메뉴 건너뛰기




Volumn 10, Issue 7, 2015, Pages

Quantitative proteomic analysis of BHK-21 cells infected with foot-And-mouth disease virus serotype Asia 1

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; SMALL INTERFERING RNA; PROTEOME; VIRAL PROTEIN;

EID: 84941272424     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0132384     Document Type: Article
Times cited : (11)

References (67)
  • 1
    • 2042459160 scopus 로고    scopus 로고
    • Foot-And-mouth disease
    • Grubman MJ, Baxt B. Foot-And-Mouth Disease. Clin Microbiol Rev. 2004; 17(2):465-93. doi: 10.1128/cmr.17.2.465-493.2004
    • (2004) Clin Microbiol Rev , vol.17 , Issue.2 , pp. 465-493
    • Grubman, M.J.1    Baxt, B.2
  • 2
    • 0022182915 scopus 로고
    • Capsid intermediates assembled in a foot-And-mouth disease virus genome RNA-programmed cell-free translation system and in infected cells
    • Grubman MJ, Morgan DO, Kendall J, Baxt B. Capsid intermediates assembled in a foot-And-mouth disease virus genome RNA-programmed cell-free translation system and in infected cells. J Virol. 1985; 56(1):120-6.
    • (1985) J Virol , vol.56 , Issue.1 , pp. 120-126
    • Grubman, M.J.1    Morgan, D.O.2    Kendall, J.3    Baxt, B.4
  • 3
    • 59649103610 scopus 로고    scopus 로고
    • A conserved domain in the leader proteinase of foot-And-mouth disease virus is required for proper subcellular localization and function
    • de los Santos T, Diaz-San Segundo F, Zhu J, Koster M, Dias CCA, Grubman MJ. A conserved domain in the leader proteinase of foot-And-mouth disease virus is required for proper subcellular localization and function. J Virol. 2009; 83(4):1800-10. doi: 10.1128/jvi.02112-08
    • (2009) J Virol , vol.83 , Issue.4 , pp. 1800-1810
    • de los Santos, T.1    Diaz-San Segundo, F.2    Zhu, J.3    Koster, M.4    Dias, C.C.A.5    Grubman, M.J.6
  • 4
    • 79952837091 scopus 로고    scopus 로고
    • The leader proteinase of foot-And-mouth disease virus negatively regulates the type i interferon pathway by acting as a viral deubiquitinase
    • Wang D, Fang LR, Li P, Sun L, Fan JX, Zhang QY, et al. The leader proteinase of foot-And-mouth disease virus negatively regulates the type i interferon pathway by acting as a viral deubiquitinase. J Virol. 2011; 85(8):3758-66. doi: 10.1128/jvi.02589-10
    • (2011) J Virol , vol.85 , Issue.8 , pp. 3758-3766
    • Wang, D.1    Fang, L.R.2    Li, P.3    Sun, L.4    Fan, J.X.5    Zhang, Q.Y.6
  • 5
    • 0033988512 scopus 로고    scopus 로고
    • Foot-And-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells
    • Belsham GJ, McInerney GM, Ross-Smith N. Foot-And-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cells. J Virol. 2000; 74(1):272-80. doi: 10.1128/jvi.74.1.272-280.2000.
    • (2000) J Virol , vol.74 , Issue.1 , pp. 272-280
    • Belsham, G.J.1    McInerney, G.M.2    Ross-Smith, N.3
  • 6
    • 0035015174 scopus 로고    scopus 로고
    • Analysis of the aphthovirus 2A/2B polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: A putative ribosomal 'skip'
    • Donnelly ML, Luke G, Mehrotra A, Li X, Hughes LE, Gani D, et al. Analysis of the aphthovirus 2A/2B polyprotein 'cleavage' mechanism indicates not a proteolytic reaction, but a novel translational effect: A putative ribosomal 'skip'. J Gen Virol 2001; 82(Pt 5):1013-25..
    • (2001) J Gen Virol , vol.82 , pp. 1013-1025
    • Donnelly, M.L.1    Luke, G.2    Mehrotra, A.3    Li, X.4    Hughes, L.E.5    Gani, D.6
  • 7
    • 0029330515 scopus 로고
    • Identification of native foot-And-mouth disease virus non-structural protein 2C as a serological indicator to differentiate infected from vaccinated livestock
    • Lubroth J, Brown F. Identification of native foot-And-mouth disease virus non-structural protein 2C as a serological indicator to differentiate infected from vaccinated livestock. Res Vet Sci 1995; 59(1):70-8. doi: 10.1016/0034-5288(95)90034-9
    • (1995) Res Vet Sci , vol.59 , Issue.1 , pp. 70-78
    • Lubroth, J.1    Brown, F.2
  • 8
    • 0035881530 scopus 로고    scopus 로고
    • Subcellular distribution of the foot-And-mouth disease virus 3A protein in cells infected with viruses encoding wild-Type and bovine-Attenuated forms of 3A
    • O'Donnell VK, Pacheco JM, Henry TM, Mason PW. Subcellular distribution of the foot-And-mouth disease virus 3A protein in cells infected with viruses encoding wild-Type and bovine-Attenuated forms of 3A. Virology. 2001; 287(1):151-62. doi: http://dx.doi.org/10.1006/viro.2001.1035.
    • (2001) Virology , vol.287 , Issue.1 , pp. 151-162
    • O'Donnell, V.K.1    Pacheco, J.M.2    Henry, T.M.3    Mason, P.W.4
  • 10
    • 35548989199 scopus 로고    scopus 로고
    • Poliovirus infection blocks ERGIC-To-Golgi trafficking and induces microtubule-dependent disruption of the Golgi complex
    • Beske O, Reichelt M, Taylor MP, Kirkegaard K, Andino R. Poliovirus infection blocks ERGIC-To-Golgi trafficking and induces microtubule-dependent disruption of the Golgi complex. J Cell Sci. 2007; 120(Pt 18):3207-18. doi: 10.1242/jcs.03483.
    • (2007) J Cell Sci , vol.120 , pp. 3207-3218
    • Beske, O.1    Reichelt, M.2    Taylor, M.P.3    Kirkegaard, K.4    Andino, R.5
  • 11
    • 19444371102 scopus 로고    scopus 로고
    • Inhibition of cellular protein secretion by picornaviral 3A proteins
    • Choe SS, Dodd DA, Kirkegaard K. Inhibition of cellular protein secretion by picornaviral 3A proteins. Virology. 2005; 337(1):18-29. doi: http://dx.doi.org/10.1016/j.virol.2005.03.036.
    • (2005) Virology , vol.337 , Issue.1 , pp. 18-29
    • Choe, S.S.1    Dodd, D.A.2    Kirkegaard, K.3
  • 12
    • 33846554150 scopus 로고    scopus 로고
    • Inhibition of the secretory pathway by foot-And-mouth disease virus 2BC protein is reproduced by coexpression of 2B with 2C, and the site of inhibition is determined by the subcellular location of 2C
    • Moffat K, Knox C, Howell G, Clark SJ, Yang H, Belsham GJ, et al. Inhibition of the secretory pathway by foot-And-mouth disease virus 2BC protein is reproduced by coexpression of 2B with 2C, and the site of inhibition is determined by the subcellular location of 2C. J Virol. 2007; 81(3):1129-39. doi: 10.1128/jvi. 00393-06
    • (2007) J Virol , vol.81 , Issue.3 , pp. 1129-1139
    • Moffat, K.1    Knox, C.2    Howell, G.3    Clark, S.J.4    Yang, H.5    Belsham, G.J.6
  • 13
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels
    • Shevchenko A, Wilm M, Vorm O, Mann M. Mass spectrometric sequencing of proteins from silver stained polyacrylamide gels. Anal Chem. 1996; 68(5):850-8. doi: 10.1021/ac950914h.
    • (1996) Anal Chem , vol.68 , Issue.5 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 14
    • 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. 2011; 11(2):995-1008. doi: 10.1021/pr200755d.
    • (2011) 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
  • 15
    • 84874091416 scopus 로고    scopus 로고
    • Quantitative proteomics by amino acid labeling in footand-mouth disease virus (FMDV)-infected cells
    • Ye Y, Yan G, Luo Y, Tong T, Liu X, Xin C, et al. Quantitative proteomics by amino acid labeling in footand-mouth disease virus (FMDV)-infected cells. J Proteome Res. 2012; 12(1):363-77. doi: 10.1021/pr300611e.
    • (2012) 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
  • 16
    • 0018194846 scopus 로고
    • Microneutralization tests for serological typing and subtyping of foot-And-mouth disease virus strains
    • Rweyemamu MM, Booth JC, Head M, Pay TWF. Microneutralization tests for serological typing and subtyping of foot-And-mouth disease virus strains. J Hyg (Lond). 1978; 81(1):107-23
    • (1978) J Hyg (Lond , vol.81 , Issue.1 , pp. 107-123
    • Rweyemamu, M.M.1    Booth, J.C.2    Head, M.3    Twf, P.4
  • 17
    • 42449121506 scopus 로고    scopus 로고
    • PKR in innate immunity, cancer, and viral oncolysis
    • Balachandran S, Barber GN. PKR in innate immunity, cancer, and viral oncolysis. Methods Mol Biol. 2007; 383:277-301. doi: 10.1007/978-1-59745-335-6-18
    • (2007) Methods Mol Biol , vol.383 , pp. 277-301
    • Balachandran, S.1    Barber, G.N.2
  • 18
    • 33845627785 scopus 로고    scopus 로고
    • Impact of protein kinase PKR in cell biology: From antiviral to antiproliferative action
    • Garcia MA, Gil J, Ventoso I, Guerra S, Domingo E, Rivas C, et al. Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative action. Microbiol Mol Biol Rev. 2006; 70(4):1032-60. doi: 10. 1128/MMBR.00027-06
    • (2006) Microbiol Mol Biol Rev , vol.70 , Issue.4 , pp. 1032-1060
    • Garcia, M.A.1    Gil, J.2    Ventoso, I.3    Guerra, S.4    Domingo, E.5    Rivas, C.6
  • 19
    • 0034663942 scopus 로고    scopus 로고
    • The protein kinase PKR is required for p38 MAPK activation and the innate immune response to bacterial endotoxin
    • Goh KC, deVeer MJ, Williams BRG. The protein kinase PKR is required for p38 MAPK activation and the innate immune response to bacterial endotoxin. Embo J. 2000; 19(16):4292-7. doi: 10.1093/emboj/19.16.4292
    • (2000) Embo J , vol.19 , Issue.16 , pp. 4292-4297
    • Goh, K.C.1    deVeer, M.J.2    Williams, B.R.G.3
  • 20
    • 75749108288 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis
    • Nakamura T, Furuhashi M, Li P, Cao H, Tuncman G, Sonenberg N, et al. Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis. Cell. 2010; 140 (3):338-48. doi: http://dx.doi.org/10.1016/j.cell.2010.01.001
    • (2011) Cell , vol.140 , Issue.3 , pp. 338-348
    • Nakamura, T.1    Furuhashi, M.2    Li, P.3    Cao, H.4    Tuncman, G.5    Sonenberg, N.6
  • 21
    • 0033621619 scopus 로고    scopus 로고
    • NF-kappaB activation by doublestranded-RNA-Activated protein kinase (PKR) is mediated through NF-kappaB-inducing kinase and IkappaB kinase
    • Zamanian-Daryoush M, Mogensen TH, DiDonato JA, Williams BRG. NF-kappaB activation by doublestranded-RNA-Activated protein kinase (PKR) is mediated through NF-kappaB-inducing kinase and IkappaB kinase. Mol Cell Biol. 2000; 20(4):1278-90. doi: 10.1128/mcb.20.4.1278-1290.2000.
    • (2000) Mol Cell Biol , vol.20 , Issue.4 , pp. 1278-1290
    • Zamanian-Daryoush, M.1    Mogensen, T.H.2    DiDonato, J.A.3    Brg, W.4
  • 22
    • 0034082457 scopus 로고    scopus 로고
    • PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex
    • Bonnet MC, Weil R, Dam E, Hovanessian AG, Meurs EF. PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex. Mol Cell Biol. 2000; 20(13):4532-42. doi: 10.1128/mcb.20.13.4532-4542.2000
    • (2000) Mol Cell Biol , vol.20 , Issue.13 , pp. 4532-4542
    • Bonnet, M.C.1    Weil, R.2    Dam, E.3    Hovanessian, A.G.4    Meurs, E.F.5
  • 23
    • 58049190885 scopus 로고    scopus 로고
    • Induction of protein kinase PKR-dependent activation of interferon regulatory factor 3 by vaccinia virus occurs through adapter IPS-1 signaling
    • Zhang P, Samuel CE. Induction of protein kinase PKR-dependent activation of interferon regulatory factor 3 by vaccinia virus occurs through adapter IPS-1 signaling. J Biol Chem. 2008; 283(50):34580-7. doi: 10.1074/jbc.M807029200
    • (2008) J Biol Chem , vol.283 , Issue.50 , pp. 34580-34587
    • Zhang, P.1    Samuel, C.E.2
  • 24
    • 0035010933 scopus 로고    scopus 로고
    • Inhibition of L-deleted foot-And-mouth disease virus replication by alpha/beta interferon involves double-stranded RNA-dependent protein kinase
    • Chinsangaram J, Koster M, Grubman MJ. Inhibition of L-deleted foot-And-mouth disease virus replication by alpha/beta interferon involves double-stranded RNA-dependent protein kinase. J Virol. 2001; 75 (12):5498-503. doi: 10.1128/jvi.75.12.5498-5503.2001
    • (2001) J Virol , vol.75 , Issue.12 , pp. 5498-5503
    • Chinsangaram, J.1    Koster, M.2    Grubman, M.J.3
  • 25
    • 32444446676 scopus 로고    scopus 로고
    • The leader proteinase of foot-And-mouth disease virus inhibits the induction of beta interferon mRNA and blocks the host innate immune response
    • de los Santos T, de Avila Botton S, Weiblen R, Grubman MJ. The leader proteinase of foot-And-mouth disease virus inhibits the induction of beta interferon mRNA and blocks the host innate immune response. J Virol. 2006; 80(4):1906-14. doi: 10.1128/jvi.80.4.1906-1914.2006
    • (2006) J Virol , vol.80 , Issue.4 , pp. 1906-1914
    • de los Santos, T.1    De Avila Botton, S.2    Weiblen, R.3    Grubman, M.J.4
  • 26
    • 41749108854 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress in disease pathogenesis
    • Lin JH, Walter P, Yen TSB. Endoplasmic reticulum stress in disease pathogenesis. Annu Rev Pathol. 2008; 3(1):399-425. doi: 10.1146/annurev.pathmechdis.3.121806.151434
    • (2008) Annu Rev Pathol , vol.3 , Issue.1 , pp. 399-425
    • Lin, J.H.1    Walter, P.2    Tsb, Y.3
  • 27
    • 33846548110 scopus 로고    scopus 로고
    • ER stress and diseases
    • Yoshida H. ER stress and diseases. FEBS J. 2007; 274(3):630-58. doi: 10.1111/j.1742-4658.2007. 05639.x.
    • (2007) FEBS J , vol.274 , Issue.3 , pp. 630-658
    • Yoshida, H.1
  • 28
    • 33645142635 scopus 로고    scopus 로고
    • Viruses, endoplasmic reticulum stress, and interferon responses
    • He B. Viruses, endoplasmic reticulum stress, and interferon responses. Cell Death Differ. 2006; 13 (3):393-403. doi: 10.1038/sj.cdd.4401833.
    • (2006) Cell Death Differ , vol.13 , Issue.3 , pp. 393-403
    • He, B.1
  • 29
    • 0034231849 scopus 로고    scopus 로고
    • Folding of viral envelope glycoproteins in the endoplasmic reticulum
    • Braakman I, Van Anken E. Folding of viral envelope glycoproteins in the endoplasmic reticulum. Traffic. 2000; 1(7):533-9. doi: 10.1034/j.1600-0854.2000.010702.x.
    • (2000) Traffic , vol.1 , Issue.7 , pp. 533-539
    • Braakman, I.1    Van Anken, E.2
  • 30
    • 32444441933 scopus 로고    scopus 로고
    • Reovirus induces and benefits from an integrated cellular stress response
    • Smith JA, Schmechel SC, Raghavan A, Abelson M, Reilly C, Katze MG, et al. Reovirus induces and benefits from an integrated cellular stress response. J Virol. 2006; 80(4):2019-33. doi: 10.1128/jvi.80.4. 2019-2033.2006
    • (2006) J Virol , vol.80 , Issue.4 , pp. 2019-2033
    • Smith, J.A.1    Schmechel, S.C.2    Raghavan, A.3    Abelson, M.4    Reilly, C.5    Katze, M.G.6
  • 31
    • 33751247922 scopus 로고    scopus 로고
    • Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress
    • Yu C-Y, Hsu Y-W, Liao C-L, Lin Y-L. Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress. J Virol. 2006; 80(23):11868-80. doi: 10. 1128/jvi.00879-06
    • (2006) J Virol , vol.80 , Issue.23 , pp. 11868-11880
    • Yu, C.-Y.1    Hsu, Y.-W.2    Liao, C.-L.3    Lin, Y.-L.4
  • 32
    • 0030928285 scopus 로고    scopus 로고
    • Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release
    • van Kuppeveld FJM, Hoenderop JGJ, Smeets RLL, Willems PHGM, Dijkman HBPM, Galama JMD, et al. Coxsackievirus protein 2B modifies endoplasmic reticulum membrane and plasma membrane permeability and facilitates virus release. Embo J. 1997; 16(12):3519-32. doi: 10.1093/emboj/16.12. 3519
    • (1997) Embo J , vol.16 , Issue.12 , pp. 3519-3532
    • van Kuppeveld FJM1    Jgj, H.2    Rll, S.3    Phgm, W.4    Hbpm, D.5    Jmd, G.6
  • 33
    • 0030728931 scopus 로고    scopus 로고
    • Inhibition of endoplasmic reticulum-To-Golgi traffic by poliovirus protein 3A: Genetic and ultrastructural analysis
    • Doedens JR, Giddings TH, Kirkegaard K. Inhibition of endoplasmic reticulum-To-Golgi traffic by poliovirus protein 3A: genetic and ultrastructural analysis. J Virol. 1997; 71(12):9054-64.
    • (1997) J Virol , vol.71 , Issue.12 , pp. 9054-9064
    • Doedens, J.R.1    Giddings, T.H.2    Kirkegaard, K.3
  • 34
    • 0033798416 scopus 로고    scopus 로고
    • Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: An autophagy-like origin for virus-induced vesicles
    • Suhy DA, Giddings TH, Kirkegaard K. Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: An autophagy-like origin for virus-induced vesicles. J Virol. 2000; 74 (19):8953-65. doi: 10.1128/jvi.74.19.8953-8965.2000
    • (2000) J Virol , vol.74 , Issue.19 , pp. 8953-8965
    • Suhy, D.A.1    Giddings, T.H.2    Kirkegaard, K.3
  • 35
    • 0025236535 scopus 로고
    • Structural organization of poliovirus RNA replication is mediated by viral proteins of the P2 genomic region
    • Bienz K, Egger D, Troxler M, Pasamontes L. Structural organization of poliovirus RNA replication is mediated by viral proteins of the P2 genomic region. J Virol. 1990; 64(3):1156-63.
    • (1990) J Virol , vol.64 , Issue.3 , pp. 1156-1163
    • Bienz, K.1    Egger, D.2    Troxler, M.3    Pasamontes, L.4
  • 36
    • 14744283953 scopus 로고    scopus 로고
    • Intracellular location and translocation of silent and active poliovirus replication complexes
    • Egger D, Bienz K. Intracellular location and translocation of silent and active poliovirus replication complexes. J Gen Virol. 2005; 86(3):707-18. doi: 10.1099/vir.0.80442-0.
    • (2005) J Gen Virol , vol.86 , Issue.3 , pp. 707-718
    • Egger, D.1    Bienz, K.2
  • 37
    • 77649164867 scopus 로고    scopus 로고
    • Evolutionary gain offunction for the ER membrane protein sec62 from yeast to humans
    • Muller L, de Escauriaza MD, Lajoie P, Theis M, Jung M, Muller A, et al. Evolutionary gain offunction for the ER membrane protein sec62 from yeast to humans. Mol Biol Cell. 2010; 21(5):691-703. doi: 10. 1091/mbc.E09-08-0730
    • (2011) Mol Biol Cell , vol.21 , Issue.5 , pp. 691-703
    • Muller, L.1    De Escauriaza, M.D.2    Lajoie, P.3    Theis, M.4    Jung, M.5    Muller, A.6
  • 38
    • 84885169812 scopus 로고    scopus 로고
    • The signal sequence influences post-Translational ER translocation at distinct stages
    • Johnson N, Habdenteufel S, Theis M, Paton AW, Paton JC, Zimmermann R, et al. The signal sequence influences post-Translational ER translocation at distinct stages. Plos One. 2013; 8(10):e75394. doi: ARTN e75394. doi: 10.1371/journal.pone.0075394
    • (2013) Plos One , vol.8 , Issue.10 , pp. e75394
    • Johnson, N.1    Habdenteufel, S.2    Theis, M.3    Paton, A.W.4    Paton, J.C.5    Zimmermann, R.6
  • 39
    • 0034053846 scopus 로고    scopus 로고
    • Aminoacyl-TRNA synthetases, the genetic code, and the evolutionary process
    • Woese CR, Olsen GJ, Ibba M, SOll D. Aminoacyl-TRNA synthetases, the genetic code, and the evolutionary process. Microbiol Mol Biol Rev. 2000; 64(1):202-36. doi: 10.1128/mmbr.64.1.202-236.2000
    • (2000) Microbiol Mol Biol Rev , vol.64 , Issue.1 , pp. 202-236
    • Woese, C.R.1    Olsen, G.J.2    Ibba, M.3    SOll, D.4
  • 40
    • 77956095201 scopus 로고    scopus 로고
    • New functions of aminoacyl-TRNA synthetases beyond translation
    • Guo M, Yang X-L, Schimmel P. New functions of aminoacyl-TRNA synthetases beyond translation. Nat Rev Mol Cell Biol. 2010; 11(9):668-74. doi: 10.1038/nrm2956
    • (2011) Nat Rev Mol Cell Biol , vol.11 , Issue.9 , pp. 668-674
    • Guo, M.1    Yang, X.-L.2    Schimmel, P.3
  • 41
    • 80053152058 scopus 로고    scopus 로고
    • Aminoacyl-TRNA synthetases and tumorigenesis: More than housekeeping
    • Kim S, You S, Hwang D. Aminoacyl-TRNA synthetases and tumorigenesis: more than housekeeping. Nat Rev Cancer. 2011; 11(10):708-18.. doi: 10.1038/nrc3124
    • (2011) Nat Rev Cancer , vol.11 , Issue.10 , pp. 708-718
    • Kim, S.1    You, S.2    Hwang, D.3
  • 42
    • 78650210763 scopus 로고    scopus 로고
    • Leukoencephalopathy with brainstem and spinal cord Involvement and Normal Lactate: A New Mutation in the DARS2 Gene
    • Lin J, Chiconelli Faria E, Da Rocha AJ, Rodrigues Masruha M, Pereira Vilanova LC, Scheper GC, et al. Leukoencephalopathy With Brainstem and Spinal Cord Involvement and Normal Lactate: A New Mutation in the DARS2 Gene. J Child Neurol. 2010; 25(11):1425-8. doi: 10.1177/0883073810370897.
    • (2011) J Child Neurol , vol.25 , Issue.11 , pp. 1425-1428
    • Lin, J.1    Chiconelli Faria, E.2    Da Rocha, A.J.3    Rodrigues Masruha, M.4    Pereira Vilanova, L.C.5    Scheper, G.C.6
  • 43
    • 78751529272 scopus 로고    scopus 로고
    • A human pathology-related mutation prevents import of an aminoacyl-TRNA synthetase into mitochondria
    • Messmer M, Florentz C, Schwenzer H, Scheper GC, van der Knaap MS, Marechal-Drouard L, et al. A human pathology-related mutation prevents import of an aminoacyl-TRNA synthetase into mitochondria. Biochem J. 2011; 433(3):441-6. doi: 10.1042/bj20101902.
    • (2011) Biochem J , vol.433 , Issue.3 , pp. 441-446
    • Messmer, M.1    Florentz, C.2    Schwenzer, H.3    Scheper, G.C.4    Van Der Knaap, M.S.5    Marechal-Drouard, L.6
  • 44
    • 0346874331 scopus 로고    scopus 로고
    • Calcium regulates the expression of a Dictyostelium discoideum asparaginyl tRNA synthetase gene
    • Jaiswal JK, Nanjundiah V. Calcium regulates the expression of a Dictyostelium discoideum asparaginyl tRNA synthetase gene. J Biosci 2003; 28(6):697-707. doi: 10.1007/bf02708430.
    • (2003) J Biosci , vol.28 , Issue.6 , pp. 697-707
    • Jaiswal, J.K.1    Nanjundiah, V.2
  • 45
    • 0030834131 scopus 로고    scopus 로고
    • Poliovirus protein 2BC increases cytosolic free calcium concentrations
    • Aldabe R, Irurzun A, Carrasco L. Poliovirus protein 2BC increases cytosolic free calcium concentrations. J Virol. 1997; 71(8):6214-7.
    • (1997) J Virol , vol.71 , Issue.8 , pp. 6214-6217
    • Aldabe, R.1    Irurzun, A.2    Carrasco, L.3
  • 46
    • 0042335650 scopus 로고    scopus 로고
    • Mechanisms of membrane permeabilization by picornavirus 2B viroporin
    • Nieva JL, Agirre A, Nir S, Carrasco L. Mechanisms of membrane permeabilization by picornavirus 2B viroporin. FEBS Lett 2003; 552(1):68-73. doi: 10.1016/S0014-5793(03)00852-4.
    • (2003) FEBS Lett , vol.552 , Issue.1 , pp. 68-73
    • Nieva, J.L.1    Agirre, A.2    Nir, S.3    Carrasco, L.4
  • 47
    • 2442475430 scopus 로고    scopus 로고
    • The coxsackievirus 2B protein suppresses apoptotic host cell responses by manipulating intracellular Ca2+ homeostasis
    • Campanella M, de Jong AS, Lanke KWH, Melchers WJG, Willems P, Pinton P, et al. The coxsackievirus 2B protein suppresses apoptotic host cell responses by manipulating intracellular Ca2+ homeostasis. J Biol Chem. 2004; 279(18):18440-50. doi: 10.1074/jbc.M309494200.
    • (2004) J Biol Chem , vol.279 , Issue.18 , pp. 18440-18450
    • Campanella, M.1    De Jong, A.S.2    Kwh, L.3    Wjg, M.4    Willems, P.5    Pinton, P.6
  • 48
    • 12944321845 scopus 로고    scopus 로고
    • Enterovirus protein 2B po(u)res out the calcium: A viral strategy to survive?
    • van Kuppeveld FJM, de Jong AS, Melchers WJG, Willems P. Enterovirus protein 2B po(u)res out the calcium: A viral strategy to survive? Trends Microbiol 2005; 13(2):41-4. doi: 10.1016/j.tim.2004.12.005.
    • (2005) Trends Microbiol , vol.13 , Issue.2 , pp. 41-44
    • van Kuppeveld FJM1    De Jong, A.S.2    Wjg, M.3    Willems, P.4
  • 49
    • 33846620628 scopus 로고    scopus 로고
    • Palmitoylation-dependent protein sorting
    • Greaves J, Chamberlain LH. Palmitoylation-dependent protein sorting. J Cell Biol. 2007; 176(3):249-54. doi: 10.1083/jcb.200610151
    • (2007) J Cell Biol , vol.176 , Issue.3 , pp. 249-254
    • Greaves, J.1    Chamberlain, L.H.2
  • 50
    • 33845794047 scopus 로고    scopus 로고
    • Palmitoylation: Policing protein stability and traffic
    • Linder ME, Deschenes RJ. Palmitoylation: policing protein stability and traffic. Nat Rev Mol Cell Biol. 2007; 8(1):74-84. doi: 10.1038/nrm2084.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , Issue.1 , pp. 74-84
    • Linder, M.E.1    Deschenes, R.J.2
  • 51
    • 0027222874 scopus 로고
    • Viral acylproteins: Greasing the wheels of assembly
    • Hruby DE, Franke CA. Viral acylproteins: Greasing the wheels of assembly. Trends Microbiol 1993; 1 (1):20-5..
    • (1993) Trends Microbiol , vol.1 , Issue.1 , pp. 20-25
    • Hruby, D.E.1    Franke, C.A.2
  • 52
    • 0035885077 scopus 로고    scopus 로고
    • Enzymatic depalmitoylation of viral glycoproteins with acyl-protein thioesterase 1 in vitro
    • Veit M, Schmidt MFG. Enzymatic depalmitoylation of viral glycoproteins with acyl-protein thioesterase 1 in vitro. Virology. 2001; 288(1):89-95. doi: 10.1006/viro.2001.1063.
    • (2001) Virology , vol.288 , Issue.1 , pp. 89-95
    • Veit, M.1    Mfg, S.2
  • 53
    • 69449086077 scopus 로고    scopus 로고
    • No strings attached: The ESCRT machinery in viral budding and cytokinesis
    • McDonald B, Martin-Serrano J. No strings attached: The ESCRT machinery in viral budding and cytokinesis. J Cell Sci. 2009; 122(13):2167-77. doi: 10.1242/jcs.028308
    • (2009) J Cell Sci , vol.122 , Issue.13 , pp. 2167-2177
    • McDonald, B.1    Martin-Serrano, J.2
  • 55
    • 29144474443 scopus 로고    scopus 로고
    • Late budding domains and host proteins in enveloped virus release
    • Bieniasz PD. Late budding domains and host proteins in enveloped virus release. Virology. 2006; 344 (1):55-63. doi: 10.1016/j.virol.2005.09.044.
    • (2006) Virology , vol.344 , Issue.1 , pp. 55-63
    • Bieniasz, P.D.1
  • 56
    • 58149103425 scopus 로고    scopus 로고
    • Functional reconstitution of ESCRT-III assembly and disassembly
    • Saksena S, Wahlman J, Teis D, Johnson AE, Emr SD. Functional reconstitution of ESCRT-III assembly and disassembly. Cell. 2009; 136(1):97-109. doi: http://dx.doi.org/10.1016/j.cell.2008.11.013
    • (2009) Cell , vol.136 , Issue.1 , pp. 97-109
    • Saksena, S.1    Wahlman, J.2    Teis, D.3    Johnson, A.E.4    Emr, S.D.5
  • 57
    • 0035853688 scopus 로고    scopus 로고
    • TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes
    • Bishop N, Woodman P. TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes. J Biol Chem. 2001; 276(15):11735-42. doi: 10.1074/jbc. M009863200.
    • (2001) J Biol Chem , vol.276 , Issue.15 , pp. 11735-11742
    • Bishop, N.1    Woodman, P.2
  • 58
    • 81355146605 scopus 로고    scopus 로고
    • Echovirus 1 infection depends on biogenesis of novel multivesicular bodies
    • Karjalainen M, Rintanen N, Lehkonen M, Kallio K, Mäki A, Hellström K, et al. Echovirus 1 infection depends on biogenesis of novel multivesicular bodies. Cell Microbiol. 2011; 13(12):1975-95. doi: 10. 1111/j.1462-5822.2011.01685.x.
    • (2011) Cell Microbiol , vol.13 , Issue.12 , pp. 1975-1995
    • Karjalainen, M.1    Rintanen, N.2    Lehkonen, M.3    Kallio, K.4    Mäki, A.5    Hellström, K.6
  • 60
    • 84865104488 scopus 로고    scopus 로고
    • Evi5 promotes collective cell migration through its Rab-GAP activity
    • Laflamme C, Assaker G, Ramel D, Dorn JF, She D, Maddox PS, et al. Evi5 promotes collective cell migration through its Rab-GAP activity. J Cell Biol. 2012; 198(1):57-67. doi: 10.1083/jcb.201112114
    • (2012) J Cell Biol , vol.198 , Issue.1 , pp. 57-67
    • Laflamme, C.1    Assaker, G.2    Ramel, D.3    Dorn, J.F.4    She, D.5    Maddox, P.S.6
  • 61
    • 0344303592 scopus 로고    scopus 로고
    • Apical recycling systems regulate directional budding of respiratory syncytial virus from polarized epithelial cells
    • Brock SC, Goldenring JR, Crowe JE. Apical recycling systems regulate directional budding of respiratory syncytial virus from polarized epithelial cells. Proc Natl Acad Sci U S A 2003; 100(25):15143-8. doi: 10.1073/pnas.2434327100
    • (2003) Proc Natl Acad Sci U S A , vol.100 , Issue.25 , pp. 15143-15148
    • Brock, S.C.1    Goldenring, J.R.2    Crowe, J.E.3
  • 63
    • 77952719625 scopus 로고    scopus 로고
    • The Rab11 pathway is required for influenza A virus budding and filament formation
    • Bruce EA, Digard P, Stuart AD. The Rab11 pathway is required for influenza A virus budding and filament formation. J Virol. 2010; 84(12):5848-59. doi: 10.1128/jvi.00307-10
    • (2011) J Virol , vol.84 , Issue.12 , pp. 5848-5859
    • Bruce, E.A.1    Digard, P.2    Stuart, A.D.3
  • 64
    • 56349103627 scopus 로고    scopus 로고
    • Roles for the recycling endosome Rab8 and Rab11 in hantavirus release from epithelial cells
    • Rowe RK, Suszko JW, Pekosz A. Roles for the recycling endosome, Rab8, and Rab11 in hantavirus release from epithelial cells. Virology. 2008; 382(2):239-49. doi: http://dx.doi.org/10.1016/j.virol.2008. 09.021
    • (2008) Virology , vol.382 , Issue.2 , pp. 239-249
    • Rowe, R.K.1    Suszko, J.W.2    Pekosz, A.3
  • 65
    • 77956205779 scopus 로고    scopus 로고
    • Trafficking of Sendai virus nucleocapsids is mediated by intracellular vesicles
    • Chambers R, Takimoto T. Trafficking of Sendai virus nucleocapsids is mediated by intracellular vesicles. Plos One. 2010; 5(6):e10994. doi: 10.1371/journal.pone.0010994.
    • (2011) Plos One , vol.5 , Issue.6 , pp. e10994
    • Chambers, R.1    Takimoto, T.2
  • 66
    • 66149117378 scopus 로고    scopus 로고
    • A dominant-negative mutant of rab5 inhibits infection of cells by foot-And-mouth disease virus: Implications for virus entry
    • Johns HL, Berryman S, Monaghan P, Belsham GJ, Jackson T. A dominant-negative mutant of rab5 inhibits infection of cells by foot-And-mouth disease virus: implications for virus entry. J Virol. 2009; 83 (12):6247-56. doi: 10.1128/jvi.02460-08
    • (2009) J Virol , vol.83 , Issue.12 , pp. 6247-6256
    • Johns, H.L.1    Berryman, S.2    Monaghan, P.3    Belsham, G.J.4    Jackson, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.