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| Hauptseite > Publikationsdatenbank > Dengue virus NS4A cytoplasmic domain binding to liposomes is sensitive to membrane curvature > print |
| Hauptseite > Publikationsdatenbank > Dengue virus NS4A cytoplasmic domain binding to liposomes is sensitive to membrane curvature > print |
| 001 | 203112 | ||
| 005 | 20210129220302.0 | ||
| 024 | 7 | _ | |a 10.1016/j.bbamem.2015.01.015 |2 doi |
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| 100 | 1 | _ | |a Hung, Yu-Fu |0 P:(DE-Juel1)140558 |b 0 |
| 245 | _ | _ | |a Dengue virus NS4A cytoplasmic domain binding to liposomes is sensitive to membrane curvature |
| 260 | _ | _ | |a Amsterdam |c 2015 |b Elsevier |
| 336 | 7 | _ | |a Journal Article |b journal |m journal |0 PUB:(DE-HGF)16 |s 1449218571_28392 |2 PUB:(DE-HGF) |
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| 520 | _ | _ | |a 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. |
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| 773 | _ | _ | |a 10.1016/j.bbamem.2015.01.015 |g Vol. 1848, no. 5, p. 1119 - 1126 |0 PERI:(DE-600)2209384-9 |n 5 |p 1119 - 1126 |t Biochimica et biophysica acta / Biomembranes |v 1848 |y 2015 |x 0005-2736 |
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