ReviewBiopolymers2013
The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamics.
Review in Biopolymers, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed.
- Two modes of fusogenic action for influenza virus fusion peptide.PLoS computational biology · 2023Article
- Membrane-Bound Configuration and Lipid Perturbing Effects of Hemagglutinin Subunit 2 N-Terminus Investigated by Computer Simulations.Frontiers in molecular biosciences · 2022Article
- Molecular mechanisms of the influenza fusion peptide: insights from experimental and simulation studies.FEBS open bio · 2021Review
- Transient Excursions to Membrane Core as Determinants of Influenza Virus Fusion Peptide Activity.International journal of molecular sciences · 2021Article
- Effect of pH on the influenza fusion peptide properties unveiled by constant-pH molecular dynamics simulations combined with experiment.Scientific reports · 2020Article
- Charged N-terminus of Influenza Fusion Peptide Facilitates Membrane Fusion.International journal of molecular sciences · 2018Article
- Atomic-level description of protein-lipid interactions using an accelerated membrane model.Biochimica et biophysica acta · 2016Review
- Fusing simulation and experiment: The effect of mutations on the structure and activity of the influenza fusion peptide.Scientific reports · 2016Article
- Kinetics of peptide folding in lipid membranes.Biopolymers · 2015Review
- Capturing Spontaneous Membrane Insertion of the Influenza Virus Hemagglutinin Fusion Peptide.The journal of physical chemistry. B · 2015Article
- 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
- The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.The Journal of biological chemistry · 2015Article
- Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations.Frontiers in molecular biosciences · 2015Article
- Structure and dynamics of a fusion peptide helical hairpin on the membrane surface: comparison of molecular simulations and NMR.The journal of physical chemistry. B · 2014Article
- Conformation and lipid interaction of the fusion peptide of the paramyxovirus PIV5 in anionic and negative-curvature membranes from solid-state NMR.Journal of the American Chemical Society · 2014Article
- Detection of closed influenza virus hemagglutinin fusion peptide structures in membranes by backbone (13)CO- (15)N rotational-echo double-resonance solid-state NMR.Journal of biomolecular NMR · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
A peptide comprising no fewer than the first 20 residues of the influenza hemagglutinin HA2 subunit suffices to induce lipid mixing between the membranes of different unilamellar vesicles. This 20-residue peptide was previously reported to adopt an open "boomerang" structure that differs significantly from the closed helical-hairpin structure of a fusion peptide consisting of the first 23 residues of the HA2 sequence. This study investigates the structural and dynamic features of fusion peptides of different length and subtype. Lacking key interactions that stabilize the closed, helical-hairpin structure, the 20-residue peptide is in a dynamic equilibrium between closed and open states, adopting a ca. 11% population of the former when solubilized by DPC micelles. Peptides shorter than 20 residues would have even fewer interactions to stabilize a helical hairpin fold, resulting in a vanishing hairpin population. Considering the conserved nature of hairpin-stabilizing interactions across all serotypes, and the minimum of 20 residues needed for fusion, we postulate that the closed state plays an essential role in the fusion process. However, opening of this hairpin structure may be essential to the formation of a membrane pore at the final stage of the fusion process.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.