Antigen distortion allows influenza virus to escape neutralization
about
A highly conserved neutralizing epitope on group 2 influenza A virusesA structure-based benchmark for protein-protein binding affinityAntibody recognition of a highly conserved influenza virus epitopeAntibody promiscuity: Understanding the paradigm shift in antigen recognitionStructural characterization of viral epitopes recognized by broadly cross-reactive antibodiesStructural consequences of target epitope-directed functional alteration of an antibody. The case of anti-hen lysozyme antibody, HyHEL-10Structural consequences of mutations in interfacial Tyr residues of a protein antigen-antibody complex. The case of HyHEL-10-HELContribution of Asparagine Residues to the Stabilization of a Proteinaceous Antigen-Antibody Complex, HyHEL-10-Hen Egg White LysozymeBroadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutininCross-neutralization of influenza A viruses mediated by a single antibody loopHeterosubtypic antibody recognition of the influenza virus hemagglutinin receptor binding site enhanced by avidityCrystal Structure of Two Anti-Porphyrin Antibodies with Peroxidase ActivityA Unique and Conserved Neutralization Epitope in H5N1 Influenza Viruses Identified by an Antibody against the A/Goose/Guangdong/1/96 HemagglutininThe impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamicsAnti-Hemagglutinin Antibody Derived Lead Peptides for Inhibitors of Influenza Virus BindingEvolution of H3N2 influenza virus in a guinea pig modelPassive immunoprophylaxis and therapy with humanized monoclonal antibody specific for influenza A H5 hemagglutinin in miceGenetic diversity of hemagglutinin gene of A(H1N1)pdm09 influenza strains isolated in Taiwan and its potential impact on HA-neutralizing epitope interactionIn silico structural homology modelling and docking for assessment of pandemic potential of a novel H7N9 influenza virus and its ability to be neutralized by existing anti-hemagglutinin antibodies.Pseudotype-based neutralization assays for influenza: a systematic analysis.The Analysis of B-Cell Epitopes of Influenza Virus Hemagglutinin.In silico characterization of the functional and structural modules of the hemagglutinin protein from the swine-origin influenza virus A (H1N1)-2009.Structural basis of influenza virus neutralization.Free-energy simulations reveal that both hydrophobic and polar interactions are important for influenza hemagglutinin antibody binding.Immunodominance of antigenic site B over site A of hemagglutinin of recent H3N2 influenza viruses.Antigenic drift of the pandemic 2009 A(H1N1) influenza virus in A ferret model.Using molecular principal axes for structural comparison: determining the tertiary changes of a FAB antibody domain induced by antigenic binding.Fatal cases of influenza A(H3N2) in children: insights from whole genome sequence analysis.The principle of delivery of T cell epitopes to antigen-presenting cells applied to peptides from influenza virus, ovalbumin, and hen egg lysozyme: implications for peptide vaccination.Transient humoral protection against H5N1 challenge after seasonal influenza vaccination of humansA computational analysis of the antigenic properties of haemagglutinin in influenza A H3N2.Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.Glycoprotein N of human cytomegalovirus protects the virus from neutralizing antibodies.Impact of valency of a glycoprotein B-specific monoclonal antibody on neutralization of herpes simplex virusAnalysis of antigenically important residues in human influenza A virus in terms of B-cell epitopes.How structure defines affinity in protein-protein interactions.Evaluation of influenza virus A/H3N2 and B vaccines on the basis of cross-reactivity of postvaccination human serum antibodies against influenza viruses A/H3N2 and B isolated in MDCK cells and embryonated hen eggs.A virus-like particle that elicits cross-reactive antibodies to the conserved stem of influenza virus hemagglutinin.Variation and infectivity neutralization in influenza.Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.
P2860
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P2860
Antigen distortion allows influenza virus to escape neutralization
description
1998 nî lūn-bûn
@nan
1998 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
Antigen distortion allows influenza virus to escape neutralization
@ast
Antigen distortion allows influenza virus to escape neutralization
@en
Antigen distortion allows influenza virus to escape neutralization
@nl
type
label
Antigen distortion allows influenza virus to escape neutralization
@ast
Antigen distortion allows influenza virus to escape neutralization
@en
Antigen distortion allows influenza virus to escape neutralization
@nl
prefLabel
Antigen distortion allows influenza virus to escape neutralization
@ast
Antigen distortion allows influenza virus to escape neutralization
@en
Antigen distortion allows influenza virus to escape neutralization
@nl
P2093
P2860
P3181
P356
P1476
Antigen distortion allows influenza virus to escape neutralization
@en
P2093
P2860
P2888
P304
P3181
P356
10.1038/NSB0298-119
P577
1998-02-01T00:00:00Z
P6179
1053315117