The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.
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Two Chikungunya isolates from the outbreak of La Reunion (Indian Ocean) exhibit different patterns of infection in the mosquito, Aedes albopictusReplication of alphaviruses: a review on the entry process of alphaviruses into cellsHerpes simplex virus glycoprotein B associates with target membranes via its fusion loopsVirus entry, assembly, budding, and membrane raftsSpecific association of glycoprotein B with lipid rafts during herpes simplex virus entryEarly Events in Chikungunya Virus Infection-From Virus Cell Binding to Membrane FusionReversible Acid-Induced Inactivation of the Membrane Fusion Protein of Semliki Forest VirusNovel mutations that control the sphingolipid and cholesterol dependence of the Semliki Forest virus fusion proteinSecond-Site Revertants of a Semliki Forest Virus Fusion-Block Mutation Reveal the Dynamics of a Class II Membrane Fusion ProteinSite-Directed Antibodies against the Stem Region Reveal Low pH-Induced Conformational Changes of the Semliki Forest Virus Fusion ProteinDifferential Cholesterol Binding by Class II Fusion Proteins Determines Membrane Fusion PropertiesStructures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common ThemeRole of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion ProteinLow pH-dependent Hepatitis C Virus Membrane Fusion Depends on E2 Integrity, Target Lipid Composition, and Density of Virus ParticlesA structural and functional perspective of alphavirus replication and assemblyA Stable Prefusion Intermediate of the Alphavirus Fusion Protein Reveals Critical Features of Class II Membrane FusionStructure of the dengue virus envelope protein after membrane fusionInfluenza virus hemagglutinin concentrates in lipid raft microdomains for efficient viral fusion.Mosquito cellular factors and functions in mediating the infectious entry of chikungunya virusVirus membrane-fusion proteins: more than one way to make a hairpinFusogenic properties of the ectodomains of hepatitis C virus envelope proteins.Identification of the membrane-active regions of the severe acute respiratory syndrome coronavirus spike membrane glycoprotein using a 16/18-mer peptide scan: implications for the viral fusion mechanismRole of cholesterol in human immunodeficiency virus type 1 envelope protein-mediated fusion with host cellsHepatitis C virus core protein binding to lipid membranes: the role of domains 1 and 2.Identification of the membrane-active regions of hepatitis C virus p7 protein: biophysical characterization of the loop region.Nuclear envelope remnants: fluid membranes enriched in sterols and polyphosphoinositidesEndocytosis of chikungunya virus into mammalian cells: role of clathrin and early endosomal compartments.Murine coronavirus requires lipid rafts for virus entry and cell-cell fusion but not for virus release.Modulation of entry of enveloped viruses by cholesterol and sphingolipids (Review).Biophysical characterization and membrane interaction of the two fusion loops of glycoprotein B from herpes simplex type I virus.Pseudorevertants of a Semliki forest virus fusion-blocking mutation reveal a critical interchain interaction in the core trimerInfluenza virus can enter and infect cells in the absence of clathrin-mediated endocytosis.Independent segregation of human immunodeficiency virus type 1 Gag protein complexes and lipid rafts.Alphavirus Entry and Membrane Fusion.Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH.Transition from hemifusion to pore opening is rate limiting for vacuole membrane fusionRequirements for CEACAMs and cholesterol during murine coronavirus cell entry.Role for influenza virus envelope cholesterol in virus entry and infection.Cholesterol dependence of HTLV-I infection.Cholesterol, regulated exocytosis and the physiological fusion machine.
P2860
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P2860
The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
name
The Fusion Peptide of Semliki Forest Virus Associates with Sterol-Rich Membrane Domains
@nl
The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.
@ast
The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.
@en
type
label
The Fusion Peptide of Semliki Forest Virus Associates with Sterol-Rich Membrane Domains
@nl
The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.
@ast
The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.
@en
prefLabel
The Fusion Peptide of Semliki Forest Virus Associates with Sterol-Rich Membrane Domains
@nl
The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.
@ast
The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.
@en
P2860
P921
P1433
P1476
The fusion peptide of Semliki Forest virus associates with sterol-rich membrane domains.
@en
P2093
Don L Gibbons
P2860
P304
P356
10.1128/JVI.76.7.3267-3275.2002
P577
2002-04-01T00:00:00Z