메뉴 건너뛰기




Volumn 23, Issue 7, 2015, Pages 1325-1335

GTP-Dependent K-Ras Dimerization

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; GLOBULAR PROTEIN; GUANOSINE TRIPHOSPHATE; HOMODIMER; ISOPROTEIN; K RAS PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN; RAF PROTEIN; KRAS PROTEIN, HUMAN; PROTEIN BINDING; PROTEIN P21;

EID: 84936847680     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2015.04.019     Document Type: Article
Times cited : (174)

References (52)
  • 1
    • 75749150934 scopus 로고    scopus 로고
    • Ras membrane orientation and nanodomain localization generate isoform diversity
    • D. Abankwa, A.A. Gorfe, K. Inder, and J.F. Hancock Ras membrane orientation and nanodomain localization generate isoform diversity Proc. Natl. Acad. Sci. USA 107 2010 1130 1135
    • (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
  • 2
    • 77955417069 scopus 로고    scopus 로고
    • Expression, purification, and characterization of soluble K-Ras4B for structural analysis
    • S.J. Abraham, I. Muhamed, R. Nolet, F. Yeung, and V. Gaponenko Expression, purification, and characterization of soluble K-Ras4B for structural analysis Protein Expr. Purif. 73 2010 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
  • 3
    • 84862588440 scopus 로고    scopus 로고
    • Enriching the human apoptosis pathway by predicting the structures of protein-protein complexes
    • S.E. Acuner Ozbabacan, O. Keskin, R. Nussinov, and A. Gursoy Enriching the human apoptosis pathway by predicting the structures of protein-protein complexes J. Struct. Biol. 179 2012 338 346
    • (2012) J. Struct. Biol. , vol.179 , pp. 338-346
    • Acuner Ozbabacan, S.E.1    Keskin, O.2    Nussinov, R.3    Gursoy, A.4
  • 4
    • 84898459926 scopus 로고    scopus 로고
    • (19)F NMR reveals multiple conformations at the dimer interface of the nonstructural protein 1 effector domain from influenza A virus
    • J.M. Aramini, K. Hamilton, L.C. Ma, G.V. Swapna, P.G. Leonard, J.E. Ladbury, R.M. Krug, and G.T. Montelione (19)F NMR reveals multiple conformations at the dimer interface of the nonstructural protein 1 effector domain from influenza A virus Structure 22 2014 515 525
    • (2014) Structure , vol.22 , pp. 515-525
    • Aramini, J.M.1    Hamilton, K.2    Ma, L.C.3    Swapna, G.V.4    Leonard, P.G.5    Ladbury, J.E.6    Krug, R.M.7    Montelione, G.T.8
  • 5
    • 20844454090 scopus 로고    scopus 로고
    • Prediction of protein-protein interactions by combining structure and sequence conservation in protein interfaces
    • A.S. Aytuna, A. Gursoy, and O. Keskin Prediction of protein-protein interactions by combining structure and sequence conservation in protein interfaces Bioinformatics 21 2005 2850 2855
    • (2005) Bioinformatics , vol.21 , pp. 2850-2855
    • Aytuna, A.S.1    Gursoy, A.2    Keskin, O.3
  • 7
    • 79960055459 scopus 로고    scopus 로고
    • RAS interaction with PI3K: more than just another effector pathway
    • E. Castellano, and J. Downward RAS interaction with PI3K: more than just another effector pathway Genes Cancer 2 2011 261 274
    • (2011) Genes Cancer , vol.2 , pp. 261-274
    • Castellano, E.1    Downward, J.2
  • 9
    • 84879628975 scopus 로고    scopus 로고
    • Application of reductive (1)(3)C-methylation of lysines to enhance the sensitivity of conventional NMR methods
    • T.S. Chavan, S. Abraham, and V. Gaponenko Application of reductive (1)(3)C-methylation of lysines to enhance the sensitivity of conventional NMR methods Molecules 18 2013 7103 7119
    • (2013) Molecules , vol.18 , pp. 7103-7119
    • Chavan, T.S.1    Abraham, S.2    Gaponenko, V.3
  • 13
    • 84887553103 scopus 로고    scopus 로고
    • The importance of Raf dimerization in cell signaling
    • A.K. Freeman, D.A. Ritt, and D.K. Morrison The importance of Raf dimerization in cell signaling Small GTPases 4 2013 180 185
    • (2013) Small GTPases , vol.4 , pp. 180-185
    • Freeman, A.K.1    Ritt, D.A.2    Morrison, D.K.3
  • 15
    • 0025013547 scopus 로고
    • A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane
    • J.F. Hancock, H. Paterson, and C.J. Marshall A polybasic domain or palmitoylation is required in addition to the CAAX motif to localize p21ras to the plasma membrane Cell 63 1990 133 139
    • (1990) Cell , vol.63 , pp. 133-139
    • Hancock, J.F.1    Paterson, H.2    Marshall, C.J.3
  • 17
    • 0034635502 scopus 로고    scopus 로고
    • Formation of the Ras dimer is essential for Raf-1 activation
    • K. Inouye, S. Mizutani, H. Koide, and Y. Kaziro Formation of the Ras dimer is essential for Raf-1 activation J. Biol. Chem. 275 2000 3737 3740
    • (2000) J. Biol. Chem. , vol.275 , pp. 3737-3740
    • Inouye, K.1    Mizutani, S.2    Koide, H.3    Kaziro, Y.4
  • 20
    • 84856657449 scopus 로고    scopus 로고
    • Human proteome-scale structural modeling of E2-E3 interactions exploiting interface motifs
    • G. Kar, O. Keskin, R. Nussinov, and A. Gursoy Human proteome-scale structural modeling of E2-E3 interactions exploiting interface motifs J. Proteome Res. 11 2012 1196 1207
    • (2012) J. Proteome Res. , vol.11 , pp. 1196-1207
    • Kar, G.1    Keskin, O.2    Nussinov, R.3    Gursoy, A.4
  • 22
    • 1842507022 scopus 로고    scopus 로고
    • A new, structurally nonredundant, diverse data set of protein-protein interfaces and its implications
    • O. Keskin, C.J. Tsai, H. Wolfson, and R. Nussinov A new, structurally nonredundant, diverse data set of protein-protein interfaces and its implications Protein Sci. 13 2004 1043 1055
    • (2004) Protein Sci. , vol.13 , pp. 1043-1055
    • Keskin, O.1    Tsai, C.J.2    Wolfson, H.3    Nussinov, R.4
  • 23
    • 43149092276 scopus 로고    scopus 로고
    • Principles of protein-protein interactions: what are the preferred ways for proteins to interact?
    • O. Keskin, A. Gursoy, B. Ma, and R. Nussinov Principles of protein-protein interactions: what are the preferred ways for proteins to interact? Chem. Rev. 108 2008 1225 1244
    • (2008) Chem. Rev. , vol.108 , pp. 1225-1244
    • Keskin, O.1    Gursoy, A.2    Ma, B.3    Nussinov, R.4
  • 24
    • 0034667593 scopus 로고    scopus 로고
    • Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions
    • W. Kolch Meaningful relationships: the regulation of the Ras/Raf/MEK/ERK pathway by protein interactions Biochem. J. 351 2000 289 305
    • (2000) Biochem. J. , vol.351 , pp. 289-305
    • Kolch, W.1
  • 28
    • 77951232176 scopus 로고    scopus 로고
    • FiberDock: flexible induced-fit backbone refinement in molecular docking
    • E. Mashiach, R. Nussinov, and H.J. Wolfson FiberDock: flexible induced-fit backbone refinement in molecular docking Proteins 78 2010 1503 1519
    • (2010) Proteins , vol.78 , pp. 1503-1519
    • Mashiach, E.1    Nussinov, R.2    Wolfson, H.J.3
  • 29
    • 22744445886 scopus 로고    scopus 로고
    • Signaling interplay in Ras superfamily function
    • N. Mitin, K.L. Rossman, and C.J. Der Signaling interplay in Ras superfamily function Curr. Biol. 15 2005 R563 R574
    • (2005) Curr. Biol. , vol.15 , pp. R563-R574
    • Mitin, N.1    Rossman, K.L.2    Der, C.J.3
  • 32
    • 84881493915 scopus 로고    scopus 로고
    • The spatial structure of cell signaling systems
    • R. Nussinov The spatial structure of cell signaling systems Phys. Biol. 10 2013 045004
    • (2013) Phys. Biol. , vol.10 , pp. 045004
    • Nussinov, R.1
  • 33
    • 84876296757 scopus 로고    scopus 로고
    • A broad view of scaffolding suggests that scaffolding proteins can actively control regulation and signaling of multienzyme complexes through allostery
    • R. Nussinov, B. Ma, and C.J. Tsai A broad view of scaffolding suggests that scaffolding proteins can actively control regulation and signaling of multienzyme complexes through allostery Biochim. Biophys. Acta 1834 2013 820 829
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 820-829
    • Nussinov, R.1    Ma, B.2    Tsai, C.J.3
  • 36
    • 84865020706 scopus 로고    scopus 로고
    • Thermodynamics of the GTP-GDP-operated conformational switch of selenocysteine-specific translation factor SelB
    • A. Paleskava, A.L. Konevega, and M.V. Rodnina Thermodynamics of the GTP-GDP-operated conformational switch of selenocysteine-specific translation factor SelB J. Biol. Chem. 287 2012 27906 27912
    • (2012) J. Biol. Chem. , vol.287 , pp. 27906-27912
    • Paleskava, A.1    Konevega, A.L.2    Rodnina, M.V.3
  • 37
    • 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
    • S.J. Plowman, C. Muncke, R.G. Parton, and J.F. Hancock 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 102 2005 15500 15505
    • (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
  • 38
    • 84861147473 scopus 로고    scopus 로고
    • A comprehensive survey of Ras mutations in cancer
    • I.A. Prior, P.D. Lewis, and C. Mattos A comprehensive survey of Ras mutations in cancer Cancer Res. 72 2012 2457 2467
    • (2012) Cancer Res. , vol.72 , pp. 2457-2467
    • Prior, I.A.1    Lewis, P.D.2    Mattos, C.3
  • 39
  • 40
    • 7444245100 scopus 로고    scopus 로고
    • Renewing the conspiracy theory debate: does Raf function alone to mediate Ras oncogenesis?
    • G.A. Repasky, E.J. Chenette, and C.J. Der Renewing the conspiracy theory debate: does Raf function alone to mediate Ras oncogenesis? Trends Cell Biol. 14 2004 639 647
    • (2004) Trends Cell Biol. , vol.14 , pp. 639-647
    • Repasky, G.A.1    Chenette, E.J.2    Der, C.J.3
  • 42
    • 84900564509 scopus 로고    scopus 로고
    • Dimerization opens new avenues into Ras signaling research
    • E. Santos Dimerization opens new avenues into Ras signaling research Sci. Signal. 7 2014 pe12
    • (2014) Sci. Signal. , vol.7 , pp. pe12
    • Santos, E.1
  • 44
    • 78650054960 scopus 로고    scopus 로고
    • Conformational states of human rat sarcoma (Ras) protein complexed with its natural ligand GTP and their role for effector interaction and GTP hydrolysis
    • M. Spoerner, C. Hozsa, J.A. Poetzl, K. Reiss, P. Ganser, M. Geyer, and H.R. Kalbitzer Conformational states of human rat sarcoma (Ras) protein complexed with its natural ligand GTP and their role for effector interaction and GTP hydrolysis J. Biol. Chem. 285 2010 39768 39778
    • (2010) J. Biol. Chem. , vol.285 , pp. 39768-39778
    • Spoerner, M.1    Hozsa, C.2    Poetzl, J.A.3    Reiss, K.4    Ganser, P.5    Geyer, M.6    Kalbitzer, H.R.7
  • 46
    • 84886745490 scopus 로고    scopus 로고
    • US National Cancer Institute's new Ras project targets an old foe
    • H. Thompson US National Cancer Institute's new Ras project targets an old foe Nat. Med. 19 2013 949 950
    • (2013) Nat. Med. , vol.19 , pp. 949-950
    • Thompson, H.1
  • 47
    • 84896353876 scopus 로고    scopus 로고
    • The free energy landscape in translational science: how can somatic mutations result in constitutive oncogenic activation?
    • C.J. Tsai, and R. Nussinov The free energy landscape in translational science: how can somatic mutations result in constitutive oncogenic activation? Phys. Chem. Chem. Phys. 16 2014 6332 6341
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , pp. 6332-6341
    • Tsai, C.J.1    Nussinov, R.2
  • 48
    • 0029988383 scopus 로고    scopus 로고
    • Protein-protein interfaces: architectures and interactions in protein-protein interfaces and in protein cores. Their similarities and differences
    • C.J. Tsai, S.L. Lin, H.J. Wolfson, and R. Nussinov Protein-protein interfaces: architectures and interactions in protein-protein interfaces and in protein cores. Their similarities and differences Crit. Rev. Biochem. Mol. Biol. 31 1996 127 152
    • (1996) Crit. Rev. Biochem. Mol. Biol. , vol.31 , pp. 127-152
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 49
    • 77954294794 scopus 로고    scopus 로고
    • HotPoint: hot spot prediction server for protein interfaces
    • N. Tuncbag, O. Keskin, and A. Gursoy HotPoint: hot spot prediction server for protein interfaces Nucleic Acids Res. 38 2010 W402 W406
    • (2010) Nucleic Acids Res. , vol.38 , pp. W402-W406
    • Tuncbag, N.1    Keskin, O.2    Gursoy, A.3
  • 50
    • 80052411919 scopus 로고    scopus 로고
    • Predicting protein-protein interactions on a proteome scale by matching evolutionary and structural similarities at interfaces using PRISM
    • N. Tuncbag, A. Gursoy, R. Nussinov, and O. Keskin Predicting protein-protein interactions on a proteome scale by matching evolutionary and structural similarities at interfaces using PRISM Nat. Protoc. 6 2011 1341 1354
    • (2011) Nat. Protoc. , vol.6 , pp. 1341-1354
    • Tuncbag, N.1    Gursoy, A.2    Nussinov, R.3    Keskin, O.4
  • 51
    • 84857790849 scopus 로고    scopus 로고
    • Fast and accurate modeling of protein-protein interactions by combining template-interface-based docking with flexible refinement
    • N. Tuncbag, O. Keskin, R. Nussinov, and A. Gursoy Fast and accurate modeling of protein-protein interactions by combining template-interface-based docking with flexible refinement Proteins 80 2012 1239 1249
    • (2012) Proteins , vol.80 , pp. 1239-1249
    • Tuncbag, N.1    Keskin, O.2    Nussinov, R.3    Gursoy, A.4
  • 52
    • 0032474838 scopus 로고    scopus 로고
    • A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity
    • G. Tzivion, Z. Luo, and J. Avruch A dimeric 14-3-3 protein is an essential cofactor for Raf kinase activity Nature 394 1998 88 92
    • (1998) Nature , vol.394 , pp. 88-92
    • Tzivion, G.1    Luo, Z.2    Avruch, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.