Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity - Wikidata - wikimedia - TriplyDB

Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

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Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion Transmission of influenza A viruses Connecting the study of wild influenza with the potential for pandemic disease Structural Insights into the Membrane Fusion Mechanism Mediated by Influenza Virus Hemagglutinin Mutations in haemagglutinin that affect receptor binding and pH stability increase replication of a PR8 influenza virus with H5 HA in the upper respiratory tract of ferrets and may contribute to transmissibility Molecular requirements for a pandemic influenza virus: An acid-stable hemagglutinin protein Mammalian adaptation of influenza A(H7N9) virus is limited by a narrow genetic bottleneck.Viral factors in influenza pandemic risk assessment.Analysis of adaptation mutants in the hemagglutinin of the influenza A(H1N1)pdm09 virus.A single amino acid in the stalk region of the H1N1pdm influenza virus HA protein affects viral fusion, stability and infectivity.The matrix gene segment destabilizes the acid and thermal stability of the hemagglutinin of pandemic live attenuated influenza virus vaccines One-way trip: influenza virus' adaptation to gallinaceous poultry may limit its pandemic potential.Characterization of H5N1 influenza virus variants with hemagglutinin mutations isolated from patients The ecology and adaptive evolution of influenza A interspecies transmission H1N1 influenza viruses varying widely in hemagglutinin stability transmit efficiently from swine to swine and to ferrets.Immune Escape Variants of H9N2 Influenza Viruses Containing Deletions at the Hemagglutinin Receptor Binding Site Retain Fitness In Vivo and Display Enhanced Zoonotic Characteristics Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: implications for host range and adaptation Increased acid stability of the hemagglutinin protein enhances H5N1 influenza virus growth in the upper respiratory tract but is insufficient for transmission in ferrets.Molecular mechanism of the airborne transmissibility of H9N2 avian influenza A viruses in chickens.The evolutionary pattern of glycosylation sites in influenza virus (H5N1) hemagglutinin and neuraminidase.Comparative structural analysis of haemagglutinin proteins from type A influenza viruses: conserved and variable features.Variations in pH sensitivity, acid stability, and fusogenicity of three influenza virus H3 subtypes.Structural differences between the avian and human H7N9 hemagglutinin proteins are attributable to modifications in salt bridge formation: a computational study with implications in viral evolution.Avian Influenza Virus Infection of Immortalized Human Respiratory Epithelial Cells Depends upon a Delicate Balance between Hemagglutinin Acid Stability and Endosomal pH.Identification of Stabilizing Mutations in an H5 Hemagglutinin Influenza Virus Protein.Incoming influenza A virus evades early host recognition, while influenza B virus induces interferon expression directly upon entry.The hemagglutinin protein of highly pathogenic H5N1 influenza viruses overcomes an early block in the replication cycle to promote productive replication in macrophages.The pH of activation of the hemagglutinin protein regulates H5N1 influenza virus replication and pathogenesis in mice Acquisition of a novel eleven amino acid insertion directly N-terminal to a tetrabasic cleavage site confers intracellular cleavage of an H7N7 influenza virus hemagglutinin.Novel Highly Pathogenic Avian A(H5N2) and A(H5N8) Influenza Viruses of Clade 2.3.4.4 from North America Have Limited Capacity for Replication and Transmission in Mammals.Characterizing a histidine switch controlling pH-dependent conformational changes of the influenza virus hemagglutinin The Hemagglutinin-Esterase Fusion Glycoprotein Is a Primary Determinant of the Exceptional Thermal and Acid Stability of Influenza D Virus.Mutations Driving Airborne Transmission of A/H5N1 Virus in Mammals Cause Substantial Attenuation in Chickens only when combined.Is the optimal pH for membrane fusion in host cells by avian influenza viruses related to host range and pathogenicity?A novel eight amino acid insertion contributes to the hemagglutinin cleavability and the virulence of a highly pathogenic avian influenza A (H7N3) virus in mice.Modulation of the pH Stability of Influenza Virus Hemagglutinin: A Host Cell Adaptation Strategy.Effects of hemagglutinin amino acid substitutions in H9 influenza A virus escape mutants.Structural insights on the potential significance of the twin Asn-residue found at the base of the hemagglutinin 2 stalk in all influenza A H1N1 strains: a computational study with clinical implications Influenza hemagglutinin (HA) stem region mutations that stabilize or destabilize the structure of multiple HA subtypes Dynamic changes during acid-induced activation of influenza hemagglutinin.

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Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

http://www.wikidata.org/entity/Q27676000

description

2011 nî lūn-bûn

@nan

2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2011 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2011年の論文

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2011年論文

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2011年論文

@zh-hant

2011年論文

@zh-hk

2011年論文

@zh-mo

2011年論文

@zh-tw

2011年论文

@wuu

name

Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

@ast

Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

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Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

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type

label

Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

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Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

@en

Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

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Acid stability of the hemagglutinin protein regulates H5N1 influenza virus pathogenicity

@en

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Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

@ast

Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

@en

Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

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JOURNAL.PPAT.1002398

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Acid Stability of the Hemagglutinin Protein Regulates H5N1 Influenza Virus Pathogenicity

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Charles J Russell

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Muralidhar Reddivari

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Richard J Heath

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Stephen W White

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P2860

The influenza virus enigma

H5N1 outbreaks and enzootic influenza

MolProbity: all-atom structure validation for macromolecular crystallography

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Processing of X-ray diffraction data collected in oscillation mode

Structural Basis of Preexisting Immunity to the 2009 H1N1 Pandemic Influenza Virus

Structure and Receptor binding properties of a pandemic H1N1 virus hemagglutinin

The Receptor-Binding Domain of Influenza Virus Hemagglutinin Produced in Escherichia coli Folds into Its Native, Immunogenic Structure

Structural Characterization of an Early Fusion Intermediate of Influenza Virus Hemagglutinin

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10.1371/JOURNAL.PPAT.1002398

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Rebecca M DuBois

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3228800

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