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@ARTICLE{Hung:203112,
      author       = {Hung, Yu-Fu and Schwarten, Melanie and Schünke, Sven and
                      Thiagarajan-Rosenkranz, Pallavi and Hoffmann, Silke and
                      Sklan, Ella H. and Willbold, Dieter and König, Bernd},
      title        = {{D}engue virus {NS}4{A} cytoplasmic domain binding to
                      liposomes is sensitive to membrane curvature},
      journal      = {Biochimica et biophysica acta / Biomembranes},
      volume       = {1848},
      number       = {5},
      issn         = {0005-2736},
      address      = {Amsterdam},
      publisher    = {Elsevier},
      reportid     = {FZJ-2015-05136},
      pages        = {1119 - 1126},
      year         = {2015},
      abstract     = {Dengue virus (DENV) infection is a growing public health
                      threat with more than one-third of the world's population at
                      risk. Non-structural protein 4A (NS4A), one of the least
                      characterized viral proteins, is a highly hydrophobic
                      transmembrane protein thought to induce the membrane
                      alterations that harbor the viral replication complex. The
                      NS4A N-terminal (amino acids 1–48), has been proposed to
                      contain an amphipathic α-helix (AH). Mutations (L6E; M10E)
                      designed to reduce the amphipathic character of the
                      predicted AH, abolished viral replication and reduced NS4A
                      oligomerization. Nuclear magnetic resonance (NMR)
                      spectroscopy was used to characterize the N-terminal
                      cytoplasmic region (amino acids 1–48) of both wild type
                      and mutant NS4A in the presence of SDS micelles. Binding of
                      the two N-terminal NS4A peptides to liposomes was studied as
                      a function of membrane curvature and lipid composition. The
                      NS4A N-terminal was found to contain two AHs separated by a
                      non-helical linker. The abovementioned mutations did not
                      significantly affect the helical secondary structure of this
                      domain. However, they reduced the affinity of the N-terminal
                      NS4A domain for lipid membranes. Binding of wild type
                      NS4A(1–48) to liposomes is highly dependent on membrane
                      curvature.},
      cin          = {ICS-6},
      ddc          = {570},
      cid          = {I:(DE-Juel1)ICS-6-20110106},
      pnm          = {553 - Physical Basis of Diseases (POF3-553)},
      pid          = {G:(DE-HGF)POF3-553},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000352041100006},
      doi          = {10.1016/j.bbamem.2015.01.015},
      url          = {https://juser.fz-juelich.de/record/203112},
}