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Volumn 13, Issue 11, 2014, Pages 2836-2854

Quantitative proteomic analysis of host-virus interactions reveals a role for golgi brefeldin a resistance factor 1 (GBF1) in dengue infection

Author keywords

[No Author keywords available]

Indexed keywords

ACYL COENZYME A; EXPORTIN 1; GOLGI BREFELDIN A RESISTANCE FACTOR 1; GUANINE NUCLEOTIDE EXCHANGE FACTOR; HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 47; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK PROTEIN 90 ALPHA; HEAT SHOCK PROTEIN 90 BETA; HELICASE; HOST FACTOR; MONTIRELIN; NONSTRUCTURAL PROTEIN 5; PROTEINASE; UNCLASSIFIED DRUG; VIRUS PROTEIN; 7-DEHYDROCHOLESTEROL REDUCTASE; ARFGEF1 PROTEIN, HUMAN; GBF1 PROTEIN, HUMAN; GREEN FLUORESCENT PROTEIN; MICROTUBULE ASSOCIATED PROTEIN; NONHISTONE PROTEIN; NS3 PROTEIN, FLAVIVIRUS; NS5 PROTEIN, DENGUE VIRUS; OXIDOREDUCTASE; RNA HELICASE; SERINE PROTEINASE; SERPINH1 PROTEIN, HUMAN; SMALL INTERFERING RNA; ZW10 PROTEIN, HUMAN;

EID: 84910613036     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.038984     Document Type: Article
Times cited : (42)

References (103)
  • 2
    • 66149146738 scopus 로고    scopus 로고
    • NS5 of dengue virus mediates STAT2 binding and degradation
    • Ashour, J., Laurent-Rolle, M., Shi, P. Y., and Garcia-Sastre, A. (2009) NS5 of dengue virus mediates STAT2 binding and degradation. J. Virol. 83, 5408-5418
    • (2009) J. Virol. , vol.83 , pp. 5408-5418
    • Ashour, J.1    Laurent-Rolle, M.2    Shi, P.Y.3    Garcia-Sastre, A.4
  • 3
    • 77958100661 scopus 로고    scopus 로고
    • Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis
    • Heaton, N. S., Perera, R., Berger, K. L., Khadka, S., Lacount, D. J., Kuhn, R. J., and Randall, G. (2010) Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis. Proc. Natl. Acad. Sci. U.S.A. 107, 17345-17350
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 17345-17350
    • Heaton, N.S.1    Perera, R.2    Berger, K.L.3    Khadka, S.4    Lacount, D.J.5    Kuhn, R.J.6    Randall, G.7
  • 4
    • 41849101685 scopus 로고    scopus 로고
    • Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex
    • Moorman, N. J., Cristea, I. M., Terhune, S. S., Rout, M. P., Chait, B. T., and Shenk, T. (2008) Human cytomegalovirus protein UL38 inhibits host cell stress responses by antagonizing the tuberous sclerosis protein complex. Cell Host Microbe 3, 253-262
    • (2008) Cell Host Microbe , vol.3 , pp. 253-262
    • Moorman, N.J.1    Cristea, I.M.2    Terhune, S.S.3    Rout, M.P.4    Chait, B.T.5    Shenk, T.6
  • 5
    • 0037771203 scopus 로고    scopus 로고
    • Host factors in positive-strand RNA virus genome replication
    • Ahlquist, P., Noueiry, A. O., Lee, W. M., Kushner, D. B., and Dye, B. T. (2003) Host factors in positive-strand RNA virus genome replication. J. Virol. 77, 8181-8186
    • (2003) J. Virol. , vol.77 , pp. 8181-8186
    • Ahlquist, P.1    Noueiry, A.O.2    Lee, W.M.3    Kushner, D.B.4    Dye, B.T.5
  • 6
    • 34748873170 scopus 로고    scopus 로고
    • In: Knipe, D. M., Howley, P.M., ed. Fields Virology 5th Ed. Lippencott-Raven Publishers, Philadelphia
    • Lindenbach, B. D., Thiel, H., Rice, C.M., (2007) Flaviviridae: The Viruses and Their Replication (33). In: Knipe, D. M., Howley, P.M., ed. Fields Virology 5th Ed., pp. 1101-1152, Lippencott-Raven Publishers, Philadelphia
    • (2007) Flaviviridae: The Viruses and Their Replication , vol.33 , pp. 1101-1152
    • Lindenbach, B.D.1    Thiel, H.2    Rice, C.M.3
  • 7
    • 50849098592 scopus 로고    scopus 로고
    • Global spread and persistence of dengue
    • Kyle, J. L., and Harris, E. (2008) Global spread and persistence of dengue. Annu. Rev. Microbiol. 62, 71-92
    • (2008) Annu. Rev. Microbiol. , vol.62 , pp. 71-92
    • Kyle, J.L.1    Harris, E.2
  • 9
    • 79953035293 scopus 로고    scopus 로고
    • Immune response to dengue virus and prospects for a vaccine
    • Murphy, B. R., and Whitehead, S. S. (2011) Immune response to dengue virus and prospects for a vaccine. Annu. Rev. Immunol. 29, 587-619
    • (2011) Annu. Rev. Immunol. , vol.29 , pp. 587-619
    • Murphy, B.R.1    Whitehead, S.S.2
  • 10
    • 4844225284 scopus 로고    scopus 로고
    • Transmission cycles, host range, evolution and emergence of arboviral disease
    • Weaver, S. C., and Barrett, A. D. (2004) Transmission cycles, host range, evolution and emergence of arboviral disease. Nat. Rev. Microbiol. 2, 789-801
    • (2004) Nat. Rev. Microbiol. , vol.2 , pp. 789-801
    • Weaver, S.C.1    Barrett, A.D.2
  • 11
    • 0025116324 scopus 로고
    • Flavivirus genome organization, expression, and replication
    • Chambers, T. J., Hahn, C. S., Galler, R., and Rice, C. M. (1990) Flavivirus genome organization, expression, and replication. Annu. Rev. Microbiol. 44, 649-688
    • (1990) Annu. Rev. Microbiol. , vol.44 , pp. 649-688
    • Chambers, T.J.1    Hahn, C.S.2    Galler, R.3    Rice, C.M.4
  • 12
    • 0029863798 scopus 로고    scopus 로고
    • Recombinant dengue type 1 virus NS5 protein expressed in Escherichia coli exhibits RNA-dependent RNA polymerase activity
    • Tan, B. H., Fu, J., Sugrue, R. J., Yap, E. H., Chan, Y. C., and Tan, Y. H. (1996) Recombinant dengue type 1 virus NS5 protein expressed in Escherichia coli exhibits RNA-dependent RNA polymerase activity. Virology 216, 317-325
    • (1996) Virology , vol.216 , pp. 317-325
    • Tan, B.H.1    Fu, J.2    Sugrue, R.J.3    Yap, E.H.4    Chan, Y.C.5    Tan, Y.H.6
  • 13
    • 0037013858 scopus 로고    scopus 로고
    • An RNA cap (nucleoside-2-O-)-methyltransferase in the flavivirus RNA polymerase NS5: Crystal structure and functional characterization
    • Egloff, M. P., Benarroch, D., Selisko, B., Romette, J. L., and Canard, B. (2002) An RNA cap (nucleoside-2-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization. EMBO J. 21, 2757-2768
    • (2002) EMBO J. , vol.21 , pp. 2757-2768
    • Egloff, M.P.1    Benarroch, D.2    Selisko, B.3    Romette, J.L.4    Canard, B.5
  • 14
    • 0024341494 scopus 로고
    • N-terminal domains of putative helicases of flavi-and pestiviruses may be serine proteases
    • Gorbalenya, A. E., Donchenko, A. P., Koonin, E. V., and Blinov, V. M. (1989) N-terminal domains of putative helicases of flavi-and pestiviruses may be serine proteases. Nucleic Acids Res. 17, 3889-3897
    • (1989) Nucleic Acids Res. , vol.17 , pp. 3889-3897
    • Gorbalenya, A.E.1    Donchenko, A.P.2    Koonin, E.V.3    Blinov, V.M.4
  • 16
    • 0027366948 scopus 로고
    • The NS 3 nonstructural protein of flaviviruses contains an RNA triphosphatase activity
    • Wengler, G. (1993) The NS 3 nonstructural protein of flaviviruses contains an RNA triphosphatase activity. Virology 197, 265-273
    • (1993) Virology , vol.197 , pp. 265-273
    • Wengler, G.1
  • 17
    • 0027446550 scopus 로고
    • RNA-stimulated NTPase activity associated with yellow fever virus NS3 protein expressed in bacteria
    • Warrener, P., Tamura, J. K., and Collett, M. S. (1993) RNA-stimulated NTPase activity associated with yellow fever virus NS3 protein expressed in bacteria. J. Virol. 67, 989-996
    • (1993) J. Virol. , vol.67 , pp. 989-996
    • Warrener, P.1    Tamura, J.K.2    Collett, M.S.3
  • 18
    • 0029027850 scopus 로고
    • Association between NS3 and NS5 proteins of dengue virus type 2 in the putative RNA replicase is linked to differential phosphorylation of NS5
    • Kapoor, M., Zhang, L., Ramachandra, M., Kusukawa, J., Ebner, K. E., and Padmanabhan, R. (1995) Association between NS3 and NS5 proteins of dengue virus type 2 in the putative RNA replicase is linked to differential phosphorylation of NS5. J. Biol. Chem. 270, 19100-19106
    • (1995) J. Biol. Chem. , vol.270 , pp. 19100-19106
    • Kapoor, M.1    Zhang, L.2    Ramachandra, M.3    Kusukawa, J.4    Ebner, K.E.5    Padmanabhan, R.6
  • 21
    • 84875040462 scopus 로고    scopus 로고
    • Mapping the interactions of dengue virus NS1 protein with human liver proteins using a yeast two-hybrid system: Identification of C1q as an interacting partner
    • Silva, E. M., Conde, J. N., Allonso, D., Nogueira, M. L., and Mohana-Borges, R. (2013) Mapping the interactions of dengue virus NS1 protein with human liver proteins using a yeast two-hybrid system: identification of C1q as an interacting partner. PLoS One 8, e57514
    • (2013) PLoS One , vol.8 , pp. e57514
    • Silva, E.M.1    Conde, J.N.2    Allonso, D.3    Nogueira, M.L.4    Mohana-Borges, R.5
  • 22
  • 23
    • 1842850947 scopus 로고    scopus 로고
    • The non-structural 3 (NS3) protein of dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure
    • Chua, J. J., Ng, M. M., and Chow, V. T. (2004) The non-structural 3 (NS3) protein of dengue virus type 2 interacts with human nuclear receptor binding protein and is associated with alterations in membrane structure. Virus Res. 102, 151-163
    • (2004) Virus Res. , vol.102 , pp. 151-163
    • Chua, J.J.1    Ng, M.M.2    Chow, V.T.3
  • 25
    • 84862814793 scopus 로고    scopus 로고
    • Dengue virus utilizes calcium modulating cyclophilin-binding ligand to subvert apoptosis
    • Li, J., Huang, R., Liao, W., Chen, Z., and Zhang, S. (2012) Dengue virus utilizes calcium modulating cyclophilin-binding ligand to subvert apoptosis. Biochem. Biophys. Res. Commun. 418, 622-627
    • (2012) Biochem. Biophys. Res. Commun. , vol.418 , pp. 622-627
    • Li, J.1    Huang, R.2    Liao, W.3    Chen, Z.4    Zhang, S.5
  • 26
    • 80051942967 scopus 로고    scopus 로고
    • The interaction of flavivirus M protein with light chain Tctex-1 of human dynein plays a role in late stages of virus replication
    • Brault, J. B., Kudelko, M., Vidalain, P. O., Tangy, F., Despres, P., and Pardigon, N. (2011) The interaction of flavivirus M protein with light chain Tctex-1 of human dynein plays a role in late stages of virus replication. Virology 417, 369-378
    • (2011) Virology , vol.417 , pp. 369-378
    • Brault, J.B.1    Kudelko, M.2    Vidalain, P.O.3    Tangy, F.4    Despres, P.5    Pardigon, N.6
  • 27
    • 72949113004 scopus 로고    scopus 로고
    • Novel binding between pre-membrane protein and claudin-1 is required for efficient dengue virus entry
    • Gao, F., Duan, X., Lu, X., Liu, Y., Zheng, L., Ding, Z., and Li, J. (2010) Novel binding between pre-membrane protein and claudin-1 is required for efficient dengue virus entry. Biochem. Biophys. Res. Commun. 391, 952-957
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 952-957
    • Gao, F.1    Duan, X.2    Lu, X.3    Liu, Y.4    Zheng, L.5    Ding, Z.6    Li, J.7
  • 29
    • 46049104671 scopus 로고    scopus 로고
    • Novel binding between premembrane protein and vacuolar ATPase is required for efficient dengue virus secretion
    • Duan, X., Lu, X., Li, J., and Liu, Y. (2008) Novel binding between premembrane protein and vacuolar ATPase is required for efficient dengue virus secretion. Biochem. Biophys. Res. Commun. 373, 319-324
    • (2008) Biochem. Biophys. Res. Commun. , vol.373 , pp. 319-324
    • Duan, X.1    Lu, X.2    Li, J.3    Liu, Y.4
  • 30
    • 67349133117 scopus 로고    scopus 로고
    • Polypyrimidine tract-binding protein influences negative strand RNA synthesis of dengue virus
    • Jiang, L., Yao, H., Duan, X., Lu, X., and Liu, Y. (2009) Polypyrimidine tract-binding protein influences negative strand RNA synthesis of dengue virus. Biochem. Biophys. Res. Commun. 385, 187-192
    • (2009) Biochem. Biophys. Res. Commun. , vol.385 , pp. 187-192
    • Jiang, L.1    Yao, H.2    Duan, X.3    Lu, X.4    Liu, Y.5
  • 31
    • 77954263501 scopus 로고    scopus 로고
    • Human Sec3 protein is a novel transcriptional and translational repressor of flavivirus
    • Bhuvanakantham, R., Li, J., Tan, T. T., and Ng, M. L. (2010) Human Sec3 protein is a novel transcriptional and translational repressor of flavivirus. Cell Microbiol. 12, 453-472
    • (2010) Cell Microbiol. , vol.12 , pp. 453-472
    • Bhuvanakantham, R.1    Li, J.2    Tan, T.T.3    Ng, M.L.4
  • 32
    • 80052361705 scopus 로고    scopus 로고
    • Dengue virus capsid protein binds core histones and inhibits nucleosome formation in human liver cells
    • Colpitts, T. M., Barthel, S., Wang, P., and Fikrig, E. (2011) Dengue virus capsid protein binds core histones and inhibits nucleosome formation in human liver cells. PLoS One 6, e24365
    • (2011) PLoS One , vol.6 , pp. e24365
    • Colpitts, T.M.1    Barthel, S.2    Wang, P.3    Fikrig, E.4
  • 34
    • 34548605608 scopus 로고    scopus 로고
    • Secreted complement regulatory protein clusterin interacts with dengue virus nonstructural protein 1
    • Kurosu, T., Chaichana, P., Yamate, M., Anantapreecha, S., and Ikuta, K. (2007) Secreted complement regulatory protein clusterin interacts with dengue virus nonstructural protein 1. Biochem. Biophys. Res. Commun. 362, 1051-1056
    • (2007) Biochem. Biophys. Res. Commun. , vol.362 , pp. 1051-1056
    • Kurosu, T.1    Chaichana, P.2    Yamate, M.3    Anantapreecha, S.4    Ikuta, K.5
  • 35
    • 79960951711 scopus 로고    scopus 로고
    • Use of a tandem affinity purification assay to detect interactions between West Nile and dengue viral proteins and proteins of the mosquito vector
    • Colpitts, T. M., Cox, J., Nguyen, A., Feitosa, F., Krishnan, M. N., and Fikrig, E. (2011) Use of a tandem affinity purification assay to detect interactions between West Nile and dengue viral proteins and proteins of the mosquito vector. Virology 417, 179-187
    • (2011) Virology , vol.417 , pp. 179-187
    • Colpitts, T.M.1    Cox, J.2    Nguyen, A.3    Feitosa, F.4    Krishnan, M.N.5    Fikrig, E.6
  • 39
    • 77954485440 scopus 로고    scopus 로고
    • Human cytomegalovirus pUL83 stimulates activity of the viral immediate-early promoter through its interaction with the cellular IFI16 protein
    • Cristea, I. M., Moorman, N. J., Terhune, S. S., Cuevas, C. D., O'Keefe, E. S., Rout, M. P., Chait, B. T., and Shenk, T. (2010) Human cytomegalovirus pUL83 stimulates activity of the viral immediate-early promoter through its interaction with the cellular IFI16 protein. J. Virol. 84, 7803-7814
    • (2010) J. Virol. , vol.84 , pp. 7803-7814
    • Cristea, I.M.1    Moorman, N.J.2    Terhune, S.S.3    Cuevas, C.D.4    O'Keefe, E.S.5    Rout, M.P.6    Chait, B.T.7    Shenk, T.8
  • 40
    • 77953320616 scopus 로고    scopus 로고
    • Host factors associated with the Sindbis virus RNA-dependent RNA polymerase: Role for G3BP1 and G3BP2 in virus replication
    • Cristea, I. M., Rozjabek, H., Molloy, K. R., Karki, S., White, L. L., Rice, C. M., Rout, M. P., Chait, B. T., and MacDonald, M. R. (2010) Host factors associated with the Sindbis virus RNA-dependent RNA polymerase: role for G3BP1 and G3BP2 in virus replication. J. Virol. 84, 6720-6732
    • (2010) J. Virol. , vol.84 , pp. 6720-6732
    • Cristea, I.M.1    Rozjabek, H.2    Molloy, K.R.3    Karki, S.4    White, L.L.5    Rice, C.M.6    Rout, M.P.7    Chait, B.T.8    Macdonald, M.R.9
  • 41
    • 77951790602 scopus 로고    scopus 로고
    • A targeted spatial-temporal proteomics approach implicates multiple cellular trafficking pathways in human cytomegalovirus virion maturation
    • Moorman, N. J., Sharon-Friling, R., Shenk, T., and Cristea, I. M. (2010) A targeted spatial-temporal proteomics approach implicates multiple cellular trafficking pathways in human cytomegalovirus virion maturation. Mol. Cell. Proteomics 9, 851-860
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 851-860
    • Moorman, N.J.1    Sharon-Friling, R.2    Shenk, T.3    Cristea, I.M.4
  • 42
    • 26844556166 scopus 로고    scopus 로고
    • I-DIRT, a general method for distinguishing between specific and nonspecific protein interactions
    • Tackett, A. J., DeGrasse, J. A., Sekedat, M. D., Oeffinger, M., Rout, M. P., and Chait, B. T. (2005) I-DIRT, a general method for distinguishing between specific and nonspecific protein interactions. J. Proteome Res. 4, 1752-1756
    • (2005) J. Proteome Res. , vol.4 , pp. 1752-1756
    • Tackett, A.J.1    Degrasse, J.A.2    Sekedat, M.D.3    Oeffinger, M.4    Rout, M.P.5    Chait, B.T.6
  • 43
    • 0035211284 scopus 로고    scopus 로고
    • Replication of dengue virus type 2 in human monocytederived macrophages: Comparisons of isolates and recombinant viruses with substitutions at amino acid 390 in the envelope glycoprotein
    • Pryor, M. J., Carr, J. M., Hocking, H., Davidson, A. D., Li, P., and Wright, P. J. (2001) Replication of dengue virus type 2 in human monocytederived macrophages: comparisons of isolates and recombinant viruses with substitutions at amino acid 390 in the envelope glycoprotein. Am. J. Trop. Med Hyg. 65, 427-434
    • (2001) Am. J. Trop. Med Hyg. , vol.65 , pp. 427-434
    • Pryor, M.J.1    Carr, J.M.2    Hocking, H.3    Davidson, A.D.4    Li, P.5    Wright, P.J.6
  • 45
    • 0035950611 scopus 로고    scopus 로고
    • Interferon inhibits dengue virus infection by preventing translation of viral RNA through a PKR-independent mechanism
    • Diamond, M. S., and Harris, E. (2001) Interferon inhibits dengue virus infection by preventing translation of viral RNA through a PKR-independent mechanism. Virology 289, 297-311
    • (2001) Virology , vol.289 , pp. 297-311
    • Diamond, M.S.1    Harris, E.2
  • 46
    • 78249237877 scopus 로고    scopus 로고
    • Poliovirus replication requires the N-terminus but not the catalytic Sec7 domain of ArfGEF GBF1
    • Belov, G. A., Kovtunovych, G., Jackson, C. L., and Ehrenfeld, E. (2010) Poliovirus replication requires the N-terminus but not the catalytic Sec7 domain of ArfGEF GBF1. Cell Microbiol. 12, 1463-1479
    • (2010) Cell Microbiol. , vol.12 , pp. 1463-1479
    • Belov, G.A.1    Kovtunovych, G.2    Jackson, C.L.3    Ehrenfeld, E.4
  • 48
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteomewide protein quantification
    • Cox, J., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p.p.b.-range mass accuracies and proteomewide protein quantification. Nat Biotechnol. 26, 1367-1372
    • (2008) Nat Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 49
    • 67649400942 scopus 로고    scopus 로고
    • A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics
    • Cox, J., Matic, I., Hilger, M., Nagaraj, N., Selbach, M., Olsen, J. V., and Mann, M. (2009) A practical guide to the MaxQuant computational platform for SILAC-based quantitative proteomics. Nat. Protoc. 4, 698-705
    • (2009) Nat. Protoc. , vol.4 , pp. 698-705
    • Cox, J.1    Matic, I.2    Hilger, M.3    Nagaraj, N.4    Selbach, M.5    Olsen, J.V.6    Mann, M.7
  • 52
    • 33846052176 scopus 로고    scopus 로고
    • QPrimerDepot: A primer database for quantitative real time PCR
    • Cui, W., Taub, D. D., and Gardner, K. (2007) qPrimerDepot: a primer database for quantitative real time PCR. Nucleic Acids Res. 35, D805-D809
    • (2007) Nucleic Acids Res. , vol.35 , pp. D805-D809
    • Cui, W.1    Taub, D.D.2    Gardner, K.3
  • 53
    • 75549089019 scopus 로고    scopus 로고
    • PrimerBank: A resource of human and mouse PCR primer pairs for gene expression detection and quantification
    • Spandidos, A., Wang, X., Wang, H., and Seed, B. (2010) PrimerBank: a resource of human and mouse PCR primer pairs for gene expression detection and quantification. Nucleic Acids Res. 38, D792-D799
    • (2010) Nucleic Acids Res. , vol.38 , pp. D792-D799
    • Spandidos, A.1    Wang, X.2    Wang, H.3    Seed, B.4
  • 54
    • 67650520190 scopus 로고    scopus 로고
    • The polypyrimidine tract-binding protein is required for efficient dengue virus propagation and associates with the viral replication machinery
    • Anwar, A., Leong, K. M., Ng, M. L., Chu, J. J., and Garcia-Blanco, M. A. (2009) The polypyrimidine tract-binding protein is required for efficient dengue virus propagation and associates with the viral replication machinery. J. Biol. Chem. 284, 17021-17029
    • (2009) J. Biol. Chem. , vol.284 , pp. 17021-17029
    • Anwar, A.1    Leong, K.M.2    Ng, M.L.3    Chu, J.J.4    Garcia-Blanco, M.A.5
  • 55
    • 34250899898 scopus 로고    scopus 로고
    • Nuclear localization of dengue virus nonstructural protein 5 through its importin alpha/beta-recognized nuclear localization sequences is integral to viral infection
    • Pryor, M. J., Rawlinson, S. M., Butcher, R. E., Barton, C. L., Waterhouse, T. A., Vasudevan, S. G., Bardin, P. G., Wright, P. J., Jans, D. A., and Davidson, A. D. (2007) Nuclear localization of dengue virus nonstructural protein 5 through its importin alpha/beta-recognized nuclear localization sequences is integral to viral infection. Traffic 8, 795-807
    • (2007) Traffic , vol.8 , pp. 795-807
    • Pryor, M.J.1    Rawlinson, S.M.2    Butcher, R.E.3    Barton, C.L.4    Waterhouse, T.A.5    Vasudevan, S.G.6    Bardin, P.G.7    Wright, P.J.8    Jans, D.A.9    Davidson, A.D.10
  • 56
    • 67650106549 scopus 로고    scopus 로고
    • CRM1-mediated nuclear export of dengue virus RNA polymerase NS5 modulates interleukin-8 induction and virus production
    • Rawlinson, S. M., Pryor, M. J., Wright, P. J., and Jans, D. A. (2009) CRM1-mediated nuclear export of dengue virus RNA polymerase NS5 modulates interleukin-8 induction and virus production. J. Biol. Chem. 284, 15589-15597
    • (2009) J. Biol. Chem. , vol.284 , pp. 15589-15597
    • Rawlinson, S.M.1    Pryor, M.J.2    Wright, P.J.3    Jans, D.A.4
  • 60
    • 80054729346 scopus 로고    scopus 로고
    • COPII and COPI traffic at the ER-Golgi interface
    • Szul, T., and Sztul, E. (2011) COPII and COPI traffic at the ER-Golgi interface. Physiology 26, 348-364
    • (2011) Physiology , vol.26 , pp. 348-364
    • Szul, T.1    Sztul, E.2
  • 61
    • 0033549576 scopus 로고    scopus 로고
    • GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5
    • Claude, A., Zhao, B. P., Kuziemsky, C. E., Dahan, S., Berger, S. J., Yan, J. P., Armold, A. D., Sullivan, E. M., and Melancon, P. (1999) GBF1: A novel Golgi-associated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. J. Cell Biol. 146, 71-84
    • (1999) J. Cell Biol. , vol.146 , pp. 71-84
    • Claude, A.1    Zhao, B.P.2    Kuziemsky, C.E.3    Dahan, S.4    Berger, S.J.5    Yan, J.P.6    Armold, A.D.7    Sullivan, E.M.8    Melancon, P.9
  • 62
    • 0033950864 scopus 로고    scopus 로고
    • Turning on ARF: The Sec7 family of guanine-nucleotide-exchange factors
    • Jackson, C. L., and Casanova, J. E. (2000) Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors. Trends Cell Biol. 10, 60-67
    • (2000) Trends Cell Biol. , vol.10 , pp. 60-67
    • Jackson, C.L.1    Casanova, J.E.2
  • 64
    • 0033617147 scopus 로고    scopus 로고
    • Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors
    • Togawa, A., Morinaga, N., Ogasawara, M., Moss, J., and Vaughan, M. (1999) Purification and cloning of a brefeldin A-inhibited guanine nucleotide-exchange protein for ADP-ribosylation factors. J. Biol. Chem. 274, 12308-12315
    • (1999) J. Biol. Chem. , vol.274 , pp. 12308-12315
    • Togawa, A.1    Morinaga, N.2    Ogasawara, M.3    Moss, J.4    Vaughan, M.5
  • 65
    • 0015583966 scopus 로고
    • Proteins specified by group B togaviruses in mammalian cells during productive infections
    • Westaway, E. G. (1973) Proteins specified by group B togaviruses in mammalian cells during productive infections. Virology 51, 454-465
    • (1973) Virology , vol.51 , pp. 454-465
    • Westaway, E.G.1
  • 66
    • 0030846512 scopus 로고    scopus 로고
    • Ultrastructure of Kunjin virus-infected cells: Colocalization of NS1 and NS3 with double-stranded RNA, and of NS2B with NS3, in virus-induced membrane structures
    • Westaway, E. G., Mackenzie, J. M., Kenney, M. T., Jones, M. K., and Khromykh, A. A. (1997) Ultrastructure of Kunjin virus-infected cells: colocalization of NS1 and NS3 with double-stranded RNA, and of NS2B with NS3, in virus-induced membrane structures. J. Virol. 71, 6650-6661
    • (1997) J. Virol. , vol.71 , pp. 6650-6661
    • Westaway, E.G.1    Mackenzie, J.M.2    Kenney, M.T.3    Jones, M.K.4    Khromykh, A.A.5
  • 68
    • 84883292729 scopus 로고    scopus 로고
    • The cellular interactome of the coronavirus infectious bronchitis virus nucleocapsid protein and functional implications for virus biology
    • Emmott, E., Munday, D., Bickerton, E., Britton, P., Rodgers, M. A., Whitehouse, A., Zhou, E. M., and Hiscox, J. A. (2013) The cellular interactome of the coronavirus infectious bronchitis virus nucleocapsid protein and functional implications for virus biology. J. Virol. 87, 9486-9500
    • (2013) J. Virol. , vol.87 , pp. 9486-9500
    • Emmott, E.1    Munday, D.2    Bickerton, E.3    Britton, P.4    Rodgers, M.A.5    Whitehouse, A.6    Zhou, E.M.7    Hiscox, J.A.8
  • 69
    • 84864390283 scopus 로고    scopus 로고
    • The interactome of the human respiratory syncytial virus NS1 protein highlights multiple effects on host cell biology
    • Wu, W., Tran, K. C., Teng, M. N., Heesom, K. J., Matthews, D. A., Barr, J. N., and Hiscox, J. A. (2012) The interactome of the human respiratory syncytial virus NS1 protein highlights multiple effects on host cell biology. J. Virol. 86, 7777-7789
    • (2012) J. Virol. , vol.86 , pp. 7777-7789
    • Wu, W.1    Tran, K.C.2    Teng, M.N.3    Heesom, K.J.4    Matthews, D.A.5    Barr, J.N.6    Hiscox, J.A.7
  • 71
    • 42949091438 scopus 로고    scopus 로고
    • Unfolded protein response and cell death after depletion of brefeldin A-inhibited guanine nucleotide-exchange protein GBF1
    • Citterio, C., Vichi, A., Pacheco-Rodriguez, G., Aponte, A. M., Moss, J., and Vaughan, M. (2008) Unfolded protein response and cell death after depletion of brefeldin A-inhibited guanine nucleotide-exchange protein GBF1. Proc. Natl. Acad. Sci. U.S.A. 105, 2877-2882
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 2877-2882
    • Citterio, C.1    Vichi, A.2    Pacheco-Rodriguez, G.3    Aponte, A.M.4    Moss, J.5    Vaughan, M.6
  • 72
    • 0032863958 scopus 로고    scopus 로고
    • Markers for trans-Golgi membranes and the intermediate compartment localize to induced membranes with distinct replication functions in flavivirusinfected cells
    • Mackenzie, J. M., Jones, M. K., and Westaway, E. G. (1999) Markers for trans-Golgi membranes and the intermediate compartment localize to induced membranes with distinct replication functions in flavivirusinfected cells. J. Virol. 73, 9555-9567
    • (1999) J. Virol. , vol.73 , pp. 9555-9567
    • Mackenzie, J.M.1    Jones, M.K.2    Westaway, E.G.3
  • 74
    • 79957473559 scopus 로고    scopus 로고
    • ARF family G proteins and their regulators: Roles in membrane transport, development and disease
    • Donaldson, J. G., and Jackson, C. L. (2011) ARF family G proteins and their regulators: roles in membrane transport, development and disease. Nat. Rev. Mol. Cell Biol. 12, 362-375
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 362-375
    • Donaldson, J.G.1    Jackson, C.L.2
  • 76
    • 80053446744 scopus 로고    scopus 로고
    • Chlamydia trachomatis co-opts GBF1 and CERT to acquire host sphingomyelin for distinct roles during intracellular development
    • Elwell, C. A., Jiang, S., Kim, J. H., Lee, A., Wittmann, T., Hanada, K., Melancon, P., and Engel, J. N. (2011) Chlamydia trachomatis co-opts GBF1 and CERT to acquire host sphingomyelin for distinct roles during intracellular development. PLoS Pathog. 7, e1002198
    • (2011) PLoS Pathog. , vol.7 , pp. e1002198
    • Elwell, C.A.1    Jiang, S.2    Kim, J.H.3    Lee, A.4    Wittmann, T.5    Hanada, K.6    Melancon, P.7    Engel, J.N.8
  • 79
    • 84885459411 scopus 로고    scopus 로고
    • Targeting of the Arf-GEF GBF1 to lipid droplets and Golgi membranes
    • Bouvet, S., Golinelli-Cohen, M. P., Contremoulins, V., and Jackson, C. L. (2013) Targeting of the Arf-GEF GBF1 to lipid droplets and Golgi membranes. J. Cell Sci. 126, 4794-4805
    • (2013) J. Cell Sci. , vol.126 , pp. 4794-4805
    • Bouvet, S.1    Golinelli-Cohen, M.P.2    Contremoulins, V.3    Jackson, C.L.4
  • 83
    • 84872840929 scopus 로고    scopus 로고
    • Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover
    • Olzmann, J. A., Richter, C. M., and Kopito, R. R. (2013) Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover. Proc. Natl. Acad. Sci. U.S.A. 110, 1345-1350
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 1345-1350
    • Olzmann, J.A.1    Richter, C.M.2    Kopito, R.R.3
  • 84
    • 0034767341 scopus 로고    scopus 로고
    • Assembly and maturation of the flavivirus Kunjin virus appear to occur in the rough endoplasmic reticulum and along the secretory pathway, respectively
    • Mackenzie, J. M., and Westaway, E. G. (2001) Assembly and maturation of the flavivirus Kunjin virus appear to occur in the rough endoplasmic reticulum and along the secretory pathway, respectively. J. Virol. 75, 10787-10799
    • (2001) J. Virol. , vol.75 , pp. 10787-10799
    • Mackenzie, J.M.1    Westaway, E.G.2
  • 85
    • 1542676405 scopus 로고    scopus 로고
    • Molecular biology of flaviviruses
    • Lindenbach, B. D., and Rice, C. M. (2003) Molecular biology of flaviviruses. Adv Virus Res. 59, 23-61
    • (2003) Adv Virus Res. , vol.59 , pp. 23-61
    • Lindenbach, B.D.1    Rice, C.M.2
  • 86
    • 26944495290 scopus 로고    scopus 로고
    • Wrapping things up about virus RNA replication
    • Mackenzie, J. (2005) Wrapping things up about virus RNA replication. Traffic 6, 967-977
    • (2005) Traffic , vol.6 , pp. 967-977
    • Mackenzie, J.1
  • 87
    • 0025943380 scopus 로고
    • Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes
    • Wood, S. A., Park, J. E., and Brown, W. J. (1991) Brefeldin A causes a microtubule-mediated fusion of the trans-Golgi network and early endosomes. Cell 67, 591-600
    • (1991) Cell , vol.67 , pp. 591-600
    • Wood, S.A.1    Park, J.E.2    Brown, W.J.3
  • 88
    • 0024237306 scopus 로고
    • Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum
    • Fujiwara, T., Oda, K., Yokota, S., Takatsuki, A., and Ikehara, Y. (1988) Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J. Biol. Chem. 263, 18545-18552
    • (1988) J. Biol. Chem. , vol.263 , pp. 18545-18552
    • Fujiwara, T.1    Oda, K.2    Yokota, S.3    Takatsuki, A.4    Ikehara, Y.5
  • 89
    • 0026533754 scopus 로고
    • Inhibition of poliovirus RNA synthesis by brefeldin A
    • Maynell, L. A., Kirkegaard, K., and Klymkowsky, M. W. (1992) Inhibition of poliovirus RNA synthesis by brefeldin A. J. Virol. 66, 1985-1994
    • (1992) J. Virol. , vol.66 , pp. 1985-1994
    • Maynell, L.A.1    Kirkegaard, K.2    Klymkowsky, M.W.3
  • 90
    • 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, V. K., Pacheco, J. M., Henry, T. M., and Mason, P. W. (2001) 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 287, 151-162
    • (2001) Virology , vol.287 , pp. 151-162
    • O'Donnell, V.K.1    Pacheco, J.M.2    Henry, T.M.3    Mason, P.W.4
  • 91
    • 0026794415 scopus 로고
    • Involvement of membrane traffic in the replication of poliovirus genomes: Effects of brefeldin A
    • Irurzun, A., Perez, L., and Carrasco, L. (1992) Involvement of membrane traffic in the replication of poliovirus genomes: effects of brefeldin A. Virology 191, 166-175
    • (1992) Virology , vol.191 , pp. 166-175
    • Irurzun, A.1    Perez, L.2    Carrasco, L.3
  • 93
    • 70349298403 scopus 로고    scopus 로고
    • Mouse norovirus replication is associated with virus-induced vesicle clusters originating from membranes derived from the secretory pathway
    • Hyde, J. L., Sosnovtsev, S. V., Green, K. Y., Wobus, C., Virgin, H. W., and Mackenzie, J. M. (2009) Mouse norovirus replication is associated with virus-induced vesicle clusters originating from membranes derived from the secretory pathway. J. Virol. 83, 9709-9719
    • (2009) J. Virol. , vol.83 , pp. 9709-9719
    • Hyde, J.L.1    Sosnovtsev, S.V.2    Green, K.Y.3    Wobus, C.4    Virgin, H.W.5    Mackenzie, J.M.6
  • 94
    • 57149096870 scopus 로고    scopus 로고
    • A critical role of a cellular membrane traffic protein in poliovirus RNA replication
    • Belov, G. A., Feng, Q., Nikovics, K., Jackson, C. L., and Ehrenfeld, E. (2008) A critical role of a cellular membrane traffic protein in poliovirus RNA replication. PLoS Pathog. 4, e1000216
    • (2008) PLoS Pathog. , vol.4 , pp. e1000216
    • Belov, G.A.1    Feng, Q.2    Nikovics, K.3    Jackson, C.L.4    Ehrenfeld, E.5
  • 99
    • 79953221885 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A protein interacts with phosphatidylinositol 4-kinase type IIIalpha and regulates viral propagation
    • Lim, Y. S., and Hwang, S. B. (2011) Hepatitis C virus NS5A protein interacts with phosphatidylinositol 4-kinase type IIIalpha and regulates viral propagation. J. Biol. Chem. 286, 11290-11298
    • (2011) J. Biol. Chem. , vol.286 , pp. 11290-11298
    • Lim, Y.S.1    Hwang, S.B.2
  • 100
    • 77954368281 scopus 로고    scopus 로고
    • The phosphatidylinositol 4-kinase PI4KIIIalpha is required for the recruitment of GBF1 to Golgi membranes
    • Dumaresq-Doiron, K., Savard, M. F., Akam, S., Costantino, S., and Lefrancois, S. (2010) The phosphatidylinositol 4-kinase PI4KIIIalpha is required for the recruitment of GBF1 to Golgi membranes. J. Cell Sci. 123, 2273-2280
    • (2010) J. Cell Sci. , vol.123 , pp. 2273-2280
    • Dumaresq-Doiron, K.1    Savard, M.F.2    Akam, S.3    Costantino, S.4    Lefrancois, S.5
  • 101
    • 84863115228 scopus 로고    scopus 로고
    • ARF1 and GBF1 generate a PI4P-enriched environment supportive of hepatitis C virus replication
    • Zhang, L., Hong, Z., Lin, W., Shao, R. X., Goto, K., Hsu, V. W., and Chung, R. T. (2012) ARF1 and GBF1 generate a PI4P-enriched environment supportive of hepatitis C virus replication. PLoS One. 7, e32135
    • (2012) PLoS One. , vol.7 , pp. e32135
    • Zhang, L.1    Hong, Z.2    Lin, W.3    Shao, R.X.4    Goto, K.5    Hsu, V.W.6    Chung, R.T.7
  • 102
    • 34248345508 scopus 로고    scopus 로고
    • Molecular determinants of the interaction between coxsackievirus protein 3A and guanine nucleotide exchange factor GBF1
    • Wessels, E., Duijsings, D., Lanke, K. H., Melchers, W. J., Jackson, C. L., and van Kuppeveld, F. J. (2007) Molecular determinants of the interaction between coxsackievirus protein 3A and guanine nucleotide exchange factor GBF1. J. Virol. 81, 5238-5245
    • (2007) J. Virol. , vol.81 , pp. 5238-5245
    • Wessels, E.1    Duijsings, D.2    Lanke, K.H.3    Melchers, W.J.4    Jackson, C.L.5    Van Kuppeveld, F.J.6


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