Conformational intermediates and fusion activity of influenza virus hemagglutinin.
about
Anti-HIV-1 activity of cellulose acetate phthalate: synergy with soluble CD4 and induction of "dead-end" gp41 six-helix bundles.Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane FusionRole of Endocytosis and Low pH in Murine Hepatitis Virus Strain A59 Cell EntryStructural Characterization of an Early Fusion Intermediate of Influenza Virus HemagglutininSynchronized activation and refolding of influenza hemagglutinin in multimeric fusion machinesReceptor-induced conformational changes in the SU subunit of the avian sarcoma/leukosis virus A envelope protein: implications for fusion activation.Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin.Architecture of a nascent viral fusion pore.Structural changes in Influenza virus at low pH characterized by cryo-electron tomographyStepwise priming by acidic pH and a high K+ concentration is required for efficient uncoating of influenza A virus cores after penetration.At low pH, influenza virus matrix protein M1 undergoes a conformational change prior to dissociating from the membrane.Reversible merger of membranes at the early stage of influenza hemagglutinin-mediated fusionHeterogeneity of early intermediates in cell-liposome fusion mediated by influenza hemagglutinin.Two distinct low-pH steps promote entry of vaccinia virus.Viral RNA Degradation and Diffusion Act as a Bottleneck for the Influenza A Virus Infection Efficiency.Analysis of residues near the fusion peptide in the influenza hemagglutinin structure for roles in triggering membrane fusion.Hydrophobic inactivation of influenza viruses confers preservation of viral structure with enhanced immunogenicityAmino acid residues in the fusion peptide pocket regulate the pH of activation of the H5N1 influenza virus hemagglutinin protein.pH-Controlled two-step uncoating of influenza virus.Hemagglutinin 1-specific immunoglobulin G and Fab molecules mediate postattachment neutralization of influenza A virus by inhibition of an early fusion event.Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37 degrees C either by soluble murine CEACAM1 receptors or by pH 8.Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin-mediated membrane fusion.Membrane fusion mediated by coiled coils: a hypothesis.Stochastic simulation of hemagglutinin-mediated fusion pore formation.Protonation and stability of the globular domain of influenza virus hemagglutinin.Measuring pKa of activation and pKi of inactivation for influenza hemagglutinin from kinetics of membrane fusion of virions and of HA expressing cells.Infectivity phenotypes of H3N2 influenza A viruses in primary swine respiratory epithelial cells are controlled by sialic acid binding.
P2860
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P2860
Conformational intermediates and fusion activity of influenza virus hemagglutinin.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Conformational intermediates and fusion activity of influenza virus hemagglutinin.
@ast
Conformational intermediates and fusion activity of influenza virus hemagglutinin.
@en
type
label
Conformational intermediates and fusion activity of influenza virus hemagglutinin.
@ast
Conformational intermediates and fusion activity of influenza virus hemagglutinin.
@en
prefLabel
Conformational intermediates and fusion activity of influenza virus hemagglutinin.
@ast
Conformational intermediates and fusion activity of influenza virus hemagglutinin.
@en
P2093
P2860
P1433
P1476
Conformational intermediates and fusion activity of influenza virus hemagglutinin
@en
P2093
P2860
P304
P577
1999-06-01T00:00:00Z