Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/834-mediated hemolysis.
about
A conformational change in Sindbis virus glycoproteins E1 and E2 is detected at the plasma membrane as a consequence of early virus-cell interaction.Conformational changes and fusion activity of influenza virus hemagglutinin of the H2 and H3 subtypes: effects of acid pretreatmentUukuniemi virus maturation: immunofluorescence microscopy with monoclonal glycoprotein-specific antibodiesBiogenesis of influenza a virus hemagglutinin cross-protective stem epitopesThe influenza hemagglutinin precursor as an acid-sensitive probe of the biosynthetic pathway.Single event recording shows that docking onto receptor alters the kinetics of membrane fusion mediated by influenza hemagglutinin.Investigation of pathways for the low-pH conformational transition in influenza hemagglutinin.A mechanistic study on the destabilization of whole inactivated influenza virus vaccine in gastric environment.Activation of fusion by the SER virus F protein: a low-pH-dependent paramyxovirus entry process.Immunogenicity of low-pH treated whole viral influenza vaccine.Intracellular neutralization of viral infection in polarized epithelial cells by neonatal Fc receptor (FcRn)-mediated IgG transport.Molecular mechanism underlying the action of a novel fusion inhibitor of influenza A virusGlycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH.Assembly of influenza hemagglutinin trimers and its role in intracellular transportAnti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin.Inactivated influenza virus, when presented on dendritic cells, elicits human CD8+ cytolytic T cell responses.The role of N-acetylneuraminic (sialic) acid in the pH dependence of influenza virion fusion with planar phospholipid membranesMutations in or near the fusion peptide of the influenza virus hemagglutinin affect an antigenic site in the globular regionIntermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformationMonoclonal antibodies to the peplomer glycoprotein of coronavirus mouse hepatitis virus identify two subunits and detect a conformational change in the subunit released under mild alkaline conditions.Influenza hemagglutinin is spring-loaded by a metastable native conformation.Monoclonal antibodies detect different forms of influenza virus hemagglutinin during viral penetration and biosynthesis.Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.Invariant chain targets HLA class II molecules to acidic endosomes containing internalized influenza virus.Hemagglutinin 1-specific immunoglobulin G and Fab molecules mediate postattachment neutralization of influenza A virus by inhibition of an early fusion event.Interference with the endosomal acidification by a monoclonal antibody directed toward the 116 (100)-kD subunit of the vacuolar type proton pump.Functional reconstitution of influenza virus envelopes.Influenza Hemagglutinin Protein Stability, Activation, and Pandemic Risk.
P2860
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P2860
Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/834-mediated hemolysis.
description
1983 nî lūn-bûn
@nan
1983年の論文
@ja
1983年論文
@yue
1983年論文
@zh-hant
1983年論文
@zh-hk
1983年論文
@zh-mo
1983年論文
@zh-tw
1983年论文
@wuu
1983年论文
@zh
1983年论文
@zh-cn
name
Monoclonal anti-hemagglutinin ...... s A/PR/834-mediated hemolysis.
@en
type
label
Monoclonal anti-hemagglutinin ...... s A/PR/834-mediated hemolysis.
@en
prefLabel
Monoclonal anti-hemagglutinin ...... s A/PR/834-mediated hemolysis.
@en
P2093
P2860
P1433
P1476
Monoclonal anti-hemagglutinin ...... s A/PR/834-mediated hemolysis.
@en
P2093
P2860
P304
P407
P577
1983-10-01T00:00:00Z