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000133638 1001_ $$0P:(DE-HGF)0$$aStern,O.$$b0$$eCorresponding author
000133638 245__ $$aAn N-terminal amphipathic helix in the Dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication.
000133638 260__ $$aBaltimore, Md.$$bSoc.$$c2013
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000133638 520__ $$aDengue virus (DENV) causes dengue fever, a major health concern worldwide. We identified an amphipathic helix (AH) in the N-terminal region of the viral nonstructural protein 4A (NS4A). Disruption of its amphipathic nature using mutagenesis reduced homo-oligomerization and abolished viral replication. These data emphasize the significance of NS4A in the life cycle of the dengue virus and demarcate it as a target for the design of novel antiviral therapy. 
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000133638 7001_ $$0P:(DE-Juel1)140558$$aHung, Yu-Fu$$b1$$ufzj
000133638 7001_ $$0P:(DE-Juel1)142009$$aValdau, Olga$$b2$$ufzj
000133638 7001_ $$0P:(DE-HGF)0$$aYaffe,Y.$$b3
000133638 7001_ $$0P:(DE-HGF)0$$aHarris,E.$$b4
000133638 7001_ $$0P:(DE-Juel1)132003$$aHoffmann, Silke$$b5$$ufzj
000133638 7001_ $$0P:(DE-Juel1)132029$$aWillbold, Dieter$$b6$$ufzj
000133638 7001_ $$0P:(DE-HGF)0$$aSklan,E.$$b7
000133638 773__ $$0PERI:(DE-600)1495529-5$$a10.1128/JVI.01900-12$$n7$$p4080-4085$$tJournal of virology$$v87$$x0022-538X
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