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Volumn 211, Issue 5, 2015, Pages 1025-1040

Reversible ubiquitination shapes NLRC5 function and modulates NF-κB activation switch

Author keywords

[No Author keywords available]

Indexed keywords

DEUBIQUITINASE; LYSINE; POLYUBIQUITIN; PROTEIN DERIVATIVE; PROTEIN NLRC5; RECEPTOR ACTIVATOR OF NUCLEAR FACTOR KAPPA B; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 6; UNCLASSIFIED DRUG; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LIPOPOLYSACCHARIDE; NFKB1 PROTEIN, HUMAN; NFKB1 PROTEIN, MOUSE; NLRC5 PROTEIN, HUMAN; NLRC5 PROTEIN, MOUSE; SIGNAL PEPTIDE; UBIQUITIN; UBIQUITIN THIOLESTERASE; USP14 PROTEIN, HUMAN; USP14 PROTEIN, MOUSE;

EID: 84959386443     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201505091     Document Type: Article
Times cited : (46)

References (47)
  • 1
    • 0034886143 scopus 로고    scopus 로고
    • Toll-like receptors: critical proteins linking innate and acquired immunity
    • Akira, S., K. Takeda, and T. Kaisho. 2001. Toll-like receptors: critical proteins linking innate and acquired immunity. Nat. Immunol. 2:675-680. http :// dx.doi.org /10.1038 /90609
    • (2001) Nat. Immunol. , vol.2 , pp. 675-680
    • Akira, S.1    Takeda, K.2    Kaisho, T.3
  • 2
    • 77956409550 scopus 로고    scopus 로고
    • NLRC5 limits the activation of inflammatory pathways
    • Benko, S., J.G. Magalhaes, D.J. Philpott, and S.E. Girardin. 2010. NLRC5 limits the activation of inflammatory pathways. J. Immunol. 185:1681-1691. http ://dx.doi.org /10.4049 /jimmunol.0903900
    • (2010) J. Immunol. , vol.185 , pp. 1681-1691
    • Benko, S.1    Magalhaes, J.G.2    Philpott, D.J.3    Girardin, S.E.4
  • 3
    • 33845372026 scopus 로고    scopus 로고
    • Utility of exhaled nitric oxide as a noninvasive biomarker of lung inflammation in a disease model
    • Birrell, M.A., K. McCluskie, E. Hardaker, R. Knowles, and M.G. Belvisi. 2006. Utility of exhaled nitric oxide as a noninvasive biomarker of lung inflammation in a disease model. Eur. Respir. J. 28:1236-1244. http ://dx .doi.org /10.1183 /09031936.00048506
    • (2006) Eur. Respir. J. , vol.28 , pp. 1236-1244
    • Birrell, M.A.1    McCluskie, K.2    Hardaker, E.3    Knowles, R.4    Belvisi, M.G.5
  • 4
    • 84863338304 scopus 로고    scopus 로고
    • Ubiquitination in signaling to and activation of IKK
    • Chen, Z.J. 2012. Ubiquitination in signaling to and activation of IKK. Immunol. Rev. 246:95-106. http ://dx.doi.org /10.1111 /j.1600 -065X.2012.01108.x
    • (2012) Immunol. Rev. , vol.246 , pp. 95-106
    • Chen, Z.J.1
  • 5
    • 77951902675 scopus 로고    scopus 로고
    • NLRC5 negatively regulates the NF-κB and type I interferon signaling pathways
    • Cui, J., L. Zhu, X. Xia, H.Y. Wang, X. Legras, J. Hong, J. Ji, P. Shen, S. Zheng, Z.J. Chen, and R.F. Wang. 2010. NLRC5 negatively regulates the NF-κB and type I interferon signaling pathways. Cell. 141:483-496. http ://dx.doi .org /10.1016 /j.cell.2010.03.040
    • (2010) Cell. , vol.141 , pp. 483-496
    • Cui, J.1    Zhu, L.2    Xia, X.3    Wang, H.Y.4    Legras, X.5    Hong, J.6    Ji, J.7    Shen, P.8    Zheng, S.9    Chen, Z.J.10    Wang, R.F.11
  • 6
    • 84862815491 scopus 로고    scopus 로고
    • NLRP4 negatively regulates type I interferon signaling by targeting the kinase TBK1 for degradation via the ubiquitin ligase DTX4
    • Cui, J., Y. Li, L. Zhu, D. Liu, Z. Songyang, H.Y. Wang, and R.F. Wang. 2012. NLRP4 negatively regulates type I interferon signaling by targeting the kinase TBK1 for degradation via the ubiquitin ligase DTX4. Nat. Immunol. 13:387-395. http ://dx.doi.org /10.1038 /ni.2239
    • (2012) Nat. Immunol. , vol.13 , pp. 387-395
    • Cui, J.1    Li, Y.2    Zhu, L.3    Liu, D.4    Songyang, Z.5    Wang, H.Y.6    Wang, R.F.7
  • 7
    • 84921752408 scopus 로고    scopus 로고
    • Mechanisms and pathways of innate immune activation and regulation in health and cancer
    • Cui, J., Y. Chen, H.Y. Wang, and R.F. Wang. 2014. Mechanisms and pathways of innate immune activation and regulation in health and cancer. Hum. Vaccin. Immunother. 10:3270-3285. http ://dx.doi.org /10.4161 /21645515 .2014.979640
    • (2014) Hum. Vaccin. Immunother. , vol.10 , pp. 3270-3285
    • Cui, J.1    Chen, Y.2    Wang, H.Y.3    Wang, R.F.4
  • 8
    • 84918837810 scopus 로고    scopus 로고
    • Ultrasensitivity part I: Michaelian responses and zero-order ultrasensitivity
    • Ferrell, J.E. Jr., and S.H. Ha. 2014. Ultrasensitivity part I: Michaelian responses and zero-order ultrasensitivity. Trends Biochem. Sci. 39:496-503. http :// dx.doi.org /10.1016 /j.tibs.2014.08.003
    • (2014) Trends Biochem. Sci. , vol.39 , pp. 496-503
    • Ferrell, J.E.1    Ha, S.H.2
  • 9
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-κB puzzle
    • Ghosh, S., and M. Karin. 2002. Missing pieces in the NF-κB puzzle. Cell. 109:S81-S96. http ://dx.doi.org /10.1016 /S0092 -8674(02)00703 -1
    • (2002) Cell. , vol.109 , pp. S81-S96
    • Ghosh, S.1    Karin, M.2
  • 10
    • 39049183044 scopus 로고    scopus 로고
    • Regulation and function of IKK and IKKrelated kinases
    • Häcker, H., and M. Karin. 2006. Regulation and function of IKK and IKKrelated kinases. Sci. STKE. 2006:re13. http ://dx.doi.org /10.1126 /stke .3572006re13
    • (2006) Sci. STKE. , vol.2006 , pp. re13
    • Häcker, H.1    Karin, M.2
  • 11
    • 79959630000 scopus 로고    scopus 로고
    • Expanding TRAF function: TRAF3 as a tri-faced immune regulator
    • Häcker, H., P.H. Tseng, and M. Karin. 2011. Expanding TRAF function: TRAF3 as a tri-faced immune regulator. Nat. Rev. Immunol. 11:457-468. http :// dx.doi.org /10.1038 /nri2998
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 457-468
    • Häcker, H.1    Tseng, P.H.2    Karin, M.3
  • 12
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-κB
    • Hayden, M.S., and S. Ghosh. 2004. Signaling to NF-κB. Genes Dev. 18:2195-2224. http ://dx.doi.org /10.1101 /gad.1228704
    • (2004) Genes Dev. , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 13
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-κB signaling
    • Hayden, M.S., and S. Ghosh. 2008. Shared principles in NF-κB signaling. Cell. 132:344-362. http ://dx.doi.org /10.1016 /j.cell.2008.01.020
    • (2008) Cell. , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 14
    • 7644238181 scopus 로고    scopus 로고
    • Biological robustness
    • Kitano, H. 2004. Biological robustness. Nat. Rev. Genet. 5:826-837. http ://dx .doi.org /10.1038 /nrg1471
    • (2004) Nat. Rev. Genet. , vol.5 , pp. 826-837
    • Kitano, H.1
  • 15
    • 84870212902 scopus 로고    scopus 로고
    • NLRC5: A key regulator of MHC class I-dependent immune responses
    • Kobayashi, K.S., and P.J. van den Elsen. 2012. NLRC5: A key regulator of MHC class I-dependent immune responses. Nat. Rev. Immunol. 12:813-820. http ://dx.doi.org /10.1038 /nri3339
    • (2012) Nat. Rev. Immunol. , vol.12 , pp. 813-820
    • Kobayashi, K.S.1    Van Den Elsen, P.J.2
  • 16
    • 84861877407 scopus 로고    scopus 로고
    • The ubiquitin code
    • Komander, D., and M. Rape. 2012. The ubiquitin code. Annu. Rev. Biochem. 81:203-229. http ://dx.doi.org /10.1146 /annurev -biochem -060310 -170328
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 203-229
    • Komander, D.1    Rape, M.2
  • 17
    • 78751495854 scopus 로고    scopus 로고
    • NLRC5 deficiency does not influence cytokine induction by virus and bacteria infections
    • Kumar, H., S. Pandey, J. Zou, Y. Kumagai, K. Takahashi, S. Akira, and T. Kawai. 2011. NLRC5 deficiency does not influence cytokine induction by virus and bacteria infections. J. Immunol. 186:994-1000. http ://dx.doi.org /10 .4049 /jimmunol.1002094
    • (2011) J. Immunol. , vol.186 , pp. 994-1000
    • Kumar, H.1    Pandey, S.2    Zou, J.3    Kumagai, Y.4    Takahashi, K.5    Akira, S.6    Kawai, T.7
  • 19
    • 84884234601 scopus 로고    scopus 로고
    • USP18 inhibits NF-κB and NFAT activation during Th17 differentiation by deubiquitinating the TAK1-TAB1 complex
    • Liu, X., H. Li, B. Zhong, M. Blonska, S. Gorjestani, M. Yan, Q. Tian, D.E. Zhang, X. Lin, and C. Dong. 2013. USP18 inhibits NF-κB and NFAT activation during Th17 differentiation by deubiquitinating the TAK1-TAB1 complex. J. Exp. Med. 210:1575-1590. http ://dx.doi.org /10.1084 /jem.20122327
    • (2013) J. Exp. Med. , vol.210 , pp. 1575-1590
    • Liu, X.1    Li, H.2    Zhong, B.3    Blonska, M.4    Gorjestani, S.5    Yan, M.6    Tian, Q.7    Zhang, D.E.8    Lin, X.9    Dong, C.10
  • 20
    • 40549103434 scopus 로고    scopus 로고
    • High-affinity interaction between IKKβ and NEMO
    • Lo, Y.C., U. Maddineni, J.Y. Chung, R.L. Rich, D.G. Myszka, and H. Wu. 2008. High-affinity interaction between IKKβ and NEMO. Biochemistry. 47:3109-3116. http ://dx.doi.org /10.1021 /bi702312c
    • (2008) Biochemistry. , vol.47 , pp. 3109-3116
    • Lo, Y.C.1    Maddineni, U.2    Chung, J.Y.3    Rich, R.L.4    Myszka, D.G.5    Wu, H.6
  • 21
    • 51749122228 scopus 로고    scopus 로고
    • Dynamical modeling and multi-experiment fitting with PottersWheel
    • Maiwald, T., and J. Timmer. 2008. Dynamical modeling and multi-experiment fitting with PottersWheel. Bioinformatics. 24:2037-2043. http ://dx.doi .org /10.1093 /bioinformatics /btn350
    • (2008) Bioinformatics. , vol.24 , pp. 2037-2043
    • Maiwald, T.1    Timmer, J.2
  • 22
    • 84871188736 scopus 로고    scopus 로고
    • Nitric oxide controls the immunopathology of tuberculosis by inhibiting NLRP3 inflammasome- dependent processing of IL-1β
    • Mishra, B.B., V.A. Rathinam, G.W. Martens, A.J. Martinot, H. Kornfeld, K.A. Fitzgerald, and C.M. Sassetti. 2013. Nitric oxide controls the immunopathology of tuberculosis by inhibiting NLRP3 inflammasome- dependent processing of IL-1β. Nat. Immunol. 14:52-60. http ://dx.doi .org /10.1038 /ni.2474
    • (2013) Nat. Immunol. , vol.14 , pp. 52-60
    • Mishra, B.B.1    Rathinam, V.A.2    Martens, G.W.3    Martinot, A.J.4    Kornfeld, H.5    Fitzgerald, K.A.6    Sassetti, C.M.7
  • 24
    • 84907515304 scopus 로고    scopus 로고
    • Cellular sensing of viral DNA and viral evasion mechanisms
    • Orzalli, M.H., and D.M. Knipe. 2014. Cellular sensing of viral DNA and viral evasion mechanisms. Annu. Rev. Microbiol. 68:477-492. http ://dx.doi .org /10.1146 /annurev -micro -091313 -103409
    • (2014) Annu. Rev. Microbiol. , vol.68 , pp. 477-492
    • Orzalli, M.H.1    Knipe, D.M.2
  • 25
    • 33644701849 scopus 로고    scopus 로고
    • The inflammasome
    • Petrilli, V., S. Papin, and J. Tschopp. 2005. The inflammasome. Curr. Biol. 15:R581. http ://dx.doi.org /10.1016 /j.cub.2005.07.049
    • (2005) Curr. Biol. , vol.15 , pp. R581
    • Petrilli, V.1    Papin, S.2    Tschopp, J.3
  • 26
    • 41149142535 scopus 로고    scopus 로고
    • Systems biology and cancer stem cells
    • Price, N.D., G. Foltz, A. Madan, L. Hood, and Q. Tian. 2008. Systems biology and cancer stem cells. J. Cell. Mol. Med. 12:97-110. http ://dx.doi.org /10 .1111 /j.1582 -4934.2007.00151.x
    • (2008) J. Cell. Mol. Med. , vol.12 , pp. 97-110
    • Price, N.D.1    Foltz, G.2    Madan, A.3    Hood, L.4    Tian, Q.5
  • 27
    • 84872782298 scopus 로고    scopus 로고
    • Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity
    • Py, B.F., M.S. Kim, H. Vakifahmetoglu-Norberg, and J. Yuan. 2013. Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity. Mol. Cell. 49:331-338. http ://dx.doi.org /10.1016 /j.molcel.2012.11.009
    • (2013) Mol. Cell. , vol.49 , pp. 331-338
    • Py, B.F.1    Kim, M.S.2    Vakifahmetoglu-Norberg, H.3    Yuan, J.4
  • 29
    • 84903647409 scopus 로고    scopus 로고
    • Unanchored K48-linked polyubiquitin synthesized by the E3- ubiquitin ligase TRIM6 stimulates the interferon-IKKε kinase-mediated antiviral response
    • Rajsbaum, R., G.A. Versteeg, S. Schmid, A.M. Maestre, A. Belicha-Villanueva, C. Martínez-Romero, J.R. Patel, J. Morrison, G. Pisanelli, L. Miorin, et al. 2014. Unanchored K48-linked polyubiquitin synthesized by the E3- ubiquitin ligase TRIM6 stimulates the interferon-IKKε kinase-mediated antiviral response. Immunity. 40:880-895. http ://dx.doi.org /10.1016 /j .immuni.2014.04.018
    • (2014) Immunity. , vol.40 , pp. 880-895
    • Rajsbaum, R.1    Versteeg, G.A.2    Schmid, S.3    Maestre, A.M.4    Belicha-Villanueva, A.5    Martínez-Romero, C.6    Patel, J.R.7    Morrison, J.8    Pisanelli, G.9    Miorin, L.10
  • 30
    • 57749186048 scopus 로고    scopus 로고
    • A simple mathematical model of signaling resulting from the binding of lipopolysaccharide with Toll-like receptor 4 demonstrates inherent preconditioning behavior
    • Rivière, B., Y. Epshteyn, D. Swigon, and Y. Vodovotz. 2009. A simple mathematical model of signaling resulting from the binding of lipopolysaccharide with Toll-like receptor 4 demonstrates inherent preconditioning behavior. Math. Biosci. 217:19-26. http ://dx.doi.org /10 .1016 /j.mbs.2008.10.002
    • (2009) Math. Biosci. , vol.217 , pp. 19-26
    • Rivière, B.1    Epshteyn, Y.2    Swigon, D.3    Vodovotz, Y.4
  • 32
    • 84900406601 scopus 로고    scopus 로고
    • Positive feedback within a kinase signaling complex functions as a switch mechanism for NF-κB activation
    • Shinohara, H., M. Behar, K. Inoue, M. Hiroshima, T. Yasuda, T. Nagashima, S. Kimura, H. Sanjo, S. Maeda, N. Yumoto, et al. 2014. Positive feedback within a kinase signaling complex functions as a switch mechanism for NF-κB activation. Science. 344:760-764. http ://dx.doi.org /10.1126 / science.1250020
    • (2014) Science. , vol.344 , pp. 760-764
    • Shinohara, H.1    Behar, M.2    Inoue, K.3    Hiroshima, M.4    Yasuda, T.5    Nagashima, T.6    Kimura, S.7    Sanjo, H.8    Maeda, S.9    Yumoto, N.10
  • 33
    • 84892634483 scopus 로고    scopus 로고
    • Switching of the relative dominance between feedback mechanisms in lipopolysaccharide-induced NF-κB signaling
    • Sung, M.H., N. Li, Q. Lao, R.A. Gottschalk, G.L. Hager, and I.D. Fraser. 2014. Switching of the relative dominance between feedback mechanisms in lipopolysaccharide-induced NF-κB signaling. Sci. Signal. 7:ra6. http ://dx .doi.org /10.1126 /scisignal.2004764
    • (2014) Sci. Signal. , vol.7 , pp. ra6
    • Sung, M.H.1    Li, N.2    Lao, Q.3    Gottschalk, R.A.4    Hager, G.L.5    Fraser, I.D.6
  • 34
    • 77950343791 scopus 로고    scopus 로고
    • Pattern recognition receptors and inflammation
    • Takeuchi, O., and S. Akira. 2010. Pattern recognition receptors and inflammation. Cell. 140:805-820 http ://dx.doi.org /10.1016 /j.cell.2010.01.022
    • (2010) Cell. , vol.140 , pp. 805-820
    • Takeuchi, O.1    Akira, S.2
  • 35
    • 77954541844 scopus 로고    scopus 로고
    • Single-cell NF-κB dynamics reveal digital activation and analogue information processing
    • Tay, S., J.J. Hughey, T.K. Lee, T. Lipniacki, S.R. Quake, and M.W. Covert. 2010. Single-cell NF-κB dynamics reveal digital activation and analogue information processing. Nature. 466:267-271. http ://dx.doi.org /10.1038 /nature09145
    • (2010) Nature. , vol.466 , pp. 267-271
    • Tay, S.1    Hughey, J.J.2    Lee, T.K.3    Lipniacki, T.4    Quake, S.R.5    Covert, M.W.6
  • 36
    • 84862007380 scopus 로고    scopus 로고
    • Enhanced TLRinduced NF-κB signaling and type I interferon responses in NLRC5 deficient mice
    • Tong, Y., J. Cui, Q. Li, J. Zou, H.Y. Wang, and R.F. Wang. 2012. Enhanced TLRinduced NF-κB signaling and type I interferon responses in NLRC5 deficient mice. Cell Res. 22:822-835. http ://dx.doi.org /10.1038 / cr.2012.53
    • (2012) Cell Res. , vol.22 , pp. 822-835
    • Tong, Y.1    Cui, J.2    Li, Q.3    Zou, J.4    Wang, H.Y.5    Wang, R.F.6
  • 37
    • 67650724069 scopus 로고    scopus 로고
    • Regulation and function of NF-κB transcription factors in the immune system
    • Vallabhapurapu, S., and M. Karin. 2009. Regulation and function of NF-κB transcription factors in the immune system. Annu. Rev. Immunol. 27:693-733. http ://dx.doi.org /10.1146 /annurev.immunol.021908.132641
    • (2009) Annu. Rev. Immunol. , vol.27 , pp. 693-733
    • Vallabhapurapu, S.1    Karin, M.2
  • 38
    • 33845428613 scopus 로고    scopus 로고
    • MD-2 expression is not required for cell surface targeting of Tolllike receptor 4 (TLR4)
    • Visintin, A., K.A. Halmen, N. Khan, B.G. Monks, D.T. Golenbock, and E. Lien. 2006. MD-2 expression is not required for cell surface targeting of Tolllike receptor 4 (TLR4). J. Leukoc. Biol. 80:1584-1592. http ://dx.doi.org /10.1189 /jlb.0606388
    • (2006) J. Leukoc. Biol. , vol.80 , pp. 1584-1592
    • Visintin, A.1    Halmen, K.A.2    Khan, N.3    Monks, B.G.4    Golenbock, D.T.5    Lien, E.6
  • 39
    • 84896958063 scopus 로고    scopus 로고
    • Innate immune sensing and signaling of cytosolic nucleic acids
    • Wu, J., and Z.J. Chen. 2014. Innate immune sensing and signaling of cytosolic nucleic acids. Annu. Rev. Immunol. 32:461-488. http ://dx.doi.org /10 .1146 /annurev -immunol -032713 -120156
    • (2014) Annu. Rev. Immunol. , vol.32 , pp. 461-488
    • Wu, J.1    Chen, Z.J.2
  • 40
    • 57649187965 scopus 로고    scopus 로고
    • Dynamic sensitivity analysis of biological systems
    • Wu, W.H., F.S. Wang, and M.S. Chang. 2008. Dynamic sensitivity analysis of biological systems. BMC Bioinformatics. 9:S17. http ://dx.doi.org /10 .1186 /1471 -2105 -9 -S12 -S17
    • (2008) BMC Bioinformatics. , vol.9 , pp. S17
    • Wu, W.H.1    Wang, F.S.2    Chang, M.S.3
  • 42
    • 69949093459 scopus 로고    scopus 로고
    • Direct activation of protein kinases by unanchored polyubiquitin chains
    • Xia, Z.P., L. Sun, X. Chen, G. Pineda, X. Jiang, A. Adhikari, W. Zeng, and Z.J. Chen. 2009. Direct activation of protein kinases by unanchored polyubiquitin chains. Nature. 461:114-119. http ://dx.doi.org /10.1038 /nature08247
    • (2009) Nature. , vol.461 , pp. 114-119
    • Xia, Z.P.1    Sun, L.2    Chen, X.3    Pineda, G.4    Jiang, X.5    Adhikari, A.6    Zeng, W.7    Chen, Z.J.8
  • 43
    • 33645758540 scopus 로고    scopus 로고
    • PPSP: Prediction of PKspecific phosphorylation site with Bayesian decision theory
    • Xue, Y., A. Li, L. Wang, H. Feng, and X. Yao. 2006. PPSP: Prediction of PKspecific phosphorylation site with Bayesian decision theory. BMC Bioinformatics. 7:163. http ://dx.doi.org /10.1186 /1471 -2105 -7 -163
    • (2006) BMC Bioinformatics. , vol.7 , pp. 163
    • Xue, Y.1    Li, A.2    Wang, L.3    Feng, H.4    Yao, X.5
  • 44
    • 0037851769 scopus 로고    scopus 로고
    • IKKβ plays an essential role in the phosphorylation of RelA/p65 on serine 536 induced by lipopolysaccharide
    • Yang, F., E. Tang, K. Guan, and C.Y. Wang. 2003. IKKβ plays an essential role in the phosphorylation of RelA/p65 on serine 536 induced by lipopolysaccharide. J. Immunol. 170:5630-5635. http ://dx.doi.org /10 .4049 /jimmunol.170.11.5630
    • (2003) J. Immunol. , vol.170 , pp. 5630-5635
    • Yang, F.1    Tang, E.2    Guan, K.3    Wang, C.Y.4
  • 45
    • 84938809839 scopus 로고    scopus 로고
    • USP18 negatively regulates NF-κB signaling by targeting TAK1 and NEMO for deubiquitination through distinct mechanisms
    • Yang, Z., H. Xian, J. Hu, S. Tian, Y. Qin, R.F. Wang, and J. Cui. 2015. USP18 negatively regulates NF-κB signaling by targeting TAK1 and NEMO for deubiquitination through distinct mechanisms. Sci. Rep. 5:12738. http :// dx.doi.org /10.1038 /srep12738
    • (2015) Sci. Rep. , vol.5 , pp. 12738
    • Yang, Z.1    Xian, H.2    Hu, J.3    Tian, S.4    Qin, Y.5    Wang, R.F.6    Cui, J.7
  • 46
    • 84862022239 scopus 로고    scopus 로고
    • NLRC5 regulates MHC class I antigen presentation in host defense against intracellular pathogens
    • Yao, Y., Y. Wang, F. Chen, Y. Huang, S. Zhu, Q. Leng, H. Wang, Y. Shi, and Y. Qian. 2012. NLRC5 regulates MHC class I antigen presentation in host defense against intracellular pathogens. Cell Res. 22:836-847. http ://dx .doi.org /10.1038 /cr.2012.56
    • (2012) Cell Res. , vol.22 , pp. 836-847
    • Yao, Y.1    Wang, Y.2    Chen, F.3    Huang, Y.4    Zhu, S.5    Leng, Q.6    Wang, H.7    Shi, Y.8    Qian, Y.9
  • 47
    • 84896344782 scopus 로고    scopus 로고
    • NLRC3, a member of the NLR family of proteins, is a negative regulator of innate immune signaling induced by the DNA sensor STI NG
    • Zhang, L., J. Mo, K.V. Swanson, H. Wen, A. Petrucelli, S.M. Gregory, Z. Zhang, M. Schneider, Y. Jiang, K.A. Fitzgerald, et al. 2014. NLRC3, a member of the NLR family of proteins, is a negative regulator of innate immune signaling induced by the DNA sensor STI NG. Immunity. 40:329-341. http ://dx.doi.org /10.1016 /j.immuni.2014.01.010
    • (2014) Immunity. , vol.40 , pp. 329-341
    • Zhang, L.1    Mo, J.2    Swanson, K.V.3    Wen, H.4    Petrucelli, A.5    Gregory, S.M.6    Zhang, Z.7    Schneider, M.8    Jiang, Y.9    Fitzgerald, K.A.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.