Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events.
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Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeThe complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interfacepH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMRMembrane fusion mechanisms: the influenza hemagglutinin paradigm and its implications for intracellular fusion.Influenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.The impact of influenza hemagglutinin fusion peptide length and viral subtype on its structure and dynamicsThe anti-influenza virus agent 4-GU-DANA (zanamivir) inhibits cell fusion mediated by human parainfluenza virus and influenza virus HA.Comprehensive kinetic analysis of influenza hemagglutinin-mediated membrane fusion: role of sialate binding.Structure and accessibility of HA trimers on intact 2009 H1N1 pandemic influenza virus to stem region-specific neutralizing antibodiesThe transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transitionA host-guest system to study structure-function relationships of membrane fusion peptides.Sequential roles of receptor binding and low pH in forming prehairpin and hairpin conformations of a retroviral envelope glycoproteinSingle vesicle millisecond fusion kinetics reveals number of SNARE complexes optimal for fast SNARE-mediated membrane fusion.Membrane structures of the hemifusion-inducing fusion peptide mutant G1S and the fusion-blocking mutant G1V of influenza virus hemagglutinin suggest a mechanism for pore opening in membrane fusion.Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machinesGeranylgeranylated SNAREs are dominant inhibitors of membrane fusionThe pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation.Dilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41Effects of spontaneous bilayer curvature on influenza virus-mediated fusion pores.pH-induced conformational changes of membrane-bound influenza hemagglutinin and its effect on target lipid bilayers.Tension of membranes expressing the hemagglutinin of influenza virus inhibits fusion.Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1New insights into the spring-loaded conformational change of influenza virus hemagglutinin.Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusionImaging individual retroviral fusion events: from hemifusion to pore formation and growth.Rapid membrane fusion of individual virus particles with supported lipid bilayers.Architecture of a nascent viral fusion pore.IL-10/TGF-beta-modified macrophages induce regulatory T cells and protect against adriamycin nephrosis.Transmembrane orientation and possible role of the fusogenic peptide from parainfluenza virus 5 (PIV5) in promoting fusionInfluenza virus-membrane fusion triggered by proton uncaging for single particle studies of fusion kineticsVisualization and Sequencing of Membrane Remodeling Leading to Influenza Virus Fusion.Mode of action of an antiviral peptide from HIV-1. Inhibition at a post-lipid mixing stage.Rabies virus-induced membrane fusion.Structural intermediates in influenza haemagglutinin-mediated fusion.The conserved glycine-rich segment linking the N-terminal fusion peptide to the coiled coil of human T-cell leukemia virus type 1 transmembrane glycoprotein gp21 is a determinant of membrane fusion function.Stoichiometry of antibody neutralization of human immunodeficiency virus type 1.Effect of cleavage mutants on syncytium formation directed by the wild-type fusion protein of Newcastle disease virusRole of the cytoplasmic tail of ecotropic moloney murine leukemia virus Env protein in fusion pore formation.Role of hemagglutinin surface density in the initial stages of influenza virus fusion: lack of evidence for cooperativityCooperation of multiple CCR5 coreceptors is required for infections by human immunodeficiency virus type 1
P2860
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P2860
Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Dilation of the influenza hema ...... idual cell-cell fusion events.
@ast
Dilation of the influenza hema ...... idual cell-cell fusion events.
@en
type
label
Dilation of the influenza hema ...... idual cell-cell fusion events.
@ast
Dilation of the influenza hema ...... idual cell-cell fusion events.
@en
prefLabel
Dilation of the influenza hema ...... idual cell-cell fusion events.
@ast
Dilation of the influenza hema ...... idual cell-cell fusion events.
@en
P2093
P2860
P356
P1476
Dilation of the influenza hema ...... idual cell-cell fusion events.
@en
P2093
P2860
P356
10.1083/JCB.135.1.63
P407
P577
1996-10-01T00:00:00Z