Structure of the dengue virus envelope protein after membrane fusion
By Yorgo Modis, Steven A. Ogata, D. Clements, S. Harrison. Nature, 2004
1,162 citations recorded by the source corpus.
Subfields: Endocrinology, Public Health, Environmental and Occupational Health, Virology
View Paper: https://www.semanticscholar.org/paper/de7a2488d1f6f170ecca66e7cd7631517729fa80
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Citations in the corpus
- Viral membrane fusion (2015, background): “Schematic diagram of stages of dengue virus fusion (modified from (Modis et al., 2004)).”
- Replication of hepatitis C virus (2007, background): “The structural basis for low pH-induced membrane fusion has been elucidated for related flaviviruses and alphaviruses, including dengue virus and Semliki Forest viru”
- Dengue and severe dengue (2025, positive): “Acidification of the endosome or phagosome leads to trimerization of the E protein that then initiates fusion with endosomal/phagosomal membranes (39).”
- Flaviviridae :T he Viruses and Their Replication (2007, background): “Although the structure of the fusogenic intermediate has not been yet been discerned, the postfusion form of the trimeric E ectodomains interact in a parallel fashion, with their fusion peptides fully extended back toward the fused membrane (73,495) (Fig.”
- A structural perspective of the flavivirus life cycle (2005, background): “X-ray crystallographic structures of the E proteins at low pH (representing the post-fusion structure) showed a trimeric arrangement, with the long dimensions of the E proteins positioned approximately parallel to each other and with their fusion peptides exposed at the tip of the trime”
- Structure of a phleboviral envelope glycoprotein reveals a consolidated model of membrane fusion (2016, background): “An essential feature of the class-II fusion glycoprotein architecture is the hydrophobic fusion loop located at the apex of domain II, which is inserted into the host membrane and draws the viral and host membranes together upon fusogenic rearrangements of the molecule (21).”
- Structure of a flavivirus envelope glycoprotein in its low‐pH‐induced membrane fusion conformation (2004, background): “…EMBO Journal VOL 23 | NO 4 | 2004 &2004 European Molecular Biology Organization736 the dengue virus sE protein in its low-pH-induced conformation (Modis et al, 2004) suggest that the interactions between the stem region and dII, required to complete the fusion process, would be potential targets…”
- Protein-Protein and Protein-Ligand Docking (2013, methodology): “As a polycationic polymer, it has a high affinity to associate macromolecules such as insulin, pDNA, siRNA, heparin, among others, with antigenic molecules, protecting them in turn from hydrolytic and enzymatic degradation [37].”