ArticleBiophysical journal2002
Functional motions of influenza virus hemagglutinin: a structure-based analytical approach.
Article in Biophysical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 86 citations in OpenAlex.
- Breathing and Tilting: Mesoscale Simulations Illuminate Influenza Glycoprotein Vulnerabilities.ACS central science · 2022Article
- Breathing and tilting: mesoscale simulations illuminate influenza glycoprotein vulnerabilities.bioRxiv : the preprint server for biology · 2022Article
- COVID-19: Myths and Reality.Biochemistry. Biokhimiia · 2021Review
- Normal mode analysis of membrane protein dynamics using the vibrational subsystem analysis.The Journal of chemical physics · 2021Article
- Potent sialic acid inhibitors that target influenza A virus hemagglutinin.Scientific reports · 2021Article
- High-Yield Expression and Purification of Recombinant Influenza Virus Proteins from Stably-Transfected Mammalian Cell Lines.Vaccines · 2020Article
- Morin Hydrate Inhibits Influenza Virus entry into Host Cells and Has Anti-inflammatory Effect in Influenza-infected Mice.Immune network · 2020Article
- Integrated Computational Approaches and Tools forAllosteric Drug Discovery.International journal of molecular sciences · 2020Review
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- Genetic and antigenic divergence in the influenza A(H3N2) virus circulating between 2016 and 2017 in Thailand.PloS one · 2017Article
- Order and disorder control the functional rearrangement of influenza hemagglutinin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Cleavage site and Ectodomain of HA2 sub-unit sequence of three equine influenza virus isolated in Morocco.BMC research notes · 2014Article
- Potential strategies and biosafety protocols used for dual-use research on highly pathogenic influenza viruses.Reviews in medical virology · 2012Review
- Identification of motions in membrane proteins by elastic network models and their experimental validation.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Molecular basis of the structure and function of H1 hemagglutinin of influenza virus.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2012Review
- Article
- Identifying ligand binding conformations of the β2-adrenergic receptor by using its agonists as computational probes.PloS one · 2012Article
- Structural insight into the role of thrombospondin-1 binding to calreticulin in calreticulin-induced focal adhesion disassembly.Biochemistry · 2010Article
- Vibrational subsystem analysis: A method for probing free energies and correlations in the harmonic limit.The Journal of chemical physics · 2008Article
- Interaction of anesthetics with open and closed conformations of a potassium channel studied via molecular dynamics and normal mode analysis.Biophysical journal · 2008Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Influenza virus hemagglutinin (HA), a homotrimeric integral membrane glycoprotein essential for viral infection, is engaged in two biological functions: recognition of target cells' receptor proteins and fusion of viral and endosomal membranes, both requiring substantial conformational flexibility from the part of the glycoprotein. The different modes of collective motions underlying the functional mobility/adaptability of the protein are determined in the present study using an extension of the Gaussian network model (GNM) to treat concerted anisotropic motions. We determine the molecular mechanisms that may underlie HA function, along with the structural regions or residues whose mutations are expected to impede function. Good agreement between theoretically predicted fluctuations of individual residues and corresponding x-ray crystallographic temperature factors is found, which lends support to the GNM elucidation of the conformational dynamics of HA by focusing upon a subset of dominant modes. The lowest frequency mode indicates a global torsion of the HA trimer about its longitudinal axis, accompanied by a substantial mobility at the viral membrane connection. This mode is proposed to constitute the dominant molecular mechanism for the translocation and aggregation of HAs, and for the opening and dilation of the fusion pore. The second and third collective modes indicate a global bending, allowing for a large lateral surface exposure, which is likely to facilitate the close association of the viral and endosomal membranes before pore opening. The analysis of kinetically hot residues, in contrast, reveals a localization of energy centered around the HA2 residue Asp112, which apparently triggers the solvent exposure of the fusion peptide.
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