Hemolytic activity of influenza virus hemagglutinin glycoproteins activated in mildly acidic environments.
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Natural history of highly pathogenic avian influenza H5N1Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: effects of acid pretreatmentStructural basis for the divergent evolution of influenza B virus hemagglutininPrevalence of gastrointestinal symptoms in patients with influenza, clinical significance, and pathophysiology of human influenza viruses in faecal samples: what do we know?A host-guest system to study structure-function relationships of membrane fusion peptides.Effectiveness of common household cleaning agents in reducing the viability of human influenza A/H1N1.Dynamic interactions of the UL16 tegument protein with the capsid of herpes simplex virus.Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin.Reconstitution of functional influenza virus envelopes and fusion with membranes and liposomes lacking virus receptorsProteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* coreThe structure of a membrane fusion mutant of the influenza virus haemagglutinin.Intermediates in influenza induced membrane fusion.Kinetics of the low pH-induced conformational changes and fusogenic activity of influenza hemagglutinin.Intermediates and kinetics of membrane fusion.Morphological changes and fusogenic activity of influenza virus hemagglutinin.Stable association of herpes simplex virus with target membranes is triggered by low pH in the presence of the gD receptor, HVEMThe final conformation of the complete ectodomain of the HA2 subunit of influenza hemagglutinin can by itself drive low pH-dependent fusionStudies of the membrane fusion activities of fusion peptide mutants of influenza virus hemagglutinin.High-efficiency incorporation of functional influenza virus glycoproteins into recombinant vesicular stomatitis viruses.Mechanism of entry into the cytosol of poliovirus type 1: requirement for low pH.Initial stages of influenza hemagglutinin-induced cell fusion monitored simultaneously by two fluorescent events: cytoplasmic continuity and lipid mixing.Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.Influenza hemagglutinin is spring-loaded by a metastable native conformation.Avian influenza virus (H5N1); effects of physico-chemical factors on its survival.Fusion of influenza virus membranes with liposomes at pH 7.5.Hemagglutinin 1-specific immunoglobulin G and Fab molecules mediate postattachment neutralization of influenza A virus by inhibition of an early fusion event.Identification of a receptor-binding domain of the spike glycoprotein of human coronavirus HCoV-229E.Requirement for vacuolar proton-ATPase activity during entry of influenza virus into cells.Characterization of Lassa virus cell entry and neutralization with Lassa virus pseudoparticlesUncoating of influenza virus in endosomes.Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/834-mediated hemolysis.Fine structure of influenza A virus observed by electron cryo-microscopy.Enhanced growth of influenza A virus by coinfection with human parainfluenza virus type 2.Membrane action of synthetic N-terminal peptides of influenza virus hemagglutinin and its mutants.Expression of the influenza virus haemagglutinin in insect cells by a baculovirus vectorRequirements for entry of poliovirus RNA into cells at low pH.Long-term shedding of influenza A virus in stool of immunocompromised child.Interference with the endosomal acidification by a monoclonal antibody directed toward the 116 (100)-kD subunit of the vacuolar type proton pump.Thermal denaturation of influenza virus and its relationship to membrane fusion.Fusion of enveloped viruses with cells and liposomes. Activity and inactivation.
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Hemolytic activity of influenza virus hemagglutinin glycoproteins activated in mildly acidic environments.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on June 1983
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Hemolytic activity of influenz ...... in mildly acidic environments.
@en
Hemolytic activity of influenz ...... in mildly acidic environments.
@nl
type
label
Hemolytic activity of influenz ...... in mildly acidic environments.
@en
Hemolytic activity of influenz ...... in mildly acidic environments.
@nl
prefLabel
Hemolytic activity of influenz ...... in mildly acidic environments.
@en
Hemolytic activity of influenz ...... in mildly acidic environments.
@nl
P2093
P2860
P356
P1476
Hemolytic activity of influenz ...... in mildly acidic environments.
@en
P2093
P2860
P304
P356
10.1073/PNAS.80.11.3153
P407
P577
1983-06-01T00:00:00Z