Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane.
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Replication of alphaviruses: a review on the entry process of alphaviruses into cellsIdentification of the myelin oligodendrocyte glycoprotein as a cellular receptor for rubella virusEarly Events in Chikungunya Virus Infection-From Virus Cell Binding to Membrane FusionReversible Acid-Induced Inactivation of the Membrane Fusion Protein of Semliki Forest VirusPE2 cleavage mutants of Sindbis virus: correlation between viral infectivity and pH-dependent membrane fusion activation of the spike heterodimer.The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.Effects of membrane potential and sphingolipid structures on fusion of Semliki Forest virus.Novel mutations that control the sphingolipid and cholesterol dependence of the Semliki Forest virus fusion proteinInvolvement of Lipids in Different Steps of the Flavivirus Fusion MechanismThe 6-kilodalton membrane protein of Semliki Forest virus is involved in the budding processSphingolipid-dependent fusion of Semliki Forest virus with cholesterol-containing liposomes requires both the 3-hydroxyl group and the double bond of the sphingolipid backboneMembrane and protein interactions of a soluble form of the Semliki Forest virus fusion proteinStructure of the St. Louis Encephalitis Virus Postfusion Envelope TrimerInvolvement of long chain fatty acid elongation in the trafficking of secretory vesicles in yeastFusion of Enveloped Viruses in Endosomes.Dengue virus ensures its fusion in late endosomes using compartment-specific lipids.Cholesterol promotes hemifusion and pore widening in membrane fusion induced by influenza hemagglutinin.Rapid membrane fusion of individual virus particles with supported lipid bilayers.Dynamics of Chikungunya Virus Cell Entry Unraveled by Single-Virus Tracking in Living Cells.The cholesterol requirement for sindbis virus entry and exit and characterization of a spike protein region involved in cholesterol dependenceBiochemical consequences of a mutation that controls the cholesterol dependence of Semliki Forest virus fusionEvidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts.Glycosphingolipids promote entry of a broad range of human immunodeficiency virus type 1 isolates into cell lines expressing CD4, CXCR4, and/or CCR5.Sindbis virus entry into cells triggers apoptosis by activating sphingomyelinase, leading to the release of ceramide.Low-pH-dependent fusion of Sindbis virus with receptor-free cholesterol- and sphingolipid-containing liposomes.Induction of apoptosis by Sindbis virus occurs at cell entry and does not require virus replication.Interactions of N-stearoyl sphingomyelin with cholesterol and dipalmitoylphosphatidylcholine in bilayer membranesImaging multiple intermediates of single-virus membrane fusion mediated by distinct fusion proteins.Macro-ripple phase formation in bilayers composed of galactosylceramide and phosphatidylcholineA single mutation in the E2 glycoprotein important for neurovirulence influences binding of sindbis virus to neuroblastoma cellsAdaptation of alphaviruses to heparan sulfate: interaction of Sindbis and Semliki forest viruses with liposomes containing lipid-conjugated heparin.Alphavirus Entry and Membrane Fusion.Cubic phases in phosphatidylcholine-cholesterol mixtures: cholesterol as membrane "fusogen"Acid sphingomyelinase deficiency increases susceptibility to fatal alphavirus encephalomyelitis.Autophagy in the light of sphingolipid metabolismTraffic, polarity, and detergent solubility of a glycosylphosphatidylinositol-anchored protein after LDL-deprivation of MDCK cells.Mechanisms of mutations inhibiting fusion and infection by Semliki Forest virus.A single point mutation controls the cholesterol dependence of Semliki Forest virus entry and exitSphingomyelinase treatment induces ATP-independent endocytosisClass II fusion protein of alphaviruses drives membrane fusion through the same pathway as class I proteins.
P2860
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P2860
Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane.
description
1994 nî lūn-bûn
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1994年の論文
@ja
1994年学术文章
@wuu
1994年学术文章
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1994年学术文章
@zh-hans
1994年学术文章
@zh-my
1994年学术文章
@zh-sg
1994年學術文章
@yue
1994年學術文章
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1994年學術文章
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name
Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane.
@en
type
label
Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane.
@en
prefLabel
Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane.
@en
P2093
P2860
P1433
P1476
Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane.
@en
P2093
P2860
P304
P407
P577
1994-06-01T00:00:00Z