Lethality of PE2 incorporation into Sindbis virus can be suppressed by second-site mutations in E3 and E2
about
The furin protease cleavage recognition sequence of Sindbis virus PE2 can mediate virion attachment to cell surface heparan sulfatePE2 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 virusSindbis Virus Vectors Designed To Express a Foreign Protein as a Cleavable Component of the Viral Structural PolyproteinDeduced consensus sequence of Sindbis virus strain AR339: mutations contained in laboratory strains which affect cell culture and in vivo phenotypesDifferential processing of sindbis virus glycoprotein PE2 in cultured vertebrate and arthropod cellsThe amino-terminal residue of Sindbis virus glycoprotein E2 influences virus maturation, specific infectivity for BHK cells, and virulence in miceA structural and functional perspective of alphavirus replication and assemblyStructural changes of envelope proteins during alphavirus fusionThe alphaviruses: gene expression, replication, and evolutionThe host range phenotype displayed by a Sindbis virus glycoprotein variant results from virion aggregation and retention on the surface of mosquito cellsStructural localization of the E3 glycoprotein in attenuated Sindbis virus mutants.An arthropod enzyme, Dfurin1, and a vertebrate furin homolog display distinct cleavage site sequence preferences for a shared viral proprotein substrateAlphavirus Entry and Membrane Fusion.Suppressors of cleavage-site mutations in the p62 envelope protein of Semliki Forest virus reveal dynamics in spike structure and function.Adaptation of Sindbis virus to BHK cells selects for use of heparan sulfate as an attachment receptor.Specific in vitro cleavage of a Leishmania virus capsid-RNA-dependent RNA polymerase polyprotein by a host cysteine-like proteaseAntibody to the E3 glycoprotein protects mice against lethal venezuelan equine encephalitis virus infection.
P2860
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P2860
Lethality of PE2 incorporation into Sindbis virus can be suppressed by second-site mutations in E3 and E2
description
1994 nî lūn-bûn
@nan
1994 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Lethality of PE2 incorporation ...... nd-site mutations in E3 and E2
@ast
Lethality of PE2 incorporation ...... nd-site mutations in E3 and E2
@en
Lethality of PE2 incorporation ...... nd-site mutations in E3 and E2
@nl
type
label
Lethality of PE2 incorporation ...... nd-site mutations in E3 and E2
@ast
Lethality of PE2 incorporation ...... nd-site mutations in E3 and E2
@en
Lethality of PE2 incorporation ...... nd-site mutations in E3 and E2
@nl
prefLabel
Lethality of PE2 incorporation ...... nd-site mutations in E3 and E2
@ast
Lethality of PE2 incorporation ...... nd-site mutations in E3 and E2
@en
Lethality of PE2 incorporation ...... nd-site mutations in E3 and E2
@nl
P2093
P2860
P1433
P1476
Lethality of PE2 incorporation ...... nd-site mutations in E3 and E2
@en
P2093
H W Heidner
K L McKnight
R E Johnston
P2860
P304
P577
1994-04-01T00:00:00Z