Delay time for influenza virus hemagglutinin-induced membrane fusion depends on hemagglutinin surface density.
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Visualizing infection of individual influenza virusesCrystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers AssemblySynchronized activation and refolding of influenza hemagglutinin in multimeric fusion machinesThe pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation.Inner but not outer membrane leaflets control the transition from glycosylphosphatidylinositol-anchored influenza hemagglutinin-induced hemifusion to full fusionMembrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.Enhancement of viral fusion by nonadsorbing polymers.Rapid membrane fusion of individual virus particles with supported lipid bilayers.Architecture of a nascent viral fusion pore.Influenza virus-membrane fusion triggered by proton uncaging for single particle studies of fusion kineticsVisualization and Sequencing of Membrane Remodeling Leading to Influenza Virus Fusion.Membrane fusion promoted by increasing surface densities of the paramyxovirus F and HN proteins: comparison of fusion reactions mediated by simian virus 5 F, human parainfluenza virus type 3 F, and influenza virus HA.Role of hemagglutinin surface density in the initial stages of influenza virus fusion: lack of evidence for cooperativityStudies on the fusion peptide of a paramyxovirus fusion glycoprotein: roles of conserved residues in cell fusion.Kinetics of the low pH-induced conformational changes and fusogenic activity of influenza hemagglutinin.Membrane fusion of Semliki Forest virus in a model system: correlation between fusion kinetics and structural changes in the envelope glycoprotein.Intermediates and kinetics of membrane fusion.A mechanism of protein-mediated fusion: coupling between refolding of the influenza hemagglutinin and lipid rearrangements.Influenza virus-mediated membrane fusion: determinants of hemagglutinin fusogenic activity and experimental approaches for assessing virus fusion.Cytoplasmic tail of Moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: implications for mechanism of action of the R Peptide.Reversible merger of membranes at the early stage of influenza hemagglutinin-mediated fusionCross-linking of glycoprotein oligomers during herpes simplex virus type 1 entry.Molecular mechanism underlying the action of a novel fusion inhibitor of influenza A virusRestricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion.Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events.Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 trimers into multiprotein aggregates.The initial fusion pore induced by baculovirus GP64 is large and forms quicklyCalcium ions are required for cell fusion mediated by the CD4-human immunodeficiency virus type 1 envelope glycoprotein interactionIntermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.Initial size and dynamics of viral fusion pores are a function of the fusion protein mediating membrane fusionG541R within the 4070A TM protein regulates fusion in murine leukemia virusesA discrete stage of baculovirus GP64-mediated membrane fusion.Role for influenza virus envelope cholesterol in virus entry and infection.Palmitoylation contributes to membrane curvature in Influenza A virus assembly and hemagglutinin-mediated membrane fusion.Altering expression levels of human immunodeficiency virus type 1 gp120-gp41 affects efficiency but not kinetics of cell-cell fusion.Stochastic simulation of hemagglutinin-mediated fusion pore formation.pH-dependence of intermediate steps of membrane fusion induced by the influenza fusion peptide.The MuLV 4070A G541R Env mutation decreases the stability and alters the conformation of the TM ectodomain.
P2860
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P2860
Delay time for influenza virus hemagglutinin-induced membrane fusion depends on hemagglutinin surface density.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
1991年论文
@zh
1991年论文
@zh-cn
name
Delay time for influenza virus ...... hemagglutinin surface density.
@ast
Delay time for influenza virus ...... hemagglutinin surface density.
@en
type
label
Delay time for influenza virus ...... hemagglutinin surface density.
@ast
Delay time for influenza virus ...... hemagglutinin surface density.
@en
prefLabel
Delay time for influenza virus ...... hemagglutinin surface density.
@ast
Delay time for influenza virus ...... hemagglutinin surface density.
@en
P2093
P2860
P1433
P1476
Delay time for influenza virus ...... hemagglutinin surface density.
@en
P2093
P2860
P304
P407
P577
1991-05-01T00:00:00Z