TY  - JOUR
AU  - Stern,O.
AU  - Hung, Yu-Fu
AU  - Valdau, Olga
AU  - Yaffe,Y.
AU  - Harris,E.
AU  - Hoffmann, Silke
AU  - Willbold, Dieter
AU  - Sklan,E.
TI  - An N-terminal amphipathic helix in the Dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication.
JO  - Journal of virology
VL  - 87
IS  - 7
SN  - 0022-538X
CY  - Baltimore, Md.
PB  - Soc.
M1  - FZJ-2013-02053
SP  - 4080-4085
PY  - 2013
AB  - 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. 
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000315957100043
DO  - DOI:10.1128/JVI.01900-12
UR  - https://juser.fz-juelich.de/record/133638
ER  -