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| Hauptseite > Publikationsdatenbank > An N-terminal amphipathic helix in the Dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication. > print |
| Hauptseite > Publikationsdatenbank > An N-terminal amphipathic helix in the Dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication. > print |
| 001 | 133638 | ||
| 005 | 20210129211514.0 | ||
| 024 | 7 | _ | |a 10.1128/JVI.01900-12 |2 doi |
| 024 | 7 | _ | |2 WOS |a WOS:000315957100043 |
| 037 | _ | _ | |a FZJ-2013-02053 |
| 082 | _ | _ | |a 570 |
| 100 | 1 | _ | |a Stern,O. |0 P:(DE-HGF)0 |b 0 |e Corresponding author |
| 245 | _ | _ | |a An N-terminal amphipathic helix in the Dengue virus nonstructural protein 4A mediates oligomerization and is essential for replication. |
| 260 | _ | _ | |a Baltimore, Md. |c 2013 |b Soc. |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1394094353_28514 |2 PUB:(DE-HGF) |
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| 336 | 7 | _ | |a article |2 DRIVER |
| 500 | _ | _ | |3 POF3_Assignment on 2016-02-29 |
| 520 | _ | _ | |a 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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| 773 | _ | _ | |a 10.1128/JVI.01900-12 |p 4080-4085 |n 7 |0 PERI:(DE-600)1495529-5 |t Journal of virology |v 87 |x 0022-538X |
| 856 | 4 | _ | |u https://juser.fz-juelich.de/record/133638/files/FZJ-2013-02053.pdf |z Published final document. |y Restricted |
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