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Volumn 9, Issue , 2011, Pages

The activation mechanism of Irga6, an interferon-inducible GTPase contributing to mouse resistance against Toxoplasma gondii

Author keywords

[No Author keywords available]

Indexed keywords

TOXOPLASMA GONDII;

EID: 79251583145     PISSN: None     EISSN: 17417007     Source Type: Journal    
DOI: 10.1186/1741-7007-9-7     Document Type: Article
Times cited : (31)

References (63)
  • 1
    • 33751189861 scopus 로고    scopus 로고
    • The interferon-inducible GTPases
    • 10.1146/annurev.cellbio.22.010305.104619, 16824009
    • Martens S, Howard J. The interferon-inducible GTPases. Annu Rev Cell Dev Biol 2006, 22:559-589. 10.1146/annurev.cellbio.22.010305.104619, 16824009.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 559-589
    • Martens, S.1    Howard, J.2
  • 2
    • 34047256441 scopus 로고    scopus 로고
    • IRG proteins: key mediators of interferon-regulated host resistance to intracellular pathogens
    • 10.1111/j.1462-5822.2007.00916.x, 17359233
    • Taylor GA. IRG proteins: key mediators of interferon-regulated host resistance to intracellular pathogens. Cell Microbiol 2007, 9:1099-1107. 10.1111/j.1462-5822.2007.00916.x, 17359233.
    • (2007) Cell Microbiol , vol.9 , pp. 1099-1107
    • Taylor, G.A.1
  • 3
    • 79951810726 scopus 로고    scopus 로고
    • The immunity-related GTPases in mammals: a fast-evolving cell-autonomous resistance system against intracellular pathogens
    • Hunn JP, Feng CG, Sher A, Howard JC. The immunity-related GTPases in mammals: a fast-evolving cell-autonomous resistance system against intracellular pathogens. Mamm Genome 2010,
    • (2010) Mamm Genome
    • Hunn, J.P.1    Feng, C.G.2    Sher, A.3    Howard, J.C.4
  • 4
    • 33744509713 scopus 로고    scopus 로고
    • The interferon-inducible p47 (IRG) GTPases in vertebrates: loss of the cell autonomous resistance mechanism in the human lineage
    • 10.1186/gb-2005-6-11-r92, 1297648, 16277747
    • Bekpen C, Hunn JP, Rohde C, Parvanova I, Guethlein L, Dunn DM, Glowalla E, Leptin M, Howard JC. The interferon-inducible p47 (IRG) GTPases in vertebrates: loss of the cell autonomous resistance mechanism in the human lineage. Genome Biol 2005, 6:R92. 10.1186/gb-2005-6-11-r92, 1297648, 16277747.
    • (2005) Genome Biol , vol.6
    • Bekpen, C.1    Hunn, J.P.2    Rohde, C.3    Parvanova, I.4    Guethlein, L.5    Dunn, D.M.6    Glowalla, E.7    Leptin, M.8    Howard, J.C.9
  • 5
    • 49649126253 scopus 로고    scopus 로고
    • Disruption of Toxoplasma gondii parasitophorous vacuoles by the mouse p47-resistance GTPases
    • 10.1371/journal.ppat.0010024, 1287907, 16304607
    • Martens S, Parvanova I, Zerrahn J, Griffiths G, Schell G, Reichmann G, Howard JC. Disruption of Toxoplasma gondii parasitophorous vacuoles by the mouse p47-resistance GTPases. PLoS Pathog 2005, 1:e24. 10.1371/journal.ppat.0010024, 1287907, 16304607.
    • (2005) PLoS Pathog , vol.1
    • Martens, S.1    Parvanova, I.2    Zerrahn, J.3    Griffiths, G.4    Schell, G.5    Reichmann, G.6    Howard, J.C.7
  • 7
    • 33748444233 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages
    • 10.1084/jem.20061318, 2118399, 16940170
    • Ling YM, Shaw MH, Ayala C, Coppens I, Taylor GA, Ferguson DJ, Yap GS. Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages. J Exp Med 2006, 203:2063-2071. 10.1084/jem.20061318, 2118399, 16940170.
    • (2006) J Exp Med , vol.203 , pp. 2063-2071
    • Ling, Y.M.1    Shaw, M.H.2    Ayala, C.3    Coppens, I.4    Taylor, G.A.5    Ferguson, D.J.6    Yap, G.S.7
  • 8
    • 61449117883 scopus 로고    scopus 로고
    • Disruption of the Toxoplasma gondii parasitophorous vacuole by IFNgamma-inducible immunity-related GTPases (IRG proteins) triggers necrotic cell death
    • 10.1371/journal.ppat.1000288, 2629126, 19197351
    • Zhao YO, Khaminets A, Hunn JP, Howard JC. Disruption of the Toxoplasma gondii parasitophorous vacuole by IFNgamma-inducible immunity-related GTPases (IRG proteins) triggers necrotic cell death. PLoS Pathog 2009, 5:e1000288. 10.1371/journal.ppat.1000288, 2629126, 19197351.
    • (2009) PLoS Pathog , vol.5
    • Zhao, Y.O.1    Khaminets, A.2    Hunn, J.P.3    Howard, J.C.4
  • 10
    • 57649115443 scopus 로고    scopus 로고
    • Inactive and Active States of the Interferon-inducible Resistance GTPase, Irga6, in Vivo
    • 10.1074/jbc.M804846200, 2581590, 18784077
    • Papic N, Hunn JP, Pawlowski N, Zerrahn J, Howard JC. Inactive and Active States of the Interferon-inducible Resistance GTPase, Irga6, in Vivo. J Biol Chem 2008, 283:32143-32151. 10.1074/jbc.M804846200, 2581590, 18784077.
    • (2008) J Biol Chem , vol.283 , pp. 32143-32151
    • Papic, N.1    Hunn, J.P.2    Pawlowski, N.3    Zerrahn, J.4    Howard, J.C.5
  • 11
    • 0043033168 scopus 로고    scopus 로고
    • IIGP1, an interferon-gamma-inducible 47-kDa GTPase of the mouse, showing cooperative enzymatic activity and GTP-dependent multimerization
    • 10.1074/jbc.M211973200, 12732635
    • Uthaiah RC, Praefcke GJ, Howard JC, Herrmann C. IIGP1, an interferon-gamma-inducible 47-kDa GTPase of the mouse, showing cooperative enzymatic activity and GTP-dependent multimerization. J Biol Chem 2003, 278:29336-29343. 10.1074/jbc.M211973200, 12732635.
    • (2003) J Biol Chem , vol.278 , pp. 29336-29343
    • Uthaiah, R.C.1    Praefcke, G.J.2    Howard, J.C.3    Herrmann, C.4
  • 12
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules?
    • 10.1038/nrm1313, 15040446
    • Praefcke GJ, McMahon HT. The dynamin superfamily: universal membrane tubulation and fission molecules?. Nat Rev Mol Cell Biol 2004, 5:133-147. 10.1038/nrm1313, 15040446.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 13
    • 78649497621 scopus 로고    scopus 로고
    • Dynamin self-assembly and the vesicle scission mechanism: How dynamin oligomers cleave the membrane neck of clathrin-coated pits during endocytosis
    • 10.1002/bies.201000086, 20957720
    • Pawlowski N. Dynamin self-assembly and the vesicle scission mechanism: How dynamin oligomers cleave the membrane neck of clathrin-coated pits during endocytosis. Bioessays 2010, 32:1033-1039. 10.1002/bies.201000086, 20957720.
    • (2010) Bioessays , vol.32 , pp. 1033-1039
    • Pawlowski, N.1
  • 14
    • 4444322564 scopus 로고    scopus 로고
    • Crystal structure of IIGP1: a paradigm for interferon-inducible p47 resistance GTPases
    • 10.1016/j.molcel.2004.07.017, 15350217
    • Ghosh A, Uthaiah R, Howard J, Herrmann C, Wolf E. Crystal structure of IIGP1: a paradigm for interferon-inducible p47 resistance GTPases. Mol Cell 2004, 15:727-739. 10.1016/j.molcel.2004.07.017, 15350217.
    • (2004) Mol Cell , vol.15 , pp. 727-739
    • Ghosh, A.1    Uthaiah, R.2    Howard, J.3    Herrmann, C.4    Wolf, E.5
  • 15
    • 0024463212 scopus 로고
    • Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation
    • 10.1038/341209a0, 2476675
    • Pai EF, Kabsch W, Krengel U, Holmes KC, John J, Wittinghofer A. Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation. Nature 1989, 341:209-214. 10.1038/341209a0, 2476675.
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.F.1    Kabsch, W.2    Krengel, U.3    Holmes, K.C.4    John, J.5    Wittinghofer, A.6
  • 16
    • 0026026818 scopus 로고
    • The GTPase superfamily: conserved structure and molecular mechanism
    • 10.1038/349117a0, 1898771
    • Bourne HR, Sanders DA, McCormick F. The GTPase superfamily: conserved structure and molecular mechanism. Nature 1991, 349:117-127. 10.1038/349117a0, 1898771.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 17
    • 0035834388 scopus 로고    scopus 로고
    • The guanine nucleotide-binding switch in three dimensions
    • 10.1126/science.1062023, 11701921
    • Vetter IR, Wittinghofer A. The guanine nucleotide-binding switch in three dimensions. Science 2001, 294:1299-1304. 10.1126/science.1062023, 11701921.
    • (2001) Science , vol.294 , pp. 1299-1304
    • Vetter, I.R.1    Wittinghofer, A.2
  • 19
    • 4043065683 scopus 로고    scopus 로고
    • Mechanisms regulating the positioning of mouse p47 resistance GTPases LRG-47 and IIGP1 on cellular membranes: retargeting to plasma membrane induced by phagocytosis
    • Martens S, Sabel K, Lange R, Uthaiah R, Wolf E, Howard JC. Mechanisms regulating the positioning of mouse p47 resistance GTPases LRG-47 and IIGP1 on cellular membranes: retargeting to plasma membrane induced by phagocytosis. J Immunol 2004, 173:2594-2606.
    • (2004) J Immunol , vol.173 , pp. 2594-2606
    • Martens, S.1    Sabel, K.2    Lange, R.3    Uthaiah, R.4    Wolf, E.5    Howard, J.C.6
  • 20
    • 0347584006 scopus 로고    scopus 로고
    • Substrate twinning activates the signal recognition particle and its receptor
    • 10.1038/nature02250, 14724630
    • Egea PF, Shan SO, Napetschnig J, Savage DF, Walter P, Stroud RM. Substrate twinning activates the signal recognition particle and its receptor. Nature 2004, 427:215-221. 10.1038/nature02250, 14724630.
    • (2004) Nature , vol.427 , pp. 215-221
    • Egea, P.F.1    Shan, S.O.2    Napetschnig, J.3    Savage, D.F.4    Walter, P.5    Stroud, R.M.6
  • 21
    • 0346373753 scopus 로고    scopus 로고
    • Heterodimeric GTPase core of the SRP targeting complex
    • 10.1126/science.1090827, 14726591
    • Focia PJ, Shepotinovskaya IV, Seidler JA, Freymann DM. Heterodimeric GTPase core of the SRP targeting complex. Science 2004, 303:373-377. 10.1126/science.1090827, 14726591.
    • (2004) Science , vol.303 , pp. 373-377
    • Focia, P.J.1    Shepotinovskaya, I.V.2    Seidler, J.A.3    Freymann, D.M.4
  • 22
    • 78650210471 scopus 로고    scopus 로고
    • Phosphorylation of mouse immunity-related GTPase (IRG) resistance proteins is an evasion strategy for virulent toxoplasma gondii
    • 10.1371/journal.pbio.1000576, 3006384, 21203588
    • Steinfeldt T, Könen-Waisman S, Tong L, Pawlowski N, Lamkemeyer T, Sibley LD, Hunn JP, Howard JC. Phosphorylation of mouse immunity-related GTPase (IRG) resistance proteins is an evasion strategy for virulent toxoplasma gondii. PLoS Biol 2010, 8:e1000576. 10.1371/journal.pbio.1000576, 3006384, 21203588.
    • (2010) PLoS Biol , vol.8
    • Steinfeldt, T.1    Könen-Waisman, S.2    Tong, L.3    Pawlowski, N.4    Lamkemeyer, T.5    Sibley, L.D.6    Hunn, J.P.7    Howard, J.C.8
  • 23
    • 0031017523 scopus 로고    scopus 로고
    • Structure of the conserved GTPase domain of the signal recognition particle
    • 10.1038/385361a0, 9002524
    • Freymann DM, Keenan RJ, Stroud RM, Walter P. Structure of the conserved GTPase domain of the signal recognition particle. Nature 1997, 385:361-364. 10.1038/385361a0, 9002524.
    • (1997) Nature , vol.385 , pp. 361-364
    • Freymann, D.M.1    Keenan, R.J.2    Stroud, R.M.3    Walter, P.4
  • 24
    • 0031030085 scopus 로고    scopus 로고
    • Crystal structure of the NG domain from the signal-recognition particle receptor FtsY
    • 10.1038/385365a0, 9002525
    • Montoya G, Svensson C, Luirink J, Sinning I. Crystal structure of the NG domain from the signal-recognition particle receptor FtsY. Nature 1997, 385:365-368. 10.1038/385365a0, 9002525.
    • (1997) Nature , vol.385 , pp. 365-368
    • Montoya, G.1    Svensson, C.2    Luirink, J.3    Sinning, I.4
  • 25
    • 0034723143 scopus 로고    scopus 로고
    • Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP
    • 10.1006/jmbi.1999.3427, 10656787
    • Jagath JR, Rodnina MV, Wintermeyer W. Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP. J Mol Biol 2000, 295:745-753. 10.1006/jmbi.1999.3427, 10656787.
    • (2000) J Mol Biol , vol.295 , pp. 745-753
    • Jagath, J.R.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 26
    • 0030845258 scopus 로고    scopus 로고
    • The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain
    • 10.1073/pnas.94.21.11339, 23460, 9326611
    • Moser C, Mol O, Goody RS, Sinning I. The signal recognition particle receptor of Escherichia coli (FtsY) has a nucleotide exchange factor built into the GTPase domain. Proc Natl Acad Sci USA 1997, 94:11339-11344. 10.1073/pnas.94.21.11339, 23460, 9326611.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 11339-11344
    • Moser, C.1    Mol, O.2    Goody, R.S.3    Sinning, I.4
  • 27
    • 0029097359 scopus 로고
    • Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases
    • 10.1126/science.7660124, 7660124
    • Powers T, Walter P. Reciprocal stimulation of GTP hydrolysis by two directly interacting GTPases. Science 1995, 269:1422-1424. 10.1126/science.7660124, 7660124.
    • (1995) Science , vol.269 , pp. 1422-1424
    • Powers, T.1    Walter, P.2
  • 28
    • 17644425296 scopus 로고    scopus 로고
    • Molecular crosstalk between the nucleotide specificity determinant of the SRP GTPase and the SRP receptor
    • 10.1021/bi0500980, 15835909
    • Shan SO, Walter P. Molecular crosstalk between the nucleotide specificity determinant of the SRP GTPase and the SRP receptor. Biochemistry 2005, 44:6214-6222. 10.1021/bi0500980, 15835909.
    • (2005) Biochemistry , vol.44 , pp. 6214-6222
    • Shan, S.O.1    Walter, P.2
  • 29
    • 0036295212 scopus 로고    scopus 로고
    • Classification and evolution of P-loop GTPases and related ATPases
    • 10.1006/jmbi.2001.5378, 11916378
    • Leipe DD, Wolf YI, Koonin EV, Aravind L. Classification and evolution of P-loop GTPases and related ATPases. J Mol Biol 2002, 317:41-72. 10.1006/jmbi.2001.5378, 11916378.
    • (2002) J Mol Biol , vol.317 , pp. 41-72
    • Leipe, D.D.1    Wolf, Y.I.2    Koonin, E.V.3    Aravind, L.4
  • 30
  • 31
    • 67651230544 scopus 로고    scopus 로고
    • Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases
    • 10.1021/bi9006989, 2883566, 19469550
    • Shan SO, Schmid SL, Zhang X. Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases. Biochemistry 2009, 48:6696-6704. 10.1021/bi9006989, 2883566, 19469550.
    • (2009) Biochemistry , vol.48 , pp. 6696-6704
    • Shan, S.O.1    Schmid, S.L.2    Zhang, X.3
  • 32
    • 35349007899 scopus 로고    scopus 로고
    • Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling
    • 10.1038/nature06173, 17914359
    • Daumke O, Lundmark R, Vallis Y, Martens S, Butler PJ, McMahon HT. Architectural and mechanistic insights into an EHD ATPase involved in membrane remodelling. Nature 2007, 449:923-927. 10.1038/nature06173, 17914359.
    • (2007) Nature , vol.449 , pp. 923-927
    • Daumke, O.1    Lundmark, R.2    Vallis, Y.3    Martens, S.4    Butler, P.J.5    McMahon, H.T.6
  • 33
    • 35748951636 scopus 로고    scopus 로고
    • Crystal structure and mutagenesis of the metallochaperone MeaB: insight into the causes of methylmalonic aciduria
    • 10.1074/jbc.M704850200, 17728257
    • Hubbard PA, Padovani D, Labunska T, Mahlstedt SA, Banerjee R, Drennan CL. Crystal structure and mutagenesis of the metallochaperone MeaB: insight into the causes of methylmalonic aciduria. J Biol Chem 2007, 282:31308-31316. 10.1074/jbc.M704850200, 17728257.
    • (2007) J Biol Chem , vol.282 , pp. 31308-31316
    • Hubbard, P.A.1    Padovani, D.2    Labunska, T.3    Mahlstedt, S.A.4    Banerjee, R.5    Drennan, C.L.6
  • 34
    • 33745520400 scopus 로고    scopus 로고
    • Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element
    • 10.1038/sj.emboj.7601171, 1500855, 16763562
    • Scrima A, Wittinghofer A. Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element. Embo J 2006, 25:2940-2951. 10.1038/sj.emboj.7601171, 1500855, 16763562.
    • (2006) Embo J , vol.25 , pp. 2940-2951
    • Scrima, A.1    Wittinghofer, A.2
  • 36
    • 78650544157 scopus 로고    scopus 로고
    • Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2)
    • 10.1073/pnas.1010322107, 21059949
    • Schwefel D, Frohlich C, Eichhorst J, Wiesner B, Behlke J, Aravind L, Daumke O. Structural basis of oligomerization in septin-like GTPase of immunity-associated protein 2 (GIMAP2). Proc Natl Acad Sci USA 2010, 107:20299-20304. 10.1073/pnas.1010322107, 21059949.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 20299-20304
    • Schwefel, D.1    Frohlich, C.2    Eichhorst, J.3    Wiesner, B.4    Behlke, J.5    Aravind, L.6    Daumke, O.7
  • 37
    • 33845672530 scopus 로고    scopus 로고
    • A bacterial dynamin-like protein
    • 10.1038/nature05312, 17122778
    • Low HH, Lowe J. A bacterial dynamin-like protein. Nature 2006, 444:766-769. 10.1038/nature05312, 17122778.
    • (2006) Nature , vol.444 , pp. 766-769
    • Low, H.H.1    Lowe, J.2
  • 39
    • 13444281991 scopus 로고    scopus 로고
    • Bacterial chromosome segregation: structure and DNA binding of the Soj dimer--a conserved biological switch
    • 10.1038/sj.emboj.7600530, 545817, 15635448
    • Leonard TA, Butler PJ, Lowe J. Bacterial chromosome segregation: structure and DNA binding of the Soj dimer--a conserved biological switch. Embo J 2005, 24:270-282. 10.1038/sj.emboj.7600530, 545817, 15635448.
    • (2005) Embo J , vol.24 , pp. 270-282
    • Leonard, T.A.1    Butler, P.J.2    Lowe, J.3
  • 40
    • 33748749374 scopus 로고    scopus 로고
    • Structural insights into HypB, a GTP-binding protein that regulates metal binding
    • 10.1074/jbc.M600809200, 16807243
    • Gasper R, Scrima A, Wittinghofer A. Structural insights into HypB, a GTP-binding protein that regulates metal binding. J Biol Chem 2006, 281:27492-27502. 10.1074/jbc.M600809200, 16807243.
    • (2006) J Biol Chem , vol.281 , pp. 27492-27502
    • Gasper, R.1    Scrima, A.2    Wittinghofer, A.3
  • 41
    • 0030611701 scopus 로고    scopus 로고
    • Structure of ADP × AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction
    • 10.1038/387370a0, 9163420
    • Schindelin H, Kisker C, Schlessman JL, Howard JB, Rees DC. Structure of ADP × AIF4(-)-stabilized nitrogenase complex and its implications for signal transduction. Nature 1997, 387:370-376. 10.1038/387370a0, 9163420.
    • (1997) Nature , vol.387 , pp. 370-376
    • Schindelin, H.1    Kisker, C.2    Schlessman, J.L.3    Howard, J.B.4    Rees, D.C.5
  • 42
    • 33644772427 scopus 로고    scopus 로고
    • How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP
    • 10.1038/nature04510, 16511497
    • Ghosh A, Praefcke GJ, Renault L, Wittinghofer A, Herrmann C. How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP. Nature 2006, 440:101-104. 10.1038/nature04510, 16511497.
    • (2006) Nature , vol.440 , pp. 101-104
    • Ghosh, A.1    Praefcke, G.J.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 43
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • 10.1038/nature09032, 2879890, 20428113
    • Chappie JS, Acharya S, Leonard M, Schmid SL, Dyda F. G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature 2010, 465:435-440. 10.1038/nature09032, 2879890, 20428113.
    • (2010) Nature , vol.465 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 44
    • 0030772378 scopus 로고    scopus 로고
    • The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants
    • 10.1126/science.277.5324.333, 9219684
    • Scheffzek K, Ahmadian MR, Kabsch W, Wiesmuller L, Lautwein A, Schmitz F, Wittinghofer A. The Ras-RasGAP complex: structural basis for GTPase activation and its loss in oncogenic Ras mutants. Science 1997, 277:333-338. 10.1126/science.277.5324.333, 9219684.
    • (1997) Science , vol.277 , pp. 333-338
    • Scheffzek, K.1    Ahmadian, M.R.2    Kabsch, W.3    Wiesmuller, L.4    Lautwein, A.5    Schmitz, F.6    Wittinghofer, A.7
  • 45
    • 0030982264 scopus 로고    scopus 로고
    • Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis
    • 10.1016/S0092-8674(00)80204-4, 9108480
    • Tesmer JJ, Berman DM, Gilman AG, Sprang SR. Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis. Cell 1997, 89:251-261. 10.1016/S0092-8674(00)80204-4, 9108480.
    • (1997) Cell , vol.89 , pp. 251-261
    • Tesmer, J.J.1    Berman, D.M.2    Gilman, A.G.3    Sprang, S.R.4
  • 46
    • 2442669194 scopus 로고    scopus 로고
    • The GTPase-activating protein Rap1GAP uses a catalytic asparagine
    • 10.1038/nature02505, 15141215
    • Daumke O, Weyand M, Chakrabarti PP, Vetter IR, Wittinghofer A. The GTPase-activating protein Rap1GAP uses a catalytic asparagine. Nature 2004, 429:197-201. 10.1038/nature02505, 15141215.
    • (2004) Nature , vol.429 , pp. 197-201
    • Daumke, O.1    Weyand, M.2    Chakrabarti, P.P.3    Vetter, I.R.4    Wittinghofer, A.5
  • 47
    • 8844253060 scopus 로고    scopus 로고
    • Mechanism of association and reciprocal activation of two GTPases
    • 10.1371/journal.pbio.0020320, 517823, 15383838
    • Shan SO, Stroud RM, Walter P. Mechanism of association and reciprocal activation of two GTPases. PLoS Biol 2004, 2:e320. 10.1371/journal.pbio.0020320, 517823, 15383838.
    • (2004) PLoS Biol , vol.2
    • Shan, S.O.1    Stroud, R.M.2    Walter, P.3
  • 48
    • 0037033983 scopus 로고    scopus 로고
    • RanGAP mediates GTP hydrolysis without an arginine finger
    • 10.1038/415662a, 11832950
    • Seewald MJ, Korner C, Wittinghofer A, Vetter IR. RanGAP mediates GTP hydrolysis without an arginine finger. Nature 2002, 415:662-666. 10.1038/415662a, 11832950.
    • (2002) Nature , vol.415 , pp. 662-666
    • Seewald, M.J.1    Korner, C.2    Wittinghofer, A.3    Vetter, I.R.4
  • 49
    • 41949114173 scopus 로고    scopus 로고
    • The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues
    • 10.1038/emboj.2008.30, 2265111, 18309292
    • Scrima A, Thomas C, Deaconescu D, Wittinghofer A. The Rap-RapGAP complex: GTP hydrolysis without catalytic glutamine and arginine residues. Embo J 2008, 27:1145-1153. 10.1038/emboj.2008.30, 2265111, 18309292.
    • (2008) Embo J , vol.27 , pp. 1145-1153
    • Scrima, A.1    Thomas, C.2    Deaconescu, D.3    Wittinghofer, A.4
  • 50
    • 65449163019 scopus 로고    scopus 로고
    • Virulent Toxoplasma gondii evade immunity-related GTPase-mediated parasite vacuole disruption within primed macrophages
    • 10.4049/jimmunol.0804190, 2848815, 19265156
    • Zhao Y, Ferguson DJ, Wilson DC, Howard JC, Sibley LD, Yap GS. Virulent Toxoplasma gondii evade immunity-related GTPase-mediated parasite vacuole disruption within primed macrophages. J Immunol 2009, 182:3775-3781. 10.4049/jimmunol.0804190, 2848815, 19265156.
    • (2009) J Immunol , vol.182 , pp. 3775-3781
    • Zhao, Y.1    Ferguson, D.J.2    Wilson, D.C.3    Howard, J.C.4    Sibley, L.D.5    Yap, G.S.6
  • 51
    • 33847332992 scopus 로고    scopus 로고
    • ROP18 is a rhoptry kinase controlling the intracellular proliferation of Toxoplasma gondii
    • 10.1371/journal.ppat.0030014, 1797617, 17305424
    • El Hajj H, Lebrun M, Arold ST, Vial H, Labesse G, Dubremetz JF. ROP18 is a rhoptry kinase controlling the intracellular proliferation of Toxoplasma gondii. PLoS Pathog 2007, 3:e14. 10.1371/journal.ppat.0030014, 1797617, 17305424.
    • (2007) PLoS Pathog , vol.3
    • El Hajj, H.1    Lebrun, M.2    Arold, S.T.3    Vial, H.4    Labesse, G.5    Dubremetz, J.F.6
  • 53
    • 0036533657 scopus 로고    scopus 로고
    • The IFN-inducible Golgi- and endoplasmic reticulum-associated 47-kDa GTPase IIGP is transiently expressed during listeriosis
    • Zerrahn J, Schaible UE, Brinkmann V, Guhlich U, Kaufmann SH. The IFN-inducible Golgi- and endoplasmic reticulum-associated 47-kDa GTPase IIGP is transiently expressed during listeriosis. J Immunol 2002, 168:3428-3436.
    • (2002) J Immunol , vol.168 , pp. 3428-3436
    • Zerrahn, J.1    Schaible, U.E.2    Brinkmann, V.3    Guhlich, U.4    Kaufmann, S.H.5
  • 54
    • 0030432118 scopus 로고    scopus 로고
    • Ras and its effectors
    • 10.1016/S0079-6107(96)00015-6, 9107131
    • Herrmann C, Nassar N. Ras and its effectors. Prog Biophys Mol Biol 1996, 66:1-41. 10.1016/S0079-6107(96)00015-6, 9107131.
    • (1996) Prog Biophys Mol Biol , vol.66 , pp. 1-41
    • Herrmann, C.1    Nassar, N.2
  • 55
    • 0032167449 scopus 로고    scopus 로고
    • Specific antiviral activity demonstrated by TGTP, a member of a new family of interferon-induced GTPases
    • Carlow DA, Teh SJ, Teh HS. Specific antiviral activity demonstrated by TGTP, a member of a new family of interferon-induced GTPases. J Immunol 1998, 161:2348-2355.
    • (1998) J Immunol , vol.161 , pp. 2348-2355
    • Carlow, D.A.1    Teh, S.J.2    Teh, H.S.3
  • 56
    • 0032521215 scopus 로고    scopus 로고
    • GRA7, an excretory 29 kDa Toxoplasma gondii dense granule antigen released by infected host cells
    • 10.1016/S0166-6851(97)00227-2, 9566518
    • Fischer HG, Stachelhaus S, Sahm M, Meyer HE, Reichmann G. GRA7, an excretory 29 kDa Toxoplasma gondii dense granule antigen released by infected host cells. Mol Biochem Parasitol 1998, 91:251-262. 10.1016/S0166-6851(97)00227-2, 9566518.
    • (1998) Mol Biochem Parasitol , vol.91 , pp. 251-262
    • Fischer, H.G.1    Stachelhaus, S.2    Sahm, M.3    Meyer, H.E.4    Reichmann, G.5
  • 58
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • 10.1002/elps.1150181505, 9504803
    • Guex N, Peitsch MC. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 1997, 18:2714-2723. 10.1002/elps.1150181505, 9504803.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 60
    • 0015222647 scopus 로고
    • The interpretation of protein structures: estimation of static accessibility
    • 10.1016/0022-2836(71)90324-X, 5551392
    • Lee B, Richards FM. The interpretation of protein structures: estimation of static accessibility. J Mol Biol 1971, 55:379-400. 10.1016/0022-2836(71)90324-X, 5551392.
    • (1971) J Mol Biol , vol.55 , pp. 379-400
    • Lee, B.1    Richards, F.M.2
  • 62
    • 2542445427 scopus 로고    scopus 로고
    • ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information
    • 10.1093/bioinformatics/19.1.163, 12499312
    • Glaser F, Pupko T, Paz I, Bell RE, Bechor-Shental D, Martz E, Ben-Tal N. ConSurf: identification of functional regions in proteins by surface-mapping of phylogenetic information. Bioinformatics 2003, 19:163-164. 10.1093/bioinformatics/19.1.163, 12499312.
    • (2003) Bioinformatics , vol.19 , pp. 163-164
    • Glaser, F.1    Pupko, T.2    Paz, I.3    Bell, R.E.4    Bechor-Shental, D.5    Martz, E.6    Ben-Tal, N.7
  • 63
    • 23144448512 scopus 로고    scopus 로고
    • ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures
    • 10.1093/nar/gki370, 1160131, 15980475
    • Landau M, Mayrose I, Rosenberg Y, Glaser F, Martz E, Pupko T, Ben-Tal N. ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures. Nucleic Acids Res 2005, 33:W299-302. 10.1093/nar/gki370, 1160131, 15980475.
    • (2005) Nucleic Acids Res , vol.33
    • Landau, M.1    Mayrose, I.2    Rosenberg, Y.3    Glaser, F.4    Martz, E.5    Pupko, T.6    Ben-Tal, N.7


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