ArticleBiophysical journal2011
Two conserved residues are important for inducing highly ordered membrane domains by the transmembrane domain of influenza hemagglutinin.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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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.
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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.
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Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- Sulfur-containing class of broad-spectrum antivirals improves influenza virus vaccine development.Nature communications · 2026Article
- Molecular Mechanisms behind Conformational Transitions of the Influenza Virus Hemagglutinin Membrane Anchor.The journal of physical chemistry. B · 2023Article
- Negatively charged residues in the membrane ordering activity of SARS-CoV-1 and -2 fusion peptides.Biophysical journal · 2022Article
- Critical Negatively Charged Residues Are Important for the Activity of SARS-CoV-1 and SARS-CoV-2 Fusion Peptides.bioRxiv : the preprint server for biology · 2021Article
- Article
- SARS-CoV-2 Fusion Peptide has a Greater Membrane Perturbating Effect than SARS-CoV with Highly Specific Dependence on CaJournal of molecular biology · 2021Article
- Influenza A H1 and H3 Transmembrane Domains Interact Differently with Each Other and with Surrounding Membrane Lipids.Viruses · 2020Article
- Lipidomics Issues on Human Positive ssRNA Virus Infection: An Update.Metabolites · 2020Review
- Viral Membrane Fusion and the Transmembrane Domain.Viruses · 2020Review
- CaJournal of virology · 2020Article
- Physiological and molecular triggers for SARS-CoV membrane fusion and entry into host cells.Virology · 2018Review
- The SARS-CoV Fusion Peptide Forms an Extended Bipartite Fusion Platform that Perturbs Membrane Order in a Calcium-Dependent Manner.Journal of molecular biology · 2017Article
- The Interaction between Influenza HA Fusion Peptide and Transmembrane Domain Affects Membrane Structure.Biophysical journal · 2015Article
- HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion.Biophysical journal · 2014Article
- Formation of raft-like assemblies within clusters of influenza hemagglutinin observed by MD simulations.PLoS computational biology · 2013Article
- Diversion of phagosome trafficking by pathogenic Rhodococcus equi depends on mycolic acid chain length.Cellular microbiology · 2013Article
- Dynamics and ordering of lipid spin-labels along the coexistence curve of two membrane phases: an ESR study.Chemistry and physics of lipids · 2012Article
- Association of influenza virus proteins with membrane rafts.Advances in virology · 2011Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The interaction with lipids of a synthetic peptide corresponding to the transmembrane domain of influenza hemagglutinin was investigated by means of electron spin resonance. A detailed analysis of the electron spin resonance spectra from spin-labeled phospholipids revealed that the major effect of the peptide on the dynamic membrane structure is to induce highly ordered membrane domains that are associated with electrostatic interactions between the peptide and negatively charged lipids. Two highly conserved residues in the peptide were identified as being important for the membrane ordering effect. Aggregation of large unilamellar vesicles induced by the peptide was also found to be correlated with the membrane ordering effect of the peptide, indicating that an increase in membrane ordering, i.e., membrane dehydration, is important for vesicle aggregation. The possibility that hydrophobic interaction between the highly ordered membrane domains plays a role in vesicle aggregation and viral fusion is discussed.
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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.