ArticleBiophysical journal2005
Plasticity of influenza haemagglutinin fusion peptides and their interaction with lipid bilayers.
Article in Biophysical journal, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 75 citations in OpenAlex.
- The Lassa virus fusion domain has structural plasticity and exploits bis(monoacylglycero)phosphate for fusion.Biophysical journal · 2026Article
- The interaction of viral fusion peptides with lipid membranes.Biophysical journal · 2022Article
- 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
- The seafood Musculus senhousei shows anti-influenza A virus activity by targeting virion envelope lipids.Biochemical pharmacology · 2020Article
- Influence of Environmental Conditions on the Fusion of Cationic Liposomes with Living Mammalian Cells.Nanomaterials (Basel, Switzerland) · 2019Article
- Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.Chemical reviews · 2019Review
- All-atom virus simulations.Current opinion in virology · 2018Review
- Influenza Hemifusion Phenotype Depends on Membrane Context: Differences in Cell-Cell and Virus-Cell Fusion.Journal of molecular biology · 2018Article
- Fusing simulation and experiment: The effect of mutations on the structure and activity of the influenza fusion peptide.Scientific reports · 2016Article
- Capturing Spontaneous Membrane Insertion of the Influenza Virus Hemagglutinin Fusion Peptide.The journal of physical chemistry. B · 2015Article
- NMR structures and localization of the potential fusion peptides and the pre-transmembrane region of SARS-CoV: Implications in membrane fusion.Biochimica et biophysica acta · 2015Article
- Assembly of Influenza Hemagglutinin Fusion Peptides in a Phospholipid Bilayer by Coarse-grained Computer Simulations.Frontiers in molecular biosciences · 2015Article
- Article
- 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
- 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
- Lipid tail protrusion in simulations predicts fusogenic activity of influenza fusion peptide mutants and conformational models.PLoS computational biology · 2013Article
- Unusual titration of the membrane-bound artificial hemagglutinin fusion peptide.European biophysics journal : EBJ · 2012Article
- The influenza fusion peptide adopts a flexible flat V conformation in membranes.Biophysical journal · 2012Article
- Helical hairpin structure of influenza hemagglutinin fusion peptide stabilized by charge-dipole interactions between the N-terminal amino group and the second helix.Journal of the American Chemical Society · 2011Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
Abstract
A detailed molecular dynamics study of the haemagglutinin fusion peptide (N-terminal 20 residues of the HA2 subunits) in a model bilayer has yielded useful information about the molecular interactions leading to insertion into the lipids. Simulations were performed on the native sequence, as well as a number of mutant sequences, which are either fusogenic or nonfusogenic. For the native sequence and fusogenic mutants, the N-terminal 11 residues of the fusion peptides are helical and insert with a tilt angle of approximately 30 degrees with respect to the membrane normal, in very good agreement with experimental data. The tilted insertion of the native sequence peptide leads to membrane bilayer thinning and the calculated order parameters show larger disorder of the alkyl chains. These results indicate that the lipid packing is perturbed by the fusion peptide and could be used to explain membrane fusion. For the nonfusogenic sequences investigated, it was found that most of them equilibrate parallel to the interface plane and do not adopt a tilted conformation. The presence of a charged residue at the beginning of the sequence (G1E mutant) resulted in a more difficult case, and the outcomes do not fall straightforwardly into the general picture. Sequence searches have revealed similarities of the fusion peptide of influenza haemagglutinin with peptide sequences such as segments of porin, amyloid alpha eta peptide, and a peptide from the prion sequence. These results confirm that the sequence can adopt different folds in different environments. The plasticity and the conformational dependence on the local environment could be used to better understand the function of fusion peptides.
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.