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Volumn 19, Issue 12, 2017, Pages

Mechanisms and functions of guanylate-binding proteins and related interferon-inducible GTPases: Roles in intracellular lysis of pathogens

Author keywords

bacteria; cell autonomous immunity; GBPs; inflammasome; innate immunity; pathogens

Indexed keywords

BINDING PROTEIN; GUANOSINE PHOSPHATE; GUANOSINE TRIPHOSPHATASE; INFLAMMASOME; INTERFERON; GUANINE NUCLEOTIDE BINDING PROTEIN; IMMUNOLOGIC FACTOR;

EID: 85031725672     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/cmi.12791     Document Type: Review
Times cited : (49)

References (73)
  • 4
    • 78650087176 scopus 로고    scopus 로고
    • Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner
    • Britzen-Laurent, N., Bauer, M., Berton, V., Fischer, N., Syguda, A., Reipschläger, S., … Stürzl, M. (2010). Intracellular trafficking of guanylate-binding proteins is regulated by heterodimerization in a hierarchical manner. PLoS One, 5, e14246.
    • (2010) PLoS One , vol.5
    • Britzen-Laurent, N.1    Bauer, M.2    Berton, V.3    Fischer, N.4    Syguda, A.5    Reipschläger, S.6    Stürzl, M.7
  • 5
    • 0022393301 scopus 로고
    • Affinity purification of an interferon-induced human guanylate-binding protein and its characterization
    • Cheng, Y. S., Becker-Manley, M. F., Chow, T. P., & Horan, D. C. (1985). Affinity purification of an interferon-induced human guanylate-binding protein and its characterization. The Journal of Biological Chemistry, 260, 15834–15839.
    • (1985) The Journal of Biological Chemistry , vol.260 , pp. 15834-15839
    • Cheng, Y.S.1    Becker-Manley, M.F.2    Chow, T.P.3    Horan, D.C.4
  • 6
    • 0020955866 scopus 로고
    • Interferon induction of fibroblast proteins with guanylate binding activity
    • Cheng, Y. S., Colonno, R. J., & Yin, F. H. (1983). Interferon induction of fibroblast proteins with guanylate binding activity. The Journal of Biological Chemistry, 258, 7746–7750.
    • (1983) The Journal of Biological Chemistry , vol.258 , pp. 7746-7750
    • Cheng, Y.S.1    Colonno, R.J.2    Yin, F.H.3
  • 7
  • 8
    • 84884688909 scopus 로고    scopus 로고
    • Self and non-self discrimination of intracellular membranes by the innate immune system
    • Coers, J. (2013). Self and non-self discrimination of intracellular membranes by the innate immune system. PLoS Pathogens, 9, e1003538.
    • (2013) PLoS Pathogens , vol.9
    • Coers, J.1
  • 13
    • 84949652170 scopus 로고    scopus 로고
    • Guanylate binding proteins enable rapid activation of canonical and noncanonical inflammasomes in Chlamydia-infected macrophages
    • Finethy, R., Jorgensen, I., Haldar, A. K., de Zoete, M. R., Strowig, T., Flavell, R. A., … Coers, J. (2015). Guanylate binding proteins enable rapid activation of canonical and noncanonical inflammasomes in Chlamydia-infected macrophages. Infection and Immunity, 83, 4740–4749.
    • (2015) Infection and Immunity , vol.83 , pp. 4740-4749
    • Finethy, R.1    Jorgensen, I.2    Haldar, A.K.3    de Zoete, M.R.4    Strowig, T.5    Flavell, R.A.6    Coers, J.7
  • 14
    • 85023761900 scopus 로고    scopus 로고
    • TRIM21 is critical for survival of Toxoplasma gondii infection and localises to GBP-positive parasite vacuoles
    • Foltz, C., Napolitano, A., Khan, R., Clough, B., Hirst, E. M., & Frickel, E. M. (2017). TRIM21 is critical for survival of Toxoplasma gondii infection and localises to GBP-positive parasite vacuoles. Scientific Reports, 7, 5209.
    • (2017) Scientific Reports , vol.7 , pp. 5209
    • Foltz, C.1    Napolitano, A.2    Khan, R.3    Clough, B.4    Hirst, E.M.5    Frickel, E.M.6
  • 15
    • 77956849101 scopus 로고    scopus 로고
    • Purification of the CaaX-modified, dynamin-related large GTPase hGBP1 by coexpression with farnesyltransferase
    • Fres, J. M., Muller, S., & Praefcke, G. J. (2010). Purification of the CaaX-modified, dynamin-related large GTPase hGBP1 by coexpression with farnesyltransferase. Journal of Lipid Research, 51, 2454–2459.
    • (2010) Journal of Lipid Research , vol.51 , pp. 2454-2459
    • Fres, J.M.1    Muller, S.2    Praefcke, G.J.3
  • 16
    • 33644772427 scopus 로고    scopus 로고
    • How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP
    • Ghosh, A., Praefcke, G. J., Renault, L., Wittinghofer, A., & Herrmann, C. (2006). How guanylate-binding proteins achieve assembly-stimulated processive cleavage of GTP to GMP. Nature, 440, 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
  • 18
    • 84879547102 scopus 로고    scopus 로고
    • IRG and GBP host resistance factors target aberrant, “non-self” vacuoles characterized by the missing of "self" IRGM proteins
    • Haldar, A. K., Saka, H. A., Piro, A. S., Dunn, J. D., Henry, S. C., Taylor, G. A., … Coers, J. (2013). IRG and GBP host resistance factors target aberrant, “non-self” vacuoles characterized by the missing of "self" IRGM proteins. PLoS Pathogens, 9, e1003414.
    • (2013) PLoS Pathogens , 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    Coers, J.7
  • 20
    • 34249044447 scopus 로고    scopus 로고
    • Type I interferon signaling is required for activation of the inflammasome during Francisella infection
    • Henry, T., Brotcke, A., Weiss, D. S., Thompson, L. J., & Monack, D. M. (2007). Type I interferon signaling is required for activation of the inflammasome during Francisella infection. The Journal of Experimental Medicine, 204, 987–994.
    • (2007) The Journal of Experimental Medicine , vol.204 , pp. 987-994
    • Henry, T.1    Brotcke, A.2    Weiss, D.S.3    Thompson, L.J.4    Monack, D.M.5
  • 22
    • 53549109432 scopus 로고    scopus 로고
    • Regulatory interactions between IRG resistance GTPases in the cellular response to Toxoplasma gondii
    • Hunn, J. P., Koenen-Waisman, S., Papic, N., Schroeder, N., Pawlowski, N., Lange, R., … Howard, J. C. (2008). Regulatory interactions between IRG resistance GTPases in the cellular response to Toxoplasma gondii. The EMBO Journal, 27, 2495–2509.
    • (2008) The EMBO Journal , 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    Howard, J.C.7
  • 26
    • 84973369598 scopus 로고    scopus 로고
    • Interferon-induced guanylate-binding proteins in inflammasome activation and host defense
    • Kim, B.-H., Chee, J. D., Bradfield, C. J., Park, E.-S., Kumar, P., & MacMicking, J. D. (2016). Interferon-induced guanylate-binding proteins in inflammasome activation and host defense. Nature Immunology, 17, 481–489.
    • (2016) Nature Immunology , vol.17 , pp. 481-489
    • Kim, B.-H.1    Chee, J.D.2    Bradfield, C.J.3    Park, E.-S.4    Kumar, P.5    MacMicking, J.D.6
  • 27
    • 79955777383 scopus 로고    scopus 로고
    • A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection
    • Kim, B. H., Shenoy, A. R., Kumar, P., Das, R., Tiwari, S., & MacMicking, J. D. (2011). A family of IFN-gamma-inducible 65-kD GTPases protects against bacterial infection. Science, 332, 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
  • 29
    • 84961951364 scopus 로고    scopus 로고
    • Guanylate binding proteins directly attack Toxoplasma gondii via supramolecular complexes
    • Kravets, E., Degrandi, D., Ma, Q., Peulen, T. O., Klumpers, V., Felekyan, S., … Pfeffer, K. (2016). Guanylate binding proteins directly attack Toxoplasma gondii via supramolecular complexes. eLife, 5.
    • (2016) eLife , vol.5
    • Kravets, E.1    Degrandi, D.2    Ma, Q.3    Peulen, T.O.4    Klumpers, V.5    Felekyan, S.6    Pfeffer, K.7
  • 31
    • 5644302356 scopus 로고    scopus 로고
    • IFN-inducible GTPases and immunity to intracellular pathogens
    • MacMicking, J. D. (2004). IFN-inducible GTPases and immunity to intracellular pathogens. Trends in Immunology, 25, 601–609.
    • (2004) Trends in Immunology , vol.25 , pp. 601-609
    • MacMicking, J.D.1
  • 32
    • 84860258296 scopus 로고    scopus 로고
    • Interferon-inducible effector mechanisms in cell-autonomous immunity
    • MacMicking, J. D. (2012). Interferon-inducible effector mechanisms in cell-autonomous immunity. Nature Reviews. Immunology, 12, 367–382.
    • (2012) Nature Reviews. Immunology , vol.12 , pp. 367-382
    • MacMicking, J.D.1
  • 33
    • 84952630550 scopus 로고    scopus 로고
    • Converging roles of caspases in inflammasome activation, cell death and innate immunity
    • Man, S. M., & Kanneganti, T.-D. (2016). Converging roles of caspases in inflammasome activation, cell death and innate immunity. Nature Reviews. Immunology, 16, 7–21.
    • (2016) Nature Reviews. Immunology , vol.16 , pp. 7-21
    • Man, S.M.1    Kanneganti, T.-D.2
  • 34
    • 84928545520 scopus 로고    scopus 로고
    • The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection
    • Man, S. M., Karki, R., Malireddi, R. K., Neale, G., Vogel, P., Yamamoto, M., … Kanneganti, T. D. (2015). The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection. Nature Immunology, 16, 467–475.
    • (2015) Nature Immunology , vol.16 , pp. 467-475
    • Man, S.M.1    Karki, R.2    Malireddi, R.K.3    Neale, G.4    Vogel, P.5    Yamamoto, M.6    Kanneganti, T.D.7
  • 35
    • 84990856288 scopus 로고    scopus 로고
    • IRGB10 liberates bacterial ligands for sensing by the AIM2 and caspase-11-NLRP3 inflammasomes
    • e317
    • Man, S. M., Karki, R., Sasai, M., Place, D. E., Kesavardhana, S., Temirov, J., … Kanneganti, T. D. (2016). IRGB10 liberates bacterial ligands for sensing by the AIM2 and caspase-11-NLRP3 inflammasomes. Cell, 167, 382–396. e317
    • (2016) Cell , vol.167 , pp. 382-396
    • Man, S.M.1    Karki, R.2    Sasai, M.3    Place, D.E.4    Kesavardhana, S.5    Temirov, J.6    Kanneganti, T.D.7
  • 36
    • 85008476077 scopus 로고    scopus 로고
    • Interferon-inducible guanylate-binding proteins at the interface of cell-autonomous immunity and inflammasome activation
    • Man, S. M., Place, D. E., Kuriakose, T., & Kanneganti, T. D. (2017). Interferon-inducible guanylate-binding proteins at the interface of cell-autonomous immunity and inflammasome activation. Journal of Leukocyte Biology, 101, 143–150.
    • (2017) Journal of Leukocyte Biology , vol.101 , pp. 143-150
    • Man, S.M.1    Place, D.E.2    Kuriakose, T.3    Kanneganti, T.D.4
  • 37
    • 84963830521 scopus 로고    scopus 로고
    • Loss of the interferon-gamma-inducible regulatory immunity-related GTPase (IRG), Irgm1, causes activation of effector IRG proteins on lysosomes, damaging lysosomal function and predicting the dramatic susceptibility of Irgm1-deficient mice to infection
    • Maric-Biresev, J., Hunn, J. P., Krut, O., Helms, J. B., Martens, S., & Howard, J. C. (2016). Loss of the interferon-gamma-inducible regulatory immunity-related GTPase (IRG), Irgm1, causes activation of effector IRG proteins on lysosomes, damaging lysosomal function and predicting the dramatic susceptibility of Irgm1-deficient mice to infection. BMC Biology, 14, 33.
    • (2016) BMC Biology , vol.14 , pp. 33
    • Maric-Biresev, J.1    Hunn, J.P.2    Krut, O.3    Helms, J.B.4    Martens, S.5    Howard, J.C.6
  • 39
    • 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, J. C. (2004). Mechanisms regulating the positioning of mouse p47 resistance GTPases LRG-47 and IIGP1 on cellular membranes: Retargeting to plasma membrane induced by phagocytosis. Journal of Immunology (Baltimore, Md.: 1950), 173, 2594–2606.
    • (2004) Journal of Immunology (Baltimore, Md.: 1950) , vol.173 , pp. 2594-2606
    • Martens, S.1    Sabel, K.2    Lange, R.3    Uthaiah, R.4    Wolf, E.5    Howard, J.C.6
  • 41
    • 84955212917 scopus 로고    scopus 로고
    • Interferon-inducible GTPases in cell autonomous and innate immunity
    • Meunier, E., & Broz, P. (2016). Interferon-inducible GTPases in cell autonomous and innate immunity. Cellular Microbiology, 18, 168–180.
    • (2016) Cellular Microbiology , vol.18 , pp. 168-180
    • Meunier, E.1    Broz, P.2
  • 42
    • 84900564237 scopus 로고    scopus 로고
    • Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases
    • Meunier, E., Dick, M. S., Dreier, R. F., Schurmann, N., Broz, D. K., Warming, S., … Broz, P. (2014). Caspase-11 activation requires lysis of pathogen-containing vacuoles by IFN-induced GTPases. Nature, 509, 366–370.
    • (2014) Nature , vol.509 , pp. 366-370
    • Meunier, E.1    Dick, M.S.2    Dreier, R.F.3    Schurmann, N.4    Broz, D.K.5    Warming, S.6    Broz, P.7
  • 43
    • 84928538482 scopus 로고    scopus 로고
    • Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida
    • Meunier, E., Wallet, P., Dreier, R. F., Costanzo, S., Anton, L., Ruhl, S., … Broz, P. (2015). Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida. Nature Immunology, 16, 476–484.
    • (2015) Nature Immunology , vol.16 , pp. 476-484
    • Meunier, E.1    Wallet, P.2    Dreier, R.F.3    Costanzo, S.4    Anton, L.5    Ruhl, S.6    Broz, P.7
  • 44
    • 20844442306 scopus 로고    scopus 로고
    • Golgi targeting of human guanylate-binding protein-1 requires nucleotide binding, isoprenylation, and an IFN-gamma-inducible cofactor
    • Modiano, N., Lu, Y. E., & Cresswell, P. (2005). Golgi targeting of human guanylate-binding protein-1 requires nucleotide binding, isoprenylation, and an IFN-gamma-inducible cofactor. Proceedings of the National Academy of Sciences of the United States of America, 102, 8680–8685.
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , pp. 8680-8685
    • Modiano, N.1    Lu, Y.E.2    Cresswell, P.3
  • 47
    • 57649115443 scopus 로고    scopus 로고
    • Inactive and active states of the interferon-inducible resistance GTPase, Irga6, in vivo
    • Papic, N., Hunn, J. P., Pawlowski, N., Zerrahn, J., & Howard, J. C. (2008). Inactive and active states of the interferon-inducible resistance GTPase, Irga6, in vivo. The Journal of Biological Chemistry, 283, 32143–32151.
    • (2008) The Journal of Biological Chemistry , vol.283 , pp. 32143-32151
    • Papic, N.1    Hunn, J.P.2    Pawlowski, N.3    Zerrahn, J.4    Howard, J.C.5
  • 49
    • 84969579633 scopus 로고    scopus 로고
    • Interferon-inducible GTPases in host resistance, inflammation and disease
    • Pilla-Moffett, D., Barber, M. F., Taylor, G. A., & Coers, J. (2016). Interferon-inducible GTPases in host resistance, inflammation and disease. Journal of Molecular Biology, 428, 3495–3513.
    • (2016) Journal of Molecular Biology , vol.428 , pp. 3495-3513
    • Pilla-Moffett, D.1    Barber, M.F.2    Taylor, G.A.3    Coers, J.4
  • 50
    • 18844457095 scopus 로고    scopus 로고
    • Mechanisms of type-I- and type-II-interferon-mediated signalling
    • Platanias, L. C. (2005). Mechanisms of type-I- and type-II-interferon-mediated signalling. Nature Reviews. Immunology, 5, 375–386.
    • (2005) Nature Reviews. Immunology , vol.5 , pp. 375-386
    • Platanias, L.C.1
  • 51
    • 77949997805 scopus 로고    scopus 로고
    • Delivery of cytosolic components by autophagic adaptor protein p62 endows autophagosomes with unique antimicrobial properties
    • Ponpuak, M., Davis, A. S., Roberts, E. A., Delgado, M. A., Dinkins, C., Zhao, Z., … Deretic, V. (2010). Delivery of cytosolic components by autophagic adaptor protein p62 endows autophagosomes with unique antimicrobial properties. Immunity, 32, 329–341.
    • (2010) Immunity , vol.32 , pp. 329-341
    • Ponpuak, M.1    Davis, A.S.2    Roberts, E.A.3    Delgado, M.A.4    Dinkins, C.5    Zhao, Z.6    Deretic, V.7
  • 52
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: Universal membrane tubulation and fission molecules?
    • Praefcke, G. J., & McMahon, H. T. (2004). The dynamin superfamily: Universal membrane tubulation and fission molecules? Nature Reviews Molecular Cell Biology, 5, 133–147.
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 54
    • 85025817200 scopus 로고    scopus 로고
    • Essential role for GABARAP autophagy proteins in interferon-inducible GTPase-mediated host defense
    • Sasai, M., Sakaguchi, N., Ma, J. S., Nakamura, S., Kawabata, T., Bando, H., … Yamamoto, M. (2017). Essential role for GABARAP autophagy proteins in interferon-inducible GTPase-mediated host defense. Nature Immunology, 18, 899–910.
    • (2017) Nature Immunology , vol.18 , pp. 899-910
    • Sasai, M.1    Sakaguchi, N.2    Ma, J.S.3    Nakamura, S.4    Kawabata, T.5    Bando, H.6    Yamamoto, M.7
  • 55
    • 0028243476 scopus 로고
    • The interferon-induced 67-kDa guanylate-binding protein (hGBP1) is a GTPase that converts GTP to GMP
    • Schwemmle, M., & Staeheli, P. (1994). The interferon-induced 67-kDa guanylate-binding protein (hGBP1) is a GTPase that converts GTP to GMP. The Journal of Biological Chemistry, 269, 11299–11305.
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 11299-11305
    • Schwemmle, M.1    Staeheli, P.2
  • 56
    • 84876857964 scopus 로고    scopus 로고
    • Guanylate-binding protein 1 (Gbp1) contributes to cell-autonomous immunity against Toxoplasma gondii
    • Epub 2013 Apr 25.
    • Selleck, E. M., Fentress, S. J., Beatty, W. L., Degrandi, D., Pfeffer, K., Virgin HW 4th, … Sibley, L. D. (2013). Guanylate-binding protein 1 (Gbp1) contributes to cell-autonomous immunity against Toxoplasma gondii. PLoS Pathogens, 9(4), e1003320. https://doi.org/10.1371/journal.ppat.1003320. Epub 2013 Apr 25.
    • (2013) PLoS Pathogens , vol.9 , Issue.4
    • Selleck, E.M.1    Fentress, S.J.2    Beatty, W.L.3    Degrandi, D.4    Pfeffer, K.5    Sibley, L.D.6
  • 57
    • 37049020693 scopus 로고    scopus 로고
    • Emerging themes in IFN-gamma-induced macrophage immunity by the p47 and p65 GTPase families
    • Shenoy, A. R., Kim, B. H., Choi, H. P., Matsuzawa, T., Tiwari, S., & MacMicking, J. D. (2007). Emerging themes in IFN-gamma-induced macrophage immunity by the p47 and p65 GTPase families. Immunobiology, 212, 771–784.
    • (2007) Immunobiology , vol.212 , pp. 771-784
    • Shenoy, A.R.1    Kim, B.H.2    Choi, H.P.3    Matsuzawa, T.4    Tiwari, S.5    MacMicking, J.D.6
  • 60
    • 0033931024 scopus 로고    scopus 로고
    • Murine guanylate-binding protein: Incomplete geranylgeranyl isoprenoid modification of an interferon-gamma-inducible guanosine triphosphate-binding protein
    • Stickney, J. T., & Buss, J. E. (2000). Murine guanylate-binding protein: Incomplete geranylgeranyl isoprenoid modification of an interferon-gamma-inducible guanosine triphosphate-binding protein. Molecular Biology of the Cell, 11, 2191–2200.
    • (2000) Molecular Biology of the Cell , vol.11 , pp. 2191-2200
    • Stickney, J.T.1    Buss, J.E.2
  • 62
    • 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
    • Tiwari, S., Choi, H. P., Matsuzawa, T., Pypaert, M., & MacMicking, J. D. (2009). 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. Nature Immunology, 10, 907–917.
    • (2009) Nature Immunology , vol.10 , pp. 907-917
    • Tiwari, S.1    Choi, H.P.2    Matsuzawa, T.3    Pypaert, M.4    MacMicking, J.D.5
  • 67
    • 84904662230 scopus 로고    scopus 로고
    • Triphosphate induced dimerization of human guanylate binding protein 1 involves association of the C-terminal helices: A joint double electron-electron resonance and FRET study
    • Vopel, T., Hengstenberg, C. S., Peulen, T. O., Ajaj, Y., Seidel, C. A., Herrmann, C., & Klare, J. P. (2014). Triphosphate induced dimerization of human guanylate binding protein 1 involves association of the C-terminal helices: A joint double electron-electron resonance and FRET study. Biochemistry, 53, 4590–4600.
    • (2014) Biochemistry , vol.53 , pp. 4590-4600
    • Vopel, T.1    Hengstenberg, C.S.2    Peulen, T.O.3    Ajaj, Y.4    Seidel, C.A.5    Herrmann, C.6    Klare, J.P.7
  • 68
    • 67349158233 scopus 로고    scopus 로고
    • Nucleotide dependent cysteine reactivity of hGBP1 uncovers a domain movement during GTP hydrolysis
    • Vopel, T., Kunzelmann, S., & Herrmann, C. (2009). Nucleotide dependent cysteine reactivity of hGBP1 uncovers a domain movement during GTP hydrolysis. FEBS Letters, 583, 1923–1927.
    • (2009) FEBS Letters , vol.583 , pp. 1923-1927
    • Vopel, T.1    Kunzelmann, S.2    Herrmann, C.3
  • 69
    • 84955654523 scopus 로고    scopus 로고
    • Protein prenylation: Unique fats make their mark on biology
    • Wang, M., & Casey, P. J. (2016). Protein prenylation: Unique fats make their mark on biology. Nature Reviews. Molecular Cell Biology, 17, 110–122.
    • (2016) Nature Reviews. Molecular Cell Biology , vol.17 , pp. 110-122
    • Wang, M.1    Casey, P.J.2
  • 70
    • 84865371084 scopus 로고    scopus 로고
    • A cluster of interferon-gamma-inducible p65 GTPases plays a critical role in host defense against Toxoplasma gondii
    • Yamamoto, M., Okuyama, M., Ma, J. S., Kimura, T., Kamiyama, N., Saiga, H., … Takeda, K. (2012). A cluster of interferon-gamma-inducible p65 GTPases plays a critical role in host defense against Toxoplasma gondii. Immunity, 37, 302–313.
    • (2012) Immunity , vol.37 , pp. 302-313
    • Yamamoto, M.1    Okuyama, M.2    Ma, J.S.3    Kimura, T.4    Kamiyama, N.5    Saiga, H.6    Takeda, K.7
  • 71
    • 61449117883 scopus 로고    scopus 로고
    • Disruption of the Toxoplasma gondii parasitophorous vacuole by IFNgamma-inducible immunity-related GTPases (IRG proteins) triggers necrotic cell death
    • Zhao, Y. O., Khaminets, A., Hunn, J. P., & Howard, J. C. (2009). Disruption of the Toxoplasma gondii parasitophorous vacuole by IFNgamma-inducible immunity-related GTPases (IRG proteins) triggers necrotic cell death. PLoS Pathogens, 5, e1000288.
    • (2009) PLoS Pathogens , vol.5
    • Zhao, Y.O.1    Khaminets, A.2    Hunn, J.P.3    Howard, J.C.4
  • 72
    • 85026310020 scopus 로고    scopus 로고
    • Guanylate-binding protein 1 inhibits nuclear delivery of Kaposi's sarcoma-associated herpesvirus virions by disrupting formation of actin filament
    • Zou, Z., Meng, Z., Ma, C., Liang, D., Sun, R., & Lan, K. (2017). Guanylate-binding protein 1 inhibits nuclear delivery of Kaposi's sarcoma-associated herpesvirus virions by disrupting formation of actin filament. Journal of Virology, 91, e00632–17.
    • (2017) Journal of Virology , vol.91 , pp. e00617-e00632
    • Zou, Z.1    Meng, Z.2    Ma, C.3    Liang, D.4    Sun, R.5    Lan, K.6
  • 73
    • 85029745013 scopus 로고    scopus 로고
    • Guanylate binding proteins regulate inflammasome activation in response to hyper-injected Yersinia translocon components
    • Zwack, E. E., Feeley, E., Burton, A. R., Hu, B., Yamamoto, M., Kanneganti, T. D., … Brodsky, I. E. (2017). Guanylate binding proteins regulate inflammasome activation in response to hyper-injected Yersinia translocon components. Infection and Immunity, 85, e00778–16.
    • (2017) Infection and Immunity , vol.85 , pp. e00716-e00778
    • Zwack, E.E.1    Feeley, E.2    Burton, A.R.3    Hu, B.4    Yamamoto, M.5    Kanneganti, T.D.6    Brodsky, I.E.7


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