ArticleJournal of biomolecular NMR2013
Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.
Article in Journal of biomolecular NMR, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Two modes of fusogenic action for influenza virus fusion peptide.PLoS computational biology · 2023Article
- Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies.FEBS open bio · 2021Review
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- Influenza hemagglutinin drives viral entry via two sequential intramembrane mechanisms.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Article
- Structure and Dynamics of Membrane Proteins from Solid-State NMR.Annual review of biophysics · 2018Review
- Fusing simulation and experiment: The effect of mutations on the structure and activity of the influenza fusion peptide.Scientific reports · 2016Article
- Full-length trimeric influenza virus hemagglutinin II membrane fusion protein and shorter constructs lacking the fusion peptide or transmembrane domain: Hyperthermostability of the full-length protein and the soluble ectodomain and fusion peptide make significant contributions to fusion of membrane vesicles.Protein expression and purification · 2016Article
- Closed and Semiclosed Interhelical Structures in Membrane vs Closed and Open Structures in Detergent for the Influenza Virus Hemagglutinin Fusion Peptide and Correlation of Hydrophobic Surface Area with Fusion Catalysis.Journal of the American Chemical Society · 2015Article
- REDOR solid-state NMR as a probe of the membrane locations of membrane-associated peptides and proteins.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
- The three lives of viral fusion peptides.Chemistry and physics of lipids · 2014Review
- REDOR NMR for drug discovery.Bioorganic & medicinal chemistry letters · 2013Article
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Authors and funding
3 authors.
Funding
Abstract
The influenza virus fusion peptide is the N-terminal ~20 residues of the HA2 subunit of the hemagglutinin protein and this peptide plays a key role in the fusion of the viral and endosomal membranes during initial infection of a cell. The fusion peptide adopts N-helix/turn/C-helix structure in both detergent and membranes with reports of both open and closed interhelical topologies. In the present study, backbone (13)CO-(15)N REDOR solid-state NMR was applied to the membrane-associated fusion peptide to detect the distribution of interhelical distances. The data clearly showed a large fraction of closed and semi-closed topologies and were best-fitted to a mixture of two structures that do not exchange. One of the earlier open structural models may have incorrect G13 dihedral angles derived from TALOS analysis of experimentally correct (13)C shifts.
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