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Volumn 33, Issue 8, 2019, Pages 8865-8877

Severe acute respiratory syndrome Coronavirus ORF3a protein activates the NLRP3 inflammasome by promoting TRAF3-dependent ubiquitination of ASC

Author keywords

SARS Coronavirus

Indexed keywords

APOPTOSIS-ASSOCIATED SPECK LIKE PROTEIN CONTAINING A CASPASE RECRUITMENT DOMAIN; BETA TUBULIN; CANAKINUMAB; CAVEOLIN; CRISPR ASSOCIATED ENDONUCLEASE CAS9; CRYOPYRIN; DEUBIQUITINASE; GUIDE RNA; HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INFLAMMASOME; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; ION CHANNEL; LAMIN A; LAMIN C; MESSENGER RNA; OPEN READING FRAME 3A PROTEIN; PROCASPASE 1; PROTEIN P50; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 3; UNCLASSIFIED DRUG; VIRAL PROTEIN; CASPASE RECRUITMENT DOMAIN SIGNALING PROTEIN; NLRP3 PROTEIN, HUMAN; ORF3A PROTEIN, SARS CORONAVIRUS; PYCARD PROTEIN, HUMAN; TRAF3 PROTEIN, HUMAN;

EID: 85070788848     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.201802418R     Document Type: Article
Times cited : (410)

References (69)
  • 1
    • 84959851955 scopus 로고    scopus 로고
    • Middle East respiratory syndrome Coronavirus: another zoonotic betacoronavirus causing SARS-like disease
    • Chan, J. F., Lau, S. K., To, K. K., Cheng, V. C., Woo, P. C., and Yuen, K. Y. (2015) Middle East respiratory syndrome Coronavirus: another zoonotic betacoronavirus causing SARS-like disease. Clin. Microbiol. Rev. 28, 465–522
    • (2015) Clin. Microbiol. Rev. , vol.28 , pp. 465-522
    • Chan, J.F.1    Lau, S.K.2    To, K.K.3    Cheng, V.C.4    Woo, P.C.5    Yuen, K.Y.6
  • 2
    • 20944452287 scopus 로고    scopus 로고
    • Comparative host gene transcription by microarray analysis early after infection of the Huh7 cell line by severe acute respiratory syndrome Coronavirus and human Coronavirus 229E
    • Tang, B. S., Chan, K. H., Cheng, V. C., Woo, P. C., Lau, S. K., Lam, C. C., Chan, T. L., Wu, A. K., Hung, I. F., Leung, S. Y., and Yuen, K. Y. (2005) Comparative host gene transcription by microarray analysis early after infection of the Huh7 cell line by severe acute respiratory syndrome Coronavirus and human Coronavirus 229E. J. Virol. 79, 6180–6193
    • (2005) J. Virol. , vol.79 , pp. 6180-6193
    • Tang, B.S.1    Chan, K.H.2    Cheng, V.C.3    Woo, P.C.4    Lau, S.K.5    Lam, C.C.6    Chan, T.L.7    Wu, A.K.8    Hung, I.F.9    Leung, S.Y.10    Yuen, K.Y.11
  • 3
    • 34548389337 scopus 로고    scopus 로고
    • Functional genomics highlights differential induction of antiviral pathways in the lungs of SARS-CoV-infected macaques
    • De Lang, A., Baas, T., Teal, T., Leijten, L. M., Rain, B., Osterhaus, A. D., Haagmans, B. L., and Katze, M. G. (2007) Functional genomics highlights differential induction of antiviral pathways in the lungs of SARS-CoV-infected macaques. PLoS Pathog. 3, e112
    • (2007) PLoS Pathog. , vol.3
    • De Lang, A.1    Baas, T.2    Teal, T.3    Leijten, L.M.4    Rain, B.5    Osterhaus, A.D.6    Haagmans, B.L.7    Katze, M.G.8
  • 4
    • 84976516826 scopus 로고    scopus 로고
    • Inflammasomes: mechanism of assembly, regulation and signalling
    • Broz, P., and Dixit, V. M. (2016) Inflammasomes: mechanism of assembly, regulation and signalling. Nat. Rev. Immunol. 16, 407–420
    • (2016) Nat. Rev. Immunol. , vol.16 , pp. 407-420
    • Broz, P.1    Dixit, V.M.2
  • 5
    • 1642285783 scopus 로고    scopus 로고
    • NALP3 forms an IL-1β-processing inflammasome with increased activity in Muckle-Wells auto-inflammatory disorder
    • Agostini, L., Martinon, F., Burns, K., McDermott, M. F., Hawkins, P. N., and Tschopp, J. (2004) NALP3 forms an IL-1β-processing inflammasome with increased activity in Muckle-Wells auto-inflammatory disorder. Immunity 20, 319–325
    • (2004) Immunity , vol.20 , pp. 319-325
    • Agostini, L.1    Martinon, F.2    Burns, K.3    McDermott, M.F.4    Hawkins, P.N.5    Tschopp, J.6
  • 6
    • 84927779736 scopus 로고    scopus 로고
    • NLRP3 at the interface of metabolism and inflammation
    • Haneklaus, M., and O'Neill, L. A. (2015) NLRP3 at the interface of metabolism and inflammation. Immunol. Rev. 265, 53–62
    • (2015) Immunol. Rev. , vol.265 , pp. 53-62
    • Haneklaus, M.1    O'Neill, L.A.2
  • 7
    • 84866307663 scopus 로고    scopus 로고
    • Inflammasomes and viruses: cellular defence versus viral offence
    • Gram, A. M., Frenkel, J., and Ressing, M. E. (2012) Inflammasomes and viruses: cellular defence versus viral offence. J. Gen. Virol. 93, 2063–2075
    • (2012) J. Gen. Virol. , vol.93 , pp. 2063-2075
    • Gram, A.M.1    Frenkel, J.2    Ressing, M.E.3
  • 8
    • 84967189059 scopus 로고    scopus 로고
    • Evasion and interference: intracellular pathogens modulate caspase-dependent inflammatory responses
    • Stewart, M. K., and Cookson, B. T. (2016) Evasion and interference: intracellular pathogens modulate caspase-dependent inflammatory responses. Nat. Rev. Microbiol. 14, 346–359
    • (2016) Nat. Rev. Microbiol. , vol.14 , pp. 346-359
    • Stewart, M.K.1    Cookson, B.T.2
  • 9
    • 77951295418 scopus 로고    scopus 로고
    • Influenza virus activates inflammasomes via its intracellular M2 ion channel
    • Ichinohe, T., Pang, I. K., and Iwasaki, A. (2010) Influenza virus activates inflammasomes via its intracellular M2 ion channel. Nat. Immunol. 11, 404–410
    • (2010) Nat. Immunol. , vol.11 , pp. 404-410
    • Ichinohe, T.1    Pang, I.K.2    Iwasaki, A.3
  • 10
    • 84866156921 scopus 로고    scopus 로고
    • Encephalomyocarditis virus viroporin 2B activates NLRP3 inflammasome
    • Ito, M., Yanagi, Y., and Ichinohe, T. (2012) Encephalomyocarditis virus viroporin 2B activates NLRP3 inflammasome. PLoS Pathog. 8, e1002857
    • (2012) PLoS Pathog. , vol.8
    • Ito, M.1    Yanagi, Y.2    Ichinohe, T.3
  • 11
    • 84936980740 scopus 로고    scopus 로고
    • NLRP3 inflammasome activation by viroporins of animal viruses
    • Guo, H. C., Jin, Y., Zhi, X. Y., Yan, D., and Sun, S. Q. (2015) NLRP3 inflammasome activation by viroporins of animal viruses. Viruses 7, 3380–3391
    • (2015) Viruses , vol.7 , pp. 3380-3391
    • Guo, H.C.1    Jin, Y.2    Zhi, X.Y.3    Yan, D.4    Sun, S.Q.5
  • 14
    • 33747617366 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome-associated Coronavirus 3a protein forms an ion channel and modulates virus release
    • Lu, W., Zheng, B. J., Xu, K., Schwarz, W., Du, L., Wong, C. K., Chen, J., Duan, S., Deubel, V., and Sun, B. (2006) Severe acute respiratory syndrome-associated Coronavirus 3a protein forms an ion channel and modulates virus release. Proc. Natl. Acad. Sci. USA 103, 12540–12545
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 12540-12545
    • Lu, W.1    Zheng, B.J.2    Xu, K.3    Schwarz, W.4    Du, L.5    Wong, C.K.6    Chen, J.7    Duan, S.8    Deubel, V.9    Sun, B.10
  • 18
    • 84922377563 scopus 로고    scopus 로고
    • The SARS Coronavirus 3a protein binds calcium in its cytoplasmic domain
    • Minakshi, R., Padhan, K., Rehman, S., Hassan, M. I., and Ahmad, F. (2014) The SARS Coronavirus 3a protein binds calcium in its cytoplasmic domain. Virus Res. 191, 180–183
    • (2014) Virus Res. , vol.191 , pp. 180-183
    • Minakshi, R.1    Padhan, K.2    Rehman, S.3    Hassan, M.I.4    Ahmad, F.5
  • 19
    • 33748467621 scopus 로고    scopus 로고
    • Understanding the accessory viral proteins unique to the severe acute respiratory syndrome (SARS) Coronavirus
    • Tan, Y. J., Lim, S. G., and Hong, W. (2006) Understanding the accessory viral proteins unique to the severe acute respiratory syndrome (SARS) Coronavirus. Antiviral Res. 72, 78–88
    • (2006) Antiviral Res. , vol.72 , pp. 78-88
    • Tan, Y.J.1    Lim, S.G.2    Hong, W.3
  • 20
    • 40649114761 scopus 로고    scopus 로고
    • SARS Coronavirus accessory proteins
    • Narayanan, K., Huang, C., and Makino, S. (2008) SARS Coronavirus accessory proteins. Virus Res. 133, 113–121
    • (2008) Virus Res. , vol.133 , pp. 113-121
    • Narayanan, K.1    Huang, C.2    Makino, S.3
  • 21
    • 27744472746 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome Coronavirus group-specific open reading frames encode nonessential functions for replication in cell cultures and mice
    • Yount, B., Roberts, R. S., Sims, A. C., Deming, D., Frieman, M. B., Sparks, J., Denison, M. R., Davis, N., and Baric, R. S. (2005) Severe acute respiratory syndrome Coronavirus group-specific open reading frames encode nonessential functions for replication in cell cultures and mice. J. Virol. 79, 14909–14922
    • (2005) J. Virol. , vol.79 , pp. 14909-14922
    • Yount, B.1    Roberts, R.S.2    Sims, A.C.3    Deming, D.4    Frieman, M.B.5    Sparks, J.6    Denison, M.R.7    Davis, N.8    Baric, R.S.9
  • 22
    • 77949519531 scopus 로고    scopus 로고
    • The SARS Coronavirus 3a protein causes endoplasmic reticulum stress and induces ligand-independent downregulation of the type 1 interferon receptor
    • Minakshi, R., Padhan, K., Rani, M., Khan, N., Ahmad, F., and Jameel, S. (2009) The SARS Coronavirus 3a protein causes endoplasmic reticulum stress and induces ligand-independent downregulation of the type 1 interferon receptor. PLoS One 4, e8342
    • (2009) PLoS One , vol.4
    • Minakshi, R.1    Padhan, K.2    Rani, M.3    Khan, N.4    Ahmad, F.5    Jameel, S.6
  • 25
    • 33144477169 scopus 로고    scopus 로고
    • Glycosylation of the severe acute respiratory syndrome Coronavirus triple-spanning membrane proteins 3a and M
    • Oostra, M., de Haan, C. A., de Groot, R. J., and Rottier, P. J. (2006) Glycosylation of the severe acute respiratory syndrome Coronavirus triple-spanning membrane proteins 3a and M. J. Virol. 80, 2326–2336
    • (2006) J. Virol. , vol.80 , pp. 2326-2336
    • Oostra, M.1    de Haan, C.A.2    de Groot, R.J.3    Rottier, P.J.4
  • 27
    • 22544483250 scopus 로고    scopus 로고
    • The severe acute respiratory syndrome Coronavirus 3a protein up-regulates expression of fibrinogen in lung epithelial cells
    • Tan, Y. J., Tham, P. Y., Chan, D. Z., Chou, C. F., Shen, S., Fielding, B. C., Tan, T. H., Lim, S. G., and Hong, W. (2005) The severe acute respiratory syndrome Coronavirus 3a protein up-regulates expression of fibrinogen in lung epithelial cells. J. Virol. 79, 10083–10087
    • (2005) J. Virol. , vol.79 , pp. 10083-10087
    • Tan, Y.J.1    Tham, P.Y.2    Chan, D.Z.3    Chou, C.F.4    Shen, S.5    Fielding, B.C.6    Tan, T.H.7    Lim, S.G.8    Hong, W.9
  • 30
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • erratum 475, 122
    • Zhou, R., Yazdi, A. S., Menu, P., and Tschopp, J. (2011) A role for mitochondria in NLRP3 inflammasome activation. Nature 469, 221–225; erratum: 475, 122
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 31
    • 18144368948 scopus 로고    scopus 로고
    • Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase γ-dependent phosphorylation
    • Reiley, W., Zhang, M., Wu, X., Granger, E., and Sun, S. C. (2005) Regulation of the deubiquitinating enzyme CYLD by IkappaB kinase γ-dependent phosphorylation. Mol. Cell. Biol. 25, 3886–3895
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3886-3895
    • Reiley, W.1    Zhang, M.2    Wu, X.3    Granger, E.4    Sun, S.C.5
  • 32
    • 70350004240 scopus 로고    scopus 로고
    • Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3
    • Zeng, W., Xu, M., Liu, S., Sun, L., and Chen, Z. J. (2009) Key role of Ubc5 and lysine-63 polyubiquitination in viral activation of IRF3. Mol. Cell 36, 315–325
    • (2009) Mol. Cell , vol.36 , pp. 315-325
    • Zeng, W.1    Xu, M.2    Liu, S.3    Sun, L.4    Chen, Z.J.5
  • 33
    • 67650230347 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome Coronavirus M protein inhibits type I interferon production by impeding the formation of TRAF3.TANK.TBK1/IKKepsilon complex
    • Siu, K. L., Kok, K. H., Ng, M. H., Poon, V. K., Yuen, K. Y., Zheng, B. J., and Jin, D. Y. (2009) Severe acute respiratory syndrome Coronavirus M protein inhibits type I interferon production by impeding the formation of TRAF3.TANK.TBK1/IKKepsilon complex. J. Biol. Chem. 284, 16202–16209
    • (2009) J. Biol. Chem. , vol.284 , pp. 16202-16209
    • Siu, K.L.1    Kok, K.H.2    Ng, M.H.3    Poon, V.K.4    Yuen, K.Y.5    Zheng, B.J.6    Jin, D.Y.7
  • 34
    • 84895546659 scopus 로고    scopus 로고
    • Suppression of innate antiviral response by severe acute respiratory syndrome Coronavirus M protein is mediated through the first transmembrane domain
    • Siu, K. L., Chan, C. P., Kok, K. H., Chiu-Yat Woo, P., and Jin, D. Y. (2014) Suppression of innate antiviral response by severe acute respiratory syndrome Coronavirus M protein is mediated through the first transmembrane domain. Cell. Mol. Immunol. 11, 141–149
    • (2014) Cell. Mol. Immunol. , vol.11 , pp. 141-149
    • Siu, K.L.1    Chan, C.P.2    Kok, K.H.3    Chiu-Yat Woo, P.4    Jin, D.Y.5
  • 35
    • 85003938202 scopus 로고    scopus 로고
    • Middle East respiratory syndrome Coronavirus M protein suppresses type I interferon expression through the inhibition of TBK1-dependent phosphorylation of IRF3
    • Lui, P. Y., Wong, L. Y., Fung, C. L., Siu, K. L., Yeung, M. L., Yuen, K. S., Chan, C. P., Woo, P. C., Yuen, K. Y., and Jin, D. Y. (2016) Middle East respiratory syndrome Coronavirus M protein suppresses type I interferon expression through the inhibition of TBK1-dependent phosphorylation of IRF3. Emerg. Microbes Infect. 5, e39
    • (2016) Emerg. Microbes Infect. , vol.5
    • Lui, P.Y.1    Wong, L.Y.2    Fung, C.L.3    Siu, K.L.4    Yeung, M.L.5    Yuen, K.S.6    Chan, C.P.7    Woo, P.C.8    Yuen, K.Y.9    Jin, D.Y.10
  • 36
    • 0033595143 scopus 로고    scopus 로고
    • The zinc finger protein A20 interacts with a novel anti-apoptotic protein which is cleaved by specific caspases
    • De Valck, D., Jin, D. Y., Heyninck, K., Van de Craen, M., Contreras, R., Fiers, W., Jeang, K. T., and Beyaert, R. (1999) The zinc finger protein A20 interacts with a novel anti-apoptotic protein which is cleaved by specific caspases. Oncogene 18, 4182–4190
    • (1999) Oncogene , vol.18 , pp. 4182-4190
    • De Valck, D.1    Jin, D.Y.2    Heyninck, K.3    Van de Craen, M.4    Contreras, R.5    Fiers, W.6    Jeang, K.T.7    Beyaert, R.8
  • 37
    • 58149286561 scopus 로고    scopus 로고
    • Activation of TORC1 transcriptional coactivator through MEKK1-induced phosphorylation
    • Siu, Y. T., Ching, Y. P., and Jin, D. Y (2008) Activation of TORC1 transcriptional coactivator through MEKK1-induced phosphorylation. Mol. Biol. Cell 19, 4750–4761
    • (2008) Mol. Biol. Cell , vol.19 , pp. 4750-4761
    • Siu, Y.T.1    Ching, Y.P.2    Jin, D.Y.3
  • 38
    • 83755195759 scopus 로고    scopus 로고
    • MIP-T3 is a negative regulator of innate type I IFN response
    • Ng, M. H., Ho, T. H., Kok, K. H., Siu, K. L., Li, J., and Jin, D. Y. (2011) MIP-T3 is a negative regulator of innate type I IFN response. J. Immunol. 187, 6473–6482
    • (2011) J. Immunol. , vol.187 , pp. 6473-6482
    • Ng, M.H.1    Ho, T.H.2    Kok, K.H.3    Siu, K.L.4    Li, J.5    Jin, D.Y.6
  • 39
    • 84946887449 scopus 로고    scopus 로고
    • Suppression of type I and type III IFN signalling by NSs protein of severe fever with thrombocytopenia syndrome virus through inhibition of STAT1 phosphorylation and activation
    • Chaudhary, V., Zhang, S., Yuen, K. S., Li, C., Lui, P. Y., Fung, S. Y., Wang, P. H., Chan, C. P., Li, D., Kok, K. H., Liang, M., and Jin, D. Y. (2015) Suppression of type I and type III IFN signalling by NSs protein of severe fever with thrombocytopenia syndrome virus through inhibition of STAT1 phosphorylation and activation. J. Gen. Virol. 96, 3204–3211
    • (2015) J. Gen. Virol. , vol.96 , pp. 3204-3211
    • Chaudhary, V.1    Zhang, S.2    Yuen, K.S.3    Li, C.4    Lui, P.Y.5    Fung, S.Y.6    Wang, P.H.7    Chan, C.P.8    Li, D.9    Kok, K.H.10    Liang, M.11    Jin, D.Y.12
  • 40
    • 85028004515 scopus 로고    scopus 로고
    • PACT facilitates RNA-induced activation of MDA5 by promoting MDA5 oligomerization
    • Lui, P. Y., Wong, L. R., Ho, T. H., Au, S. W. N., Chan, C. P., Kok, K. H., and Jin, D. Y. (2017) PACT facilitates RNA-induced activation of MDA5 by promoting MDA5 oligomerization. J. Immunol. 199, 1846–1855
    • (2017) J. Immunol. , vol.199 , pp. 1846-1855
    • Lui, P.Y.1    Wong, L.R.2    Ho, T.H.3    Au, S.W.N.4    Chan, C.P.5    Kok, K.H.6    Jin, D.Y.7
  • 41
    • 84962781992 scopus 로고    scopus 로고
    • β-TrCP-mediated ubiquitination and degradation of liver-enriched transcription factor CREB-H
    • Cheng, Y., Gao, W. W., Tang, H. M., Deng, J. J., Wong, C. M., Chan, C. P., and Jin, D. Y. (2016) β-TrCP-mediated ubiquitination and degradation of liver-enriched transcription factor CREB-H. Sci. Rep. 6, 23938
    • (2016) Sci. Rep. , vol.6 , pp. 23938
    • Cheng, Y.1    Gao, W.W.2    Tang, H.M.3    Deng, J.J.4    Wong, C.M.5    Chan, C.P.6    Jin, D.Y.7
  • 42
    • 84878553478 scopus 로고    scopus 로고
    • Complete protection against severe acute respiratory syndrome coronavirus-mediated lethal respiratory disease in aged mice by immunization with a mouse-adapted virus lacking E protein
    • Fett, C., DeDiego, M. L., Regla-Nava, J. A., Enjuanes, L., and Perlman, S. (2013) Complete protection against severe acute respiratory syndrome coronavirus-mediated lethal respiratory disease in aged mice by immunization with a mouse-adapted virus lacking E protein. J. Virol. 87, 6551–6559
    • (2013) J. Virol. , vol.87 , pp. 6551-6559
    • Fett, C.1    DeDiego, M.L.2    Regla-Nava, J.A.3    Enjuanes, L.4    Perlman, S.5
  • 47
    • 85050865853 scopus 로고    scopus 로고
    • Antiviral activity of double-stranded RNA-binding protein PACT against influenza A virus mediated via suppression of viral RNA polymerase
    • Chan, C. P., Yuen, C. K., Cheung, P. H., Fung, S. Y., Lui, P. Y., Chen, H., Kok, K. H., and Jin, D. Y. (2018) Antiviral activity of double-stranded RNA-binding protein PACT against influenza A virus mediated via suppression of viral RNA polymerase. FASEB J. 32, 4380–4393
    • (2018) FASEB J. , vol.32 , pp. 4380-4393
    • Chan, C.P.1    Yuen, C.K.2    Cheung, P.H.3    Fung, S.Y.4    Lui, P.Y.5    Chen, H.6    Kok, K.H.7    Jin, D.Y.8
  • 50
    • 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. (2013) Synthetic oligodeoxynucleotides containing suppressive TTAGGG motifs inhibit AIM2 inflammasome activation. J. Immunol. 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
  • 51
    • 85033380926 scopus 로고    scopus 로고
    • Recent advances in inflammasome biology
    • Place, D. E., and Kanneganti, T. D. (2018) Recent advances in inflammasome biology. Curr. Opin. Immunol. 50, 32–38
    • (2018) Curr. Opin. Immunol. , vol.50 , pp. 32-38
    • Place, D.E.1    Kanneganti, T.D.2
  • 54
    • 80051987703 scopus 로고    scopus 로고
    • Crosstalk in NF-κB signaling pathways
    • Oeckinghaus, A., Hayden, M. S., and Ghosh, S. (2011) Crosstalk in NF-κB signaling pathways. Nat. Immunol. 12, 695–708
    • (2011) Nat. Immunol. , vol.12 , pp. 695-708
    • Oeckinghaus, A.1    Hayden, M.S.2    Ghosh, S.3
  • 55
    • 0033197872 scopus 로고    scopus 로고
    • The structural basis for the recognition of diverse receptor sequences by TRAF2
    • Ye, H., Park, Y. C., Kreishman, M., Kieff, E., and Wu, H. (1999) The structural basis for the recognition of diverse receptor sequences by TRAF2. Mol. Cell 4, 321–330
    • (1999) Mol. Cell , vol.4 , pp. 321-330
    • Ye, H.1    Park, Y.C.2    Kreishman, M.3    Kieff, E.4    Wu, H.5
  • 56
    • 84957634376 scopus 로고    scopus 로고
    • Far-infrared promotes burn wound healing by suppressing NLRP3 inflammasome caused by enhanced autophagy
    • erratum 821
    • Chiu, H. W., Chen, C. H., Chang, J. N., Chen, C. H., and Hsu, Y. H. (2016) Far-infrared promotes burn wound healing by suppressing NLRP3 inflammasome caused by enhanced autophagy. J. Mol. Med. (Berl.) 94, 809–819; erratum: 821
    • (2016) J. Mol. Med. (Berl.) , vol.94 , pp. 809-819
    • Chiu, H.W.1    Chen, C.H.2    Chang, J.N.3    Chen, C.H.4    Hsu, Y.H.5
  • 57
    • 77956570532 scopus 로고    scopus 로고
    • Lung cancer cell lines as tools for biomedical discovery and research
    • Gazdar, A. F., Girard, L., Lockwood, W. W., Lam, W. L., and Minna, J. D. (2010) Lung cancer cell lines as tools for biomedical discovery and research. J. Natl. Cancer Inst. 102, 1310–1321
    • (2010) J. Natl. Cancer Inst. , vol.102 , pp. 1310-1321
    • Gazdar, A.F.1    Girard, L.2    Lockwood, W.W.3    Lam, W.L.4    Minna, J.D.5
  • 58
    • 84893835896 scopus 로고    scopus 로고
    • Activation of the NLRP1b inflammasome independently of ASC-mediated caspase-1 autoproteolysis and speck formation
    • Van Opdenbosch, N., Gurung, P., Vande Walle, L., Fossoul, A., Kanneganti, T. D., and Lamkanfi, M. (2014) Activation of the NLRP1b inflammasome independently of ASC-mediated caspase-1 autoproteolysis and speck formation. Nat. Commun. 5, 3209
    • (2014) Nat. Commun. , vol.5 , pp. 3209
    • Van Opdenbosch, N.1    Gurung, P.2    Vande Walle, L.3    Fossoul, A.4    Kanneganti, T.D.5    Lamkanfi, M.6
  • 60
    • 0032939356 scopus 로고    scopus 로고
    • The cytokine-inducible zinc finger protein A20 inhibits IL-1-induced NF-kappaB activation at the level of TRAF6
    • Heyninck, K., and Beyaert, R. (1999) The cytokine-inducible zinc finger protein A20 inhibits IL-1-induced NF-kappaB activation at the level of TRAF6. FEBS Lett. 442, 147–150
    • (1999) FEBS Lett. , vol.442 , pp. 147-150
    • Heyninck, K.1    Beyaert, R.2
  • 61
    • 77952060367 scopus 로고    scopus 로고
    • TAX1BP1 and A20 inhibit antiviral signaling by targeting TBK1-IKKi kinases
    • Parvatiyar, K., Barber, G. N., and Harhaj, E. W. (2010) TAX1BP1 and A20 inhibit antiviral signaling by targeting TBK1-IKKi kinases. J. Biol. Chem. 285, 14999–15009
    • (2010) J. Biol. Chem. , vol.285 , pp. 14999-15009
    • Parvatiyar, K.1    Barber, G.N.2    Harhaj, E.W.3
  • 62
    • 0042467558 scopus 로고    scopus 로고
    • CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members
    • Trompouki, E., Hatzivassiliou, E., Tsichritzis, T., Farmer, H., Ashworth, A., and Mosialos, G. (2003) CYLD is a deubiquitinating enzyme that negatively regulates NF-kappaB activation by TNFR family members. Nature 424, 793–796
    • (2003) Nature , vol.424 , pp. 793-796
    • Trompouki, E.1    Hatzivassiliou, E.2    Tsichritzis, T.3    Farmer, H.4    Ashworth, A.5    Mosialos, G.6
  • 63
    • 84880499903 scopus 로고    scopus 로고
    • ASC speck formation as a readout for inflammasome activation
    • Stutz, A., Horvath, G. L., Monks, B. G., and Latz, E. (2013) ASC speck formation as a readout for inflammasome activation. Methods Mol. Biol. 1040, 91–101
    • (2013) Methods Mol. Biol. , vol.1040 , pp. 91-101
    • Stutz, A.1    Horvath, G.L.2    Monks, B.G.3    Latz, E.4
  • 66
    • 85064394329 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome Coronavirus viroporin 3a activates the NLRP3 inflammasome
    • Chen, I. Y., Moriyama, M., Chang, M. F., and Ichinohe, T. (2019) Severe acute respiratory syndrome Coronavirus viroporin 3a activates the NLRP3 inflammasome. Front. Microbiol. 10, 50
    • (2019) Front. Microbiol. , vol.10 , pp. 50
    • Chen, I.Y.1    Moriyama, M.2    Chang, M.F.3    Ichinohe, T.4
  • 67
    • 84875532782 scopus 로고    scopus 로고
    • Inflammasome adaptor protein Apoptosis-associated speck-like protein containing CARD (ASC) is critical for the immune response and survival in west Nile virus encephalitis
    • erratum 92, e02176-17
    • Kumar, M., Roe, K., Orillo, B., Muruve, D. A., Nerurkar, V. R., Gale, M. Jr., and Verma, S. (2013) Inflammasome adaptor protein Apoptosis-associated speck-like protein containing CARD (ASC) is critical for the immune response and survival in west Nile virus encephalitis. J. Virol. 87, 3655–3667; erratum: 92, e02176-17
    • (2013) J. Virol. , vol.87 , pp. 3655-3667
    • Kumar, M.1    Roe, K.2    Orillo, B.3    Muruve, D.A.4    Nerurkar, V.R.5    Gale, M.6    Verma, S.7
  • 68
    • 0031892786 scopus 로고    scopus 로고
    • NF-κ B p105 processing via the ubiquitin-proteasome pathway
    • Sears, C., Olesen, J., Rubin, D., Finley, D., and Maniatis, T. (1998) NF-κ B p105 processing via the ubiquitin-proteasome pathway. J. Biol. Chem. 273, 1409–1419
    • (1998) J. Biol. Chem. , vol.273 , pp. 1409-1419
    • Sears, C.1    Olesen, J.2    Rubin, D.3    Finley, D.4    Maniatis, T.5


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