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Volumn 290, Issue 15, 2015, Pages 9465-9477

Mechanisms of membrane binding of small GTPase K-Ras4B farnesylated hypervariable region

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; MOLECULAR DYNAMICS; PHOSPHOLIPIDS; SURFACE PLASMON RESONANCE;

EID: 84927144988     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.620724     Document Type: Article
Times cited : (94)

References (91)
  • 1
    • 0033835421 scopus 로고    scopus 로고
    • The importance of being K-Ras
    • Ellis, C. A., and Clark, G. (2000) The importance of being K-Ras. Cell. Signal. 12, 425-434
    • (2000) Cell. Signal. , vol.12 , pp. 425-434
    • Ellis, C.A.1    Clark, G.2
  • 5
  • 6
    • 0037054546 scopus 로고    scopus 로고
    • Phospholipids undergo hop diffusion in compartmentalized cell membrane
    • Fujiwara, T., Ritchie, K., Murakoshi, H., Jacobson, K., and Kusumi, A. (2002) Phospholipids undergo hop diffusion in compartmentalized cell membrane. J. Cell Biol. 157, 1071-1081
    • (2002) J. Cell Biol. , vol.157 , pp. 1071-1081
    • Fujiwara, T.1    Ritchie, K.2    Murakoshi, H.3    Jacobson, K.4    Kusumi, A.5
  • 9
    • 36248934768 scopus 로고    scopus 로고
    • Interactions of Ras proteins with the plasma membrane and their roles in signaling
    • Eisenberg, S., and Henis, Y. I. (2008) Interactions of Ras proteins with the plasma membrane and their roles in signaling. Cell. Signal. 20, 31-39
    • (2008) Cell. Signal. , vol.20 , pp. 31-39
    • Eisenberg, S.1    Henis, Y.I.2
  • 11
    • 0034699336 scopus 로고    scopus 로고
    • Structure and function of the C-terminal hypervariable region of K-Ras4B in plasma membrane targeting and transformation
    • Welman, A., Burger, M. M., and Hagmann, J. (2000) Structure and function of the C-terminal hypervariable region of K-Ras4B in plasma membrane targeting and transformation. Oncogene 19, 4582-4591
    • (2000) Oncogene , vol.19 , pp. 4582-4591
    • Welman, A.1    Burger, M.M.2    Hagmann, J.3
  • 12
    • 77955417069 scopus 로고    scopus 로고
    • Expression, purification, and characterization of soluble K-Ras4B for structural analysis
    • Abraham, S. J., Muhamed, I., Nolet, R., Yeung, F., and Gaponenko, V. (2010) Expression, purification, and characterization of soluble K-Ras4B for structural analysis. Protein Expr. Purif. 73, 125-131
    • (2010) Protein Expr. Purif. , vol.73 , pp. 125-131
    • Abraham, S.J.1    Muhamed, I.2    Nolet, R.3    Yeung, F.4    Gaponenko, V.5
  • 13
    • 44849117286 scopus 로고    scopus 로고
    • Identification of essential interacting elements in K-Ras/calmodulin binding and its role in K-Ras localization
    • Lopez-Alcalá, C., Alvarez-Moya, B., Villalonga, P., Calvo, M., Bachs, O., and Agell, N. (2008) Identification of essential interacting elements in K-Ras/calmodulin binding and its role in K-Ras localization. J. Biol. Chem. 283, 10621-10631
    • (2008) J. Biol. Chem. , vol.283 , pp. 10621-10631
    • Lopez-Alcalá, C.1    Alvarez-Moya, B.2    Villalonga, P.3    Calvo, M.4    Bachs, O.5    Agell, N.6
  • 14
    • 84898606304 scopus 로고    scopus 로고
    • KRas localizes to the plasma membrane by spatial cycles of solubilization, trapping and vesicular transport
    • Schmick, M., Vartak, N., Papke, B., Kovacevic, M., Truxius, D. C., Rossmannek, L., and Bastiaens, P. I. (2014) KRas localizes to the plasma membrane by spatial cycles of solubilization, trapping and vesicular transport. Cell 157, 459-471
    • (2014) Cell , vol.157 , pp. 459-471
    • Schmick, M.1    Vartak, N.2    Papke, B.3    Kovacevic, M.4    Truxius, D.C.5    Rossmannek, L.6    Bastiaens, P.I.7
  • 15
    • 0035860727 scopus 로고    scopus 로고
    • Agonist-dependent traffic of raft-associated Ras and Raf-1 is required for activation of the mitogen-activated protein kinase cascade
    • Rizzo, M. A., Kraft, C. A., Watkins, S. C., Levitan, E. S., and Romero, G. (2001) Agonist-dependent traffic of raft-associated Ras and Raf-1 is required for activation of the mitogen-activated protein kinase cascade. J. Biol. Chem. 276, 34928-34933
    • (2001) J. Biol. Chem. , vol.276 , pp. 34928-34933
    • Rizzo, M.A.1    Kraft, C.A.2    Watkins, S.C.3    Levitan, E.S.4    Romero, G.5
  • 17
    • 15844431258 scopus 로고    scopus 로고
    • Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane
    • Mineo, C., James, G. L., Smart, E. J., and Anderson, R. G. (1996) Localization of epidermal growth factor-stimulated Ras/Raf-1 interaction to caveolae membrane. J. Biol. Chem. 271, 11930-11935
    • (1996) J. Biol. Chem. , vol.271 , pp. 11930-11935
    • Mineo, C.1    James, G.L.2    Smart, E.J.3    Anderson, R.G.4
  • 18
    • 0034998678 scopus 로고    scopus 로고
    • Compartmentalization of Ras proteins
    • Prior, I. A., and Hancock, J. F. (2001) Compartmentalization of Ras proteins. J. Cell Sci. 114, 1603-1608
    • (2001) J. Cell Sci. , vol.114 , pp. 1603-1608
    • Prior, I.A.1    Hancock, J.F.2
  • 19
    • 75749150934 scopus 로고    scopus 로고
    • Ras membrane orientation and nanodomain localization generate isoform diversity
    • Abankwa, D., Gorfe, A. A., Inder, K., and Hancock, J. F. (2010) Ras membrane orientation and nanodomain localization generate isoform diversity. Proc. Natl. Acad. Sci. U.S.A. 107, 1130-1135
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1130-1135
    • Abankwa, D.1    Gorfe, A.A.2    Inder, K.3    Hancock, J.F.4
  • 20
    • 84861438588 scopus 로고    scopus 로고
    • Organization, dynamics, and segregation of Ras nanoclusters in membrane domains
    • Janosi, L., Li, Z., Hancock, J. F., and Gorfe, A. A. (2012) Organization, dynamics, and segregation of Ras nanoclusters in membrane domains. Proc. Natl. Acad. Sci. U.S.A. 109, 8097-8102
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 8097-8102
    • Janosi, L.1    Li, Z.2    Hancock, J.F.3    Gorfe, A.A.4
  • 21
    • 0037182579 scopus 로고    scopus 로고
    • Activated K-Ras and H-Ras display different interactions with saturable nonraft sites at the surface of live cells
    • Niv, H., Gutman, O., Kloog, Y., and Henis, Y. I. (2002) Activated K-Ras and H-Ras display different interactions with saturable nonraft sites at the surface of live cells. J. Cell Biol. 157, 865-872
    • (2002) J. Cell Biol. , vol.157 , pp. 865-872
    • Niv, H.1    Gutman, O.2    Kloog, Y.3    Henis, Y.I.4
  • 23
    • 0032516835 scopus 로고    scopus 로고
    • Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK)
    • Furuchi, T., and Anderson, R. G. (1998) Cholesterol depletion of caveolae causes hyperactivation of extracellular signal-related kinase (ERK). J. Biol. Chem. 273, 21099-21104
    • (1998) J. Biol. Chem. , vol.273 , pp. 21099-21104
    • Furuchi, T.1    Anderson, R.G.2
  • 25
    • 33644864788 scopus 로고    scopus 로고
    • Compartmentalized Ras/MAPK signaling
    • Mor, A., and Philips, M. R. (2006) Compartmentalized Ras/MAPK signaling. Annu. Rev. Immunol. 24, 771-800
    • (2006) Annu. Rev. Immunol. , vol.24 , pp. 771-800
    • Mor, A.1    Philips, M.R.2
  • 26
    • 1642382983 scopus 로고    scopus 로고
    • Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size
    • Denisov, I. G., Grinkova, Y. V., Lazarides, A. A., and Sligar, S. G. (2004) Directed self-assembly of monodisperse phospholipid bilayer Nanodiscs with controlled size. J. Am. Chem. Soc. 126, 3477-3487
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3477-3487
    • Denisov, I.G.1    Grinkova, Y.V.2    Lazarides, A.A.3    Sligar, S.G.4
  • 28
    • 84879628975 scopus 로고    scopus 로고
    • Application of reductive 13C-methylation of lysines to enhance the sensitivity of conven-tional NMR methods
    • Chavan, T. S., Abraham, S., and Gaponenko, V. (2013) Application of reductive 13C-methylation of lysines to enhance the sensitivity of conven-tional NMR methods. Molecules 18, 7103-7119
    • (2013) Molecules , vol.18 , pp. 7103-7119
    • Chavan, T.S.1    Abraham, S.2    Gaponenko, V.3
  • 34
    • 84859622200 scopus 로고    scopus 로고
    • Effects of point substitutions on the structure of toxic Alzheimer's β-amyloid channels: Atomic force microscopy and molecular dynamics simulations
    • Connelly, L., Jang, H., Arce, F. T., Ramachandran, S., Kagan, B. L., Nussinov, R., and Lal, R. (2012) Effects of point substitutions on the structure of toxic Alzheimer's β-amyloid channels: atomic force microscopy and molecular dynamics simulations. Biochemistry 51, 3031-3038
    • (2012) Biochemistry , vol.51 , pp. 3031-3038
    • Connelly, L.1    Jang, H.2    Arce, F.T.3    Ramachandran, S.4    Kagan, B.L.5    Nussinov, R.6    Lal, R.7
  • 35
    • 84856298593 scopus 로고    scopus 로고
    • Atomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: Relevance to the ion channel mechanism of AD pathology
    • Connelly, L., Jang, H., Arce, F. T., Capone, R., Kotler, S. A., Ramachandran, S., Kagan, B. L., Nussinov, R., and Lal, R. (2012) Atomic force microscopy and MD simulations reveal pore-like structures of all-D-enantiomer of Alzheimer's β-amyloid peptide: relevance to the ion channel mechanism of AD pathology. J. Phys. Chem. B. 116, 1728-1735
    • (2012) J. Phys. Chem. B. , vol.116 , pp. 1728-1735
    • Connelly, L.1    Jang, H.2    Arce, F.T.3    Capone, R.4    Kotler, S.A.5    Ramachandran, S.6    Kagan, B.L.7    Nussinov, R.8    Lal, R.9
  • 36
    • 84856262919 scopus 로고    scopus 로고
    • Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions
    • Capone, R., Jang, H., Kotler, S. A., Kagan, B. L., Nussinov, R., and Lal, R. (2012) Probing structural features of Alzheimer's amyloid-β pores in bilayers using site-specific amino acid substitutions. Biochemistry 51, 776-785
    • (2012) Biochemistry , vol.51 , pp. 776-785
    • Capone, R.1    Jang, H.2    Kotler, S.A.3    Kagan, B.L.4    Nussinov, R.5    Lal, R.6
  • 38
    • 77952960621 scopus 로고    scopus 로고
    • Antimicrobial protegrin-1 forms ion channels: Molecular dynamic simulation, atomic force microscopy, and electrical conductance studies
    • Capone, R., Mustata, M., Jang, H., Arce, F. T., Nussinov, R., and Lal, R. (2010) Antimicrobial protegrin-1 forms ion channels: molecular dynamic simulation, atomic force microscopy, and electrical conductance studies. Biophys. J. 98, 2644-2652
    • (2010) Biophys. J. , vol.98 , pp. 2644-2652
    • Capone, R.1    Mustata, M.2    Jang, H.3    Arce, F.T.4    Nussinov, R.5    Lal, R.6
  • 39
    • 58149311146 scopus 로고    scopus 로고
    • Models of toxic β-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic Alzheimer β-amyloid ion channels
    • Jang, H., Ma, B., Lal, R., and Nussinov, R. (2008) Models of toxic β-sheet channels of protegrin-1 suggest a common subunit organization motif shared with toxic Alzheimer β-amyloid ion channels. Biophys. J. 95, 4631-4642
    • (2008) Biophys. J. , vol.95 , pp. 4631-4642
    • Jang, H.1    Ma, B.2    Lal, R.3    Nussinov, R.4
  • 40
    • 44949233215 scopus 로고    scopus 로고
    • How to lose a kink and gain a helix: PH independent conformational changes of the fusion domains from influenza hemagglutinin in heterogeneous lipid bilayers
    • Jang, H., Michaud-Agrawal, N., Johnston, J. M., and Woolf, T. B. (2008) How to lose a kink and gain a helix: pH independent conformational changes of the fusion domains from influenza hemagglutinin in heterogeneous lipid bilayers. Proteins 72, 299-312
    • (2008) Proteins , vol.72 , pp. 299-312
    • Jang, H.1    Michaud-Agrawal, N.2    Johnston, J.M.3    Woolf, T.B.4
  • 41
    • 84902091498 scopus 로고    scopus 로고
    • Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs
    • Jang, H., Arce, F. T., Ramachandran, S., Kagan, B. L., Lal, R., and Nussinov, R. (2014) Disordered amyloidogenic peptides may insert into the membrane and assemble into common cyclic structural motifs. Chem. Soc. Rev. 43, 6750-6764
    • (2014) Chem. Soc. Rev. , vol.43 , pp. 6750-6764
    • Jang, H.1    Arce, F.T.2    Ramachandran, S.3    Kagan, B.L.4    Lal, R.5    Nussinov, R.6
  • 42
    • 0028020035 scopus 로고
    • Molecular dynamics simulation of the gramicidin channel in a phospholipid bilayer
    • Woolf, T. B., and Roux, B. (1994) Molecular dynamics simulation of the gramicidin channel in a phospholipid bilayer. Proc. Natl. Acad. Sci. U.S.A. 91, 11631-11635
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11631-11635
    • Woolf, T.B.1    Roux, B.2
  • 43
    • 0030038849 scopus 로고    scopus 로고
    • Structure, energetics, and dynamics of lipid-protein interactions: A molecular dynamics study of the gramicidin A channel in a DMPC bilayer
    • Woolf, T. B., and Roux, B. (1996) Structure, energetics, and dynamics of lipid-protein interactions: A molecular dynamics study of the gramicidin A channel in a DMPC bilayer. Proteins 24, 92-114
    • (1996) Proteins , vol.24 , pp. 92-114
    • Woolf, T.B.1    Roux, B.2
  • 44
    • 0024378918 scopus 로고
    • Hydration forces between phospholipid bilayers
    • Rand, R. P., and Parsegian, V. A. (1989) Hydration forces between phospholipid bilayers. Biochim. Biophys. Acta 988, 351-376
    • (1989) Biochim. Biophys. Acta , vol.988 , pp. 351-376
    • Rand, R.P.1    Parsegian, V.A.2
  • 45
    • 33646446451 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains
    • Kucerka, N., Tristram-Nagle, S., and Nagle, J. F. (2005) Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains. J. Membr. Biol. 208, 193-202
    • (2005) J. Membr. Biol. , vol.208 , pp. 193-202
    • Kucerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 48
    • 33751157933 scopus 로고
    • Solvent-induced forces between two hydrophilic groups
    • Durell, S. R., Brooks, B. R., and Bennaim, A. (1994) Solvent-induced forces between two hydrophilic groups. J. Phys. Chem. 98, 2198-2202
    • (1994) J. Phys. Chem. , vol.98 , pp. 2198-2202
    • Durell, S.R.1    Brooks, B.R.2    Bennaim, A.3
  • 50
    • 0035845497 scopus 로고    scopus 로고
    • Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers
    • Dietrich, C., Volovyk, Z. N., Levi, M., Thompson, N. L., and Jacobson, K. (2001) Partitioning of Thy-1, GM1, and cross-linked phospholipid analogs into lipid rafts reconstituted in supported model membrane monolayers. Proc. Natl. Acad. Sci. U.S.A. 98, 10642-10647
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 10642-10647
    • Dietrich, C.1    Volovyk, Z.N.2    Levi, M.3    Thompson, N.L.4    Jacobson, K.5
  • 51
    • 27144546396 scopus 로고    scopus 로고
    • Cholera toxin B-subunit prevents activation and proliferation of human CD4+ T cells by activation of a neutral sphingomyelinase in lipid rafts
    • Rouquette-Jazdanian, A. K., Foussat, A., Lamy, L., Pelassy, C., Lagadec, P., Breittmayer, J. P., and Aussel, C. (2005) Cholera toxin B-subunit prevents activation and proliferation of human CD4+ T cells by activation of a neutral sphingomyelinase in lipid rafts. J. Immunol. 175, 5637-5648
    • (2005) J. Immunol. , vol.175 , pp. 5637-5648
    • Rouquette-Jazdanian, A.K.1    Foussat, A.2    Lamy, L.3    Pelassy, C.4    Lagadec, P.5    Breittmayer, J.P.6    Aussel, C.7
  • 52
    • 0041494100 scopus 로고    scopus 로고
    • Lipid rafts: Bringing order to chaos
    • Pike, L. J. (2003) Lipid rafts: bringing order to chaos. J. Lipid Res. 44, 655-667
    • (2003) J. Lipid Res. , vol.44 , pp. 655-667
    • Pike, L.J.1
  • 54
    • 0036639438 scopus 로고    scopus 로고
    • Alterations in membrane-bound and cytoplasmic K-ras protein levels in mouse lung induced by treatment with lovastatin, cholestyramine, or niacin: Effects are highly mouse strain dependent
    • Calvert, R. J., Ramakrishna, G., Tepper, S., Diwan, B. A., Anderson, L. M., and Kritchevsky, D. (2002) Alterations in membrane-bound and cytoplasmic K-ras protein levels in mouse lung induced by treatment with lovastatin, cholestyramine, or niacin: effects are highly mouse strain dependent. Biochem. Pharmacol. 64, 41-48
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 41-48
    • Calvert, R.J.1    Ramakrishna, G.2    Tepper, S.3    Diwan, B.A.4    Anderson, L.M.5    Kritchevsky, D.6
  • 55
    • 2942668382 scopus 로고    scopus 로고
    • Investigation of temperature-induced phase transitions in DOPC and DPPC phospholipid bilayers using temperature-controlled scanning force microscopy
    • Leonenko, Z. V., Finot, E., Ma, H., Dahms, T. E., and Cramb, D. T. (2004) Investigation of temperature-induced phase transitions in DOPC and DPPC phospholipid bilayers using temperature-controlled scanning force microscopy. Biophys. J. 86, 3783-3793
    • (2004) Biophys. J. , vol.86 , pp. 3783-3793
    • Leonenko, Z.V.1    Finot, E.2    Ma, H.3    Dahms, T.E.4    Cramb, D.T.5
  • 56
    • 0027026591 scopus 로고
    • Protein prenylation: More than just glue?
    • Cox, A. D., and Der, C. J. (1992) Protein prenylation: more than just glue? Curr. Opin. Cell Biol. 4, 1008-1016
    • (1992) Curr. Opin. Cell Biol. , vol.4 , pp. 1008-1016
    • Cox, A.D.1    Der, C.J.2
  • 57
    • 70450188170 scopus 로고    scopus 로고
    • Protein lipid modifications in signaling and subcellular targeting
    • Sorek, N., Bloch, D., and Yalovsky, S. (2009) Protein lipid modifications in signaling and subcellular targeting. Curr. Opin. Plant Biol. 12, 714-720
    • (2009) Curr. Opin. Plant Biol. , vol.12 , pp. 714-720
    • Sorek, N.1    Bloch, D.2    Yalovsky, S.3
  • 58
    • 33750266831 scopus 로고    scopus 로고
    • Trafficking and signaling by fatty-acylated and prenylated proteins
    • Resh, M. D. (2006) Trafficking and signaling by fatty-acylated and prenylated proteins. Nat. Chem. Biol. 2, 584-590
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 584-590
    • Resh, M.D.1
  • 59
    • 23044507603 scopus 로고    scopus 로고
    • Role of the isoprenoid pathway in ras transforming activity, cytoskeleton organization, cell proliferation, and apoptosis
    • Bifulco, M. (2005) Role of the isoprenoid pathway in ras transforming activity, cytoskeleton organization, cell proliferation, and apoptosis. Life Sci. 77, 1740-1749
    • (2005) Life Sci. , vol.77 , pp. 1740-1749
    • Bifulco, M.1
  • 60
    • 0034062298 scopus 로고    scopus 로고
    • Low levels of Ypt protein prenylation cause vesicle polarization defects and thermosensitive growth that can be suppressed by genes involved in cell wall maintenance
    • Bialek-Wyrzykowska, U., Bauer, B. E., Wagner, W., Kohlwein, S. D., Schweyen, R. J., and Ragnini, A. (2000) Low levels of Ypt protein prenylation cause vesicle polarization defects and thermosensitive growth that can be suppressed by genes involved in cell wall maintenance. Mol. Microbiol. 35, 1295-1311
    • (2000) Mol. Microbiol. , vol.35 , pp. 1295-1311
    • Bialek-Wyrzykowska, U.1    Bauer, B.E.2    Wagner, W.3    Kohlwein, S.D.4    Schweyen, R.J.5    Ragnini, A.6
  • 61
    • 0346888680 scopus 로고    scopus 로고
    • Prenylation inhibitors: A novel class of antiviral agents
    • Einav, S., and Glenn, J. S. (2003) Prenylation inhibitors: a novel class of antiviral agents. J. Antimicrob. Chemother. 52, 883-886
    • (2003) J. Antimicrob. Chemother. , vol.52 , pp. 883-886
    • Einav, S.1    Glenn, J.S.2
  • 63
    • 69249219178 scopus 로고    scopus 로고
    • Targeting the mevalonate pathway for improved anticancer therapy
    • Fritz, G. (2009) Targeting the mevalonate pathway for improved anticancer therapy. Curr. Cancer Drug Targets 9, 626-638
    • (2009) Curr. Cancer Drug Targets , vol.9 , pp. 626-638
    • Fritz, G.1
  • 64
    • 0141924553 scopus 로고    scopus 로고
    • Anovel pleiotropic effect of statins: Prevention of cardiac hypertrophy by cholesterol-independent mechanisms
    • Nakagami, H., Jensen, K. S., and Liao, J. K. (2003)Anovel pleiotropic effect of statins: prevention of cardiac hypertrophy by cholesterol-independent mechanisms. Ann. Med. 35, 398-403
    • (2003) Ann. Med. , vol.35 , pp. 398-403
    • Nakagami, H.1    Jensen, K.S.2    Liao, J.K.3
  • 65
    • 33646777423 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications: CAAX modification and membrane targeting of Ras
    • Wright, L. P., and Philips, M. R. (2006) Thematic review series: lipid posttranslational modifications: CAAX modification and membrane targeting of Ras. J. Lipid Res. 47, 883-891
    • (2006) J. Lipid Res. , vol.47 , pp. 883-891
    • Wright, L.P.1    Philips, M.R.2
  • 66
    • 23344435930 scopus 로고    scopus 로고
    • Protein farnesyl transferase inhibitors for the treat-ment of malaria and African trypanosomiasis
    • Buckner, F. S., Eastman, R. T., Yokoyama, K., Gelb, M. H., and Van Voorhis, W. C. (2005) Protein farnesyl transferase inhibitors for the treat-ment of malaria and African trypanosomiasis. Curr. Opin. Investig. Drugs 6, 791-797
    • (2005) Curr. Opin. Investig. Drugs , vol.6 , pp. 791-797
    • Buckner, F.S.1    Eastman, R.T.2    Yokoyama, K.3    Gelb, M.H.4    Van Voorhis, W.C.5
  • 67
    • 33847190634 scopus 로고    scopus 로고
    • Current status and progresses made in malaria chemotherapy
    • Liñares, G. E., and Rodriguez, J. B. (2007) Current status and progresses made in malaria chemotherapy. Curr. Med. Chem. 14, 289-314
    • (2007) Curr. Med. Chem. , vol.14 , pp. 289-314
    • Liñares, G.E.1    Rodriguez, J.B.2
  • 68
    • 80053165077 scopus 로고    scopus 로고
    • A-type lamins and Hutchinson-Gilford progeria syndrome: Pathogenesis and therapy
    • Gonzalez, J. M., Pla, D., Perez-Sala, D., and Andres, V. (2011) A-type lamins and Hutchinson-Gilford progeria syndrome: pathogenesis and therapy. Front. Biosci. S3, 1133-1146
    • (2011) Front. Biosci. , vol.S3 , pp. 1133-1146
    • Gonzalez, J.M.1    Pla, D.2    Perez-Sala, D.3    Andres, V.4
  • 70
    • 38949093546 scopus 로고    scopus 로고
    • Inhibitors of chronically active ras: Potential for treatment of human malignancies. Recent Pat
    • Blum, R., Cox, A. D., and Kloog, Y. (2008) Inhibitors of chronically active ras: potential for treatment of human malignancies. Recent Pat. Anticancer Drug Discov. 3, 31-47
    • (2008) Anticancer Drug Discov , vol.3 , pp. 31-47
    • Blum, R.1    Cox, A.D.2    Kloog, Y.3
  • 71
    • 33845451653 scopus 로고    scopus 로고
    • Hydrophobic modifications of Ras proteins by isoprenoid groups and fatty acids: More than just membrane anchoring
    • Pechlivanis, M., and Kuhlmann, J. (2006) Hydrophobic modifications of Ras proteins by isoprenoid groups and fatty acids: more than just membrane anchoring. Biochim. Biophys. Acta 1764, 1914-1931
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 1914-1931
    • Pechlivanis, M.1    Kuhlmann, J.2
  • 72
    • 84881539880 scopus 로고    scopus 로고
    • Lessons from computer simulations of Ras proteins in solution and in membrane
    • Prakash, P., and Gorfe, A. A. (2013) Lessons from computer simulations of Ras proteins in solution and in membrane. Biochim. Biophys. Acta 1830, 5211-5218
    • (2013) Biochim. Biophys. Acta , vol.1830 , pp. 5211-5218
    • Prakash, P.1    Gorfe, A.A.2
  • 73
    • 33746858605 scopus 로고    scopus 로고
    • Insertion of lipidated Ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS)
    • Meister, A., Nicolini, C., Waldmann, H., Kuhlmann, J., Kerth, A., Winter, R., and Blume, A. (2006) Insertion of lipidated Ras proteins into lipid monolayers studied by infrared reflection absorption spectroscopy (IRRAS). Biophys. J. 91, 1388-1401
    • (2006) Biophys. J. , vol.91 , pp. 1388-1401
    • Meister, A.1    Nicolini, C.2    Waldmann, H.3    Kuhlmann, J.4    Kerth, A.5    Winter, R.6    Blume, A.7
  • 74
    • 0021528719 scopus 로고
    • Harvey murine sarcoma virus p21 ras protein: Biological and biochemical significance of the cysteine nearest the carboxy terminus
    • Willumsen, B. M., Norris, K., Papageorge, A. G., Hubbert, N. L., and Lowy, D. R. (1984) Harvey murine sarcoma virus p21 ras protein: biological and biochemical significance of the cysteine nearest the carboxy terminus. EMBO J. 3, 2581-2585
    • (1984) EMBO J. , vol.3 , pp. 2581-2585
    • Willumsen, B.M.1    Norris, K.2    Papageorge, A.G.3    Hubbert, N.L.4    Lowy, D.R.5
  • 76
    • 45549094796 scopus 로고    scopus 로고
    • Analysis of K-Ras phosphorylation, translocation, and induction of apoptosis
    • Quatela, S. E., Sung, P. J., Ahearn, I. M., Bivona, T. G., and Philips, M. R. (2008) Analysis of K-Ras phosphorylation, translocation, and induction of apoptosis. Methods Enzymol. 439, 87-102
    • (2008) Methods Enzymol. , vol.439 , pp. 87-102
    • Quatela, S.E.1    Sung, P.J.2    Ahearn, I.M.3    Bivona, T.G.4    Philips, M.R.5
  • 77
    • 34247346010 scopus 로고    scopus 로고
    • Electrical properties of plasma membrane modulate subcellular distribution of K-Ras
    • Gomez, G. A., and Daniotti, J. L. (2007) Electrical properties of plasma membrane modulate subcellular distribution of K-Ras. FEBS J. 274, 2210-2228
    • (2007) FEBS J. , vol.274 , pp. 2210-2228
    • Gomez, G.A.1    Daniotti, J.L.2
  • 79
    • 84924080511 scopus 로고    scopus 로고
    • Dynamic multiprotein assemblies shape the spatial structure of cell signaling
    • Nussinov, R., and Jang, H. (2014) Dynamic multiprotein assemblies shape the spatial structure of cell signaling. Prog. Biophys. Mol. Biol. 116, 158-164
    • (2014) Prog. Biophys. Mol. Biol. , vol.116 , pp. 158-164
    • Nussinov, R.1    Jang, H.2
  • 80
    • 84927036139 scopus 로고    scopus 로고
    • Oligomerization and nanocluster organization render specificity
    • Nussinov, R., Jang, H., and Tsai, C. J. (2014) Oligomerization and nanocluster organization render specificity. Biol. Rev. Camb. Philos. Soc. 10.1111/brv.12124
    • (2014) Biol. Rev. Camb. Philos. Soc.
    • Nussinov, R.1    Jang, H.2    Tsai, C.J.3
  • 81
    • 84881493915 scopus 로고    scopus 로고
    • The spatial structure of cell signaling systems
    • Nussinov, R. (2013) The spatial structure of cell signaling systems. Phys. Biol. 10, 045004
    • (2013) Phys. Biol. , vol.10 , pp. 045004
    • Nussinov, R.1
  • 84
    • 0029127725 scopus 로고
    • Binding of prenylated and polybasic peptides to membranes: Affinities and intervesicle exchange
    • Ghomashchi, F., Zhang, X., Liu, L., and Gelb, M. H. (1995) Binding of prenylated and polybasic peptides to membranes: affinities and intervesicle exchange. Biochemistry 34, 11910-11918
    • (1995) Biochemistry , vol.34 , pp. 11910-11918
    • Ghomashchi, F.1    Zhang, X.2    Liu, L.3    Gelb, M.H.4
  • 85
    • 33746943292 scopus 로고    scopus 로고
    • Nonconventional trafficking of Ras associated with Ras signal organization
    • Ashery, U., Yizhar, O., Rotblat, B., and Kloog, Y. (2006) Nonconventional trafficking of Ras associated with Ras signal organization. Traffic 7, 119-126
    • (2006) Traffic , vol.7 , pp. 119-126
    • Ashery, U.1    Yizhar, O.2    Rotblat, B.3    Kloog, Y.4
  • 86
    • 46149107301 scopus 로고    scopus 로고
    • Electrostatic interactions positively regulate K-Ras nanocluster formation and function
    • Plowman, S. J., Ariotti, N., Goodall, A., Parton, R. G., and Hancock, J. F. (2008) Electrostatic interactions positively regulate K-Ras nanocluster formation and function. Mol. Cell. Biol. 28, 4377-4385
    • (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
  • 90
    • 84885138277 scopus 로고    scopus 로고
    • Familial Alzheimer's disease Osaka mutant (ΔE22) δ-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment
    • Jang, H., Arce, F. T., Ramachandran, S., Kagan, B. L., Lal, R., and Nussinov, R. (2013) Familial Alzheimer's disease Osaka mutant (ΔE22) δ-barrels suggest an explanation for the different Aβ1-40/42 preferred conformational states observed by experiment. J. Phys. Chem. B 117, 11518-11529
    • (2013) J. Phys. Chem. B , vol.117 , pp. 11518-11529
    • Jang, H.1    Arce, F.T.2    Ramachandran, S.3    Kagan, B.L.4    Lal, R.5    Nussinov, R.6
  • 91
    • 3042730827 scopus 로고    scopus 로고
    • How environment supports a state: Molecular dynamics simulations of two states in bacteriorhodopsin suggest lipid and water compensation
    • Jang, H., Crozier, P. S., Stevens, M. J., and Woolf, T. B. (2004) How environment supports a state: molecular dynamics simulations of two states in bacteriorhodopsin suggest lipid and water compensation. Biophys. J. 87, 129-145
    • (2004) Biophys. J. , vol.87 , pp. 129-145
    • Jang, H.1    Crozier, P.S.2    Stevens, M.J.3    Woolf, T.B.4


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