메뉴 건너뛰기




Volumn 28, Issue 4, 2010, Pages 687-694

An inhibitor κB homologue from bay scallop Argopecten irradians

Author keywords

Argopecten irradians; Gene cloning; Innate immunity; I B; NF B; Signaling pathway

Indexed keywords

ARGOPECTEN IRRADIANS; BACTERIA (MICROORGANISMS); INVERTEBRATA; LISTONELLA ANGUILLARUM; MAMMALIA; PECTINIDAE;

EID: 77949914613     PISSN: 10504648     EISSN: 10959947     Source Type: Journal    
DOI: 10.1016/j.fsi.2010.01.005     Document Type: Article
Times cited : (27)

References (41)
  • 1
    • 0023724778 scopus 로고
    • I kappa B: a specific inhibitor of the NF-kappa B transcription factor
    • Baeuerle P.A., and Baltimore D. I kappa B: a specific inhibitor of the NF-kappa B transcription factor. Science 242 (1988) 540-546
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 2
    • 0034668206 scopus 로고    scopus 로고
    • Nuclear factor-kappa B activation and innate immune response in microbial pathogen infection
    • Naumann M. Nuclear factor-kappa B activation and innate immune response in microbial pathogen infection. Biochem Pharmacol 60 (2000) 1109-1114
    • (2000) Biochem Pharmacol , vol.60 , pp. 1109-1114
    • Naumann, M.1
  • 3
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses
    • Ghosh S., May M.J., and Kopp E.B. NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 16 (1998) 225-260
    • (1998) Annu Rev Immunol , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 4
    • 0028174061 scopus 로고
    • Function and activation of NF-kappa B in the immune system
    • Baeuerle P.A., and Henkel T. Function and activation of NF-kappa B in the immune system. Annu Rev Immunol 12 (1994) 141-179
    • (1994) Annu Rev Immunol , vol.12 , pp. 141-179
    • Baeuerle, P.A.1    Henkel, T.2
  • 5
    • 0029874138 scopus 로고    scopus 로고
    • The NF-kappa B and I kappa B proteins: new discoveries and insights
    • Baldwin Jr. A.S. The NF-kappa B and I kappa B proteins: new discoveries and insights. Annu Rev Immunol 14 (1996) 649-683
    • (1996) Annu Rev Immunol , vol.14 , pp. 649-683
    • Baldwin Jr., A.S.1
  • 6
    • 27844487939 scopus 로고    scopus 로고
    • The NF-kappaB pathway
    • Moynagh P.N. The NF-kappaB pathway. J Cell Sci 118 (2005) 4589-4592
    • (2005) J Cell Sci , vol.118 , pp. 4589-4592
    • Moynagh, P.N.1
  • 7
    • 0028986193 scopus 로고
    • NF-kappa B: a lesson in family values
    • Thanos D., and Maniatis T. NF-kappa B: a lesson in family values. Cell 80 (1995) 529-532
    • (1995) Cell , vol.80 , pp. 529-532
    • Thanos, D.1    Maniatis, T.2
  • 8
    • 0035920176 scopus 로고    scopus 로고
    • A novel IkappaB protein, IkappaB-zeta, induced by proinflammatory stimuli, negatively regulates nuclear factor-kappaB in the nuclei
    • Yamazaki S., Muta T., and Takeshige K. A novel IkappaB protein, IkappaB-zeta, induced by proinflammatory stimuli, negatively regulates nuclear factor-kappaB in the nuclei. J Biol Chem 276 (2001) 27657-27662
    • (2001) J Biol Chem , vol.276 , pp. 27657-27662
    • Yamazaki, S.1    Muta, T.2    Takeshige, K.3
  • 9
    • 0027332498 scopus 로고
    • The I kappa B proteins: multifunctional regulators of Rel/NF-kappa B transcription factors
    • Beg A.A., and Baldwin Jr. A.S. The I kappa B proteins: multifunctional regulators of Rel/NF-kappa B transcription factors. Genes Dev 7 (1993) 2064-2070
    • (1993) Genes Dev , vol.7 , pp. 2064-2070
    • Beg, A.A.1    Baldwin Jr., A.S.2
  • 10
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity
    • Karin M., and Ben-Neriah Y. Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu Rev Immunol 18 (2000) 621-663
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 11
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • Segal A. How neutrophils kill microbes. Annu Rev Immunol 23 (2005) 197-223
    • (2005) Annu Rev Immunol , vol.23 , pp. 197-223
    • Segal, A.1
  • 12
    • 0037157177 scopus 로고    scopus 로고
    • Hydrogen peroxide activates IkappaB kinases through phosphorylation of serine residues in the activation loops
    • Kamata H., Manabe T., Oka S., Kamata K., and Hirata H. Hydrogen peroxide activates IkappaB kinases through phosphorylation of serine residues in the activation loops. FEBS Lett 519 (2002) 231-237
    • (2002) FEBS Lett , vol.519 , pp. 231-237
    • Kamata, H.1    Manabe, T.2    Oka, S.3    Kamata, K.4    Hirata, H.5
  • 13
    • 1642422755 scopus 로고    scopus 로고
    • The immune response of Drosophila melanogaster
    • Leclerc V., and Reichhart J.M. The immune response of Drosophila melanogaster. Immunol Rev 198 (2004) 59-71
    • (2004) Immunol Rev , vol.198 , pp. 59-71
    • Leclerc, V.1    Reichhart, J.M.2
  • 14
    • 0032815497 scopus 로고    scopus 로고
    • Molluscan aquaculture in China
    • Guo X., Ford E., and Zhang F. Molluscan aquaculture in China. J Shellfish Res 18 (1999) 19-31
    • (1999) J Shellfish Res , vol.18 , pp. 19-31
    • Guo, X.1    Ford, E.2    Zhang, F.3
  • 15
    • 33646476745 scopus 로고    scopus 로고
    • Development of expressed sequence tags from the bay scallop, Argopecten irradians irradians
    • Song L., Xu W., Li C., Li H., Wu L., Xiang J., et al. Development of expressed sequence tags from the bay scallop, Argopecten irradians irradians. Mar Biotechnol (NY) 8 (2006) 161-169
    • (2006) Mar Biotechnol (NY) , vol.8 , pp. 161-169
    • Song, L.1    Xu, W.2    Li, C.3    Li, H.4    Wu, L.5    Xiang, J.6
  • 16
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling
    • Arnold K., Bordoli L., Kopp J., and Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22 (2006) 195-201
    • (2006) Bioinformatics , vol.22 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 17
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: an automated protein homology-modeling server
    • Schwede T., Kopp J., Guex N., and Peitsch M.C. SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res 31 (2003) 3381-3385
    • (2003) Nucleic Acids Res , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 18
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 19
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N., Gammeltoft S., and Brunak S. Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 294 (1999) 1351-1362
    • (1999) J Mol Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 20
    • 45949109669 scopus 로고    scopus 로고
    • MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences
    • Kumar S., Nei M., Dudley J., and Tamura K. MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences. Brief Bioinform 9 (2008) 299-306
    • (2008) Brief Bioinform , vol.9 , pp. 299-306
    • Kumar, S.1    Nei, M.2    Dudley, J.3    Tamura, K.4
  • 21
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • Tamura K., Dudley J., Nei M., and Kumar S. MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0. Mol Biol Evol 24 (2007) 1596-1599
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 22
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., and Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25 (1997) 4876-4882
    • (1997) Nucleic Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 23
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method
    • Livak K.J., and Schmittgen T.D. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 25 (2001) 402-408
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 24
    • 0027445190 scopus 로고
    • The Drosophila ankyrin repeat protein cactus has a predominantly alpha-helical secondary structure
    • Gay N.J., and Ntwasa M. The Drosophila ankyrin repeat protein cactus has a predominantly alpha-helical secondary structure. FEBS Lett 335 (1993) 155-160
    • (1993) FEBS Lett , vol.335 , pp. 155-160
    • Gay, N.J.1    Ntwasa, M.2
  • 25
    • 0028986075 scopus 로고
    • Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation
    • Brown K., Gerstberger S., Carlson L., Franzoso G., and Siebenlist U. Control of I kappa B-alpha proteolysis by site-specific, signal-induced phosphorylation. Science 267 (1995) 1485-1488
    • (1995) Science , vol.267 , pp. 1485-1488
    • Brown, K.1    Gerstberger, S.2    Carlson, L.3    Franzoso, G.4    Siebenlist, U.5
  • 26
    • 36549033242 scopus 로고    scopus 로고
    • Cg-IkappaB, a new member of the IkappaB protein family characterized in the pacific oyster Crassostrea gigas
    • Montagnani C., Labreuche Y., and Escoubas J.M. Cg-IkappaB, a new member of the IkappaB protein family characterized in the pacific oyster Crassostrea gigas. Dev Comp Immunol 32 (2008) 182-190
    • (2008) Dev Comp Immunol , vol.32 , pp. 182-190
    • Montagnani, C.1    Labreuche, Y.2    Escoubas, J.M.3
  • 27
    • 0442307969 scopus 로고    scopus 로고
    • IkappaB kinases: key regulators of the NF-kappaB pathway
    • Yamamoto Y., and Gaynor R.B. IkappaB kinases: key regulators of the NF-kappaB pathway. Trends Biochem Sci 29 (2004) 72-79
    • (2004) Trends Biochem Sci , vol.29 , pp. 72-79
    • Yamamoto, Y.1    Gaynor, R.B.2
  • 28
    • 0032217268 scopus 로고    scopus 로고
    • The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation
    • Huxford T., Huang D.B., Malek S., and Ghosh G. The crystal structure of the IkappaBalpha/NF-kappaB complex reveals mechanisms of NF-kappaB inactivation. Cell 95 (1998) 759-770
    • (1998) Cell , vol.95 , pp. 759-770
    • Huxford, T.1    Huang, D.B.2    Malek, S.3    Ghosh, G.4
  • 29
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner M., and Rogers S.W. PEST sequences and regulation by proteolysis. Trends Biochem Sci 21 (1996) 267-271
    • (1996) Trends Biochem Sci , vol.21 , pp. 267-271
    • Rechsteiner, M.1    Rogers, S.W.2
  • 30
    • 0034602312 scopus 로고    scopus 로고
    • A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity
    • Decatur A.L., and Portnoy D.A. A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity. Science 290 (2000) 992-995
    • (2000) Science , vol.290 , pp. 992-995
    • Decatur, A.L.1    Portnoy, D.A.2
  • 31
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis
    • Rogers S., Wells R., and Rechsteiner M. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234 (1986) 364-368
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 32
    • 0031035117 scopus 로고    scopus 로고
    • Casein kinase II phosphorylates Ser468 in the PEST domain of the Drosophila IkappaB homologue cactus
    • Packman L.C., Kubota K., Parker J., and Gay N.J. Casein kinase II phosphorylates Ser468 in the PEST domain of the Drosophila IkappaB homologue cactus. FEBS Lett 400 (1997) 45-50
    • (1997) FEBS Lett , vol.400 , pp. 45-50
    • Packman, L.C.1    Kubota, K.2    Parker, J.3    Gay, N.J.4
  • 33
    • 59549084520 scopus 로고    scopus 로고
    • Molecular characterization and expression analysis of the I kappa B gene from pearl oyster Pinctada fucata
    • Zhang D., Jiang S., Qiu L., Su T., Wu K., Li Y., et al. Molecular characterization and expression analysis of the I kappa B gene from pearl oyster Pinctada fucata. Fish Shellfish Immunol 26 (2009) 84-90
    • (2009) Fish Shellfish Immunol , vol.26 , pp. 84-90
    • Zhang, D.1    Jiang, S.2    Qiu, L.3    Su, T.4    Wu, K.5    Li, Y.6
  • 34
    • 0028978032 scopus 로고
    • Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli
    • Traenckner E.B., Pahl H.L., Henkel T., Schmidt K.N., Wilk S., and Baeuerle P.A. Phosphorylation of human I kappa B-alpha on serines 32 and 36 controls I kappa B-alpha proteolysis and NF-kappa B activation in response to diverse stimuli. EMBO J 14 (1995) 2876-2883
    • (1995) EMBO J , vol.14 , pp. 2876-2883
    • Traenckner, E.B.1    Pahl, H.L.2    Henkel, T.3    Schmidt, K.N.4    Wilk, S.5    Baeuerle, P.A.6
  • 36
    • 0030613646 scopus 로고    scopus 로고
    • Catalysis by a multiprotein IkappaB kinase complex
    • Maniatis T. Catalysis by a multiprotein IkappaB kinase complex. Science 278 (1997) 818-819
    • (1997) Science , vol.278 , pp. 818-819
    • Maniatis, T.1
  • 37
    • 0030613555 scopus 로고    scopus 로고
    • IkappaB kinase: beginning, not the end
    • Verma I.M., and Stevenson J. IkappaB kinase: beginning, not the end. Proc Natl Acad Sci U S A 94 (1997) 11758-11760
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11758-11760
    • Verma, I.M.1    Stevenson, J.2
  • 38
    • 2442706456 scopus 로고    scopus 로고
    • The ankyrin repeat as molecular architecture for protein recognition
    • Mosavi L.K., Cammett T.J., Desrosiers D.C., and Peng Z.Y. The ankyrin repeat as molecular architecture for protein recognition. Protein Sci 13 (2004) 1435-1448
    • (2004) Protein Sci , vol.13 , pp. 1435-1448
    • Mosavi, L.K.1    Cammett, T.J.2    Desrosiers, D.C.3    Peng, Z.Y.4
  • 39
    • 0028971291 scopus 로고
    • Constitutive NF-kappa B activation, enhanced granulopoiesis, and neonatal lethality in I kappa B alpha-deficient mice
    • Beg A.A., Sha W.C., Bronson R.T., and Baltimore D. Constitutive NF-kappa B activation, enhanced granulopoiesis, and neonatal lethality in I kappa B alpha-deficient mice. Genes Dev 9 (1995) 2736-2746
    • (1995) Genes Dev , vol.9 , pp. 2736-2746
    • Beg, A.A.1    Sha, W.C.2    Bronson, R.T.3    Baltimore, D.4
  • 40
    • 33645234317 scopus 로고    scopus 로고
    • Evidence for the ancient origin of the NF-kappaB/IkappaB cascade: its archaic role in pathogen infection and immunity
    • Wang X.W., Tan N.S., Ho B., and Ding J.L. Evidence for the ancient origin of the NF-kappaB/IkappaB cascade: its archaic role in pathogen infection and immunity. Proc Natl Acad Sci U S A 103 (2006) 4204-4209
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4204-4209
    • Wang, X.W.1    Tan, N.S.2    Ho, B.3    Ding, J.L.4
  • 41
    • 0033597935 scopus 로고    scopus 로고
    • Interaction and specificity of Rel-related proteins in regulating Drosophila immunity gene expression
    • Han Z.S., and Ip Y.T. Interaction and specificity of Rel-related proteins in regulating Drosophila immunity gene expression. J Biol Chem 274 (1999) 21355-21361
    • (1999) J Biol Chem , vol.274 , pp. 21355-21361
    • Han, Z.S.1    Ip, Y.T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.