Semliki Forest virus particles containing only the E1 envelope glycoprotein are infectious and can induce cell-cell fusion.
about
Replication of alphaviruses: a review on the entry process of alphaviruses into cellsA single deletion in the membrane-proximal region of the Sindbis virus glycoprotein E2 endodomain blocks virus assemblyEntry and uncoating of enveloped virusesEffects of membrane potential and sphingolipid structures on fusion of Semliki Forest virus.Events in the endoplasmic reticulum abrogate the temperature sensitivity of Sindbis virus mutant ts23The formation of intramolecular disulfide bridges is required for induction of the Sindbis virus mutant ts23 phenotypeCholesterol 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 cellsOligomerization-dependent folding of the membrane fusion protein of Semliki Forest virusFormation and rearrangement of disulfide bonds during maturation of the Sindbis virus E1 glycoproteinMembrane and protein interactions of a soluble form of the Semliki Forest virus fusion proteinSindbis virus attachment: isolation and characterization of mutants with impaired binding to vertebrate cellsRole of spike protein conformational changes in fusion of Semliki Forest virusProtein-protein interactions in an alphavirus membraneMembrane fusion of Semliki Forest virus involves homotrimers of the fusion proteinBiosynthesis, maturation, and acid activation of the Semliki Forest virus fusion proteinIn vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: the small 6,000-molecular-weight membrane protein modulates virus releaseMutagenesis of the putative fusion domain of the Semliki Forest virus spike proteinFusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62Deletions in the Transmembrane Domain of a Sindbis Virus Glycoprotein Alter Virus Infectivity, Stability, and Host RangeMolecular Links between the E2 Envelope Glycoprotein and Nucleocapsid Core in Sindbis VirusThe alphaviruses: gene expression, replication, and evolutionCell-based analysis of Chikungunya virus E1 protein in membrane fusion.The surface conformation of Sindbis virus glycoproteins E1 and E2 at neutral and low pH, as determined by mass spectrometry-based mappingMembrane fusion of Semliki Forest virus in a model system: correlation between fusion kinetics and structural changes in the envelope glycoprotein.The alphavirus E3 glycoprotein functions in a clade-specific manner.Lentiviruses with trastuzumab bound to their envelopes can target and kill prostate cancer cells.Natural resistance-associated macrophage protein is a cellular receptor for sindbis virus in both insect and mammalian hosts.Mutating conserved cysteines in the alphavirus e2 glycoprotein causes virus-specific assembly defects.Membrane fusion process of Semliki Forest virus. II: Cleavage-dependent reorganization of the spike protein complex controls virus entryFunctional characterization of the alphavirus TF proteinRotavirus gene structure and function.Role of conserved cysteines in the alphavirus E3 proteinFusion of mApple and Venus fluorescent proteins to the Sindbis virus E2 protein leads to different cell-binding properties.Deletions in the putative cell receptor-binding domain of Sindbis virus strain MRE16 E2 glycoprotein reduce midgut infectivity in Aedes aegypti.Genome-Wide Screening Uncovers the Significance of N-Sulfation of Heparan Sulfate as a Host Cell Factor for Chikungunya Virus Infection.The nucleocapsid-binding spike subunit E2 of Semliki Forest virus requires complex formation with the E1 subunit for activity.Spike protein oligomerization control of Semliki Forest virus fusion.Membrane fusion of Semliki Forest virus requires sphingolipids in the target membrane.Identification of the pore forming element of Semliki Forest virus spikes.
P2860
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P2860
Semliki Forest virus particles containing only the E1 envelope glycoprotein are infectious and can induce cell-cell fusion.
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年学术文章
@wuu
1988年学术文章
@zh-cn
1988年学术文章
@zh-hans
1988年学术文章
@zh-my
1988年学术文章
@zh-sg
1988年學術文章
@yue
1988年學術文章
@zh
1988年學術文章
@zh-hant
name
Semliki Forest virus particles ...... d can induce cell-cell fusion.
@en
Semliki Forest virus particles ...... d can induce cell-cell fusion.
@nl
type
label
Semliki Forest virus particles ...... d can induce cell-cell fusion.
@en
Semliki Forest virus particles ...... d can induce cell-cell fusion.
@nl
prefLabel
Semliki Forest virus particles ...... d can induce cell-cell fusion.
@en
Semliki Forest virus particles ...... d can induce cell-cell fusion.
@nl
P1433
P1476
Semliki Forest virus particles ...... d can induce cell-cell fusion.
@en
P356
10.1016/0042-6822(88)90141-9
P407
P577
1988-09-01T00:00:00Z