about
Fusion of Rous sarcoma virus with host cells does not require exposure to low pHEntry and uncoating of enveloped virusesBiological function of the low-pH, fusion-inactive conformation of rabies virus glycoprotein (G): G is transported in a fusion-inactive state-like conformationCholesterol is required in the exit pathway of Semliki Forest virusMembrane fusion process of Semliki Forest virus. I: Low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cellsMembrane and protein interactions of a soluble form of the Semliki Forest virus fusion proteinRole of spike protein conformational changes in fusion of Semliki Forest virusMembrane fusion of Semliki Forest virus involves homotrimers of the fusion proteinTransport of incoming influenza virus nucleocapsids into the nucleusA fusion-defective mutant of the vesicular stomatitis virus glycoproteinMutagenesis of the putative fusion domain of the Semliki Forest virus spike proteinThe alphaviruses: gene expression, replication, and evolutionMembrane fusion mechanisms: the influenza hemagglutinin paradigm and its implications for intracellular fusion.Nuclear import of influenza virus RNA can be mediated by viral nucleoprotein and transport factors required for protein import.Fus2 localizes near the site of cell fusion and is required for both cell fusion and nuclear alignment during zygote formation.Biochemical characterization of nuclear pore complex protein gp210 oligomersEffects of amino acid changes in the extracellular domain of the human immunodeficiency virus type 1 gp41 envelope glycoproteinStructural features of membrane fusion between influenza virus and liposome as revealed by quick-freezing electron microscopyAntiviral activity of acidic polysaccharides from Coccomyxa gloeobotrydiformi, a green alga, against an in vitro human influenza A virus infection.Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.The receptor for the subgroup A avian leukosis-sarcoma viruses binds to subgroup A but not to subgroup C envelope glycoprotein.The amino-terminal region of the fusion peptide of influenza virus hemagglutinin HA2 inserts into sodium dodecyl sulfate micelle with residues 16-18 at the aqueous boundary at acidic pH. Oligomerization and the conformational flexibility.Inhibition of influenza A virus replication by compounds interfering with the fusogenic function of the viral hemagglutininInitial events in infectious salmon anemia virus infection: evidence for the requirement of a low-pH step.Intermediates in influenza induced membrane fusion.Fusomorphogenesis: cell fusion in organ formation.Studies on the fusion peptide of a paramyxovirus fusion glycoprotein: roles of conserved residues in cell fusion.Lack of correlation between soluble CD4-induced shedding of the human immunodeficiency virus type 1 exterior envelope glycoprotein and subsequent membrane fusion events.The cytosolic domain of Fis1 binds and reversibly clusters lipid vesicles.BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complexMembrane fusion of Semliki Forest virus in a model system: correlation between fusion kinetics and structural changes in the envelope glycoprotein.Micropipette manipulation technique for the monitoring of pH-dependent membrane lysis as induced by the fusion peptide of influenza virusGreasing membrane fusion and fission machineries.Statistical thermodynamics of membrane bending-mediated protein-protein attractions.Glycoproteins gB, gD, and gHgL of herpes simplex virus type 1 are necessary and sufficient to mediate membrane fusion in a Cos cell transfection system.Murine leukemia virus R Peptide inhibits influenza virus hemagglutinin-induced membrane fusion.Determinants of human immunodeficiency virus type 1 entry in the CDR2 loop of the CD4 glycoprotein.Control of baculovirus gp64-induced syncytium formation by membrane lipid compositionAnalysis of the murine leukemia virus R peptide: delineation of the molecular determinants which are important for its fusion inhibition activityFatty acylation promotes fusion of transport vesicles with Golgi cisternae.
P2860
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P2860
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年学术文章
@wuu
1989年学术文章
@zh-cn
1989年学术文章
@zh-hans
1989年学术文章
@zh-my
1989年学术文章
@zh-sg
1989年學術文章
@yue
1989年學術文章
@zh
1989年學術文章
@zh-hant
name
Protein-mediated membrane fusion.
@en
type
label
Protein-mediated membrane fusion.
@en
prefLabel
Protein-mediated membrane fusion.
@en
P2093
P1476
Protein-mediated membrane fusion.
@en
P2093
P304
P356
10.1146/ANNUREV.BB.18.060189.001155
P577
1989-01-01T00:00:00Z