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Volumn 13, Issue 4, 2015, Pages 595-603

The Ras-membrane interface: Isoform-specific differences in the catalytic domain

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; RAS ASSOCIATION DOMAIN FAMILY PROTEIN 1A; PROTEIN BINDING; RAS PROTEIN;

EID: 84927615339     PISSN: 15417786     EISSN: 15573125     Source Type: Journal    
DOI: 10.1158/1541-7786.MCR-14-0535     Document Type: Review
Times cited : (48)

References (75)
  • 1
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne HR, Sanders DA, McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature 1991;349:117-27.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 3242811317 scopus 로고    scopus 로고
    • GTP hydrolysis mechanism of Ras-like GTPases
    • Li G, Zhang XC. GTP hydrolysis mechanism of Ras-like GTPases. J Mol Biol 2004;340:921-32.
    • (2004) J Mol Biol , vol.340 , pp. 921-932
    • Li, G.1    Zhang, X.C.2
  • 3
    • 22144479017 scopus 로고    scopus 로고
    • Ras plasma membrane signalling platforms
    • Hancock JF, Parton RG. Ras plasma membrane signalling platforms. Biochem J 2005;389:1-11.
    • (2005) Biochem J , vol.389 , pp. 1-11
    • Hancock, J.F.1    Parton, R.G.2
  • 5
    • 84861147473 scopus 로고    scopus 로고
    • A comprehensive survey of Ras mutations in cancer
    • Prior IA, Lewis PD, Mattos C. A comprehensive survey of Ras mutations in cancer. Cancer Res 2012;72:2457-67.
    • (2012) Cancer Res , vol.72 , pp. 2457-2467
    • Prior, I.A.1    Lewis, P.D.2    Mattos, C.3
  • 6
    • 54049150339 scopus 로고    scopus 로고
    • Fluoride complexes of oncogenic Ras mutants to study the Ras-RasGap interaction
    • Gremer L, Gilsbach B, Ahmadian MR, Wittinghofer A. Fluoride complexes of oncogenic Ras mutants to study the Ras-RasGap interaction. Biol Chem 2008;389:1163-71.
    • (2008) Biol Chem , vol.389 , pp. 1163-1171
    • Gremer, L.1    Gilsbach, B.2    Ahmadian, M.R.3    Wittinghofer, A.4
  • 7
    • 61449215145 scopus 로고    scopus 로고
    • Ras acylation, compartmentalization and signaling nanoclusters
    • Henis YI, Hancock JF, Prior IA. Ras acylation, compartmentalization and signaling nanoclusters. Mol Membr Biol 2009;26:80-92.
    • (2009) Mol Membr Biol , vol.26 , pp. 80-92
    • Henis, Y.I.1    Hancock, J.F.2    Prior, I.A.3
  • 8
    • 84858796808 scopus 로고    scopus 로고
    • Ras trafficking, localization and compartmentalized signalling
    • Prior IA, Hancock JF. Ras trafficking, localization and compartmentalized signalling. Semin Cell Dev Biol 2012;23:145-53.
    • (2012) Semin Cell Dev Biol , vol.23 , pp. 145-153
    • Prior, I.A.1    Hancock, J.F.2
  • 9
    • 50849107378 scopus 로고    scopus 로고
    • Mechanisms of Ras membrane organization and signalling: Ras on a rocker
    • Abankwa D, Gorfe AA, Hancock JF. Mechanisms of Ras membrane organization and signalling: Ras on a rocker. Cell Cycle 2008;7:2667-73.
    • (2008) Cell Cycle , vol.7 , pp. 2667-2673
    • Abankwa, D.1    Gorfe, A.A.2    Hancock, J.F.3
  • 11
    • 84870208145 scopus 로고    scopus 로고
    • Latest developments in experimental and computational approaches to characterize protein-lipid interactions
    • Cho H, Wu M, Bilgin B, Walton SP, Chan C. Latest developments in experimental and computational approaches to characterize protein-lipid interactions. Proteomics 2012;12:3273-85.
    • (2012) Proteomics , vol.12 , pp. 3273-3285
    • Cho, H.1    Wu, M.2    Bilgin, B.3    Walton, S.P.4    Chan, C.5
  • 14
    • 4544295231 scopus 로고    scopus 로고
    • Galectin-3 augments K-Ras activation and triggers a Ras signal that attenuates ERK but not phosphoinositide 3-kinase activity
    • Elad-Sfadia G, Haklai R, Balan E, Kloog Y. Galectin-3 augments K-Ras activation and triggers a Ras signal that attenuates ERK but not phosphoinositide 3-kinase activity. J Biol Chem 2004;279:34922-30.
    • (2004) J Biol Chem , vol.279 , pp. 34922-34930
    • Elad-Sfadia, G.1    Haklai, R.2    Balan, E.3    Kloog, Y.4
  • 15
    • 21744432683 scopus 로고    scopus 로고
    • GDIs: Central regulatory molecules in Rho GTPase activation
    • DerMardirossian C, Bokoch GM.GDIs: central regulatory molecules in Rho GTPase activation. Trends Cell Biol 2005;15:356-63.
    • (2005) Trends Cell Biol , vol.15 , pp. 356-363
    • Dermardirossian, C.1    Bokoch, G.M.2
  • 16
    • 32444441115 scopus 로고    scopus 로고
    • PKC regulates a farnesyl-electrostatic switch on K-Ras that promotes its association with Bcl-XL on mitochondria and induces apoptosis
    • Bivona TG, Quatela SE, Bodemann BO, Ahearn IM, Soskis MJ, Mor A, et al. PKC regulates a farnesyl-electrostatic switch on K-Ras that promotes its association with Bcl-XL on mitochondria and induces apoptosis. Mol Cell 2006;21:481-93.
    • (2006) Mol Cell , vol.21 , pp. 481-493
    • Bivona, T.G.1    Quatela, S.E.2    Bodemann, B.O.3    Ahearn, I.M.4    Soskis, M.J.5    Mor, A.6
  • 18
  • 20
    • 58149197889 scopus 로고    scopus 로고
    • Membrane binding of lipidated Ras peptides and proteins-The structural point of view
    • Brunsveld L, Waldmann H, Huster D. Membrane binding of lipidated Ras peptides and proteins-The structural point of view. Biochim Biophys Acta 2009;1788:273-88.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 273-288
    • Brunsveld, L.1    Waldmann, H.2    Huster, D.3
  • 21
    • 77950397231 scopus 로고    scopus 로고
    • Allosteric modulation of Ras positions Q61 for a direct role in catalysis
    • Buhrman G, Holzapfel G, Fetics S, Mattos C. Allosteric modulation of Ras positions Q61 for a direct role in catalysis. Proc Natl Acad Sci USA 2010;107:4931-6.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4931-4936
    • Buhrman, G.1    Holzapfel, G.2    Fetics, S.3    Mattos, C.4
  • 22
    • 2542434848 scopus 로고    scopus 로고
    • A designed probe for acidic phospholipids reveals the unique enriched anionic character of the cytosolic face of the mammalian plasma membrane
    • Okeley NM, Gelb MH. A designed probe for acidic phospholipids reveals the unique enriched anionic character of the cytosolic face of the mammalian plasma membrane. J Biol Chem 2004;279:21833-40.
    • (2004) J Biol Chem , vol.279 , pp. 21833-21840
    • Okeley, N.M.1    Gelb, M.H.2
  • 24
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: From modelmembranes to cells
    • EdidinM. The state of lipid rafts: from modelmembranes to cells. Annu Rev Biophys Biomol Struct 2003;32:257-83.
    • (2003) Annu Rev Biophys Biomol Struct , vol.32 , pp. 257-283
    • Edidin, M.1
  • 25
    • 84896813530 scopus 로고    scopus 로고
    • Key molecular requirements for raft formation in lipid/cholesterol membranes
    • Hakobyan D, Heuer A. Key molecular requirements for raft formation in lipid/cholesterol membranes. PLoS ONE 2014;9:e87369.
    • (2014) PLoS ONE , vol.9 , pp. e87369
    • Hakobyan, D.1    Heuer, A.2
  • 26
    • 1842482773 scopus 로고    scopus 로고
    • Model systems, lipid rafts, and cell membranes
    • Simons K, Vaz WL. Model systems, lipid rafts, and cell membranes. Annu Rev Biophys Biomol Struct 2004;33:269-95.
    • (2004) Annu Rev Biophys Biomol Struct , vol.33 , pp. 269-295
    • Simons, K.1    Vaz, W.L.2
  • 27
    • 0037455589 scopus 로고    scopus 로고
    • Direct visualization of Ras proteins in spatially distinct cell surface microdomains
    • Prior IA, Muncke C, Parton RG, Hancock JF. Direct visualization of Ras proteins in spatially distinct cell surface microdomains. J Cell Biol 2003;160:165-70.
    • (2003) J Cell Biol , vol.160 , pp. 165-170
    • Prior, I.A.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 28
    • 3242657115 scopus 로고    scopus 로고
    • Three separable domains regulate GTP-dependent association of H-ras with the plasma membrane
    • Rotblat B, Prior IA, Muncke C, Parton RG, Kloog Y, Henis YI, et al. Three separable domains regulate GTP-dependent association of H-ras with the plasma membrane. Mol Cell Biol 2004;24:6799-810.
    • (2004) Mol Cell Biol , vol.24 , pp. 6799-6810
    • Rotblat, B.1    Prior, I.A.2    Muncke, C.3    Parton, R.G.4    Kloog, Y.5    Henis, Y.I.6
  • 29
    • 40949127740 scopus 로고    scopus 로고
    • Palmitoylation and localisation of RAS isoforms are modulated by the hypervariable linker domain
    • Laude AJ, Prior IA. Palmitoylation and localisation of RAS isoforms are modulated by the hypervariable linker domain. J Cell Sci 2008;121:421-7.
    • (2008) J Cell Sci , vol.121 , pp. 421-427
    • Laude, A.J.1    Prior, I.A.2
  • 30
    • 84867572593 scopus 로고    scopus 로고
    • The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction
    • Kapoor S, Weise K, Erlkamp M, Triola G, Waldmann H, Winter R. The role of G-domain orientation and nucleotide state on the Ras isoform-specific membrane interaction. Eur Biophys J 2012;41:801-13.
    • (2012) Eur Biophys J , vol.41 , pp. 801-813
    • Kapoor, S.1    Weise, K.2    Erlkamp, M.3    Triola, G.4    Waldmann, H.5    Winter, R.6
  • 31
    • 0032763121 scopus 로고    scopus 로고
    • Electrostatic properties of membranes containing acidic lipids and absorbed basic peptides: Theory and experiment
    • Murray D, Arbuziva A, Hangyas-Mihalyne G, Gambhir A, Ben-Tal N, Honig B, et al. Electrostatic properties of membranes containing acidic lipids and absorbed basic peptides: theory and experiment. Biophys J 1999;77: 3176-88.
    • (1999) Biophys J , vol.77 , pp. 3176-3188
    • Murray, D.1    Arbuziva, A.2    Hangyas-Mihalyne, G.3    Gambhir, A.4    Ben-Tal, N.5    Honig, B.6
  • 32
    • 33748745926 scopus 로고    scopus 로고
    • Cell migration and signaling specificity is determined by the phosphatidylserine recognition motif of Rac1
    • Finkielstein CV, Overduin M, Capelluto DG. Cell migration and signaling specificity is determined by the phosphatidylserine recognition motif of Rac1. J Biol Chem 2006;281:27317-26.
    • (2006) J Biol Chem , vol.281 , pp. 27317-27326
    • Finkielstein, C.V.1    Overduin, M.2    Capelluto, D.G.3
  • 33
    • 84903399695 scopus 로고    scopus 로고
    • Dynamic membrane structure induces temporal pattern formation
    • Lippoldt J, Handel C, Dietrich U, Kas JA. Dynamic membrane structure induces temporal pattern formation. Biochim Biophys Acta 2014; 1838:2380-90.
    • (2014) Biochim Biophys Acta , vol.1838 , pp. 2380-2390
    • Lippoldt, J.1    Handel, C.2    Dietrich, U.3    Kas, J.A.4
  • 34
    • 79851483766 scopus 로고    scopus 로고
    • Membranemediated induction and sorting of K-Ras microdomain signaling platforms
    • Weise K, Kapoor S, Denter C, Nikolaus J, Opitz N, Koch S, et al. Membranemediated induction and sorting of K-Ras microdomain signaling platforms. J Am Chem Soc 2011;133:880-7.
    • (2011) J Am Chem Soc , vol.133 , pp. 880-887
    • Weise, K.1    Kapoor, S.2    Denter, C.3    Nikolaus, J.4    Opitz, N.5    Koch, S.6
  • 35
    • 1942519695 scopus 로고    scopus 로고
    • Electrostatic seuqestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins
    • Gambhir A, Hangyas-Mihalyne G, Zaitseva I, Cafiso D, Wang J, Pentyala S, et al. Electrostatic seuqestration of PIP2 on phospholipid membranes by basic/aromatic regions of proteins. Biophys J 2004;86:2188-207.
    • (2004) Biophys J , vol.86 , pp. 2188-2207
    • Gambhir, A.1    Hangyas-Mihalyne, G.2    Zaitseva, I.3    Cafiso, D.4    Wang, J.5    Pentyala, S.6
  • 36
    • 33845313646 scopus 로고    scopus 로고
    • PI( 3, 4,5) P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane
    • Heo WD, Inoue T, Park WS, Kim ML, Park BO, Wandless TJ, et al. PI(3,4,5) P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane. Science 2006;314:1458-61.
    • (2006) Science , vol.314 , pp. 1458-1461
    • Heo, W.D.1    Inoue, T.2    Park, W.S.3    Kim, M.L.4    Park, B.O.5    Wandless, T.J.6
  • 37
    • 28444477387 scopus 로고    scopus 로고
    • Plasma membrane phosphoinositide organization by protein electrostatics
    • McLaughlin S, Murray D. Plasma membrane phosphoinositide organization by protein electrostatics. Nature 2005;438:605-11.
    • (2005) Nature , vol.438 , pp. 605-611
    • McLaughlin, S.1    Murray, D.2
  • 38
    • 46149107301 scopus 로고    scopus 로고
    • Electrostatic interactions positively regulate K-Ras nanocluster formation and function
    • Plowman SJ, Ariotti N, Goodall A, Parton RG, Hancock JF. Electrostatic interactions positively regulate K-Ras nanocluster formation and function. Mol Cell Biol 2008;28:4377-85.
    • (2008) Mol Cell Biol , vol.28 , pp. 4377-4385
    • Plowman, S.J.1    Ariotti, N.2    Goodall, A.3    Parton, R.G.4    Hancock, J.F.5
  • 39
    • 66349087046 scopus 로고    scopus 로고
    • The challenge of lipid rafts
    • Pike LJ. The challenge of lipid rafts. J Lipid Res 2009;50:S323-8.
    • (2009) J Lipid Res , vol.50 , pp. S323-S328
    • Pike, L.J.1
  • 41
    • 27344456331 scopus 로고    scopus 로고
    • H-ras K-ras and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton
    • Plowman SJ, Muncke C, Parton RG, Hancock JF. H-ras, K-ras, and inner plasma membrane raft proteins operate in nanoclusters with differential dependence on the actin cytoskeleton. Proc Natl Acad Sci USA 2005; 102:15500-5.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 15500-15505
    • Plowman, S.J.1    Muncke, C.2    Parton, R.G.3    Hancock, J.F.4
  • 42
    • 84872959202 scopus 로고    scopus 로고
    • Caveolae as plasma membrane sensors, protectors and organizers
    • Parton RG, del Pozo MA. Caveolae as plasma membrane sensors, protectors and organizers. Nat Rev Mol Cell Biol 2013;14:98-112.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 98-112
    • Parton, R.G.1    Del Pozo, M.A.2
  • 43
    • 84895770533 scopus 로고    scopus 로고
    • Caveolae regulate the nanoscale organization of the plasma membrane to remotely control Ras signaling
    • Ariotti N, Fernandez-Rojo MA, Zhou Y, Hill MM, Rodkey TL, Inder KL, et al. Caveolae regulate the nanoscale organization of the plasma membrane to remotely control Ras signaling. J Cell Biol 2014;204:777-92.
    • (2014) J Cell Biol , vol.204 , pp. 777-792
    • Ariotti, N.1    Fernandez-Rojo, M.A.2    Zhou, Y.3    Hill, M.M.4    Rodkey, T.L.5    Inder, K.L.6
  • 44
  • 46
    • 20144375061 scopus 로고    scopus 로고
    • An acylation cycle regulates localization and activity of palmitoylated Ras isoforms
    • Rocks O, Peyker A, Kahms M, Verveer PJ, Koerner C, LumbierresM, et al. An acylation cycle regulates localization and activity of palmitoylated Ras isoforms. Science 2005;307:1746-52.
    • (2005) Science , vol.307 , pp. 1746-1752
    • Rocks, O.1    Peyker, A.2    Kahms, M.3    Verveer, P.J.4    Koerner, C.5    Lumbierres, M.6
  • 48
    • 84878635230 scopus 로고    scopus 로고
    • TCR-stimulated T-cells, N-Ras regulates specific genes and signal transduction pathways
    • Lynch SJ, Zavadil J, Pellicer A. In TCR-stimulated T-cells, N-Ras regulates specific genes and signal transduction pathways. PLoS ONE 2013;8: e63193.
    • (2013) PLoS ONE , vol.8 , pp. e63193
    • Lynch, S.J.1    Zavadil, J.2    Pellicer, A.3
  • 49
    • 33749264618 scopus 로고    scopus 로고
    • Structural and functional consequences of c-N-Ras constitutively associated with intact mitochondria
    • Wolfman JC, Planchon SM, Liao J, Wolfman A. Structural and functional consequences of c-N-Ras constitutively associated with intact mitochondria. Biochim Biophys Acta 2006;1763:1108-24.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 1108-1124
    • Wolfman, J.C.1    Planchon, S.M.2    Liao, J.3    Wolfman, A.4
  • 50
    • 78651287877 scopus 로고    scopus 로고
    • Making heads or tails of phospholipids in mitochondria
    • Osman C, Voelker DR, Langer T. Making heads or tails of phospholipids in mitochondria. J Cell Biol 2011;192:7-16.
    • (2011) J Cell Biol , vol.192 , pp. 7-16
    • Osman, C.1    Voelker, D.R.2    Langer, T.3
  • 51
    • 0035067187 scopus 로고    scopus 로고
    • GTP-dependent segregation of H-ras from lipid rafts is required for biological activity
    • Prior IA, Harding A, Yan J, Sluimer J, Parton R,Hancock JF. GTP-dependent segregation of H-ras from lipid rafts is required for biological activity. Nat Cell Biol 2001;3:368-75.
    • (2001) Nat Cell Biol , vol.3 , pp. 368-375
    • Prior, I.A.1    Harding, A.2    Yan, J.3    Sluimer, J.4    Parton Rhancock, J.F.5
  • 52
    • 40949130399 scopus 로고    scopus 로고
    • A novel switch region regultes H-Ras membrane orientation and signal output
    • Abankwa D, Hanzel-Bayer M, Ariotti N, Plowman S, Gorfe A, Parton R, et al. A novel switch region regultes H-Ras membrane orientation and signal output. EMBO J 2008;27:727-35.
    • (2008) EMBO J , vol.27 , pp. 727-735
    • Abankwa, D.1    Hanzel-Bayer, M.2    Ariotti, N.3    Plowman, S.4    Gorfe, A.5    Parton, R.6
  • 53
    • 84892531631 scopus 로고    scopus 로고
    • DRoP: A water analysis program identifies Ras-GTP-specific pathway of communication between membrane-interacting regions and the active site
    • Kearney BM, Johnson CW, Roberts DM, Swartz P, Mattos C. DRoP: A water analysis program identifies Ras-GTP-specific pathway of communication between membrane-interacting regions and the active site. J Mol Biol 2014;426:611-29.
    • (2014) J Mol Biol , vol.426 , pp. 611-629
    • Kearney, B.M.1    Johnson, C.W.2    Roberts, D.M.3    Swartz, P.4    Mattos, C.5
  • 54
    • 33847413103 scopus 로고    scopus 로고
    • Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-Dimyristoylglycero-3-phosphocholine bilayer
    • Gorfe A, Hanzel-Bayer M, Abankwa D, Hancock J, McCammon J. Structure and dynamics of the full-length lipid-modified H-Ras protein in a 1,2-Dimyristoylglycero-3-phosphocholine bilayer. J Med Chem 2007;50: 674-84.
    • (2007) J Med Chem , vol.50 , pp. 674-684
    • Gorfe, A.1    Hanzel-Bayer, M.2    Abankwa, D.3    Hancock, J.4    McCammon, J.5
  • 55
    • 84881539880 scopus 로고    scopus 로고
    • Lessons from computer simulations of Ras proteins in solution and in membrane
    • Prakash P, Gorfe AA. Lessons from computer simulations of Ras proteins in solution and in membrane. Biochim Biophys Acta 2013;1830:5211-8.
    • (2013) Biochim Biophys Acta , vol.1830 , pp. 5211-5218
    • Prakash, P.1    Gorfe, A.A.2
  • 56
    • 84898063580 scopus 로고    scopus 로고
    • The efficacy of Raf kinase recruitment to the GTPase H-ras depends on H-ras membrane conformer specific nanoclustering
    • Guzmán C, S?olman M, Ligabue A, Blaževits? O, Andrade DM, Reymond L, et al. The efficacy of Raf kinase recruitment to the GTPase H-ras depends on H-ras membrane conformer specific nanoclustering. J Biol Chem 2014;289:9519-33.
    • (2014) J Biol Chem , vol.289 , pp. 9519-9533
    • Guzmán, C.1    Solman, M.2    Ligabue, A.3    Blaževits, O.4    Andrade, D.M.5    Reymond, L.6
  • 60
    • 75749150934 scopus 로고    scopus 로고
    • Ras membrane orientation and nanodomain localization generate isoform diversity
    • Abankwa D, Gorfe AA, Inder K, Hancock JF. Ras membrane orientation and nanodomain localization generate isoform diversity. Proc Natl Acad Sci USA 2010;107:1130-5.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 1130-1135
    • Abankwa, D.1    Gorfe, A.A.2    Inder, K.3    Hancock, J.F.4
  • 62
    • 0034635502 scopus 로고    scopus 로고
    • Formation of the Ras dimer is essential for Raf-1 activation
    • Inouye K, Mizutani S, Koide H, Kaziro Y. Formation of the Ras dimer is essential for Raf-1 activation. J Biol Chem 2000;275:3737-40.
    • (2000) J Biol Chem , vol.275 , pp. 3737-3740
    • Inouye, K.1    Mizutani, S.2    Koide, H.3    Kaziro, Y.4
  • 64
    • 79952811451 scopus 로고    scopus 로고
    • Allosteric modulation of Ras-GTP is linked to signal transduction through RAF kinase
    • Buhrman G, Kumar VS, Cirit M, Haugh JM, Mattos C. Allosteric modulation of Ras-GTP is linked to signal transduction through RAF kinase. J Biol Chem 2011;286:3323-31.
    • (2011) J Biol Chem , vol.286 , pp. 3323-3331
    • Buhrman, G.1    Kumar, V.S.2    Cirit, M.3    Haugh, J.M.4    Mattos, C.5
  • 65
    • 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 1998;273:24052-6.
    • (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
  • 66
    • 0038143229 scopus 로고    scopus 로고
    • Distinct rates of palmitate turnover on membrane-bound cellular and oncogenic H-ras
    • Baker TL, Zheng H, Walker J, Coloff JL, Buss JE. Distinct rates of palmitate turnover on membrane-bound cellular and oncogenic H-ras. J Biol Chem 2003;278:19292-300.
    • (2003) J Biol Chem , vol.278 , pp. 19292-19300
    • Baker, T.L.1    Zheng, H.2    Walker, J.3    Coloff, J.L.4    Buss, J.E.5
  • 68
    • 52949089338 scopus 로고    scopus 로고
    • Global conformational dynamics in Ras
    • O'Connor C, Kovrigin E. Global conformational dynamics in Ras. Biochemistry 2008;47:10244-6.
    • (2008) Biochemistry , vol.47 , pp. 10244-10246
    • O'Connor, C.1    Kovrigin, E.2
  • 69
    • 80655149448 scopus 로고    scopus 로고
    • Solution structure of the state 1 conformer of GTP-bound H-Ras protein and distinct dynamic properties between the state 1 and state 2 conformers
    • Araki M, Shima F, Yoshikawa Y, Muraoka S, Ijiri Y, Nagahara Y, et al. Solution structure of the state 1 conformer of GTP-bound H-Ras protein and distinct dynamic properties between the state 1 and state 2 conformers. J Biol Chem 2011;286:39644-53.
    • (2011) J Biol Chem , vol.286 , pp. 39644-39653
    • Araki, M.1    Shima, F.2    Yoshikawa, Y.3    Muraoka, S.4    Ijiri, Y.5    Nagahara, Y.6
  • 70
    • 84865463399 scopus 로고    scopus 로고
    • Ras inhibition via direct Ras binding-is there a path forward?
    • Wang W, FangG, Rudolph J. Ras inhibition via direct Ras binding-is there a path forward? Bioorg Med Chem Lett 2012;22:5766-76.
    • (2012) Bioorg Med Chem Lett , vol.22 , pp. 5766-5776
    • Wang, W.1    Fangg Rudolph, J.2
  • 72
    • 84871491627 scopus 로고    scopus 로고
    • Ras/Raf/MEK/ERK and PI3K/PTEN/Akt/mTOR cascade inhibitors: How mutations can result in therapy resistance and how to overcome resistance
    • McCubrey JA, Steelman LS, Chappell WH, Abrams SL, Franklin RA, Montalto G, et al. Ras/Raf/MEK/ERK and PI3K/PTEN/Akt/mTOR cascade inhibitors: how mutations can result in therapy resistance and how to overcome resistance. Oncotarget 2012;3:1068-111.
    • (2012) Oncotarget , vol.3 , pp. 1068-1111
    • McCubrey, J.A.1    Steelman, L.S.2    Chappell, W.H.3    Abrams, S.L.4    Franklin, R.A.5    Montalto, G.6
  • 73
    • 0030923192 scopus 로고    scopus 로고
    • K-and N-Ras are geranylgeranylated in cells treated with farnesyl protein transferase inhibitors
    • Whyte DB, Kirschmeier P, Hockenberry TN, Nunez-Oliva I, James L, Catino JJ, et al. K-and N-Ras are geranylgeranylated in cells treated with farnesyl protein transferase inhibitors. J Biol Chem 1997;272:14459-64.
    • (1997) J Biol Chem , vol.272 , pp. 14459-14464
    • Whyte, D.B.1    Kirschmeier, P.2    Hockenberry, T.N.3    Nunez-Oliva, I.4    James, L.5    Catino, J.J.6
  • 74
    • 84875534210 scopus 로고    scopus 로고
    • Integrated preclinical and clinical development of S-trans, trans-Farnesylthiosalicylic Acid (FTS, Salirasib) in pancreatic cancer
    • Laheru D, Shah P, Rajeshkumar NV, McAllister F, Taylor G, Goldsweig H, et al. Integrated preclinical and clinical development of S-trans, trans-Farnesylthiosalicylic Acid (FTS, Salirasib) in pancreatic cancer. Invest New Drugs 2012;30:2391-9.
    • (2012) Invest New Drugs , vol.30 , pp. 2391-2399
    • Laheru, D.1    Shah, P.2    Rajeshkumar, N.V.3    McAllister, F.4    Taylor, G.5    Goldsweig, H.6


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