메뉴 건너뛰기




Volumn 33, Issue , 2013, Pages 1-14

The ras superfamily g-proteins

Author keywords

Arf; Crystal structure; Effectors; G motifs; GAP; GEF; Membrane association; NMR structure; Posttranslational modification; Rab; Ran; Ras; Ras superfamily G proteins; Rho

Indexed keywords

RAS PROTEIN;

EID: 84881489098     PISSN: 18746047     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-416749-0.00001-4     Document Type: Chapter
Times cited : (15)

References (53)
  • 2
    • 0026669471 scopus 로고
    • Differentiation factors, including nerve growth-factor, fibroblast growth-factor, and interleukin-6, induce an accumulation of an active ras. Gtp complex in rat pheochromocytoma PC12 cells
    • Nakafuku M., Satoh T., Kaziro Y. Differentiation factors, including nerve growth-factor, fibroblast growth-factor, and interleukin-6, induce an accumulation of an active ras. Gtp complex in rat pheochromocytoma PC12 cells. J. Biol. Chem. 1992, 267:19448-19454.
    • (1992) J. Biol. Chem. , vol.267 , pp. 19448-19454
    • Nakafuku, M.1    Satoh, T.2    Kaziro, Y.3
  • 3
    • 0026581423 scopus 로고
    • Nerve growth factor induces rapid accumulation of the GTP-bound form of p21ras in rat pheochromocytoma PC12 cells
    • Muroya K., Hattori S., Nakamura S. Nerve growth factor induces rapid accumulation of the GTP-bound form of p21ras in rat pheochromocytoma PC12 cells. Oncogene 1992, 7:277-281.
    • (1992) Oncogene , vol.7 , pp. 277-281
    • Muroya, K.1    Hattori, S.2    Nakamura, S.3
  • 4
    • 3142546236 scopus 로고    scopus 로고
    • The Rheb family of GTP-binding proteins
    • Aspuria P.J., Tamanoi F. The Rheb family of GTP-binding proteins. Cell. Signal. 2004, 16:1105-1112.
    • (2004) Cell. Signal. , vol.16 , pp. 1105-1112
    • Aspuria, P.J.1    Tamanoi, F.2
  • 5
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: new insights into their functions from in vivo studies
    • Heasman S.J., Ridley A.J. Mammalian Rho GTPases: new insights into their functions from in vivo studies. Nat. Rev. Mol. Cell Biol. 2008, 9:690-701.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 6
    • 59949090255 scopus 로고    scopus 로고
    • Wnt signaling pathways meet Rho GTPases
    • Schlessinger K., Hall A., Tolwinski N. Wnt signaling pathways meet Rho GTPases. Genes Dev. 2009, 23:265-277.
    • (2009) Genes Dev. , vol.23 , pp. 265-277
    • Schlessinger, K.1    Hall, A.2    Tolwinski, N.3
  • 8
    • 0028929866 scopus 로고
    • Crystal-structure of the nuclear Ras-related protein Ran in its Gdp-bound form
    • Scheffzek K., Klebe C., Fritzwolf K., Kabsch W., Wittinghofer A. Crystal-structure of the nuclear Ras-related protein Ran in its Gdp-bound form. Nature 1995, 374:378-381.
    • (1995) Nature , vol.374 , pp. 378-381
    • Scheffzek, K.1    Klebe, C.2    Fritzwolf, K.3    Kabsch, W.4    Wittinghofer, A.5
  • 9
    • 0345482977 scopus 로고
    • GTP-binding domain: three consensus sequence elements with distinct spacing
    • Dever T.E., Glynias M.J., Merrick W.C. GTP-binding domain: three consensus sequence elements with distinct spacing. Proc. Natl. Acad. Sci. U.S.A. 1987, 84:1814-1818.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 1814-1818
    • Dever, T.E.1    Glynias, M.J.2    Merrick, W.C.3
  • 10
    • 0029790535 scopus 로고    scopus 로고
    • C-terminal motifs found in Ras-superfamily G-proteins: CAAX and C-seven motifs
    • Del Villar K., Dorin D., Sattler I., Urano J., Poullet P., et al. C-terminal motifs found in Ras-superfamily G-proteins: CAAX and C-seven motifs. Biochem. Soc. Trans. 1996, 24:709-713.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 709-713
    • Del Villar, K.1    Dorin, D.2    Sattler, I.3    Urano, J.4    Poullet, P.5
  • 11
    • 0026026818 scopus 로고
    • The GTPase superfamily: conserved structure and molecular mechanism
    • Bourne H.R., Sanders D.A., McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature 1991, 349:117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 12
    • 0025310575 scopus 로고
    • Refined crystal-structure of the triphosphate conformation of H-Ras P21 at 1.35 a resolution-implications for the mechanism of Gtp hydrolysis
    • Pai E.F., Krengel U., Petsko G.A., Goody R.S., Kabsch W., et al. Refined crystal-structure of the triphosphate conformation of H-Ras P21 at 1.35 a resolution-implications for the mechanism of Gtp hydrolysis. EMBO J. 1990, 9:2351-2359.
    • (1990) EMBO J. , vol.9 , pp. 2351-2359
    • Pai, E.F.1    Krengel, U.2    Petsko, G.A.3    Goody, R.S.4    Kabsch, W.5
  • 13
    • 0031226057 scopus 로고    scopus 로고
    • Crystal structure of RhoA-GDP and its functional implications
    • Wei Y., Zhang Y., Derewenda U., Liu X., Minor W., et al. Crystal structure of RhoA-GDP and its functional implications. Nat. Struct. Biol. 1997, 4:699-703.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 699-703
    • Wei, Y.1    Zhang, Y.2    Derewenda, U.3    Liu, X.4    Minor, W.5
  • 14
    • 0030759770 scopus 로고    scopus 로고
    • Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP
    • Rittinger K., Walker P.A., Eccleston J.F., Nurmahomed K., Owen D., et al. Crystal structure of a small G protein in complex with the GTPase-activating protein rhoGAP. Nature 1997, 388:693-697.
    • (1997) Nature , vol.388 , pp. 693-697
    • Rittinger, K.1    Walker, P.A.2    Eccleston, J.F.3    Nurmahomed, K.4    Owen, D.5
  • 15
    • 77949498580 scopus 로고    scopus 로고
    • Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA
    • Zhu Y., Hu L., Zhou Y., Yao Q., Liu L., et al. Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:4699-4704.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 4699-4704
    • Zhu, Y.1    Hu, L.2    Zhou, Y.3    Yao, Q.4    Liu, L.5
  • 16
    • 0029113233 scopus 로고
    • The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms
    • Greasley S.E., Jhoti H., Teahan C., Solari R., Fensome A., et al. The structure of rat ADP-ribosylation factor-1 (ARF-1) complexed to GDP determined from two different crystal forms. Nat. Struct. Biol. 1995, 2:797-806.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 797-806
    • Greasley, S.E.1    Jhoti, H.2    Teahan, C.3    Solari, R.4    Fensome, A.5
  • 17
    • 0032478537 scopus 로고    scopus 로고
    • Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran
    • Stewart M., Kent H.M., McCoy A.J. Structural basis for molecular recognition between nuclear transport factor 2 (NTF2) and the GDP-bound form of the Ras-family GTPase Ran. J. Mol. Biol. 1998, 277:635-646.
    • (1998) J. Mol. Biol. , vol.277 , pp. 635-646
    • Stewart, M.1    Kent, H.M.2    McCoy, A.J.3
  • 18
    • 20444442724 scopus 로고    scopus 로고
    • Structural basis for the unique biological function of small GTPase RHEB
    • Yu Y., Li S., Xu X., Li Y., Guan K., et al. Structural basis for the unique biological function of small GTPase RHEB. J. Biol. Chem. 2005, 280:17093-17100.
    • (2005) J. Biol. Chem. , vol.280 , pp. 17093-17100
    • Yu, Y.1    Li, S.2    Xu, X.3    Li, Y.4    Guan, K.5
  • 19
    • 33746178724 scopus 로고    scopus 로고
    • Crystal structure of human Rad GTPase of the RGK-family
    • Yanuar A., Sakurai S., Kitano K., Hakoshima T. Crystal structure of human Rad GTPase of the RGK-family. Genes Cells 2006, 11:961-968.
    • (2006) Genes Cells , vol.11 , pp. 961-968
    • Yanuar, A.1    Sakurai, S.2    Kitano, K.3    Hakoshima, T.4
  • 20
    • 0029107760 scopus 로고
    • The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
    • Nassar N., Horn G., Herrmann C., Scherer A., McCormick F., et al. The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature 1995, 375:554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5
  • 21
    • 0035756318 scopus 로고    scopus 로고
    • Structure of small G proteins and their regulators
    • Paduch M., Jelen F., Otlewski J. Structure of small G proteins and their regulators. Acta Biochim. Pol. 2001, 48:829-850.
    • (2001) Acta Biochim. Pol. , vol.48 , pp. 829-850
    • Paduch, M.1    Jelen, F.2    Otlewski, J.3
  • 22
    • 6344234904 scopus 로고    scopus 로고
    • NMR characterization of full-length farnesylated and non-farnesylated H-Ras and its implications for Raf activation
    • Thapar R., Williams J.G., Campbell S.L. NMR characterization of full-length farnesylated and non-farnesylated H-Ras and its implications for Raf activation. J. Mol. Biol. 2004, 343:1391-1408.
    • (2004) J. Mol. Biol. , vol.343 , pp. 1391-1408
    • Thapar, R.1    Williams, J.G.2    Campbell, S.L.3
  • 23
    • 84875233112 scopus 로고    scopus 로고
    • NMR-based functional profiling of RASopathies and oncogenic RAS mutations
    • Smith M.J., Neel B.G., Ikura M. NMR-based functional profiling of RASopathies and oncogenic RAS mutations. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:4574-4579.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 4574-4579
    • Smith, M.J.1    Neel, B.G.2    Ikura, M.3
  • 24
    • 64349107039 scopus 로고    scopus 로고
    • Solution structure and dynamics of the small GTPase RalB in its active conformation: significance for effector protein binding
    • Fenwick R.B., Prasannan S., Campbell L.J., Nietlispach D., Evetts K.A., et al. Solution structure and dynamics of the small GTPase RalB in its active conformation: significance for effector protein binding. Biochemistry 2009, 48:2192-2206.
    • (2009) Biochemistry , vol.48 , pp. 2192-2206
    • Fenwick, R.B.1    Prasannan, S.2    Campbell, L.J.3    Nietlispach, D.4    Evetts, K.A.5
  • 25
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: critical elements in the control of small G proteins
    • Bos J.L., Rehmann H., Wittinghofer A. GEFs and GAPs: critical elements in the control of small G proteins. Cell 2007, 129:865-877.
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 26
    • 41949114173 scopus 로고    scopus 로고
    • The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues
    • Scrima A., Thomas C., Deaconescu D., Wittinghofer A. The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues. EMBO J. 2008, 27:1145-1153.
    • (2008) EMBO J. , vol.27 , pp. 1145-1153
    • Scrima, A.1    Thomas, C.2    Deaconescu, D.3    Wittinghofer, A.4
  • 27
    • 33746356908 scopus 로고    scopus 로고
    • TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism
    • Pan X., Eathiraj S., Munson M., Lambright D.G. TBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism. Nature 2006, 442:303-306.
    • (2006) Nature , vol.442 , pp. 303-306
    • Pan, X.1    Eathiraj, S.2    Munson, M.3    Lambright, D.G.4
  • 28
    • 0037033983 scopus 로고    scopus 로고
    • RanGAP mediates GTP hydrolysis without an arginine finger
    • Seewald M.J., Korner C., Wittinghofer A., Vetter I.R. RanGAP mediates GTP hydrolysis without an arginine finger. Nature 2002, 415:662-666.
    • (2002) Nature , vol.415 , pp. 662-666
    • Seewald, M.J.1    Korner, C.2    Wittinghofer, A.3    Vetter, I.R.4
  • 29
    • 7044226349 scopus 로고    scopus 로고
    • Structural analysis of autoinhibition in the Ras activator Son of sevenless
    • Sondermann H., Soisson S.M., Boykevisch S., Yang S.S., Bar-Sagi D., et al. Structural analysis of autoinhibition in the Ras activator Son of sevenless. Cell 2004, 119:393-405.
    • (2004) Cell , vol.119 , pp. 393-405
    • Sondermann, H.1    Soisson, S.M.2    Boykevisch, S.3    Yang, S.S.4    Bar-Sagi, D.5
  • 30
    • 70249105718 scopus 로고    scopus 로고
    • Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor
    • Yang J., Zhang Z., Roe S.M., Marshall C.J., Barford D. Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor. Science 2009, 325:1398-1402.
    • (2009) Science , vol.325 , pp. 1398-1402
    • Yang, J.1    Zhang, Z.2    Roe, S.M.3    Marshall, C.J.4    Barford, D.5
  • 31
    • 0032538316 scopus 로고    scopus 로고
    • Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein
    • Soisson S.M., Nimnual A.S., Uy M., Bar-Sagi D., Kuriyan J. Crystal structure of the Dbl and pleckstrin homology domains from the human Son of sevenless protein. Cell 1998, 95:259-268.
    • (1998) Cell , vol.95 , pp. 259-268
    • Soisson, S.M.1    Nimnual, A.S.2    Uy, M.3    Bar-Sagi, D.4    Kuriyan, J.5
  • 32
    • 0031023505 scopus 로고    scopus 로고
    • Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI
    • DiracSvejstrup A.B., Sumizawa T., Pfeffer S.R. Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI. EMBO J. 1997, 16:465-472.
    • (1997) EMBO J. , vol.16 , pp. 465-472
    • DiracSvejstrup, A.B.1    Sumizawa, T.2    Pfeffer, S.R.3
  • 33
    • 0027418539 scopus 로고
    • Rab GDI: a solubilizing and recycling factor for rab9 protein
    • Soldati T., Riederer M.A., Pfeffer S.R. Rab GDI: a solubilizing and recycling factor for rab9 protein. Mol. Biol. Cell 1993, 4:425-434.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 425-434
    • Soldati, T.1    Riederer, M.A.2    Pfeffer, S.R.3
  • 35
    • 33748767111 scopus 로고    scopus 로고
    • Therapeutic intervention based on protein prenylation and associated modifications
    • Gelb M.H., Brunsveld L., Hrycyna C.A., Michaelis S., Tamanoi F., et al. Therapeutic intervention based on protein prenylation and associated modifications. Nat. Chem. Biol. 2006, 2:518-528.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 518-528
    • Gelb, M.H.1    Brunsveld, L.2    Hrycyna, C.A.3    Michaelis, S.4    Tamanoi, F.5
  • 36
    • 0035825193 scopus 로고    scopus 로고
    • Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding
    • Michaelson D., Silletti J., Murphy G., D'Eustachio P., Rush M., et al. Differential localization of Rho GTPases in live cells: regulation by hypervariable regions and RhoGDI binding. J. Cell Biol. 2001, 152:111-126.
    • (2001) J. Cell Biol. , vol.152 , pp. 111-126
    • Michaelson, D.1    Silletti, J.2    Murphy, G.3    D'Eustachio, P.4    Rush, M.5
  • 37
    • 34347369084 scopus 로고    scopus 로고
    • Post-translational modifications and regulation of the RAS superfamily of GTPases as anticancer targets
    • Konstantinopoulos P.A., Karamouzis M.V., Papavassiliou A.G. Post-translational modifications and regulation of the RAS superfamily of GTPases as anticancer targets. Nat. Rev. Drug Discov. 2007, 6:540-555.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 540-555
    • Konstantinopoulos, P.A.1    Karamouzis, M.V.2    Papavassiliou, A.G.3
  • 38
    • 0032493812 scopus 로고    scopus 로고
    • Increasing complexity of the Ras signaling pathway
    • Vojtek A.B., Der C.J. Increasing complexity of the Ras signaling pathway. J. Biol. Chem. 1998, 273:19925-19928.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19925-19928
    • Vojtek, A.B.1    Der, C.J.2
  • 40
    • 0032538295 scopus 로고    scopus 로고
    • NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor trio
    • Liu X.H., Wang H., Eberstadt M., Schnuchel A., Olejniczak E.T., et al. NMR structure and mutagenesis of the N-terminal Dbl homology domain of the nucleotide exchange factor trio. Cell 1998, 95:269-277.
    • (1998) Cell , vol.95 , pp. 269-277
    • Liu, X.H.1    Wang, H.2    Eberstadt, M.3    Schnuchel, A.4    Olejniczak, E.T.5
  • 41
    • 0034619877 scopus 로고    scopus 로고
    • Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1
    • Worthylake D.K., Rossman K.L., Sondek J. Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1. Nature 2000, 408:682-688.
    • (2000) Nature , vol.408 , pp. 682-688
    • Worthylake, D.K.1    Rossman, K.L.2    Sondek, J.3
  • 42
    • 0035836791 scopus 로고    scopus 로고
    • Rho signals to cell growth and apoptosis
    • Aznar S., Lacal J.C. Rho signals to cell growth and apoptosis. Cancer Lett. 2001, 165:1-10.
    • (2001) Cancer Lett. , vol.165 , pp. 1-10
    • Aznar, S.1    Lacal, J.C.2
  • 43
    • 84861147473 scopus 로고    scopus 로고
    • A comprehensive survey of Ras mutations in cancer
    • Prior I.A., Lewis P.D., Mattos C. A comprehensive survey of Ras mutations in cancer. Cancer Res. 2012, 72:2457-2467.
    • (2012) Cancer Res. , vol.72 , pp. 2457-2467
    • Prior, I.A.1    Lewis, P.D.2    Mattos, C.3
  • 44
    • 4344572283 scopus 로고    scopus 로고
    • Rho overexpression leads to mitosis-associated detachment of cells from epithelial sheets: a link to the mechanism of cancer dissemination
    • Vasiliev J.M., Omelchenko T., Gelfand I.M., Feder H.H., Bonder E.M. Rho overexpression leads to mitosis-associated detachment of cells from epithelial sheets: a link to the mechanism of cancer dissemination. Proc. Natl. Acad. Sci. U.S.A. 2004, 101:12526-12530.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 12526-12530
    • Vasiliev, J.M.1    Omelchenko, T.2    Gelfand, I.M.3    Feder, H.H.4    Bonder, E.M.5
  • 45
    • 15144353776 scopus 로고    scopus 로고
    • Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav
    • Han J., Luby-Phelps K., Das B., Shu X., Xia Y., et al. Role of substrates and products of PI 3-kinase in regulating activation of Rac-related guanosine triphosphatases by Vav. Science 1998, 279:558-560.
    • (1998) Science , vol.279 , pp. 558-560
    • Han, J.1    Luby-Phelps, K.2    Das, B.3    Shu, X.4    Xia, Y.5
  • 46
    • 84862655609 scopus 로고    scopus 로고
    • Overexpressed hPTTG1 promotes breast cancer cell invasion and metastasis by regulating GEF-H1/RhoA signalling
    • Liao Y.C., Ruan J.W., Lua I., Li M.H., Chen W.L., et al. Overexpressed hPTTG1 promotes breast cancer cell invasion and metastasis by regulating GEF-H1/RhoA signalling. Oncogene 2012, 31:3086-3097.
    • (2012) Oncogene , vol.31 , pp. 3086-3097
    • Liao, Y.C.1    Ruan, J.W.2    Lua, I.3    Li, M.H.4    Chen, W.L.5
  • 47
    • 42049094628 scopus 로고    scopus 로고
    • Epidermal growth factor receptor gene amplication is acquired in association with tumor progression of EGFR-mutated lung cancer
    • Yatabe Y., Takahashi T., Mitsudomi T. Epidermal growth factor receptor gene amplication is acquired in association with tumor progression of EGFR-mutated lung cancer. Cancer Res. 2008, 68:2106-2111.
    • (2008) Cancer Res. , vol.68 , pp. 2106-2111
    • Yatabe, Y.1    Takahashi, T.2    Mitsudomi, T.3
  • 48
    • 0034947649 scopus 로고    scopus 로고
    • EGF mutant receptor vIII as a molecular target in cancer therapy
    • Kuan C.T., Wikstrand C.J., Bigner D.D. EGF mutant receptor vIII as a molecular target in cancer therapy. Endocr. Relat. Cancer 2001, 8:83-96.
    • (2001) Endocr. Relat. Cancer , vol.8 , pp. 83-96
    • Kuan, C.T.1    Wikstrand, C.J.2    Bigner, D.D.3
  • 49
    • 77956513286 scopus 로고    scopus 로고
    • Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma
    • Bollag G., Hirth P., Tsai J., Zhang J., Ibrahim P.N., et al. Clinical efficacy of a RAF inhibitor needs broad target blockade in BRAF-mutant melanoma. Nature 2010, 467:596-599.
    • (2010) Nature , vol.467 , pp. 596-599
    • Bollag, G.1    Hirth, P.2    Tsai, J.3    Zhang, J.4    Ibrahim, P.N.5
  • 50
    • 78650303507 scopus 로고    scopus 로고
    • Melanomas acquire resistance to B-RAF(V600E) inhibition by RTK or N-RAS upregulation
    • Nazarian R., Shi H., Wang Q., Kong X., Koya R.C., et al. Melanomas acquire resistance to B-RAF(V600E) inhibition by RTK or N-RAS upregulation. Nature 2010, 468:973-977.
    • (2010) Nature , vol.468 , pp. 973-977
    • Nazarian, R.1    Shi, H.2    Wang, Q.3    Kong, X.4    Koya, R.C.5
  • 51
    • 84862571677 scopus 로고    scopus 로고
    • Prognostic and predictive value of K-RAS mutations in non-small cell lung cancer
    • Califano R., Landi L., Cappuzzo F. Prognostic and predictive value of K-RAS mutations in non-small cell lung cancer. Drugs 2012, 72(Suppl 1):28-36.
    • (2012) Drugs , vol.72 , Issue.SUPPL. 1 , pp. 28-36
    • Califano, R.1    Landi, L.2    Cappuzzo, F.3
  • 52
    • 16644370412 scopus 로고    scopus 로고
    • Human RAS superfamily proteins and related GTPases
    • Colicelli J. Human RAS superfamily proteins and related GTPases. Sci. STKE 2004, 2004:RE13.
    • (2004) Sci. STKE , vol.2004
    • Colicelli, J.1
  • 53
    • 0037542854 scopus 로고    scopus 로고
    • Ras proteins: different signals from different locations
    • Hancock J.F. Ras proteins: different signals from different locations. Nat. Rev. Mol. Cell Biol. 2003, 4:373-384.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 373-384
    • Hancock, J.F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.