Versatility of the accessory C proteins of Sendai virus: contribution to virus assembly as an additional role.
about
The C proteins of human parainfluenza virus type 1 block IFN signaling by binding and retaining Stat1 in perinuclear aggregates at the late endosomeThe nonstructural proteins of Nipah virus play a key role in pathogenicity in experimentally infected animals.Conserved charged amino acids within Sendai virus C protein play multiple roles in the evasion of innate immune responsesStringent requirement for the C protein of wild-type measles virus for growth both in vitro and in macaques.Y2, the smallest of the Sendai virus C proteins, is fully capable of both counteracting the antiviral action of interferons and inhibiting viral RNA synthesis.AIP1/Alix is a binding partner of Sendai virus C protein and facilitates virus budding.Paramyxovirus assembly and budding: building particles that transmit infections.The amino-terminal half of Sendai virus C protein is not responsible for either counteracting the antiviral action of interferons or down-regulating viral RNA synthesisC-terminal region of STAT-1alpha is not necessary for its ubiquitination and degradation caused by mumps virus V proteinThe C-terminal end of parainfluenza virus 5 NP protein is important for virus-like particle production and M-NP protein interaction.Passage of a Sendai virus recombinant in embryonated chicken eggs leads to markedly rapid accumulation of U-to-C transitions in a limited region of the viral genomeParamyxovirus accessory proteins as interferon antagonists.Clustered basic amino acids of the small sendai virus C protein Y1 are critical to its RAN GTPase-mediated nuclear localization.Characterization of the amino acid residues of sendai virus C protein that are critically involved in its interferon antagonism and RNA synthesis down-regulation.Expression of the Sendai (murine parainfluenza) virus C protein alleviates restriction of measles virus growth in mouse cells.Antagonism of innate immunity by paramyxovirus accessory proteins.Importance of the anti-interferon capacity of Sendai virus C protein for pathogenicity in mice.Novel Strategy to Control Transgene Expression Mediated by a Sendai Virus-Based Vector Using a Nonstructural C Protein and Endogenous MicroRNAs.Nonstructural Nipah virus C protein regulates both the early host proinflammatory response and viral virulence.Structural Basis of the Inhibition of STAT1 Activity by Sendai Virus C Protein.Human parainfluenza virus type 1 C proteins are nonessential proteins that inhibit the host interferon and apoptotic responses and are required for efficient replication in nonhuman primates.Sendai virus C protein plays a role in restricting PKR activation by limiting the generation of intracellular double-stranded RNA.Studies on the paramyxovirus accessory genes by reverse genetics in the Sendai virus-mouse system.The C proteins of human parainfluenza virus type 1 (HPIV1) control the transcription of a broad array of cellular genes that would otherwise respond to HPIV1 infectionN-terminally truncated C protein, CNDelta25, of human parainfluenza virus type 3 is a potent inhibitor of viral replication.A novel human parainfluenza virus type 1 (HPIV1) with separated P and C genes is useful for generating C gene mutants for evaluation as live-attenuated virus vaccine candidates.Sendai virus C proteins regulate viral genome and antigenome synthesis to dictate the negative genome polarity.Measles virus phosphoprotein gene products: conformational flexibility of the P/V protein amino-terminal domain and C protein infectivity factor functionSendai virus targets inflammatory responses, as well as the interferon-induced antiviral state, in a multifaceted manner.Viral protein requirements for assembly and release of human parainfluenza virus type 3 virus-like particles.Methyl-beta cyclodextrin alters the production and infectivity of Sendai virus.Longer and shorter forms of Sendai virus C proteins play different roles in modulating the cellular antiviral response.Identification of a mutation in editing of defective Newcastle disease virus recombinants that modulates P-gene mRNA editing and restores virus replication and pathogenicity in chicken embryos.Loss of Sendai virus C protein leads to accumulation of RIG-I immunostimulatory defective interfering RNA.Evidence for phosphorylation of human parainfluenza virus type 3 C protein: mutant C proteins exhibit variable inhibitory activities in vitro.Measles virus circumvents the host interferon response by different actions of the C and V proteins.Sendai virus C protein impairs both phosphorylation and dephosphorylation processes of Stat1.Intracellular processing of the Sendai virus C' protein leads to the generation of a Y protein module: structure-functional implications.
P2860
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P2860
Versatility of the accessory C proteins of Sendai virus: contribution to virus assembly as an additional role.
description
2000 nî lūn-bûn
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2000 թվականի հունիսին հրատարակված գիտական հոդված
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2000年の論文
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2000年論文
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2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
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2000年论文
@wuu
name
Versatility of the accessory C ...... ssembly as an additional role.
@ast
Versatility of the accessory C ...... ssembly as an additional role.
@en
type
label
Versatility of the accessory C ...... ssembly as an additional role.
@ast
Versatility of the accessory C ...... ssembly as an additional role.
@en
prefLabel
Versatility of the accessory C ...... ssembly as an additional role.
@ast
Versatility of the accessory C ...... ssembly as an additional role.
@en
P2093
P2860
P1433
P1476
Versatility of the accessory C ...... ssembly as an additional role.
@en
P2093
M Muranaka
R Yamaguchi
P2860
P304
P356
10.1128/JVI.74.12.5619-5628.2000
P577
2000-06-01T00:00:00Z