Journal Article

FZJ-2013-02053

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png An N-terminal amphipathic helix in the Dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication.

Stern,O. (Corresponding author) ; Hung, Y.-F.FZJ* ; Valdau, O.FZJ* ; Yaffe,Y. ; Harris,E. ; Hoffmann, S.FZJ* ; Willbold, D.FZJ* ; Sklan,E.

2013
Soc. Baltimore, Md.

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Please use a persistent id in citations: doi:10.1128/JVI.01900-12

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.

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Contributing Institute(s):

1. Strukturbiochemie (ICS-6)

Research Program(s):

1. 452 - Structural Biology (POF2-452) (POF2-452)
2. 331 - Signalling Pathways and Mechanisms in the Nervous System (POF2-331) (POF2-331)

Appears in the scientific report 2013

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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