Structure of a flavivirus envelope glycoprotein in its low‐pH‐induced membrane fusion conformation

By S. Bressanelli, K. Stiasny, S. L. Allison, E. Stura, S. Duquerroy, J. Lescar, F. Heinz, F. Rey. EMBO Journal, 2004

602 citations recorded by the source corpus.

Subfields: Epidemiology, Infectious Diseases, Public Health, Environmental and Occupational Health

View Paper: https://www.semanticscholar.org/paper/9f606edfada75790378a247d186f12274c8ed255

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In Epidemiology

1. Brett D. Lindenbach Heinz-J
2. Charles M. Rice
3. Joël Janin

In Public Health, Environmental and Occupational Health

1. S. Harrison

Citations in the corpus

• Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common Theme (2008, background): “The crystal structures of pre-fusion and post-fusion forms of the TBEV E protein are shown in Figure 6C (Bressanelli et al., 2004; Rey et al., 1995).”
• 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”
• Protein–protein interaction and quaternary structure (2008, background): “A remarkable exception has been the envelope glycoprotein of a flavivirus, known to exist both as a dimer in the viral particle, and as a trimer in the form that promotes membrane fusion when the virus infects a cell (Bressanelli et al. 2004).”
• Assessing predictions of protein–protein interaction: The CAPRI experiment (2005, neutral): “17 0 0 T10 TBE virus E trimer Bressanelli et al. 2004 20 1 3 T11 Cohesin/dockerin (unbound) Carvalho et al. 2004 19 0 13 T12 Cohesin/dockerin (bound) Carvalho et al. 2004 22 20 10 T13 SAG1/Fab M. Graille and F. Ducancel, in prep.”
• Flaviviridae :T he Viruses and Their Replication (2007, methodology): “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.”