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 synthesis

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 synthesis

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http://www.wikidata.org/entity/Q34341904
The C proteins of human parainfluenza virus type 1 block IFN signaling by binding and retaining Stat1 in perinuclear aggregates at the late endosomeTrafficking of Sendai virus nucleocapsids is mediated by intracellular vesiclesConserved charged amino acids within Sendai virus C protein play multiple roles in the evasion of innate immune responsesPassage 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 genomeClustered basic amino acids of the small sendai virus C protein Y1 are critical to its RAN GTPase-mediated nuclear localization.Evolution and structural organization of the C proteins of paramyxovirinae.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.Structural Basis of the Inhibition of STAT1 Activity by Sendai Virus C Protein.Studies on the paramyxovirus accessory genes by reverse genetics in the Sendai virus-mouse system.N-terminally truncated C protein, CNDelta25, of human parainfluenza virus type 3 is a potent inhibitor of viral replication.Paramyxovirus evasion of innate immunity: Diverse strategies for common targets.The STAT2 activation process is a crucial target of Sendai virus C protein for the blockade of alpha interferon signalingThe matrix protein of measles virus regulates viral RNA synthesis and assembly by interacting with the nucleocapsid protein.
P2860

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 synthesis

Item
http://www.wikidata.org/entity/Q34341904
description
2002 nî lūn-bûn
@nan
2002 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
The amino-terminal half of Sen ...... regulating viral RNA synthesis
@ast
The amino-terminal half of Sen ...... regulating viral RNA synthesis
@en
The amino-terminal half of Sen ...... regulating viral RNA synthesis
@nl
type
label
The amino-terminal half of Sen ...... regulating viral RNA synthesis
@ast
The amino-terminal half of Sen ...... regulating viral RNA synthesis
@en
The amino-terminal half of Sen ...... regulating viral RNA synthesis
@nl
prefLabel
The amino-terminal half of Sen ...... regulating viral RNA synthesis
@ast
The amino-terminal half of Sen ...... regulating viral RNA synthesis
@en
The amino-terminal half of Sen ...... regulating viral RNA synthesis
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921
P932
P356
P1433
P1476
The amino-terminal half of Sen ...... regulating viral RNA synthesis
@en
P2093
P2860
P304
P31
P356
10.1128/JVI.76.14.7114-7124.2002
P407
P433
P478
P577
P698
P921
P932