메뉴 건너뛰기




Volumn 79, Issue 10, 2007, Pages 1431-1439

The membrane protein of SARS-CoV suppresses NF-κB activation

Author keywords

Cox 2; IKK ; Membrane protein; NF B; SARS CoV

Indexed keywords

CYCLOOXYGENASE 2; I KAPPA B KINASE ALPHA; I KAPPA B KINASE BETA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; LUCIFERASE; M PROTEIN; MEMBRANE PROTEIN; TUMOR NECROSIS FACTOR ALPHA;

EID: 34548278414     PISSN: 01466615     EISSN: 10969071     Source Type: Journal    
DOI: 10.1002/jmv.20953     Document Type: Article
Times cited : (69)

References (43)
  • 1
    • 0035163739 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor kappaB-dependent expression of antiapoptotic factors
    • Akari H, Bour S, Kao S, Adachi A, Strebel K. 2001. The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor kappaB-dependent expression of antiapoptotic factors. J Exp Med 194:1299-1311.
    • (2001) J Exp Med , vol.194 , pp. 1299-1311
    • Akari, H.1    Bour, S.2    Kao, S.3    Adachi, A.4    Strebel, K.5
  • 3
    • 0035844173 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of Ikappa B
    • Bour S, Perrin C, Akari H, Strebel K. 2001. The human immunodeficiency virus type 1 Vpu protein inhibits NF-kappa B activation by interfering with beta TrCP-mediated degradation of Ikappa B. J Biol Chem 276:15920-15928.
    • (2001) J Biol Chem , vol.276 , pp. 15920-15928
    • Bour, S.1    Perrin, C.2    Akari, H.3    Strebel, K.4
  • 5
    • 0035983295 scopus 로고    scopus 로고
    • NF-kappaB family of transcription factors: Central regulators of innate and adaptive immune functions
    • Caamano J, Hunter CA. 2002. NF-kappaB family of transcription factors: Central regulators of innate and adaptive immune functions. Clin Microbiol Rev 15:414-429.
    • (2002) Clin Microbiol Rev , vol.15 , pp. 414-429
    • Caamano, J.1    Hunter, C.A.2
  • 6
    • 0035966082 scopus 로고    scopus 로고
    • The induction of cyclooxygenase-2 mRNA in macrophages is biphasic and requires both CCAAT enhancer-binding protein beta (C/EBP beta) and C/EBP delta transcription factors
    • Caivano M, Gorgoni B, Cohen P, Poli V. 2001. The induction of cyclooxygenase-2 mRNA in macrophages is biphasic and requires both CCAAT enhancer-binding protein beta (C/EBP beta) and C/EBP delta transcription factors. J Biol Chem 276:48693-48701.
    • (2001) J Biol Chem , vol.276 , pp. 48693-48701
    • Caivano, M.1    Gorgoni, B.2    Cohen, P.3    Poli, V.4
  • 7
    • 2442676378 scopus 로고    scopus 로고
    • Peptidoglycan induces nuclear factor-kappaB activation and cyclooxygenase-2 expression via Ras, Raf-1, and ERK in RAW 264.7 macrophages
    • Chen BC, Chang YS, Kang JC, Hsu MJ, Sheu JR, Chen TL, Teng CM, Lin CH. 2004. Peptidoglycan induces nuclear factor-kappaB activation and cyclooxygenase-2 expression via Ras, Raf-1, and ERK in RAW 264.7 macrophages. J Biol Chem 279:20889-20897.
    • (2004) J Biol Chem , vol.279 , pp. 20889-20897
    • Chen, B.C.1    Chang, Y.S.2    Kang, J.C.3    Hsu, M.J.4    Sheu, J.R.5    Chen, T.L.6    Teng, C.M.7    Lin, C.H.8
  • 8
    • 0030608878 scopus 로고    scopus 로고
    • Involvement of NF-kappaB in the regulation of cyclooxygenase-2 protein expression in LPS-stimulated J774 macrophages
    • D'Acquisto F, Iuvone T, Rombola L, Sautebin L, Di Rosa M, Carnuccio R. 1997. Involvement of NF-kappaB in the regulation of cyclooxygenase-2 protein expression in LPS-stimulated J774 macrophages. FEBS Lett 418:175-178.
    • (1997) FEBS Lett , vol.418 , pp. 175-178
    • D'Acquisto, F.1    Iuvone, T.2    Rombola, L.3    Sautebin, L.4    Di Rosa, M.5    Carnuccio, R.6
  • 9
    • 0031950008 scopus 로고    scopus 로고
    • Coronavirus particle assembly: Primary structure requirements of the membrane protein
    • de Haan CA, Kuo L, Masters PS, Vennema H, Rottier PJ. 1998. Coronavirus particle assembly: Primary structure requirements of the membrane protein. J Virol 72:6838-6850.
    • (1998) J Virol , vol.72 , pp. 6838-6850
    • de Haan, C.A.1    Kuo, L.2    Masters, P.S.3    Vennema, H.4    Rottier, P.J.5
  • 10
    • 0034067478 scopus 로고    scopus 로고
    • Assembly of the coronavirus envelope: Homotypic interactions between the M proteins
    • de Haan CA, Vennema H, Rottier PJ. 2000. Assembly of the coronavirus envelope: Homotypic interactions between the M proteins. J Virol 74:4967-4978.
    • (2000) J Virol , vol.74 , pp. 4967-4978
    • de Haan, C.A.1    Vennema, H.2    Rottier, P.J.3
  • 13
    • 29844434283 scopus 로고    scopus 로고
    • Peptide domain involved in the interaction between membrane protein and nucleocapsid protein of SARS-associated coronavirus
    • Fang X, Ye L, Timani KA, Li S, Zen Y, Zhao M, Zheng H, Wu Z. 2005. Peptide domain involved in the interaction between membrane protein and nucleocapsid protein of SARS-associated coronavirus. J Biochem Mol Biol 38:381-385.
    • (2005) J Biochem Mol Biol , vol.38 , pp. 381-385
    • Fang, X.1    Ye, L.2    Timani, K.A.3    Li, S.4    Zen, Y.5    Zhao, M.6    Zheng, H.7    Wu, Z.8
  • 14
    • 0242690224 scopus 로고    scopus 로고
    • COX-2 and beyond: Approaches to prostaglandin inhibition in human disease
    • FitzGerald GA. 2003. COX-2 and beyond: Approaches to prostaglandin inhibition in human disease. Nat Rev Drug Discov 2:879-890.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 879-890
    • FitzGerald, G.A.1
  • 15
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: Evolutionary conserved mediators of immune responses
    • Ghosh S, May MJ, Kopp EB. 1998. NF-kappa B and Rel proteins: Evolutionary conserved mediators of immune responses. Annu Rev Immunol 16:225-260.
    • (1998) Annu Rev Immunol , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 16
    • 0032881384 scopus 로고    scopus 로고
    • Mice lacking the transcription factor subunit Rel can clear an influenza infection and have functional anti-viral cytotoxic T cells but do not develop an optimal antibody response
    • Harling-McNabb L, Deliyannis G, Jackson DC, Gerondakis S, Grigoriadis G, Brown LE. 1999. Mice lacking the transcription factor subunit Rel can clear an influenza infection and have functional anti-viral cytotoxic T cells but do not develop an optimal antibody response. Int Immunol 11:1431-1439.
    • (1999) Int Immunol , vol.11 , pp. 1431-1439
    • Harling-McNabb, L.1    Deliyannis, G.2    Jackson, D.C.3    Gerondakis, S.4    Grigoriadis, G.5    Brown, L.E.6
  • 18
    • 0036156424 scopus 로고    scopus 로고
    • Cyclooxygenase-2-10 years later
    • Hinz B, Brune K. 2002. Cyclooxygenase-2-10 years later. J Pharmacol Exp Ther 300:367-375.
    • (2002) J Pharmacol Exp Ther , vol.300 , pp. 367-375
    • Hinz, B.1    Brune, K.2
  • 19
    • 0038326554 scopus 로고    scopus 로고
    • SARS-associated coronavirus
    • Holmes KV. 2003. SARS-associated coronavirus. N Engl J Med 348:1948-1951.
    • (2003) N Engl J Med , vol.348 , pp. 1948-1951
    • Holmes, K.V.1
  • 20
    • 0030805596 scopus 로고    scopus 로고
    • Expression of mitogen-inducible cyclooxygenase induced by lipopolysaccharide: Mediation through both mitogen-activated protein kinase and NF-kappaB signaling pathways in macrophages
    • Hwang D, Jang BC, Yu G, Boudreau M. 1997. Expression of mitogen-inducible cyclooxygenase induced by lipopolysaccharide: Mediation through both mitogen-activated protein kinase and NF-kappaB signaling pathways in macrophages. Biochem Pharmacol 54:87-96.
    • (1997) Biochem Pharmacol , vol.54 , pp. 87-96
    • Hwang, D.1    Jang, B.C.2    Yu, G.3    Boudreau, M.4
  • 21
    • 0037163089 scopus 로고    scopus 로고
    • Activation of monocyte cyclooxygenase-2 gene expression by human herpesvirus 6. Role for cyclic AMP-responsive element-binding protein and activator protein-1
    • Janelle ME, Gravel A, Gosselin J, Tremblay MJ, Flamand L. 2002. Activation of monocyte cyclooxygenase-2 gene expression by human herpesvirus 6. Role for cyclic AMP-responsive element-binding protein and activator protein-1. J Biol Chem 277:30665-30674.
    • (2002) J Biol Chem , vol.277 , pp. 30665-30674
    • Janelle, M.E.1    Gravel, A.2    Gosselin, J.3    Tremblay, M.J.4    Flamand, L.5
  • 23
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-[kappa]B activity
    • Karin M, Ben-Neriah Y. 2000. Phosphorylation meets ubiquitination: The control of NF-[kappa]B activity. Annu Rev Immunol 18:621-663.
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 24
    • 0029150389 scopus 로고
    • Mice lacking the c-rel proto-oncogene exhibit defects in lymphocyte proliferation, humoral immunity, and interleukin-2 expression
    • Kontgen F, Grumont RJ, Strasser A, Metcalf D, Li R, Tarlinton D, Gerondakis S. 1995. Mice lacking the c-rel proto-oncogene exhibit defects in lymphocyte proliferation, humoral immunity, and interleukin-2 expression. Genes Dev 9:1965-1977.
    • (1995) Genes Dev , vol.9 , pp. 1965-1977
    • Kontgen, F.1    Grumont, R.J.2    Strasser, A.3    Metcalf, D.4    Li, R.5    Tarlinton, D.6    Gerondakis, S.7
  • 27
    • 0033532386 scopus 로고    scopus 로고
    • The IKKbeta subunit of IkappaB kinase (IKK) is essential for nuclear factor kappaB activation and prevention of apoptosis
    • Li ZW, Chu W, Hu Y, Delhase M, Deerinck T, Ellisman M, Johnson R, Karin M. 1999. The IKKbeta subunit of IkappaB kinase (IKK) is essential for nuclear factor kappaB activation and prevention of apoptosis. J Exp Med 189:1839-1845.
    • (1999) J Exp Med , vol.189 , pp. 1839-1845
    • Li, Z.W.1    Chu, W.2    Hu, Y.3    Delhase, M.4    Deerinck, T.5    Ellisman, M.6    Johnson, R.7    Karin, M.8
  • 28
    • 0026801535 scopus 로고
    • Membrane assembly of the triple-spanning coronavirus M protein. Individual transmembrane domains show preferred orientation
    • Locker JK, Rose JK, Horzinek MC, Rottier PJ. 1992. Membrane assembly of the triple-spanning coronavirus M protein. Individual transmembrane domains show preferred orientation. J Biol Chem 267:21911-21918.
    • (1992) J Biol Chem , vol.267 , pp. 21911-21918
    • Locker, J.K.1    Rose, J.K.2    Horzinek, M.C.3    Rottier, P.J.4
  • 29
    • 0035884902 scopus 로고    scopus 로고
    • Cowpox virus and other members of the orthopoxvirus genus interfere with the regulation of NF-kappaB activation
    • Oie KL, Pickup DJ. 2001. Cowpox virus and other members of the orthopoxvirus genus interfere with the regulation of NF-kappaB activation. Virology 288:175-187.
    • (2001) Virology , vol.288 , pp. 175-187
    • Oie, K.L.1    Pickup, D.J.2
  • 30
    • 0037437765 scopus 로고    scopus 로고
    • Advances in the pathophysiology of constitutive and inducible cyclooxygenases: Two enzymes in the spotlight
    • Parente L, Perretti M. 2003. Advances in the pathophysiology of constitutive and inducible cyclooxygenases: Two enzymes in the spotlight. Biochem Pharmacol 65:153-159.
    • (2003) Biochem Pharmacol , vol.65 , pp. 153-159
    • Parente, L.1    Perretti, M.2
  • 36
    • 0028804551 scopus 로고
    • Targeted disruption of the p50 subunit of NF-kappa B leads to multifocal defects in immune responses
    • Sha WC, Liou HC, Tuomanen EI, Baltimore D. 1995. Targeted disruption of the p50 subunit of NF-kappa B leads to multifocal defects in immune responses. Cell 80:321-330.
    • (1995) Cell , vol.80 , pp. 321-330
    • Sha, W.C.1    Liou, H.C.2    Tuomanen, E.I.3    Baltimore, D.4
  • 38
    • 0347362590 scopus 로고    scopus 로고
    • The role and regulation of COX-2 during viral infection
    • Steer SA, Corbett JA. 2003. The role and regulation of COX-2 during viral infection. Viral Immunol 16:447-460.
    • (2003) Viral Immunol , vol.16 , pp. 447-460
    • Steer, S.A.1    Corbett, J.A.2
  • 39
    • 0036081269 scopus 로고    scopus 로고
    • Host-pathogen interactions: Subversion and utilization of the NF-kappa B pathway during infection
    • Tato CM, Hunter CA. 2002. Host-pathogen interactions: Subversion and utilization of the NF-kappa B pathway during infection. Infect Immun 70:3311-3317.
    • (2002) Infect Immun , vol.70 , pp. 3311-3317
    • Tato, C.M.1    Hunter, C.A.2
  • 40
    • 0036177671 scopus 로고    scopus 로고
    • Cyclooxygenase-2: A therapeutic target
    • Turini ME, DuBois RN. 2002. Cyclooxygenase-2: A therapeutic target. Annu Rev Med 53:35-57.
    • (2002) Annu Rev Med , vol.53 , pp. 35-57
    • Turini, M.E.1    DuBois, R.N.2
  • 41
    • 0030826370 scopus 로고    scopus 로고
    • Regulation of macrophage cytokine production by prostaglandin E2.Distinct roles of cyclooxygenase-1 and -2
    • Williams JA, Shacter E. 1997. Regulation of macrophage cytokine production by prostaglandin E2.Distinct roles of cyclooxygenase-1 and -2. J Biol Chem 272:25693-25699.
    • (1997) J Biol Chem , vol.272 , pp. 25693-25699
    • Williams, J.A.1    Shacter, E.2
  • 42
    • 33646168070 scopus 로고    scopus 로고
    • Nucleocapsid protein of SARS-CoV activates the expression of cyclooxygenase-2 by binding directly to regulatory elements for nuclear factor-kappa B and CCAAT/enhancer binding protein
    • Yan X, Hao Q, Mu Y, Timani KA, Ye L, Zhu Y, Wu J. 2006. Nucleocapsid protein of SARS-CoV activates the expression of cyclooxygenase-2 by binding directly to regulatory elements for nuclear factor-kappa B and CCAAT/enhancer binding protein. Int J Biochem Cell Biol 38:1417-1428.
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 1417-1428
    • Yan, X.1    Hao, Q.2    Mu, Y.3    Timani, K.A.4    Ye, L.5    Zhu, Y.6    Wu, J.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.