Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins
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Glycosylation changes in the globular head of H3N2 influenza hemagglutinin modulate receptor binding without affecting virus virulenceRecent H3N2 Viruses Have Evolved Specificity for Extended, Branched Human-type Receptors, Conferring Potential for Increased Avidity.The 150-Loop Restricts the Host Specificity of Human H10N8 Influenza Virus.Effects of egg-adaptation on receptor-binding and antigenic properties of recent influenza A (H3N2) vaccine viruses.Structural and Functional Studies of Influenza Virus A/H6 Hemagglutinin.A Miniaturized Glycan Microarray Assay for Assessing Avidity and Specificity of Influenza A Virus Hemagglutinins.H3N2 Mismatch of 2014-15 Northern Hemisphere Influenza Vaccines and Head-to-head Comparison between Human and Ferret Antisera derived Antigenic MapsEmergence of a novel subclade of influenza A(H3N2) virus in London, December 2016 to January 2017.New insights into influenza A specificity: an evolution of paradigms.Charged amino acid variability related to N-glyco -sylation and epitopes in A/H3N2 influenza: Hem -agglutinin and neuraminidase.Diversity of Functionally Permissive Sequences in the Receptor-Binding Site of Influenza Hemagglutinin.Novel multiplex assay platforms to detect influenza A hemagglutinin subtype-specific antibody responses for high-throughput and in-field applications.Assessment of Molecular, Antigenic, and Pathological Features of Canine Influenza A(H3N2) Viruses That Emerged in the United States.Genetic and antigenic divergence in the influenza A(H3N2) virus circulating between 2016 and 2017 in Thailand.Infection and replication of influenza virus at the ocular surface.A complex epistatic network limits the mutational reversibility in the influenza hemagglutinin receptor-binding site.Molecular genetic characteristics of influenza A virus clinically isolated during 2011-2016 influenza seasons in Korea.H3N2 influenza viruses in humans: Viral mechanisms, evolution, and evaluation.Development of a high-throughput assay to detect antibody inhibition of low pH induced conformational changes of influenza virus hemagglutinin.Deep mutational scanning of hemagglutinin helps predict evolutionary fates of human H3N2 influenza variants
P2860
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P2860
Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins
description
2015 nî lūn-bûn
@nan
2015 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2015 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
name
Structure and receptor binding ...... n A(H3N2) virus hemagglutinins
@ast
Structure and receptor binding ...... n A(H3N2) virus hemagglutinins
@en
Structure and receptor binding ...... n A(H3N2) virus hemagglutinins
@nl
type
label
Structure and receptor binding ...... n A(H3N2) virus hemagglutinins
@ast
Structure and receptor binding ...... n A(H3N2) virus hemagglutinins
@en
Structure and receptor binding ...... n A(H3N2) virus hemagglutinins
@nl
prefLabel
Structure and receptor binding ...... n A(H3N2) virus hemagglutinins
@ast
Structure and receptor binding ...... n A(H3N2) virus hemagglutinins
@en
Structure and receptor binding ...... n A(H3N2) virus hemagglutinins
@nl
P2093
P2860
P3181
P1433
P1476
Structure and receptor binding ...... n A(H3N2) virus hemagglutinins
@en
P2093
James Stevens
Jessie C Chang
Julie M Villanueva
Paul J Carney
P2860
P3181
P356
10.1016/J.VIROL.2014.12.024
P407
P577
2015-01-22T00:00:00Z