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Volumn 11, Issue 1, 2013, Pages

Hierarchical scaffolding of an ERK1/2 activation pathway

Author keywords

Actin; Extracellular signal regulated kinase; Mitogen activated kinase; Phorbol ester; Scaffold protein

Indexed keywords

CAVEOLIN 1; IQ MOTIF CONTAINING GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN 1; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN KINASE C; RAF PROTEIN; SMALL INTERFERING RNA; B RAF KINASE; BRAF PROTEIN, RAT; CAV PROTEIN, RAT; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; KSR 1 PROTEIN KINASE; KSR-1 PROTEIN KINASE; PROTEIN KINASE; CAV1 PROTEIN, RAT;

EID: 84883292777     PISSN: None     EISSN: 1478811X     Source Type: Journal    
DOI: 10.1186/1478-811X-11-65     Document Type: Article
Times cited : (32)

References (58)
  • 1
    • 84865342852 scopus 로고    scopus 로고
    • Modularity and functional plasticity of scaffold proteins as p(l)acemakers in cell signaling
    • 10.1016/j.cellsig.2012.06.002 22743133
    • Modularity and functional plasticity of scaffold proteins as p(l)acemakers in cell signaling. Pan CQ, Sudol M, Sheetz M, Low BC, Cell Signal 2012 24 2143 2165 10.1016/j.cellsig.2012.06.002 22743133
    • (2012) Cell Signal , vol.24 , pp. 2143-2165
    • Pan, C.Q.1    Sudol, M.2    Sheetz, M.3    Low, B.C.4
  • 2
    • 0028046412 scopus 로고
    • Protein-Protein Interactions in the yeast pheromone response pathway stesp interacts with all members of the map kinase cascade
    • 7851759
    • Protein-Protein Interactions in the yeast pheromone response pathway stesp interacts with all members of the map kinase cascade. Printen JA, Sprague GF, Genetics 1994 138 609 619 7851759
    • (1994) Genetics , vol.138 , pp. 609-619
    • Printen, J.A.1    Sprague, G.F.2
  • 3
    • 0029850713 scopus 로고    scopus 로고
    • KSR modulates signal propagation within the MAPK cascade
    • 10.1101/gad.10.21.2684 8946910
    • KSR modulates signal propagation within the MAPK cascade. Therrien M, Michaud NR, Rubin GM, Morrison DK, Genes Dev 1996 10 2684 2695 10.1101/gad.10.21.2684 8946910
    • (1996) Genes Dev , vol.10 , pp. 2684-2695
    • Therrien, M.1    Michaud, N.R.2    Rubin, G.M.3    Morrison, D.K.4
  • 4
    • 27644575157 scopus 로고    scopus 로고
    • Coordinating ERK/MAPK signalling through scaffolds and inhibitors
    • 10.1038/nrm1743 16227978
    • Coordinating ERK/MAPK signalling through scaffolds and inhibitors. Kolch W, Nat Rev Mol Cell Biol 2005 6 827 37 10.1038/nrm1743 16227978
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 827-837
    • Kolch, W.1
  • 5
    • 79960039308 scopus 로고    scopus 로고
    • The ERK cascade: Distinct functions within various subcellular organelles
    • 10.1177/1947601911407328 21779493
    • The ERK cascade: distinct functions within various subcellular organelles. Wortzel I, Seger R, Genes Cancer 2011 2 195 209 10.1177/ 1947601911407328 21779493
    • (2011) Genes Cancer , vol.2 , pp. 195-209
    • Wortzel, I.1    Seger, R.2
  • 6
    • 0344845048 scopus 로고    scopus 로고
    • Phosphorylation-dependent paxillin-erk association mediates hepatocyte growth factor-stimulated epithelial morphogenesis
    • 10.1016/S1097-2765(03)00406-4 14636584
    • Phosphorylation-dependent paxillin-erk association mediates hepatocyte growth factor-stimulated epithelial morphogenesis. Ishibe S, Joly D, Zhu X, Cantley LG, Haven N, Mol Cell 2003 12 1275 1285 10.1016/S1097-2765(03)00406-4 14636584
    • (2003) Mol Cell , vol.12 , pp. 1275-1285
    • Ishibe, S.1    Joly, D.2    Zhu, X.3    Cantley, L.G.4    Haven, N.5
  • 7
    • 0031455589 scopus 로고    scopus 로고
    • Caveolin interaction with protein kinase C. Isoenzyme-dependent regulation of kinase activity by the caveolin scaffolding domain peptide
    • 10.1074/jbc.272.52.33416 9407137
    • Caveolin interaction with protein kinase C. Isoenzyme-dependent regulation of kinase activity by the caveolin scaffolding domain peptide. Oka N, Yamamoto M, Schwencke C, Kawabe J, Ebina T, Ohno S, Couet J, Lisanti MP, Ishikawa Y, J Biol Chem 1997 272 33416 33421 10.1074/jbc.272.52.33416 9407137
    • (1997) J Biol Chem , vol.272 , pp. 33416-33421
    • Oka, N.1    Yamamoto, M.2    Schwencke, C.3    Kawabe, J.4    Ebina, T.5    Ohno, S.6    Couet, J.7    Lisanti, M.P.8    Ishikawa, Y.9
  • 8
    • 0029912981 scopus 로고    scopus 로고
    • Co-purification and direct interaction of ras with caveolin, an integral membrane protein of caveolae microdomains
    • 10.1074/jbc.271.16.9690 8621645
    • Co-purification and direct interaction of ras with caveolin, an integral membrane protein of caveolae microdomains. Song KS, Li S, Okamoto T, Quilliam LA, Sargiacomo M, Lisanti MP, J Biol Chem 1996 271 9690 9697 10.1074/jbc.271.16.9690 8621645
    • (1996) J Biol Chem , vol.271 , pp. 9690-9697
    • Song, K.S.1    Li, S.2    Okamoto, T.3    Quilliam, L.A.4    Sargiacomo, M.5    Lisanti, M.P.6
  • 9
    • 15844431258 scopus 로고    scopus 로고
    • Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane
    • 10.1074/jbc.271.20.11930 8662667
    • Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane. Mineo C, James GL, Smart EJ, Anderson RG, J Biol Chem 1996 271 11930 11935 10.1074/jbc.271.20.11930 8662667
    • (1996) J Biol Chem , vol.271 , pp. 11930-11935
    • Mineo, C.1    James, G.L.2    Smart, E.J.3    Anderson, R.G.4
  • 10
    • 0032577647 scopus 로고    scopus 로고
    • Caveolin-mediated regulation of signaling along the p42/44 MAP kinase cascade in vivo. A role for the caveolin-scaffolding domain
    • 10.1016/S0014-5793(98)00470-0 9654135
    • Caveolin-mediated regulation of signaling along the p42/44 MAP kinase cascade in vivo. A role for the caveolin-scaffolding domain. Engelman JA, Chu C, Lin A, Jo H, Ikezu T, Okamoto T, Kohtz DS, Lisanti MP, FEBS Lett 1998 428 205 211 10.1016/S0014-5793(98)00470-0 9654135
    • (1998) FEBS Lett , vol.428 , pp. 205-211
    • Engelman, J.A.1    Chu, C.2    Lin, A.3    Jo, H.4    Ikezu, T.5    Okamoto, T.6    Kohtz, D.S.7    Lisanti, M.P.8
  • 11
    • 84857377693 scopus 로고    scopus 로고
    • Stimulus-specific activation and actin dependency of distinct, spatially separated ERK1/2 fractions in A7r5 smooth muscle cells
    • 10.1371/journal.pone.0030409 22363435
    • Stimulus-specific activation and actin dependency of distinct, spatially separated ERK1/2 fractions in A7r5 smooth muscle cells. Vetterkind S, Saphirstein RJ, Morgan KG, PLoS one 2012 7 30409 10.1371/journal.pone.0030409 22363435
    • (2012) PLoS One , vol.7 , pp. 530409
    • Vetterkind, S.1    Saphirstein, R.J.2    Morgan, K.G.3
  • 13
    • 0032538790 scopus 로고    scopus 로고
    • Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade
    • 10.1093/emboj/17.22.6633 9822607
    • Targeted downregulation of caveolin-1 is sufficient to drive cell transformation and hyperactivate the p42/44 MAP kinase cascade. Galbiati F, Volonte D, Engelman JA, Watanabe G, Burk R, Pestell RG, Lisanti MP, EMBO J 1998 17 6633 48 10.1093/emboj/17.22.6633 9822607
    • (1998) EMBO J , vol.17 , pp. 6633-6648
    • Galbiati, F.1    Volonte, D.2    Engelman, J.A.3    Watanabe, G.4    Burk, R.5    Pestell, R.G.6    Lisanti, M.P.7
  • 14
    • 0033571710 scopus 로고    scopus 로고
    • Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins
    • 10548541
    • Extracellular regulated kinase (ERK) interaction with actin and the calponin homology (CH) domain of actin-binding proteins. Leinweber BD, Leavis PC, Grabarek Z, Wang CL, Morgan KG, Biochem J 1999 344 Pt 1 117 123 10548541
    • (1999) Biochem J , vol.344 , Issue.PART 1 , pp. 117-123
    • Leinweber, B.D.1    Leavis, P.C.2    Grabarek, Z.3    Wang, C.L.4    Morgan, K.G.5
  • 15
    • 19344362697 scopus 로고    scopus 로고
    • Podosome-mediated matrix resorption and cell motility in vascular smooth muscle cells
    • 10.1152/ajpheart.01002.2004 15695563
    • Podosome-mediated matrix resorption and cell motility in vascular smooth muscle cells. Burgstaller G, Gimona M, Am J Physiol-Heart Circ Physiol 2005 288 3001 H3005 10.1152/ajpheart.01002.2004 15695563
    • (2005) Am J Physiol - Heart Circ Physiol , vol.288
    • Burgstaller, G.1    Gimona, M.2
  • 16
    • 67650488974 scopus 로고    scopus 로고
    • Signaling dynamics of the KSR1 scaffold complex
    • 10.1073/pnas.0901590106 19541618
    • Signaling dynamics of the KSR1 scaffold complex. McKay MM, Ritt D, Morrison DK, Proc Natl Acad Sci USA 2009 106 11022 7 10.1073/pnas.0901590106 19541618
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 11022-11027
    • McKay, M.M.1    Ritt, D.2    Morrison, D.K.3
  • 17
    • 40549129346 scopus 로고    scopus 로고
    • A dual role for IQGAP1 in regulating exocytosis
    • 18216334
    • A dual role for IQGAP1 in regulating exocytosis. Rittmeyer EN, Daniel S, Hsu S-C, Osman M, J Cell Sci 2008 121 Pt 3 391 403 18216334
    • (2008) J Cell Sci , vol.121 , Issue.PART 3 , pp. 391-403
    • Rittmeyer, E.N.1    Daniel, S.2    Hsu, S.-C.3    Osman, M.4
  • 18
    • 0037423218 scopus 로고    scopus 로고
    • Elucidation of the interaction of calmodulin with the IQ motifs of IQGAP1
    • 10.1074/jbc.M208579200 12446675
    • Elucidation of the interaction of calmodulin with the IQ motifs of IQGAP1. Li Z, Sacks DB, J Biol Chem 2003 278 4347 52 10.1074/jbc.M208579200 12446675
    • (2003) J Biol Chem , vol.278 , pp. 4347-4352
    • Li, Z.1    Sacks, D.B.2
  • 19
    • 24344491858 scopus 로고    scopus 로고
    • IQGAP1 is a scaffold for mitogen-activated protein kinase signaling
    • 10.1128/MCB.25.18.7940-7952.2005 16135787
    • IQGAP1 is a scaffold for mitogen-activated protein kinase signaling. Roy M, Li Z, Sacks DB, Mol Cell Biol 2005 25 7940 7952 10.1128/MCB.25.18.7940-7952. 2005 16135787
    • (2005) Mol Cell Biol , vol.25 , pp. 7940-7952
    • Roy, M.1    Li, Z.2    Sacks, D.B.3
  • 20
    • 53149154520 scopus 로고    scopus 로고
    • IQGAP1 integrates Ca2+/calmodulin and B-Raf signaling
    • 10.1074/jbc.M804626200 18567582
    • IQGAP1 integrates Ca2+/calmodulin and B-Raf signaling. Ren J-G, Li Z, Sacks DB, J Biol Chem 2008 283 22972 82 10.1074/jbc.M804626200 18567582
    • (2008) J Biol Chem , vol.283 , pp. 22972-22982
    • Ren, J.-G.1    Li, Z.2    Sacks, D.B.3
  • 22
    • 0032879692 scopus 로고    scopus 로고
    • Melusin Is a New Muscle-specific Interactor for beta 1 Integrin Cytoplasmic Domain
    • 10.1074/jbc.274.41.29282 10506186
    • Melusin Is a New Muscle-specific Interactor for beta 1 Integrin Cytoplasmic Domain. Brancaccio M, J Biol Chem 1999 274 29282 29288 10.1074/jbc.274.41.29282 10506186
    • (1999) J Biol Chem , vol.274 , pp. 29282-29288
    • Brancaccio, M.1
  • 24
    • 79952111024 scopus 로고    scopus 로고
    • Kinase suppressor of Ras 1 is required for full ERK activation in thymocytes but not for thymocyte selection
    • 10.1002/eji.201040349 20865788
    • Kinase suppressor of Ras 1 is required for full ERK activation in thymocytes but not for thymocyte selection. Filbert EL, Nguyen A, Markiewicz MA, Fowlkes BJ, Huang YH, Shaw AS, Eur J Immunol 2010 40 3226 3234 10.1002/eji.201040349 20865788
    • (2010) Eur J Immunol , vol.40 , pp. 3226-3234
    • Filbert, E.L.1    Nguyen, A.2    Markiewicz, M.A.3    Fowlkes, B.J.4    Huang, Y.H.5    Shaw, A.S.6
  • 25
    • 33646848241 scopus 로고    scopus 로고
    • Kinase suppressor of Ras1 compartmentalizes hippocampal signal transduction and subserves synaptic plasticity and memory formation
    • 10.1016/j.neuron.2006.04.029 16731514
    • Kinase suppressor of Ras1 compartmentalizes hippocampal signal transduction and subserves synaptic plasticity and memory formation. Shalin SC, Hernandez CM, Dougherty MK, Morrison DK, Sweatt JD, Neuron 2006 50 765 779 10.1016/j.neuron.2006.04.029 16731514
    • (2006) Neuron , vol.50 , pp. 765-779
    • Shalin, S.C.1    Hernandez, C.M.2    Dougherty, M.K.3    Morrison, D.K.4    Sweatt, J.D.5
  • 26
    • 0034009390 scopus 로고    scopus 로고
    • Signal transduction: Hanging on a scaffold
    • 10.1016/S0955-0674(99)00078-2 10712921
    • Signal transduction: hanging on a scaffold. Burack WR, Shaw a S, Curr Opin Cell Biol 2000 12 211 216 10.1016/S0955-0674(99)00078-2 10712921
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 211-216
    • Burack, W.R.1    Shaw, A.S.2
  • 27
    • 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
    • 10.1074/jbc.273.13.7743 9516483
    • 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, J Biol Chem 1998 273 7743 7748 10.1074/jbc.273.13.7743 9516483
    • (1998) J Biol Chem , vol.273 , pp. 7743-7748
    • Joneson, T.1
  • 28
    • 84867146993 scopus 로고    scopus 로고
    • Pravastatin normalizes ET-1-induced contraction in the aorta of type 2 diabetic OLETF rats by suppressing the KSR1/ERK complex
    • 10.1152/ajpheart.01128.2011 22886408
    • Pravastatin normalizes ET-1-induced contraction in the aorta of type 2 diabetic OLETF rats by suppressing the KSR1/ERK complex. Nemoto S, Taguchi K, Matsumoto T, Kamata K, Kobayashi T, Am J Physiol-Heart Circ Physiol 2012 303 893 902 10.1152/ajpheart.01128.2011 22886408
    • (2012) Am J Physiol - Heart Circ Physiol , vol.303 , pp. 8893-8902
    • Nemoto, S.1    Taguchi, K.2    Matsumoto, T.3    Kamata, K.4    Kobayashi, T.5
  • 29
    • 0030929148 scopus 로고    scopus 로고
    • IQGAP1, a Rac- and Cdc42-binding protein, directly binds and cross-links microfilaments
    • 10.1083/jcb.137.7.1555 9199170
    • IQGAP1, a Rac- and Cdc42-binding protein, directly binds and cross-links microfilaments. Bashour a M, Fullerton a T, Hart MJ, Bloom GS, J Cell Biol 1997 137 1555 1566 10.1083/jcb.137.7.1555 9199170
    • (1997) J Cell Biol , vol.137 , pp. 1555-1566
    • Bashour, A.M.1    Fullerton, A.T.2    Hart, M.J.3    Bloom, G.S.4
  • 31
    • 79251602272 scopus 로고    scopus 로고
    • Scaffolding proteins and non-proliferative functions of ERK1/2
    • 10.4161/cib.3.4.11832 20798825
    • Scaffolding proteins and non-proliferative functions of ERK1/2. Appel S, Morgan KG, Commun Integr Biol 2010 3 354 356 10.4161/cib.3.4.11832 20798825
    • (2010) Commun Integr Biol , vol.3 , pp. 354-356
    • Appel, S.1    Morgan, K.G.2
  • 32
    • 65949095208 scopus 로고    scopus 로고
    • ERK dimers and scaffold proteins: Unexpected partners for a forgotton (cytoplasmic) task
    • 10.4161/cc.8.7.8078 19279408
    • ERK dimers and scaffold proteins: unexpected partners for a forgotton (cytoplasmic) task. Casar B, Crespo P, Cell Cycle 2009 8 1007 1013 10.4161/cc.8.7.8078 19279408
    • (2009) Cell Cycle , vol.8 , pp. 1007-1013
    • Casar, B.1    Crespo, P.2
  • 33
    • 0030825396 scopus 로고    scopus 로고
    • Mechanisms of inhibition by heparin of PDGF stimulated MAP kinase activation in vascular smooth muscle cells
    • 10.1002/(SICI)1097-4652(199707)172:1<69: AID-JCP8>3.0.CO;2-B 9207927
    • Mechanisms of inhibition by heparin of PDGF stimulated MAP kinase activation in vascular smooth muscle cells. Pukac L, Carter JE, Ottlinger ME, Karnovsky MJ, J Cell Physiol 1997 172 69 78 10.1002/(SICI)1097-4652(199707)172: 1<69::AID-JCP8>3.0.CO;2-B 9207927
    • (1997) J Cell Physiol , vol.172 , pp. 69-78
    • Pukac, L.1    Carter, J.E.2    Ottlinger, M.E.3    Karnovsky, M.J.4
  • 35
    • 1842482350 scopus 로고    scopus 로고
    • Regulation of phorbol ester-mediated TRAF1 induction in human colon cancer cells through a PKC/RAF/ERK/NF-kappaB-dependent pathway
    • 10.1038/sj.onc.1207312 14981539
    • Regulation of phorbol ester-mediated TRAF1 induction in human colon cancer cells through a PKC/RAF/ERK/NF-kappaB-dependent pathway. Wang X, Wang Q, Hu W, Evers BM, Oncogene 2004 23 1885 1895 10.1038/sj.onc.1207312 14981539
    • (2004) Oncogene , vol.23 , pp. 1885-1895
    • Wang, X.1    Wang, Q.2    Hu, W.3    Evers, B.M.4
  • 36
    • 0032511882 scopus 로고    scopus 로고
    • The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338
    • 10.1038/24184 9823899
    • The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338. King AJ, Sun H, Diaz B, Barnard D, Miao W, Bagrodia SMM, Nature 1998 396 180 183 10.1038/24184 9823899
    • (1998) Nature , vol.396 , pp. 180-183
    • King, A.J.1    Sun, H.2    Diaz, B.3    Barnard, D.4    Miao, W.5    Bagrodia, S.M.M.6
  • 37
    • 34547548629 scopus 로고    scopus 로고
    • IQGAP1 modulates activation of B-Raf
    • 10.1073/pnas.0611308104 17563371
    • IQGAP1 modulates activation of B-Raf. Ren J-G, Li Z, Sacks DB, Proc Natl Acad Sci U S A 2007 104 10465 10469 10.1073/pnas.0611308104 17563371
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 10465-10469
    • Ren, J.-G.1    Li, Z.2    Sacks, D.B.3
  • 38
    • 0032436774 scopus 로고    scopus 로고
    • Isolated endosomes from quiescent rat liver contain the signal transduction machinery: Differential distribution of activated Raf-1 and Mek in the endocytic compartment
    • 10.1016/S0014-5793(98)01517-8 9877160
    • Isolated endosomes from quiescent rat liver contain the signal transduction machinery: differential distribution of activated Raf-1 and Mek in the endocytic compartment. Pol a, Calvo M, Enrich C, FEBS Lett 1998 441 34 38 10.1016/S0014-5793(98)01517-8 9877160
    • (1998) FEBS Lett , vol.441 , pp. 34-38
    • Pol, A.1    Calvo, M.2    Enrich, C.3
  • 40
    • 78649322633 scopus 로고    scopus 로고
    • Partner exchange: Protein-protein interactions in the Raf pathway
    • 10.1016/j.tibs.2010.06.001 20621483
    • Partner exchange: protein-protein interactions in the Raf pathway. Wimmer R, Baccarini M, Trends Biochem Sci 2010 35 660 668 10.1016/j.tibs.2010.06.001 20621483
    • (2010) Trends Biochem Sci , vol.35 , pp. 660-668
    • Wimmer, R.1    Baccarini, M.2
  • 42
    • 84874225181 scopus 로고    scopus 로고
    • Effects of Raf dimerization and its inhibition on normal and disease-associated Raf signaling
    • 10.1016/j.molcel.2012.12.018 23352452
    • Effects of Raf dimerization and its inhibition on normal and disease-associated Raf signaling. Freeman AK, Ritt D, Morrison DK, Mol Cell 2013 49 751 758 10.1016/j.molcel.2012.12.018 23352452
    • (2013) Mol Cell , vol.49 , pp. 751-758
    • Freeman, A.K.1    Ritt, D.2    Morrison, D.K.3
  • 43
    • 29144462587 scopus 로고    scopus 로고
    • Wild-type and mutant B-RAF activate C-RAF through distinct mechanisms involving heterodimerization
    • 10.1016/j.molcel.2005.10.022 16364920
    • Wild-type and mutant B-RAF activate C-RAF through distinct mechanisms involving heterodimerization. Garnett MJ, Rana S, Paterson H, Barford D, Marais R, Mol Cell 2005 20 963 969 10.1016/j.molcel.2005.10.022 16364920
    • (2005) Mol Cell , vol.20 , pp. 963-969
    • Garnett, M.J.1    Rana, S.2    Paterson, H.3    Barford, D.4    Marais, R.5
  • 44
    • 75149117479 scopus 로고    scopus 로고
    • Impact of feedback phosphorylation and Raf heterodimerization on normal and mutant B-Raf signaling
    • 10.1128/MCB.00569-09 19933846
    • Impact of feedback phosphorylation and Raf heterodimerization on normal and mutant B-Raf signaling. Ritt D, Monson DM, Specht SI, Morrison DK, Mol Cell Biol 2010 30 806 819 10.1128/MCB.00569-09 19933846
    • (2010) Mol Cell Biol , vol.30 , pp. 806-819
    • Ritt, D.1    Monson, D.M.2    Specht, S.I.3    Morrison, D.K.4
  • 45
    • 0035328521 scopus 로고    scopus 로고
    • Active Ras induces heterodimerization of cRaf and BRaf
    • 11325826
    • Active Ras induces heterodimerization of cRaf and BRaf. Weber CK, Slupsky JR, Kalmes H, Rapp UR, Cancer Res 2001 61 3595 3598 11325826
    • (2001) Cancer Res , vol.61 , pp. 3595-3598
    • Weber, C.K.1    Slupsky, J.R.2    Kalmes, H.3    Rapp, U.R.4
  • 46
    • 33644786244 scopus 로고    scopus 로고
    • Regulation and Role of Raf-1 / B-Raf Heterodimerization
    • 10.1128/MCB.26.6.2262-2272.2006 16508002
    • Regulation and Role of Raf-1 / B-Raf Heterodimerization. Rushworth LK, Hindley AD, Neill EO, Kolch W, Mol Cell Biol 2006 26 2262 2272 10.1128/MCB.26.6.2262-2272.2006 16508002
    • (2006) Mol Cell Biol , vol.26 , pp. 2262-2272
    • Rushworth, L.K.1    Hindley, A.D.2    Neill, E.O.3    Kolch, W.4
  • 47
    • 0347363834 scopus 로고    scopus 로고
    • Identification of novel ERK-mediated feedback phosphorylation sites at the C-terminus of B-Raf
    • 10.1038/sj.onc.1207185 14654779
    • Identification of novel ERK-mediated feedback phosphorylation sites at the C-terminus of B-Raf. Brummer T, Naegele H, Reth M, Misawa Y, Oncogene 2003 22 8823 8834 10.1038/sj.onc.1207185 14654779
    • (2003) Oncogene , vol.22 , pp. 8823-8834
    • Brummer, T.1    Naegele, H.2    Reth, M.3    Misawa, Y.4
  • 48
    • 34248591612 scopus 로고    scopus 로고
    • Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer
    • 10.1038/sj.onc.1210422 17496923
    • Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer. Roberts PJ, Der CJ, Oncogene 2007 26 3291 310 10.1038/sj.onc.1210422 17496923
    • (2007) Oncogene , vol.26 , pp. 3291-3310
    • Roberts, P.J.1    Der, C.J.2
  • 49
    • 0037805547 scopus 로고    scopus 로고
    • RAS oncogenes: The first 30 years
    • 10.1038/nrc1097 12778136
    • RAS oncogenes: the first 30 years. Malumbres M, Barbacid M, Nat Rev Cancer 2003 3 459 465 10.1038/nrc1097 12778136
    • (2003) Nat Rev Cancer , vol.3 , pp. 459-465
    • Malumbres, M.1    Barbacid, M.2
  • 51
    • 33749524271 scopus 로고    scopus 로고
    • Dimethyl sulfoxide inhibits tissue factor expression, thrombus formation, and vascular smooth muscle cell activation: A potential treatment strategy for drug-eluting stents
    • 10.1161/CIRCULATIONAHA.106.638460 17000906
    • Dimethyl sulfoxide inhibits tissue factor expression, thrombus formation, and vascular smooth muscle cell activation: a potential treatment strategy for drug-eluting stents. Camici GG, Steffel J, Akhmedov A, Schafer N, Baldinger J, Schulz U, Shojaati K, Matter CM, Yang Z, Lüscher TF, Tanner FC, Circulation 2006 114 1512 1521 10.1161/CIRCULATIONAHA.106.638460 17000906
    • (2006) Circulation , vol.114 , pp. 1512-1521
    • Camici, G.G.1    Steffel, J.2    Akhmedov, A.3    Schafer, N.4    Baldinger, J.5    Schulz, U.6    Shojaati, K.7    Matter, C.M.8    Yang, Z.9    Lüscher, T.F.10    Tanner, F.C.11
  • 52
    • 49149099329 scopus 로고    scopus 로고
    • BMI-1026 treatment can induce SAHF formation by activation of Erk1/2
    • 10.5483/BMBRep.2008.41.7.523 18682036
    • BMI-1026 treatment can induce SAHF formation by activation of Erk1/2. Seo H-J, Park HJ, Choi HS, Hwang S-Y, Park J-S, Seong Y-S, BMB Rep 2008 41 523 528 10.5483/BMBRep.2008.41.7.523 18682036
    • (2008) BMB Rep , vol.41 , pp. 523-528
    • Seo, H.-J.1    Park, H.J.2    Choi, H.S.3    Hwang, S.-Y.4    Park, J.-S.5    Seong, Y.-S.6
  • 54
    • 0017104962 scopus 로고
    • Characterization of two putative smooth muscle cell lines from rat thoracic aorta
    • 10.1016/0014-4827(76)90446-8 943301
    • Characterization of two putative smooth muscle cell lines from rat thoracic aorta. Kimes BW, Brandt BL, Exp Cell Res 1976 98 349 366 10.1016/0014-4827(76)90446-8 943301
    • (1976) Exp Cell Res , vol.98 , pp. 349-366
    • Kimes, B.W.1    Brandt, B.L.2


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