메뉴 건너뛰기




Volumn 12, Issue 6, 2013, Pages 1513-1529

Quantitation of the dynamic profiles of the innate immune response using multiplex selected reaction monitoring-mass spectrometry

Author keywords

[No Author keywords available]

Indexed keywords

DOUBLE STRANDED RNA; I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERFERON REGULATORY FACTOR 3; SMALL INTERFERING RNA;

EID: 84878577969     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M112.023465     Document Type: Article
Times cited : (30)

References (70)
  • 3
  • 4
    • 0034798380 scopus 로고    scopus 로고
    • NEMO/IKKγ: Linking NF-κB to human disease
    • DOI 10.1016/S1471-4914(01)02154-2
    • Courtois, G., Smahi, A., and Israel, A. (2001) NEMO/IKK gamma: linking NF-kappa B to human disease. Trends Mol. Med. 7, 427-430 (Pubitemid 32964151)
    • (2001) Trends in Molecular Medicine , vol.7 , Issue.10 , pp. 427-430
    • Courtois, G.1    Smahi, A.2    Israel, A.3
  • 5
    • 53149137461 scopus 로고    scopus 로고
    • Respiratory syncytial virus induces RelA release from cytoplasmic 100-kDa NF-kappa B2 complexes via a novel retinoic acid-inducible gene-I{middle dot}NFkappa B-inducing kinase signaling pathway
    • Liu, P., Li, K., Garofalo, R. P., and Brasier, A. R. (2008) Respiratory syncytial virus induces RelA release from cytoplasmic 100-kDa NF-kappa B2 complexes via a novel retinoic acid-inducible gene-I{middle dot}NFkappa B-inducing kinase signaling pathway. J. Biol. Chem. 283, 23169-23178
    • (2008) J. Biol. Chem. , vol.283 , pp. 23169-23178
    • Liu, P.1    Li, K.2    Garofalo, R.P.3    Brasier, A.R.4
  • 6
    • 77951235286 scopus 로고    scopus 로고
    • Expression of an IKKgamma splice variant determines IRF3 and canonical NF-kappaB pathway utilization in ssRNA virus infection
    • Liu, P., Lu, M., Tian, B., Li, K., Garofalo, R. P., Prusak, D., Wood, T. G., and Brasier, A. R. (2009) Expression of an IKKgamma splice variant determines IRF3 and canonical NF-kappaB pathway utilization in ssRNA virus infection. PLoS One 4, e8079
    • (2009) PLoS One , vol.4
    • Liu, P.1    Lu, M.2    Tian, B.3    Li, K.4    Garofalo, R.P.5    Prusak, D.6    Wood, T.G.7    Brasier, A.R.8
  • 7
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IκB kinase complex essential for NF-κB activation
    • DOI 10.1016/S0092-8674(00)81466-X
    • Yamaoka, S., Courtois, G., Bessia, C., Whiteside, S. T., Weil, R., Agou, F., Kirk, H. E., Kay, R. J., and Israel, A. (1998) Complementation cloning ofNEMO, a component of the IkappaB kinase complex essential for NFkappaB activation. Cell 93, 1231-1240 (Pubitemid 28307427)
    • (1998) Cell , vol.93 , Issue.7 , pp. 1231-1240
    • Yamaoka, S.1    Courtois, G.2    Bessia, C.3    Whiteside, S.T.4    Weil, R.5    Agou, F.6    Kirk, H.E.7    Kay, R.J.8    Israel, A.9
  • 9
    • 34249058119 scopus 로고    scopus 로고
    • The NEMO adaptor bridges the nuclear factor-κB and interferon regulatory factor signaling pathways
    • DOI 10.1038/ni1465, PII NI1465
    • Zhao, T., Yang, L., Sun, Q., Arguello, M., Ballard, D. W., Hiscott, J., and Lin, R. (2007) The NEMO adaptor bridges the nuclear factor-kappaB andinterferon regulatory factor signaling pathways. Nat. Immunol. 8, 592-600 (Pubitemid 46785123)
    • (2007) Nature Immunology , vol.8 , Issue.6 , pp. 592-600
    • Zhao, T.1    Yang, L.2    Sun, Q.3    Arguello, M.4    Ballard, D.W.5    Hiscott, J.6    Lin, R.7
  • 11
    • 21644463312 scopus 로고    scopus 로고
    • Respiratory syncytial virus influences NF-κB-dependent gene expression through a novel pathway involving MAP3K14/NIK expression and nuclear complex formation with NF-κB2
    • DOI 10.1128/JVI.79.14.8948-8959.2005
    • Choudhary, S., Boldogh, S., Garofalo, R., Jamaluddin, M., and Brasier, A. R. (2005) Respiratory syncytial virus influences NF-kappaB-dependent gene expression through a novel pathway involving MAP3K14/NIKexpression and nuclear complex formation with NF-kappaB2. J. Virol. 79, 8948-8959 (Pubitemid 40934806)
    • (2005) Journal of Virology , vol.79 , Issue.14 , pp. 8948-8959
    • Choudhary, S.1    Boldogh, S.2    Garofalo, R.3    Jamaluddin, M.4    Brasier, A.R.5
  • 13
    • 0032131490 scopus 로고    scopus 로고
    • Role of the interferon regulatory factors (IRFs) in virus-mediated signaling and regulation of cell growth
    • DOI 10.1016/S0300-9084(99)80018-2
    • Pitha, P. M., Au, W. C., Lowther, W., Juang, Y. T., Schafer, S. L., Burysek, L., Hiscott, J., and Moore, P. A. (1998) Role of the interferon regulatory factors (IRFs) in virus-mediated signaling and regulation of cell growth. Biochimie (Paris) 80, 651-658 (Pubitemid 29497582)
    • (1998) Biochimie , vol.80 , Issue.8-9 , pp. 651-658
    • Pitha, P.M.1    Au, W.-C.2    Lowther, W.3    Juang, Y.-T.4    Schafer, S.L.5    Burysek, L.6    Hiscott, J.7    Moore, P.A.8
  • 16
    • 0034292429 scopus 로고    scopus 로고
    • Identification of a novel cytokine response element in the human IFN regulatory factor-1 gene promoter
    • Imanishi, D., Yamamoto, K., Tsushima, H., Miyazaki, Y., Kuriyama, K., Tomonaga, M., and Matsuyama, T. (2000) Identification of a novel cytokine response element in the human IFN regulatory factor-1 gene promoter. J. Immunol. 165, 3907-3916 (Pubitemid 32057299)
    • (2000) Journal of Immunology , vol.165 , Issue.7 , pp. 3907-3916
    • Imanishi, D.1    Yamamoto, K.2    Tsushima, H.3    Miyazaki, Y.4    Kuriyama, K.5    Tomonaga, M.6    Matsuyama, T.7
  • 17
    • 0032538891 scopus 로고    scopus 로고
    • Differential viral induction of distinct interferon-α genes by positive feedback through interferon regulatory factor-7
    • Marie, I., Durbin, J. E., and Levy, D. E. (1998) Differential viral induction of distinct interferon-alpha genes by positive feedback through interferon regulatory factor-7. EMBO J. 17, 6660-6669 (Pubitemid 28521799)
    • (1998) EMBO Journal , vol.17 , Issue.22 , pp. 6660-6669
    • Marie, I.1    Durbin, J.E.2    Levy, D.E.3
  • 18
    • 79951676291 scopus 로고    scopus 로고
    • Systems biology approaches to dissect mammalian innate immunity
    • Shapira, S. D., and Hacohen, N. (2011) Systems biology approaches to dissect mammalian innate immunity. Curr. Opin. Immunol. 23, 71-77
    • (2011) Curr. Opin. Immunol. , vol.23 , pp. 71-77
    • Shapira, S.D.1    Hacohen, N.2
  • 19
    • 58049203835 scopus 로고    scopus 로고
    • Systems biology of innate immunity
    • Zak, D. E., and Aderem, A. (2009) Systems biology of innate immunity. Immunol. Rev. 227, 264-282
    • (2009) Immunol. Rev. , vol.227 , pp. 264-282
    • Zak, D.E.1    Aderem, A.2
  • 22
    • 77955345941 scopus 로고    scopus 로고
    • Profiling of protein interaction networks of protein complexes using affinity purification and quantitative mass spectrometry
    • Kaake, R. M., Wang, X., and Huang, L. (2010) Profiling of protein interaction networks of protein complexes using affinity purification and quantitative mass spectrometry. Mol. Cell. Proteomics 9, 1650-1665
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1650-1665
    • Kaake, R.M.1    Wang, X.2    Huang, L.3
  • 23
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-based proteomics
    • Choudhary, C., and Mann, M. (2010) Decoding signalling networks by mass spectrometry-based proteomics. Nat. Rev. Mol. Cell. Biol. 11, 427-439
    • (2010) Nat. Rev. Mol. Cell. Biol. , vol.11 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 24
    • 33947182552 scopus 로고    scopus 로고
    • An integrated mass spectrometric and computational framework for the analysis of protein interaction networks
    • DOI 10.1038/nbt1289, PII NBT1289
    • Rinner, O., Mueller, L. N., Hubalek, M., Muller, M., Gstaiger, M., and Aebersold, R. (2007) An integrated mass spectrometric and computational framework for the analysis of protein interaction networks. Nat. Biotechnol. 25, 345-352 (Pubitemid 46398770)
    • (2007) Nature Biotechnology , vol.25 , Issue.3 , pp. 345-352
    • Rinner, O.1    Mueller, L.N.2    Hubalek, M.3    Muller, M.4    Gstaiger, M.5    Aebersold, R.6
  • 25
    • 54049090766 scopus 로고    scopus 로고
    • Selected reaction monitoring for quantitative proteomics: A tutorial
    • Lange, V., Picotti, P., Domon, B., and Aebersold, R. (2008) Selected reaction monitoring for quantitative proteomics: a tutorial. Mol. Syst. Biol. 4, 222
    • (2008) Mol. Syst. Biol. , vol.4 , pp. 222
    • Lange, V.1    Picotti, P.2    Domon, B.3    Aebersold, R.4
  • 27
    • 68749094119 scopus 로고    scopus 로고
    • Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics
    • Picotti, P., Bodenmiller, B., Mueller, L. N., Domon, B., and Aebersold, R. (2009) Full dynamic range proteome analysis of S. cerevisiae by targeted proteomics. Cell 138, 795-806
    • (2009) Cell , vol.138 , pp. 795-806
    • Picotti, P.1    Bodenmiller, B.2    Mueller, L.N.3    Domon, B.4    Aebersold, R.5
  • 28
    • 79960245388 scopus 로고    scopus 로고
    • Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor
    • Bisson, N., James, D. A., Ivosev, G., Tate, S. A., Bonner, R., Taylor, L., and Pawson, T. (2011) Selected reaction monitoring mass spectrometry reveals the dynamics of signaling through the GRB2 adaptor. Nat. Biotechnol. 29, 653-658
    • (2011) Nat. Biotechnol. , vol.29 , pp. 653-658
    • Bisson, N.1    James, D.A.2    Ivosev, G.3    Tate, S.A.4    Bonner, R.5    Taylor, L.6    Pawson, T.7
  • 29
    • 34547810054 scopus 로고    scopus 로고
    • Quantitative mass spectrometry identifies insulin signaling targets in C. elegans
    • DOI 10.1126/science.1139952
    • Dong, M. Q., Venable, J. D., Au, N., Xu, T., Park, S. K., Cociorva, D., Johnson, J. R., Dillin, A., and Yates, J. R., III (2007) Quantitative mass spectrometry identifies insulin signaling targets in C. elegans. Science 317, 660-663 (Pubitemid 47229964)
    • (2007) Science , vol.317 , Issue.5838 , pp. 660-663
    • Dong, M.-Q.1    Venable, J.D.2    Au, N.3    Xu, T.4    Sung, K.P.5    Cociorva, D.6    Johnson, J.R.7    Dillin, A.8    Yates III, J.R.9
  • 30
    • 80655146232 scopus 로고    scopus 로고
    • RelA Ser276 phosphorylation-coupled Lys310 acetylation controls transcriptional elongation of inflammatory cytokines in respiratory syncytial virus infection
    • Brasier, A. R., Tian, B., Jamaluddin, M., Kalita, M. K., Garofalo, R. P., and Lu, M. (2011) RelA Ser276 phosphorylation-coupled Lys310 acetylation controls transcriptional elongation of inflammatory cytokines in respiratory syncytial virus infection. J. Virol. 85, 11752-11769
    • (2011) J. Virol. , vol.85 , pp. 11752-11769
    • Brasier, A.R.1    Tian, B.2    Jamaluddin, M.3    Kalita, M.K.4    Garofalo, R.P.5    Lu, M.6
  • 31
    • 84879597199 scopus 로고    scopus 로고
    • Applications of selected reaction monitoring (SRM)-mass spectrometry (MS) for quantitative measurement of signaling pathways (2013)
    • Zhao, Y., and Brasier, A. R. (2013) Applications of selected reaction monitoring (SRM)-mass spectrometry (MS) for quantitative measurement of signaling pathways (2013). Methods http://dx.doi.org/10.1016/j.ymeth.2013.02.001
    • (2013) Methods
    • Zhao, Y.1    Brasier, A.R.2
  • 32
    • 11144320641 scopus 로고    scopus 로고
    • Open source system for analyzing, validating, and storing protein identification data
    • DOI 10.1021/pr049882h
    • Craig, R., Cortens, J. P., and Beavis, R. C. (2004) Open source system for analyzing, validating, and storing protein identification data. J. Proteome Res. 3, 1234-1242 (Pubitemid 40040378)
    • (2004) Journal of Proteome Research , vol.3 , Issue.6 , pp. 1234-1242
    • Craig, R.1    Cortens, J.P.2    Beavis, R.C.3
  • 33
    • 59849093889 scopus 로고    scopus 로고
    • Prediction of high-responding peptides for targeted protein assays by mass spectrometry
    • Fusaro, V. A., Mani, D. R., Mesirov, J. P., and Carr, S. A. (2009) Prediction of high-responding peptides for targeted protein assays by mass spectrometry. Nat. Biotechnol. 27, 190-198
    • (2009) Nat. Biotechnol. , vol.27 , pp. 190-198
    • Fusaro, V.A.1    Mani, D.R.2    Mesirov, J.P.3    Carr, S.A.4
  • 34
    • 33646729680 scopus 로고    scopus 로고
    • Functional analysis of the nuclear proteome of human A549 alveolar epithelial cells by HPLC-high resolution 2-D gel electrophoresis
    • Forbus, J., Spratt, H., Wiktorowicz, J., Wu, Z., Boldogh, I., Denner, L., Kurosky, A., Brasier, R. C., Luxon, B., and Brasier, A. R. (2006) Functional analysis of the nuclear proteome of human A549 alveolar epithelial cells by HPLC-high resolution 2-D gel electrophoresis. Proteomics 6, 2656-2672
    • (2006) Proteomics , vol.6 , pp. 2656-2672
    • Forbus, J.1    Spratt, H.2    Wiktorowicz, J.3    Wu, Z.4    Boldogh, I.5    Denner, L.6    Kurosky, A.7    Brasier, R.C.8    Luxon, B.9    Brasier, A.R.10
  • 36
    • 55349139657 scopus 로고    scopus 로고
    • Quantification of thyroglobulin, a low-abundance serum protein, by immunoaffinity peptide enrichment and tandem mass spectrometry
    • Hoofnagle, A. N., Becker, J. O., Wener, M. H., and Heinecke, J. W. (2008) Quantification of thyroglobulin, a low-abundance serum protein, by immunoaffinity peptide enrichment and tandem mass spectrometry. Clin. Chem. 54, 1796-1804
    • (2008) Clin. Chem. , vol.54 , pp. 1796-1804
    • Hoofnagle, A.N.1    Becker, J.O.2    Wener, M.H.3    Heinecke, J.W.4
  • 37
    • 38349068918 scopus 로고    scopus 로고
    • Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution
    • Keshishian, H., Addona, T., Burgess, M., Kuhn, E., and Carr, S. A. (2007) Quantitative, multiplexed assays for low abundance proteins in plasma by targeted mass spectrometry and stable isotope dilution. Mol. Cell. Proteomics 6, 2212-2229
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 2212-2229
    • Keshishian, H.1    Addona, T.2    Burgess, M.3    Kuhn, E.4    Carr, S.A.5
  • 39
    • 66449083773 scopus 로고    scopus 로고
    • Developing multiplexed assays for troponin i and interleukin-33 in plasma by peptide immunoaffinity enrichment and targeted mass spectrometry
    • Kuhn, E., Addona, T., Keshishian, H., Burgess, M., Mani, D. R., Lee, R. T., Sabatine, M. S., Gerszten, R. E., and Carr, S. A. (2009) Developing multiplexed assays for troponin I and interleukin-33 in plasma by peptide immunoaffinity enrichment and targeted mass spectrometry. Clin. Chem. 55, 1108-1117
    • (2009) Clin. Chem. , vol.55 , pp. 1108-1117
    • Kuhn, E.1    Addona, T.2    Keshishian, H.3    Burgess, M.4    Mani, D.R.5    Lee, R.T.6    Sabatine, M.S.7    Gerszten, R.E.8    Carr, S.A.9
  • 40
    • 79958019911 scopus 로고    scopus 로고
    • Quantification of activated NF-kappaB/RelA complexes using ssDNA aptamer affinity-stable isotope dilution-selected reaction monitoring-mass spectrometry
    • M111.008771
    • Zhao, Y., Widen, S. G., Jamaluddin, M., Tian, B., Wood, T. G., Edeh, C. B., and Brasier, A. R. (2011) Quantification of activated NF-kappaB/RelA complexes using ssDNA aptamer affinity-stable isotope dilution-selected reaction monitoring-mass spectrometry. Mol. Cell. Proteomics 10, M111.008771
    • (2011) Mol. Cell. Proteomics , vol.10
    • Zhao, Y.1    Widen, S.G.2    Jamaluddin, M.3    Tian, B.4    Wood, T.G.5    Edeh, C.B.6    Brasier, A.R.7
  • 41
    • 0001229909 scopus 로고    scopus 로고
    • A practical guide to analytical method validation
    • Green, J. M. (1996) A practical guide to analytical method validation. Anal. Chem. 68, A305-A309
    • (1996) Anal. Chem. , vol.68
    • Green, J.M.1
  • 43
    • 79961202534 scopus 로고    scopus 로고
    • The importance of the digest: Proteolysis and absolute quantification in proteomics
    • Brownridge, P., and Beynon, R. J. (2011) The importance of the digest: proteolysis and absolute quantification in proteomics. Methods 54, 351-360
    • (2011) Methods , vol.54 , pp. 351-360
    • Brownridge, P.1    Beynon, R.J.2
  • 44
    • 44949092745 scopus 로고    scopus 로고
    • Protein quantification by isotope dilution mass spectrometry of proteolytic fragments: Cleavage rate and accuracy
    • DOI 10.1021/ac7024738
    • Arsene, C. G., Ohlendorf, R., Burkitt, W., Pritchard, C., Henrion, A.,O'Connor, G., Bunk, D. M., and Guttler, B. (2008) Protein quantification by isotope dilution mass spectrometry of proteolytic fragments: cleavage rate and accuracy. Anal. Chem. 80, 4154-4160 (Pubitemid 351812769)
    • (2008) Analytical Chemistry , vol.80 , Issue.11 , pp. 4154-4160
    • Arsene, C.G.1    Ohlendorf, R.2    Burkitt, W.3    Pritchard, C.4    Henrion, A.5    O'Connor, G.6    Bunk, D.M.7    Guttler, B.8
  • 45
    • 0030729481 scopus 로고    scopus 로고
    • Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold
    • DOI 10.1074/jbc.272.48.29987
    • Perona, J. J., and Craik, C. S. (1997) Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. J. Biol. Chem. 272, 29987-29990 (Pubitemid 27512189)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.48 , pp. 29987-29990
    • Perona, J.J.1    Craik, C.S.2
  • 46
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I., and Berger, A. (1967) On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 47
    • 33846632267 scopus 로고    scopus 로고
    • Prediction of missed cleavage sites in tryptic peptides aids protein identification in proteomics
    • DOI 10.1021/pr060507u
    • Siepen, J. A., Keevil, E. J., Knight, D., and Hubbard, S. J. (2007) Prediction of missed cleavage sites in tryptic peptides aids protein identification in proteomics. J. Proteome Res. 6, 399-408 (Pubitemid 46173693)
    • (2007) Journal of Proteome Research , vol.6 , Issue.1 , pp. 399-408
    • Siepen, J.A.1    Keevil, E.-J.2    Knight, D.3    Hubbard, S.J.4
  • 48
    • 0035909372 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA and activation of NF-κB by Toll-like receptor 3
    • DOI 10.1038/35099560
    • Alexopoulou, L., Holt, A. C., Medzhitov, R., and Flavell, R. A. (2001) Recognition of double-stranded RNA and activation of NF-kappaB by Tolllike receptor 3. Nature 413, 732-738 (Pubitemid 33009951)
    • (2001) Nature , vol.413 , Issue.6857 , pp. 732-738
    • Alexopoulou, L.1    Holt, A.C.2    Medzhitov, R.3    Flavell, R.A.4
  • 50
    • 0035047145 scopus 로고    scopus 로고
    • Induction of IRF-3/-7 kinase and NF-κB in response to double-stranded RNA and virus infection: Common and unique pathways
    • DOI 10.1046/j.1365-2443.2001.00426.x
    • Iwamura, T., Yoneyama, M., Yamaguchi, K., Suhara, W., Mori, W., Shiota, K., Okabe, Y., Namiki, H., and Fujita, T. (2001) Induction of IRF-3/-7 kinase and NF-kappaB in response to double-stranded RNA and virus infection: common and unique pathways. Genes Cells 6, 375-388 (Pubitemid 32401282)
    • (2001) Genes to Cells , vol.6 , Issue.4 , pp. 375-388
    • Iwamura, T.1    Yoneyama, M.2    Yamaguchi, K.3    Suhara, W.4    Mori, W.5    Shiota, K.6    Okabe, Y.7    Namiki, H.8    Fujita, T.9
  • 51
    • 0024516201 scopus 로고
    • The involvement of NF-κB in β-interferon gene regulation reveals its role as widely inducible mediator of signal transduction
    • DOI 10.1016/0092-8674(89)90966-5
    • Lenardo, M. J., Fan, C. M., Maniatis, T., and Baltimore, D. (1989) The involvement of NF-kappa B in beta-interferon gene regulation reveals its role as widely inducible mediator of signal transduction. Cell 57, 287-294 (Pubitemid 19112367)
    • (1989) Cell , vol.57 , Issue.2 , pp. 287-294
    • Lenardo, M.J.1    Fan, C.-M.2    Maniatis, T.3    Baltimore, D.4
  • 52
    • 0024380583 scopus 로고
    • Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes
    • DOI 10.1016/0092-8674(89)90107-4
    • Harada, H., Fujita, T., Miyamoto, M., Kimura, Y., Maruyama, M., Furia, A.,Miyata, T., and Taniguchi, T. (1989) Structurally similar but functionally distinct factors, IRF-1 and IRF-2, bind to the same regulatory elements of IFN and IFN-inducible genes. Cell 58, 729-739 (Pubitemid 19210966)
    • (1989) Cell , vol.58 , Issue.4 , pp. 729-739
    • Harada, H.1    Fujita, T.2    Miyamoto, M.3    Kimura, Y.4    Maruyama, M.5    Furia, A.6    Miyata, T.7    Taniguchi, T.8
  • 53
    • 0032481352 scopus 로고    scopus 로고
    • Direct triggering of the type I interferon system by virus infection: Activation of a transcription factor complex containing IRF-3 and CBP/p300
    • DOI 10.1093/emboj/17.4.1087
    • Yoneyama, M., Suhara, W., Fukuhara, Y., Fukuda, M., Nishida, E., and Fujita, T. (1998) Direct triggering of the type I interferon system by virus infection: activation of a transcription factor complex containing IRF-3 and CBP/p300. EMBO J. 17, 1087-1095 (Pubitemid 28077662)
    • (1998) EMBO Journal , vol.17 , Issue.4 , pp. 1087-1095
    • Yoneyama, M.1    Suhara, W.2    Fukuhara, Y.3    Fukuda, M.4    Nishida, E.5    Fujita, T.6
  • 54
    • 6344262160 scopus 로고    scopus 로고
    • Nuclear heat shock response and novel nuclear domain 10 reorganization in respiratory syncytial virus-infected A549 cells identified by high-resolution two-dimensional gel electrophoresis
    • DOI 10.1128/JVI.78.21.11461-11476.2004
    • Brasier, A. R., Spratt, H., Wu, Z., Boldogh, I., Zhang, Y., Garofalo, R. P., Casola, A., Pashmi, J., Haag, A., Luxon, B., and Kurosky, A. (2004) Nuclear heat shock response and novel nuclear domain 10 reorganization in respiratory syncytial virus-infected a549 cells identified by high-resolution two-dimensional gel electrophoresis. J. Virol. 78, 11461-11476 (Pubitemid 39390734)
    • (2004) Journal of Virology , vol.78 , Issue.21 , pp. 11461-11476
    • Brasier, A.R.1    Spratt, H.2    Wu, Z.3    Boldogh, I.4    Zhang, Y.5    Garofalo, R.P.6    Casola, A.7    Pashmi, J.8    Haag, A.9    Luxon, B.10    Kurosky, A.11
  • 55
    • 0030942258 scopus 로고    scopus 로고
    • Mechanism for biphasic Rel A. NF-κB1 nuclear translocation in tumor necrosis factor α-stimulated hepatocytes
    • DOI 10.1074/jbc.272.15.9825
    • Han, Y., and Brasier, A. R. (1997) Mechanism for biphasic rel A. NFkappaB1 nuclear translocation in tumor necrosis factor alpha-stimulated hepatocytes. J. Biol. Chem. 272, 9825-9832 (Pubitemid 27171648)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.15 , pp. 9825-9832
    • Han, Y.1    Brasier, A.R.2
  • 56
    • 0031897632 scopus 로고    scopus 로고
    • NF-κB and rel proteins: Evolutionarily conserved mediators of immune responses
    • DOI 10.1146/annurev.immunol.16.1.225
    • Ghosh, S., May, M. J., and Kopp, E. B. (1998) NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu. Rev.Immunol. 16, 225-260 (Pubitemid 28183365)
    • (1998) Annual Review of Immunology , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 57
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: The control of NF-κB activity
    • DOI 10.1146/annurev.immunol.18.1.621
    • Karin, M., and Ben-Neriah, Y. (2000) Phosphorylation meets ubiquitination: the control of NF-[kappa]B activity. Annu. Rev. Immunol. 18, 621-663 (Pubitemid 30365393)
    • (2000) Annual Review of Immunology , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 59
    • 0028967819 scopus 로고
    • Inducible nuclear expression of newly synthesized i kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B
    • Arenzana-Seisdedos, F., Thompson, J., Rodriguez, M. S., Bachelerie, F., Thomas, D., and Hay, R. T. (1995) Inducible nuclear expression of newly synthesized I kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B. Mol. Cell. Biol. 15, 2689-2696
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2689-2696
    • Arenzana-Seisdedos, F.1    Thompson, J.2    Rodriguez, M.S.3    Bachelerie, F.4    Thomas, D.5    Hay, R.T.6
  • 60
    • 0033953587 scopus 로고    scopus 로고
    • A nuclear export signal in the N-terminal regulatory domain of IκBα controls cytoplasmic localization of inactive NF-κB/IκBα complexes
    • DOI 10.1073/pnas.97.3.1014
    • Huang, T. T., Kudo, N., Yoshida, M., and Miyamoto, S. (2000) A nuclear export signal in the N-terminal regulatory domain of IkappaBalpha controls cytoplasmic localization of inactive NF-kappaB/IkappaBalpha complexes. Proc. Natl. Acad. Sci. U.S.A. 97, 1014-1019 (Pubitemid 30080804)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.3 , pp. 1014-1019
    • Huang, T.T.1    Kudo, N.2    Yoshida, M.3    Miyamoto, S.4
  • 61
    • 0017887029 scopus 로고
    • Inhibition of protein synthesis by double-stranded RNA and phosphorylation of initiation factor, eIF-2
    • Lenz, J. R., and Baglioni, C. (1978) Inhibition of protein synthesis by double-stranded RNA and phosphorylation of initiation factor, eIF-2. J. Biol. Chem. 253, 4219-4223 (Pubitemid 8380643)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.12 , pp. 4219-4223
    • Lenz, J.R.1    Baglioni, C.2
  • 62
    • 17944378526 scopus 로고    scopus 로고
    • Activation by IKKα of a second, evolutionary conserved, NF-κB signaling pathway
    • DOI 10.1126/science.1062677
    • Senftleben, U., Cao, Y., Xiao, G., Greten, F. R., Krahn, G., Bonizzi, G., Chen, Y., Hu, Y., Fong, A., Sun, S. C., and Karin, M. (2001) Activation by IKKalpha of a second, evolutionary conserved, NF-kappa B signaling pathway. Science 293, 1495-1499 (Pubitemid 32801552)
    • (2001) Science , vol.293 , Issue.5534 , pp. 1495-1499
    • Senftleben, U.1    Cao, Y.2    Xiao, G.3    Greten, F.R.4    Krahn, G.5    Bonizzi, G.6    Chen, Y.7    Hu, Y.8    Fong, A.9    Sun, S.-C.10    Karin, M.11
  • 63
    • 80054829921 scopus 로고    scopus 로고
    • Sources of cell-to-cell variability in canonical nuclear factor-kappaB (NF-kappaB) signaling pathway inferred from single cell dynamic images
    • Kalita, M. K., Sargsyan, K., Tian, B., Paulucci-Holthauzen, A., Najm, H. N., Debusschere, B. J., and Brasier, A. R. (2011) Sources of cell-to-cell variability in canonical nuclear factor-kappaB (NF-kappaB) signaling pathway inferred from single cell dynamic images. J. Biol. Chem. 286, 37741-37757
    • (2011) J. Biol. Chem. , vol.286 , pp. 37741-37757
    • Kalita, M.K.1    Sargsyan, K.2    Tian, B.3    Paulucci-Holthauzen, A.4    Najm, H.N.5    Debusschere, B.J.6    Brasier, A.R.7
  • 64
    • 33847112418 scopus 로고    scopus 로고
    • The NF-kappaB regulatory network
    • Brasier, A. R. (2006) The NF-kappaB regulatory network. Cardiovasc. Toxicol. 6, 111-130
    • (2006) Cardiovasc. Toxicol. , vol.6 , pp. 111-130
    • Brasier, A.R.1
  • 65
    • 0027168447 scopus 로고
    • NF-κB controls expression of inhibitor IκBα: Evidence for an inducible autoregulatory pathway
    • Sun, S. C., Ganchi, P. A., Ballard, D. W., and Greene, W. C. (1993) NFkappa B controls expression of inhibitor I kappa B alpha: evidence for an inducible autoregulatory pathway. Science 259, 1912-1915 (Pubitemid 23124465)
    • (1993) Science , vol.259 , Issue.5103 , pp. 1912-1915
    • Sun, S.-C.1    Ganchi, P.A.2    Ballard, D.W.3    Greene, W.C.4
  • 66
    • 34247341367 scopus 로고    scopus 로고
    • TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity
    • DOI 10.1038/nature05732, PII NATURE05732
    • Gack, M. U., Shin, Y. C., Joo, C. H., Urano, T., Liang, C., Sun, L., Takeuchi, O., Akira, S., Chen, Z., Inoue, S., and Jung, J. U. (2007) TRIM25 RINGfinger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity. Nature 446, 916-920 (Pubitemid 46633167)
    • (2007) Nature , vol.446 , Issue.7138 , pp. 916-920
    • Gack, M.U.1    Shin, Y.C.2    Joo, C.-H.3    Urano, T.4    Liang, C.5    Sun, L.6    Takeuchi, O.7    Akira, S.8    Chen, Z.9    Inoue, S.10    Jung, J.U.11
  • 68
    • 73549097331 scopus 로고    scopus 로고
    • The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS signaling pathway by targeting TRAF3 for degradation
    • Nakhaei, P., Mesplede, T., Solis, M., Sun, Q., Zhao, T., Yang, L., Chuang, T. H., Ware, C. F., Lin, R., and Hiscott, J. (2009) The E3 ubiquitin ligase Triad3A negatively regulates the RIG-I/MAVS signaling pathway by targeting TRAF3 for degradation. PLoS Pathog. 5, e1000650
    • (2009) PLoS Pathog , vol.5
    • Nakhaei, P.1    Mesplede, T.2    Solis, M.3    Sun, Q.4    Zhao, T.5    Yang, L.6    Chuang, T.H.7    Ware, C.F.8    Lin, R.9    Hiscott, J.10
  • 69
    • 84862094248 scopus 로고    scopus 로고
    • CD40 Stimulates A "feed-forward" NF-kappaB-driven molecular pathway that regulates IFN-beta expression in carcinoma cells
    • Moschonas, A., Ioannou, M., and Eliopoulos, A. G. (2012) CD40 stimulates a "feed-forward" NF-kappaB-driven molecular pathway that regulates IFN-beta expression in carcinoma cells. J. Immunol. 188, 5521-5527
    • (2012) J. Immunol. , vol.188 , pp. 5521-5527
    • Moschonas, A.1    Ioannou, M.2    Eliopoulos, A.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.