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Volumn 46, Issue 2, 2016, Pages 269-280

AIM2 inflammasome in infection, cancer, and autoimmunity: Role in DNA sensing, inflammation, and innate immunity

Author keywords

AIM2 inflammasome; Autoimmunity; Bacterial viral infection; Cancer; DNA sensing; Gut microbiota

Indexed keywords

AIM2 INFLAMMASOME; DNA; INFLAMMASOME; UNCLASSIFIED DRUG; AIM2 PROTEIN, HUMAN; DNA BINDING PROTEIN; PATTERN RECOGNITION RECEPTOR;

EID: 84956825823     PISSN: 00142980     EISSN: 15214141     Source Type: Journal    
DOI: 10.1002/eji.201545839     Document Type: Review
Times cited : (263)

References (124)
  • 2
    • 29244471275 scopus 로고    scopus 로고
    • A Toll-like receptor-independent antiviral response induced by double-stranded B-form DNA
    • Ishii, K. J., Coban, C., Kato, H., Takahashi, K., Torii, Y., Takeshita, F., Ludwig, H. et al., A Toll-like receptor-independent antiviral response induced by double-stranded B-form DNA. Nat. Immunol. 2006. 7: 40-48.
    • (2006) Nat. Immunol. , vol.7 , pp. 40-48
    • Ishii, K.J.1    Coban, C.2    Kato, H.3    Takahashi, K.4    Torii, Y.5    Takeshita, F.6    Ludwig, H.7
  • 3
    • 30444450839 scopus 로고    scopus 로고
    • Recognition of cytosolic DNA activates an IRF3-dependent innate immune response
    • Stetson, D. B. and Medzhitov, R., Recognition of cytosolic DNA activates an IRF3-dependent innate immune response. Immunity 2006. 24: 93-103.
    • (2006) Immunity , vol.24 , pp. 93-103
    • Stetson, D.B.1    Medzhitov, R.2
  • 4
    • 84874223452 scopus 로고    scopus 로고
    • Molecular basis of DNA recognition in the immune system
    • Atianand, M. K. and Fitzgerald, K. A., Molecular basis of DNA recognition in the immune system. J. Immunol. 2013. 190: 1911-1918.
    • (2013) J. Immunol. , vol.190 , pp. 1911-1918
    • Atianand, M.K.1    Fitzgerald, K.A.2
  • 5
    • 84893934506 scopus 로고    scopus 로고
    • Recognition of cytosolic DNA by cGAS and other STING-dependent sensors
    • Bhat, N. and Fitzgerald, K. A., Recognition of cytosolic DNA by cGAS and other STING-dependent sensors. Eur. J. Immunol. 2014. 44: 634-640.
    • (2014) Eur. J. Immunol. , vol.44 , pp. 634-640
    • Bhat, N.1    Fitzgerald, K.A.2
  • 6
    • 84861678659 scopus 로고    scopus 로고
    • Induction of type I IFNs by intracellular DNA-sensing pathways
    • Cavlar, T., Ablasser, A. and Hornung, V., Induction of type I IFNs by intracellular DNA-sensing pathways. Immunol. Cell Biol. 2012. 90: 474-482.
    • (2012) Immunol. Cell Biol. , vol.90 , pp. 474-482
    • Cavlar, T.1    Ablasser, A.2    Hornung, V.3
  • 7
    • 84899131835 scopus 로고    scopus 로고
    • The cGAS-cGAMP-STING pathway of cytosolic DNA sensing and signaling
    • Cai, X., Chiu, Y. H. and Chen, Z. J., The cGAS-cGAMP-STING pathway of cytosolic DNA sensing and signaling. Mol. Cell 2014. 54: 289-296.
    • (2014) Mol. Cell , vol.54 , pp. 289-296
    • Cai, X.1    Chiu, Y.H.2    Chen, Z.J.3
  • 8
    • 40449097257 scopus 로고    scopus 로고
    • The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response
    • Muruve, D. A., Petrilli, V., Zaiss, A. K., White, L. R., Clark, S. A., Ross, P. J., Parks, R. J. et al., The inflammasome recognizes cytosolic microbial and host DNA and triggers an innate immune response. Nature 2008. 452: 103-107.
    • (2008) Nature , vol.452 , pp. 103-107
    • Muruve, D.A.1    Petrilli, V.2    Zaiss, A.K.3    White, L.R.4    Clark, S.A.5    Ross, P.J.6    Parks, R.J.7
  • 9
    • 0027465288 scopus 로고
    • Electroporation and DNA-dependent cell death in murine macrophages
    • Stacey, K. J., Ross, I. L. and Hume, D. A., Electroporation and DNA-dependent cell death in murine macrophages. Immunol. Cell Biol. 1993. 71 (Pt 2): 75-85.
    • (1993) Immunol. Cell Biol. , vol.71 , pp. 75-85
    • Stacey, K.J.1    Ross, I.L.2    Hume, D.A.3
  • 10
    • 84927732725 scopus 로고    scopus 로고
    • Regulation of inflammasome activation
    • Man, S. M. and Kanneganti, T. D., Regulation of inflammasome activation. Immunol. Rev. 2015. 265: 6-21.
    • (2015) Immunol. Rev. , vol.265 , pp. 6-21
    • Man, S.M.1    Kanneganti, T.D.2
  • 12
    • 63649145255 scopus 로고    scopus 로고
    • AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA
    • Fernandes-Alnemri, T., Yu, J. W., Datta, P., Wu, J. and Alnemri, E. S., AIM2 activates the inflammasome and cell death in response to cytoplasmic DNA. Nature 2009. 458: 509-513.
    • (2009) Nature , vol.458 , pp. 509-513
    • Fernandes-Alnemri, T.1    Yu, J.W.2    Datta, P.3    Wu, J.4    Alnemri, E.S.5
  • 13
    • 60749136484 scopus 로고    scopus 로고
    • An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome
    • Burckstummer, T., Baumann, C., Bluml, S., Dixit, E., Durnberger, G., Jahn, H., Planyavsky, M. et al., An orthogonal proteomic-genomic screen identifies AIM2 as a cytoplasmic DNA sensor for the inflammasome. Nat. Immunol. 2009. 10: 266-272.
    • (2009) Nat. Immunol. , vol.10 , pp. 266-272
    • Burckstummer, T.1    Baumann, C.2    Bluml, S.3    Dixit, E.4    Durnberger, G.5    Jahn, H.6    Planyavsky, M.7
  • 14
    • 60749104535 scopus 로고    scopus 로고
    • HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA
    • Roberts, T. L., Idris, A., Dunn, J. A., Kelly, G. M., Burnton, C. M., Hodgson, S., Hardy, L. L. et al., HIN-200 proteins regulate caspase activation in response to foreign cytoplasmic DNA. Science 2009. 323: 1057-1060.
    • (2009) Science , vol.323 , pp. 1057-1060
    • Roberts, T.L.1    Idris, A.2    Dunn, J.A.3    Kelly, G.M.4    Burnton, C.M.5    Hodgson, S.6    Hardy, L.L.7
  • 16
    • 84870275730 scopus 로고    scopus 로고
    • Extensive evolutionary and functional diversity among mammalian AIM2-like receptors
    • Brunette, R. L., Young, J. M., Whitley, D. G., Brodsky, I. E., Malik, H. S. and Stetson, D. B., Extensive evolutionary and functional diversity among mammalian AIM2-like receptors. J. Exp. Med. 2012. 209: 1969-1983.
    • (2012) J. Exp. Med. , vol.209 , pp. 1969-1983
    • Brunette, R.L.1    Young, J.M.2    Whitley, D.G.3    Brodsky, I.E.4    Malik, H.S.5    Stetson, D.B.6
  • 18
    • 84859986329 scopus 로고    scopus 로고
    • Structures of the HIN domain: DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor
    • Jin, T., Perry, A., Jiang, J., Smith, P., Curry, J. A., Unterholzner, L., Jiang, Z. et al., Structures of the HIN domain: DNA complexes reveal ligand binding and activation mechanisms of the AIM2 inflammasome and IFI16 receptor. Immunity 2012. 36: 561-571.
    • (2012) Immunity , vol.36 , pp. 561-571
    • Jin, T.1    Perry, A.2    Jiang, J.3    Smith, P.4    Curry, J.A.5    Unterholzner, L.6    Jiang, Z.7
  • 19
    • 84877692253 scopus 로고    scopus 로고
    • Structure of the absent in melanoma 2 (AIM2) pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly
    • Jin, T., Perry, A., Smith, P., Jiang, J. and Xiao, T. S., Structure of the absent in melanoma 2 (AIM2) pyrin domain provides insights into the mechanisms of AIM2 autoinhibition and inflammasome assembly. J. Biol. Chem. 2013. 288: 13225-13235.
    • (2013) J. Biol. Chem. , vol.288 , pp. 13225-13235
    • Jin, T.1    Perry, A.2    Smith, P.3    Jiang, J.4    Xiao, T.S.5
  • 20
    • 84895923768 scopus 로고    scopus 로고
    • Crystal structure of the F27G AIM2 PYD mutant and similarities of its self-association to DED/DED interactions
    • Lu, A., Kabaleeswaran, V., Fu, T., Magupalli, V. G. and Wu, H., Crystal structure of the F27G AIM2 PYD mutant and similarities of its self-association to DED/DED interactions. J. Mol. Biol. 2014. 426: 1420-1427.
    • (2014) J. Mol. Biol. , vol.426 , pp. 1420-1427
    • Lu, A.1    Kabaleeswaran, V.2    Fu, T.3    Magupalli, V.G.4    Wu, H.5
  • 21
    • 84937759923 scopus 로고    scopus 로고
    • The NMR solution structure of AIM2 PYD domain from Mus musculus reveals a distinct alpha2-alpha3 helix conformation from its human homologues
    • Hou, X. and Niu, X., The NMR solution structure of AIM2 PYD domain from Mus musculus reveals a distinct alpha2-alpha3 helix conformation from its human homologues. Biochem. Biophys. Res. Commun. 2015. 461: 396-400.
    • (2015) Biochem. Biophys. Res. Commun. , vol.461 , pp. 396-400
    • Hou, X.1    Niu, X.2
  • 22
    • 84896332642 scopus 로고    scopus 로고
    • Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes
    • Lu, A., Magupalli, V. G., Ruan, J., Yin, Q., Atianand, M. K., Vos, M. R., Schroder, G. F. et al., Unified polymerization mechanism for the assembly of ASC-dependent inflammasomes. Cell 2014. 156: 1193-1206.
    • (2014) Cell , vol.156 , pp. 1193-1206
    • Lu, A.1    Magupalli, V.G.2    Ruan, J.3    Yin, Q.4    Atianand, M.K.5    Vos, M.R.6    Schroder, G.F.7
  • 23
    • 84896381627 scopus 로고    scopus 로고
    • Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation
    • Cai, X., Chen, J., Xu, H., Liu, S., Jiang, Q. X., Halfmann, R. and Chen, Z. J., Prion-like polymerization underlies signal transduction in antiviral immune defense and inflammasome activation. Cell 2014. 156: 1207-1222.
    • (2014) Cell , vol.156 , pp. 1207-1222
    • Cai, X.1    Chen, J.2    Xu, H.3    Liu, S.4    Jiang, Q.X.5    Halfmann, R.6    Chen, Z.J.7
  • 24
    • 77955390094 scopus 로고    scopus 로고
    • Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella
    • Broz, P., Newton, K., Lamkanfi, M., Mariathasan, S., Dixit, V. M. and Monack, D. M., Redundant roles for inflammasome receptors NLRP3 and NLRC4 in host defense against Salmonella. J. Exp. Med. 2010. 207: 1745-1755.
    • (2010) J. Exp. Med. , vol.207 , pp. 1745-1755
    • Broz, P.1    Newton, K.2    Lamkanfi, M.3    Mariathasan, S.4    Dixit, V.M.5    Monack, D.M.6
  • 26
    • 83655163772 scopus 로고    scopus 로고
    • Francisella infection triggers activation of the AIM2 inflammasome in murine dendritic cells
    • Belhocine, K. and Monack, D. M., Francisella infection triggers activation of the AIM2 inflammasome in murine dendritic cells. Cell Microbiol. 2012. 14: 71-80.
    • (2012) Cell Microbiol. , vol.14 , pp. 71-80
    • Belhocine, K.1    Monack, D.M.2
  • 27
    • 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., Lamkanfi, M. et al., The transcription factor IRF1 and guanylate-binding proteins target activation of the AIM2 inflammasome by Francisella infection. Nat. Immunol. 2015. 16: 467-475.
    • (2015) Nat. Immunol. , 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    Lamkanfi, M.7
  • 28
    • 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., Dussurgey, S. et al., Guanylate-binding proteins promote activation of the AIM2 inflammasome during infection with Francisella novicida. Nat. Immunol. 2015. 16: 476-484.
    • (2015) Nat. Immunol. , vol.16 , pp. 476-484
    • Meunier, E.1    Wallet, P.2    Dreier, R.F.3    Costanzo, S.4    Anton, L.5    Ruhl, S.6    Dussurgey, S.7
  • 30
    • 84937902109 scopus 로고    scopus 로고
    • Assembly-driven activation of the AIM2 foreign-dsDNA sensor provides a polymerization template for downstream ASC
    • Morrone, S. R., Matyszewski, M., Yu, X., Delannoy, M., Egelman, E. H. and Sohn, J., Assembly-driven activation of the AIM2 foreign-dsDNA sensor provides a polymerization template for downstream ASC. Nat. Commun. 2015. 6: 7827.
    • (2015) Nat. Commun. , vol.6 , pp. 7827
    • Morrone, S.R.1    Matyszewski, M.2    Yu, X.3    Delannoy, M.4    Egelman, E.H.5    Sohn, J.6
  • 31
    • 84942892037 scopus 로고    scopus 로고
    • Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death
    • Shi, J., Zhao, Y., Wang, K., Shi, X., Wang, Y., Huang, H., Zhuang, Y. et al., Cleavage of GSDMD by inflammatory caspases determines pyroptotic cell death. Nature 2015. 526: 660-665.
    • (2015) Nature , vol.526 , pp. 660-665
    • Shi, J.1    Zhao, Y.2    Wang, K.3    Shi, X.4    Wang, Y.5    Huang, H.6    Zhuang, Y.7
  • 33
    • 84887897805 scopus 로고    scopus 로고
    • Phosphorylation of the adaptor ASC acts as a molecular switch that controls the formation of speck-like aggregates and inflammasome activity
    • Hara, H., Tsuchiya, K., Kawamura, I., Fang, R., Hernandez-Cuellar, E., Shen, Y., Mizuguchi, J. et al., Phosphorylation of the adaptor ASC acts as a molecular switch that controls the formation of speck-like aggregates and inflammasome activity. Nat. Immunol. 2013. 14: 1247-1255.
    • (2013) Nat. Immunol. , vol.14 , pp. 1247-1255
    • Hara, H.1    Tsuchiya, K.2    Kawamura, I.3    Fang, R.4    Hernandez-Cuellar, E.5    Shen, Y.6    Mizuguchi, J.7
  • 34
    • 84903761551 scopus 로고    scopus 로고
    • The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation
    • Rodgers, M. A., Bowman, J. W., Fujita, H., Orazio, N., Shi, M., Liang, Q., Amatya, R. et al., The linear ubiquitin assembly complex (LUBAC) is essential for NLRP3 inflammasome activation. J. Exp. Med. 2014. 211: 1333-1347.
    • (2014) J. Exp. Med. , vol.211 , pp. 1333-1347
    • Rodgers, M.A.1    Bowman, J.W.2    Fujita, H.3    Orazio, N.4    Shi, M.5    Liang, Q.6    Amatya, R.7
  • 35
    • 84857195479 scopus 로고    scopus 로고
    • Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction
    • Shi, C. S., Shenderov, K., Huang, N. N., Kabat, J., Abu-Asab, M., Fitzgerald, K. A., Sher, A. et al., Activation of autophagy by inflammatory signals limits IL-1beta production by targeting ubiquitinated inflammasomes for destruction. Nat. Immunol. 2012. 13: 255-263.
    • (2012) Nat. Immunol. , vol.13 , pp. 255-263
    • Shi, C.S.1    Shenderov, K.2    Huang, N.N.3    Kabat, J.4    Abu-Asab, M.5    Fitzgerald, K.A.6    Sher, A.7
  • 36
    • 84896638307 scopus 로고    scopus 로고
    • The PYRIN domain-only protein POP3 inhibits ALR inflammasomes and regulates responses to infection with DNA viruses
    • Khare, S., Ratsimandresy, R. A., de Almeida, L., Cuda, C. M., Rellick, S. L., Misharin, A. V., Wallin, M. C. et al., The PYRIN domain-only protein POP3 inhibits ALR inflammasomes and regulates responses to infection with DNA viruses. Nat. Immunol. 2014. 15: 343-353.
    • (2014) Nat. Immunol. , vol.15 , pp. 343-353
    • Khare, S.1    Ratsimandresy, R.A.2    de Almeida, L.3    Cuda, C.M.4    Rellick, S.L.5    Misharin, A.V.6    Wallin, M.C.7
  • 37
    • 80055045773 scopus 로고    scopus 로고
    • IFI16 protein mediates the anti-inflammatory actions of the type-I interferons through suppression of activation of caspase-1 by inflammasomes
    • Veeranki, S., Duan, X., Panchanathan, R., Liu, H. and Choubey, D., IFI16 protein mediates the anti-inflammatory actions of the type-I interferons through suppression of activation of caspase-1 by inflammasomes. PLoS One 2011. 6: e27040.
    • (2011) PLoS One , vol.6 , pp. e27040
    • Veeranki, S.1    Duan, X.2    Panchanathan, R.3    Liu, H.4    Choubey, D.5
  • 39
    • 84940970623 scopus 로고    scopus 로고
    • The PYRIN domain-only protein POP1 inhibits inflammasome assembly and ameliorates inflammatory disease
    • de Almeida, L., Khare, S., Misharin, A. V., Patel, R., Ratsimandresy, R. A., Wallin, M. C., Perlman, H. et al., The PYRIN domain-only protein POP1 inhibits inflammasome assembly and ameliorates inflammatory disease. Immunity 2015. 43: 264-276.
    • (2015) Immunity , vol.43 , pp. 264-276
    • de Almeida, L.1    Khare, S.2    Misharin, A.V.3    Patel, R.4    Ratsimandresy, R.A.5    Wallin, M.C.6    Perlman, H.7
  • 40
    • 0034716983 scopus 로고    scopus 로고
    • Cytoplasmic localization of the interferon-inducible protein that is encoded by the AIM2 (absent in melanoma) gene from the 200-gene family
    • Choubey, D., Walter, S., Geng, Y. and Xin, H., Cytoplasmic localization of the interferon-inducible protein that is encoded by the AIM2 (absent in melanoma) gene from the 200-gene family. FEBS Lett. 2000. 474: 38-42.
    • (2000) FEBS Lett. , vol.474 , pp. 38-42
    • Choubey, D.1    Walter, S.2    Geng, Y.3    Xin, H.4
  • 41
    • 84880818953 scopus 로고    scopus 로고
    • Molecular mechanism for p202-mediated specific inhibition of AIM2 inflammasome activation
    • Yin, Q., Sester, D. P., Tian, Y., Hsiao, Y. S., Lu, A., Cridland, J. A., Sagulenko, V. et al., Molecular mechanism for p202-mediated specific inhibition of AIM2 inflammasome activation. Cell Rep. 2013. 4: 327-339.
    • (2013) Cell Rep. , vol.4 , pp. 327-339
    • Yin, Q.1    Sester, D.P.2    Tian, Y.3    Hsiao, Y.S.4    Lu, A.5    Cridland, J.A.6    Sagulenko, V.7
  • 42
    • 47149108866 scopus 로고    scopus 로고
    • Interferon-inducible Ifi200-family genes in systemic lupus erythematosus
    • Choubey, D. and Panchanathan, R., Interferon-inducible Ifi200-family genes in systemic lupus erythematosus. Immunol. Lett. 2008. 119: 32-41.
    • (2008) Immunol. Lett. , vol.119 , pp. 32-41
    • Choubey, D.1    Panchanathan, R.2
  • 44
    • 77951269392 scopus 로고    scopus 로고
    • The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses
    • Rathinam, V. A., Jiang, Z., Waggoner, S. N., Sharma, S., Cole, L. E., Waggoner, L., Vanaja, S. K. et al., The AIM2 inflammasome is essential for host defense against cytosolic bacteria and DNA viruses. Nat. Immunol. 2010. 11: 395-402.
    • (2010) Nat. Immunol. , vol.11 , pp. 395-402
    • Rathinam, V.A.1    Jiang, Z.2    Waggoner, S.N.3    Sharma, S.4    Cole, L.E.5    Waggoner, L.6    Vanaja, S.K.7
  • 47
    • 84866087868 scopus 로고    scopus 로고
    • AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages
    • Pierini, R., Juruj, C., Perret, M., Jones, C. L., Mangeot, P., Weiss, D. S. and Henry, T., AIM2/ASC triggers caspase-8-dependent apoptosis in Francisella-infected caspase-1-deficient macrophages. Cell Death Differ. 2012. 19: 1709-1721.
    • (2012) Cell Death Differ. , vol.19 , pp. 1709-1721
    • Pierini, R.1    Juruj, C.2    Perret, M.3    Jones, C.L.4    Mangeot, P.5    Weiss, D.S.6    Henry, T.7
  • 48
    • 80655125021 scopus 로고    scopus 로고
    • Francisella tularensis reveals a disparity between human and mouse NLRP3 inflammasome activation
    • Atianand, M. K., Duffy, E. B., Shah, A., Kar, S., Malik, M. and Harton, J. A., Francisella tularensis reveals a disparity between human and mouse NLRP3 inflammasome activation. J. Biol. Chem. 2011. 286: 39033-39042.
    • (2011) J. Biol. Chem. , vol.286 , pp. 39033-39042
    • Atianand, M.K.1    Duffy, E.B.2    Shah, A.3    Kar, S.4    Malik, M.5    Harton, J.A.6
  • 50
    • 77955294800 scopus 로고    scopus 로고
    • Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol
    • Sauer, J. D., Witte, C. E., Zemansky, J., Hanson, B., Lauer, P. and Portnoy, D. A., Listeria monocytogenes triggers AIM2-mediated pyroptosis upon infrequent bacteriolysis in the macrophage cytosol. Cell Host Microbe 2010. 7: 412-419.
    • (2010) Cell Host Microbe , vol.7 , pp. 412-419
    • Sauer, J.D.1    Witte, C.E.2    Zemansky, J.3    Hanson, B.4    Lauer, P.5    Portnoy, D.A.6
  • 52
    • 77957578665 scopus 로고    scopus 로고
    • Involvement of the AIM2, NLRC4, and NLRP3 inflammasomes in caspase-1 activation by Listeria monocytogenes
    • Wu, J., Fernandes-Alnemri, T. and Alnemri, E. S., Involvement of the AIM2, NLRC4, and NLRP3 inflammasomes in caspase-1 activation by Listeria monocytogenes. J. Clin. Immunol. 2010. 30: 693-702.
    • (2010) J. Clin. Immunol. , vol.30 , pp. 693-702
    • Wu, J.1    Fernandes-Alnemri, T.2    Alnemri, E.S.3
  • 53
    • 80555133274 scopus 로고    scopus 로고
    • Critical roles of ASC inflammasomes in caspase-1 activation and host innate resistance to Streptococcus pneumoniae infection
    • Fang, R., Tsuchiya, K., Kawamura, I., Shen, Y., Hara, H., Sakai, S., Yamamoto, T. et al., Critical roles of ASC inflammasomes in caspase-1 activation and host innate resistance to Streptococcus pneumoniae infection. J. Immunol. 2011. 187: 4890-4899.
    • (2011) J. Immunol. , vol.187 , pp. 4890-4899
    • Fang, R.1    Tsuchiya, K.2    Kawamura, I.3    Shen, Y.4    Hara, H.5    Sakai, S.6    Yamamoto, T.7
  • 54
    • 84930254935 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis differentially activates cGAS- and inflammasome-dependent intracellular immune responses through ESX-1
    • Wassermann, R., Gulen, M. F., Sala, C., Perin, S. G., Lou, Y., Rybniker, J., Schmid-Burgk, J. L. et al., Mycobacterium tuberculosis differentially activates cGAS- and inflammasome-dependent intracellular immune responses through ESX-1. Cell Host Microbe 2015. 17: 799-810.
    • (2015) Cell Host Microbe , vol.17 , pp. 799-810
    • Wassermann, R.1    Gulen, M.F.2    Sala, C.3    Perin, S.G.4    Lou, Y.5    Rybniker, J.6    Schmid-Burgk, J.L.7
  • 57
    • 84888593652 scopus 로고    scopus 로고
    • The AIM2 inflammasome is involved in macrophage activation during infection with virulent Mycobacterium bovis strain
    • Yang, Y., Zhou, X., Kouadir, M., Shi, F., Ding, T., Liu, C., Liu, J. et al., The AIM2 inflammasome is involved in macrophage activation during infection with virulent Mycobacterium bovis strain. J. Infect. Dis. 2013. 208: 1849-1858.
    • (2013) J. Infect. Dis. , vol.208 , pp. 1849-1858
    • Yang, Y.1    Zhou, X.2    Kouadir, M.3    Shi, F.4    Ding, T.5    Liu, C.6    Liu, J.7
  • 58
    • 84890829177 scopus 로고    scopus 로고
    • Activation of NLRP3 and AIM2 inflammasomes by Porphyromonas gingivalis infection
    • Park, E., Na, H. S., Song, Y. R., Shin, S. Y., Kim, Y. M. and Chung, J., Activation of NLRP3 and AIM2 inflammasomes by Porphyromonas gingivalis infection. Infect. Immun. 2014. 82: 112-123.
    • (2014) Infect. Immun. , vol.82 , pp. 112-123
    • Park, E.1    Na, H.S.2    Song, Y.R.3    Shin, S.Y.4    Kim, Y.M.5    Chung, J.6
  • 59
    • 84899474093 scopus 로고    scopus 로고
    • Critical role for the AIM2 inflammasome during acute CNS bacterial infection
    • Hanamsagar, R., Aldrich, A. and Kielian, T., Critical role for the AIM2 inflammasome during acute CNS bacterial infection. J. Neurochem. 2014. 129: 704-711.
    • (2014) J. Neurochem. , vol.129 , pp. 704-711
    • Hanamsagar, R.1    Aldrich, A.2    Kielian, T.3
  • 60
    • 84875431649 scopus 로고    scopus 로고
    • Critical role of ASC inflammasomes and bacterial type IV secretion system in caspase-1 activation and host innate resistance to Brucella abortus infection
    • Gomes, M. T., Campos, P. C., Oliveira, F. S., Corsetti, P. P., Bortoluci, K. R., Cunha, L. D., Zamboni, D. S. et al., Critical role of ASC inflammasomes and bacterial type IV secretion system in caspase-1 activation and host innate resistance to Brucella abortus infection. J. Immunol. 2013. 190: 3629-3638.
    • (2013) J. Immunol. , vol.190 , pp. 3629-3638
    • Gomes, M.T.1    Campos, P.C.2    Oliveira, F.S.3    Corsetti, P.P.4    Bortoluci, K.R.5    Cunha, L.D.6    Zamboni, D.S.7
  • 61
    • 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., Yamamoto, M. et al., Guanylate binding proteins enable rapid activation of canonical and noncanonical inflammasomes in chlamydia-infected macrophages. Infect. Immun. 2015. 83: 4740-4749.
    • (2015) Infect. Immun. , 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    Yamamoto, M.7
  • 63
    • 80052813504 scopus 로고    scopus 로고
    • Elevated AIM2-mediated pyroptosis triggered by hypercytotoxic Francisella mutant strains is attributed to increased intracellular bacteriolysis
    • Peng, K., Broz, P., Jones, J., Joubert, L. M. and Monack, D., Elevated AIM2-mediated pyroptosis triggered by hypercytotoxic Francisella mutant strains is attributed to increased intracellular bacteriolysis. Cell Microbiol. 2011. 13: 1586-1600.
    • (2011) Cell Microbiol. , vol.13 , pp. 1586-1600
    • Peng, K.1    Broz, P.2    Jones, J.3    Joubert, L.M.4    Monack, D.5
  • 64
    • 26844452231 scopus 로고    scopus 로고
    • Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis
    • Mariathasan, S., Weiss, D. S., Dixit, V. M. and Monack, D. M., Innate immunity against Francisella tularensis is dependent on the ASC/caspase-1 axis. J. Exp. Med. 2005. 202: 1043-1049.
    • (2005) J. Exp. Med. , vol.202 , pp. 1043-1049
    • Mariathasan, S.1    Weiss, D.S.2    Dixit, V.M.3    Monack, D.M.4
  • 65
    • 34748882473 scopus 로고    scopus 로고
    • The Francisella pathogenicity island
    • Nano, F. E. and Schmerk, C., The Francisella pathogenicity island. Ann. NY Acad. Sci. 2007. 1105: 122-137.
    • (2007) Ann. NY Acad. Sci. , vol.1105 , pp. 122-137
    • Nano, F.E.1    Schmerk, C.2
  • 66
    • 77955480358 scopus 로고    scopus 로고
    • Involvement of absent in melanoma 2 in inflammasome activation in macrophages infected with Listeria monocytogenes
    • Tsuchiya, K., Hara, H., Kawamura, I., Nomura, T., Yamamoto, T., Daim, S., Dewamitta, S. R. et al., Involvement of absent in melanoma 2 in inflammasome activation in macrophages infected with Listeria monocytogenes. J. Immunol. 2010. 185: 1186-1195.
    • (2010) J. Immunol. , vol.185 , pp. 1186-1195
    • Tsuchiya, K.1    Hara, H.2    Kawamura, I.3    Nomura, T.4    Yamamoto, T.5    Daim, S.6    Dewamitta, S.R.7
  • 67
    • 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. and Monack, D. M., Type I interferon signaling is required for activation of the inflammasome during Francisella infection. J. Exp. Med. 2007. 204: 987-994.
    • (2007) J. Exp. Med. , vol.204 , pp. 987-994
    • Henry, T.1    Brotcke, A.2    Weiss, D.S.3    Thompson, L.J.4    Monack, D.M.5
  • 68
    • 84900401399 scopus 로고    scopus 로고
    • Type I interferon signaling regulates activation of the absent in melanoma 2 inflammasome during Streptococcus pneumoniae infection
    • Fang, R., Hara, H., Sakai, S., Hernandez-Cuellar, E., Mitsuyama, M., Kawamura, I. and Tsuchiya, K., Type I interferon signaling regulates activation of the absent in melanoma 2 inflammasome during Streptococcus pneumoniae infection. Infect. Immun. 2014. 82: 2310-2317.
    • (2014) Infect. Immun. , vol.82 , pp. 2310-2317
    • Fang, R.1    Hara, H.2    Sakai, S.3    Hernandez-Cuellar, E.4    Mitsuyama, M.5    Kawamura, I.6    Tsuchiya, K.7
  • 69
    • 84925841637 scopus 로고    scopus 로고
    • cGAS and Ifi204 cooperate to produce type I IFNs in response to Francisella infection
    • Storek, K. M., Gertsvolf, N. A., Ohlson, M. B. and Monack, D. M., cGAS and Ifi204 cooperate to produce type I IFNs in response to Francisella infection. J. Immunol. 2015. 194: 3236-3245.
    • (2015) J. Immunol. , vol.194 , pp. 3236-3245
    • Storek, K.M.1    Gertsvolf, N.A.2    Ohlson, M.B.3    Monack, D.M.4
  • 70
    • 84893075305 scopus 로고    scopus 로고
    • Regulation of type I interferon responses
    • Ivashkiv, L. B. and Donlin, L. T., Regulation of type I interferon responses. Nat. Rev. Immunol. 2014. 14: 36-49.
    • (2014) Nat. Rev. Immunol. , vol.14 , pp. 36-49
    • Ivashkiv, L.B.1    Donlin, L.T.2
  • 71
    • 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., Ohshima, J. et al., A cluster of interferon-gamma-inducible p65 GTPases plays a critical role in host defense against Toxoplasma gondii. Immunity 2012. 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    Ohshima, J.7
  • 72
    • 84987837682 scopus 로고    scopus 로고
    • Mitochondrial ROS potentiates indirect activation of the AIM2 inflammasome
    • Crane, D. D., Bauler, T. J., Wehrly, T. D. and Bosio, C. M., Mitochondrial ROS potentiates indirect activation of the AIM2 inflammasome. Front. Microbiol. 2014. 5: 438.
    • (2014) Front. Microbiol. , vol.5 , pp. 438
    • Crane, D.D.1    Bauler, T.J.2    Wehrly, T.D.3    Bosio, C.M.4
  • 73
    • 79960542894 scopus 로고    scopus 로고
    • Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome
    • Bauernfeind, F., Bartok, E., Rieger, A., Franchi, L., Nunez, G. and Hornung, V., Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome. J. Immunol. 2011. 187: 613-617.
    • (2011) J. Immunol. , vol.187 , pp. 613-617
    • Bauernfeind, F.1    Bartok, E.2    Rieger, A.3    Franchi, L.4    Nunez, G.5    Hornung, V.6
  • 74
    • 78149489515 scopus 로고    scopus 로고
    • Deletion of ripA alleviates suppression of the inflammasome and MAPK by Francisella tularensis
    • Huang, M. T., Mortensen, B. L., Taxman, D. J., Craven, R. R., Taft-Benz, S., Kijek, T. M., Fuller, J. R. et al., Deletion of ripA alleviates suppression of the inflammasome and MAPK by Francisella tularensis. J. Immunol. 2010. 185: 5476-5485.
    • (2010) J. Immunol. , vol.185 , pp. 5476-5485
    • Huang, M.T.1    Mortensen, B.L.2    Taxman, D.J.3    Craven, R.R.4    Taft-Benz, S.5    Kijek, T.M.6    Fuller, J.R.7
  • 75
    • 78049394393 scopus 로고    scopus 로고
    • Cutting edge: mutation of Francisella tularensis mviN leads to increased macrophage absent in melanoma 2 inflammasome activation and a loss of virulence
    • Ulland, T. K., Buchan, B. W., Ketterer, M. R., Fernandes-Alnemri, T., Meyerholz, D. K., Apicella, M. A., Alnemri, E. S. et al., Cutting edge: mutation of Francisella tularensis mviN leads to increased macrophage absent in melanoma 2 inflammasome activation and a loss of virulence. J. Immunol. 2010. 185: 2670-2674.
    • (2010) J. Immunol. , vol.185 , pp. 2670-2674
    • Ulland, T.K.1    Buchan, B.W.2    Ketterer, M.R.3    Fernandes-Alnemri, T.4    Meyerholz, D.K.5    Apicella, M.A.6    Alnemri, E.S.7
  • 76
    • 84871886258 scopus 로고    scopus 로고
    • Francisella tularensis live vaccine strain folate metabolism and pseudouridine synthase gene mutants modulate macrophage caspase-1 activation
    • Ulland, T. K., Janowski, A. M., Buchan, B. W., Faron, M., Cassel, S. L., Jones, B. D. and Sutterwala, F. S., Francisella tularensis live vaccine strain folate metabolism and pseudouridine synthase gene mutants modulate macrophage caspase-1 activation. Infect. Immun. 2013. 81: 201-208.
    • (2013) Infect. Immun. , vol.81 , pp. 201-208
    • Ulland, T.K.1    Janowski, A.M.2    Buchan, B.W.3    Faron, M.4    Cassel, S.L.5    Jones, B.D.6    Sutterwala, F.S.7
  • 77
  • 78
    • 84859945146 scopus 로고    scopus 로고
    • Preventing bacterial DNA release and absent in melanoma 2 inflammasome activation by a Legionella effector functioning in membrane trafficking
    • Ge, J., Gong, Y. N., Xu, Y. and Shao, F., Preventing bacterial DNA release and absent in melanoma 2 inflammasome activation by a Legionella effector functioning in membrane trafficking. Proc. Natl. Acad. Sci. USA 2012. 109: 6193-6198.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 6193-6198
    • Ge, J.1    Gong, Y.N.2    Xu, Y.3    Shao, F.4
  • 80
    • 77957228318 scopus 로고    scopus 로고
    • Central roles of NLRs and inflammasomes in viral infection
    • Kanneganti, T. D., Central roles of NLRs and inflammasomes in viral infection. Nat. Rev. Immunol. 2010. 10: 688-698.
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 688-698
    • Kanneganti, T.D.1
  • 83
    • 84896350371 scopus 로고    scopus 로고
    • AIM2 mediates inflammation-associated renal damage in hepatitis B virus-associated glomerulonephritis by regulating caspase-1, IL-1beta, and IL-18
    • Zhen, J., Zhang, L., Pan, J., Ma, S., Yu, X., Li, X., Chen, S. et al., AIM2 mediates inflammation-associated renal damage in hepatitis B virus-associated glomerulonephritis by regulating caspase-1, IL-1beta, and IL-18. Mediators Inflamm. 2014. 2014: 190860.
    • (2014) Mediators Inflamm. , vol.2014 , pp. 190860
    • Zhen, J.1    Zhang, L.2    Pan, J.3    Ma, S.4    Yu, X.5    Li, X.6    Chen, S.7
  • 84
    • 84876335304 scopus 로고    scopus 로고
    • Correlation of AIM2 expression in peripheral blood mononuclear cells from humans with acute and chronic hepatitis B
    • Wu, D. L., Xu, G. H., Lu, S. M., Ma, B. L., Miao, N. Z., Liu, X. B., Cheng, Y. P. et al., Correlation of AIM2 expression in peripheral blood mononuclear cells from humans with acute and chronic hepatitis B. Hum. Immunol. 2013. 74: 514-521.
    • (2013) Hum. Immunol. , vol.74 , pp. 514-521
    • Wu, D.L.1    Xu, G.H.2    Lu, S.M.3    Ma, B.L.4    Miao, N.Z.5    Liu, X.B.6    Cheng, Y.P.7
  • 85
    • 84939516334 scopus 로고    scopus 로고
    • Expression of AIM2 is correlated with increased inflammation in chronic hepatitis B patients
    • Han, Y., Chen, Z., Hou, R., Yan, D., Liu, C., Chen, S., Li, X. et al., Expression of AIM2 is correlated with increased inflammation in chronic hepatitis B patients. Virol. J. 2015. 12: 129.
    • (2015) Virol. J. , vol.12 , pp. 129
    • Han, Y.1    Chen, Z.2    Hou, R.3    Yan, D.4    Liu, C.5    Chen, S.6    Li, X.7
  • 86
    • 84874246480 scopus 로고    scopus 로고
    • Proteasomal degradation of herpes simplex virus capsids in macrophages releases DNA to the cytosol for recognition by DNA sensors
    • Horan, K. A., Hansen, K., Jakobsen, M. R., Holm, C. K., Soby, S., Unterholzner, L., Thompson, M. et al., Proteasomal degradation of herpes simplex virus capsids in macrophages releases DNA to the cytosol for recognition by DNA sensors. J. Immunol. 2013. 190: 2311-2319.
    • (2013) J. Immunol. , vol.190 , pp. 2311-2319
    • Horan, K.A.1    Hansen, K.2    Jakobsen, M.R.3    Holm, C.K.4    Soby, S.5    Unterholzner, L.6    Thompson, M.7
  • 87
  • 90
    • 70349459734 scopus 로고    scopus 로고
    • RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate
    • Ablasser, A., Bauernfeind, F., Hartmann, G., Latz, E., Fitzgerald, K. A. and Hornung, V., RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate. Nat. Immunol. 2009. 10: 1065-1072.
    • (2009) Nat. Immunol. , vol.10 , pp. 1065-1072
    • Ablasser, A.1    Bauernfeind, F.2    Hartmann, G.3    Latz, E.4    Fitzgerald, K.A.5    Hornung, V.6
  • 91
    • 68049092912 scopus 로고    scopus 로고
    • RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway
    • Chiu, Y. H., Macmillan, J. B. and Chen, Z. J., RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway. Cell 2009. 138: 576-591.
    • (2009) Cell , vol.138 , pp. 576-591
    • Chiu, Y.H.1    Macmillan, J.B.2    Chen, Z.J.3
  • 93
    • 84926164932 scopus 로고    scopus 로고
    • Concerted activation of the AIM2 and NLRP3 inflammasomes orchestrates host protection against Aspergillus infection
    • Karki, R., Man, S. M., Malireddi, R. K., Gurung, P., Vogel, P., Lamkanfi, M. and Kanneganti, T. D., Concerted activation of the AIM2 and NLRP3 inflammasomes orchestrates host protection against Aspergillus infection. Cell Host Microbe 2015. 17: 357-368.
    • (2015) Cell Host Microbe , vol.17 , pp. 357-368
    • Karki, R.1    Man, S.M.2    Malireddi, R.K.3    Gurung, P.4    Vogel, P.5    Lamkanfi, M.6    Kanneganti, T.D.7
  • 94
    • 84892552656 scopus 로고    scopus 로고
    • Dual engagement of the NLRP3 and AIM2 inflammasomes by plasmodium-derived hemozoin and DNA during malaria
    • Kalantari, P., DeOliveira, R. B., Chan, J., Corbett, Y., Rathinam, V., Stutz, A., Latz, E. et al., Dual engagement of the NLRP3 and AIM2 inflammasomes by plasmodium-derived hemozoin and DNA during malaria. Cell Rep. 2014. 6: 196-210.
    • (2014) Cell Rep. , vol.6 , pp. 196-210
    • Kalantari, P.1    DeOliveira, R.B.2    Chan, J.3    Corbett, Y.4    Rathinam, V.5    Stutz, A.6    Latz, E.7
  • 95
    • 84934346989 scopus 로고    scopus 로고
    • Critical role for the DNA sensor AIM2 in stem cell proliferation and cancer
    • Man, S. M., Zhu, Q., Zhu, L., Liu, Z., Karki, R., Malik, A., Sharma, D. et al., Critical role for the DNA sensor AIM2 in stem cell proliferation and cancer. Cell 2015. 162: 45-58.
    • (2015) Cell , vol.162 , pp. 45-58
    • Man, S.M.1    Zhu, Q.2    Zhu, L.3    Liu, Z.4    Karki, R.5    Malik, A.6    Sharma, D.7
  • 96
    • 84938996802 scopus 로고    scopus 로고
    • Inflammasome-independent role of AIM2 in suppressing colon tumorigenesis via DNA-PK and Akt
    • Wilson, J. E., Petrucelli, A. S., Chen, L., Koblansky, A. A., Truax, A. D., Oyama, Y., Rogers, A. B. et al., Inflammasome-independent role of AIM2 in suppressing colon tumorigenesis via DNA-PK and Akt. Nat. Med. 2015. 21: 906-913.
    • (2015) Nat. Med. , vol.21 , pp. 906-913
    • Wilson, J.E.1    Petrucelli, A.S.2    Chen, L.3    Koblansky, A.A.4    Truax, A.D.5    Oyama, Y.6    Rogers, A.B.7
  • 97
    • 0030775488 scopus 로고    scopus 로고
    • Cloning a novel member of the human interferon-inducible gene family associated with control of tumorigenicity in a model of human melanoma
    • DeYoung, K. L., Ray, M. E., Su, Y. A., Anzick, S. L., Johnstone, R. W., Trapani, J. A., Meltzer, P. S. et al., Cloning a novel member of the human interferon-inducible gene family associated with control of tumorigenicity in a model of human melanoma. Oncogene 1997. 15: 453-457.
    • (1997) Oncogene , vol.15 , pp. 453-457
    • DeYoung, K.L.1    Ray, M.E.2    Su, Y.A.3    Anzick, S.L.4    Johnstone, R.W.5    Trapani, J.A.6    Meltzer, P.S.7
  • 98
    • 84909945799 scopus 로고    scopus 로고
    • Lack of absent in Melanoma 2 (AIM2) expression in tumor cells is closely associated with poor survival in colorectal cancer patients
    • Dihlmann, S., Tao, S., Echterdiek, F., Herpel, E., Jansen, L., Chang-Claude, J., Brenner, H. et al., Lack of absent in Melanoma 2 (AIM2) expression in tumor cells is closely associated with poor survival in colorectal cancer patients. Int. J. Cancer 2014. 135: 2387-2396.
    • (2014) Int. J. Cancer , vol.135 , pp. 2387-2396
    • Dihlmann, S.1    Tao, S.2    Echterdiek, F.3    Herpel, E.4    Jansen, L.5    Chang-Claude, J.6    Brenner, H.7
  • 100
    • 35349011610 scopus 로고    scopus 로고
    • The putative tumor suppressor AIM2 is frequently affected by different genetic alterations in microsatellite unstable colon cancers
    • Woerner, S. M., Kloor, M., Schwitalle, Y., Youmans, H., Doeberitz, M., Gebert, J. and Dihlmann, S., The putative tumor suppressor AIM2 is frequently affected by different genetic alterations in microsatellite unstable colon cancers. Genes Chromosomes Cancer 2007. 46: 1080-1089.
    • (2007) Genes Chromosomes Cancer , vol.46 , pp. 1080-1089
    • Woerner, S.M.1    Kloor, M.2    Schwitalle, Y.3    Youmans, H.4    Doeberitz, M.5    Gebert, J.6    Dihlmann, S.7
  • 101
    • 84887924524 scopus 로고    scopus 로고
    • The landscape of microsatellite instability in colorectal and endometrial cancer genomes
    • Kim, T. M., Laird, P. W. and Park, P. J., The landscape of microsatellite instability in colorectal and endometrial cancer genomes. Cell 2013. 155: 858-868.
    • (2013) Cell , vol.155 , pp. 858-868
    • Kim, T.M.1    Laird, P.W.2    Park, P.J.3
  • 102
    • 84886384437 scopus 로고    scopus 로고
    • AIM2, an IFN-inducible cytosolic DNA sensor, in the development of benign prostate hyperplasia and prostate cancer
    • Ponomareva, L., Liu, H., Duan, X., Dickerson, E., Shen, H., Panchanathan, R. and Choubey, D., AIM2, an IFN-inducible cytosolic DNA sensor, in the development of benign prostate hyperplasia and prostate cancer. Mol. Cancer Res. 2013. 11: 1193-1202.
    • (2013) Mol. Cancer Res. , vol.11 , pp. 1193-1202
    • Ponomareva, L.1    Liu, H.2    Duan, X.3    Dickerson, E.4    Shen, H.5    Panchanathan, R.6    Choubey, D.7
  • 103
    • 84869219269 scopus 로고    scopus 로고
    • Interactome-wide analysis identifies end-binding protein 1 as a crucial component for the speck-like particle formation of activated absence in melanoma 2 (AIM2) inflammasomes
    • Wang, L. J., Hsu, C. W., Chen, C. C., Liang, Y., Chen, L. C., Ojcius, D. M., Tsang, N. M. et al., Interactome-wide analysis identifies end-binding protein 1 as a crucial component for the speck-like particle formation of activated absence in melanoma 2 (AIM2) inflammasomes. Mol. Cell. Proteomics 2012. 11: 1230-1244.
    • (2012) Mol. Cell. Proteomics , vol.11 , pp. 1230-1244
    • Wang, L.J.1    Hsu, C.W.2    Chen, C.C.3    Liang, Y.4    Chen, L.C.5    Ojcius, D.M.6    Tsang, N.M.7
  • 104
    • 84872402053 scopus 로고    scopus 로고
    • Tumour inflammasome-derived IL-1beta recruits neutrophils and improves local recurrence-free survival in EBV-induced nasopharyngeal carcinoma
    • Chen, L. C., Wang, L. J., Tsang, N. M., Ojcius, D. M., Chen, C. C., Ouyang, C. N., Hsueh, C. et al., Tumour inflammasome-derived IL-1beta recruits neutrophils and improves local recurrence-free survival in EBV-induced nasopharyngeal carcinoma. EMBO Mol. Med. 2012. 4: 1276-1293.
    • (2012) EMBO Mol. Med. , vol.4 , pp. 1276-1293
    • Chen, L.C.1    Wang, L.J.2    Tsang, N.M.3    Ojcius, D.M.4    Chen, C.C.5    Ouyang, C.N.6    Hsueh, C.7
  • 105
    • 84859007742 scopus 로고    scopus 로고
    • Overexpression of the DNA sensor proteins, absent in melanoma 2 and interferon-inducible 16, contributes to tumorigenesis of oral squamous cell carcinoma with p53 inactivation
    • Kondo, Y., Nagai, K., Nakahata, S., Saito, Y., Ichikawa, T., Suekane, A., Taki, T. et al., Overexpression of the DNA sensor proteins, absent in melanoma 2 and interferon-inducible 16, contributes to tumorigenesis of oral squamous cell carcinoma with p53 inactivation. Cancer Sci. 2012. 103: 782-790.
    • (2012) Cancer Sci. , vol.103 , pp. 782-790
    • Kondo, Y.1    Nagai, K.2    Nakahata, S.3    Saito, Y.4    Ichikawa, T.5    Suekane, A.6    Taki, T.7
  • 106
    • 84944278525 scopus 로고    scopus 로고
    • Differential expression of inflammasomes in lung cancer cell lines and tissues
    • Kong, H., Wang, Y., Zeng, X., Wang, Z., Wang, H. and Xie, W., Differential expression of inflammasomes in lung cancer cell lines and tissues. Tumour Biol. 2015. 36: 7501-7513.
    • (2015) Tumour Biol. , vol.36 , pp. 7501-7513
    • Kong, H.1    Wang, Y.2    Zeng, X.3    Wang, Z.4    Wang, H.5    Xie, W.6
  • 107
    • 77949892176 scopus 로고    scopus 로고
    • Restoration of absent in melanoma 2 (AIM2) induces G2/M cell cycle arrest and promotes invasion of colorectal cancer cells
    • Patsos, G., Germann, A., Gebert, J. and Dihlmann, S., Restoration of absent in melanoma 2 (AIM2) induces G2/M cell cycle arrest and promotes invasion of colorectal cancer cells. Int. J. Cancer 2010. 126: 1838-1849.
    • (2010) Int. J. Cancer , vol.126 , pp. 1838-1849
    • Patsos, G.1    Germann, A.2    Gebert, J.3    Dihlmann, S.4
  • 108
    • 4644359805 scopus 로고    scopus 로고
    • Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase
    • Feng, J., Park, J., Cron, P., Hess, D. and Hemmings, B. A., Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase. J. Biol. Chem. 2004. 279: 41189-41196.
    • (2004) J. Biol. Chem. , vol.279 , pp. 41189-41196
    • Feng, J.1    Park, J.2    Cron, P.3    Hess, D.4    Hemmings, B.A.5
  • 109
    • 33747356750 scopus 로고    scopus 로고
    • Protein kinase Cepsilon activates protein kinase B/Akt via DNA-PK to protect against tumor necrosis factor-alpha-induced cell death
    • Lu, D., Huang, J. and Basu, A., Protein kinase Cepsilon activates protein kinase B/Akt via DNA-PK to protect against tumor necrosis factor-alpha-induced cell death. J. Biol. Chem. 2006. 281: 22799-22807.
    • (2006) J. Biol. Chem. , vol.281 , pp. 22799-22807
    • Lu, D.1    Huang, J.2    Basu, A.3
  • 111
    • 84925581290 scopus 로고    scopus 로고
    • Sex-dependent differential activation of NLRP3 and AIM2 inflammasomes in SLE macrophages
    • Yang, C. A., Huang, S. T. and Chiang, B. L., Sex-dependent differential activation of NLRP3 and AIM2 inflammasomes in SLE macrophages. Rheumatology 2015. 54: 324-331.
    • (2015) Rheumatology , vol.54 , pp. 324-331
    • Yang, C.A.1    Huang, S.T.2    Chiang, B.L.3
  • 112
    • 70349503643 scopus 로고    scopus 로고
    • Expression profile of HIN200 in leukocytes and renal biopsy of SLE patients by real-time RT-PCR
    • Kimkong, I., Avihingsanon, Y. and Hirankarn, N., Expression profile of HIN200 in leukocytes and renal biopsy of SLE patients by real-time RT-PCR. Lupus 2009. 18: 1066-1072.
    • (2009) Lupus , vol.18 , pp. 1066-1072
    • Kimkong, I.1    Avihingsanon, Y.2    Hirankarn, N.3
  • 114
  • 115
  • 116
    • 84908238878 scopus 로고    scopus 로고
    • Both bone marrow-derived and non-bone marrow-derived cells contribute to AIM2 and NLRP3 inflammasome activation in a MyD88-dependent manner in dietary steatohepatitis
    • Csak, T., Pillai, A., Ganz, M., Lippai, D., Petrasek, J., Park, J. K., Kodys, K. et al., Both bone marrow-derived and non-bone marrow-derived cells contribute to AIM2 and NLRP3 inflammasome activation in a MyD88-dependent manner in dietary steatohepatitis. Liver Int. 2014. 34: 1402-1413.
    • (2014) Liver Int. , vol.34 , pp. 1402-1413
    • Csak, T.1    Pillai, A.2    Ganz, M.3    Lippai, D.4    Petrasek, J.5    Park, J.K.6    Kodys, K.7
  • 119
    • 0035947178 scopus 로고    scopus 로고
    • Requirement of DNase II for definitive erythropoiesis in the mouse fetal liver
    • Kawane, K., Fukuyama, H., Kondoh, G., Takeda, J., Ohsawa, Y., Uchiyama, Y. and Nagata, S., Requirement of DNase II for definitive erythropoiesis in the mouse fetal liver. Science 2001. 292: 1546-1549.
    • (2001) Science , vol.292 , pp. 1546-1549
    • Kawane, K.1    Fukuyama, H.2    Kondoh, G.3    Takeda, J.4    Ohsawa, Y.5    Uchiyama, Y.6    Nagata, S.7
  • 120
    • 12344290452 scopus 로고    scopus 로고
    • Lethal anemia caused by interferon-beta produced in mouse embryos carrying undigested DNA
    • Yoshida, H., Okabe, Y., Kawane, K., Fukuyama, H. and Nagata, S., Lethal anemia caused by interferon-beta produced in mouse embryos carrying undigested DNA. Nat. Immunol. 2005. 6: 49-56.
    • (2005) Nat. Immunol. , vol.6 , pp. 49-56
    • Yoshida, H.1    Okabe, Y.2    Kawane, K.3    Fukuyama, H.4    Nagata, S.5
  • 121
    • 33750465224 scopus 로고    scopus 로고
    • Chronic polyarthritis caused by mammalian DNA that escapes from degradation in macrophages
    • Kawane, K., Ohtani, M., Miwa, K., Kizawa, T., Kanbara, Y., Yoshioka, Y., Yoshikawa, H. et al., Chronic polyarthritis caused by mammalian DNA that escapes from degradation in macrophages. Nature 2006. 443: 998-1002.
    • (2006) Nature , vol.443 , pp. 998-1002
    • Kawane, K.1    Ohtani, M.2    Miwa, K.3    Kizawa, T.4    Kanbara, Y.5    Yoshioka, Y.6    Yoshikawa, H.7
  • 122
    • 84921478452 scopus 로고    scopus 로고
    • Cutting edge: AIM2 and endosomal TLRs differentially regulate arthritis and autoantibody production in DNase II-deficient mice
    • Baum, R., Sharma, S., Carpenter, S., Li, Q. Z., Busto, P., Fitzgerald, K. A., Marshak-Rothstein, A. et al., Cutting edge: AIM2 and endosomal TLRs differentially regulate arthritis and autoantibody production in DNase II-deficient mice. J. Immunol. 2015. 194: 873-877.
    • (2015) J. Immunol. , vol.194 , pp. 873-877
    • Baum, R.1    Sharma, S.2    Carpenter, S.3    Li, Q.Z.4    Busto, P.5    Fitzgerald, K.A.6    Marshak-Rothstein, A.7
  • 123
    • 84938515167 scopus 로고    scopus 로고
    • AIM2 drives joint inflammation in a self-DNA triggered model of chronic polyarthritis
    • Jakobs, C., Perner, S. and Hornung, V., AIM2 drives joint inflammation in a self-DNA triggered model of chronic polyarthritis. PLoS One 2015. 10: e0131702.
    • (2015) PLoS One , vol.10 , pp. e0131702
    • Jakobs, C.1    Perner, S.2    Hornung, V.3
  • 124
    • 84885157623 scopus 로고    scopus 로고
    • Synthetic oligodeoxynucleotides containing suppressive TTAGGG motifs inhibit AIM2 inflammasome activation
    • Kaminski, J. J., Schattgen, S. A., Tzeng, T. C., Bode, C., Klinman, D. M. and Fitzgerald, K. A., Synthetic oligodeoxynucleotides containing suppressive TTAGGG motifs inhibit AIM2 inflammasome activation. J. Immunol. 2013. 191: 3876-3883.
    • (2013) J. Immunol. , vol.191 , pp. 3876-3883
    • Kaminski, J.J.1    Schattgen, S.A.2    Tzeng, T.C.3    Bode, C.4    Klinman, D.M.5    Fitzgerald, K.A.6


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