메뉴 건너뛰기




Volumn 11, Issue 4, 2008, Pages 369-377

Structural proteomics of dengue virus

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; METHYLTRANSFERASE; NONSTRUCTURAL PROTEIN 3; NONSTRUCTURAL PROTEIN 5; VIRUS PROTEIN; VIRUS RNA;

EID: 48749123790     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2008.06.004     Document Type: Review
Times cited : (328)

References (70)
  • 1
    • 38049156543 scopus 로고    scopus 로고
    • Dengue and hemorrhagic fever: a potential threat to public health in the United States
    • Describes dengue virus as an emerging threat to global and national health.
    • Morens D.M., and Fauci A.S. Dengue and hemorrhagic fever: a potential threat to public health in the United States. JAMA 299 (2008) 214-216. Describes dengue virus as an emerging threat to global and national health.
    • (2008) JAMA , vol.299 , pp. 214-216
    • Morens, D.M.1    Fauci, A.S.2
  • 2
    • 38849209154 scopus 로고    scopus 로고
    • Pathogenic flaviviruses
    • Gould E.A., and Solomon T. Pathogenic flaviviruses. Lancet 371 (2008) 500-509
    • (2008) Lancet , vol.371 , pp. 500-509
    • Gould, E.A.1    Solomon, T.2
  • 3
    • 48749098857 scopus 로고    scopus 로고
    • The Flaviviruses
    • Acheson N.H. (Ed), John Wiley and Sons
    • Kuhn R.J. The Flaviviruses. In: Acheson N.H. (Ed). Fundamentals of Molecular Virology (2004), John Wiley and Sons 182-190
    • (2004) Fundamentals of Molecular Virology , pp. 182-190
    • Kuhn, R.J.1
  • 4
  • 5
    • 0037495036 scopus 로고    scopus 로고
    • A ligand-binding pocket in the dengue virus envelope glycoprotein
    • Modis Y., Ogata S., Clements D., and Harrison S.C. A ligand-binding pocket in the dengue virus envelope glycoprotein. Proc Natl Acad Sci U S A 100 (2003) 6986-6991
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6986-6991
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 6
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the Dengue virus envelope protein after fusion
    • Modis Y., Ogata S., Clements D., and Harrison S.C. Structure of the Dengue virus envelope protein after fusion. Nature 427 (2004) 313-319
    • (2004) Nature , vol.427 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 7
    • 11144244755 scopus 로고    scopus 로고
    • Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein
    • Modis Y., Ogata S., Clements D., and Harrison S.C. Variable surface epitopes in the crystal structure of dengue virus type 3 envelope glycoprotein. J Virol 79 (2005) 1223-1231
    • (2005) J Virol , vol.79 , pp. 1223-1231
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 9
  • 13
    • 41349112506 scopus 로고    scopus 로고
    • Structure of the flavivirus precursor membrane-envelope protein complex and its implication for maturation
    • This paper describes the atomic structure of the DENV pre-membrane protein (prM).
    • Li L., Lok S.-M., Yu I.-M., Zhang Y., Kuhn R., Chen J., and Rossmann M.G. Structure of the flavivirus precursor membrane-envelope protein complex and its implication for maturation. Science 319 (2008) 1830-1834. This paper describes the atomic structure of the DENV pre-membrane protein (prM).
    • (2008) Science , vol.319 , pp. 1830-1834
    • Li, L.1    Lok, S.-M.2    Yu, I.-M.3    Zhang, Y.4    Kuhn, R.5    Chen, J.6    Rossmann, M.G.7
  • 14
    • 41349112304 scopus 로고    scopus 로고
    • Structure of immature dengue virus at low pH primes proteolytic maturation
    • This paper examines an intermediate in the DENV assembly pathway. The study also demonstrates the reversible nature of structural protein rearrangements in the DENV particle.
    • Yu I.-M., Zhang W., Holdaway H.A., Li L., Kostyuchenko V.A., Chipman P.R., Kuhn R., Rossmann M.G., and Chen J. Structure of immature dengue virus at low pH primes proteolytic maturation. Science 319 (2008) 1834-1837. This paper examines an intermediate in the DENV assembly pathway. The study also demonstrates the reversible nature of structural protein rearrangements in the DENV particle.
    • (2008) Science , vol.319 , pp. 1834-1837
    • Yu, I.-M.1    Zhang, W.2    Holdaway, H.A.3    Li, L.4    Kostyuchenko, V.A.5    Chipman, P.R.6    Kuhn, R.7    Rossmann, M.G.8    Chen J9
  • 15
    • 0041563793 scopus 로고    scopus 로고
    • Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses
    • Navarro-Sanchez E., Altmeyer R., Amara A., Schwartz O., Fieschi F., Virelizier J.L., Arenzana-Seisdedos F., and Despres P. Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses. EMBO Rep 4 (2003) 723-728
    • (2003) EMBO Rep , vol.4 , pp. 723-728
    • Navarro-Sanchez, E.1    Altmeyer, R.2    Amara, A.3    Schwartz, O.4    Fieschi, F.5    Virelizier, J.L.6    Arenzana-Seisdedos, F.7    Despres, P.8
  • 17
    • 36049048272 scopus 로고    scopus 로고
    • Does Japanese encephalitis virus share the same cellular receptor with other mosquito-borne flaviviruses on the C6/36 mosquito cells?
    • Ren J., Ding T., Zhang W., Song J., and Ma W. Does Japanese encephalitis virus share the same cellular receptor with other mosquito-borne flaviviruses on the C6/36 mosquito cells?. Virol J 4 (2007) 83
    • (2007) Virol J , vol.4 , pp. 83
    • Ren, J.1    Ding, T.2    Zhang, W.3    Song, J.4    Ma, W.5
  • 19
    • 2442457815 scopus 로고    scopus 로고
    • Identification of GRP 78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2
    • Jindadamrongwech S., Thepparit C., and Smith D.R. Identification of GRP 78 (BiP) as a liver cell expressed receptor element for dengue virus serotype 2. Arch Virol 149 (2004) 915-927
    • (2004) Arch Virol , vol.149 , pp. 915-927
    • Jindadamrongwech, S.1    Thepparit, C.2    Smith, D.R.3
  • 20
    • 1542304538 scopus 로고    scopus 로고
    • Differential binding efficiency between the envelope protein of Japanese encephalitis virus variants and heparan sulfate on the cell surface
    • Liu H., Chiou S.S., and Chen W.J. Differential binding efficiency between the envelope protein of Japanese encephalitis virus variants and heparan sulfate on the cell surface. J Med Virol 72 (2004) 618-624
    • (2004) J Med Virol , vol.72 , pp. 618-624
    • Liu, H.1    Chiou, S.S.2    Chen, W.J.3
  • 23
    • 0028849770 scopus 로고
    • Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum
    • Falgout B., and Markoff L. Evidence that flavivirus NS1-NS2A cleavage is mediated by a membrane-bound host protease in the endoplasmic reticulum. J Virol 69 (1995) 7232-7243
    • (1995) J Virol , vol.69 , pp. 7232-7243
    • Falgout, B.1    Markoff, L.2
  • 24
    • 0025864149 scopus 로고
    • Both nonstructural proteins NS2B anbd NS3 are required for the proteolytic processing of dengue virus nonstructural proteins
    • Falgout B., Pethel M., Zhang Y.-M., and Lai C.-J. Both nonstructural proteins NS2B anbd NS3 are required for the proteolytic processing of dengue virus nonstructural proteins. J Virol 65 (1991) 2467-2475
    • (1991) J Virol , vol.65 , pp. 2467-2475
    • Falgout, B.1    Pethel, M.2    Zhang, Y.-M.3    Lai, C.-J.4
  • 25
    • 0025309446 scopus 로고
    • Production of yellow fever virus proteins in infected cells: identification of discrete polyprotein species and analysis of cleavage kinetics using region-specific polyclonal antisera
    • Chambers T.J., McCourt D.W., and Rice C.M. Production of yellow fever virus proteins in infected cells: identification of discrete polyprotein species and analysis of cleavage kinetics using region-specific polyclonal antisera. Virology 177 (1990) 159-174
    • (1990) Virology , vol.177 , pp. 159-174
    • Chambers, T.J.1    McCourt, D.W.2    Rice, C.M.3
  • 26
    • 0032863958 scopus 로고    scopus 로고
    • Markers for trans-Golgi membranes and the intermediate compartment localize to induced membranes with distinct replication functions in flavivirus-infected cells
    • Mackenzie J.M., Jones M.K., and Westaway E.G. Markers for trans-Golgi membranes and the intermediate compartment localize to induced membranes with distinct replication functions in flavivirus-infected cells. J Virol 73 (1999) 9555-9567
    • (1999) J Virol , vol.73 , pp. 9555-9567
    • Mackenzie, J.M.1    Jones, M.K.2    Westaway, E.G.3
  • 27
    • 34247848008 scopus 로고    scopus 로고
    • The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner
    • Predicts membrane topology of NS4A and is role in virus replication. In the absence of a crystal structure, these studies provide structural insight on this transmembrane protein.
    • Miller S., Kastner S., Krijnse-Locker J., Buhler S., and Bartenschlager R. The non-structural protein 4A of dengue virus is an integral membrane protein inducing membrane alterations in a 2K-regulated manner. J Biol Chem 282 (2007) 8873-8882. Predicts membrane topology of NS4A and is role in virus replication. In the absence of a crystal structure, these studies provide structural insight on this transmembrane protein.
    • (2007) J Biol Chem , vol.282 , pp. 8873-8882
    • Miller, S.1    Kastner, S.2    Krijnse-Locker, J.3    Buhler, S.4    Bartenschlager, R.5
  • 28
    • 0027486484 scopus 로고
    • Mutagenesis of the yellow fever virus NS2B protein: effects on proteolytic processing, NS2B-NS3 complex formation, and viral replication
    • Chambers T.J., Nestorowicz A., Amberg S.M., and Rice C.M. Mutagenesis of the yellow fever virus NS2B protein: effects on proteolytic processing, NS2B-NS3 complex formation, and viral replication. J Virol 67 (1993) 6797-6807
    • (1993) J Virol , vol.67 , pp. 6797-6807
    • Chambers, T.J.1    Nestorowicz, A.2    Amberg, S.M.3    Rice, C.M.4
  • 29
    • 0242362792 scopus 로고    scopus 로고
    • Activation of dengue protease autocleavage at the NS2B-NS3 junction by recombinant NS3 and GST-NS2B fusion proteins
    • Wu C.F., Wang S.H., Sun C.M., Hu S.T., and Syu W.J. Activation of dengue protease autocleavage at the NS2B-NS3 junction by recombinant NS3 and GST-NS2B fusion proteins. J Virol Methods 114 (2003) 45-54
    • (2003) J Virol Methods , vol.114 , pp. 45-54
    • Wu, C.F.1    Wang, S.H.2    Sun, C.M.3    Hu, S.T.4    Syu, W.J.5
  • 30
    • 37349023165 scopus 로고    scopus 로고
    • Crystal structure of the NS3 protease-helicase from dengue virus
    • This is the first crystal structure of a full-length multidomain protein of DENV.
    • Luo D., Xu T., Hunke C., Gruber G., Vasudevan S.G., and Lescar J. Crystal structure of the NS3 protease-helicase from dengue virus. J Virol 82 (2008) 173-183. This is the first crystal structure of a full-length multidomain protein of DENV.
    • (2008) J Virol , vol.82 , pp. 173-183
    • Luo, D.1    Xu, T.2    Hunke, C.3    Gruber, G.4    Vasudevan, S.G.5    Lescar, J.6
  • 32
    • 34247625945 scopus 로고    scopus 로고
    • Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold
    • Provides an interesting comparison of flaviviral protease structures including that of HCV.
    • Aleshin A.E., Shiryaev S.A., Strongin A.Y., and Liddington R.C. Structural evidence for regulation and specificity of flaviviral proteases and evolution of the Flaviviridae fold. Protein Sci 16 (2007) 795-806. Provides an interesting comparison of flaviviral protease structures including that of HCV.
    • (2007) Protein Sci , vol.16 , pp. 795-806
    • Aleshin, A.E.1    Shiryaev, S.A.2    Strongin, A.Y.3    Liddington, R.C.4
  • 33
    • 0030667792 scopus 로고    scopus 로고
    • Cotranslational membrane insertion of the serine proteinase precursor NS2B-NS3(Pro) of dengue virus type 2 is required for efficient in vitro processing and is mediated through the hydrophobic regions of NS2B
    • Clum S., Ebner K.E., and Padmanbhan R. Cotranslational membrane insertion of the serine proteinase precursor NS2B-NS3(Pro) of dengue virus type 2 is required for efficient in vitro processing and is mediated through the hydrophobic regions of NS2B. J Biol Chem 272 (1997) 30715-30723
    • (1997) J Biol Chem , vol.272 , pp. 30715-30723
    • Clum, S.1    Ebner, K.E.2    Padmanbhan, R.3
  • 34
    • 34250346935 scopus 로고    scopus 로고
    • Functional characterization of cis and trans protease activity of the flavivirus NS2B-NS3 protease
    • Examines the cis-trans activity of the flaviviral NS2B/NS3 protease.
    • Bera A.K., Kuhn R.J., and Smith J.L. Functional characterization of cis and trans protease activity of the flavivirus NS2B-NS3 protease. J Biol Chem 282 (2007) 12883-12892. Examines the cis-trans activity of the flaviviral NS2B/NS3 protease.
    • (2007) J Biol Chem , vol.282 , pp. 12883-12892
    • Bera, A.K.1    Kuhn, R.J.2    Smith, J.L.3
  • 36
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequencecomparisons and structure-function relationships
    • Gorbalenya A.E., and Koonin E.V. Helicases: Amino acid sequencecomparisons and structure-function relationships. Curr Opin Struct Biol 34 (1993) 419-429
    • (1993) Curr Opin Struct Biol , vol.34 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 37
    • 23244450531 scopus 로고    scopus 로고
    • Structure of the flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing
    • Wu J., Bera K., Kuhn R.J., and Smith J.L. Structure of the flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing. J Virol 79 (2005) 10268-10277
    • (2005) J Virol , vol.79 , pp. 10268-10277
    • Wu, J.1    Bera, K.2    Kuhn, R.J.3    Smith, J.L.4
  • 38
    • 40849130890 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of Japanese encephalitis virus NS3 helicase/nucleoside triphosphatase at a resolution of 1.8 Å
    • Yamashita T., Unno H., Mori Y., Tani H., Moriishi K., Takamizawa A., Agoh M., Tsukihara T., and Matsuura Y. Crystal structure of the catalytic domain of Japanese encephalitis virus NS3 helicase/nucleoside triphosphatase at a resolution of 1.8 Å. Virology 373 (2008) 426-436
    • (2008) Virology , vol.373 , pp. 426-436
    • Yamashita, T.1    Unno, H.2    Mori, Y.3    Tani, H.4    Moriishi, K.5    Takamizawa, A.6    Agoh, M.7    Tsukihara, T.8    Matsuura, Y.9
  • 39
    • 23244464646 scopus 로고    scopus 로고
    • Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 Å
    • Xu T., Sampath A., Chao A., Wen D., Nanao M., Chene P., Vasudevan S.G., and Lescar J. Structure of the Dengue virus helicase/nucleoside triphosphatase catalytic domain at a resolution of 2.4 Å. J Virol 79 (2005) 10278-10288
    • (2005) J Virol , vol.79 , pp. 10278-10288
    • Xu, T.1    Sampath, A.2    Chao, A.3    Wen, D.4    Nanao, M.5    Chene, P.6    Vasudevan, S.G.7    Lescar, J.8
  • 41
    • 0032518490 scopus 로고    scopus 로고
    • Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding
    • Kim J.L., Morgenstern K.A., Griffith J.P., Dwyer M.D., Thomson J.A., Murcko M.A., Lin C., and Caron P.R. Hepatitis C virus NS3 RNA helicase domain with a bound oligonucleotide: the crystal structure provides insights into the mode of unwinding. Structure 6 (1998) 89-100
    • (1998) Structure , vol.6 , pp. 89-100
    • Kim, J.L.1    Morgenstern, K.A.2    Griffith, J.P.3    Dwyer, M.D.4    Thomson, J.A.5    Murcko, M.A.6    Lin, C.7    Caron, P.R.8
  • 42
    • 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. 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 (1995) 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
  • 44
    • 41149101538 scopus 로고    scopus 로고
    • Yellow fever virus NS3 plays an essential role in virus assembly independent of its known enzymatic functions
    • This study describes a yet unidentified role for NS3 in flavivirus assembly.
    • Patkar C.G., and Kuhn R.J. Yellow fever virus NS3 plays an essential role in virus assembly independent of its known enzymatic functions. J Virol 82 (2008) 3342-3352. This study describes a yet unidentified role for NS3 in flavivirus assembly.
    • (2008) J Virol , vol.82 , pp. 3342-3352
    • Patkar, C.G.1    Kuhn, R.J.2
  • 45
    • 30844434186 scopus 로고    scopus 로고
    • Host cell killing by the West Nile Virus NS2B-NS3 proteolytic complex: NS3 alone is sufficient to recruit caspase-8-based apoptotic pathway
    • Ramanathan M.P., Chambers J.A., Pankhong P., Chattergoon M., Attatippaholkun W., Dang K., Shah N., and Weiner D.B. Host cell killing by the West Nile Virus NS2B-NS3 proteolytic complex: NS3 alone is sufficient to recruit caspase-8-based apoptotic pathway. Virology 345 (2006) 56-72
    • (2006) Virology , vol.345 , pp. 56-72
    • Ramanathan, M.P.1    Chambers, J.A.2    Pankhong, P.3    Chattergoon, M.4    Attatippaholkun, W.5    Dang, K.6    Shah, N.7    Weiner, D.B.8
  • 46
    • 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. An RNA cap (nucleoside-2′-O-)-methyltransferase in the flavivirus RNA polymerase NS5: crystal structure and functional characterization. EMBO J 21 (2002) 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
  • 48
    • 33748669852 scopus 로고    scopus 로고
    • West Nile virus 5′-cap structure is formed by sequential guanine N-7 and ribose 2′-O methylations by nonstructural protein 5
    • Ray D., Shah A., Tilgner M., Guo Y., Zhao Y., Dong H., Deas T.S., Zhou Y., Li H., and Shi P.Y. West Nile virus 5′-cap structure is formed by sequential guanine N-7 and ribose 2′-O methylations by nonstructural protein 5. J Virol 80 (2006) 8362-8370
    • (2006) J Virol , vol.80 , pp. 8362-8370
    • Ray, D.1    Shah, A.2    Tilgner, M.3    Guo, Y.4    Zhao, Y.5    Dong, H.6    Deas, T.S.7    Zhou, Y.8    Li, H.9    Shi, P.Y.10
  • 49
    • 34247610261 scopus 로고    scopus 로고
    • Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution
    • Structure of the DENV RNA-dependant RNA polymerase and highlights the functional regions of the protein.
    • Yap T.L., Xu T., Chen Y.L., Malet H., Egloff M.P., Canard B., Vasudevan S.G., and Lescar J. Crystal structure of the dengue virus RNA-dependent RNA polymerase catalytic domain at 1.85-angstrom resolution. J Virol 81 (2007) 4753-4765. Structure of the DENV RNA-dependant RNA polymerase and highlights the functional regions of the protein.
    • (2007) J Virol , vol.81 , pp. 4753-4765
    • Yap, T.L.1    Xu, T.2    Chen, Y.L.3    Malet, H.4    Egloff, M.P.5    Canard, B.6    Vasudevan, S.G.7    Lescar, J.8
  • 52
    • 0035061425 scopus 로고    scopus 로고
    • A small region of the dengue virus-encoded RNA-dependent RNA polymerase, NS5, confers interaction with both the nuclear transport receptor importin-β and the viral helicase, NS3
    • Johansson M., Brookes A.J., Jans D.A., and Vasudevan S.G. A small region of the dengue virus-encoded RNA-dependent RNA polymerase, NS5, confers interaction with both the nuclear transport receptor importin-β and the viral helicase, NS3. J Gen Virol 82 (2001) 735-745
    • (2001) J Gen Virol , vol.82 , pp. 735-745
    • Johansson, M.1    Brookes, A.J.2    Jans, D.A.3    Vasudevan, S.G.4
  • 53
    • 0037184036 scopus 로고    scopus 로고
    • The interdomain region of dengue NS5 protein that binds to the viral helicase NS3 contains independently functional importin β1 and importin α/β-recognised nuclear localisation signals (NLSs)
    • Brooks A.J., Johansson M., John A.V., Xu Y., Jans D.A., and Vasudevan S.G. The interdomain region of dengue NS5 protein that binds to the viral helicase NS3 contains independently functional importin β1 and importin α/β-recognised nuclear localisation signals (NLSs). J Biol Chem 277 (2002) 36399-36407
    • (2002) J Biol Chem , vol.277 , pp. 36399-36407
    • Brooks, A.J.1    Johansson, M.2    John, A.V.3    Xu, Y.4    Jans, D.A.5    Vasudevan, S.G.6
  • 54
    • 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
    • Demonstration of a cytoplasmic viral enzyme (NS5) localizing to the nucleus and discusses implication for viral-host interactions.
    • 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. Nuclear localization of dengue virus nonstructural protein 5 through its importin alpha/beta-recognized nuclear localization sequences is integral to viral infection. Traffic 8 (2007) 795-807. Demonstration of a cytoplasmic viral enzyme (NS5) localizing to the nucleus and discusses implication for viral-host interactions.
    • (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
  • 55
    • 0024502091 scopus 로고
    • Maturation of Japanese encephalitis virus glycoproteins produced by infected mammalian and mosquito cells
    • Mason P.W. Maturation of Japanese encephalitis virus glycoproteins produced by infected mammalian and mosquito cells. Virology 169 (1989) 354-364
    • (1989) Virology , vol.169 , pp. 354-364
    • Mason, P.W.1
  • 56
    • 0025373742 scopus 로고
    • Cell surface expression of yellow fever virus non-structural glycoprotein NS1: consequences of interaction with antibody
    • Schlesinger J.J., Brandriss M.W., Putnak J.R., and Walsh E.E. Cell surface expression of yellow fever virus non-structural glycoprotein NS1: consequences of interaction with antibody. J Gen Virol 71 Pt 3 (1990) 593-599
    • (1990) J Gen Virol , vol.71 , Issue.PART 3 , pp. 593-599
    • Schlesinger, J.J.1    Brandriss, M.W.2    Putnak, J.R.3    Walsh, E.E.4
  • 58
    • 0033602697 scopus 로고    scopus 로고
    • Nascent flavivirus RNA colocalized in situ with double-stranded RNA in stable replication complexes
    • Westaway E.G., Khromykh A.A., and Mackenzie J.M. Nascent flavivirus RNA colocalized in situ with double-stranded RNA in stable replication complexes. Virology 258 (1999) 108-117
    • (1999) Virology , vol.258 , pp. 108-117
    • Westaway, E.G.1    Khromykh, A.A.2    Mackenzie, J.M.3
  • 59
    • 0030774240 scopus 로고    scopus 로고
    • trans-Complementation of yellow fever virus NS1 reveals a role in early RNA replication
    • Lindenbach B.D., and Rice C.M. trans-Complementation of yellow fever virus NS1 reveals a role in early RNA replication. J Virol 71 (1997) 9608-9617
    • (1997) J Virol , vol.71 , pp. 9608-9617
    • Lindenbach, B.D.1    Rice, C.M.2
  • 60
    • 0033034992 scopus 로고    scopus 로고
    • Genetic interaction of flavivirus nonstructural proteins NS1 and NS4A as a determinant of replicase function
    • Lindenbach B.D., and Rice C.M. Genetic interaction of flavivirus nonstructural proteins NS1 and NS4A as a determinant of replicase function. J Virol 73 (1999) 4611-4621
    • (1999) J Virol , vol.73 , pp. 4611-4621
    • Lindenbach, B.D.1    Rice, C.M.2
  • 61
    • 31144442443 scopus 로고    scopus 로고
    • Antibodies against West Nile Virus nonstructural protein NS1 prevent lethal infection through Fc gamma receptor-dependent and -independent mechanisms
    • Chung K.M., Nybakken G.E., Thompson B.S., Engle M.J., Marri A., Fremont D.H., and Diamond M.S. Antibodies against West Nile Virus nonstructural protein NS1 prevent lethal infection through Fc gamma receptor-dependent and -independent mechanisms. J Virol 80 (2006) 1340-1351
    • (2006) J Virol , vol.80 , pp. 1340-1351
    • Chung, K.M.1    Nybakken, G.E.2    Thompson, B.S.3    Engle, M.J.4    Marri, A.5    Fremont, D.H.6    Diamond, M.S.7
  • 62
    • 0032994359 scopus 로고    scopus 로고
    • Dengue virus type 1 nonstructural glycoprotein NS1 is secreted from mammalian cells as a soluble hexamer in a glycosylation-dependent fashion
    • Flamand M., Megret F., Mathieu M., Lepault J., Rey F.A., and Deubel V. Dengue virus type 1 nonstructural glycoprotein NS1 is secreted from mammalian cells as a soluble hexamer in a glycosylation-dependent fashion. J Virol 73 (1999) 6104-6110
    • (1999) J Virol , vol.73 , pp. 6104-6110
    • Flamand, M.1    Megret, F.2    Mathieu, M.3    Lepault, J.4    Rey, F.A.5    Deubel, V.6
  • 63
    • 0024345888 scopus 로고
    • Newly synthesized dengue-2 virus nonstructural protein NS1 is a soluble protein but becomes partially hydrophobic and membrane-associated after dimerization
    • Winkler G., Maxwell S.E., Ruemmler C., and Stollar V. Newly synthesized dengue-2 virus nonstructural protein NS1 is a soluble protein but becomes partially hydrophobic and membrane-associated after dimerization. Virology 171 (1989) 302-305
    • (1989) Virology , vol.171 , pp. 302-305
    • Winkler, G.1    Maxwell, S.E.2    Ruemmler, C.3    Stollar, V.4
  • 64
    • 0024590191 scopus 로고
    • Yellow fever virus proteins NS2A, NS2B, and NS4B: identification and partial N-terminal amino acid sequence analysis
    • Chambers T.J., McCourt D.W., and Rice C.M. Yellow fever virus proteins NS2A, NS2B, and NS4B: identification and partial N-terminal amino acid sequence analysis. Virology 169 (1989) 100-109
    • (1989) Virology , vol.169 , pp. 100-109
    • Chambers, T.J.1    McCourt, D.W.2    Rice, C.M.3
  • 65
    • 0036232747 scopus 로고    scopus 로고
    • Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles
    • Kummerer B.M., and Rice C.M. Mutations in the yellow fever virus nonstructural protein NS2A selectively block production of infectious particles. J Virol 76 (2002) 4773-4784
    • (2002) J Virol , vol.76 , pp. 4773-4784
    • Kummerer, B.M.1    Rice, C.M.2
  • 66
    • 33646167045 scopus 로고    scopus 로고
    • Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein
    • Roosendaal J., Westaway E.G., Khromykh A., and Mackenzie J.M. Regulated cleavages at the West Nile virus NS4A-2K-NS4B junctions play a major role in rearranging cytoplasmic membranes and Golgi trafficking of the NS4A protein. J Virol 80 (2006) 4623-4632
    • (2006) J Virol , vol.80 , pp. 4623-4632
    • Roosendaal, J.1    Westaway, E.G.2    Khromykh, A.3    Mackenzie, J.M.4
  • 67
    • 33747338217 scopus 로고    scopus 로고
    • Dengue virus NS4B interacts with NS3 and dissociates it from single-stranded RNA
    • Umareddy I., Chao A., Sampath A., Gu F., and Vasudevan S.G. Dengue virus NS4B interacts with NS3 and dissociates it from single-stranded RNA. J Gen Virol 87 (2006) 2605-2614
    • (2006) J Gen Virol , vol.87 , pp. 2605-2614
    • Umareddy, I.1    Chao, A.2    Sampath, A.3    Gu, F.4    Vasudevan, S.G.5
  • 70
    • 33646851580 scopus 로고    scopus 로고
    • Subcellular localization and membrane topology of the Dengue virus type 2 Non-structural protein 4B
    • Miller S., Sparacio S., and Bartenschlager R. Subcellular localization and membrane topology of the Dengue virus type 2 Non-structural protein 4B. J Biol Chem 281 (2006) 8854-8863
    • (2006) J Biol Chem , vol.281 , pp. 8854-8863
    • Miller, S.1    Sparacio, S.2    Bartenschlager, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.