메뉴 건너뛰기




Volumn 13, Issue 3, 2014, Pages 1270-1280

Label-free quantitative phosphoproteomic analysis reveals differentially regulated proteins and pathway in PRRSV-infected pulmonary alveolar macrophages

Author keywords

label free; PAMs; pathway analysis; PRRSV; quantitative phosphoproteomic

Indexed keywords

IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOPROTEIN;

EID: 84896803423     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr400852d     Document Type: Article
Times cited : (33)

References (54)
  • 2
    • 0034106003 scopus 로고    scopus 로고
    • Current knowledge on the structural proteins of porcine reproductive and respiratory syndrome (PRRS) virus: Comparison of the North American and European isolates
    • Dea, S.; Gagnon, C. A.; Mardassi, H.; Pirzadeh, B.; Rogan, D. Current knowledge on the structural proteins of porcine reproductive and respiratory syndrome (PRRS) virus: comparison of the North American and European isolates Arch. Virol. 2000, 145 (4) 659-88
    • (2000) Arch. Virol. , vol.145 , Issue.4 , pp. 659-688
    • Dea, S.1    Gagnon, C.A.2    Mardassi, H.3    Pirzadeh, B.4    Rogan, D.5
  • 3
    • 79955574664 scopus 로고    scopus 로고
    • Novel structural protein in porcine reproductive and respiratory syndrome virus encoded by an alternative ORF5 present in all arteriviruses
    • Johnson, C. R.; Griggs, T. F.; Gnanandarajah, J.; Murtaugh, M. P. Novel structural protein in porcine reproductive and respiratory syndrome virus encoded by an alternative ORF5 present in all arteriviruses J. Gen. Virol. 2011, 92 (Pt 5) 1107-16
    • (2011) J. Gen. Virol. , vol.92 , Issue.5 , pp. 1107-1116
    • Johnson, C.R.1    Griggs, T.F.2    Gnanandarajah, J.3    Murtaugh, M.P.4
  • 5
    • 0034520364 scopus 로고    scopus 로고
    • Full-length sequence of a Canadian porcine reproductive and respiratory syndrome virus (PRRSV) isolate
    • Wootton, S.; Yoo, D.; Rogan, D. Full-length sequence of a Canadian porcine reproductive and respiratory syndrome virus (PRRSV) isolate Arch. Virol. 2000, 145 (11) 2297-323
    • (2000) Arch. Virol. , vol.145 , Issue.11 , pp. 2297-2323
    • Wootton, S.1    Yoo, D.2    Rogan, D.3
  • 6
    • 84863255662 scopus 로고    scopus 로고
    • Identification of porcine reproductive and respiratory syndrome virus ORF1a-encoded non-structural proteins in virus-infected cells
    • Li, Y.; Tas, A.; Snijder, E. J.; Fang, Y. Identification of porcine reproductive and respiratory syndrome virus ORF1a-encoded non-structural proteins in virus-infected cells J. Gen. Virol. 2012, 93 (Pt 4) 829-39
    • (2012) J. Gen. Virol. , vol.93 , Issue.4 , pp. 829-839
    • Li, Y.1    Tas, A.2    Snijder, E.J.3    Fang, Y.4
  • 7
    • 84860235854 scopus 로고    scopus 로고
    • Interplay between interferon-mediated innate immunity and porcine reproductive and respiratory syndrome virus
    • Sun, Y.; Han, M.; Kim, C.; Calvert, J. G.; Yoo, D. Interplay between interferon-mediated innate immunity and porcine reproductive and respiratory syndrome virus Viruses 2012, 4 (4) 424-46
    • (2012) Viruses , vol.4 , Issue.4 , pp. 424-446
    • Sun, Y.1    Han, M.2    Kim, C.3    Calvert, J.G.4    Yoo, D.5
  • 8
    • 0030739090 scopus 로고    scopus 로고
    • Virus quantification and identification of cellular targets in the lungs and lymphoid tissues of pigs at different time intervals after inoculation with porcine reproductive and respiratory syndrome virus (PRRSV)
    • Duan, X.; Nauwynck, H. J.; Pensaert, M. B. Virus quantification and identification of cellular targets in the lungs and lymphoid tissues of pigs at different time intervals after inoculation with porcine reproductive and respiratory syndrome virus (PRRSV) Vet. Microbiol. 1997, 56 (1-2) 9-19
    • (1997) Vet. Microbiol. , vol.56 , Issue.12 , pp. 9-19
    • Duan, X.1    Nauwynck, H.J.2    Pensaert, M.B.3
  • 9
    • 46149122330 scopus 로고    scopus 로고
    • The challenge of PRRS immunology
    • Mateu, E.; Diaz, I. The challenge of PRRS immunology Vet. J. 2008, 177 (3) 345-51
    • (2008) Vet. J. , vol.177 , Issue.3 , pp. 345-351
    • Mateu, E.1    Diaz, I.2
  • 10
    • 0030876795 scopus 로고    scopus 로고
    • Comparative morphogenesis of three PRRS virus strains
    • Pol, J. M.; Wagenaar, F.; Reus, J. E. Comparative morphogenesis of three PRRS virus strains Vet. Microbiol. 1997, 55 (1-4) 203-8
    • (1997) Vet. Microbiol. , vol.55 , Issue.14 , pp. 203-208
    • Pol, J.M.1    Wagenaar, F.2    Reus, J.E.3
  • 11
    • 0031404350 scopus 로고    scopus 로고
    • Effect of porcine reproductive and respiratory syndrome virus (PRRSV) (isolate ATCC VR-2385) infection on bactericidal activity of porcine pulmonary intravascular macrophages (PIMs): In vitro comparisons with pulmonary alveolar macrophages (PAMs)
    • Thanawongnuwech, R.; Thacker, E. L.; Halbur, P. G. Effect of porcine reproductive and respiratory syndrome virus (PRRSV) (isolate ATCC VR-2385) infection on bactericidal activity of porcine pulmonary intravascular macrophages (PIMs): in vitro comparisons with pulmonary alveolar macrophages (PAMs) Vet. Immunol. Immunopathol. 1997, 59 (3-4) 323-35
    • (1997) Vet. Immunol. Immunopathol. , vol.59 , Issue.34 , pp. 323-335
    • Thanawongnuwech, R.1    Thacker, E.L.2    Halbur, P.G.3
  • 12
    • 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.; Digard, P.; Hiscox, J. A. 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 (10) 5335-45
    • (2010) J. Proteome Res. , vol.9 , Issue.10 , pp. 5335-5345
    • Emmott, E.1    Wise, H.2    Loucaides, E.M.3    Matthews, D.A.4    Digard, P.5    Hiscox, J.A.6
  • 13
    • 77952878717 scopus 로고    scopus 로고
    • Gene expression profiling of Pseudorabies virus (PrV) infected bovine cells by combination of transcript analysis and quantitative proteomic techniques
    • Skiba, M.; Glowinski, F.; Koczan, D.; Mettenleiter, T. C.; Karger, A. Gene expression profiling of Pseudorabies virus (PrV) infected bovine cells by combination of transcript analysis and quantitative proteomic techniques Vet. Microbiol. 2010, 143 (1) 14-20
    • (2010) Vet. Microbiol. , vol.143 , Issue.1 , pp. 14-20
    • Skiba, M.1    Glowinski, F.2    Koczan, D.3    Mettenleiter, T.C.4    Karger, A.5
  • 14
    • 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.; Ajuh, P.; Hiscox, J. A. 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 (9) 1920-36
    • (2010) Mol. Cell. Proteomics , vol.9 , Issue.9 , pp. 1920-1936
    • Emmott, E.1    Rodgers, M.A.2    Macdonald, A.3    McCrory, S.4    Ajuh, P.5    Hiscox, J.A.6
  • 16
    • 84856645718 scopus 로고    scopus 로고
    • Quantitative proteomics using stable isotope labeling with amino acids in cell culture reveals protein and pathway regulation in porcine circovirus type 2 infected PK-15 cells
    • Fan, H.; Ye, Y.; Luo, Y.; Tong, T.; Yan, G.; Liao, M. Quantitative proteomics using stable isotope labeling with amino acids in cell culture reveals protein and pathway regulation in porcine circovirus type 2 infected PK-15 cells J. Proteome Res. 2012, 11 (2) 995-1008
    • (2012) J. Proteome Res. , vol.11 , Issue.2 , pp. 995-1008
    • Fan, H.1    Ye, Y.2    Luo, Y.3    Tong, T.4    Yan, G.5    Liao, M.6
  • 17
    • 84874091416 scopus 로고    scopus 로고
    • Quantitative proteomics by amino acid labeling in foot-and-mouth disease virus (FMDV)-infected cells
    • Ye, Y.; Yan, G.; Luo, Y.; Tong, T.; Liu, X.; Xin, C.; Liao, M.; Fan, H. Quantitative proteomics by amino acid labeling in foot-and-mouth disease virus (FMDV)-infected cells J. Proteome Res. 2013, 12 (1) 363-77
    • (2013) J. Proteome Res. , vol.12 , Issue.1 , pp. 363-377
    • Ye, Y.1    Yan, G.2    Luo, Y.3    Tong, T.4    Liu, X.5    Xin, C.6    Liao, M.7    Fan, H.8
  • 18
    • 67049117503 scopus 로고    scopus 로고
    • Changes in the cellular proteins of pulmonary alveolar macrophage infected with porcine reproductive and respiratory syndrome virus by proteomics analysis
    • Zhang, H.; Guo, X.; Ge, X.; Chen, Y.; Sun, Q.; Yang, H. Changes in the cellular proteins of pulmonary alveolar macrophage infected with porcine reproductive and respiratory syndrome virus by proteomics analysis J. Proteome Res. 2009, 8 (6) 3091-7
    • (2009) J. Proteome Res. , vol.8 , Issue.6 , pp. 3091-3097
    • Zhang, H.1    Guo, X.2    Ge, X.3    Chen, Y.4    Sun, Q.5    Yang, H.6
  • 19
    • 77952626152 scopus 로고    scopus 로고
    • Proteome changes of lungs artificially infected with H-PRRSV and N-PRRSV by two-dimensional fluorescence difference gel electrophoresis
    • Xiao, S.; Wang, Q.; Jia, J.; Cong, P.; Mo, D.; Yu, X.; Qin, L.; Li, A.; Niu, Y.; Zhu, K.; Wang, X.; Liu, X.; Chen, Y. Proteome changes of lungs artificially infected with H-PRRSV and N-PRRSV by two-dimensional fluorescence difference gel electrophoresis Virol. J. 2010, 7, 107
    • (2010) Virol. J. , vol.7 , pp. 107
    • Xiao, S.1    Wang, Q.2    Jia, J.3    Cong, P.4    Mo, D.5    Yu, X.6    Qin, L.7    Li, A.8    Niu, Y.9    Zhu, K.10    Wang, X.11    Liu, X.12    Chen, Y.13
  • 20
    • 84860621147 scopus 로고    scopus 로고
    • Two-dimensional liquid chromatography-tandem mass spectrometry coupled with isobaric tags for relative and absolute quantification (iTRAQ) labeling approach revealed first proteome profiles of pulmonary alveolar macrophages infected with porcine reproductive and respiratory syndrome virus
    • Lu, Q.; Bai, J.; Zhang, L.; Liu, J.; Jiang, Z.; Michal, J. J.; He, Q.; Jiang, P. Two-dimensional liquid chromatography-tandem mass spectrometry coupled with isobaric tags for relative and absolute quantification (iTRAQ) labeling approach revealed first proteome profiles of pulmonary alveolar macrophages infected with porcine reproductive and respiratory syndrome virus J. Proteome Res. 2012, 11 (5) 2890-903
    • (2012) J. Proteome Res. , vol.11 , Issue.5 , pp. 2890-2903
    • Lu, Q.1    Bai, J.2    Zhang, L.3    Liu, J.4    Jiang, Z.5    Michal, J.J.6    He, Q.7    Jiang, P.8
  • 21
    • 49749113582 scopus 로고    scopus 로고
    • Functional proteomics to identify critical proteins in signal transduction pathways
    • Yan, G. R.; He, Q. Y. Functional proteomics to identify critical proteins in signal transduction pathways Amino Acids 2008, 35 (2) 267-74
    • (2008) Amino Acids , vol.35 , Issue.2 , pp. 267-274
    • Yan, G.R.1    He, Q.Y.2
  • 22
    • 41849125938 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus (PRRSV) suppresses interferon-beta production by interfering with the RIG-I signaling pathway
    • Luo, R.; Xiao, S.; Jiang, Y.; Jin, H.; Wang, D.; Liu, M.; Chen, H.; Fang, L. Porcine reproductive and respiratory syndrome virus (PRRSV) suppresses interferon-beta production by interfering with the RIG-I signaling pathway Mol. Immunol. 2008, 45 (10) 2839-46
    • (2008) Mol. Immunol. , vol.45 , Issue.10 , pp. 2839-2846
    • Luo, R.1    Xiao, S.2    Jiang, Y.3    Jin, H.4    Wang, D.5    Liu, M.6    Chen, H.7    Fang, L.8
  • 23
    • 77953028825 scopus 로고    scopus 로고
    • Modulation of type i interferon induction by porcine reproductive and respiratory syndrome virus and degradation of CREB-binding protein by non-structural protein 1 in MARC-145 and HeLa cells
    • Kim, O.; Sun, Y.; Lai, F. W.; Song, C.; Yoo, D. Modulation of type I interferon induction by porcine reproductive and respiratory syndrome virus and degradation of CREB-binding protein by non-structural protein 1 in MARC-145 and HeLa cells Virology 2010, 402 (2) 315-26
    • (2010) Virology , vol.402 , Issue.2 , pp. 315-326
    • Kim, O.1    Sun, Y.2    Lai, F.W.3    Song, C.4    Yoo, D.5
  • 24
    • 27444448127 scopus 로고    scopus 로고
    • Porcine arterivirus activates the NF-kappaB pathway through IkappaB degradation
    • Lee, S. M.; Kleiboeker, S. B. Porcine arterivirus activates the NF-kappaB pathway through IkappaB degradation Virology 2005, 342 (1) 47-59
    • (2005) Virology , vol.342 , Issue.1 , pp. 47-59
    • Lee, S.M.1    Kleiboeker, S.B.2
  • 25
    • 33745800293 scopus 로고    scopus 로고
    • Interpreting the protein language using proteomics
    • Jensen, O. N. Interpreting the protein language using proteomics Nat. Rev. Mol. Cell Biol. 2006, 7 (6) 391-403
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , Issue.6 , pp. 391-403
    • Jensen, O.N.1
  • 26
    • 77952956167 scopus 로고    scopus 로고
    • Decoding signalling networks by mass spectrometry-based proteomics
    • Choudhary, C.; Mann, M. Decoding signalling networks by mass spectrometry-based proteomics Nat. Rev. Mol. Cell Biol. 2010, 11 (6) 427-39
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , Issue.6 , pp. 427-439
    • Choudhary, C.1    Mann, M.2
  • 27
    • 65249137629 scopus 로고    scopus 로고
    • Global and site-specific quantitative phosphoproteomics: Principles and applications
    • Macek, B.; Mann, M.; Olsen, J. V. Global and site-specific quantitative phosphoproteomics: principles and applications Annu. Rev. Pharmacol. Toxicol. 2009, 49, 199-221
    • (2009) Annu. Rev. Pharmacol. Toxicol. , vol.49 , pp. 199-221
    • Macek, B.1    Mann, M.2    Olsen, J.V.3
  • 29
    • 3242688830 scopus 로고    scopus 로고
    • Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns
    • Pinkse, M. W.; Uitto, P. M.; Hilhorst, M. J.; Ooms, B.; Heck, A. J. Selective isolation at the femtomole level of phosphopeptides from proteolytic digests using 2D-NanoLC-ESI-MS/MS and titanium oxide precolumns Anal. Chem. 2004, 76 (14) 3935-43
    • (2004) Anal. Chem. , vol.76 , Issue.14 , pp. 3935-3943
    • Pinkse, M.W.1    Uitto, P.M.2    Hilhorst, M.J.3    Ooms, B.4    Heck, A.J.5
  • 30
    • 33847616949 scopus 로고    scopus 로고
    • Reproducible isolation of distinct, overlapping segments of the phosphoproteome
    • Bodenmiller, B.; Mueller, L. N.; Mueller, M.; Domon, B.; Aebersold, R. Reproducible isolation of distinct, overlapping segments of the phosphoproteome Nat. Methods 2007, 4 (3) 231-7
    • (2007) Nat. Methods , vol.4 , Issue.3 , pp. 231-237
    • Bodenmiller, B.1    Mueller, L.N.2    Mueller, M.3    Domon, B.4    Aebersold, R.5
  • 31
    • 33750456519 scopus 로고    scopus 로고
    • Global, in vivo, and site-specific phosphorylation dynamics in signaling networks
    • Olsen, J. V.; Blagoev, B.; Gnad, F.; Macek, B.; Kumar, C.; Mortensen, P.; Mann, M. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks Cell 2006, 127 (3) 635-48
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7
  • 32
    • 84862777819 scopus 로고    scopus 로고
    • Stress-activated protein kinases are involved in porcine reproductive and respiratory syndrome virus infection and modulate virus-induced cytokine production
    • Lee, Y. J.; Lee, C. Stress-activated protein kinases are involved in porcine reproductive and respiratory syndrome virus infection and modulate virus-induced cytokine production Virology 2012, 427 (2) 80-9
    • (2012) Virology , vol.427 , Issue.2 , pp. 80-89
    • Lee, Y.J.1    Lee, C.2
  • 33
    • 77955275486 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus replication is suppressed by inhibition of the extracellular signal-regulated kinase (ERK) signaling pathway
    • Lee, Y. J.; Lee, C. Porcine reproductive and respiratory syndrome virus replication is suppressed by inhibition of the extracellular signal-regulated kinase (ERK) signaling pathway Virus Res. 2010, 152 (1-2) 50-8
    • (2010) Virus Res. , vol.152 , Issue.12 , pp. 50-58
    • Lee, Y.J.1    Lee, C.2
  • 34
    • 84878567357 scopus 로고    scopus 로고
    • Control of the PI3K/Akt pathway by porcine reproductive and respiratory syndrome virus
    • Zhu, L.; Yang, S.; Tong, W.; Zhu, J.; Yu, H.; Zhou, Y.; Morrison, R. B.; Tong, G. Control of the PI3K/Akt pathway by porcine reproductive and respiratory syndrome virus Arch. Virol. 2013, 158 (6) 1227-34
    • (2013) Arch. Virol. , vol.158 , Issue.6 , pp. 1227-1234
    • Zhu, L.1    Yang, S.2    Tong, W.3    Zhu, J.4    Yu, H.5    Zhou, Y.6    Morrison, R.B.7    Tong, G.8
  • 35
    • 84863729076 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus induces interleukin-15 through the NF-kappaB signaling pathway
    • Fu, Y.; Quan, R.; Zhang, H.; Hou, J.; Tang, J.; Feng, W. H. Porcine reproductive and respiratory syndrome virus induces interleukin-15 through the NF-kappaB signaling pathway J. Virol. 2012, 86 (14) 7625-36
    • (2012) J. Virol. , vol.86 , Issue.14 , pp. 7625-7636
    • Fu, Y.1    Quan, R.2    Zhang, H.3    Hou, J.4    Tang, J.5    Feng, W.H.6
  • 36
    • 78650629125 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus (PRRSV) infection activates chemokine RANTES in MARC-145 cells
    • Wang, Y.; Luo, R.; Fang, L.; Wang, D.; Bi, J.; Chen, H.; Xiao, S. Porcine reproductive and respiratory syndrome virus (PRRSV) infection activates chemokine RANTES in MARC-145 cells Mol. Immunol. 2011, 48 (4) 586-91
    • (2011) Mol. Immunol. , vol.48 , Issue.4 , pp. 586-591
    • Wang, Y.1    Luo, R.2    Fang, L.3    Wang, D.4    Bi, J.5    Chen, H.6    Xiao, S.7
  • 37
    • 73949087536 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus nonstructural protein 1beta modulates host innate immune response by antagonizing IRF3 activation
    • Beura, L. K.; Sarkar, S. N.; Kwon, B.; Subramaniam, S.; Jones, C.; Pattnaik, A. K.; Osorio, F. A. Porcine reproductive and respiratory syndrome virus nonstructural protein 1beta modulates host innate immune response by antagonizing IRF3 activation J. Virol. 2010, 84 (3) 1574-84
    • (2010) J. Virol. , vol.84 , Issue.3 , pp. 1574-1584
    • Beura, L.K.1    Sarkar, S.N.2    Kwon, B.3    Subramaniam, S.4    Jones, C.5    Pattnaik, A.K.6    Osorio, F.A.7
  • 38
    • 77957931265 scopus 로고    scopus 로고
    • Porcine reproductive and respiratory syndrome virus inhibits type i interferon signaling by blocking STAT1/STAT2 nuclear translocation
    • Patel, D.; Nan, Y.; Shen, M.; Ritthipichai, K.; Zhu, X.; Zhang, Y. J. Porcine reproductive and respiratory syndrome virus inhibits type I interferon signaling by blocking STAT1/STAT2 nuclear translocation J. Virol. 2010, 84 (21) 11045-55
    • (2010) J. Virol. , vol.84 , Issue.21 , pp. 11045-11055
    • Patel, D.1    Nan, Y.2    Shen, M.3    Ritthipichai, K.4    Zhu, X.5    Zhang, Y.J.6
  • 39
    • 74049115774 scopus 로고    scopus 로고
    • Mass spectrometry-based label-free quantitative proteomics
    • Zhu, W.; Smith, J. W.; Huang, C. M. Mass spectrometry-based label-free quantitative proteomics J. Biomed. Biotechnol. 2010, 2010, 840518
    • (2010) J. Biomed. Biotechnol. , vol.2010 , pp. 840518
    • Zhu, W.1    Smith, J.W.2    Huang, C.M.3
  • 42
    • 0142061504 scopus 로고    scopus 로고
    • Expression and function of chemokines during viral infections: From molecular mechanisms to in vivo function
    • Melchjorsen, J.; Sorensen, L. N.; Paludan, S. R. Expression and function of chemokines during viral infections: from molecular mechanisms to in vivo function J. Leukocyte Biol. 2003, 74 (3) 331-43
    • (2003) J. Leukocyte Biol. , vol.74 , Issue.3 , pp. 331-343
    • Melchjorsen, J.1    Sorensen, L.N.2    Paludan, S.R.3
  • 43
    • 84884478326 scopus 로고    scopus 로고
    • Protein kinase CK2 phosphorylates and activates p21-activated kinase 1
    • Shin, Y. J.; Kim, Y. B.; Kim, J. H. Protein kinase CK2 phosphorylates and activates p21-activated kinase 1 Mol. Biol. Cell 2013, 24 (18) 2990-9
    • (2013) Mol. Biol. Cell , vol.24 , Issue.18 , pp. 2990-2999
    • Shin, Y.J.1    Kim, Y.B.2    Kim, J.H.3
  • 44
    • 84872675863 scopus 로고    scopus 로고
    • Diversion of stress granules and P-bodies during viral infection
    • Reineke, L. C.; Lloyd, R. E. Diversion of stress granules and P-bodies during viral infection Virology 2013, 436 (2) 255-67
    • (2013) Virology , vol.436 , Issue.2 , pp. 255-267
    • Reineke, L.C.1    Lloyd, R.E.2
  • 45
    • 0034775591 scopus 로고    scopus 로고
    • RasGAP-associated endoribonuclease G3Bp: Selective RNA degradation and phosphorylation-dependent localization
    • Tourriere, H.; Gallouzi, I. E.; Chebli, K.; Capony, J. P.; Mouaikel, J.; van der Geer, P.; Tazi, J. RasGAP-associated endoribonuclease G3Bp: selective RNA degradation and phosphorylation-dependent localization Mol. Cell. Biol. 2001, 21 (22) 7747-60
    • (2001) Mol. Cell. Biol. , vol.21 , Issue.22 , pp. 7747-7760
    • Tourriere, H.1    Gallouzi, I.E.2    Chebli, K.3    Capony, J.P.4    Mouaikel, J.5    Van Der Geer, P.6    Tazi, J.7
  • 46
    • 33749079186 scopus 로고    scopus 로고
    • Subproteomic study of hepatitis C virus replicon reveals Ras-GTPase-activating protein binding protein 1 as potential HCV RC component
    • Yi, Z.; Fang, C.; Pan, T.; Wang, J.; Yang, P.; Yuan, Z. Subproteomic study of hepatitis C virus replicon reveals Ras-GTPase-activating protein binding protein 1 as potential HCV RC component Biochem. Biophys. Res. Commun. 2006, 350 (1) 174-8
    • (2006) Biochem. Biophys. Res. Commun. , vol.350 , Issue.1 , pp. 174-178
    • Yi, Z.1    Fang, C.2    Pan, T.3    Wang, J.4    Yang, P.5    Yuan, Z.6
  • 47
    • 79960401766 scopus 로고    scopus 로고
    • Hepatitis C virus co-opts Ras-GTPase-activating protein-binding protein 1 for its genome replication
    • Yi, Z.; Pan, T.; Wu, X.; Song, W.; Wang, S.; Xu, Y.; Rice, C. M.; Macdonald, M. R.; Yuan, Z. Hepatitis C virus co-opts Ras-GTPase-activating protein-binding protein 1 for its genome replication J. Virol. 2011, 85 (14) 6996-7004
    • (2011) J. Virol. , vol.85 , Issue.14 , pp. 6996-7004
    • Yi, Z.1    Pan, T.2    Wu, X.3    Song, W.4    Wang, S.5    Xu, Y.6    Rice, C.M.7    Macdonald, M.R.8    Yuan, Z.9
  • 48
    • 78049506923 scopus 로고    scopus 로고
    • Respiratory syncytial virus induces host RNA stress granules to facilitate viral replication
    • Lindquist, M. E.; Lifland, A. W.; Utley, T. J.; Santangelo, P. J.; Crowe, J. E., Jr. Respiratory syncytial virus induces host RNA stress granules to facilitate viral replication J. Virol. 2010, 84 (23) 12274-84
    • (2010) J. Virol. , vol.84 , Issue.23 , pp. 12274-12284
    • Lindquist, M.E.1    Lifland, A.W.2    Utley, T.J.3    Santangelo, P.J.4    Crowe Jr., J.E.5
  • 49
    • 84883271505 scopus 로고    scopus 로고
    • Encephalomyocarditis virus disrupts stress granules, the critical platform for triggering antiviral innate immune responses
    • Ng, C. S.; Jogi, M.; Yoo, J. S.; Onomoto, K.; Koike, S.; Iwasaki, T.; Yoneyama, M.; Kato, H.; Fujita, T. Encephalomyocarditis virus disrupts stress granules, the critical platform for triggering antiviral innate immune responses J. Virol. 2013, 87 (17) 9511-22
    • (2013) J. Virol. , vol.87 , Issue.17 , pp. 9511-9522
    • Ng, C.S.1    Jogi, M.2    Yoo, J.S.3    Onomoto, K.4    Koike, S.5    Iwasaki, T.6    Yoneyama, M.7    Kato, H.8    Fujita, T.9
  • 50
    • 0031832234 scopus 로고    scopus 로고
    • A novel phosphorylation-dependent RNase activity of GAP-SH3 binding protein: A potential link between signal transduction and RNA stability
    • Gallouzi, I. E.; Parker, F.; Chebli, K.; Maurier, F.; Labourier, E.; Barlat, I.; Capony, J. P.; Tocque, B.; Tazi, J. A novel phosphorylation- dependent RNase activity of GAP-SH3 binding protein: a potential link between signal transduction and RNA stability Mol. Cell. Biol. 1998, 18 (7) 3956-65
    • (1998) Mol. Cell. Biol. , vol.18 , Issue.7 , pp. 3956-3965
    • Gallouzi, I.E.1    Parker, F.2    Chebli, K.3    Maurier, F.4    Labourier, E.5    Barlat, I.6    Capony, J.P.7    Tocque, B.8    Tazi, J.9
  • 51
    • 84857049091 scopus 로고    scopus 로고
    • Broad action of Hsp90 as a host chaperone required for viral replication
    • Geller, R.; Taguwa, S.; Frydman, J. Broad action of Hsp90 as a host chaperone required for viral replication Biochim. Biophys. Acta 2012, 1823 (3) 698-706
    • (2012) Biochim. Biophys. Acta , vol.1823 , Issue.3 , pp. 698-706
    • Geller, R.1    Taguwa, S.2    Frydman, J.3
  • 52
    • 79952071414 scopus 로고    scopus 로고
    • Emerging picture of host chaperone and cyclophilin roles in RNA virus replication
    • Nagy, P. D.; Wang, R. Y.; Pogany, J.; Hafren, A.; Makinen, K. Emerging picture of host chaperone and cyclophilin roles in RNA virus replication Virology 2011, 411 (2) 374-82
    • (2011) Virology , vol.411 , Issue.2 , pp. 374-382
    • Nagy, P.D.1    Wang, R.Y.2    Pogany, J.3    Hafren, A.4    Makinen, K.5
  • 53
    • 0035980061 scopus 로고    scopus 로고
    • Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein
    • Zhao, Y. G.; Gilmore, R.; Leone, G.; Coffey, M. C.; Weber, B.; Lee, P. W. Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein J. Biol. Chem. 2001, 276 (35) 32822-7
    • (2001) J. Biol. Chem. , vol.276 , Issue.35 , pp. 32822-32827
    • Zhao, Y.G.1    Gilmore, R.2    Leone, G.3    Coffey, M.C.4    Weber, B.5    Lee, P.W.6
  • 54
    • 70350474677 scopus 로고    scopus 로고
    • Heat shock protein 27 phosphorylation: Kinases, phosphatases, functions and pathology
    • Kostenko, S.; Moens, U. Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology Cell. Mol. Life Sci. 2009, 66 (20) 3289-307
    • (2009) Cell. Mol. Life Sci. , vol.66 , Issue.20 , pp. 3289-3307
    • Kostenko, S.1    Moens, U.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.