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@ARTICLE{Stern:133638,
      author       = {Stern,O. and Hung, Yu-Fu and Valdau, Olga and Yaffe,Y. and
                      Harris,E. and Hoffmann, Silke and Willbold, Dieter and
                      Sklan,E.},
      title        = {{A}n {N}-terminal amphipathic helix in the {D}engue virus
                      nonstructural protein 4{A} mediates oligomerization and is
                      essential for replication.},
      journal      = {Journal of virology},
      volume       = {87},
      number       = {7},
      issn         = {0022-538X},
      address      = {Baltimore, Md.},
      publisher    = {Soc.},
      reportid     = {FZJ-2013-02053},
      pages        = {4080-4085},
      year         = {2013},
      abstract     = {Dengue virus (DENV) causes dengue fever, a major health
                      concern worldwide. We identified an amphipathic helix (AH)
                      in the N-terminal region of the viral nonstructural protein
                      4A (NS4A). Disruption of its amphipathic nature using
                      mutagenesis reduced homo-oligomerization and abolished viral
                      replication. These data emphasize the significance of NS4A
                      in the life cycle of the dengue virus and demarcate it as a
                      target for the design of novel antiviral therapy.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {452 - Structural Biology (POF2-452) / 331 - Signalling
                      Pathways and Mechanisms in the Nervous System (POF2-331)},
      pid          = {G:(DE-HGF)POF2-452 / G:(DE-HGF)POF2-331},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000315957100043},
      doi          = {10.1128/JVI.01900-12},
      url          = {https://juser.fz-juelich.de/record/133638},
}