Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
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Biological function of the low-pH, fusion-inactive conformation of rabies virus glycoprotein (G): G is transported in a fusion-inactive state-like conformationCrystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteinsDistinct functional determinants of influenza hemagglutinin-mediated membrane fusionInfluenza virus M2 protein ion channel activity helps to maintain pandemic 2009 H1N1 virus hemagglutinin fusion competence during transport to the cell surface.Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machinesSpecific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity.Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes.Structural studies on membrane-embedded influenza hemagglutinin and its fragmentsEffect of the N-terminal glycine on the secondary structure, orientation, and interaction of the influenza hemagglutinin fusion peptide with lipid bilayers.Influenza hemagglutinin assumes a tilted conformation during membrane fusion as determined by attenuated total reflection FTIR spectroscopy.Structure-based identification of an inducer of the low-pH conformational change in the influenza virus hemagglutinin: irreversible inhibition of infectivity.New insights into the spring-loaded conformational change of influenza virus hemagglutinin.Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin.Architecture of a nascent viral fusion pore.Structural organization of a filamentous influenza A virus.A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation.Influenza A virus can undergo multiple cycles of replication without M2 ion channel activity.Order and disorder control the functional rearrangement of influenza hemagglutinin.Morphological changes and fusogenic activity of influenza virus hemagglutinin.A mechanism of protein-mediated fusion: coupling between refolding of the influenza hemagglutinin and lipid rearrangements.Variations in pH sensitivity, acid stability, and fusogenicity of three influenza virus H3 subtypes.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.Capturing a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugated peptide, a new antiviral strategy for influenza virus.Assembly of a rod-shaped chimera of a trimeric GCN4 zipper and the HIV-1 gp41 ectodomain expressed in Escherichia coli.Rabies virus-induced membrane fusion pathway.Retroviral vectors preloaded with a viral receptor-ligand bridge protein are targeted to specific cell types.Studies using double mutants of the conformational transitions in influenza hemagglutinin required for its membrane fusion activity.Influenza hemagglutinin is spring-loaded by a metastable native conformation.Characterizing a histidine switch controlling pH-dependent conformational changes of the influenza virus hemagglutininProtein intrinsic disorder and influenza virulence: the 1918 H1N1 and H5N1 viruses.The central structural feature of the membrane fusion protein subunit from the Ebola virus glycoprotein is a long triple-stranded coiled coil.Elongation of the cytoplasmic tail interferes with the fusion activity of influenza virus hemagglutinin.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.Rotation-Activated and Cooperative Zipping Characterize Class I Viral Fusion Protein Dynamics.Influenza Hemagglutinin Protein Stability, Activation, and Pandemic Risk.
P2860
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P2860
Electron microscopy of antibody complexes of influenza virus haemagglutinin in the fusion pH conformation
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
Electron microscopy of antibod ...... in the fusion pH conformation
@ast
Electron microscopy of antibod ...... in the fusion pH conformation
@en
type
label
Electron microscopy of antibod ...... in the fusion pH conformation
@ast
Electron microscopy of antibod ...... in the fusion pH conformation
@en
prefLabel
Electron microscopy of antibod ...... in the fusion pH conformation
@ast
Electron microscopy of antibod ...... in the fusion pH conformation
@en
P2093
P2860
P1433
P1476
Electron microscopy of antibod ...... in the fusion pH conformation
@en
P2093
D A Steinhauer
J J Skehel
L J Calder
R W Ruigrok
S A Wharton
P2860
P304
P407
P577
1995-01-01T00:00:00Z