A dissection of steps leading to viral envelope protein-mediated membrane fusion.
about
Crystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers AssemblyDilation of the human immunodeficiency virus-1 envelope glycoprotein fusion pore revealed by the inhibitory action of a synthetic peptide from gp41Enhancement of viral fusion by nonadsorbing polymers.Influenza virus-membrane fusion triggered by proton uncaging for single particle studies of fusion kineticsRole of hemagglutinin surface density in the initial stages of influenza virus fusion: lack of evidence for cooperativityConformational intermediates and fusion activity of influenza virus hemagglutinin.Infectious entry by amphotropic as well as ecotropic murine leukemia viruses occurs through an endocytic pathwayModulation of entry of enveloped viruses by cholesterol and sphingolipids (Review).Kinetics of the low pH-induced conformational changes and fusogenic activity of influenza hemagglutinin.Fusion flashes illuminate kinetics.Intermediates and kinetics of membrane fusion.Delay of influenza hemagglutinin refolding into a fusion-competent conformation by receptor binding: a hypothesisControl of baculovirus gp64-induced syncytium formation by membrane lipid compositionRestricted 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.Hemagglutinin-neuraminidase enhances F protein-mediated membrane fusion of reconstituted Sendai virus envelopes with cellsResonance energy transfer imaging of phospholipid vesicle interaction with a planar phospholipid membrane: undulations and attachment sites in the region of calcium-mediated membrane--membrane adhesion.Conformational changes in cell surface HIV-1 envelope glycoproteins are triggered by cooperation between cell surface CD4 and co-receptors.A GxxxG-like motif within HIV-1 fusion peptide is critical to its immunosuppressant activity, structure, and interaction with the transmembrane domain of the T-cell receptor.A trans-dominant mutation in human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein gp41 inhibits membrane fusion when expressed in target cells.Membrane perturbation and fusion pore formation in influenza hemagglutinin-mediated membrane fusion. A new model for fusion.Fusion peptides derived from the HIV type 1 glycoprotein 41 associate within phospholipid membranes and inhibit cell-cell Fusion. Structure-function study.Lysolipids do not inhibit influenza virus fusion by interaction with hemagglutinin.Role of target membrane structure in fusion with influenza virus: effect of modulating erythrocyte transbilayer phospholipid distribution.
P2860
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P2860
A dissection of steps leading to viral envelope protein-mediated membrane fusion.
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
A dissection of steps leading to viral envelope protein-mediated membrane fusion.
@en
type
label
A dissection of steps leading to viral envelope protein-mediated membrane fusion.
@en
prefLabel
A dissection of steps leading to viral envelope protein-mediated membrane fusion.
@en
P2093
P2860
P1476
A dissection of steps leading to viral envelope protein-mediated membrane fusion.
@en
P2093
P2860
P304
P356
10.1111/J.1749-6632.1991.TB36499.X
P407
P577
1991-01-01T00:00:00Z