Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62
about
Replication of alphaviruses: a review on the entry process of alphaviruses into cellsStudy of the early steps of the Hepatitis B Virus life cycleAcid-resistant bovine pestivirus requires activation for pH-triggered fusion during entry.PE2 cleavage mutants of Sindbis virus: correlation between viral infectivity and pH-dependent membrane fusion activation of the spike heterodimer.Resuscitating mutations in a furin cleavage-deficient mutant of the flavivirus tick-borne encephalitis virusMolecular genetic study of the interaction of Sindbis virus E2 with Ross River virus E1 for virus budding.Time- and Temperature-Dependent Activation of Hepatitis C Virus for Low-pH-Triggered EntryFurin Processing and Proteolytic Activation of Semliki Forest VirusBiological function of the low-pH, fusion-inactive conformation of rabies virus glycoprotein (G): G is transported in a fusion-inactive state-like conformationEvents in the endoplasmic reticulum abrogate the temperature sensitivity of Sindbis virus mutant ts23Proteolytic activation of tick-borne encephalitis virus by furinThe oligomerization reaction of the Semliki Forest virus membrane protein subunitsCholesterol is required for infection by 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 virusLethality of PE2 incorporation into Sindbis virus can be suppressed by second-site mutations in E3 and E2The amino-terminal residue of Sindbis virus glycoprotein E2 influences virus maturation, specific infectivity for BHK cells, and virulence in miceMembrane fusion of Semliki Forest virus involves homotrimers of the fusion proteinSpike protein-nucleocapsid interactions drive the budding of alphavirusesBiosynthesis, 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 proteinA structural and functional perspective of alphavirus replication and assemblyThe alphaviruses: gene expression, replication, and evolutionViral membrane fusion.Low-pH-dependent fusion of Sindbis virus with receptor-free cholesterol- and sphingolipid-containing liposomes.Furin cleavage potentiates the membrane fusion-controlling intersubunit disulfide bond isomerization activity of leukemia virus Env.Mutating conserved cysteines in the alphavirus e2 glycoprotein causes virus-specific assembly defects.Protease-induced infectivity of hepatitis B virus for a human hepatoblastoma cell line.Flavivirus premembrane protein cleavage and spike heterodimer secretion require the function of the viral proteinase NS3.Stabilization of TM trimer interactions during activation of moloney murine leukemia virus Env.Membrane fusion process of Semliki Forest virus. II: Cleavage-dependent reorganization of the spike protein complex controls virus entryFunction of Semliki Forest virus E3 peptide in virus assembly: replacement of E3 with an artificial signal peptide abolishes spike heterodimerization and surface expression of E1.Role of conserved cysteines in the alphavirus E3 proteinCharacterization of pH-sensitive molecular switches that trigger the structural transition of vesicular stomatitis virus glycoprotein from the postfusion state toward the prefusion state.Two-helper RNA system for production of recombinant Semliki forest virus particles.Protease cleavage of reovirus capsid protein mu1/mu1C is blocked by alkyl sulfate detergents, yielding a new type of infectious subvirion particle.fus-1, a pH shift mutant of Semliki Forest virus, acts by altering spike subunit interactions via a mutation in the E2 subunitSuppressors of cleavage-site mutations in the p62 envelope protein of Semliki Forest virus reveal dynamics in spike structure and function.Mutagenesis of varicella-zoster virus glycoprotein B: putative fusion loop residues are essential for viral replication, and the furin cleavage motif contributes to pathogenesis in skin tissue in vivo.
P2860
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P2860
Fusion function of the Semliki Forest virus spike is activated by proteolytic cleavage of the envelope glycoprotein precursor p62
description
1990 nî lūn-bûn
@nan
1990 թուականի Մարտին հրատարակուած գիտական յօդուած
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1990 թվականի մարտին հրատարակված գիտական հոդված
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1990年の論文
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1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Fusion function of the Semliki ...... ope glycoprotein precursor p62
@ast
Fusion function of the Semliki ...... ope glycoprotein precursor p62
@en
Fusion function of the Semliki ...... ope glycoprotein precursor p62
@nl
type
label
Fusion function of the Semliki ...... ope glycoprotein precursor p62
@ast
Fusion function of the Semliki ...... ope glycoprotein precursor p62
@en
Fusion function of the Semliki ...... ope glycoprotein precursor p62
@nl
prefLabel
Fusion function of the Semliki ...... ope glycoprotein precursor p62
@ast
Fusion function of the Semliki ...... ope glycoprotein precursor p62
@en
Fusion function of the Semliki ...... ope glycoprotein precursor p62
@nl
P2860
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P1433
P1476
Fusion function of the Semliki ...... ope glycoprotein precursor p62
@en
P2093
P2860
P304
P577
1990-03-01T00:00:00Z