) Gene , vol.224 , pp. 53-58
    • Watari, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.