메뉴 건너뛰기




Volumn 428, Issue 17, 2016, Pages 3495-3513

Interferon-Inducible GTPases in Host Resistance, Inflammation and Disease

Author keywords

Crohn's disease; GBP; Inflammasome; IRG; IRGM

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; INFLAMMASOME; INTERFERON; INTERFERON INDUCIBLE GUANOSINE TRIPHOSPHATASE; MYXOVIRUS RESISTANCE PROTEIN; UNCLASSIFIED DRUG;

EID: 84969579633     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2016.04.032     Document Type: Review
Times cited : (167)

References (141)
  • 1
    • 84877605000 scopus 로고    scopus 로고
    • Cellular self-defense: how cell-autonomous immunity protects against pathogens
    • [1] Randow, F., MacMicking, J.D., James, L.C., Cellular self-defense: how cell-autonomous immunity protects against pathogens. Science 340 (2013), 701–706.
    • (2013) Science , vol.340 , pp. 701-706
    • Randow, F.1    MacMicking, J.D.2    James, L.C.3
  • 2
    • 34547697113 scopus 로고    scopus 로고
    • Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymes
    • [2] Kawahara, T., Quinn, M.T., Lambeth, J.D., Molecular evolution of the reactive oxygen-generating NADPH oxidase (Nox/Duox) family of enzymes. BMC Evol. Biol., 7, 2007, 109.
    • (2007) BMC Evol. Biol. , vol.7 , pp. 109
    • Kawahara, T.1    Quinn, M.T.2    Lambeth, J.D.3
  • 4
    • 18844457095 scopus 로고    scopus 로고
    • Mechanisms of type-I- and type-II-interferon-mediated signalling
    • [4] Platanias, L.C., Mechanisms of type-I- and type-II-interferon-mediated signalling. Nat. Rev. Immunol. 5 (2005), 375–386.
    • (2005) Nat. Rev. Immunol. , vol.5 , pp. 375-386
    • Platanias, L.C.1
  • 5
    • 0020607951 scopus 로고
    • Interferon induces a unique protein in mouse cells bearing a gene for resistance to influenza virus
    • [5] Horisberger, M.A., Staeheli, P., Haller, O., Interferon induces a unique protein in mouse cells bearing a gene for resistance to influenza virus. Proc. Natl. Acad. Sci. U. S. A. 80 (1983), 1910–1914.
    • (1983) Proc. Natl. Acad. Sci. U. S. A. , vol.80 , pp. 1910-1914
    • Horisberger, M.A.1    Staeheli, P.2    Haller, O.3
  • 6
    • 0020955866 scopus 로고
    • Interferon induction of fibroblast proteins with guanylate binding activity
    • [6] Cheng, Y.S., Colonno, R.J., Yin, F.H., Interferon induction of fibroblast proteins with guanylate binding activity. J. Biol. Chem. 258 (1983), 7746–7750.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7746-7750
    • Cheng, Y.S.1    Colonno, R.J.2    Yin, F.H.3
  • 7
    • 0022540467 scopus 로고
    • Mx protein: constitutive expression in 3 T3 cells transformed with cloned Mx cDNA confers selective resistance to influenza virus
    • [7] Staeheli, P., Haller, O., Boll, W., Lindenmann, J., Weissmann, C., Mx protein: constitutive expression in 3 T3 cells transformed with cloned Mx cDNA confers selective resistance to influenza virus. Cell 44 (1986), 147–158.
    • (1986) Cell , vol.44 , pp. 147-158
    • Staeheli, P.1    Haller, O.2    Boll, W.3    Lindenmann, J.4    Weissmann, C.5
  • 8
    • 0023791475 scopus 로고
    • Influenza virus-susceptible mice carry mx genes with a large deletion or a nonsense mutation
    • [8] Staeheli, P., Grob, R., Meier, E., Sutcliffe, J.G., Haller, O., Influenza virus-susceptible mice carry mx genes with a large deletion or a nonsense mutation. Mol. Cell. Biol. 8 (1988), 4518–4523.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4518-4523
    • Staeheli, P.1    Grob, R.2    Meier, E.3    Sutcliffe, J.G.4    Haller, O.5
  • 9
    • 0023470520 scopus 로고
    • Influenza virus resistance of wild mice: wild-type and mutant mx alleles occur at comparable frequencies
    • [9] Haller, O., Acklin, M., Staeheli, P., Influenza virus resistance of wild mice: wild-type and mutant mx alleles occur at comparable frequencies. J. Interf. Res. 7 (1987), 647–656.
    • (1987) J. Interf. Res. , vol.7 , pp. 647-656
    • Haller, O.1    Acklin, M.2    Staeheli, P.3
  • 10
    • 0001368677 scopus 로고
    • Resistance of mice to mouse-adapted influenza A virus
    • [10] Lindenmann, J., Resistance of mice to mouse-adapted influenza A virus. Virology 16 (1962), 203–204.
    • (1962) Virology , vol.16 , pp. 203-204
    • Lindenmann, J.1
  • 12
    • 33748506089 scopus 로고    scopus 로고
    • Human IRGM induces autophagy to eliminate intracellular mycobacteria
    • [12] Singh, S.B., Davis, A.S., Taylor, G.A., Deretic, V., Human IRGM induces autophagy to eliminate intracellular mycobacteria. Science 313 (2006), 1438–1441.
    • (2006) Science , vol.313 , pp. 1438-1441
    • Singh, S.B.1    Davis, A.S.2    Taylor, G.A.3    Deretic, V.4
  • 13
    • 0142240338 scopus 로고    scopus 로고
    • Immune control of tuberculosis by IFN-gamma-inducible LRG-47
    • [13] MacMicking, J.D., Taylor, G.A., McKinney, J.D., Immune control of tuberculosis by IFN-gamma-inducible LRG-47. Science 302 (2003), 654–659.
    • (2003) Science , vol.302 , pp. 654-659
    • MacMicking, J.D.1    Taylor, G.A.2    McKinney, J.D.3
  • 14
    • 33748995352 scopus 로고    scopus 로고
    • The p47 GTPases Igtp and Irgb10 map to the Chlamydia trachomatis susceptibility locus Ctrq-3 and mediate cellular resistance in mice
    • [14] Bernstein-Hanley, I., Coers, J., Balsara, Z.R., Taylor, G.A., Starnbach, M.N., Dietrich, W.F., The p47 GTPases Igtp and Irgb10 map to the Chlamydia trachomatis susceptibility locus Ctrq-3 and mediate cellular resistance in mice. Proc. Natl. Acad. Sci. U. S. A. 103 (2006), 14,092–14,097.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 14092-14097
    • Bernstein-Hanley, I.1    Coers, J.2    Balsara, Z.R.3    Taylor, G.A.4    Starnbach, M.N.5    Dietrich, W.F.6
  • 15
    • 34347338690 scopus 로고    scopus 로고
    • Sequence variants in the autophagy gene IRGM and multiple other replicating loci contribute to Crohn's disease susceptibility
    • [15] Parkes, M., Barrett, J.C., Prescott, N.J., Tremelling, M., Anderson, C.A., Fisher, S.A., et al. Sequence variants in the autophagy gene IRGM and multiple other replicating loci contribute to Crohn's disease susceptibility. Nat. Genet. 39 (2007), 830–832.
    • (2007) Nat. Genet. , vol.39 , pp. 830-832
    • Parkes, M.1    Barrett, J.C.2    Prescott, N.J.3    Tremelling, M.4    Anderson, C.A.5    Fisher, S.A.6
  • 16
    • 34247554965 scopus 로고    scopus 로고
    • Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis
    • [16] Rioux, J.D., Xavier, R.J., Taylor, K.D., Silverberg, M.S., Goyette, P., Huett, A., et al. Genome-wide association study identifies new susceptibility loci for Crohn disease and implicates autophagy in disease pathogenesis. Nat. Genet. 39 (2007), 596–604.
    • (2007) Nat. Genet. , vol.39 , pp. 596-604
    • Rioux, J.D.1    Xavier, R.J.2    Taylor, K.D.3    Silverberg, M.S.4    Goyette, P.5    Huett, A.6
  • 17
    • 84925410974 scopus 로고    scopus 로고
    • Mx GTPases: dynamin-like antiviral machines of innate immunity
    • [17] Haller, O., Staeheli, P., Schwemmle, M., Kochs, G., Mx GTPases: dynamin-like antiviral machines of innate immunity. Trends Microbiol. 23 (2015), 154–163.
    • (2015) Trends Microbiol. , vol.23 , pp. 154-163
    • Haller, O.1    Staeheli, P.2    Schwemmle, M.3    Kochs, G.4
  • 18
    • 34447268941 scopus 로고    scopus 로고
    • Induction of MxA gene expression by influenza A virus requires type I or type III interferon signaling
    • [18] Holzinger, D., Jorns, C., Stertz, S., Boisson-Dupuis, S., Thimme, R., Weidmann, M., et al. Induction of MxA gene expression by influenza A virus requires type I or type III interferon signaling. J. Virol. 81 (2007), 7776–7785.
    • (2007) J. Virol. , vol.81 , pp. 7776-7785
    • Holzinger, D.1    Jorns, C.2    Stertz, S.3    Boisson-Dupuis, S.4    Thimme, R.5    Weidmann, M.6
  • 19
    • 0025369703 scopus 로고
    • Transgenic mice with intracellular immunity to influenza virus
    • [19] Arnheiter, H., Skuntz, S., Noteborn, M., Chang, S., Meier, E., Transgenic mice with intracellular immunity to influenza virus. Cell 62 (1990), 51–61.
    • (1990) Cell , vol.62 , pp. 51-61
    • Arnheiter, H.1    Skuntz, S.2    Noteborn, M.3    Chang, S.4    Meier, E.5
  • 20
    • 0029029528 scopus 로고
    • Enhanced virus resistance of transgenic mice expressing the human MxA protein
    • [20] Pavlovic, J., Arzet, H.A., Hefti, H.P., Frese, M., Rost, D., Ernst, B., et al. Enhanced virus resistance of transgenic mice expressing the human MxA protein. J. Virol. 69 (1995), 4506–4510.
    • (1995) J. Virol. , vol.69 , pp. 4506-4510
    • Pavlovic, J.1    Arzet, H.A.2    Hefti, H.P.3    Frese, M.4    Rost, D.5    Ernst, B.6
  • 21
    • 84875985517 scopus 로고    scopus 로고
    • Pandemic influenza A viruses escape from restriction by human MxA through adaptive mutations in the nucleoprotein
    • e1003279
    • [21] Manz, B., Dornfeld, D., Gotz, V., Zell, R., Zimmermann, P., Haller, O., et al. Pandemic influenza A viruses escape from restriction by human MxA through adaptive mutations in the nucleoprotein. PLoS Pathog., 9, 2013, e1003279.
    • (2013) PLoS Pathog. , vol.9
    • Manz, B.1    Dornfeld, D.2    Gotz, V.3    Zell, R.4    Zimmermann, P.5    Haller, O.6
  • 22
    • 84886949134 scopus 로고    scopus 로고
    • MX2 is an interferon-induced inhibitor of HIV-1 infection
    • [22] Kane, M., Yadav, S.S., Bitzegeio, J., Kutluay, S.B., Zang, T., Wilson, S.J., et al. MX2 is an interferon-induced inhibitor of HIV-1 infection. Nature 502 (2013), 563–566.
    • (2013) Nature , vol.502 , pp. 563-566
    • Kane, M.1    Yadav, S.S.2    Bitzegeio, J.3    Kutluay, S.B.4    Zang, T.5    Wilson, S.J.6
  • 23
    • 84886953102 scopus 로고    scopus 로고
    • Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection
    • [23] Goujon, C., Moncorge, O., Bauby, H., Doyle, T., Ward, C.C., Schaller, T., et al. Human MX2 is an interferon-induced post-entry inhibitor of HIV-1 infection. Nature 502 (2013), 559–562.
    • (2013) Nature , vol.502 , pp. 559-562
    • Goujon, C.1    Moncorge, O.2    Bauby, H.3    Doyle, T.4    Ward, C.C.5    Schaller, T.6
  • 24
    • 84885987626 scopus 로고    scopus 로고
    • The interferon-inducible MxB protein inhibits HIV-1 infection
    • [24] Liu, Z., Pan, Q., Ding, S., Qian, J., Xu, F., Zhou, J., et al. The interferon-inducible MxB protein inhibits HIV-1 infection. Cell Host Microbe 14 (2013), 398–410.
    • (2013) Cell Host Microbe , vol.14 , pp. 398-410
    • Liu, Z.1    Pan, Q.2    Ding, S.3    Qian, J.4    Xu, F.5    Zhou, J.6
  • 25
    • 84953211349 scopus 로고    scopus 로고
    • Evolutionary analyses suggest a function of MxB immunity proteins beyond Lentivirus restriction
    • e1005304
    • [25] Mitchell, P.S., Young, J.M., Emerman, M., Malik, H.S., Evolutionary analyses suggest a function of MxB immunity proteins beyond Lentivirus restriction. PLoS Pathog., 11, 2015, e1005304.
    • (2015) PLoS Pathog. , vol.11
    • Mitchell, P.S.1    Young, J.M.2    Emerman, M.3    Malik, H.S.4
  • 26
    • 84882883270 scopus 로고    scopus 로고
    • An evolutionary perspective on the broad antiviral specificity of MxA
    • [26] Mitchell, P.S., Emerman, M., Malik, H.S., An evolutionary perspective on the broad antiviral specificity of MxA. Curr. Opin. Microbiol. 16 (2013), 493–499.
    • (2013) Curr. Opin. Microbiol. , vol.16 , pp. 493-499
    • Mitchell, P.S.1    Emerman, M.2    Malik, H.S.3
  • 27
    • 80755153638 scopus 로고    scopus 로고
    • Structure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the antiviral function
    • [27] Gao, S., von der Malsburg, A., Dick, A., Faelber, K., Schroder, G.F., Haller, O., et al. Structure of myxovirus resistance protein a reveals intra- and intermolecular domain interactions required for the antiviral function. Immunity 35 (2011), 514–525.
    • (2011) Immunity , vol.35 , pp. 514-525
    • Gao, S.1    von der Malsburg, A.2    Dick, A.3    Faelber, K.4    Schroder, G.F.5    Haller, O.6
  • 28
    • 77953028450 scopus 로고    scopus 로고
    • Structural basis of oligomerization in the stalk region of dynamin-like MxA
    • [28] Gao, S., von der Malsburg, A., Paeschke, S., Behlke, J., Haller, O., Kochs, G., et al. Structural basis of oligomerization in the stalk region of dynamin-like MxA. Nature 465 (2010), 502–506.
    • (2010) Nature , vol.465 , pp. 502-506
    • Gao, S.1    von der Malsburg, A.2    Paeschke, S.3    Behlke, J.4    Haller, O.5    Kochs, G.6
  • 29
    • 0026524496 scopus 로고
    • Human and mouse Mx proteins inhibit different steps of the influenza virus multiplication cycle
    • [29] Pavlovic, J., Haller, O., Staeheli, P., Human and mouse Mx proteins inhibit different steps of the influenza virus multiplication cycle. J. Virol. 66 (1992), 2564–2569.
    • (1992) J. Virol. , vol.66 , pp. 2564-2569
    • Pavlovic, J.1    Haller, O.2    Staeheli, P.3
  • 30
    • 0022374451 scopus 로고
    • Inhibition of influenza viral mRNA synthesis in cells expressing the interferon-induced Mx gene product
    • [30] Krug, R.M., Shaw, M., Broni, B., Shapiro, G., Haller, O., Inhibition of influenza viral mRNA synthesis in cells expressing the interferon-induced Mx gene product. J. Virol. 56 (1985), 201–206.
    • (1985) J. Virol. , vol.56 , pp. 201-206
    • Krug, R.M.1    Shaw, M.2    Broni, B.3    Shapiro, G.4    Haller, O.5
  • 31
    • 0026550735 scopus 로고
    • Mouse Mx2 protein inhibits vesicular stomatitis virus but not influenza virus
    • [31] Zurcher, T., Pavlovic, J., Staeheli, P., Mouse Mx2 protein inhibits vesicular stomatitis virus but not influenza virus. Virology 187 (1992), 796–800.
    • (1992) Virology , vol.187 , pp. 796-800
    • Zurcher, T.1    Pavlovic, J.2    Staeheli, P.3
  • 32
    • 67649376348 scopus 로고    scopus 로고
    • The evolutionarily dynamic IFN-inducible GTPase proteins play conserved immune functions in vertebrates and cephalochordates
    • [32] Li, G., Zhang, J., Sun, Y., Wang, H., Wang, Y., The evolutionarily dynamic IFN-inducible GTPase proteins play conserved immune functions in vertebrates and cephalochordates. Mol. Biol. Evol. 26 (2009), 1619–1630.
    • (2009) Mol. Biol. Evol. , vol.26 , pp. 1619-1630
    • Li, G.1    Zhang, J.2    Sun, Y.3    Wang, H.4    Wang, Y.5
  • 33
    • 33744509713 scopus 로고    scopus 로고
    • The interferon-inducible p47 (IRG) GTPases in vertebrates: loss of the cell autonomous resistance mechanism in the human lineage
    • [33] Bekpen, C., Hunn, J.P., Rohde, C., Parvanova, I., Guethlein, L., Dunn, D.M., et al. The interferon-inducible p47 (IRG) GTPases in vertebrates: loss of the cell autonomous resistance mechanism in the human lineage. Genome Biol., 6, 2005, R92.
    • (2005) Genome Biol. , vol.6 , pp. R92
    • Bekpen, C.1    Hunn, J.P.2    Rohde, C.3    Parvanova, I.4    Guethlein, L.5    Dunn, D.M.6
  • 35
    • 84867647908 scopus 로고    scopus 로고
    • Rules of engagement: molecular insights from host-virus arms races
    • [35] Daugherty, M.D., Malik, H.S., Rules of engagement: molecular insights from host-virus arms races. Annu. Rev. Genet. 46 (2012), 677–700.
    • (2012) Annu. Rev. Genet. , vol.46 , pp. 677-700
    • Daugherty, M.D.1    Malik, H.S.2
  • 36
    • 79959348595 scopus 로고    scopus 로고
    • Virulence differences in toxoplasma mediated by amplification of a family of polymorphic pseudokinases
    • [36] Behnke, M.S., Khan, A., Wootton, J.C., Dubey, J.P., Tang, K., Sibley, L.D., Virulence differences in toxoplasma mediated by amplification of a family of polymorphic pseudokinases. Proc. Natl. Acad. Sci. U. S. A. 108 (2011), 9631–9636.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 9631-9636
    • Behnke, M.S.1    Khan, A.2    Wootton, J.C.3    Dubey, J.P.4    Tang, K.5    Sibley, L.D.6
  • 38
    • 84887340478 scopus 로고    scopus 로고
    • Reciprocal virulence and resistance polymorphism in the relationship between Toxoplasma gondii and the house mouse
    • e01298
    • [38] Lilue, J., Muller, U.B., Steinfeldt, T., Howard, J.C., Reciprocal virulence and resistance polymorphism in the relationship between Toxoplasma gondii and the house mouse. Elife, 2, 2013, e01298.
    • (2013) Elife , vol.2
    • Lilue, J.1    Muller, U.B.2    Steinfeldt, T.3    Howard, J.C.4
  • 39
    • 53549109432 scopus 로고    scopus 로고
    • Regulatory interactions between IRG resistance GTPases in the cellular response to Toxoplasma gondii
    • [39] Hunn, J.P., Koenen-Waisman, S., Papic, N., Schroeder, N., Pawlowski, N., Lange, R., et al. Regulatory interactions between IRG resistance GTPases in the cellular response to Toxoplasma gondii. EMBO J. 27 (2008), 2495–2509.
    • (2008) EMBO J. , vol.27 , pp. 2495-2509
    • Hunn, J.P.1    Koenen-Waisman, S.2    Papic, N.3    Schroeder, N.4    Pawlowski, N.5    Lange, R.6
  • 40
    • 44449088023 scopus 로고    scopus 로고
    • Chlamydia muridarum evades growth restriction by the IFN-gamma-inducible host resistance factor Irgb10
    • [40] Coers, J., Bernstein-Hanley, I., Grotsky, D., Parvanova, I., Howard, J.C., Taylor, G.A., et al. Chlamydia muridarum evades growth restriction by the IFN-gamma-inducible host resistance factor Irgb10. J. Immunol. 180 (2008), 6237–6245.
    • (2008) J. Immunol. , vol.180 , pp. 6237-6245
    • Coers, J.1    Bernstein-Hanley, I.2    Grotsky, D.3    Parvanova, I.4    Howard, J.C.5    Taylor, G.A.6
  • 41
    • 84879547102 scopus 로고    scopus 로고
    • IRG and GBP host resistance factors target aberrant, “non-self” vacuoles characterized by the missing of “self” IRGM proteins
    • e1003414
    • [41] Haldar, A.K., Saka, H.A., Piro, A.S., Dunn, J.D., Henry, S.C., Taylor, G.A., et al. IRG and GBP host resistance factors target aberrant, “non-self” vacuoles characterized by the missing of “self” IRGM proteins. PLoS Pathog., 9, 2013, e1003414.
    • (2013) PLoS Pathog. , vol.9
    • Haldar, A.K.1    Saka, H.A.2    Piro, A.S.3    Dunn, J.D.4    Henry, S.C.5    Taylor, G.A.6
  • 42
    • 49649126253 scopus 로고    scopus 로고
    • Disruption of Toxoplasma gondii parasitophorous vacuoles by the mouse p47-resistance GTPases
    • e24
    • [42] Martens, S., Parvanova, I., Zerrahn, J., Griffiths, G., Schell, G., Reichmann, G., et al. Disruption of Toxoplasma gondii parasitophorous vacuoles by the mouse p47-resistance GTPases. PLoS Pathog., 1, 2005, e24.
    • (2005) PLoS Pathog. , vol.1
    • Martens, S.1    Parvanova, I.2    Zerrahn, J.3    Griffiths, G.4    Schell, G.5    Reichmann, G.6
  • 43
    • 84884688909 scopus 로고    scopus 로고
    • Self and non-self discrimination of intracellular membranes by the innate immune system
    • e1003538
    • [43] Coers, J., Self and non-self discrimination of intracellular membranes by the innate immune system. PLoS Pathog., 9, 2013, e1003538.
    • (2013) PLoS Pathog. , vol.9
    • Coers, J.1
  • 44
    • 84908330381 scopus 로고    scopus 로고
    • Identification of the microsporidian Encephalitozoon cuniculi as a new target of the IFNgamma-inducible IRG resistance system
    • e1004449
    • [44] Ferreira-da-Silva Mda, F., Springer-Frauenhoff, H.M., Bohne, W., Howard, J.C., Identification of the microsporidian Encephalitozoon cuniculi as a new target of the IFNgamma-inducible IRG resistance system. PLoS Pathog., 10, 2014, e1004449.
    • (2014) PLoS Pathog. , vol.10
    • Ferreira-da-Silva Mda, F.1    Springer-Frauenhoff, H.M.2    Bohne, W.3    Howard, J.C.4
  • 45
    • 67651174262 scopus 로고    scopus 로고
    • Targeting of the GTPase Irgm1 to the phagosomal membrane via PtdIns(3,4)P(2) and PtdIns(3,4,5)P(3) promotes immunity to mycobacteria
    • [45] Tiwari, S., Choi, H.P., Matsuzawa, T., Pypaert, M., MacMicking, J.D., Targeting of the GTPase Irgm1 to the phagosomal membrane via PtdIns(3,4)P(2) and PtdIns(3,4,5)P(3) promotes immunity to mycobacteria. Nat. Immunol. 10 (2009), 907–917.
    • (2009) Nat. Immunol. , vol.10 , pp. 907-917
    • Tiwari, S.1    Choi, H.P.2    Matsuzawa, T.3    Pypaert, M.4    MacMicking, J.D.5
  • 46
    • 84881452463 scopus 로고    scopus 로고
    • Irgm1 (LRG-47), a regulator of cell-autonomous immunity, does not localize to mycobacterial or listerial phagosomes in IFN-gamma-induced mouse cells
    • [46] Springer, H.M., Schramm, M., Taylor, G.A., Howard, J.C., Irgm1 (LRG-47), a regulator of cell-autonomous immunity, does not localize to mycobacterial or listerial phagosomes in IFN-gamma-induced mouse cells. J. Immunol. 191 (2013), 1765–1774.
    • (2013) J. Immunol. , vol.191 , pp. 1765-1774
    • Springer, H.M.1    Schramm, M.2    Taylor, G.A.3    Howard, J.C.4
  • 48
    • 84902829671 scopus 로고    scopus 로고
    • The parasitophorous vacuole membrane of Toxoplasma gondii is targeted for disruption by ubiquitin-like conjugation systems of autophagy
    • [48] Choi, J., Park, S., Biering, S.B., Selleck, E., Liu, C.Y., Zhang, X., et al. The parasitophorous vacuole membrane of Toxoplasma gondii is targeted for disruption by ubiquitin-like conjugation systems of autophagy. Immunity 40 (2014), 924–935.
    • (2014) Immunity , vol.40 , pp. 924-935
    • Choi, J.1    Park, S.2    Biering, S.B.3    Selleck, E.4    Liu, C.Y.5    Zhang, X.6
  • 49
    • 84864290306 scopus 로고    scopus 로고
    • IFN-gamma-inducible Irga6 mediates host resistance against chlamydia trachomatis via autophagy
    • e4588
    • [49] Al-Zeer, M.A., Al-Younes, H.M., Braun, P.R., Zerrahn, J., Meyer, T.F., IFN-gamma-inducible Irga6 mediates host resistance against chlamydia trachomatis via autophagy. PLoS One, 4, 2009, e4588.
    • (2009) PLoS One , vol.4
    • Al-Zeer, M.A.1    Al-Younes, H.M.2    Braun, P.R.3    Zerrahn, J.4    Meyer, T.F.5
  • 50
    • 84898471391 scopus 로고    scopus 로고
    • The E2-like conjugation enzyme Atg3 promotes binding of IRG and Gbp proteins to Chlamydia- and Toxoplasma-containing vacuoles and host resistance
    • e86684
    • [50] Haldar, A.K., Piro, A.S., Pilla, D.M., Yamamoto, M., Coers, J., The E2-like conjugation enzyme Atg3 promotes binding of IRG and Gbp proteins to Chlamydia- and Toxoplasma-containing vacuoles and host resistance. PLoS One, 9, 2014, e86684.
    • (2014) PLoS One , vol.9
    • Haldar, A.K.1    Piro, A.S.2    Pilla, D.M.3    Yamamoto, M.4    Coers, J.5
  • 51
    • 84897535028 scopus 로고    scopus 로고
    • Role of mouse and human autophagy proteins in IFN-gamma-induced cell-autonomous responses against Toxoplasma gondii
    • [51] Ohshima, J., Lee, Y., Sasai, M., Saitoh, T., Su Ma, J., Kamiyama, N., et al. Role of mouse and human autophagy proteins in IFN-gamma-induced cell-autonomous responses against Toxoplasma gondii. J. Immunol. 192 (2014), 3328–3335.
    • (2014) J. Immunol. , vol.192 , pp. 3328-3335
    • Ohshima, J.1    Lee, Y.2    Sasai, M.3    Saitoh, T.4    Su Ma, J.5    Kamiyama, N.6
  • 52
    • 84944242576 scopus 로고    scopus 로고
    • Ubiquitin systems mark pathogen-containing vacuoles as targets for host defense by guanylate binding proteins
    • [52] Haldar, A.K., Foltz, C., Finethy, R., Piro, A.S., Feeley, E.M., Pilla-Moffett, D.M., et al. Ubiquitin systems mark pathogen-containing vacuoles as targets for host defense by guanylate binding proteins. Proc. Natl. Acad. Sci. U. S. A. 112 (2015), E5628–E5637.
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. E5628-E5637
    • Haldar, A.K.1    Foltz, C.2    Finethy, R.3    Piro, A.S.4    Feeley, E.M.5    Pilla-Moffett, D.M.6
  • 53
    • 61449117883 scopus 로고    scopus 로고
    • Disruption of the Toxoplasma gondii parasitophorous vacuole by IFNgamma-inducible immunity-related GTPases (IRG proteins) triggers necrotic cell death
    • e1000288
    • [53] Zhao, Y.O., Khaminets, A., Hunn, J.P., Howard, J.C., Disruption of the Toxoplasma gondii parasitophorous vacuole by IFNgamma-inducible immunity-related GTPases (IRG proteins) triggers necrotic cell death. PLoS Pathog., 5, 2009, e1000288.
    • (2009) PLoS Pathog. , vol.5
    • Zhao, Y.O.1    Khaminets, A.2    Hunn, J.P.3    Howard, J.C.4
  • 54
    • 33748444233 scopus 로고    scopus 로고
    • Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages
    • [54] Ling, Y.M., Shaw, M.H., Ayala, C., Coppens, I., Taylor, G.A., Ferguson, D.J., et al. Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages. J. Exp. Med. 203 (2006), 2063–2071.
    • (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
  • 55
    • 84929044812 scopus 로고    scopus 로고
    • From membranes to organelles: emerging roles for dynamin-like proteins in diverse cellular processes
    • [55] Williams, M., Kim, K., From membranes to organelles: emerging roles for dynamin-like proteins in diverse cellular processes. Eur. J. Cell Biol. 93 (2014), 267–277.
    • (2014) Eur. J. Cell Biol. , vol.93 , pp. 267-277
    • Williams, M.1    Kim, K.2
  • 56
    • 84865371084 scopus 로고    scopus 로고
    • A cluster of interferon-gamma-inducible p65 GTPases plays a critical role in host defense against Toxoplasma gondii
    • [56] Yamamoto, M., Okuyama, M., Ma, J.S., Kimura, T., Kamiyama, N., Saiga, H., et al. A cluster of interferon-gamma-inducible p65 GTPases plays a critical role in host defense against Toxoplasma gondii. Immunity, 2012.
    • (2012) Immunity
    • Yamamoto, M.1    Okuyama, M.2    Ma, J.S.3    Kimura, T.4    Kamiyama, N.5    Saiga, H.6
  • 57
    • 0033559566 scopus 로고    scopus 로고
    • Differential sensitivity of distinct Chlamydia trachomatis isolates to IFN-gamma-mediated inhibition
    • [57] Perry, L.L., Su, H., Feilzer, K., Messer, R., Hughes, S., Whitmire, W., et al. Differential sensitivity of distinct Chlamydia trachomatis isolates to IFN-gamma-mediated inhibition. J. Immunol. 162 (1999), 3541–3548.
    • (1999) J. Immunol. , vol.162 , pp. 3541-3548
    • Perry, L.L.1    Su, H.2    Feilzer, K.3    Messer, R.4    Hughes, S.5    Whitmire, W.6
  • 59
    • 84893933058 scopus 로고    scopus 로고
    • Innate resistance against Toxoplasma gondii: an evolutionary tale of mice, cats, and men
    • [59] Gazzinelli, R.T., Mendonca-Neto, R., Lilue, J., Howard, J., Sher, A., Innate resistance against Toxoplasma gondii: an evolutionary tale of mice, cats, and men. Cell Host Microbe 15 (2014), 132–138.
    • (2014) Cell Host Microbe , vol.15 , pp. 132-138
    • Gazzinelli, R.T.1    Mendonca-Neto, R.2    Lilue, J.3    Howard, J.4    Sher, A.5
  • 60
    • 0035898464 scopus 로고    scopus 로고
    • Inactivation of LRG-47 and IRG-47 reveals a family of interferon gamma-inducible genes with essential, pathogen-specific roles in resistance to infection
    • [60] Collazo, C.M., Yap, G.S., Sempowski, G.D., Lusby, K.C., Tessarollo, L., Woude, G.F., et al. Inactivation of LRG-47 and IRG-47 reveals a family of interferon gamma-inducible genes with essential, pathogen-specific roles in resistance to infection. J. Exp. Med. 194 (2001), 181–188.
    • (2001) J. Exp. Med. , vol.194 , pp. 181-188
    • Collazo, C.M.1    Yap, G.S.2    Sempowski, G.D.3    Lusby, K.C.4    Tessarollo, L.5    Woude, G.F.6
  • 61
    • 77954430293 scopus 로고    scopus 로고
    • Coordinated loading of IRG resistance GTPases on to the Toxoplasma gondii parasitophorous vacuole
    • [61] Khaminets, A., Hunn, J.P., Konen-Waisman, S., Zhao, Y.O., Preukschat, D., Coers, J., et al. Coordinated loading of IRG resistance GTPases on to the Toxoplasma gondii parasitophorous vacuole. Cell. Microbiol. 12 (2010), 939–961.
    • (2010) Cell. Microbiol. , vol.12 , pp. 939-961
    • Khaminets, A.1    Hunn, J.P.2    Konen-Waisman, S.3    Zhao, Y.O.4    Preukschat, D.5    Coers, J.6
  • 62
    • 65449163019 scopus 로고    scopus 로고
    • Virulent Toxoplasma gondii evade immunity-related GTPase-mediated parasite vacuole disruption within primed macrophages
    • [62] Zhao, Y., Ferguson, D.J., Wilson, D.C., Howard, J.C., Sibley, L.D., Yap, G.S., Virulent Toxoplasma gondii evade immunity-related GTPase-mediated parasite vacuole disruption within primed macrophages. J. Immunol. 182 (2009), 3775–3781.
    • (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
  • 63
    • 84864075588 scopus 로고    scopus 로고
    • The rhoptry proteins ROP18 and ROP5 mediate Toxoplasma gondii evasion of the murine, but not the human, interferon-gamma response
    • e1002784
    • [63] Niedelman, W., Gold, D.A., Rosowski, E.E., Sprokholt, J.K., Lim, D., Farid Arenas, A., et al. The rhoptry proteins ROP18 and ROP5 mediate Toxoplasma gondii evasion of the murine, but not the human, interferon-gamma response. PLoS Pathog., 8, 2012, e1002784.
    • (2012) PLoS Pathog. , vol.8
    • Niedelman, W.1    Gold, D.A.2    Rosowski, E.E.3    Sprokholt, J.K.4    Lim, D.5    Farid Arenas, A.6
  • 64
    • 84889001769 scopus 로고    scopus 로고
    • Structure of the Toxoplasma gondii ROP18 kinase domain reveals a second ligand binding pocket required for acute virulence
    • [64] Lim, D., Gold, D.A., Julien, L., Rosowski, E.E., Niedelman, W., Yaffe, M.B., et al. Structure of the Toxoplasma gondii ROP18 kinase domain reveals a second ligand binding pocket required for acute virulence. J. Biol. Chem. 288 (2013), 34968–34980.
    • (2013) J. Biol. Chem. , vol.288 , pp. 34968-34980
    • Lim, D.1    Gold, D.A.2    Julien, L.3    Rosowski, E.E.4    Niedelman, W.5    Yaffe, M.B.6
  • 65
    • 78650194774 scopus 로고    scopus 로고
    • Phosphorylation of immunity-related GTPases by a Toxoplasma gondii-secreted kinase promotes macrophage survival and virulence
    • [65] Fentress, S.J., Behnke, M.S., Dunay, I.R., Mashayekhi, M., Rommereim, L.M., Fox, B.A., et al. Phosphorylation of immunity-related GTPases by a Toxoplasma gondii-secreted kinase promotes macrophage survival and virulence. Cell Host Microbe 8 (2010), 484–495.
    • (2010) Cell Host Microbe , vol.8 , pp. 484-495
    • Fentress, S.J.1    Behnke, M.S.2    Dunay, I.R.3    Mashayekhi, M.4    Rommereim, L.M.5    Fox, B.A.6
  • 67
    • 78650210471 scopus 로고    scopus 로고
    • Phosphorylation of mouse immunity-related GTPase (IRG) resistance proteins is an evasion strategy for virulent Toxoplasma gondii
    • e1000576
    • [67] Steinfeldt, T., Konen-Waisman, S., Tong, L., Pawlowski, N., Lamkemeyer, T., Sibley, L.D., et al. Phosphorylation of mouse immunity-related GTPase (IRG) resistance proteins is an evasion strategy for virulent Toxoplasma gondii. PLoS Biol., 8, 2010, e1000576.
    • (2010) PLoS Biol. , vol.8
    • Steinfeldt, T.1    Konen-Waisman, S.2    Tong, L.3    Pawlowski, N.4    Lamkemeyer, T.5    Sibley, L.D.6
  • 68
    • 84928926952 scopus 로고    scopus 로고
    • IRGM governs the core autophagy machinery to conduct antimicrobial defense
    • [68] Chauhan, S., Mandell, M.A., Deretic, V., IRGM governs the core autophagy machinery to conduct antimicrobial defense. Mol. Cell 58 (2015), 507–521.
    • (2015) Mol. Cell , vol.58 , pp. 507-521
    • Chauhan, S.1    Mandell, M.A.2    Deretic, V.3
  • 69
    • 78649833818 scopus 로고    scopus 로고
    • Human IRGM regulates autophagy and cell-autonomous immunity functions through mitochondria
    • [69] Singh, S.B., Ornatowski, W., Vergne, I., Naylor, J., Delgado, M., Roberts, E., et al. Human IRGM regulates autophagy and cell-autonomous immunity functions through mitochondria. Nat. Cell Biol. 12 (2010), 1154–1165.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 1154-1165
    • Singh, S.B.1    Ornatowski, W.2    Vergne, I.3    Naylor, J.4    Delgado, M.5    Roberts, E.6
  • 70
    • 70349672696 scopus 로고    scopus 로고
    • Autophagy gene variant IRGM -261 T contributes to protection from tuberculosis caused by Mycobacterium tuberculosis but not by M. africanum strains
    • e1000577
    • [70] Intemann, C.D., Thye, T., Niemann, S., Browne, E.N., Amanua Chinbuah, M., Enimil, A., et al. Autophagy gene variant IRGM -261 T contributes to protection from tuberculosis caused by Mycobacterium tuberculosis but not by M. africanum strains. PLoS Pathog.(5), 2009, e1000577.
    • (2009) PLoS Pathog. , Issue.5
    • Intemann, C.D.1    Thye, T.2    Niemann, S.3    Browne, E.N.4    Amanua Chinbuah, M.5    Enimil, A.6
  • 71
    • 84861186087 scopus 로고    scopus 로고
    • Defects in autophagy favour adherent-invasive Escherichia Coli persistence within macrophages leading to increased pro-inflammatory response
    • [71] Lapaquette, P., Bringer, M.A., Darfeuille-Michaud, A., Defects in autophagy favour adherent-invasive Escherichia Coli persistence within macrophages leading to increased pro-inflammatory response. Cell. Microbiol. 14 (2012), 791–807.
    • (2012) Cell. Microbiol. , vol.14 , pp. 791-807
    • Lapaquette, P.1    Bringer, M.A.2    Darfeuille-Michaud, A.3
  • 72
    • 50449091647 scopus 로고    scopus 로고
    • Deletion polymorphism upstream of IRGM associated with altered IRGM expression and Crohn's disease
    • [72] McCarroll, S.A., Huett, A., Kuballa, P., Chilewski, S.D., Landry, A., Goyette, P., et al. Deletion polymorphism upstream of IRGM associated with altered IRGM expression and Crohn's disease. Nat. Genet., 2008.
    • (2008) Nat. Genet.
    • McCarroll, S.A.1    Huett, A.2    Kuballa, P.3    Chilewski, S.D.4    Landry, A.5    Goyette, P.6
  • 73
    • 10944253145 scopus 로고    scopus 로고
    • Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages
    • [73] Gutierrez, M.G., Master, S.S., Singh, S.B., Taylor, G.A., Colombo, M.I., Deretic, V., Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages. Cell 119 (2004), 753–766.
    • (2004) Cell , vol.119 , pp. 753-766
    • Gutierrez, M.G.1    Master, S.S.2    Singh, S.B.3    Taylor, G.A.4    Colombo, M.I.5    Deretic, V.6
  • 75
    • 84922489435 scopus 로고    scopus 로고
    • Oxidative stress and autophagy: the clash between damage and metabolic needs
    • [75] Filomeni, G., De Zio, D., Cecconi, F., Oxidative stress and autophagy: the clash between damage and metabolic needs. Cell Death Differ. 22 (2015), 377–388.
    • (2015) Cell Death Differ. , vol.22 , pp. 377-388
    • Filomeni, G.1    De Zio, D.2    Cecconi, F.3
  • 76
  • 77
    • 84899734546 scopus 로고    scopus 로고
    • Palmitoylation of the immunity related GTPase, Irgm1: impact on membrane localization and ability to promote mitochondrial fission
    • e95021
    • [77] Henry, S.C., Schmidt, E.A., Fessler, M.B., Taylor, G.A., Palmitoylation of the immunity related GTPase, Irgm1: impact on membrane localization and ability to promote mitochondrial fission. PLoS One, 9, 2014, e95021.
    • (2014) PLoS One , vol.9
    • Henry, S.C.1    Schmidt, E.A.2    Fessler, M.B.3    Taylor, G.A.4
  • 78
    • 79959853767 scopus 로고    scopus 로고
    • Compensatory T cell responses in IRG-deficient mice prevent sustained Chlamydia trachomatis infections
    • e1001346
    • [78] Coers, J., Gondek, D.C., Olive, A.J., Rohlfing, A., Taylor, G.A., Starnbach, M.N., Compensatory T cell responses in IRG-deficient mice prevent sustained Chlamydia trachomatis infections. PLoS Pathog., 7, 2011, e1001346.
    • (2011) PLoS Pathog. , vol.7
    • Coers, J.1    Gondek, D.C.2    Olive, A.J.3    Rohlfing, A.4    Taylor, G.A.5    Starnbach, M.N.6
  • 79
    • 54549089752 scopus 로고    scopus 로고
    • The immunity-related GTPase Irgm1 promotes the expansion of activated CD4 + T cell populations by preventing interferon-gamma-induced cell death
    • [79] Feng, C.G., Zheng, L., Jankovic, D., Bafica, A., Cannons, J.L., Watford, W.T., et al. The immunity-related GTPase Irgm1 promotes the expansion of activated CD4 + T cell populations by preventing interferon-gamma-induced cell death. Nat. Immunol. 9 (2008), 1279–1287.
    • (2008) Nat. Immunol. , vol.9 , pp. 1279-1287
    • Feng, C.G.1    Zheng, L.2    Jankovic, D.3    Bafica, A.4    Cannons, J.L.5    Watford, W.T.6
  • 80
    • 38449116497 scopus 로고    scopus 로고
    • Impaired macrophage function underscores susceptibility to Salmonella in mice lacking Irgm1 (LRG-47)
    • [80] Henry, S.C., Daniell, X., Indaram, M., Whitesides, J.F., Sempowski, G.D., Howell, D., et al. Impaired macrophage function underscores susceptibility to Salmonella in mice lacking Irgm1 (LRG-47). J. Immunol. 179 (2007), 6963–6972.
    • (2007) J. Immunol. , vol.179 , pp. 6963-6972
    • Henry, S.C.1    Daniell, X.2    Indaram, M.3    Whitesides, J.F.4    Sempowski, G.D.5    Howell, D.6
  • 82
    • 0041344461 scopus 로고    scopus 로고
    • A giant GTPase, very large inducible GTPase-1, is inducible by IFNs
    • [82] Klamp, T., Boehm, U., Schenk, D., Pfeffer, K., Howard, J.C., A giant GTPase, very large inducible GTPase-1, is inducible by IFNs. J. Immunol. 171 (2003), 1255–1265.
    • (2003) J. Immunol. , vol.171 , pp. 1255-1265
    • Klamp, T.1    Boehm, U.2    Schenk, D.3    Pfeffer, K.4    Howard, J.C.5
  • 83
    • 0018691394 scopus 로고
    • Interferon action: induction of specific proteins in mouse and human cells by homologous interferons
    • [83] Gupta, S.L., Rubin, B.Y., Holmes, S.L., Interferon action: induction of specific proteins in mouse and human cells by homologous interferons. Proc. Natl. Acad. Sci. U. S. A. 76 (1979), 4817–4821.
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4817-4821
    • Gupta, S.L.1    Rubin, B.Y.2    Holmes, S.L.3
  • 84
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules?
    • [84] Praefcke, G.J., McMahon, H.T., The dynamin superfamily: universal membrane tubulation and fission molecules?. Nat. Rev. Mol. Cell Biol. 5 (2004), 133–147.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 85
    • 44149120744 scopus 로고    scopus 로고
    • Analyses of murine GBP homology clusters based on in silico, in vitro, and in vivo studies
    • [85] Kresse, A., Konermann, C., Degrandi, D., Beuter-Gunia, C., Wuerthner, J., Pfeffer, K., et al. Analyses of murine GBP homology clusters based on in silico, in vitro, and in vivo studies. BMC Genomics, 9, 2008, 158.
    • (2008) BMC Genomics , vol.9 , pp. 158
    • Kresse, A.1    Konermann, C.2    Degrandi, D.3    Beuter-Gunia, C.4    Wuerthner, J.5    Pfeffer, K.6
  • 86
    • 0025900442 scopus 로고
    • Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP
    • [86] Cheng, Y.S., Patterson, C.E., Staeheli, P., Interferon-induced guanylate-binding proteins lack an N(T)KXD consensus motif and bind GMP in addition to GDP and GTP. Mol. Cell. Biol. 11 (1991), 4717–4725.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 4717-4725
    • Cheng, Y.S.1    Patterson, C.E.2    Staeheli, P.3
  • 87
    • 0034598734 scopus 로고    scopus 로고
    • Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins
    • [87] Prakash, B., Praefcke, G.J., Renault, L., Wittinghofer, A., Herrmann, C., Structure of human guanylate-binding protein 1 representing a unique class of GTP-binding proteins. Nature 403 (2000), 567–571.
    • (2000) Nature , vol.403 , pp. 567-571
    • Prakash, B.1    Praefcke, G.J.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 88
    • 33644772427 scopus 로고    scopus 로고
    • How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP
    • [88] Ghosh, A., Praefcke, G.J., Renault, L., Wittinghofer, A., Herrmann, C., How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP. Nature 440 (2006), 101–104.
    • (2006) Nature , vol.440 , pp. 101-104
    • Ghosh, A.1    Praefcke, G.J.2    Renault, L.3    Wittinghofer, A.4    Herrmann, C.5
  • 89
    • 33744463639 scopus 로고    scopus 로고
    • In silico genomic analysis of the human and murine guanylate-binding protein (GBP) gene clusters
    • [89] Olszewski, M.A., Gray, J., Vestal, D.J., In silico genomic analysis of the human and murine guanylate-binding protein (GBP) gene clusters. J. Interf. Cytokine Res. 26 (2006), 328–352.
    • (2006) J. Interf. Cytokine Res. , vol.26 , pp. 328-352
    • Olszewski, M.A.1    Gray, J.2    Vestal, D.J.3
  • 90
    • 0042525961 scopus 로고    scopus 로고
    • The guanylate binding protein-1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP-1 expression
    • [90] Guenzi, E., Topolt, K., Lubeseder-Martellato, C., Jorg, A., Naschberger, E., Benelli, R., et al. The guanylate binding protein-1 GTPase controls the invasive and angiogenic capability of endothelial cells through inhibition of MMP-1 expression. EMBO J. 22 (2003), 3772–3782.
    • (2003) EMBO J. , vol.22 , pp. 3772-3782
    • Guenzi, E.1    Topolt, K.2    Lubeseder-Martellato, C.3    Jorg, A.4    Naschberger, E.5    Benelli, R.6
  • 91
    • 17944366368 scopus 로고    scopus 로고
    • The helical domain of GBP-1 mediates the inhibition of endothelial cell proliferation by inflammatory cytokines
    • [91] Guenzi, E., Topolt, K., Cornali, E., Lubeseder-Martellato, C., Jorg, A., Matzen, K., et al. The helical domain of GBP-1 mediates the inhibition of endothelial cell proliferation by inflammatory cytokines. EMBO J. 20 (2001), 5568–5577.
    • (2001) EMBO J. , vol.20 , pp. 5568-5577
    • Guenzi, E.1    Topolt, K.2    Cornali, E.3    Lubeseder-Martellato, C.4    Jorg, A.5    Matzen, K.6
  • 92
    • 0033616531 scopus 로고    scopus 로고
    • Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus
    • [92] Anderson, S.L., Carton, J.M., Lou, J., Xing, L., Rubin, B.Y., Interferon-induced guanylate binding protein-1 (GBP-1) mediates an antiviral effect against vesicular stomatitis virus and encephalomyocarditis virus. Virology 256 (1999), 8–14.
    • (1999) Virology , vol.256 , pp. 8-14
    • Anderson, S.L.1    Carton, J.M.2    Lou, J.3    Xing, L.4    Rubin, B.Y.5
  • 93
    • 20144368807 scopus 로고    scopus 로고
    • Inhibition of VSV and EMCV replication by the interferon-induced GTPase, mGBP-2: differential requirement for wild-type GTP binding domain
    • [93] Carter, C.C., Gorbacheva, V.Y., Vestal, D.J., Inhibition of VSV and EMCV replication by the interferon-induced GTPase, mGBP-2: differential requirement for wild-type GTP binding domain. Arch. Virol. 150 (2005), 1213–1220.
    • (2005) Arch. Virol. , vol.150 , pp. 1213-1220
    • Carter, C.C.1    Gorbacheva, V.Y.2    Vestal, D.J.3
  • 94
    • 84857732857 scopus 로고    scopus 로고
    • A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication
    • [94] Nordmann, A., Wixler, L., Boergeling, Y., Wixler, V., Ludwig, S., A new splice variant of the human guanylate-binding protein 3 mediates anti-influenza activity through inhibition of viral transcription and replication. FASEB J. 26 (2012), 1290–1300.
    • (2012) FASEB J. , vol.26 , pp. 1290-1300
    • Nordmann, A.1    Wixler, L.2    Boergeling, Y.3    Wixler, V.4    Ludwig, S.5
  • 95
    • 84961221171 scopus 로고    scopus 로고
    • Guanylate binding protein (GBP) 5 is an interferon-inducible inhibitor of HIV-1 infectivity
    • [95] Krapp, C., Hotter, D., Gawanbacht, A., McLaren, P.J., Kluge, S.F., Sturzel, C.M., et al. Guanylate binding protein (GBP) 5 is an interferon-inducible inhibitor of HIV-1 infectivity. Cell Host Microbe 19 (2016), 504–514.
    • (2016) Cell Host Microbe , vol.19 , pp. 504-514
    • Krapp, C.1    Hotter, D.2    Gawanbacht, A.3    McLaren, P.J.4    Kluge, S.F.5    Sturzel, C.M.6
  • 96
    • 38849193453 scopus 로고    scopus 로고
    • Extensive characterization of IFN-induced GTPases mGBP1 to mGBP10 involved in host defense
    • [96] Degrandi, D., Konermann, C., Beuter-Gunia, C., Kresse, A., Wurthner, J., Kurig, S., et al. Extensive characterization of IFN-induced GTPases mGBP1 to mGBP10 involved in host defense. J. Immunol. 179 (2007), 7729–7740.
    • (2007) J. Immunol. , vol.179 , pp. 7729-7740
    • Degrandi, D.1    Konermann, C.2    Beuter-Gunia, C.3    Kresse, A.4    Wurthner, J.5    Kurig, S.6
  • 97
    • 68349127168 scopus 로고    scopus 로고
    • Human guanylate binding proteins potentiate the anti-chlamydia effects of interferon-gamma
    • e6499
    • [97] Tietzel, I., El-Haibi, C., Carabeo, R.A., Human guanylate binding proteins potentiate the anti-chlamydia effects of interferon-gamma. PLoS One, 4, 2009, e6499.
    • (2009) PLoS One , vol.4
    • Tietzel, I.1    El-Haibi, C.2    Carabeo, R.A.3
  • 98
    • 84872194128 scopus 로고    scopus 로고
    • Autophagy restricts Chlamydia trachomatis growth in human macrophages via IFNG-inducible guanylate binding proteins
    • [98] Al-Zeer, M.A., Al-Younes, H.M., Lauster, D., Abu Lubad, M., Meyer, T.F., Autophagy restricts Chlamydia trachomatis growth in human macrophages via IFNG-inducible guanylate binding proteins. Autophagy 9 (2013), 50–62.
    • (2013) Autophagy , vol.9 , pp. 50-62
    • Al-Zeer, M.A.1    Al-Younes, H.M.2    Lauster, D.3    Abu Lubad, M.4    Meyer, T.F.5
  • 100
    • 79955777383 scopus 로고    scopus 로고
    • A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection
    • [100] Kim, B.H., Shenoy, A.R., Kumar, P., Das, R., Tiwari, S., MacMicking, J.D., A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection. Science 332 (2011), 717–721.
    • (2011) Science , vol.332 , pp. 717-721
    • Kim, B.H.1    Shenoy, A.R.2    Kumar, P.3    Das, R.4    Tiwari, S.5    MacMicking, J.D.6
  • 102
    • 84961951364 scopus 로고    scopus 로고
    • Guanylate binding proteins (GBPs) directly attack via supramolecular complexes
    • [102] Kravets, E., Degrandi, D., Ma, Q., Peulen, T.O., Klumpers, V., Felekyan, S., et al. Guanylate binding proteins (GBPs) directly attack via supramolecular complexes. Elife, 5, 2016.
    • (2016) Elife , vol.5
    • Kravets, E.1    Degrandi, D.2    Ma, Q.3    Peulen, T.O.4    Klumpers, V.5    Felekyan, S.6
  • 103
    • 84876857964 scopus 로고    scopus 로고
    • Guanylate-binding protein 1 (Gbp1) contributes to cell-autonomous immunity against Toxoplasma gondii
    • e1003320
    • [103] Selleck, E.M., Fentress, S.J., Beatty, W.L., Degrandi, D., Pfeffer, K., Virgin, H.W., et al. Guanylate-binding protein 1 (Gbp1) contributes to cell-autonomous immunity against Toxoplasma gondii. PLoS Pathog., 9, 2013, e1003320.
    • (2013) PLoS Pathog. , vol.9
    • Selleck, E.M.1    Fentress, S.J.2    Beatty, W.L.3    Degrandi, D.4    Pfeffer, K.5    Virgin, H.W.6
  • 104
    • 0033652395 scopus 로고    scopus 로고
    • Different subcellular localizations for the related interferon-induced GTPases, MuGBP-1 and MuGBP-2: implications for different functions?
    • [104] Vestal, D.J., Gorbacheva, V.Y., Sen, G.C., Different subcellular localizations for the related interferon-induced GTPases, MuGBP-1 and MuGBP-2: implications for different functions?. J. Interf. Cytokine Res. 20 (2000), 991–1000.
    • (2000) J. Interf. Cytokine Res. , vol.20 , pp. 991-1000
    • Vestal, D.J.1    Gorbacheva, V.Y.2    Sen, G.C.3
  • 105
    • 78650087176 scopus 로고    scopus 로고
    • Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner
    • e14246
    • [105] Britzen-Laurent, N., Bauer, M., Berton, V., Fischer, N., Syguda, A., Reipschlager, S., et al. Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner. PLoS One, 5, 2010, e14246.
    • (2010) PLoS One , vol.5
    • Britzen-Laurent, N.1    Bauer, M.2    Berton, V.3    Fischer, N.4    Syguda, A.5    Reipschlager, S.6
  • 106
    • 0033931024 scopus 로고    scopus 로고
    • Murine guanylate-binding protein: incomplete geranylgeranyl isoprenoid modification of an interferon-gamma-inducible guanosine triphosphate-binding protein
    • [106] Stickney, J.T., Buss, J.E., Murine guanylate-binding protein: incomplete geranylgeranyl isoprenoid modification of an interferon-gamma-inducible guanosine triphosphate-binding protein. Mol. Biol. Cell 11 (2000), 2191–2200.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 2191-2200
    • Stickney, J.T.1    Buss, J.E.2
  • 107
    • 80052549593 scopus 로고    scopus 로고
    • Determinants of GBP recruitment to Toxoplasma gondii vacuoles and the parasitic factors that control it
    • e24434
    • [107] Virreira Winter, S., Niedelman, W., Jensen, K.D., Rosowski, E.E., Julien, L., Spooner, E., et al. Determinants of GBP recruitment to Toxoplasma gondii vacuoles and the parasitic factors that control it. PLoS One, 6, 2011, e24434.
    • (2011) PLoS One , vol.6
    • Virreira Winter, S.1    Niedelman, W.2    Jensen, K.D.3    Rosowski, E.E.4    Julien, L.5    Spooner, E.6
  • 108
    • 84864989434 scopus 로고    scopus 로고
    • The GTPase activity of murine guanylate-binding protein 2 (mGBP2) controls the intracellular localization and recruitment to the parasitophorous vacuole of Toxoplasma gondii
    • [108] Kravets, E., Degrandi, D., Weidtkamp-Peters, S., Ries, B., Konermann, C., Felekyan, S., et al. The GTPase activity of murine guanylate-binding protein 2 (mGBP2) controls the intracellular localization and recruitment to the parasitophorous vacuole of Toxoplasma gondii. J. Biol. Chem. 287 (2012), 27452–27466.
    • (2012) J. Biol. Chem. , vol.287 , pp. 27452-27466
    • Kravets, E.1    Degrandi, D.2    Weidtkamp-Peters, S.3    Ries, B.4    Konermann, C.5    Felekyan, S.6
  • 109
    • 84939856356 scopus 로고    scopus 로고
    • RabGDIalpha is a negative regulator of interferon-gamma-inducible GTPase-dependent cell-autonomous immunity to Toxoplasma gondii
    • [109] Ohshima, J., Sasai, M., Liu, J., Yamashita, K., Ma, J.S., Lee, Y., et al. RabGDIalpha is a negative regulator of interferon-gamma-inducible GTPase-dependent cell-autonomous immunity to Toxoplasma gondii. Proc. Natl. Acad. Sci. U. S. A. 112 (2015), E4581–E4590.
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. E4581-E4590
    • Ohshima, J.1    Sasai, M.2    Liu, J.3    Yamashita, K.4    Ma, J.S.5    Lee, Y.6
  • 110
    • 80052235117 scopus 로고    scopus 로고
    • Immunity-related gtpase M (IRGM) proteins influence the localization of guanylate-binding protein 2 (GBP2) by modulating macroautophagy
    • [110] Traver, M.K., Henry, S.C., Cantillana, V., Oliver, T., Hunn, J.P., Howard, J.C., et al. Immunity-related gtpase M (IRGM) proteins influence the localization of guanylate-binding protein 2 (GBP2) by modulating macroautophagy. J. Biol. Chem., 2011.
    • (2011) J. Biol. Chem.
    • Traver, M.K.1    Henry, S.C.2    Cantillana, V.3    Oliver, T.4    Hunn, J.P.5    Howard, J.C.6
  • 111
  • 112
    • 60749133895 scopus 로고    scopus 로고
    • Polymorphism of the IRGM gene might predispose to fistulizing behavior in Crohn's disease
    • [112] Latiano, A., Palmieri, O., Cucchiara, S., Castro, M., D'Inca, R., Guariso, G., et al. Polymorphism of the IRGM gene might predispose to fistulizing behavior in Crohn's disease. Am. J. Gastroenterol. 104 (2009), 110–116.
    • (2009) Am. J. Gastroenterol. , vol.104 , pp. 110-116
    • Latiano, A.1    Palmieri, O.2    Cucchiara, S.3    Castro, M.4    D'Inca, R.5    Guariso, G.6
  • 113
    • 84857943512 scopus 로고    scopus 로고
    • Mutations in IRGM are associated with more frequent need for surgery in patients with ileocolonic Crohn's disease
    • [113] Sehgal, R., Berg, A., Polinski, J.I., Hegarty, J.P., Lin, Z., McKenna, K.J., et al. Mutations in IRGM are associated with more frequent need for surgery in patients with ileocolonic Crohn's disease. Dis. Colon & Rectum 55 (2012), 115–121.
    • (2012) Dis. Colon & Rectum , vol.55 , pp. 115-121
    • Sehgal, R.1    Berg, A.2    Polinski, J.I.3    Hegarty, J.P.4    Lin, Z.5    McKenna, K.J.6
  • 114
    • 44349136821 scopus 로고    scopus 로고
    • Genetic determinants of ulcerative colitis include the ECM1 locus and five loci implicated in Crohn's disease
    • [114] Fisher, S.A., Tremelling, M., Anderson, C.A., Gwilliam, R., Bumpstead, S., Prescott, N.J., et al. Genetic determinants of ulcerative colitis include the ECM1 locus and five loci implicated in Crohn's disease. Nat. Genet. 40 (2008), 710–712.
    • (2008) Nat. Genet. , vol.40 , pp. 710-712
    • Fisher, S.A.1    Tremelling, M.2    Anderson, C.A.3    Gwilliam, R.4    Bumpstead, S.5    Prescott, N.J.6
  • 115
    • 44349173654 scopus 로고    scopus 로고
    • Replication of signals from recent studies of Crohn's disease identifies previously unknown disease loci for ulcerative colitis
    • [115] Franke, A., Balschun, T., Karlsen, T.H., Hedderich, J., May, S., Lu, T., et al. Replication of signals from recent studies of Crohn's disease identifies previously unknown disease loci for ulcerative colitis. Nat. Genet. 40 (2008), 713–715.
    • (2008) Nat. Genet. , vol.40 , pp. 713-715
    • Franke, A.1    Balschun, T.2    Karlsen, T.H.3    Hedderich, J.4    May, S.5    Lu, T.6
  • 117
    • 66749106217 scopus 로고    scopus 로고
    • Association of ATG16L1 and IRGM genes polymorphisms with inflammatory bowel disease: a meta-analysis approach
    • [117] Palomino-Morales, R.J., Oliver, J., Gomez-Garcia, M., Lopez-Nevot, M.A., Rodrigo, L., Nieto, A., et al. Association of ATG16L1 and IRGM genes polymorphisms with inflammatory bowel disease: a meta-analysis approach. Genes Immun. 10 (2009), 356–364.
    • (2009) Genes Immun. , vol.10 , pp. 356-364
    • Palomino-Morales, R.J.1    Oliver, J.2    Gomez-Garcia, M.3    Lopez-Nevot, M.A.4    Rodrigo, L.5    Nieto, A.6
  • 118
    • 84919348931 scopus 로고    scopus 로고
    • Correlation between IRGM genetic polymorphisms and Crohn's disease risk: a meta-analysis of case-control studies
    • [118] Li, Y., Feng, S.T., Yao, Y., Yang, L., Xing, Y., Wang, Y., et al. Correlation between IRGM genetic polymorphisms and Crohn's disease risk: a meta-analysis of case-control studies. Genet. Mol. Res. 13 (2014), 10,741–10,753.
    • (2014) Genet. Mol. Res. , vol.13 , pp. 10741-10753
    • Li, Y.1    Feng, S.T.2    Yao, Y.3    Yang, L.4    Xing, Y.5    Wang, Y.6
  • 119
    • 50449091647 scopus 로고    scopus 로고
    • Deletion polymorphism upstream of IRGM associated with altered IRGM expression and Crohn's disease
    • [119] McCarroll, S.A., Huett, A., Kuballa, P., Chilewski, S.D., Landry, A., Goyette, P., et al. Deletion polymorphism upstream of IRGM associated with altered IRGM expression and Crohn's disease. Nat. Genet. 40 (2008), 1107–1112.
    • (2008) Nat. Genet. , vol.40 , pp. 1107-1112
    • McCarroll, S.A.1    Huett, A.2    Kuballa, P.3    Chilewski, S.D.4    Landry, A.5    Goyette, P.6
  • 121
    • 79952134938 scopus 로고    scopus 로고
    • A synonymous variant in IRGM alters a binding site for miR-196 and causes deregulation of IRGM-dependent xenophagy in Crohn's disease
    • [121] Brest, P., Lapaquette, P., Souidi, M., Lebrigand, K., Cesaro, A., Vouret-Craviari, V., et al. A synonymous variant in IRGM alters a binding site for miR-196 and causes deregulation of IRGM-dependent xenophagy in Crohn's disease. Nat. Genet. 43 (2011), 242–245.
    • (2011) Nat. Genet. , vol.43 , pp. 242-245
    • Brest, P.1    Lapaquette, P.2    Souidi, M.3    Lebrigand, K.4    Cesaro, A.5    Vouret-Craviari, V.6
  • 122
    • 34347262689 scopus 로고    scopus 로고
    • Chemically induced mouse models of intestinal inflammation
    • [122] Wirtz, S., Neufert, C., Weigmann, B., Neurath, M.F., Chemically induced mouse models of intestinal inflammation. Nat. Protoc. 2 (2007), 541–546.
    • (2007) Nat. Protoc. , vol.2 , pp. 541-546
    • Wirtz, S.1    Neufert, C.2    Weigmann, B.3    Neurath, M.F.4
  • 123
    • 0028837679 scopus 로고
    • Identification of an endotoxin and IFN-inducible cDNA: possible identification of a novel protein family
    • [123] Sorace, J.M., Johnson, R.J., Howard, D.L., Drysdale, B.E., Identification of an endotoxin and IFN-inducible cDNA: possible identification of a novel protein family. J. Leukoc. Biol. 58 (1995), 477–484.
    • (1995) J. Leukoc. Biol. , vol.58 , pp. 477-484
    • Sorace, J.M.1    Johnson, R.J.2    Howard, D.L.3    Drysdale, B.E.4
  • 124
    • 61649114427 scopus 로고    scopus 로고
    • A common role for Atg16L1, Atg5 and Atg7 in small intestinal Paneth cells and Crohn disease
    • [124] Cadwell, K., Patel, K.K., Komatsu, M., Virgin, H.W., Stappenbeck, T.S., A common role for Atg16L1, Atg5 and Atg7 in small intestinal Paneth cells and Crohn disease. Autophagy 5 (2009), 250–252.
    • (2009) Autophagy , vol.5 , pp. 250-252
    • Cadwell, K.1    Patel, K.K.2    Komatsu, M.3    Virgin, H.W.4    Stappenbeck, T.S.5
  • 125
    • 56249135538 scopus 로고    scopus 로고
    • A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells
    • [125] Cadwell, K., Liu, J.Y., Brown, S.L., Miyoshi, H., Loh, J., Lennerz, J.K., et al. A key role for autophagy and the autophagy gene Atg16l1 in mouse and human intestinal Paneth cells. Nature 456 (2008), 259–263.
    • (2008) Nature , vol.456 , pp. 259-263
    • Cadwell, K.1    Liu, J.Y.2    Brown, S.L.3    Miyoshi, H.4    Loh, J.5    Lennerz, J.K.6
  • 126
    • 56249090667 scopus 로고    scopus 로고
    • Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production
    • [126] Saitoh, T., Fujita, N., Jang, M.H., Uematsu, S., Yang, B.G., Satoh, T., et al. Loss of the autophagy protein Atg16L1 enhances endotoxin-induced IL-1beta production. Nature 456 (2008), 264–268.
    • (2008) Nature , vol.456 , pp. 264-268
    • Saitoh, T.1    Fujita, N.2    Jang, M.H.3    Uematsu, S.4    Yang, B.G.5    Satoh, T.6
  • 127
    • 77953904042 scopus 로고    scopus 로고
    • Virus-plus-susceptibility gene interaction determines Crohn's disease gene Atg16L1 phenotypes in intestine
    • [127] Cadwell, K., Patel, K.K., Maloney, N.S., Liu, T.C., Ng, A.C., Storer, C.E., et al. Virus-plus-susceptibility gene interaction determines Crohn's disease gene Atg16L1 phenotypes in intestine. Cell 141 (2010), 1135–1145.
    • (2010) Cell , vol.141 , pp. 1135-1145
    • Cadwell, K.1    Patel, K.K.2    Maloney, N.S.3    Liu, T.C.4    Ng, A.C.5    Storer, C.E.6
  • 128
    • 46249109359 scopus 로고    scopus 로고
    • Induction of guanylate binding protein 5 by gamma interferon increases susceptibility to Salmonella enterica serovar Typhimurium-induced pyroptosis in RAW 264.7 cells
    • [128] Rupper, A.C., Cardelli, J.A., Induction of guanylate binding protein 5 by gamma interferon increases susceptibility to Salmonella enterica serovar Typhimurium-induced pyroptosis in RAW 264.7 cells. Infect. Immun. 76 (2008), 2304–2315.
    • (2008) Infect. Immun. , vol.76 , pp. 2304-2315
    • Rupper, A.C.1    Cardelli, J.A.2
  • 129
  • 130
    • 84928545520 scopus 로고    scopus 로고
    • The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection
    • [130] Man, S.M., Karki, R., Malireddi, R.K., Neale, G., Vogel, P., Yamamoto, M., et al. The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection. Nat. Immunol., 2015.
    • (2015) Nat. Immunol.
    • Man, S.M.1    Karki, R.2    Malireddi, R.K.3    Neale, G.4    Vogel, P.5    Yamamoto, M.6
  • 131
    • 84900564237 scopus 로고    scopus 로고
    • Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases
    • [131] Meunier, E., Dick, M.S., Dreier, R.F., Schurmann, N., Kenzelmann Broz, D., Warming, S., et al. Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases. Nature 509 (2014), 366–370.
    • (2014) Nature , vol.509 , pp. 366-370
    • Meunier, E.1    Dick, M.S.2    Dreier, R.F.3    Schurmann, N.4    Kenzelmann Broz, D.5    Warming, S.6
  • 132
    • 0036403795 scopus 로고    scopus 로고
    • Murine GBP-5, a new member of the murine guanylate-binding protein family, is coordinately regulated with other GBPs in vivo and in vitro
    • [132] Nguyen, T.T., Hu, Y., Widney, D.P., Mar, R.A., Smith, J.B., Murine GBP-5, a new member of the murine guanylate-binding protein family, is coordinately regulated with other GBPs in vivo and in vitro. J. Interf. Cytokine Res. 22 (2002), 899–909.
    • (2002) J. Interf. Cytokine Res. , vol.22 , pp. 899-909
    • Nguyen, T.T.1    Hu, Y.2    Widney, D.P.3    Mar, R.A.4    Smith, J.B.5
  • 133
    • 0021220522 scopus 로고
    • Genetic control of interferon action: mouse strain distribution and inheritance of an induced protein with guanylate-binding property
    • [133] Staeheli, P., Prochazka, M., Steigmeier, P.A., Haller, O., Genetic control of interferon action: mouse strain distribution and inheritance of an induced protein with guanylate-binding property. Virology 137 (1984), 135–142.
    • (1984) Virology , vol.137 , pp. 135-142
    • Staeheli, P.1    Prochazka, M.2    Steigmeier, P.A.3    Haller, O.4
  • 134
    • 84949652170 scopus 로고    scopus 로고
    • Guanylate binding proteins enable rapid activation of canonical and noncanonical inflammasomes in Chlamydia-infected macrophages
    • [134] Finethy, R., Jorgensen, I., Haldar, A.K., de Zoete, M.R., Strowig, T., Flavell, R.A., et al. Guanylate binding proteins enable rapid activation of canonical and noncanonical inflammasomes in Chlamydia-infected macrophages. Infect. Immun., 2015.
    • (2015) Infect. Immun.
    • Finethy, R.1    Jorgensen, I.2    Haldar, A.K.3    de Zoete, M.R.4    Strowig, T.5    Flavell, R.A.6
  • 135
    • 84928538482 scopus 로고    scopus 로고
    • Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida
    • [135] Meunier, E., Wallet, P., Dreier, R.F., Costanzo, S., Anton, L., Ruhl, S., et al. Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida. Nat. Immunol., 2015.
    • (2015) Nat. Immunol.
    • Meunier, E.1    Wallet, P.2    Dreier, R.F.3    Costanzo, S.4    Anton, L.5    Ruhl, S.6
  • 136
    • 84899098318 scopus 로고    scopus 로고
    • Guanylate binding proteins promote caspase-11-dependent pyroptosis in response to cytoplasmic LPS
    • [136] Pilla, D.M., Hagar, J.A., Haldar, A.K., Mason, A.K., Degrandi, D., Pfeffer, K., et al. Guanylate binding proteins promote caspase-11-dependent pyroptosis in response to cytoplasmic LPS. Proc. Natl. Acad. Sci. U. S. A. 111 (2014), 6046–6051.
    • (2014) Proc. Natl. Acad. Sci. U. S. A. , vol.111 , pp. 6046-6051
    • Pilla, D.M.1    Hagar, J.A.2    Haldar, A.K.3    Mason, A.K.4    Degrandi, D.5    Pfeffer, K.6
  • 137
    • 58749102026 scopus 로고    scopus 로고
    • Protein kinase R reveals an evolutionary model for defeating viral mimicry
    • [137] Elde, N.C., Child, S.J., Geballe, A.P., Malik, H.S., Protein kinase R reveals an evolutionary model for defeating viral mimicry. Nature 457 (2009), 485–489.
    • (2009) Nature , vol.457 , pp. 485-489
    • Elde, N.C.1    Child, S.J.2    Geballe, A.P.3    Malik, H.S.4
  • 138
    • 14544281087 scopus 로고    scopus 로고
    • Positive selection of primate TRIM5alpha identifies a critical species-specific retroviral restriction domain
    • [138] Sawyer, S.L., Wu, L.I., Emerman, M., Malik, H.S., Positive selection of primate TRIM5alpha identifies a critical species-specific retroviral restriction domain. Proc. Natl. Acad. Sci. U. S. A. 102 (2005), 2832–2837.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 2832-2837
    • Sawyer, S.L.1    Wu, L.I.2    Emerman, M.3    Malik, H.S.4
  • 139
    • 84916936154 scopus 로고    scopus 로고
    • Nutritional immunity. Escape from bacterial iron piracy through rapid evolution of transferrin
    • [139] Barber, M.F., Elde, N.C., Nutritional immunity. Escape from bacterial iron piracy through rapid evolution of transferrin. Science 346 (2014), 1362–1366.
    • (2014) Science , vol.346 , pp. 1362-1366
    • Barber, M.F.1    Elde, N.C.2
  • 140
    • 84867659115 scopus 로고    scopus 로고
    • Evolution-guided identification of antiviral specificity determinants in the broadly acting interferon-induced innate immunity factor MxA
    • [140] Mitchell, P.S., Patzina, C., Emerman, M., Haller, O., Malik, H.S., Kochs, G., Evolution-guided identification of antiviral specificity determinants in the broadly acting interferon-induced innate immunity factor MxA. Cell Host Microbe 12 (2012), 598–604.
    • (2012) Cell Host Microbe , vol.12 , pp. 598-604
    • Mitchell, P.S.1    Patzina, C.2    Emerman, M.3    Haller, O.4    Malik, H.S.5    Kochs, G.6
  • 141


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.