Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.
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Structure-based analysis of the herpes simplex virus glycoprotein D binding site present on herpesvirus entry mediator HveA (HVEM).An induced pocket for the binding of potent fusion inhibitor CL-385319 with H5N1 influenza virus hemagglutininThe complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interfacepH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMRIntermonomer Interactions in Hemagglutinin Subunits HA1 and HA2 Affecting Hemagglutinin Stability and Influenza Virus InfectivityMembrane Fusion and Infection of the Influenza Hemagglutinin.Molecular basis of the structure and function of H1 hemagglutinin of influenza virus.Plasma membrane localization of Solanum tuberosum remorin from group 1, homolog 3 is mediated by conformational changes in a novel C-terminal anchor and required for the restriction of potato virus X movement].Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusionAntigenic and immunogenic properties of recombinant hemagglutinin proteins from H1N1 A/Brisbane/59/07 and B/Florida/04/06 when produced in various protein expression systems.Atypical fusion peptide of Nelson Bay virus fusion-associated small transmembrane proteinChimeric influenza virus hemagglutinin proteins containing large domains of the Bacillus anthracis protective antigen: protein characterization, incorporation into infectious influenza viruses, and antigenicity.Transmembrane glycine zippers: physiological and pathological roles in membrane proteins.Bilayer conformation of fusion peptide of influenza virus hemagglutinin: a molecular dynamics simulation study.Orientation and interaction of oblique cylindrical inclusions embedded in a lipid monolayer: a theoretical model for viral fusion peptides.Plasticity of influenza haemagglutinin fusion peptides and their interaction with lipid bilayersMurine leukemia virus R Peptide inhibits influenza virus hemagglutinin-induced membrane fusion.Activation of fusion by the SER virus F protein: a low-pH-dependent paramyxovirus entry process.Analysis of the genetic diversity of influenza A viruses using next-generation DNA sequencing.Fusogenic variants of a noncytopathic paramyxovirus.Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion.Virus membrane fusion.Amino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein.Conserved glycine residues in the fusion peptide of the paramyxovirus fusion protein regulate activation of the native state.Length requirements for membrane fusion of influenza virus hemagglutinin peptide linkers to transmembrane or fusion peptide domains.The membrane-proximal region of vesicular stomatitis virus glycoprotein G ectodomain is critical for fusion and virus infectivity.A new approach to an influenza live vaccine: modification of the cleavage site of hemagglutinin.Functional analysis of the putative fusion domain of the baculovirus envelope fusion protein F.Influenza hemagglutinin (HA) stem region mutations that stabilize or destabilize the structure of multiple HA subtypesInfluenza M2 envelope protein augments avian influenza hemagglutinin pseudotyping of lentiviral vectors.The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.Exploring the early stages of the pH-induced conformational change of influenza hemagglutinin.NMR structures of fusion peptide from influenza hemagglutinin H3 subtype and its mutants.Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif.Influenza Hemifusion Phenotype Depends on Membrane Context: Differences in Cell-Cell and Virus-Cell Fusion.Rotation-Activated and Cooperative Zipping Characterize Class I Viral Fusion Protein Dynamics.
P2860
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P2860
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.
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2001 nî lūn-bûn
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2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics
@nl
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.
@ast
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.
@en
type
label
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics
@nl
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.
@ast
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.
@en
prefLabel
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics
@nl
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.
@ast
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.
@en
P2093
P2860
P356
P1433
P1476
Studies on influenza haemagglutinin fusion peptide mutants generated by reverse genetics.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/20.16.4432
P407
P577
2001-08-01T00:00:00Z