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Volumn 7, Issue 11, 2012, Pages

Identification and Characterisation of the RalA-ERp57 Interaction: Evidence for GDI Activity of ERp57

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; GUANOSINE DIPHOSPHATE; HYDROGEN PEROXIDE; MEMBRANE PROTEIN; OXIDOREDUCTASE; PROTEIN DISULFIDE ISOMERASE; PROTEIN ERP57; PROTEIN RALA; PROTEIN RALBP1; RAL PROTEIN; REDUCING AGENT; UNCLASSIFIED DRUG;

EID: 84870626185     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0050879     Document Type: Article
Times cited : (5)

References (61)
  • 3
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: critical elements in the control of small G proteins
    • Bos JL, Rehmann H, Wittinghofer A, (2007) GEFs and GAPs: critical elements in the control of small G proteins. Cell 129: 865-877.
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 5
    • 0034603198 scopus 로고    scopus 로고
    • Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI
    • Hoffman GR, Nassar N, Cerione RA, (2000) Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI. Cell 100: 345-356.
    • (2000) Cell , vol.100 , pp. 345-356
    • Hoffman, G.R.1    Nassar, N.2    Cerione, R.A.3
  • 6
    • 77953809435 scopus 로고    scopus 로고
    • Membrane targeting mechanism of Rab GTPases elucidated by semisynthetic protein probes
    • Wu YW, Oesterlin LK, Tan KT, Waldmann H, Alexandrov K, et al. (2010) Membrane targeting mechanism of Rab GTPases elucidated by semisynthetic protein probes. Nat Chem Biol 6: 534-540.
    • (2010) Nat Chem Biol , vol.6 , pp. 534-540
    • Wu, Y.W.1    Oesterlin, L.K.2    Tan, K.T.3    Waldmann, H.4    Alexandrov, K.5
  • 7
    • 23844445866 scopus 로고    scopus 로고
    • The structural and mechanistic basis for recycling of Rab proteins between membrane compartments
    • Goody RS, Rak A, Alexandrov K, (2005) The structural and mechanistic basis for recycling of Rab proteins between membrane compartments. Cell Mol Life Sci 62: 1657-1670.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1657-1670
    • Goody, R.S.1    Rak, A.2    Alexandrov, K.3
  • 8
    • 69949132404 scopus 로고    scopus 로고
    • New insights into how the Rho guanine nucleotide dissociation inhibitor regulates the interaction of Cdc42 with membranes
    • Johnson JL, Erickson JW, Cerione RA, (2009) New insights into how the Rho guanine nucleotide dissociation inhibitor regulates the interaction of Cdc42 with membranes. J Biol Chem 284: 23860-23871.
    • (2009) J Biol Chem , vol.284 , pp. 23860-23871
    • Johnson, J.L.1    Erickson, J.W.2    Cerione, R.A.3
  • 9
    • 0037408391 scopus 로고    scopus 로고
    • The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI
    • Yamashita T, Tohyama M, (2003) The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI. Nat Neurosci 6: 461-467.
    • (2003) Nat Neurosci , vol.6 , pp. 461-467
    • Yamashita, T.1    Tohyama, M.2
  • 10
    • 77949893465 scopus 로고    scopus 로고
    • Differential phosphorylation of RhoGDI mediates the distinct cycling of Cdc42 and Rac1 to regulate second-phase insulin secretion
    • Wang Z, Thurmond DC, (2010) Differential phosphorylation of RhoGDI mediates the distinct cycling of Cdc42 and Rac1 to regulate second-phase insulin secretion. J Biol Chem 285: 6186-6197.
    • (2010) J Biol Chem , vol.285 , pp. 6186-6197
    • Wang, Z.1    Thurmond, D.C.2
  • 11
    • 81355127367 scopus 로고    scopus 로고
    • Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo
    • Ismail SA, Chen YX, Rusinova A, Chandra A, Bierbaum M, et al. (2011) Arl2-GTP and Arl3-GTP regulate a GDI-like transport system for farnesylated cargo. Nat Chem Biol 7: 942-949.
    • (2011) Nat Chem Biol , vol.7 , pp. 942-949
    • Ismail, S.A.1    Chen, Y.X.2    Rusinova, A.3    Chandra, A.4    Bierbaum, M.5
  • 12
    • 79551713764 scopus 로고    scopus 로고
    • RhoGDI: A rheostat for the Rho switch
    • Boulter E, Garcia-Mata R, (2010) RhoGDI: A rheostat for the Rho switch. Small Gtpases 1: 65-68.
    • (2010) Small Gtpases , vol.1 , pp. 65-68
    • Boulter, E.1    Garcia-Mata, R.2
  • 13
    • 0041846652 scopus 로고    scopus 로고
    • Ral-GTPases: approaching their 15 minutes of fame
    • Feig LA, (2003) Ral-GTPases: approaching their 15 minutes of fame. Trends Cell Biol 13: 419-425.
    • (2003) Trends Cell Biol , vol.13 , pp. 419-425
    • Feig, L.A.1
  • 14
    • 51949085937 scopus 로고    scopus 로고
    • Distinct roles of RalA and RalB in the progression of cytokinesis are supported by distinct RalGEFs
    • Cascone I, Selimoglu R, Ozdemir C, Del Nery E, Yeaman C, et al. (2008) Distinct roles of RalA and RalB in the progression of cytokinesis are supported by distinct RalGEFs. Embo J 27: 2375-2387.
    • (2008) Embo J , vol.27 , pp. 2375-2387
    • Cascone, I.1    Selimoglu, R.2    Ozdemir, C.3    Del Nery, E.4    Yeaman, C.5
  • 15
    • 78651488777 scopus 로고    scopus 로고
    • RalB and the exocyst mediate the cellular starvation response by direct activation of autophagosome assembly
    • Bodemann BO, Orvedahl A, Cheng T, Ram RR, Ou YH, et al. (2011) RalB and the exocyst mediate the cellular starvation response by direct activation of autophagosome assembly. Cell 144: 253-267.
    • (2011) Cell , vol.144 , pp. 253-267
    • Bodemann, B.O.1    Orvedahl, A.2    Cheng, T.3    Ram, R.R.4    Ou, Y.H.5
  • 16
    • 38849147752 scopus 로고    scopus 로고
    • Ral GTPases and cancer: linchpin support of the tumorigenic platform
    • Bodemann BO, White MA, (2008) Ral GTPases and cancer: linchpin support of the tumorigenic platform. Nat Rev Cancer 8: 133-140.
    • (2008) Nat Rev Cancer , vol.8 , pp. 133-140
    • Bodemann, B.O.1    White, M.A.2
  • 17
    • 0036141434 scopus 로고    scopus 로고
    • The exocyst complex binds the small GTPase RalA to mediate filopodia formation
    • Sugihara K, Asano S, Tanaka K, Iwamatsu A, Okawa K, et al. (2002) The exocyst complex binds the small GTPase RalA to mediate filopodia formation. Nat Cell Biol 4: 73-78.
    • (2002) Nat Cell Biol , vol.4 , pp. 73-78
    • Sugihara, K.1    Asano, S.2    Tanaka, K.3    Iwamatsu, A.4    Okawa, K.5
  • 19
    • 0035839569 scopus 로고    scopus 로고
    • The brain exocyst complex interacts with RalA in a GTP-dependent manner: identification of a novel mammalian Sec3 gene and a second Sec15 gene
    • Brymora A, Valova VA, Larsen MR, Roufogalis BD, Robinson PJ, (2001) The brain exocyst complex interacts with RalA in a GTP-dependent manner: identification of a novel mammalian Sec3 gene and a second Sec15 gene. J Biol Chem 276: 29792-29797.
    • (2001) J Biol Chem , vol.276 , pp. 29792-29797
    • Brymora, A.1    Valova, V.A.2    Larsen, M.R.3    Roufogalis, B.D.4    Robinson, P.J.5
  • 22
    • 78751487053 scopus 로고    scopus 로고
    • RalGDS family members couple Ras to Ral signalling and that's not all
    • Ferro E, Trabalzini L, (2010) RalGDS family members couple Ras to Ral signalling and that's not all. Cell Signal 22: 1804-1810.
    • (2010) Cell Signal , vol.22 , pp. 1804-1810
    • Ferro, E.1    Trabalzini, L.2
  • 23
    • 34249985839 scopus 로고    scopus 로고
    • Functional analysis of RalGPS2, a murine guanine nucleotide exchange factor for RalA GTPase
    • Ceriani M, Scandiuzzi C, Amigoni L, Tisi R, Berruti G, et al. (2007) Functional analysis of RalGPS2, a murine guanine nucleotide exchange factor for RalA GTPase. Exp Cell Res 313: 2293-2307.
    • (2007) Exp Cell Res , vol.313 , pp. 2293-2307
    • Ceriani, M.1    Scandiuzzi, C.2    Amigoni, L.3    Tisi, R.4    Berruti, G.5
  • 24
    • 0034607989 scopus 로고    scopus 로고
    • Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral
    • Rebhun JF, Chen H, Quilliam LA, (2000) Identification and characterization of a new family of guanine nucleotide exchange factors for the ras-related GTPase Ral. J Biol Chem 275: 13406-13410.
    • (2000) J Biol Chem , vol.275 , pp. 13406-13410
    • Rebhun, J.F.1    Chen, H.2    Quilliam, L.A.3
  • 25
    • 0025912628 scopus 로고
    • Characterization of a GTPase-activating protein for the Ras-related Ral protein
    • Emkey R, Freedman S, Feig LA, (1991) Characterization of a GTPase-activating protein for the Ras-related Ral protein. J Biol Chem 266: 9703-9706.
    • (1991) J Biol Chem , vol.266 , pp. 9703-9706
    • Emkey, R.1    Freedman, S.2    Feig, L.A.3
  • 26
    • 0029931220 scopus 로고    scopus 로고
    • Characterization of human platelet GTPase activating protein for the Ral GTP-binding protein
    • Bhullar RP, Seneviratne HD, (1996) Characterization of human platelet GTPase activating protein for the Ral GTP-binding protein. Biochim Biophys Acta 1311: 181-188.
    • (1996) Biochim Biophys Acta , vol.1311 , pp. 181-188
    • Bhullar, R.P.1    Seneviratne, H.D.2
  • 27
    • 0030611196 scopus 로고    scopus 로고
    • RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas
    • Adra CN, Manor D, Ko JL, Zhu S, Horiuchi T, et al. (1997) RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas. Proc Natl Acad Sci U S A 94: 4279-4284.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 4279-4284
    • Adra, C.N.1    Manor, D.2    Ko, J.L.3    Zhu, S.4    Horiuchi, T.5
  • 28
    • 0026475383 scopus 로고
    • The identification and characterization of a GDP-dissociation inhibitor (GDI) for the CDC42Hs protein
    • Leonard D, Hart MJ, Platko JV, Eva A, Henzel W, et al. (1992) The identification and characterization of a GDP-dissociation inhibitor (GDI) for the CDC42Hs protein. J Biol Chem 267: 22860-22868.
    • (1992) J Biol Chem , vol.267 , pp. 22860-22868
    • Leonard, D.1    Hart, M.J.2    Platko, J.V.3    Eva, A.4    Henzel, W.5
  • 30
    • 0035424890 scopus 로고    scopus 로고
    • Enhanced protein recovery and reproducibility from pull-down assays and immunoprecipitations using spin columns
    • Brymora A, Cousin MA, Roufogalis BD, Robinson PJ, (2001) Enhanced protein recovery and reproducibility from pull-down assays and immunoprecipitations using spin columns. Anal Biochem 295: 119-122.
    • (2001) Anal Biochem , vol.295 , pp. 119-122
    • Brymora, A.1    Cousin, M.A.2    Roufogalis, B.D.3    Robinson, P.J.4
  • 31
    • 41549159471 scopus 로고    scopus 로고
    • The human PDI family: versatility packed into a single fold
    • Appenzeller-Herzog C, Ellgaard L, (2008) The human PDI family: versatility packed into a single fold. Biochim Biophys Acta 1783: 535-548.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 535-548
    • Appenzeller-Herzog, C.1    Ellgaard, L.2
  • 32
    • 33746822999 scopus 로고    scopus 로고
    • Crystal structure of the bb' domains of the protein disulfide isomerase ERp57
    • Kozlov G, Maattanen P, Schrag JD, Pollock S, Cygler M, et al. (2006) Crystal structure of the bb' domains of the protein disulfide isomerase ERp57. Structure 14: 1331-1339.
    • (2006) Structure , vol.14 , pp. 1331-1339
    • Kozlov, G.1    Maattanen, P.2    Schrag, J.D.3    Pollock, S.4    Cygler, M.5
  • 33
    • 27144497781 scopus 로고    scopus 로고
    • Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex
    • Peaper DR, Wearsch PA, Cresswell P, (2005) Tapasin and ERp57 form a stable disulfide-linked dimer within the MHC class I peptide-loading complex. Embo J 24: 3613-3623.
    • (2005) Embo J , vol.24 , pp. 3613-3623
    • Peaper, D.R.1    Wearsch, P.A.2    Cresswell, P.3
  • 34
    • 0038602702 scopus 로고    scopus 로고
    • Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex
    • Fukai S, Matern HT, Jagath JR, Scheller RH, Brunger AT, (2003) Structural basis of the interaction between RalA and Sec5, a subunit of the sec6/8 complex. Embo J 22: 3267-3278.
    • (2003) Embo J , vol.22 , pp. 3267-3278
    • Fukai, S.1    Matern, H.T.2    Jagath, J.R.3    Scheller, R.H.4    Brunger, A.T.5
  • 35
    • 0037082127 scopus 로고    scopus 로고
    • Oxidation of proteinaceous cysteine residues by dopamine-derived H2O2 in PC12 cells
    • Kim JR, Kwon KS, Yoon HW, Lee SR, Rhee SG, (2002) Oxidation of proteinaceous cysteine residues by dopamine-derived H2O2 in PC12 cells. Arch Biochem Biophys 397: 414-423.
    • (2002) Arch Biochem Biophys , vol.397 , pp. 414-423
    • Kim, J.R.1    Kwon, K.S.2    Yoon, H.W.3    Lee, S.R.4    Rhee, S.G.5
  • 36
    • 0036401454 scopus 로고    scopus 로고
    • Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis
    • Lind C, Gerdes R, Hamnell Y, Schuppe-Koistinen I, von Lowenhielm HB, et al. (2002) Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis. Arch Biochem Biophys 406: 229-240.
    • (2002) Arch Biochem Biophys , vol.406 , pp. 229-240
    • Lind, C.1    Gerdes, R.2    Hamnell, Y.3    Schuppe-Koistinen, I.4    von Lowenhielm, H.B.5
  • 37
    • 34249844125 scopus 로고    scopus 로고
    • DNA-binding activity of the ERp57 C-terminal domain is related to a redox-dependent conformational change
    • Grillo C, D'Ambrosio C, Consalvi V, Chiaraluce R, Scaloni A, et al. (2007) DNA-binding activity of the ERp57 C-terminal domain is related to a redox-dependent conformational change. J Biol Chem 282: 10299-10310.
    • (2007) J Biol Chem , vol.282 , pp. 10299-10310
    • Grillo, C.1    D'Ambrosio, C.2    Consalvi, V.3    Chiaraluce, R.4    Scaloni, A.5
  • 38
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • Vetter IR, Wittinghofer A, (2001) The guanine nucleotide-binding switch in three dimensions. Science 294: 1299-1304.
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 39
    • 1642307142 scopus 로고    scopus 로고
    • An activating mutant of Rac1 that fails to interact with Rho GDP-dissociation inhibitor stimulates membrane ruffling in mammalian cells
    • Gandhi PN, Gibson RM, Tong X, Miyoshi J, Takai Y, et al. (2004) An activating mutant of Rac1 that fails to interact with Rho GDP-dissociation inhibitor stimulates membrane ruffling in mammalian cells. Biochem J 378: 409-419.
    • (2004) Biochem J , vol.378 , pp. 409-419
    • Gandhi, P.N.1    Gibson, R.M.2    Tong, X.3    Miyoshi, J.4    Takai, Y.5
  • 40
    • 0035887166 scopus 로고    scopus 로고
    • RhoGDI-binding-defective mutant of Cdc42Hs targets to membranes and activates filopodia formation but does not cycle with the cytosol of mammalian cells
    • Gibson RM, Wilson-Delfosse AL, (2001) RhoGDI-binding-defective mutant of Cdc42Hs targets to membranes and activates filopodia formation but does not cycle with the cytosol of mammalian cells. Biochem J 359: 285-294.
    • (2001) Biochem J , vol.359 , pp. 285-294
    • Gibson, R.M.1    Wilson-Delfosse, A.L.2
  • 41
    • 0031930873 scopus 로고    scopus 로고
    • The putative "switch 2" domain of the Ras-related GTPase, Rab1B, plays an essential role in the interaction with Rab escort protein
    • Overmeyer JH, Wilson AL, Erdman RA, Maltese WA, (1998) The putative "switch 2" domain of the Ras-related GTPase, Rab1B, plays an essential role in the interaction with Rab escort protein. Mol Biol Cell 9: 223-235.
    • (1998) Mol Biol Cell , vol.9 , pp. 223-235
    • Overmeyer, J.H.1    Wilson, A.L.2    Erdman, R.A.3    Maltese, W.A.4
  • 42
    • 0035827523 scopus 로고    scopus 로고
    • Membrane targeting of a Rab GTPase that fails to associate with Rab escort protein (REP) or guanine nucleotide dissociation inhibitor (GDI)
    • Overmeyer JH, Wilson AL, Maltese WA, (2001) Membrane targeting of a Rab GTPase that fails to associate with Rab escort protein (REP) or guanine nucleotide dissociation inhibitor (GDI). J Biol Chem 276: 20379-20386.
    • (2001) J Biol Chem , vol.276 , pp. 20379-20386
    • Overmeyer, J.H.1    Wilson, A.L.2    Maltese, W.A.3
  • 43
    • 2442586577 scopus 로고    scopus 로고
    • RalA-exocyst interaction mediates GTP-dependent exocytosis
    • Wang L, Li G, Sugita S, (2004) RalA-exocyst interaction mediates GTP-dependent exocytosis. J Biol Chem 279: 19875-19881.
    • (2004) J Biol Chem , vol.279 , pp. 19875-19881
    • Wang, L.1    Li, G.2    Sugita, S.3
  • 44
    • 0028935835 scopus 로고
    • The antioxidant N-acetyl-cysteine protects cultured epithelial cells from menadione-induced cytopathology
    • Malorni W, Rivabene R, Matarrese P, (1995) The antioxidant N-acetyl-cysteine protects cultured epithelial cells from menadione-induced cytopathology. Chem Biol Interact 96: 113-123.
    • (1995) Chem Biol Interact , vol.96 , pp. 113-123
    • Malorni, W.1    Rivabene, R.2    Matarrese, P.3
  • 45
    • 79958242400 scopus 로고    scopus 로고
    • Assessment of redox changes to hydrogen peroxide-sensitive proteins during EGF signaling
    • Cuddihy SL, Winterbourn CC, Hampton MB, (2011) Assessment of redox changes to hydrogen peroxide-sensitive proteins during EGF signaling. Antioxid Redox Signal 15: 167-174.
    • (2011) Antioxid Redox Signal , vol.15 , pp. 167-174
    • Cuddihy, S.L.1    Winterbourn, C.C.2    Hampton, M.B.3
  • 46
    • 0033020660 scopus 로고    scopus 로고
    • Ral-specific guanine nucleotide exchange factor activity opposes other Ras effectors in PC12 cells by inhibiting neurite outgrowth
    • Goi T, Rusanescu G, Urano T, Feig LA, (1999) Ral-specific guanine nucleotide exchange factor activity opposes other Ras effectors in PC12 cells by inhibiting neurite outgrowth. Mol Cell Biol 19: 1731-1741.
    • (1999) Mol Cell Biol , vol.19 , pp. 1731-1741
    • Goi, T.1    Rusanescu, G.2    Urano, T.3    Feig, L.A.4
  • 47
    • 77953809347 scopus 로고    scopus 로고
    • ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase
    • Coe H, Michalak M, (2010) ERp57, a multifunctional endoplasmic reticulum resident oxidoreductase. Int J Biochem Cell Biol 42: 796-799.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 796-799
    • Coe, H.1    Michalak, M.2
  • 48
    • 58149215628 scopus 로고    scopus 로고
    • Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer
    • Dong G, Wearsch PA, Peaper DR, Cresswell P, Reinisch KM, (2009) Insights into MHC class I peptide loading from the structure of the tapasin-ERp57 thiol oxidoreductase heterodimer. Immunity 30: 21-32.
    • (2009) Immunity , vol.30 , pp. 21-32
    • Dong, G.1    Wearsch, P.A.2    Peaper, D.R.3    Cresswell, P.4    Reinisch, K.M.5
  • 49
    • 34247555889 scopus 로고    scopus 로고
    • The ERp57/GRp58/1,25D3-MARRS receptor: multiple functional roles in diverse cell systems
    • Khanal RC, Nemere I, (2007) The ERp57/GRp58/1,25D3-MARRS receptor: multiple functional roles in diverse cell systems. Curr Med Chem 14: 1087-1093.
    • (2007) Curr Med Chem , vol.14 , pp. 1087-1093
    • Khanal, R.C.1    Nemere, I.2
  • 52
    • 33646882179 scopus 로고    scopus 로고
    • A role for sperm surface protein disulfide isomerase activity in gamete fusion: evidence for the participation of ERp57
    • Ellerman DA, Myles DG, Primakoff P, (2006) A role for sperm surface protein disulfide isomerase activity in gamete fusion: evidence for the participation of ERp57. Dev Cell 10: 831-837.
    • (2006) Dev Cell , vol.10 , pp. 831-837
    • Ellerman, D.A.1    Myles, D.G.2    Primakoff, P.3
  • 53
    • 84870613000 scopus 로고    scopus 로고
    • The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosis
    • Wu Y, Ahmad SS, Zhou J, Wang L, Cully MP, et al. (2011) The disulfide isomerase ERp57 mediates platelet aggregation, hemostasis, and thrombosis. Blood.
    • (2011) Blood
    • Wu, Y.1    Ahmad, S.S.2    Zhou, J.3    Wang, L.4    Cully, M.P.5
  • 54
    • 23944518413 scopus 로고    scopus 로고
    • RhoGDI: multiple functions in the regulation of Rho family GTPase activities
    • Dovas A, Couchman JR, (2005) RhoGDI: multiple functions in the regulation of Rho family GTPase activities. Biochem J 390: 1-9.
    • (2005) Biochem J , vol.390 , pp. 1-9
    • Dovas, A.1    Couchman, J.R.2
  • 55
    • 7944229257 scopus 로고    scopus 로고
    • Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap
    • Nicely NI, Kosak J, de Serrano V, Mattos C, (2004) Crystal structures of Ral-GppNHp and Ral-GDP reveal two binding sites that are also present in Ras and Rap. 12: 2025-2036.
    • (2004) , vol.12 , pp. 2025-2036
    • Nicely, N.I.1    Kosak, J.2    de Serrano, V.3    Mattos, C.4
  • 56
    • 27144457720 scopus 로고    scopus 로고
    • Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme
    • Pautsch A, Vogelsgesang M, Trankle J, Herrmann C, Aktories K, (2005) Crystal structure of the C3bot-RalA complex reveals a novel type of action of a bacterial exoenzyme. Embo J 24: 3670-3680.
    • (2005) Embo J , vol.24 , pp. 3670-3680
    • Pautsch, A.1    Vogelsgesang, M.2    Trankle, J.3    Herrmann, C.4    Aktories, K.5
  • 57
    • 0035964281 scopus 로고    scopus 로고
    • Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation
    • Grizot S, Faure J, Fieschi F, Vignais PV, Dagher MC, et al. (2001) Crystal structure of the Rac1-RhoGDI complex involved in nadph oxidase activation. Biochemistry 40: 10007-10013.
    • (2001) Biochemistry , vol.40 , pp. 10007-10013
    • Grizot, S.1    Faure, J.2    Fieschi, F.3    Vignais, P.V.4    Dagher, M.C.5
  • 58
    • 0031845771 scopus 로고    scopus 로고
    • Modulation of GDP-dissociation inhibitor protein membrane retention by the cellular redox state in adipocytes
    • Chinni SR, Brenz M, Shisheva A, (1998) Modulation of GDP-dissociation inhibitor protein membrane retention by the cellular redox state in adipocytes. Exp Cell Res 242: 373-380.
    • (1998) Exp Cell Res , vol.242 , pp. 373-380
    • Chinni, S.R.1    Brenz, M.2    Shisheva, A.3
  • 59
    • 84856492497 scopus 로고    scopus 로고
    • The GDI-like solubilizing factor PDEdelta sustains the spatial organization and signalling of Ras family proteins
    • Chandra A, Grecco HE, Pisupati V, Perera D, Cassidy L, et al. (2012) The GDI-like solubilizing factor PDEdelta sustains the spatial organization and signalling of Ras family proteins. Nat Cell Biol 14: 148-158.
    • (2012) Nat Cell Biol , vol.14 , pp. 148-158
    • Chandra, A.1    Grecco, H.E.2    Pisupati, V.3    Perera, D.4    Cassidy, L.5
  • 61
    • 15144343374 scopus 로고    scopus 로고
    • Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation
    • Bae YS, Kang SW, Seo MS, Baines IC, Tekle E, et al. (1997) Epidermal growth factor (EGF)-induced generation of hydrogen peroxide. Role in EGF receptor-mediated tyrosine phosphorylation. J Biol Chem 272: 217-221.
    • (1997) J Biol Chem , vol.272 , pp. 217-221
    • Bae, Y.S.1    Kang, S.W.2    Seo, M.S.3    Baines, I.C.4    Tekle, E.5


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