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Volumn 4, Issue 3, 2008, Pages 213-222

RasGAPs: A crucial regulator of extracellular stimuli for homeostasis of cellular functions

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MUS;

EID: 39449114738     PISSN: 1742206X     EISSN: 17422051     Source Type: Journal    
DOI: 10.1039/b716357f     Document Type: Article
Times cited : (21)

References (99)
  • 1
    • 0037075886 scopus 로고    scopus 로고
    • GTPase activating proteins: Critical regulators of intracellular signaling
    • -45
    • S. Donovan K. M. Shannon G. Bollag GTPase activating proteins: critical regulators of intracellular signaling Biochim. Biophys. Acta 2002 1602 1 23 45
    • (2002) Biochim. Biophys. Acta , vol.1602 , Issue.1 , pp. 23
    • Donovan, S.1    Shannon, K.M.2    Bollag, G.3
  • 2
    • 3042796979 scopus 로고    scopus 로고
    • GAP control: Regulating the regulators of small GTPases
    • -85
    • A. Bernards J. Settleman GAP control: regulating the regulators of small GTPases Trends Cell Biol. 2004 14 7 377 85
    • (2004) Trends Cell Biol. , vol.14 , Issue.7 , pp. 377
    • Bernards, A.1    Settleman, J.2
  • 3
    • 25444528729 scopus 로고    scopus 로고
    • The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits
    • -66
    • D. P. Siderovski F. S. Willard The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits Int. J. Biol. Sci. 2005 1 2 51 66
    • (2005) Int. J. Biol. Sci. , vol.1 , Issue.2 , pp. 51
    • Siderovski, D.P.1    Willard, F.S.2
  • 4
    • 33645769516 scopus 로고    scopus 로고
    • Comparative and evolutionary analysis of genes encoding small GTPases and their activating proteins in eukaryotic genomes
    • -51
    • S. Y. Jiang S. Ramachandran Comparative and evolutionary analysis of genes encoding small GTPases and their activating proteins in eukaryotic genomes Physiol. Genomics 2006 24 3 235 51
    • (2006) Physiol. Genomics , vol.24 , Issue.3 , pp. 235
    • Jiang, S.Y.1    Ramachandran, S.2
  • 5
    • 13744265036 scopus 로고
    • Signal transduction system for growth factor receptors associated with tyrosine kinase activity: Epidermal growth factor receptor signaling and its regulation
    • -32
    • S. Iwashita M. Kobayashi Signal transduction system for growth factor receptors associated with tyrosine kinase activity: epidermal growth factor receptor signaling and its regulation Cell. Signalling 1992 4 2 123 32
    • (1992) Cell. Signalling , vol.4 , Issue.2 , pp. 123
    • Iwashita, S.1    Kobayashi, M.2
  • 6
    • 0142252552 scopus 로고    scopus 로고
    • Analysis of the small GTPase gene superfamily of Arabidopsis
    • -208
    • V. Vernoud A. C. Horton Z. Yang E. Nielsen Analysis of the small GTPase gene superfamily of Arabidopsis Plant Physiol. 2003 131 3 1191 208
    • (2003) Plant Physiol. , vol.131 , Issue.3 , pp. 1191
    • Vernoud, V.1    Horton, A.C.2    Yang, Z.3    Nielsen, E.4
  • 9
    • 0032937404 scopus 로고    scopus 로고
    • Modulation of the immune response and tumor growth by activated Ras
    • -13
    • S. Weijzen M. P. Velders W. M. Kast Modulation of the immune response and tumor growth by activated Ras Leukemia 1999 13 4 502 13
    • (1999) Leukemia , vol.13 , Issue.4 , pp. 502
    • Weijzen, S.1    Velders, M.P.2    Kast, W.M.3
  • 10
    • 0023619575 scopus 로고
    • A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants
    • -5
    • M. Trahey F. McCormick A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants Science 1987 238 4826 542 5
    • (1987) Science , vol.238 , Issue.4826 , pp. 542
    • Trahey, M.1    McCormick, F.2
  • 11
    • 0025765803 scopus 로고
    • SH2 and SH3 domains: Elements that control interactions of cytoplasmic signaling proteins
    • -74
    • C. A. Koch D. Anderson M. F. Moran C. Ellis T. Pawson SH2 and SH3 domains: elements that control interactions of cytoplasmic signaling proteins Science 1991 252 5006 668 74
    • (1991) Science , vol.252 , Issue.5006 , pp. 668
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 12
    • 0027339729 scopus 로고
    • Identification of the SH3 domain of GAP as an essential sequence for Ras-GAP-mediated signaling
    • -8
    • M. Duchesne F. Schweighoffer F. Parker F. Clerc Y. Frobert M. N. Thang B. Tocque Identification of the SH3 domain of GAP as an essential sequence for Ras-GAP-mediated signaling Science 1993 259 5094 525 8
    • (1993) Science , vol.259 , Issue.5094 , pp. 525
    • Duchesne, M.1    Schweighoffer, F.2    Parker, F.3    Clerc, F.4    Frobert, Y.5    Thang, M.N.6    Tocque, B.7
  • 13
    • 0025965048 scopus 로고
    • IRA2, an upstream negative regulator of RAS in yeast, is a RAS GTPase-activating protein
    • -72
    • K. Tanaka B. K. Lin D. R. Wood F. Tamanoi IRA2, an upstream negative regulator of RAS in yeast, is a RAS GTPase-activating protein Proc. Natl. Acad. Sci. U. S. A. 1991 88 2 468 72
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , Issue.2 , pp. 468
    • Tanaka, K.1    Lin, B.K.2    Wood, D.R.3    Tamanoi, F.4
  • 14
    • 0026588783 scopus 로고
    • A putative Ras GTPase activating protein acts as a negative regulator of signaling by the Sevenless receptor tyrosine kinase
    • -19
    • U. Gaul G. Mardon G. M. Rubin A putative Ras GTPase activating protein acts as a negative regulator of signaling by the Sevenless receptor tyrosine kinase Cell 1992 68 6 1007 19
    • (1992) Cell , vol.68 , Issue.6 , pp. 1007
    • Gaul, U.1    Mardon, G.2    Rubin, G.M.3
  • 15
    • 0026528368 scopus 로고
    • Abnormal regulation of mammalian p21ras contributes to malignant tumor growth in von Recklinghausen (type 1) neurofibromatosis
    • -73
    • J. E. DeClue A. G. Papageorge J. A. Fletcher S. R. Diehl N. Ratner W. C. Vass D. R. Lowy Abnormal regulation of mammalian p21ras contributes to malignant tumor growth in von Recklinghausen (type 1) neurofibromatosis Cell 1992 69 2 265 73
    • (1992) Cell , vol.69 , Issue.2 , pp. 265
    • Declue, J.E.1    Papageorge, A.G.2    Fletcher, J.A.3    Diehl, S.R.4    Ratner, N.5    Vass, W.C.6    Lowy, D.R.7
  • 16
    • 14044272770 scopus 로고    scopus 로고
    • A novel role for Gab1 and SHP2 in epidermal growth factor-induced Ras activation
    • -60
    • A. Montagner A. Yart M. Dance B. Perret J. P. Salles P. Raynal A novel role for Gab1 and SHP2 in epidermal growth factor-induced Ras activation J. Biol. Chem. 2005 280 7 5350 60
    • (2005) J. Biol. Chem. , vol.280 , Issue.7 , pp. 5350
    • Montagner, A.1    Yart, A.2    Dance, M.3    Perret, B.4    Salles, J.P.5    Raynal, P.6
  • 19
    • 0033408321 scopus 로고    scopus 로고
    • Platelet-derived growth factor-dependent association of the GTPase-activating protein of Ras and Src
    • -26
    • T. K. Schlesinger K. A. DeMali G. L. Johnson A. Kazlauskas Platelet-derived growth factor-dependent association of the GTPase-activating protein of Ras and Src Biochem. J. 1999 344 2 519 26
    • (1999) Biochem. J. , vol.344 , Issue.2 , pp. 519
    • Schlesinger, T.K.1    Demali, K.A.2    Johnson, G.L.3    Kazlauskas, A.4
  • 21
    • 0031724591 scopus 로고    scopus 로고
    • Phosphotyrosine (p-Tyr)-dependent and -independent mechanisms of p190 RhoGAP-p120 RasGAP interaction: Tyr 1105 of p190, a substrate for c-Src, is the sole p-Tyr mediator of complex formation
    • -63
    • R. W. Roof M. D. Haskell B. D. Dukes N. Sherman M. Kinter S. J. Parsons Phosphotyrosine (p-Tyr)-dependent and -independent mechanisms of p190 RhoGAP-p120 RasGAP interaction: Tyr 1105 of p190, a substrate for c-Src, is the sole p-Tyr mediator of complex formation Mol. Cell. Biol. 1998 18 12 7052 63
    • (1998) Mol. Cell. Biol. , vol.18 , Issue.12 , pp. 7052
    • Roof, R.W.1    Haskell, M.D.2    Dukes, B.D.3    Sherman, N.4    Kinter, M.5    Parsons, S.J.6
  • 22
    • 33750527971 scopus 로고    scopus 로고
    • Integrin signaling through Arg activates p190RhoGAP by promoting its binding to p120RasGAP and recruitment to the membrane
    • -36
    • W. D. Bradley S. E. Hernandez J. Settleman A. J. Koleske Integrin signaling through Arg activates p190RhoGAP by promoting its binding to p120RasGAP and recruitment to the membrane Mol. Biol. Cell 2006 17 11 4827 36
    • (2006) Mol. Biol. Cell , vol.17 , Issue.11 , pp. 4827
    • Bradley, W.D.1    Hernandez, S.E.2    Settleman, J.3    Koleske, A.J.4
  • 23
    • 0032560744 scopus 로고    scopus 로고
    • Rapid recruitment of p120RasGAP and its associated protein, p190RhoGAP, to the cytoskeleton during integrin mediated cell-substrate interaction
    • -81
    • S. V. Sharma Rapid recruitment of p120RasGAP and its associated protein, p190RhoGAP, to the cytoskeleton during integrin mediated cell-substrate interaction Oncogene 1998 17 3 271 81
    • (1998) Oncogene , vol.17 , Issue.3 , pp. 271
    • Sharma, S.V.1
  • 24
    • 0038054300 scopus 로고    scopus 로고
    • Structural fingerprints of the Ras-GTPase activating proteins neurofibromin and p120GAP
    • -710
    • M. R. Ahmadian C. Kiel P. Stege K. Scheffzek Structural fingerprints of the Ras-GTPase activating proteins neurofibromin and p120GAP J. Mol. Biol. 2003 329 4 699 710
    • (2003) J. Mol. Biol. , vol.329 , Issue.4 , pp. 699
    • Ahmadian, M.R.1    Kiel, C.2    Stege, P.3    Scheffzek, K.4
  • 26
    • 0028822429 scopus 로고
    • A conserved region of c-Ha-Ras is required for efficient GTPase stimulation by GTPase activating protein but not neurofibromin
    • -21
    • J. Yoder-Hill M. Golubic D. W. Stacey A conserved region of c-Ha-Ras is required for efficient GTPase stimulation by GTPase activating protein but not neurofibromin J. Biol. Chem. 1995 270 46 27615 21
    • (1995) J. Biol. Chem. , vol.270 , Issue.46 , pp. 27615
    • Yoder-Hill, J.1    Golubic, M.2    Stacey, D.W.3
  • 27
    • 0030798170 scopus 로고    scopus 로고
    • Activation of R-Ras GTPase by GTPase-activating proteins for Ras, Gap1m, and p120GAP
    • -32
    • S. Li S. Nakamura S. Hattori Activation of R-Ras GTPase by GTPase-activating proteins for Ras, Gap1m, and p120GAP J. Biol. Chem. 1997 272 31 19328 32
    • (1997) J. Biol. Chem. , vol.272 , Issue.31 , pp. 19328
    • Li, S.1    Nakamura, S.2    Hattori, S.3
  • 28
    • 19444387096 scopus 로고    scopus 로고
    • RASA1: Variable phenotype with capillary and arteriovenous malformations
    • -9
    • L. M. Boon J. B. Mulliken M. Vikkula RASA1: variable phenotype with capillary and arteriovenous malformations Curr. Opin. Genet. Dev. 2005 15 3 265 9
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , Issue.3 , pp. 265
    • Boon, L.M.1    Mulliken, J.B.2    Vikkula, M.3
  • 32
  • 33
    • 0031832234 scopus 로고    scopus 로고
    • A novel phosphorylation-dependent RNase activity of GAP-SH3 binding protein: A potential link between signal transduction and RNA stability
    • -65
    • I. E. Gallouzi F. Parker K. Chebli F. Maurier E. Labourier I. Barlat J. P. Capony B. Tocque J. Tazi A novel phosphorylation-dependent RNase activity of GAP-SH3 binding protein: a potential link between signal transduction and RNA stability Mol. Cell. Biol. 1998 18 7 3956 65
    • (1998) Mol. Cell. Biol. , vol.18 , Issue.7 , pp. 3956
    • Gallouzi, I.E.1    Parker, F.2    Chebli, K.3    Maurier, F.4    Labourier, E.5    Barlat, I.6    Capony, J.P.7    Tocque, B.8    Tazi, J.9
  • 35
    • 0037189527 scopus 로고    scopus 로고
    • Identification of Aurora kinases as RasGAP Src homology 3 domain-binding proteins
    • -6
    • V. Gigoux S. L'Hoste F. Raynaud J. Camonis C. Garbay Identification of Aurora kinases as RasGAP Src homology 3 domain-binding proteins J. Biol. Chem. 2002 277 26 23742 6
    • (2002) J. Biol. Chem. , vol.277 , Issue.26 , pp. 23742
    • Gigoux, V.1    L'Hoste, S.2    Raynaud, F.3    Camonis, J.4    Garbay, C.5
  • 36
    • 0031030580 scopus 로고    scopus 로고
    • A role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domain
    • -32
    • I. Barlat F. Maurier M. Duchesne E. Guitard B. Tocque F. Schweighoffer A role for Sam68 in cell cycle progression antagonized by a spliced variant within the KH domain J. Biol. Chem. 1997 272 6 3129 32
    • (1997) J. Biol. Chem. , vol.272 , Issue.6 , pp. 3129
    • Barlat, I.1    Maurier, F.2    Duchesne, M.3    Guitard, E.4    Tocque, B.5    Schweighoffer, F.6
  • 38
    • 0032958429 scopus 로고    scopus 로고
    • Cleavage of RasGAP and phosphorylation of mitogen-activated protein kinase in the course of coxsackievirus B3 replication
    • -94
    • M. Huber K. A. Watson H. C. Selinka C. M. Carthy K. Klingel B. M. McManus R. Kandolf Cleavage of RasGAP and phosphorylation of mitogen-activated protein kinase in the course of coxsackievirus B3 replication J. Virol. 1999 73 5 3587 94
    • (1999) J. Virol. , vol.73 , Issue.5 , pp. 3587
    • Huber, M.1    Watson, K.A.2    Selinka, H.C.3    Carthy, C.M.4    Klingel, K.5    McManus, B.M.6    Kandolf, R.7
  • 39
    • 13944267564 scopus 로고    scopus 로고
    • Sam68 is absolutely required for Rev function and HIV-1 production
    • -9
    • S. Modem K. R. Badri T. C. Holland T. R. Reddy Sam68 is absolutely required for Rev function and HIV-1 production Nucleic Acids Res. 2005 33 3 873 9
    • (2005) Nucleic Acids Res. , vol.33 , Issue.3 , pp. 873
    • Modem, S.1    Badri, K.R.2    Holland, T.C.3    Reddy, T.R.4
  • 40
    • 0032530286 scopus 로고    scopus 로고
    • Sam68 association with p120GAP in CD4+ T cells is dependent on CD4 molecule expression
    • -803
    • N. Jabado S. Jauliac A. Pallier F. Bernard A. Fischer C. Hivroz Sam68 association with p120GAP in CD4+ T cells is dependent on CD4 molecule expression J. Immunol. 1998 161 6 2798 803
    • (1998) J. Immunol. , vol.161 , Issue.6 , pp. 2798
    • Jabado, N.1    Jauliac, S.2    Pallier, A.3    Bernard, F.4    Fischer, A.5    Hivroz, C.6
  • 41
    • 1842581856 scopus 로고    scopus 로고
    • Ras GTPase-activating protein binds to Akt and is required for its activation
    • -9
    • Y. Yue J. Lypowy N. Hedhli M. Abdellatif Ras GTPase-activating protein binds to Akt and is required for its activation J. Biol. Chem. 2004 279 13 12883 9
    • (2004) J. Biol. Chem. , vol.279 , Issue.13 , pp. 12883
    • Yue, Y.1    Lypowy, J.2    Hedhli, N.3    Abdellatif, M.4
  • 42
    • 0032549670 scopus 로고    scopus 로고
    • Caspase-dependent cleavage of signaling proteins during apoptosis, A turn-off mechanism for anti-apoptotic signals
    • -7
    • C. Widmann S. Gibson G. L. Johnson Caspase-dependent cleavage of signaling proteins during apoptosis, A turn-off mechanism for anti-apoptotic signals J. Biol. Chem. 1998 273 12 7141 7
    • (1998) J. Biol. Chem. , vol.273 , Issue.12 , pp. 7141
    • Widmann, C.1    Gibson, S.2    Johnson, G.L.3
  • 43
    • 3042733029 scopus 로고    scopus 로고
    • RasGTPase-activating protein is a target of caspases in spontaneous apoptosis of lung carcinoma cells and in response to etoposide
    • -21
    • B. Bartling J. Y. Yang D. Michod C. Widmann R. Lewensohn B. Zhivotovsky RasGTPase-activating protein is a target of caspases in spontaneous apoptosis of lung carcinoma cells and in response to etoposide Carcinogenesis 2004 25 6 909 21
    • (2004) Carcinogenesis , vol.25 , Issue.6 , pp. 909
    • Bartling, B.1    Yang, J.Y.2    Michod, D.3    Widmann, C.4    Lewensohn, R.5    Zhivotovsky, B.6
  • 44
  • 46
    • 0028196619 scopus 로고
    • Species specificity and organ, cellular and subcellular localization of the 100 kDa Ras GTPase activating protein
    • -35
    • P. Mollat A. Fournier C. Z. Yang E. Alsat Y. Zhang D. Evain-Brion J. Grassi M. N. Thang Species specificity and organ, cellular and subcellular localization of the 100 kDa Ras GTPase activating protein J. Cell Sci. 1994 107 3 427 35
    • (1994) J. Cell Sci. , vol.107 , Issue.3 , pp. 427
    • Mollat, P.1    Fournier, A.2    Yang, C.Z.3    Alsat, E.4    Zhang, Y.5    Evain-Brion, D.6    Grassi, J.7    Thang, M.N.8
  • 47
    • 0028017571 scopus 로고
    • Activation of Ras and formation of GAP complex during TPA-induced monocytic differentiation of HL-60 cells
    • -9
    • K. Katagiri S. Hattori S. Nakamura T. Yamamoto T. Yoshida T. Katagiri Activation of Ras and formation of GAP complex during TPA-induced monocytic differentiation of HL-60 cells Blood 1994 84 6 1780 9
    • (1994) Blood , vol.84 , Issue.6 , pp. 1780
    • Katagiri, K.1    Hattori, S.2    Nakamura, S.3    Yamamoto, T.4    Yoshida, T.5    Katagiri, T.6
  • 51
    • 0037443055 scopus 로고    scopus 로고
    • Dynamic regulation of the Ras pathway via proteolysis of the NF1 tumor suppressor
    • -54
    • K. Cichowski S. Santiago M. Jardim B. W. Johnson T. Jacks Dynamic regulation of the Ras pathway via proteolysis of the NF1 tumor suppressor Genes Dev. 2003 17 4 449 54
    • (2003) Genes Dev. , vol.17 , Issue.4 , pp. 449
    • Cichowski, K.1    Santiago, S.2    Jardim, M.3    Johnson, B.W.4    Jacks, T.5
  • 52
    • 34047151226 scopus 로고    scopus 로고
    • Life extension through neurofibromin mitochondrial regulation and antioxidant therapy for neurofibromatosis-1 in Drosophila melanogaster
    • -85
    • J. J. Tong S. E. Schriner D. McCleary B. J. Day D. C. Wallace Life extension through neurofibromin mitochondrial regulation and antioxidant therapy for neurofibromatosis-1 in Drosophila melanogaster Nat. Genet. 2007 39 4 476 85
    • (2007) Nat. Genet. , vol.39 , Issue.4 , pp. 476
    • Tong, J.J.1    Schriner, S.E.2    McCleary, D.3    Day, B.J.4    Wallace, D.C.5
  • 53
    • 1642573162 scopus 로고    scopus 로고
    • PKA phosphorylation and 14-3-3 interaction regulate the function of neurofibromatosis type i tumor suppressor, neurofibromin
    • -82
    • L. Feng S. Yunoue H. Tokuo T. Ozawa D. Zhang S. Patrakitkomjorn T. Ichimura H. Saya N. Araki PKA phosphorylation and 14-3-3 interaction regulate the function of neurofibromatosis type I tumor suppressor, neurofibromin FEBS Lett. 2004 557 1-3 275 82
    • (2004) FEBS Lett. , vol.557 , Issue.3 , pp. 275
    • Feng, L.1    Yunoue, S.2    Tokuo, H.3    Ozawa, T.4    Zhang, D.5    Patrakitkomjorn, S.6    Ichimura, T.7    Saya, H.8    Araki, N.9
  • 54
    • 34250320958 scopus 로고    scopus 로고
    • PU.1, interferon regulatory factor (IRF) 2, and the interferon consensus sequence-binding protein (ICSBP/IRF8) cooperate to activate NF1 transcription in differentiating myeloid cells
    • -43
    • W. Huang E. Horvath E. A. Eklund PU.1, interferon regulatory factor (IRF) 2, and the interferon consensus sequence-binding protein (ICSBP/IRF8) cooperate to activate NF1 transcription in differentiating myeloid cells J. Biol. Chem. 2007 282 9 6629 43
    • (2007) J. Biol. Chem. , vol.282 , Issue.9 , pp. 6629
    • Huang, W.1    Horvath, E.2    Eklund, E.A.3
  • 55
    • 0031919430 scopus 로고    scopus 로고
    • Upregulation of tumor suppressor protein neurofibromin in normal human wound healing and in vitro evidence for platelet derived growth factor (PDGF) and transforming growth factor-β1 (TGF-β1) elicited increase in neurofibromin mRNA steady-state levels in dermal fibroblasts
    • -7
    • H. Yla-Outinen V. Aaltonen A. S. Bjorkstrand O. Hirvonen J. Lakkakorpi M. Vaha-Kreula M. Laato J. Peltonen Upregulation of tumor suppressor protein neurofibromin in normal human wound healing and in vitro evidence for platelet derived growth factor (PDGF) and transforming growth factor-β1 (TGF-β1) elicited increase in neurofibromin mRNA steady-state levels in dermal fibroblasts J. Invest. Dermatol. 1998 110 3 232 7
    • (1998) J. Invest. Dermatol. , vol.110 , Issue.3 , pp. 232
    • Yla-Outinen, H.1    Aaltonen, V.2    Bjorkstrand, A.S.3    Hirvonen, O.4    Lakkakorpi, J.5    Vaha-Kreula, M.6    Laato, M.7    Peltonen, J.8
  • 58
    • 0032558834 scopus 로고    scopus 로고
    • The G protein Gα12 stimulates Bruton's tyrosine kinase and a rasGAP through a conserved PH/BM domain
    • -13
    • Y. Jiang W. Ma Y. Wan T. Kozasa S. Hattori X. Y. Huang The G protein Gα12 stimulates Bruton's tyrosine kinase and a rasGAP through a conserved PH/BM domain Nature 1998 395 6704 808 13
    • (1998) Nature , vol.395 , Issue.6704 , pp. 808
    • Jiang, Y.1    Ma, W.2    Wan, Y.3    Kozasa, T.4    Hattori, S.5    Huang, X.Y.6
  • 62
    • 0042734450 scopus 로고    scopus 로고
    • Oxidized phospholipid-induced endothelial cell/monocyte interaction is mediated by a cAMP-dependent R-Ras/PI3-kinase pathway
    • -90
    • A. L. Cole G. Subbanagounder S. Mukhopadhyay J. A. Berliner D. K. Vora Oxidized phospholipid-induced endothelial cell/monocyte interaction is mediated by a cAMP-dependent R-Ras/PI3-kinase pathway Arterioscler. Thromb. Vasc. Biol. 2003 23 8 1384 90
    • (2003) Arterioscler. Thromb. Vasc. Biol. , vol.23 , Issue.8 , pp. 1384
    • Cole, A.L.1    Subbanagounder, G.2    Mukhopadhyay, S.3    Berliner, J.A.4    Vora, D.K.5
  • 63
  • 64
    • 0032544675 scopus 로고    scopus 로고
    • Restricted tissue expression pattern of a novel human rasGAP-related gene and its murine ortholog
    • -25
    • M. Allen S. Chu S. Brill C. Stotler A. Buckler Restricted tissue expression pattern of a novel human rasGAP-related gene and its murine ortholog Gene 1998 218 1-2 17 25
    • (1998) Gene , vol.218 , Issue.2 , pp. 17
    • Allen, M.1    Chu, S.2    Brill, S.3    Stotler, C.4    Buckler, A.5
  • 66
    • 24944460781 scopus 로고    scopus 로고
    • An essential function for the calcium-promoted Ras inactivator in Fcγreceptor-mediated phagocytosis
    • -9
    • J. Zhang J. Guo I. Dzhagalov Y. W. He An essential function for the calcium-promoted Ras inactivator in Fcγreceptor-mediated phagocytosis Nat. Immunol. 2005 6 9 911 9
    • (2005) Nat. Immunol. , vol.6 , Issue.9 , pp. 911
    • Zhang, J.1    Guo, J.2    Dzhagalov, I.3    He, Y.W.4
  • 68
    • 0032078872 scopus 로고    scopus 로고
    • A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by CaM kinase II
    • -904
    • H. J. Chen M. Rojas-Soto A. Oguni M. B. Kennedy A synaptic Ras-GTPase activating protein (p135 SynGAP) inhibited by CaM kinase II Neuron 1998 20 5 895 904
    • (1998) Neuron , vol.20 , Issue.5 , pp. 895
    • Chen, H.J.1    Rojas-Soto, M.2    Oguni, A.3    Kennedy, M.B.4
  • 69
    • 0032055396 scopus 로고    scopus 로고
    • SynGAP: A synaptic RasGAP that associates with the PSD-95/SAP90 protein family
    • -91
    • J. H. Kim D. Liao L. F. Lau R. L. Huganir SynGAP: a synaptic RasGAP that associates with the PSD-95/SAP90 protein family Neuron 1998 20 4 683 91
    • (1998) Neuron , vol.20 , Issue.4 , pp. 683
    • Kim, J.H.1    Liao, D.2    Lau, L.F.3    Huganir, R.L.4
  • 70
    • 0037442509 scopus 로고    scopus 로고
    • The role of synaptic GTPase-activating protein in neuronal development and synaptic plasticity
    • -24
    • J. H. Kim H. K. Lee K. Takamiya R. L. Huganir The role of synaptic GTPase-activating protein in neuronal development and synaptic plasticity J. Neurosci. 2003 23 4 1119 24
    • (2003) J. Neurosci. , vol.23 , Issue.4 , pp. 1119
    • Kim, J.H.1    Lee, H.K.2    Takamiya, K.3    Huganir, R.L.4
  • 71
    • 2342437016 scopus 로고    scopus 로고
    • Regulation of the neuron-specific Ras GTPase-activating protein, synGAP, by Ca2+/calmodulin-dependent protein kinase II
    • -8
    • J. S. Oh P. Manzerra M. B. Kennedy Regulation of the neuron-specific Ras GTPase-activating protein, synGAP, by Ca2+/calmodulin-dependent protein kinase II J. Biol. Chem. 2004 279 17 17980 8
    • (2004) J. Biol. Chem. , vol.279 , Issue.17 , pp. 17980
    • Oh, J.S.1    Manzerra, P.2    Kennedy, M.B.3
  • 72
    • 1642417689 scopus 로고    scopus 로고
    • Role of Unc51.1 and its binding partners in CNS axon outgrowth
    • -58
    • T. Tomoda J. H. Kim C. Zhan M. E. Hatten Role of Unc51.1 and its binding partners in CNS axon outgrowth Genes Dev. 2004 18 5 541 58
    • (2004) Genes Dev. , vol.18 , Issue.5 , pp. 541
    • Tomoda, T.1    Kim, J.H.2    Zhan, C.3    Hatten, M.E.4
  • 74
    • 0037066783 scopus 로고    scopus 로고
    • The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate cancer. Characterization of a novel GTPase-activating protein associated with N-terminal domain of DOC-2/DAB2
    • -31
    • Z. Wang C. P. Tseng R. C. Pong H. Chen J. D. McConnell N. Navone J. T. Hsieh The mechanism of growth-inhibitory effect of DOC-2/DAB2 in prostate cancer. Characterization of a novel GTPase-activating protein associated with N-terminal domain of DOC-2/DAB2 J. Biol. Chem. 2002 277 15 12622 31
    • (2002) J. Biol. Chem. , vol.277 , Issue.15 , pp. 12622
    • Wang, Z.1    Tseng, C.P.2    Pong, R.C.3    Chen, H.4    McConnell, J.D.5    Navone, N.6    Hsieh, J.T.7
  • 75
    • 0041743148 scopus 로고    scopus 로고
    • AIP1 mediates TNF-α-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3
    • -43
    • R. Zhang X. He W. Liu M. Lu J. T. Hsieh W. Min AIP1 mediates TNF-α-induced ASK1 activation by facilitating dissociation of ASK1 from its inhibitor 14-3-3 J. Clin. Invest. 2003 111 12 1933 43
    • (2003) J. Clin. Invest. , vol.111 , Issue.12 , pp. 1933
    • Zhang, R.1    He, X.2    Liu, W.3    Lu, M.4    Hsieh, J.T.5    Min, W.6
  • 76
    • 34447531013 scopus 로고    scopus 로고
    • RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation
    • -96
    • R. Zhang H. Zhang Y. Lin J. Li J. S. Pober W. Min RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation J. Biol. Chem. 2007 282 20 14788 96
    • (2007) J. Biol. Chem. , vol.282 , Issue.20 , pp. 14788
    • Zhang, R.1    Zhang, H.2    Lin, Y.3    Li, J.4    Pober, J.S.5    Min, W.6
  • 79
    • 0038118495 scopus 로고    scopus 로고
    • VEGF receptor expression and signaling in human bladder tumors
    • -70
    • W. Wu X. Shu H. Hovsepyan R. D. Mosteller D. Broek VEGF receptor expression and signaling in human bladder tumors Oncogene 2003 22 22 3361 70
    • (2003) Oncogene , vol.22 , Issue.22 , pp. 3361
    • Wu, W.1    Shu, X.2    Hovsepyan, H.3    Mosteller, R.D.4    Broek, D.5
  • 81
    • 16844375160 scopus 로고    scopus 로고
    • Proteomic analysis reveals hyperactivation of the mammalian target of rapamycin pathway in neurofibromatosis 1-associated human and mouse brain tumors
    • -60
    • B. Dasgupta Y. Yi D. Y. Chen J. D. Weber D. H. Gutmann Proteomic analysis reveals hyperactivation of the mammalian target of rapamycin pathway in neurofibromatosis 1-associated human and mouse brain tumors Cancer Res. 2005 65 7 2755 60
    • (2005) Cancer Res. , vol.65 , Issue.7 , pp. 2755
    • Dasgupta, B.1    Yi, Y.2    Chen, D.Y.3    Weber, J.D.4    Gutmann, D.H.5
  • 82
    • 34250379843 scopus 로고    scopus 로고
    • Nucleophosmin mediates mammalian target of rapamycin-dependent actin cytoskeleton dynamics and proliferation in neurofibromin-deficient astrocytes
    • -9
    • D. K. Sandsmark H. Zhang B. Hegedus C. L. Pelletier J. D. Weber D. H. Gutmann Nucleophosmin mediates mammalian target of rapamycin-dependent actin cytoskeleton dynamics and proliferation in neurofibromin-deficient astrocytes Cancer Res. 2007 67 10 4790 9
    • (2007) Cancer Res. , vol.67 , Issue.10 , pp. 4790
    • Sandsmark, D.K.1    Zhang, H.2    Hegedus, B.3    Pelletier, C.L.4    Weber, J.D.5    Gutmann, D.H.6
  • 84
    • 0036838359 scopus 로고    scopus 로고
    • Increased production of bioactive lysophosphatidic acid by serum lysophospholipase D in human pregnancy
    • -92
    • A. Tokumura Y. Kanaya M. Miyake S. Yamano M. Irahara K. Fukuzawa Increased production of bioactive lysophosphatidic acid by serum lysophospholipase D in human pregnancy Biol. Reprod. 2002 67 5 1386 92
    • (2002) Biol. Reprod. , vol.67 , Issue.5 , pp. 1386
    • Tokumura, A.1    Kanaya, Y.2    Miyake, M.3    Yamano, S.4    Irahara, M.5    Fukuzawa, K.6
  • 85
    • 4344706187 scopus 로고    scopus 로고
    • The ins and outs of lysophosphatidic acid signaling
    • -81
    • W. H. Moolenaar L. A. van Meeteren B. N. Giepmans The ins and outs of lysophosphatidic acid signaling Bioessays 2004 26 8 870 81
    • (2004) Bioessays , vol.26 , Issue.8 , pp. 870
    • Moolenaar, W.H.1    Van Meeteren, L.A.2    Giepmans, B.N.3
  • 86
    • 33847711059 scopus 로고    scopus 로고
    • Neurofibromin-deficient Schwann cells have increased lysophosphatidic acid dependent survival and migration-implications for increased neurofibroma formation during pregnancy
    • -36
    • T. D. Nebesio W. Ming S. Chen T. Clegg J. Yuan Y. Yang S. A. Estwick Y. Li X. Li C. M. Hingtgen F. C. Yang Neurofibromin-deficient Schwann cells have increased lysophosphatidic acid dependent survival and migration-implications for increased neurofibroma formation during pregnancy Glia 2007 55 5 527 36
    • (2007) Glia , vol.55 , Issue.5 , pp. 527
    • Nebesio, T.D.1    Ming, W.2    Chen, S.3    Clegg, T.4    Yuan, J.5    Yang, Y.6    Estwick, S.A.7    Li, Y.8    Li, X.9    Hingtgen, C.M.10    Yang, F.C.11
  • 87
    • 0038711739 scopus 로고    scopus 로고
    • Neurofibromatosis type i tumor suppressor neurofibromin regulates neuronal differentiation via its GTPase-activating protein function toward Ras
    • -69
    • S. Yunoue H. Tokuo K. Fukunaga L. Feng T. Ozawa T. Nishi A. Kikuchi S. Hattori J. Kuratsu H. Saya N. Araki Neurofibromatosis type I tumor suppressor neurofibromin regulates neuronal differentiation via its GTPase-activating protein function toward Ras J. Biol. Chem. 2003 278 29 26958 69
    • (2003) J. Biol. Chem. , vol.278 , Issue.29 , pp. 26958
    • Yunoue, S.1    Tokuo, H.2    Fukunaga, K.3    Feng, L.4    Ozawa, T.5    Nishi, T.6    Kikuchi, A.7    Hattori, S.8    Kuratsu, J.9    Saya, H.10    Araki, N.11
  • 88
    • 33845540298 scopus 로고    scopus 로고
    • Molecular mechanisms involved in Ras inactivation: The annexin A6-p120GAP complex
    • -20
    • T. Grewal C. Enrich Molecular mechanisms involved in Ras inactivation: the annexin A6-p120GAP complex BioEssays 2006 28 12 1211 20
    • (2006) BioEssays , vol.28 , Issue.12 , pp. 1211
    • Grewal, T.1    Enrich, C.2
  • 89
    • 33748337958 scopus 로고    scopus 로고
    • Ras activation in response to phorbol ester proceeds independently of the EGFR via an unconventional nucleotide-exchange factor system in COS-7 cells
    • -56
    • I. Rubio K. Rennert U. Wittig K. Beer M. Durst S. L. Stang J. Stone R. Wetzker Ras activation in response to phorbol ester proceeds independently of the EGFR via an unconventional nucleotide-exchange factor system in COS-7 cells Biochem. J. 2006 398 2 243 56
    • (2006) Biochem. J. , vol.398 , Issue.2 , pp. 243
    • Rubio, I.1    Rennert, K.2    Wittig, U.3    Beer, K.4    Durst, M.5    Stang, S.L.6    Stone, J.7    Wetzker, R.8
  • 92
    • 0032562579 scopus 로고    scopus 로고
    • Catalytic domain of the p120 Ras GAP binds to Rab5 and stimulates its GTPase activity
    • -90
    • K. Liu G. Li Catalytic domain of the p120 Ras GAP binds to Rab5 and stimulates its GTPase activity J. Biol. Chem. 1998 273 17 10087 90
    • (1998) J. Biol. Chem. , vol.273 , Issue.17 , pp. 10087
    • Liu, K.1    Li, G.2
  • 95
    • 0030803674 scopus 로고    scopus 로고
    • A new function of p120-GTPase-activating protein. Prevention of the guanine nucleotide exchange factor-stimulated nucleotide exchange on the active form of Ha-Ras p21
    • -34
    • C. Giglione M. C. Parrini S. Baouz A. Bernardi A. Parmeggiani A new function of p120-GTPase-activating protein. Prevention of the guanine nucleotide exchange factor-stimulated nucleotide exchange on the active form of Ha-Ras p21 J. Biol. Chem. 1997 272 40 25128 34
    • (1997) J. Biol. Chem. , vol.272 , Issue.40 , pp. 25128
    • Giglione, C.1    Parrini, M.C.2    Baouz, S.3    Bernardi, A.4    Parmeggiani, A.5
  • 96
    • 33846916195 scopus 로고    scopus 로고
    • K-ras is critical for modulating multiple c-kit-mediated cellular functions in wild-type and Nf1+/-mast cells
    • -34
    • W. F. Khalaf F. C. Yang S. Chen H. White W. Bessler D. A. Ingram D. W. Clapp K-ras is critical for modulating multiple c-kit-mediated cellular functions in wild-type and Nf1+/-mast cells J. Immunol. 2007 178 4 2527 34
    • (2007) J. Immunol. , vol.178 , Issue.4 , pp. 2527
    • Khalaf, W.F.1    Yang, F.C.2    Chen, S.3    White, H.4    Bessler, W.5    Ingram, D.A.6    Clapp, D.W.7
  • 97
    • 3042744944 scopus 로고    scopus 로고
    • P120 Ras GTPase-activating protein associates with fibroblast growth factor receptors in Drosophila
    • -74
    • S. A. Woodcock D. A. Hughes p120 Ras GTPase-activating protein associates with fibroblast growth factor receptors in Drosophila Biochem. J. 2004 380 3 767 74
    • (2004) Biochem. J. , vol.380 , Issue.3 , pp. 767
    • Woodcock, S.A.1    Hughes, D.A.2
  • 98
    • 33645290264 scopus 로고    scopus 로고
    • A rancid culprit in vascular inflammation acts on the prostaglandin receptor EP2
    • -9
    • N. Leitinger A rancid culprit in vascular inflammation acts on the prostaglandin receptor EP2 Circ. Res. 2006 98 5 587 9
    • (2006) Circ. Res. , vol.98 , Issue.5 , pp. 587
    • Leitinger, N.1
  • 99
    • 33645741111 scopus 로고    scopus 로고
    • Rho GTPases and leukocyte adhesion receptor expression and function in endothelial cells
    • -767
    • E. Cernuda-Morollón A. J. Ridley Rho GTPases and leukocyte adhesion receptor expression and function in endothelial cells Circ. Res. 2006 98 6 757 767
    • (2006) Circ. Res. , vol.98 , Issue.6 , pp. 757
    • Cernuda-Morollón, E.1    Ridley, A.J.2


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