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Melo M.B., Jensen K.D., Saeij J.P. Toxoplasma gondii effectors are master regulators of the inflammatory response. Trends Parasitol. 2011, 27:487-495.
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Complex immune cell interplay in the gamma interferon response during Toxoplasma gondii infection
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Sturge C.R., Yarovinsky F. Complex immune cell interplay in the gamma interferon response during Toxoplasma gondii infection. Infect Immun. 2014, 82:3090-3097.
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Cohen S.B., Denkers E.Y. The gut mucosal immune response to Toxoplasma gondii. Parasite Immunol. 2015, 37:108-117.
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Dual role for inflammasome sensors NLRP1 and NLRP3 in murine resistance to Toxoplasma gondii
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pii: e01117-13
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Gorfu G., Cirelli K.M., Melo M.B., Mayer-Barber K., Crown D., Koller B.H., Masters S., Sher A., Leppla S.H., Moayeri M., Saeij J.P., Grigg M.E. Dual role for inflammasome sensors NLRP1 and NLRP3 in murine resistance to Toxoplasma gondii. MBio 2014, 5. (pii: e01117-13).
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Gorfu, G.1
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Masters, S.7
Sher, A.8
Leppla, S.H.9
Moayeri, M.10
Saeij, J.P.11
Grigg, M.E.12
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5
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Toxoplasma gondii dysregulates IFN-gamma-inducible gene expression in human fibroblasts: insights from a genome-wide transcriptional profiling
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Kim S.K., Fouts A.E., Boothroyd J.C. Toxoplasma gondii dysregulates IFN-gamma-inducible gene expression in human fibroblasts: insights from a genome-wide transcriptional profiling. J. Immunol. 2007, 178:5154-5165.
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Kim, S.K.1
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Toxoplasma co-opts host gene expression by injection of a polymorphic kinase homologue
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Saeij J.P., Coller S., Boyle J.P., Jerome M.E., White M.W., Boothroyd J.C. Toxoplasma co-opts host gene expression by injection of a polymorphic kinase homologue. Nature 2007, 445:324-327.
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Saeij, J.P.1
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Boothroyd, J.C.6
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7
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Transcriptional analysis of murine macrophages infected with different Toxoplasma strains identifies novel regulation of host signaling pathways
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Melo M.B., Nguyen Q.P., Cordeiro C., Hassan M.A., Yang N., McKell R., Rosowski E.E., Julien L., Butty V., Dardé M.L., Ajzenberg D., Fitzgerald K., Young L.H., Saeij J.P. Transcriptional analysis of murine macrophages infected with different Toxoplasma strains identifies novel regulation of host signaling pathways. PLoS Pathog. 2013, 9:e1003779.
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McKell, R.6
Rosowski, E.E.7
Julien, L.8
Butty, V.9
Dardé, M.L.10
Ajzenberg, D.11
Fitzgerald, K.12
Young, L.H.13
Saeij, J.P.14
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8
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84906259458
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Effector bottleneck: microbial reprogramming of parasitized host cell transcription by epigenetic remodeling of chromatin structure
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Sinclair S.H., Rennoll-Bankert K.E., Dumler J.S. Effector bottleneck: microbial reprogramming of parasitized host cell transcription by epigenetic remodeling of chromatin structure. Front. Genet. 2014, 5:274.
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Sinclair, S.H.1
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Pathogens hijack the epigenome: a new twist on host-pathogen interactions
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Silmon de Monerri N.C., Kim K. Pathogens hijack the epigenome: a new twist on host-pathogen interactions. Am. J. Pathol. 2014, 184:897-911.
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Silmon de Monerri, N.C.1
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10
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Toxoplasma gondii prevents chromatin remodeling initiated by TLR-triggered macrophage activation
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Leng J., Butcher B.A., Egan C.E., Abi Abdallah D.S., Denkers E.Y. Toxoplasma gondii prevents chromatin remodeling initiated by TLR-triggered macrophage activation. J. Immunol. 2009, 182:489-497.
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Leng, J.1
Butcher, B.A.2
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Denkers, E.Y.5
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11
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70449568923
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Toxoplasma gondii inhibits covalent modification of histone H3 at the IL-10 promoter in infected macrophages
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Leng J., Denkers E.Y. Toxoplasma gondii inhibits covalent modification of histone H3 at the IL-10 promoter in infected macrophages. PLoS ONE 2009, 4:e7589.
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Leng, J.1
Denkers, E.Y.2
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12
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84895929015
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MiR-146a and miR-155 delineate a microRNA fingerprint associated with Toxoplasma persistence in the host brain
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Cannella D., Brenier-Pinchart M.P., Braun L., van Rooyen J.M., Bougdour A., Bastien O., Behnke M.S., Curt R.L., Curt A., Saeij J.P., Sibley L.D., Pelloux H., Hakimi M.A. miR-146a and miR-155 delineate a microRNA fingerprint associated with Toxoplasma persistence in the host brain. Cell Rep. 2014, 6:928-937.
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Cannella, D.1
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Bastien, O.6
Behnke, M.S.7
Curt, R.L.8
Curt, A.9
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Sibley, L.D.11
Pelloux, H.12
Hakimi, M.A.13
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13
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84867751254
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Modulation of innate immunity by Toxoplasma gondii virulence effectors
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This excellent review describes how parasite-derived effectors modulate immune responses and likely virulence in mice model
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Hunter C.A., Sibley L.D. Modulation of innate immunity by Toxoplasma gondii virulence effectors. Nat. Rev. Microbiol. 2012, 10:766-778. This excellent review describes how parasite-derived effectors modulate immune responses and likely virulence in mice model.
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Hunter, C.A.1
Sibley, L.D.2
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14
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73349119704
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A single polymorphic amino acid on Toxoplasma gondii kinase ROP16 determines the direct and strain-specific activation of Stat3
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Yamamoto M., Standley D.M., Takashima S., Saiga H., Okuyama M., Kayama H., Kubo E., Ito H., Takaura M., Matsuda T., Soldati-Favre D., Takeda K. A single polymorphic amino acid on Toxoplasma gondii kinase ROP16 determines the direct and strain-specific activation of Stat3. J. Exp. Med. 2009, 206:2747-2760.
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Yamamoto, M.1
Standley, D.M.2
Takashima, S.3
Saiga, H.4
Okuyama, M.5
Kayama, H.6
Kubo, E.7
Ito, H.8
Takaura, M.9
Matsuda, T.10
Soldati-Favre, D.11
Takeda, K.12
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15
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77956538745
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Toxoplasma rhoptry protein 16 (ROP16) subverts host function by direct tyrosine phosphorylation of STAT6
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Ong Y.C., Reese M.L., Boothroyd J.C. Toxoplasma rhoptry protein 16 (ROP16) subverts host function by direct tyrosine phosphorylation of STAT6. J. Biol. Chem. 2010, 285:28731-28740.
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Ong, Y.C.1
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Boothroyd, J.C.3
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16
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84871122856
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Toxoplasma gondii clonal strains all inhibit STAT1 transcriptional activity but polymorphic effectors differentially modulate IFNγ induced gene expression and STAT1 phosphorylation
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Rosowski E.E., Saeij J.P. Toxoplasma gondii clonal strains all inhibit STAT1 transcriptional activity but polymorphic effectors differentially modulate IFNγ induced gene expression and STAT1 phosphorylation. PLoS ONE 2012, 7:e51448.
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Rosowski, E.E.1
Saeij, J.P.2
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17
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84877835069
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Toxoplasma gondii rhoptry 16 kinase promotes host resistance to oral infection and intestinal inflammation only in the context of the dense granule protein GRA15
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Jensen K.D., Hu K., Whitmarsh R.J., Hassan M.A., Julien L., Lu D., Chen L., Hunter C.A., Saeij J.P. Toxoplasma gondii rhoptry 16 kinase promotes host resistance to oral infection and intestinal inflammation only in the context of the dense granule protein GRA15. Infect. Immun. 2013, 81:2156-2167.
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Jensen, K.D.1
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Hassan, M.A.4
Julien, L.5
Lu, D.6
Chen, L.7
Hunter, C.A.8
Saeij, J.P.9
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18
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78651504365
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Strain-specific activation of the NF-kappaB pathway by GRA15, a novel Toxoplasma gondii dense granule protein
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Rosowski E.E., Lu D., Julien L., Rodda L., Gaiser R.A., Jensen K.D., Saeij J.P. Strain-specific activation of the NF-kappaB pathway by GRA15, a novel Toxoplasma gondii dense granule protein. J. Exp. Med. 2011, 208:195-212.
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Rosowski, E.E.1
Lu, D.2
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Jensen, K.D.6
Saeij, J.P.7
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19
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84907201011
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Selective and strain-specific NFAT4 activation by the Toxoplasma gondii polymorphic dense granule protein GRA6
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The authors show here that previously identified dense granule protein GRA6, known for its association with nanotubular structures in the PV, interacts directly with host Calcium modulating ligand (CAMLG) through its polymorphic C-terminal region to modulate NFAT4 activity. Thus, this paper confirms that vacuolar dense granule proteins could act as parasite-derived effector by altering host gene expression
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Ma J.S., Sasai M., Ohshima J., Lee Y., Bando H., Takeda K., Yamamoto M. Selective and strain-specific NFAT4 activation by the Toxoplasma gondii polymorphic dense granule protein GRA6. J. Exp. Med. 2014, 211:2013-2032. The authors show here that previously identified dense granule protein GRA6, known for its association with nanotubular structures in the PV, interacts directly with host Calcium modulating ligand (CAMLG) through its polymorphic C-terminal region to modulate NFAT4 activity. Thus, this paper confirms that vacuolar dense granule proteins could act as parasite-derived effector by altering host gene expression.
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J. Exp. Med.
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Ma, J.S.1
Sasai, M.2
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Lee, Y.4
Bando, H.5
Takeda, K.6
Yamamoto, M.7
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20
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84900454698
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GRA25 is a novel virulence factor of Toxoplasma gondii and influences the host immune response
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Shastri A.J., Marino N.D., Franco M., Lodoen M.B., Boothroyd J.C. GRA25 is a novel virulence factor of Toxoplasma gondii and influences the host immune response. Infect. Immun. 2014, 82:2595-2605.
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Shastri, A.J.1
Marino, N.D.2
Franco, M.3
Lodoen, M.B.4
Boothroyd, J.C.5
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21
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84876391823
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Host cell subversion by Toxoplasma GRA16, an exported dense granule protein that targets the host cell nucleus and alters gene expression
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This study reports the discovery of GRA16, the first dense granule to be released from the dense granules and exported beyond the vacuole-containing parasites into the host cell nucleus where the protein contributes to reshape the host transcriptome
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Bougdour A., Durandau E., Brenier-Pinchart M.P., Ortet P., Barakat M., Kieffer S., Curt-Varesano A., Curt-Bertini R.L., Bastien O., Coute Y., Pelloux H., Hakimi M.A. Host cell subversion by Toxoplasma GRA16, an exported dense granule protein that targets the host cell nucleus and alters gene expression. Cell Host Microbe. 2013, 13:489-500. This study reports the discovery of GRA16, the first dense granule to be released from the dense granules and exported beyond the vacuole-containing parasites into the host cell nucleus where the protein contributes to reshape the host transcriptome.
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Cell Host Microbe.
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Bougdour, A.1
Durandau, E.2
Brenier-Pinchart, M.P.3
Ortet, P.4
Barakat, M.5
Kieffer, S.6
Curt-Varesano, A.7
Curt-Bertini, R.L.8
Bastien, O.9
Coute, Y.10
Pelloux, H.11
Hakimi, M.A.12
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22
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84885444878
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A Toxoplasma dense granule protein, GRA24, modulates the early immune response to infection by promoting a direct and sustained host p38 MAPK activation
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This study describes how GRA24, following its release in the host cell, triggers activation of the MAP kinase p38α, leading to a broad inflammatory response which eventually leads to control parasite burden at the site of infection
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Braun L., Brenier-Pinchart M.P., Yogavel M., Curt-Varesano A., Curt-Bertini R.L., Hussain T., Kieffer-Jaquinod S., Coute Y., Pelloux H., Tardieux I., Sharma A., Belrhali H., Bougdour A., Hakimi M.A. A Toxoplasma dense granule protein, GRA24, modulates the early immune response to infection by promoting a direct and sustained host p38 MAPK activation. J. Exp. Med. 2013, 210:2071-2086. This study describes how GRA24, following its release in the host cell, triggers activation of the MAP kinase p38α, leading to a broad inflammatory response which eventually leads to control parasite burden at the site of infection.
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J. Exp. Med.
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Braun, L.1
Brenier-Pinchart, M.P.2
Yogavel, M.3
Curt-Varesano, A.4
Curt-Bertini, R.L.5
Hussain, T.6
Kieffer-Jaquinod, S.7
Coute, Y.8
Pelloux, H.9
Tardieux, I.10
Sharma, A.11
Belrhali, H.12
Bougdour, A.13
Hakimi, M.A.14
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23
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20144386721
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Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization
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Saridakis V., Sheng Y., Sarkari F., Holowaty M.N., Shire K., Nguyen T., Zhang R.G., Liao J., Lee W., Edwards A.M., Arrowsmith C.H., Frappier L. Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization. Mol. Cell. 2005, 18:25-36.
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Saridakis, V.1
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Nguyen, T.6
Zhang, R.G.7
Liao, J.8
Lee, W.9
Edwards, A.M.10
Arrowsmith, C.H.11
Frappier, L.12
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24
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84893839615
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Toxoplasma exports dense granule proteins beyond the vacuole to the host cell nucleus and rewires the host genome expression
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Bougdour A., Tardieux I., Hakimi M.A. Toxoplasma exports dense granule proteins beyond the vacuole to the host cell nucleus and rewires the host genome expression. Cell. Microbiol. 2014, 16:334-343.
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Bougdour, A.1
Tardieux, I.2
Hakimi, M.A.3
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25
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80054761315
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Tumor suppressor protein (p)53, is a regulator of NF-kappaB repression by the glucocorticoid receptor
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Murphy S.H., Suzuki K., Downes M., Welch G.L., De Jesus P., Miraglia L.J., Orth A.P., Chanda S.K., Evans R.M., Verma I.M. Tumor suppressor protein (p)53, is a regulator of NF-kappaB repression by the glucocorticoid receptor. Proc. Natl. Acad. Sci. U.S.A. 2011, 108:17117-17122.
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Murphy, S.H.1
Suzuki, K.2
Downes, M.3
Welch, G.L.4
De Jesus, P.5
Miraglia, L.J.6
Orth, A.P.7
Chanda, S.K.8
Evans, R.M.9
Verma, I.M.10
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26
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84885462754
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CD4+ T cells are trigger and target of the glucocorticoid response that prevents lethal immunopathology in toxoplasma infection
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The authors have identified glucocorticoids as important regulators of Th1 cell responses in mice infected with T. gondii
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Kugler D.G., Mittelstadt P.R., Ashwell J.D., Sher A., Jankovic D. CD4+ T cells are trigger and target of the glucocorticoid response that prevents lethal immunopathology in toxoplasma infection. J. Exp. Med. 2013, 210:1919-1927. The authors have identified glucocorticoids as important regulators of Th1 cell responses in mice infected with T. gondii.
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Kugler, D.G.1
Mittelstadt, P.R.2
Ashwell, J.D.3
Sher, A.4
Jankovic, D.5
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27
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78651305134
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Factor binding and chromatin modification in the promoter of murine Egr1 gene upon induction
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Tur G., Georgieva E.I., Gagete A., López-Rodas G., Rodríguez J.L., Franco L. Factor binding and chromatin modification in the promoter of murine Egr1 gene upon induction. Cell. Mol. Life Sci. 2010, 67:4065-4077.
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Tur, G.1
Georgieva, E.I.2
Gagete, A.3
López-Rodas, G.4
Rodríguez, J.L.5
Franco, L.6
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28
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84866354593
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MiR-146a controls the resolution of T cell responses in mice
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Yang L., Boldin M.P., Yu Y., Liu C.S., Ea C.K., Ramakrishnan P., Taganov K.D., Zhao J.L., Baltimore D. miR-146a controls the resolution of T cell responses in mice. J. Exp. Med. 2012, 209:1655-1670.
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J. Exp. Med.
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Yang, L.1
Boldin, M.P.2
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Ramakrishnan, P.6
Taganov, K.D.7
Zhao, J.L.8
Baltimore, D.9
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29
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79958695985
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Toxoplasma polymorphic effectors determine macrophage polarization and intestinal inflammation
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This paper demonstrates a cross-talk between a rhoptry protein, ROP16 and a dense granule protein, GRA15 that contributes to macrophage polarization early during Toxoplasma infection.
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Jensen K.D., Wang Y., Wojno E.D., Shastri A.J., Hu K., Cornel L., Boedec E., Ong Y.C., Chien Y.H., Hunter C.A., Boothroyd J.C., Saeij J.P. Toxoplasma polymorphic effectors determine macrophage polarization and intestinal inflammation. Cell Host Microbe. 2011, 9:472-483. This paper demonstrates a cross-talk between a rhoptry protein, ROP16 and a dense granule protein, GRA15 that contributes to macrophage polarization early during Toxoplasma infection.
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Cell Host Microbe.
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Jensen, K.D.1
Wang, Y.2
Wojno, E.D.3
Shastri, A.J.4
Hu, K.5
Cornel, L.6
Boedec, E.7
Ong, Y.C.8
Chien, Y.H.9
Hunter, C.A.10
Boothroyd, J.C.11
Saeij, J.P.12
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30
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Integrative genomic approaches highlight a family of parasite-specific kinases that regulate host responses
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Peixoto L., Chen F., Harb O.S., Davis P.H., Beiting D.P., Brownback C.S., Ouloguem D., Roos D.S. Integrative genomic approaches highlight a family of parasite-specific kinases that regulate host responses. Cell Host Microbe. 2010, 8:208-218.
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Cell Host Microbe.
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Peixoto, L.1
Chen, F.2
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Beiting, D.P.5
Brownback, C.S.6
Ouloguem, D.7
Roos, D.S.8
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31
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82655175482
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Attributes of short linear motifs
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Davey N.E., Van Roey K., Weatheritt R.J., Toedt G., Uyar B., Altenberg B., Budd A., Diella F., Dinkel H., Gibson T.J. Attributes of short linear motifs. Mol. Biosyst. 2012, 8:268-281.
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Altenberg, B.6
Budd, A.7
Diella, F.8
Dinkel, H.9
Gibson, T.J.10
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32
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84902318220
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Use of host-like peptide motifs in viral proteins is a prevalent strategy in host-virus interactions
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Hagai T., Azia A., Babu M.M., Andino R. Use of host-like peptide motifs in viral proteins is a prevalent strategy in host-virus interactions. Cell Rep. 2014, 7:1729-1739.
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A million peptide motifs for the molecular biologist
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Tompa P., Davey N.E., Gibson T.J., Babu M.M. A million peptide motifs for the molecular biologist. Mol. Cell. 2014, 55:161-169.
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How pathogens use linear motifs to perturb host cell networks
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Via A., Uyar B., Brun C., Zanzoni A. How pathogens use linear motifs to perturb host cell networks. Trends Biochem. Sci. 2015, 40:36-48.
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Elde N.C., Malik H.S. The evolutionary conundrum of pathogen mimicry. Nat. Rev. Microbiol. 2009, 7:787-797.
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Systems-based analysis of the Sarcocystis neurona genome identifies pathways that contribute to a heteroxenous life cycle
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This study presents the first genome sequence of Sarcocystis neurona, a coccidia that develops in host cell cytoplasm without forming a vacuole. S. neurona genome is missing most of the GRA- and ROP-encoding genes and therefore makes a fantastic tool for comparative genomics to identify bona fide Toxoplasma-specific effectors
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Blazejewski T., Nursimulu N., Pszenny V., Dangoudoubiyam S., Namasivayam S., Chiasson M.A., Chessman K., Tonkin M., Swapna L.S., Hung S.S., Bridgers J., Ricklefs S.M., Boulanger M.J., Dubey J.P., Porcella S.F., Kissinger J.C., Howe D.K., Grigg M.E., Parkinson J. Systems-based analysis of the Sarcocystis neurona genome identifies pathways that contribute to a heteroxenous life cycle. MBio 2015, 6:e02445-e2514. This study presents the first genome sequence of Sarcocystis neurona, a coccidia that develops in host cell cytoplasm without forming a vacuole. S. neurona genome is missing most of the GRA- and ROP-encoding genes and therefore makes a fantastic tool for comparative genomics to identify bona fide Toxoplasma-specific effectors.
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Blazejewski, T.1
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Chiasson, M.A.6
Chessman, K.7
Tonkin, M.8
Swapna, L.S.9
Hung, S.S.10
Bridgers, J.11
Ricklefs, S.M.12
Boulanger, M.J.13
Dubey, J.P.14
Porcella, S.F.15
Kissinger, J.C.16
Howe, D.K.17
Grigg, M.E.18
Parkinson, J.19
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Infection by Toxoplasma gondii specifically induces host c-Myc and the genes this pivotal transcription factor regulates
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Franco M., Shastri A.J., Boothroyd J.C. Infection by Toxoplasma gondii specifically induces host c-Myc and the genes this pivotal transcription factor regulates. Eukaryot. Cell. 2014, 13:483-493.
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Toxoplasma gondii rhoptry discharge correlates with activation of the early growth response 2 host cell transcription factor
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Phelps E.D., Sweeney K.R., Blader I.J. Toxoplasma gondii rhoptry discharge correlates with activation of the early growth response 2 host cell transcription factor. Infect. Immun. 2008, 76:4703-4712.
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Phelps, E.D.1
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