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Volumn 9, Issue 4, 2014, Pages

Alteration of protein levels during influenza virus H1N1 infection in host cells: A proteomic survey of host and virus reveals differential dynamics

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; PROTEOME; VIRUS PROTEIN;

EID: 84899510608     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0094257     Document Type: Article
Times cited : (35)

References (87)
  • 1
    • 70349466529 scopus 로고    scopus 로고
    • Population context determines cell-to-cell variability in endocytosis and virus infection
    • Snijder B, Sacher R, Ramo P, Damm EM, Liberali P, et al. (2009) Population context determines cell-to-cell variability in endocytosis and virus infection. Nature 461: 520-523.
    • (2009) Nature , vol.461 , pp. 520-523
    • Snijder, B.1    Sacher, R.2    Ramo, P.3    Damm, E.M.4    Liberali, P.5
  • 2
    • 0036210827 scopus 로고    scopus 로고
    • The influenza virus nucleoprotein: A multifunctional RNA-binding protein pivotal to virus replication
    • Portela A, Digard P (2002) The influenza virus nucleoprotein: a multifunctional RNA-binding protein pivotal to virus replication. J Gen Virol 83: 723-734. (Pubitemid 34284855)
    • (2002) Journal of General Virology , vol.83 , Issue.4 , pp. 723-734
    • Portela, A.1    Digard, P.2
  • 3
    • 0028274131 scopus 로고
    • The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear export of mRNAs containing poly(A)
    • Qiu Y, Krug RM (1994) The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear export of mRNAs containing poly(A). J Virol 68: 2425-2432. (Pubitemid 24091922)
    • (1994) Journal of Virology , vol.68 , Issue.4 , pp. 2425-2432
    • Qiu, Y.1    Krug, R.M.2
  • 4
    • 0026089363 scopus 로고
    • Regulation of the Extent of Splicing of Influenza Virus NS1 mRNA: Role of the Rates of Splicing and of the Nucleocytoplasmic Transport of NS1 mRNA
    • Alonso-Caplen FV, Krug RM (1991) Regulation of the extent of splicing of influenza virus NS1 mRNA: role of the rates of splicing and of the nucleocytoplasmic transport of NS1 mRNA. Mol Cell Biol 11: 1092-1098. (Pubitemid 21895460)
    • (1991) Molecular and Cellular Biology , vol.11 , Issue.2 , pp. 1092-1098
    • Alonso-Caplen, F.V.1    Krug, R.M.2
  • 5
    • 0023155247 scopus 로고
    • Influenza virus gene expression: Control mechanisms at early and late times of infection and nuclear-cytoplasmic transport of virus-specific RNAs
    • Shapiro GI, Gurney T Jr, Krug RM (1987) Influenza virus gene expression: control mechanisms at early and late times of infection and nuclear-cytoplasmic transport of virus-specific RNAs. J Virol 61: 764-773. (Pubitemid 17040204)
    • (1987) Journal of Virology , vol.61 , Issue.3 , pp. 764-773
    • Shapiro, G.I.1    Gurney Jr., T.2    Krug, R.M.3
  • 6
    • 84862777909 scopus 로고    scopus 로고
    • Suppression of the antiviral response by an influenza histone mimic
    • Marazzi I, Ho JS, Kim J, Manicassamy B, Dewell S, et al. (2012) Suppression of the antiviral response by an influenza histone mimic. Nature 483: 428-433.
    • (2012) Nature , vol.483 , pp. 428-433
    • Marazzi, I.1    Ho, J.S.2    Kim, J.3    Manicassamy, B.4    Dewell, S.5
  • 7
    • 76749108989 scopus 로고    scopus 로고
    • Human host factors required for influenza virus replication
    • Konig R, Stertz S, Zhou Y, Inoue A, Hoffmann HH, et al. (2010) Human host factors required for influenza virus replication. Nature 463: 813-817.
    • (2010) Nature , vol.463 , pp. 813-817
    • Konig, R.1    Stertz, S.2    Zhou, Y.3    Inoue, A.4    Hoffmann, H.H.5
  • 8
    • 76749090540 scopus 로고    scopus 로고
    • Genome-wide RNAi screen identifies human host factors crucial for influenza virus replication
    • Karlas A, Machuy N, Shin Y, Pleissner KP, Artarini A, et al. (2010) Genome-wide RNAi screen identifies human host factors crucial for influenza virus replication. Nature 463: 818-822.
    • (2010) Nature , vol.463 , pp. 818-822
    • Karlas, A.1    Machuy, N.2    Shin, Y.3    Pleissner, K.P.4    Artarini, A.5
  • 9
    • 51649095289 scopus 로고    scopus 로고
    • RNA interference screen for human genes associated with West Nile virus infection
    • Krishnan MN, Ng A, Sukumaran B, Gilfoy FD, Uchil PD, et al. (2008) RNA interference screen for human genes associated with West Nile virus infection. Nature 455: 242-245.
    • (2008) Nature , vol.455 , pp. 242-245
    • Krishnan, M.N.1    Ng, A.2    Sukumaran, B.3    Gilfoy, F.D.4    Uchil, P.D.5
  • 10
    • 72549116887 scopus 로고    scopus 로고
    • The IFITM proteins mediate cellular resistance to influenza A H1N1 virus, West Nile virus, and dengue virus
    • Brass AL, Huang IC, Benita Y, John SP, Krishnan MN, et al. (2009) The IFITM proteins mediate cellular resistance to influenza A H1N1 virus, West Nile virus, and dengue virus. Cell 139: 1243-1254.
    • (2009) Cell , vol.139 , pp. 1243-1254
    • Brass, A.L.1    Huang, I.C.2    Benita, Y.3    John, S.P.4    Krishnan, M.N.5
  • 11
    • 72249103485 scopus 로고    scopus 로고
    • A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection
    • Shapira SD, Gat-Viks I, Shum BO, Dricot A, de Grace MM, et al. (2009) A physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infection. Cell 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    De Grace, M.M.5
  • 13
    • 84879414041 scopus 로고    scopus 로고
    • Systems virology: Host-directed approaches to viral pathogenesis and drug targeting
    • Law GL, Korth MJ, Benecke AG, Katze MG (2013) Systems virology: host-directed approaches to viral pathogenesis and drug targeting. Nat Rev Microbiol 11: 455-466.
    • (2013) Nat Rev Microbiol , vol.11 , pp. 455-466
    • Law, G.L.1    Korth, M.J.2    Benecke, A.G.3    Katze, M.G.4
  • 14
    • 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 EM, Matthews DA, Digard P, et al. (2010) Quantitative proteomics using SILAC coupled to LC-MS/MS reveals changes in the nucleolar proteome in influenza A virus-infected cells. J Proteome Res 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    Digard, P.5
  • 15
    • 80054964202 scopus 로고    scopus 로고
    • Predicting the pathogenesis of influenza from genomic response: A step toward early diagnosis
    • Bortz E, Garcia-Sastre A (2011) Predicting the pathogenesis of influenza from genomic response: a step toward early diagnosis. Genome Med 3: 67.
    • (2011) Genome Med , vol.3 , pp. 67
    • Bortz, E.1    Garcia-Sastre, A.2
  • 16
    • 79958048266 scopus 로고    scopus 로고
    • Quantitative subcellular proteome and secretome profiling of influenza A virus-infected human primary macrophages
    • Lietzen N, Ohman T, Rintahaka J, Julkunen I, Aittokallio T, et al. (2011) Quantitative subcellular proteome and secretome profiling of influenza A virus-infected human primary macrophages. PLoS Pathog 7: e1001340.
    • (2011) PLoS Pathog , vol.7
    • Lietzen, N.1    Ohman, T.2    Rintahaka, J.3    Julkunen, I.4    Aittokallio, T.5
  • 17
    • 77957192535 scopus 로고    scopus 로고
    • Quantitative proteomic analyses of influenza virus-infected cultured human lung cells
    • Coombs KM, Berard A, Xu W, Krokhin O, Meng X, et al. (2010) Quantitative proteomic analyses of influenza virus-infected cultured human lung cells. J Virol 84: 10888-10906.
    • (2010) J Virol , vol.84 , pp. 10888-10906
    • Coombs, K.M.1    Berard, A.2    Xu, W.3    Krokhin, O.4    Meng, X.5
  • 18
    • 84879986129 scopus 로고    scopus 로고
    • Influenza A Infection of Primary Human Airway Epithelial Cells Up-Regulates Proteins Related to Purine Metabolism and Ubiquitin-Related Signaling
    • Kroeker AL, Ezzati P, Coombs KM, Halayko AJ (2013) Influenza A Infection of Primary Human Airway Epithelial Cells Up-Regulates Proteins Related to Purine Metabolism and Ubiquitin-Related Signaling. Journal of Proteome Research 12: 3139-3151.
    • (2013) Journal of Proteome Research , vol.12 , pp. 3139-3151
    • Kroeker, A.L.1    Ezzati, P.2    Coombs, K.M.3    Halayko, A.J.4
  • 19
    • 84861125134 scopus 로고    scopus 로고
    • A quantitative proteomic analysis of lung epithelial (A549) cells infected with 2009 pandemic influenza A virus using stable isotope labelling with amino acids in cell culture
    • Dove BK, Surtees R, Bean TJH, Munday D, Wise HM, et al. (2012) A quantitative proteomic analysis of lung epithelial (A549) cells infected with 2009 pandemic influenza A virus using stable isotope labelling with amino acids in cell culture. Proteomics 12: 1431-1436.
    • (2012) Proteomics , vol.12 , pp. 1431-1436
    • Dove, B.K.1    Surtees, R.2    Bean, T.J.H.3    Munday, D.4    Wise, H.M.5
  • 20
    • 33744904964 scopus 로고    scopus 로고
    • Mutations in influenza virus M1 CCHH, the putative zinc finger motif, cause attenuation in mice and protect mice against lethal influenza virus infection
    • DOI 10.1128/JVI.02729-05
    • Hui EK, Smee DF, Wong MH, Nayak DP (2006) Mutations in influenza virus M1 CCHH, the putative zinc finger motif, cause attenuation in mice and protect mice against lethal influenza virus infection. J Virol 80: 5697-5707. (Pubitemid 43849147)
    • (2006) Journal of Virology , vol.80 , Issue.12 , pp. 5697-5707
    • Hui, E.K.-W.1    Smee, D.F.2    Wong, M.-H.3    Nayak, D.P.4
  • 21
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Mann S-EOM (2006) A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nature Protocols 1: 2650
    • (2006) Nature Protocols , vol.1 , pp. 2650
    • Mann, S.-E.1
  • 22
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong SE, Blagoev B, Kratchmarova I, Kristensen DB, Steen H, et al. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol Cell Proteomics 1: 376-386.
    • (2002) Mol Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5
  • 23
    • 33644675365 scopus 로고    scopus 로고
    • Stable isotope labeling with amino acids in cell culture (SILAC) for studying dynamics of protein abundance and posttranslational modifications
    • Amanchy R, Kalume DE, Pandey A (2005) Stable isotope labeling with amino acids in cell culture (SILAC) for studying dynamics of protein abundance and posttranslational modifications. Sci STKE 2005: pl2.
    • (2005) Sci STKE , vol.2005
    • Amanchy, R.1    Kalume, D.E.2    Pandey, A.3
  • 24
    • 0021767950 scopus 로고
    • Studies on the adaptation of influenza viruses to MDCK cells
    • Rott R, Orlich M, Klenk HD, Wang ML, Skehel JJ, et al. (1984) Studies on the adaptation of influenza viruses to MDCK cells. EMBO J 3: 3329-3332.
    • (1984) EMBO J , vol.3 , pp. 3329-3332
    • Rott, R.1    Orlich, M.2    Klenk, H.D.3    Wang, M.L.4    Skehel, J.J.5
  • 25
    • 59449085150 scopus 로고    scopus 로고
    • Global analysis of cellular protein translation by pulsed SILAC
    • Schwanhausser B, Gossen M, Dittmar G, Selbach M (2009) Global analysis of cellular protein translation by pulsed SILAC. Proteomics 9: 205-209.
    • (2009) Proteomics , vol.9 , pp. 205-209
    • Schwanhausser, B.1    Gossen, M.2    Dittmar, G.3    Selbach, M.4
  • 26
    • 36048949060 scopus 로고    scopus 로고
    • Lipid raft disruption by cholesterol depletion enhances influenza A virus budding from MDCK cells
    • DOI 10.1128/JVI.00835-07
    • Barman S, Nayak DP (2007) Lipid raft disruption by cholesterol depletion enhances influenza A virus budding from MDCK cells. J Virol 81: 12169-12178. (Pubitemid 350085832)
    • (2007) Journal of Virology , vol.81 , Issue.22 , pp. 12169-12178
    • Barman, S.1    Nayak, D.P.2
  • 27
    • 0037225270 scopus 로고    scopus 로고
    • Influenza a virus hemagglutinin containing basolateral localization signal does not alter the apical budding of a recombinant influenza a virus in polarized MDCK cells
    • DOI 10.1006/viro.2002.1731
    • Barman S, Adhikary L, Kawaoka Y, Nayak DP (2003) Influenza A virus hemagglutinin containing basolateral localization signal does not alter the apical budding of a recombinant influenza A virus in polarized MDCK cells. Virology 305: 138-152. (Pubitemid 36062819)
    • (2003) Virology , vol.305 , Issue.1 , pp. 138-152
    • Barman, S.1    Adhikary, L.2    Kawaoka, Y.3    Nayak, D.P.4
  • 28
    • 77952065243 scopus 로고    scopus 로고
    • Metabolic effects of influenza virus infection in cultured animal cells: Intra- and extracellular metabolite profiling
    • Ritter JB, Wahl AS, Freund S, Genzel Y, Reichl U (2010) Metabolic effects of influenza virus infection in cultured animal cells: Intra- and extracellular metabolite profiling. BMC Syst Biol 4: 61.
    • (2010) BMC Syst Biol , vol.4 , pp. 61
    • Ritter, J.B.1    Wahl, A.S.2    Freund, S.3    Genzel, Y.4    Reichl, U.5
  • 29
    • 0032484479 scopus 로고    scopus 로고
    • The M1 and M2 proteins of influenza a virus are important determinants in filamentous particle formation
    • DOI 10.1006/viro.1997.8916
    • Roberts PC, Lamb RA, Compans RW (1998) The M1 and M2 proteins of influenza A virus are important determinants in filamentous particle formation. Virology 240: 127-137. (Pubitemid 28394131)
    • (1998) Virology , vol.240 , Issue.1 , pp. 127-137
    • Roberts, P.C.1    Lamb, R.A.2    Compans, R.W.3
  • 30
    • 0030830205 scopus 로고    scopus 로고
    • Influenza virus NS1 protein interacts with viral transcription- replication complexes in vivo
    • Marion RM, Zurcher T, de la Luna S, Ortin J (1997) Influenza virus NS1 protein interacts with viral transcription-replication complexes in vivo. J Gen Virol 78 (Pt 10): 2447-2451. (Pubitemid 27469985)
    • (1997) Journal of General Virology , vol.78 , Issue.10 , pp. 2447-2451
    • Marion, R.Ma.1    Zurcher, T.2    De La, L.S.3    Ortin, J.4
  • 31
    • 0032086357 scopus 로고    scopus 로고
    • Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3′ end formation of cellular pre-mRNAs
    • Nemeroff ME, Barabino SM, Li Y, Keller W, Krug RM (1998) Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3′end formation of cellular pre-mRNAs. Mol Cell 1: 991-1000. (Pubitemid 128379260)
    • (1998) Molecular Cell , vol.1 , Issue.7 , pp. 991-1000
    • Nemeroff, M.E.1    Barabino, S.M.L.2    Li, Y.3    Keller, W.4    Krug, R.M.5
  • 32
    • 0033560753 scopus 로고    scopus 로고
    • Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3'-end processing machinery
    • Chen Z, Li Y, Krug RM (1999) Influenza A virus NS1 protein targets poly(A)-binding protein II of the cellular 3′-end processing machinery. EMBO J 18: 2273-2283. (Pubitemid 29179183)
    • (1999) EMBO Journal , vol.18 , Issue.8 , pp. 2273-2283
    • Chen, Z.1    Li, Y.2    Krug, R.M.3
  • 33
    • 0028923921 scopus 로고
    • Influenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs
    • de la Luna S, Fortes P, Beloso A, Ortin J (1995) Influenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs. J Virol 69: 2427-2433.
    • (1995) J Virol , vol.69 , pp. 2427-2433
    • De La Luna, S.1    Fortes, P.2    Beloso, A.3    Ortin, J.4
  • 34
    • 34250355170 scopus 로고    scopus 로고
    • Biology of influenza a virus
    • DOI 10.1196/annals.1408.001, Biology of Emerging Viruses: SARS, Avian and Human Influenza, Metapneumovirus, Nipah, West Nile, and Ross River Virus
    • Cheung TK, Poon LL (2007) Biology of influenza a virus. Ann N Y Acad Sci 1102: 1-25. (Pubitemid 47084906)
    • (2007) Annals of the New York Academy of Sciences , vol.1102 , pp. 1-25
    • Cheung, T.K.W.1    Poon, L.L.M.2
  • 37
    • 0028847292 scopus 로고
    • Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-2 translation initiation factor
    • Lu Y, Wambach M, Katze MG, Krug RM (1995) Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-2 translation initiation factor. Virology 214: 222-228.
    • (1995) Virology , vol.214 , pp. 222-228
    • Lu, Y.1    Wambach, M.2    Katze, M.G.3    Krug, R.M.4
  • 38
    • 79958838725 scopus 로고    scopus 로고
    • Influenza A virus nucleoprotein exploits Hsp40 to inhibit PKR activation
    • Sharma K, Tripathi S, Ranjan P, Kumar P, Garten R, et al. (2011) Influenza A virus nucleoprotein exploits Hsp40 to inhibit PKR activation. PLoS One 6: e20215.
    • (2011) PLoS One , vol.6
    • Sharma, K.1    Tripathi, S.2    Ranjan, P.3    Kumar, P.4    Garten, R.5
  • 39
    • 0032472328 scopus 로고    scopus 로고
    • The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins
    • DOI 10.1093/emboj/17.1.288
    • O'Neill RE, Talon J, Palese P (1998) The influenza virus NEP (NS2 protein) mediates the nuclear export of viral ribonucleoproteins. EMBO J 17:288-296. (Pubitemid 28041069)
    • (1998) EMBO Journal , vol.17 , Issue.1 , pp. 288-296
    • O'Neill, R.E.1    Talon, J.2    Palese, P.3
  • 41
    • 77956536783 scopus 로고    scopus 로고
    • Influenza A virus polymerase: Structural insights into replication and host adaptation mechanisms
    • Boivin S, Cusack S, Ruigrok RW, Hart DJ (2010) Influenza A virus polymerase: structural insights into replication and host adaptation mechanisms. J Biol Chem 285: 28411-28417.
    • (2010) J Biol Chem , vol.285 , pp. 28411-28417
    • Boivin, S.1    Cusack, S.2    Ruigrok, R.W.3    Hart, D.J.4
  • 42
    • 0029069869 scopus 로고
    • Identification of an RNA binding region within the N-terminal third of the influenza A virus nucleoprotein
    • Albo C, Valencia A, Portela A (1995) Identification of an RNA binding region within the N-terminal third of the influenza A virus nucleoprotein. J Virol 69: 3799-3806.
    • (1995) J Virol , vol.69 , pp. 3799-3806
    • Albo, C.1    Valencia, A.2    Portela, A.3
  • 43
    • 0028275669 scopus 로고
    • Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent
    • Baudin F, Bach C, Cusack S, Ruigrok RW (1994) Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent. EMBO J 13: 3158-3165. (Pubitemid 24213467)
    • (1994) EMBO Journal , vol.13 , Issue.13 , pp. 3158-3165
    • Baudin, F.1    Bach, C.2    Cusack, S.3    Ruigrok, R.W.H.4
  • 44
    • 0023948949 scopus 로고
    • Influenza virus RNA replication in vitro: Synthesis of viral template RNAs and virion RNAs in the absence of an added primer
    • Shapiro GI, Krug RM (1988) Influenza virus RNA replication in vitro: synthesis of viral template RNAs and virion RNAs in the absence of an added primer. J Virol 62: 2285-2290.
    • (1988) J Virol , vol.62 , pp. 2285-2290
    • Shapiro, G.I.1    Krug, R.M.2
  • 45
    • 0035450255 scopus 로고    scopus 로고
    • Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export
    • DOI 10.1006/viro.2001.1067
    • Huang X, Liu T, Muller J, Levandowski RA, Ye Z (2001) Effect of influenza virus matrix protein and viral RNA on ribonucleoprotein formation and nuclear export. Virology 287: 405-416. (Pubitemid 32804025)
    • (2001) Virology , vol.287 , Issue.2 , pp. 405-416
    • Huang, X.1    Liu, T.2    Muller, J.3    Levandowski, R.A.4    Ye, Z.5
  • 46
    • 0034671826 scopus 로고    scopus 로고
    • Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1
    • DOI 10.1093/emboj/19.24.6751
    • Neumann G, Hughes MT, Kawaoka Y (2000) Influenza A virus NS2 protein mediates vRNP nuclear export through NES-independent interaction with hCRM1. EMBO J 19: 6751-6758. (Pubitemid 32011668)
    • (2000) EMBO Journal , vol.19 , Issue.24 , pp. 6751-6758
    • Neumann, G.1    Hughes, M.T.2    Kawaoka, Y.3
  • 47
    • 0030991137 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape
    • DOI 10.1093/emboj/16.6.1236
    • Jin H, Leser GP, Zhang J, Lamb RA (1997) Influenza virus hemagglutinin and neuraminidase cytoplasmic tails control particle shape. EMBO J 16: 1236-1247. (Pubitemid 27136090)
    • (1997) EMBO Journal , vol.16 , Issue.6 , pp. 1236-1247
    • Jin, H.1    Leser, G.P.2    Zhang, J.3    Lamb, R.A.4
  • 48
    • 34250792678 scopus 로고    scopus 로고
    • Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles
    • DOI 10.1128/JVI.00361-07
    • Chen BJ, Leser GP, Morita E, Lamb RA (2007) Influenza virus hemagglutinin and neuraminidase, but not the matrix protein, are required for assembly and budding of plasmid-derived virus-like particles. J Virol 81: 7111-7123. (Pubitemid 46986647)
    • (2007) Journal of Virology , vol.81 , Issue.13 , pp. 7111-7123
    • Chen, B.J.1    Leser, G.P.2    Morita, E.3    Lamb, R.A.4
  • 49
    • 9644283009 scopus 로고    scopus 로고
    • Assembly and budding of influenza virus
    • DOI 10.1016/j.virusres.2004.08.012, PII S0168170204003235
    • Nayak DP, Hui EK, Barman S (2004) Assembly and budding of influenza virus. Virus Res 106: 147-165. (Pubitemid 39572961)
    • (2004) Virus Research , vol.106 , Issue.2 SPEC.ISS. , pp. 147-165
    • Nayak, D.P.1    Hui, E.K.-W.2    Barman, S.3
  • 50
    • 0001178028 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • Lamb RAK, Krug RM (1996) Orthomyxoviridae: The viruses and their replication. In Fields Virology 3: 1353-1445.
    • (1996) Fields Virology , vol.3 , pp. 1353-1445
    • Lamb, R.A.K.1    Krug, R.M.2
  • 51
    • 22544432531 scopus 로고    scopus 로고
    • Noise-robust soft clustering of gene expression time-course data
    • DOI 10.1142/S0219720005001375, PII S0219720005001375
    • Futschik ME, Carlisle B (2005) Noise-robust soft clustering of gene expression time-course data. Journal of bioinformatics and computational biology 3: 965-988. (Pubitemid 41015297)
    • (2005) Journal of Bioinformatics and Computational Biology , vol.3 , Issue.4 , pp. 965-988
    • Futschik, M.E.1    Carlisle, B.2
  • 53
    • 0033982936 scopus 로고    scopus 로고
    • KEGG: Kyoto Encyclopedia of Genes and Genomes
    • Kanehisa M (2000) KEGG: Kyoto Encyclopedia of Genes and Genomes. Nucleic Acids Research 28: 27-30.
    • (2000) Nucleic Acids Research , vol.28 , pp. 27-30
    • Kanehisa, M.1
  • 54
    • 0030589648 scopus 로고    scopus 로고
    • Surprising function of the three influenza viral polymerase proteins: Selective protection of viral mRNAs against the cap-snatching reaction catalyzed by the same polymerase proteins
    • Shih SR, Krug RM (1996) Surprising function of the three influenza viral polymerase proteins: selective protection of viral mRNAs against the cap-snatching reaction catalyzed by the same polymerase proteins. Virology 226: 430-435.
    • (1996) Virology , vol.226 , pp. 430-435
    • Shih, S.R.1    Krug, R.M.2
  • 55
    • 79956322553 scopus 로고    scopus 로고
    • Global quantification of mammalian gene expression control
    • Schwanhausser B, Busse D, Li N, Dittmar G, Schuchhardt J, et al. (2011) Global quantification of mammalian gene expression control. Nature 473: 337-342.
    • (2011) Nature , vol.473 , pp. 337-342
    • Schwanhausser, B.1    Busse, D.2    Li, N.3    Dittmar, G.4    Schuchhardt, J.5
  • 56
    • 0036401535 scopus 로고    scopus 로고
    • A functional link between the actin cytoskeleton and lipid rafts during budding of filamentous influenza virions
    • DOI 10.1006/viro.2002.1595
    • Simpson-Holley M, Ellis D, Fisher D, Elton D, McCauley J, et al. (2002) A functional link between the actin cytoskeleton and lipid rafts during budding of filamentous influenza virions. Virology 301: 212-225. (Pubitemid 35176546)
    • (2002) Virology , vol.301 , Issue.2 , pp. 212-225
    • Simpson-Holley, M.1    Ellis, D.2    Fisher, D.3    Elton, D.4    McCauley, J.5    Digard, P.6
  • 57
  • 58
    • 0030440695 scopus 로고    scopus 로고
    • Identification of host factors that regulate the influenza virus RNA polymerase activity
    • DOI 10.1016/S0300-9084(97)86736-3
    • Momose F, Handa H, Nagata K (1996) Identification of host factors that regulate the influenza virus RNA polymerase activity. Biochimie 78: 1103-1108. (Pubitemid 27193133)
    • (1996) Biochimie , vol.78 , Issue.11-12 , pp. 1103-1108
    • Momose, F.1    Handa, H.2    Nagata, K.3
  • 59
    • 80054743835 scopus 로고    scopus 로고
    • Effect of sorafenib on the energy metabolism of hepatocellular carcinoma cells
    • Fiume L, Manerba M, Vettraino M, Di Stefano G (2011) Effect of sorafenib on the energy metabolism of hepatocellular carcinoma cells. Eur J Pharmacol 670: 39-43.
    • (2011) Eur J Pharmacol , vol.670 , pp. 39-43
    • Fiume, L.1    Manerba, M.2    Vettraino, M.3    Di Stefano, G.4
  • 60
    • 77952509221 scopus 로고    scopus 로고
    • Glycolysis links p53 function with NF-kappaB signaling: Impact on cancer and aging process
    • Salminen A, Kaarniranta K (2010) Glycolysis links p53 function with NF-kappaB signaling: impact on cancer and aging process. J Cell Physiol 224: 1-6.
    • (2010) J Cell Physiol , vol.224 , pp. 1-6
    • Salminen, A.1    Kaarniranta, K.2
  • 61
    • 70349464738 scopus 로고    scopus 로고
    • Advanced glycation end product accumulation in rho(0) cells without a functional respiratory chain
    • Nass N, Kukat A, Seibel P, Bromme HJ, Schinzel R, et al. (2009) Advanced glycation end product accumulation in rho(0) cells without a functional respiratory chain. Biol Chem 390: 915-919.
    • (2009) Biol Chem , vol.390 , pp. 915-919
    • Nass, N.1    Kukat, A.2    Seibel, P.3    Bromme, H.J.4    Schinzel, R.5
  • 62
    • 0024438704 scopus 로고
    • Enhanced erythropoietin secretion in hepatoblastoma cells in response to hypoxia
    • Ueno M, Seferynska I, Beckman B, Brookins J, Nakashima J, et al. (1989) Enhanced erythropoietin secretion in hepatoblastoma cells in response to hypoxia. Am J Physiol 257: C743-749.
    • (1989) Am J Physiol , vol.257
    • Ueno, M.1    Seferynska, I.2    Beckman, B.3    Brookins, J.4    Nakashima, J.5
  • 63
    • 63049110388 scopus 로고    scopus 로고
    • Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions
    • Pan C, Kumar C, Bohl S, Klingmueller U, Mann M (2009) Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions. Mol Cell Proteomics 8: 443-450.
    • (2009) Mol Cell Proteomics , vol.8 , pp. 443-450
    • Pan, C.1    Kumar, C.2    Bohl, S.3    Klingmueller, U.4    Mann, M.5
  • 65
    • 77956528167 scopus 로고    scopus 로고
    • Cellular networks involved in the influenza virus life cycle
    • Watanabe T, Watanabe S, Kawaoka Y (2010) Cellular networks involved in the influenza virus life cycle. Cell Host Microbe 7: 427-439.
    • (2010) Cell Host Microbe , vol.7 , pp. 427-439
    • Watanabe, T.1    Watanabe, S.2    Kawaoka, Y.3
  • 66
    • 53549130711 scopus 로고    scopus 로고
    • Contact structures in the poultry industry in Great Britain: Exploring transmission routes for a potential avian influenza virus epidemic
    • Dent JE, Kao RR, Kiss IZ, Hyder K, Arnold M (2008) Contact structures in the poultry industry in Great Britain: exploring transmission routes for a potential avian influenza virus epidemic. BMC Vet Res 4: 27.
    • (2008) BMC Vet Res , vol.4 , pp. 27
    • Dent, J.E.1    Kao, R.R.2    Kiss, I.Z.3    Hyder, K.4    Arnold, M.5
  • 67
    • 76749108989 scopus 로고    scopus 로고
    • Human host factors required for influenza virus replication
    • König R, Stertz S, Zhou Y, Inoue A, Hoffmann HH, et al. (2009) Human host factors required for influenza virus replication. Nature 463: 813-817.
    • (2009) Nature , vol.463 , pp. 813-817
    • König, R.1    Stertz, S.2    Zhou, Y.3    Inoue, A.4    Hoffmann, H.H.5
  • 68
    • 76749090540 scopus 로고    scopus 로고
    • Genome-wide RNAi screen identifies human host factors crucial for influenza virus replication
    • Karlas A, Machuy N, Shin Y, Pleissner K-P, Artarini A, et al. (2010) Genome-wide RNAi screen identifies human host factors crucial for influenza virus replication. Nature 463: 818-822.
    • (2010) Nature , vol.463 , pp. 818-822
    • Karlas, A.1    Machuy, N.2    Shin, Y.3    Pleissner, K.-P.4    Artarini, A.5
  • 69
    • 0025126351 scopus 로고
    • Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis
    • DeLuca-Flaherty C, McKay DB, Parham P, Hill BL (1990) Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis. Cell 62: 875-887.
    • (1990) Cell , vol.62 , pp. 875-887
    • DeLuca-Flaherty, C.1    McKay, D.B.2    Parham, P.3    Hill, B.L.4
  • 70
    • 4644278442 scopus 로고    scopus 로고
    • Karyopherins: From nuclear-transport mediators to nuclear-function regulators
    • DOI 10.1016/j.tcb.2004.09.004, PII S0962892404002363
    • Mosammaparast N, Pemberton LF (2004) Karyopherins: from nuclear-transport mediators to nuclear-function regulators. Trends Cell Biol 14: 547-556. (Pubitemid 39296617)
    • (2004) Trends in Cell Biology , vol.14 , Issue.10 , pp. 547-556
    • Mosammaparast, N.1    Pemberton, L.F.2
  • 71
    • 0033567847 scopus 로고    scopus 로고
    • Nuclear import of HPV11 L1 capsid protein is mediated by karyopherin alpha2beta1 heterodimers
    • DOI 10.1002/(SICI)1097-4644(19990915)74:4<628::AID
    • Merle E, Rose RC, LeRoux L, Moroianu J (1999) Nuclear import of HPV11 L1 capsid protein is mediated by karyopherin alpha2beta1 heterodimers. J Cell Biochem 74: 628-637. (Pubitemid 29372502)
    • (1999) Journal of Cellular Biochemistry , vol.74 , Issue.4 , pp. 628-637
    • Merle, E.1    Rose, R.C.2    LeRoux, L.3    Moroianu, J.4
  • 73
    • 77956528167 scopus 로고    scopus 로고
    • Cellular networks involved in the influenza virus life cycle
    • Watanabe T, Watanabe S, Kawaoka Y (2010) Cellular networks involved in the influenza virus life cycle. Cell host & microbe 7: 427-439.
    • (2010) Cell Host & Microbe , vol.7 , pp. 427-439
    • Watanabe, T.1    Watanabe, S.2    Kawaoka, Y.3
  • 74
    • 63649157049 scopus 로고    scopus 로고
    • How common are extraribosomal functions of ribosomal proteins?
    • Warner JR, McIntosh KB (2009) How common are extraribosomal functions of ribosomal proteins? Molecular cell 34: 3-11.
    • (2009) Molecular Cell , vol.34 , pp. 3-11
    • Warner, J.R.1    McIntosh, K.B.2
  • 75
    • 32044467711 scopus 로고    scopus 로고
    • Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast
    • DOI 10.1128/MCB.26.4.1355-1372.2006
    • Jivotovskaya AV, Valasek L, Hinnebusch AG, Nielsen KH (2006) Eukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast. Mol Cell Biol 26: 1355-1372. (Pubitemid 43202562)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.4 , pp. 1355-1372
    • Jivotovskaya, A.V.1    Valasek, L.2    Hinnebusch, A.G.3    Nielsen, K.H.4
  • 76
    • 0035396727 scopus 로고    scopus 로고
    • Internal ribosome entry sites in eukaryotic mRNA molecules
    • DOI 10.1101/gad.891101
    • Hellen CU, Sarnow P (2001) Internal ribosome entry sites in eukaryotic mRNA molecules. Genes Dev 15: 1593-1612. (Pubitemid 32702581)
    • (2001) Genes and Development , vol.15 , Issue.13 , pp. 1593-1612
    • Hellen, C.U.T.1    Sarnow, P.2
  • 77
    • 34247396011 scopus 로고    scopus 로고
    • A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC)
    • Ong SE, Mann M (2006) A practical recipe for stable isotope labeling by amino acids in cell culture (SILAC). Nat Protoc 1: 2650-2660.
    • (2006) Nat Protoc , vol.1 , pp. 2650-2660
    • Ong, S.E.1    Mann, M.2
  • 78
    • 0030953859 scopus 로고    scopus 로고
    • Transient changes of the conformation of hemagglutinin of influenza virus at low pH detected by time-resolved circular dichroism spectroscopy
    • DOI 10.1074/jbc.272.15.9764
    • Korte T, Ludwig K, Krumbiegel M, Zirwer D, Damaschun G, et al. (1997) Transient changes of the conformation of hemagglutinin of influenza virus at low pH detected by time-resolved circular dichroism spectroscopy. J Biol Chem 272: 9764-9770. (Pubitemid 27171640)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.15 , pp. 9764-9770
    • Korte, T.1    Ludwig, K.2    Krumbiegel, M.3    Zirwer, D.4    Damaschun, G.5    Herrmann, A.6
  • 79
    • 34548183872 scopus 로고    scopus 로고
    • Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips
    • DOI 10.1038/nprot.2007.261, PII NPROT.2007.261
    • Rappsilber J, Mann M, Ishihama Y (2007) Protocol for micro-purification, enrichment, pre-fractionation and storage of peptides for proteomics using StageTips. Nat Protoc 2: 1896-1906. (Pubitemid 47308128)
    • (2007) Nature Protocols , vol.2 , Issue.8 , pp. 1896-1906
    • Rappsilber, J.1    Mann, M.2    Ishihama, Y.3
  • 80
    • 0037032628 scopus 로고    scopus 로고
    • Microcolumns with self-assembled particle frits for proteomics
    • DOI 10.1016/S0021-9673(02)01402-4, PII S0021967302014024
    • Ishihama Y, Rappsilber J, Andersen JS, Mann M (2002) Microcolumns with self-assembled particle frits for proteomics. J Chromatogr A 979: 233-239. (Pubitemid 35341547)
    • (2002) Journal of Chromatography A , vol.979 , Issue.1-2 , pp. 233-239
    • Ishihama, Y.1    Rappsilber, J.2    Andersen, J.S.3    Mann, M.4
  • 81
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification
    • Cox J, Mann M (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteome-wide protein quantification. Nat Biotechnol 26: 1367-1372.
    • (2008) Nat Biotechnol , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 82
    • 33847630405 scopus 로고    scopus 로고
    • Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry
    • DOI 10.1038/nmeth1019, PII NMETH1019
    • Elias JE, Gygi SP (2007) Target-decoy search strategy for increased confidence in large-scale protein identifications by mass spectrometry. Nat Methods 4: 207-214. (Pubitemid 46358868)
    • (2007) Nature Methods , vol.4 , Issue.3 , pp. 207-214
    • Elias, J.E.1    Gygi, S.P.2
  • 83
    • 79953701087 scopus 로고    scopus 로고
    • Andromeda: A peptide search engine integrated into the MaxQuant environment
    • Cox J, Neuhauser N, Michalski A, Scheltema RA, Olsen JV, et al. (2011) Andromeda: a peptide search engine integrated into the MaxQuant environment. J Proteome Res 10: 1794-1805.
    • (2011) J Proteome Res , vol.10 , pp. 1794-1805
    • Cox, J.1    Neuhauser, N.2    Michalski, A.3    Scheltema, R.A.4    Olsen, J.V.5
  • 85
  • 86
    • 33846689706 scopus 로고    scopus 로고
    • Using GOstats to test gene lists for GO term association
    • DOI 10.1093/bioinformatics/btl567
    • Falcon S, Gentleman R (2007) Using GOstats to test gene lists for GO term association. Bioinformatics (Oxford, England) 23: 257-258. (Pubitemid 46189622)
    • (2007) Bioinformatics , vol.23 , Issue.2 , pp. 257-258
    • Falcon, S.1    Gentleman, R.2
  • 87
    • 63049110388 scopus 로고    scopus 로고
    • Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions
    • Pan C, Kumar C, Bohl S, Klingmueller U, Mann M (2009) Comparative proteomic phenotyping of cell lines and primary cells to assess preservation of cell type-specific functions. Molecular & cellular proteomics: MCP 8: 443-450.
    • (2009) Molecular & Cellular Proteomics: MCP , vol.8 , pp. 443-450
    • Pan, C.1    Kumar, C.2    Bohl, S.3    Klingmueller, U.4    Mann, M.5


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