메뉴 건너뛰기




Volumn 13, Issue 22, 2013, Pages 3309-3326

Subcellular proteomic analysis of human host cells infected with H3N2 swine influenza virus

Author keywords

2DE; A549 cells; Interaction; Microbiology; Subcellular proteomics; Swine influenza

Indexed keywords

CYTOPLASM PROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN C; NONSTRUCTURAL PROTEIN 1; TRYPTOPHAN TRANSFER RNA LIGASE; PROTEIN; PROTEOME; TRANSCRIPTOME;

EID: 84888058998     PISSN: 16159853     EISSN: 16159861     Source Type: Journal    
DOI: 10.1002/pmic.201300180     Document Type: Article
Times cited : (28)

References (65)
  • 1
    • 22144490541 scopus 로고    scopus 로고
    • The threat of pandemic influenza: are we ready
    • Lemon, S. M., Mahmoud, A. A., The threat of pandemic influenza: are we ready? Biosecur. Bioterror. 2005, 3, 70-73.
    • (2005) Biosecur. Bioterror. , vol.3 , pp. 70-73
    • Lemon, S.M.1    Mahmoud, A.A.2
  • 2
    • 79957602568 scopus 로고    scopus 로고
    • Long-term evolution and transmission dynamics of swine influenza A virus
    • Vijaykrishna, D., Smith, G. J., Pybus, O. G., Zhu, H. et al., Long-term evolution and transmission dynamics of swine influenza A virus. Nature 2011, 473, 519-522.
    • (2011) Nature , vol.473 , pp. 519-522
    • Vijaykrishna, D.1    Smith, G.J.2    Pybus, O.G.3    Zhu, H.4
  • 3
    • 22944457912 scopus 로고    scopus 로고
    • Influenza: lessons from past pandemics, warnings from current incidents
    • Horimoto, T., Kawaoka, Y., Influenza: lessons from past pandemics, warnings from current incidents. Nat. Rev. Microbiol. 2005, 3, 591-600.
    • (2005) Nat. Rev. Microbiol. , vol.3 , pp. 591-600
    • Horimoto, T.1    Kawaoka, Y.2
  • 4
    • 0031457476 scopus 로고    scopus 로고
    • The impact of influenza epidemics on mortality: introducing a severity index
    • Simonsen, L., Clarke, M. J., Williamson, G. D., Stroup, D. F. et al., The impact of influenza epidemics on mortality: introducing a severity index. Am. J. Public Health 1997, 87, 1944-1950.
    • (1997) Am. J. Public Health , vol.87 , pp. 1944-1950
    • Simonsen, L.1    Clarke, M.J.2    Williamson, G.D.3    Stroup, D.F.4
  • 5
    • 0037425564 scopus 로고    scopus 로고
    • Mortality associated with influenza and respiratory syncytial virus in the United States
    • Thompson, W. W., Shay, D. K., Weintraub, E., Brammer, L. et al., Mortality associated with influenza and respiratory syncytial virus in the United States. JAMA 2003, 289, 179-186.
    • (2003) JAMA , vol.289 , pp. 179-186
    • Thompson, W.W.1    Shay, D.K.2    Weintraub, E.3    Brammer, L.4
  • 6
    • 66449099742 scopus 로고    scopus 로고
    • Unraveling the mystery of swine influenza virus
    • Wang, T. T., Palese, P., Unraveling the mystery of swine influenza virus. Cell 2009, 137, 983-985.
    • (2009) Cell , vol.137 , pp. 983-985
    • Wang, T.T.1    Palese, P.2
  • 7
    • 72249103485 scopus 로고    scopus 로고
    • A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection
    • Shapira, S. D., Gat-Viks, I., Shum, B. O., Dricot, A. et al., A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection. Cell 2009, 139, 1255-1267.
    • (2009) Cell , vol.139 , pp. 1255-1267
    • Shapira, S.D.1    Gat-Viks, I.2    Shum, B.O.3    Dricot, A.4
  • 8
    • 0037053093 scopus 로고    scopus 로고
    • The emergence of novel swine influenza viruses in North America
    • Olsen, C. W., The emergence of novel swine influenza viruses in North America. Virus Res. 2002, 85, 199-210.
    • (2002) Virus Res. , vol.85 , pp. 199-210
    • Olsen, C.W.1
  • 9
    • 43549083241 scopus 로고    scopus 로고
    • Proteomics analysis of differential expression of cellular proteins in response to avian H9N2 virus infection in human cells
    • Liu, N., Song, W., Wang, P., Lee, K. et al., Proteomics analysis of differential expression of cellular proteins in response to avian H9N2 virus infection in human cells. Proteomics 2008, 8, 1851-1858.
    • (2008) Proteomics , vol.8 , pp. 1851-1858
    • Liu, N.1    Song, W.2    Wang, P.3    Lee, K.4
  • 10
    • 77957192535 scopus 로고    scopus 로고
    • Quantitative proteomic analyses of influenza virus-infected cultured human lung cells
    • Coombs, K. M., Berard, A., Xu, W., Krokhin, O. et al., Quantitative proteomic analyses of influenza virus-infected cultured human lung cells. J. Virol. 2010, 84, 10888-10906.
    • (2010) J. Virol. , vol.84 , pp. 10888-10906
    • Coombs, K.M.1    Berard, A.2    Xu, W.3    Krokhin, O.4
  • 11
    • 67650713700 scopus 로고    scopus 로고
    • Quantitative analysis of cellular proteome alterations in human influenza A virus-infected mammalian cell lines
    • Vester, D., Rapp, E., Gade, D., Genzel, Y., Reichl, U., Quantitative analysis of cellular proteome alterations in human influenza A virus-infected mammalian cell lines. Proteomics 2009, 9, 3316-3327.
    • (2009) Proteomics , vol.9 , pp. 3316-3327
    • Vester, D.1    Rapp, E.2    Gade, D.3    Genzel, Y.4    Reichl, U.5
  • 12
    • 33750362127 scopus 로고    scopus 로고
    • Integrated molecular signature of disease: analysis of influenza virus-infected macaques through functional genomics and proteomics
    • Baas, T., Baskin, C. R., Diamond, D. L., Garcia-Sastre, A. et al., Integrated molecular signature of disease: analysis of influenza virus-infected macaques through functional genomics and proteomics. J. Virol. 2006, 80, 10813-10828.
    • (2006) J. Virol. , vol.80 , pp. 10813-10828
    • Baas, T.1    Baskin, C.R.2    Diamond, D.L.3    Garcia-Sastre, A.4
  • 13
    • 77954657137 scopus 로고    scopus 로고
    • Virus-host cell interactions in vaccine production cell lines infected with different human influenza A virus variants: a proteomic approach
    • Vester, D., Rapp, E., Kluge, S., Genzel, Y., Reichl, U., Virus-host cell interactions in vaccine production cell lines infected with different human influenza A virus variants: a proteomic approach. J. Proteomics 2010, 73, 1656-1669.
    • (2010) J. Proteomics , vol.73 , pp. 1656-1669
    • Vester, D.1    Rapp, E.2    Kluge, S.3    Genzel, Y.4    Reichl, U.5
  • 14
    • 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
    • Brasier, A. R., Spratt, H., Wu, Z., Boldogh, I. et al., 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. 2004, 78, 11461-11476.
    • (2004) J. Virol. , vol.78 , pp. 11461-11476
    • Brasier, A.R.1    Spratt, H.2    Wu, Z.3    Boldogh, I.4
  • 15
    • 66949149847 scopus 로고    scopus 로고
    • Actin and RIG-I/MAVS signaling components translocate to mitochondria upon influenza A virus infection of human primary macrophages
    • Ohman, T., Rintahaka, J., Kalkkinen, N., Matikainen, S., Nyman, T. A., Actin and RIG-I/MAVS signaling components translocate to mitochondria upon influenza A virus infection of human primary macrophages. J. Immunol. 2009, 182, 5682-5692.
    • (2009) J. Immunol. , vol.182 , pp. 5682-5692
    • Ohman, T.1    Rintahaka, J.2    Kalkkinen, N.3    Matikainen, S.4    Nyman, T.A.5
  • 17
    • 77956497028 scopus 로고    scopus 로고
    • Quantitative proteomics using stable isotope labeling with amino acids in cell culture reveals changes in the cytoplasmic, nuclear, and nucleolar proteomes in Vero cells infected with the coronavirus infectious bronchitis virus
    • Emmott, E., Rodgers, M. A., Macdonald, A., McCrory, S. et al., Quantitative proteomics using stable isotope labeling with amino acids in cell culture reveals changes in the cytoplasmic, nuclear, and nucleolar proteomes in Vero cells infected with the coronavirus infectious bronchitis virus. Mol. Cell. Proteomics 2010, 9, 1920-1936.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1920-1936
    • Emmott, E.1    Rodgers, M.A.2    Macdonald, A.3    McCrory, S.4
  • 18
    • 77957355995 scopus 로고    scopus 로고
    • Quantitative proteomics using SILAC coupled to LC-MS/MS reveals changes in the nucleolar proteome in influenza A virus-infected cells
    • Emmott, E., Wise, H., Loucaides, E. M., Matthews, D. A. et al., Quantitative proteomics using SILAC coupled to LC-MS/MS reveals changes in the nucleolar proteome in influenza A virus-infected cells. J. Proteome Res. 2010, 9, 5335-5345.
    • (2010) J. Proteome Res. , vol.9 , pp. 5335-5345
    • Emmott, E.1    Wise, H.2    Loucaides, E.M.3    Matthews, D.A.4
  • 19
    • 41549087403 scopus 로고    scopus 로고
    • Proteomics analysis of host cells infected with infectious bursal disease virus
    • Zheng, X. J., Hong, L. L., Shi, L. X., Guo, J. Q. et al., Proteomics analysis of host cells infected with infectious bursal disease virus. Mol. Cell. Proteomics 2008, 7, 612-625.
    • (2008) Mol. Cell. Proteomics , vol.7 , pp. 612-625
    • Zheng, X.J.1    Hong, L.L.2    Shi, L.X.3    Guo, J.Q.4
  • 20
    • 0033662168 scopus 로고    scopus 로고
    • A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry
    • Yan, J. X., Wait, R., Berkelman, T., Harry, R. A. et al., A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry. Electrophoresis 2000, 21, 3666-3672.
    • (2000) Electrophoresis , vol.21 , pp. 3666-3672
    • Yan, J.X.1    Wait, R.2    Berkelman, T.3    Harry, R.A.4
  • 21
    • 34249062964 scopus 로고    scopus 로고
    • The minimum information about a proteomics experiment (MIAPE)
    • Taylor, C. F., Paton, N. W., Lilley, K. S., Binz, P. A. et al., The minimum information about a proteomics experiment (MIAPE). Nat. Biotechnol. 2007, 25, 887-893.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 887-893
    • Taylor, C.F.1    Paton, N.W.2    Lilley, K.S.3    Binz, P.A.4
  • 22
    • 77957194867 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of A549 cells infected with human respiratory syncytial virus
    • Munday, D. C., Emmott, E., Surtees, R., Lardeau, C. H. et al., Quantitative proteomic analysis of A549 cells infected with human respiratory syncytial virus. Mol. Cell. Proteomics 2010, 9, 2438-2459.
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2438-2459
    • Munday, D.C.1    Emmott, E.2    Surtees, R.3    Lardeau, C.H.4
  • 23
    • 20944435993 scopus 로고    scopus 로고
    • Regulation of urokinase receptor mRNA stability by hnRNP C in lung epithelial cells
    • Shetty, S., Regulation of urokinase receptor mRNA stability by hnRNP C in lung epithelial cells. Mol. Cell. Biochem 2005, 272, 107-118.
    • (2005) Mol. Cell. Biochem , vol.272 , pp. 107-118
    • Shetty, S.1
  • 24
    • 0026740718 scopus 로고
    • Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box
    • Kiledjian, M., Dreyfuss, G., Primary structure and binding activity of the hnRNP U protein: binding RNA through RGG box. EMBO J. 1992, 11, 2655-2664.
    • (1992) EMBO J. , vol.11 , pp. 2655-2664
    • Kiledjian, M.1    Dreyfuss, G.2
  • 25
    • 0027159055 scopus 로고
    • Interferon inducibility of mammalian tryptophanyl-tRNA synthetase: new perspectives
    • Kisselev, L., Frolova, L., Haenni, A. L., Interferon inducibility of mammalian tryptophanyl-tRNA synthetase: new perspectives. Trends Biochem. Sci. 1993, 18, 263-267.
    • (1993) Trends Biochem. Sci. , vol.18 , pp. 263-267
    • Kisselev, L.1    Frolova, L.2    Haenni, A.L.3
  • 26
    • 77953114765 scopus 로고    scopus 로고
    • The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15
    • Durfee, L. A., Lyon, N., Seo, K., Huibregtse, J. M., The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15. Mol. Cell 2010, 38, 722-732.
    • (2010) Mol. Cell , vol.38 , pp. 722-732
    • Durfee, L.A.1    Lyon, N.2    Seo, K.3    Huibregtse, J.M.4
  • 27
    • 0036788192 scopus 로고    scopus 로고
    • Interferon-induced mx proteins: dynamin-like GTPases with antiviral activity
    • Haller, O., Kochs, G., Interferon-induced mx proteins: dynamin-like GTPases with antiviral activity. Traffic 2002, 3, 710-717.
    • (2002) Traffic , vol.3 , pp. 710-717
    • Haller, O.1    Kochs, G.2
  • 28
    • 42449086890 scopus 로고    scopus 로고
    • Interaction of heterogeneous nuclear ribonucleoprotein C1/C2 with a novel cis-regulatory element within p53 mRNA as a response to cytostatic drug treatment
    • Christian, K. J., Lang, M. A., Raffalli-Mathieu, F., Interaction of heterogeneous nuclear ribonucleoprotein C1/C2 with a novel cis-regulatory element within p53 mRNA as a response to cytostatic drug treatment. Mol. Pharmacol. 2008, 73, 1558-1567.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1558-1567
    • Christian, K.J.1    Lang, M.A.2    Raffalli-Mathieu, F.3
  • 29
    • 79952532839 scopus 로고    scopus 로고
    • Minute virus of mice (MVMp) infection and NS1 expression induce p53 independent apoptosis in transformed rat fibroblast cells
    • Mincberg, M., Gopas, J., Tal, J., Minute virus of mice (MVMp) infection and NS1 expression induce p53 independent apoptosis in transformed rat fibroblast cells. Virology 2011, 412, 233-243.
    • (2011) Virology , vol.412 , pp. 233-243
    • Mincberg, M.1    Gopas, J.2    Tal, J.3
  • 31
    • 0035863125 scopus 로고    scopus 로고
    • Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition
    • Gustin, K. E., Sarnow, P., Effects of poliovirus infection on nucleo-cytoplasmic trafficking and nuclear pore complex composition. EMBO J. 2001, 20, 240-249.
    • (2001) EMBO J. , vol.20 , pp. 240-249
    • Gustin, K.E.1    Sarnow, P.2
  • 32
    • 0031663258 scopus 로고    scopus 로고
    • Specific interaction of heterogeneous nuclear ribonucleoprotein particle U with the leader RNA sequence of vesicular stomatitis virus
    • Gupta, A. K., Drazba, J. A., Banerjee, A. K., Specific interaction of heterogeneous nuclear ribonucleoprotein particle U with the leader RNA sequence of vesicular stomatitis virus. J. Virol. 1998, 72, 8532-8540.
    • (1998) J. Virol. , vol.72 , pp. 8532-8540
    • Gupta, A.K.1    Drazba, J.A.2    Banerjee, A.K.3
  • 33
    • 54449099369 scopus 로고    scopus 로고
    • The multifunctional NS1 protein of influenza A viruses
    • Hale, B. G., Randall, R. E., Ortin, J., Jackson, D., The multifunctional NS1 protein of influenza A viruses. J. Gen. Virol. 2008, 89, 2359-2376.
    • (2008) J. Gen. Virol. , vol.89 , pp. 2359-2376
    • Hale, B.G.1    Randall, R.E.2    Ortin, J.3    Jackson, D.4
  • 34
    • 34249785982 scopus 로고    scopus 로고
    • Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes
    • Melen, K., Kinnunen, L., Fagerlund, R., Ikonen, N. et al., Nuclear and nucleolar targeting of influenza A virus NS1 protein: striking differences between different virus subtypes. J. Virol. 2007, 81, 5995-6006.
    • (2007) J. Virol. , vol.81 , pp. 5995-6006
    • Melen, K.1    Kinnunen, L.2    Fagerlund, R.3    Ikonen, N.4
  • 35
    • 77951226285 scopus 로고    scopus 로고
    • Nucleolar localization of influenza A NS1: striking differences between mammalian and avian cells
    • Volmer, R., Mazel-Sanchez, B., Volmer, C., Soubies, S. M., Guerin, J. L., Nucleolar localization of influenza A NS1: striking differences between mammalian and avian cells. Virol. J. 2010, 7, 63.
    • (2010) Virol. J. , vol.7 , pp. 63
    • Volmer, R.1    Mazel-Sanchez, B.2    Volmer, C.3    Soubies, S.M.4    Guerin, J.L.5
  • 36
    • 73949148579 scopus 로고    scopus 로고
    • Direct interaction of cellular hnRNP-F and NS1 of influenza A virus accelerates viral replication by modulation of viral transcriptional activity and host gene expression
    • Lee, J. H., Kim, S. H., Pascua, P. N., Song, M. S. et al., Direct interaction of cellular hnRNP-F and NS1 of influenza A virus accelerates viral replication by modulation of viral transcriptional activity and host gene expression. Virology 2010, 397, 89-99.
    • (2010) Virology , vol.397 , pp. 89-99
    • Lee, J.H.1    Kim, S.H.2    Pascua, P.N.3    Song, M.S.4
  • 37
    • 0027992089 scopus 로고
    • The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins
    • Gorlach, M., Burd, C. G., Dreyfuss, G., The determinants of RNA-binding specificity of the heterogeneous nuclear ribonucleoprotein C proteins. J. Biol. Chem. 1994, 269, 23074-23078.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23074-23078
    • Gorlach, M.1    Burd, C.G.2    Dreyfuss, G.3
  • 38
    • 0036337963 scopus 로고    scopus 로고
    • Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus
    • Gustin, K. E., Sarnow, P., Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus. J. Virol. 2002, 76, 8787-8796.
    • (2002) J. Virol. , vol.76 , pp. 8787-8796
    • Gustin, K.E.1    Sarnow, P.2
  • 39
    • 48349132088 scopus 로고    scopus 로고
    • Concomitant transitory up-regulation of X-linked inhibitor of apoptosis protein (XIAP) and the heterogeneous nuclear ribonucleoprotein C1-C2 in surviving cells during neuronal apoptosis
    • Spahn, A., Blondeau, N., Heurteaux, C., Dehghani, F., Rami, A., Concomitant transitory up-regulation of X-linked inhibitor of apoptosis protein (XIAP) and the heterogeneous nuclear ribonucleoprotein C1-C2 in surviving cells during neuronal apoptosis. Neurochem. Res. 2008, 33, 1859-1868.
    • (2008) Neurochem. Res. , vol.33 , pp. 1859-1868
    • Spahn, A.1    Blondeau, N.2    Heurteaux, C.3    Dehghani, F.4    Rami, A.5
  • 41
    • 78649644728 scopus 로고    scopus 로고
    • Quantitative proteomic analysis of A549 cells infected with human respiratory syncytial virus subgroup B using SILAC coupled to LC-MS/MS
    • Munday, D. C., Hiscox, J. A., Barr, J. N., Quantitative proteomic analysis of A549 cells infected with human respiratory syncytial virus subgroup B using SILAC coupled to LC-MS/MS. Proteomics 2010, 10, 4320-4334.
    • (2010) Proteomics , vol.10 , pp. 4320-4334
    • Munday, D.C.1    Hiscox, J.A.2    Barr, J.N.3
  • 42
    • 33748958673 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in hepatitis C virus infection
    • Piccoli, C., Scrima, R., D'Aprile, A., Ripoli, M. et al., Mitochondrial dysfunction in hepatitis C virus infection. Biochim. Biophys. Acta 2006, 1757, 1429-1437.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1429-1437
    • Piccoli, C.1    Scrima, R.2    D'Aprile, A.3    Ripoli, M.4
  • 43
    • 79551641146 scopus 로고    scopus 로고
    • Gene expression meta-analysis identifies VDAC1 as a predictor of poor outcome in early stage non-small cell lung cancer
    • Grills, C., Jithesh, P. V., Blayney, J., Zhang, S. D., Fennell, D. A., Gene expression meta-analysis identifies VDAC1 as a predictor of poor outcome in early stage non-small cell lung cancer. PLoS One 2011, 6, e14635.
    • (2011) PLoS One , vol.6
    • Grills, C.1    Jithesh, P.V.2    Blayney, J.3    Zhang, S.D.4    Fennell, D.A.5
  • 44
    • 38749097018 scopus 로고    scopus 로고
    • NLRX1 is a regulator of mitochondrial antiviral immunity
    • Moore, C. B., Bergstralh, D. T., Duncan, J. A., Lei, Y. et al., NLRX1 is a regulator of mitochondrial antiviral immunity. Nature 2008, 451, 573-577.
    • (2008) Nature , vol.451 , pp. 573-577
    • Moore, C.B.1    Bergstralh, D.T.2    Duncan, J.A.3    Lei, Y.4
  • 45
    • 80054772211 scopus 로고    scopus 로고
    • Structure-functions of HspB1 (Hsp27)
    • Arrigo, A. P., Structure-functions of HspB1 (Hsp27). Methods Mol. Biol. 2011, 787, 105-119.
    • (2011) Methods Mol. Biol. , vol.787 , pp. 105-119
    • Arrigo, A.P.1
  • 46
    • 2342651518 scopus 로고    scopus 로고
    • Molecular chaperones and the stress of oncogenesis
    • Mosser, D. D., Morimoto, R. I., Molecular chaperones and the stress of oncogenesis. Oncogene 2004, 23, 2907-2918.
    • (2004) Oncogene , vol.23 , pp. 2907-2918
    • Mosser, D.D.1    Morimoto, R.I.2
  • 47
    • 3042734117 scopus 로고    scopus 로고
    • Identification of cellular proteins modified in response to African swine fever virus infection by proteomics
    • Alfonso, P., Rivera, J., Hernaez, B., Alonso, C., Escribano, J. M., Identification of cellular proteins modified in response to African swine fever virus infection by proteomics. Proteomics 2004, 4, 2037-2046.
    • (2004) Proteomics , vol.4 , pp. 2037-2046
    • Alfonso, P.1    Rivera, J.2    Hernaez, B.3    Alonso, C.4    Escribano, J.M.5
  • 48
    • 33644863314 scopus 로고    scopus 로고
    • Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection
    • Leong, W. F., Chow, V. T., Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell. Microbiol. 2006, 8, 565-580.
    • (2006) Cell. Microbiol. , vol.8 , pp. 565-580
    • Leong, W.F.1    Chow, V.T.2
  • 49
    • 42449091104 scopus 로고    scopus 로고
    • IFP35 is involved in the antiviral function of interferon by association with the viral tas transactivator of bovine foamy virus
    • Tan, J., Qiao, W., Wang, J., Xu, F. et al., IFP35 is involved in the antiviral function of interferon by association with the viral tas transactivator of bovine foamy virus. J. Virol. 2008, 82, 4275-4283.
    • (2008) J. Virol. , vol.82 , pp. 4275-4283
    • Tan, J.1    Qiao, W.2    Wang, J.3    Xu, F.4
  • 50
    • 77951487843 scopus 로고    scopus 로고
    • New genetic associations detected in a host response study to hepatitis B vaccine
    • Davila, S., Froeling, F. E., Tan, A., Bonnard, C. et al., New genetic associations detected in a host response study to hepatitis B vaccine. Genes Immun. 2010, 11, 232-238.
    • (2010) Genes Immun. , vol.11 , pp. 232-238
    • Davila, S.1    Froeling, F.E.2    Tan, A.3    Bonnard, C.4
  • 51
    • 33947259324 scopus 로고    scopus 로고
    • The PH domain containing protein CKIP-1 binds to IFP35 and Nmi and is involved in cytokine signaling
    • Zhang, L., Tang, Y., Tie, Y., Tian, C. et al., The PH domain containing protein CKIP-1 binds to IFP35 and Nmi and is involved in cytokine signaling. Cell. Signal. 2007, 19, 932-944.
    • (2007) Cell. Signal. , vol.19 , pp. 932-944
    • Zhang, L.1    Tang, Y.2    Tie, Y.3    Tian, C.4
  • 52
    • 67650088521 scopus 로고    scopus 로고
    • Nmi (N-Myc interactor) inhibits Wnt/beta-catenin signaling and retards tumor growth
    • Fillmore, R. A., Mitra, A., Xi, Y., Ju, J. et al., Nmi (N-Myc interactor) inhibits Wnt/beta-catenin signaling and retards tumor growth. Int. J. Cancer 2009, 125, 556-564.
    • (2009) Int. J. Cancer , vol.125 , pp. 556-564
    • Fillmore, R.A.1    Mitra, A.2    Xi, Y.3    Ju, J.4
  • 53
    • 0032706379 scopus 로고    scopus 로고
    • Subcellular localization of interferon-inducible Myc/stat-interacting protein Nmi is regulated by a novel IFP 35 homologous domain
    • Lee, N. D., Chen, J., Shpall, R. L., Naumovski, L., Subcellular localization of interferon-inducible Myc/stat-interacting protein Nmi is regulated by a novel IFP 35 homologous domain. J. Interferon Cytokine Res. 1999, 19, 1245-1252.
    • (1999) J. Interferon Cytokine Res. , vol.19 , pp. 1245-1252
    • Lee, N.D.1    Chen, J.2    Shpall, R.L.3    Naumovski, L.4
  • 54
    • 0034647521 scopus 로고    scopus 로고
    • Interferon-alpha induces nmi-IFP35 heterodimeric complex formation that is affected by the phosphorylation of IFP35
    • Zhou, X., Liao, J., Meyerdierks, A., Feng, L. et al., Interferon-alpha induces nmi-IFP35 heterodimeric complex formation that is affected by the phosphorylation of IFP35. J. Biol. Chem. 2000, 275, 21364-21371.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21364-21371
    • Zhou, X.1    Liao, J.2    Meyerdierks, A.3    Feng, L.4
  • 55
    • 22844450969 scopus 로고    scopus 로고
    • Crystal structure of the interferon-induced ubiquitin-like protein ISG15
    • Narasimhan, J., Wang, M., Fu, Z., Klein, J. M. et al., Crystal structure of the interferon-induced ubiquitin-like protein ISG15. J. Biol. Chem. 2005, 280, 27356-27365.
    • (2005) J. Biol. Chem. , vol.280 , pp. 27356-27365
    • Narasimhan, J.1    Wang, M.2    Fu, Z.3    Klein, J.M.4
  • 56
    • 6344282196 scopus 로고    scopus 로고
    • Interferon-inducible ubiquitin E2, Ubc8, is a conjugating enzyme for protein ISGylation
    • Kim, K. I., Giannakopoulos, N. V., Virgin, H. W., Zhang, D. E., Interferon-inducible ubiquitin E2, Ubc8, is a conjugating enzyme for protein ISGylation. Mol. Cell. Biol. 2004, 24, 9592-9600.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9592-9600
    • Kim, K.I.1    Giannakopoulos, N.V.2    Virgin, H.W.3    Zhang, D.E.4
  • 57
    • 70349737879 scopus 로고    scopus 로고
    • The NS1 protein of the 1918 pandemic influenza virus blocks host interferon and lipid metabolism pathways
    • Billharz, R., Zeng, H., Proll, S. C., Korth, M. J. et al., The NS1 protein of the 1918 pandemic influenza virus blocks host interferon and lipid metabolism pathways. J. Virol. 2009, 83, 10557-10570.
    • (2009) J. Virol. , vol.83 , pp. 10557-10570
    • Billharz, R.1    Zeng, H.2    Proll, S.C.3    Korth, M.J.4
  • 58
    • 78651387047 scopus 로고    scopus 로고
    • Pandemic swine-origin H1N1 influenza A virus isolates show heterogeneous virulence in macaques
    • Safronetz, D., Rockx, B., Feldmann, F., Belisle, S. E. et al., Pandemic swine-origin H1N1 influenza A virus isolates show heterogeneous virulence in macaques. J. Virol. 2011, 85, 1214-1223.
    • (2011) J. Virol. , vol.85 , pp. 1214-1223
    • Safronetz, D.1    Rockx, B.2    Feldmann, F.3    Belisle, S.E.4
  • 59
    • 80655143492 scopus 로고    scopus 로고
    • pandemic H1N1 influenza virus causes disease and upregulation of genes related to inflammatory and immune responses, cell death, and lipid metabolism in pigs
    • Ma, W., Belisle, S. E., Mosier, D., Li, X. et al., 2009 pandemic H1N1 influenza virus causes disease and upregulation of genes related to inflammatory and immune responses, cell death, and lipid metabolism in pigs. J. Virol. 2011, 85, 11626-11637.
    • (2009) J. Virol. 2011 , vol.85 , pp. 11626-11637
    • Ma, W.1    Belisle, S.E.2    Mosier, D.3    Li, X.4
  • 60
    • 77954215846 scopus 로고    scopus 로고
    • Implications for lipids during replication of enveloped viruses
    • Chan, R. B., Tanner, L., Wenk, M. R., Implications for lipids during replication of enveloped viruses. Chem. Phys. Lipids 2010, 163, 449-459.
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 449-459
    • Chan, R.B.1    Tanner, L.2    Wenk, M.R.3
  • 61
    • 79959882330 scopus 로고    scopus 로고
    • Multifaceted roles for lipids in viral infection
    • Heaton, N. S., Randall, G., Multifaceted roles for lipids in viral infection. Trends Microbiol. 2011, 19, 368-375.
    • (2011) Trends Microbiol. , vol.19 , pp. 368-375
    • Heaton, N.S.1    Randall, G.2
  • 62
    • 65249110368 scopus 로고    scopus 로고
    • Molecular cloning and oxidative modification of human lens ALDH1A1: implication in impaired detoxification of lipid aldehydes
    • Xiao, T., Shoeb, M., Siddiqui, M. S., Zhang, M. et al., Molecular cloning and oxidative modification of human lens ALDH1A1: implication in impaired detoxification of lipid aldehydes. J. Toxicol. Environ. Health A 2009, 72, 577-584.
    • (2009) J. Toxicol. Environ. Health A , vol.72 , pp. 577-584
    • Xiao, T.1    Shoeb, M.2    Siddiqui, M.S.3    Zhang, M.4
  • 63
    • 79959817797 scopus 로고    scopus 로고
    • HSV-2 infection of dendritic cells amplifies a highly susceptible HIV-1 cell target
    • Martinelli, E., Tharinger, H., Frank, I., Arthos, J. et al., HSV-2 infection of dendritic cells amplifies a highly susceptible HIV-1 cell target. PLoS Pathog. 2011, 7, e1002109.
    • (2011) PLoS Pathog. , vol.7
    • Martinelli, E.1    Tharinger, H.2    Frank, I.3    Arthos, J.4
  • 64
    • 71249114040 scopus 로고    scopus 로고
    • Glucocorticoid-stimulated, transcription-independent release of annexin A1 by cochlear Hensen cells
    • Kalinec, F., Webster, P., Maricle, A., Guerrero, D. et al., Glucocorticoid-stimulated, transcription-independent release of annexin A1 by cochlear Hensen cells. Br. J. Pharmacol. 2009, 158, 1820-1834.
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 1820-1834
    • Kalinec, F.1    Webster, P.2    Maricle, A.3    Guerrero, D.4
  • 65
    • 0034826533 scopus 로고    scopus 로고
    • An annexin 1 (ANXA1)-derived peptide inhibits prototype antigen-driven human T cell Th1 and Th2 responses in vitro
    • Kamal, A. M., Smith, S. F., De Silva Wijayasinghe, M., Solito, E., Corrigan, C. J., An annexin 1 (ANXA1)-derived peptide inhibits prototype antigen-driven human T cell Th1 and Th2 responses in vitro. Clin. Exp. Allergy 2001, 31, 1116-1125.
    • (2001) Clin. Exp. Allergy , vol.31 , pp. 1116-1125
    • Kamal, A.M.1    Smith, S.F.2    De Silva Wijayasinghe, M.3    Solito, E.4    Corrigan, C.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.