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http://purl.uniprot.org/citations/15280488http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15280488http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15280488http://www.w3.org/2000/01/rdf-schema#comment"The Sendai virus C protein acts to dismantle the interferon-induced cellular antiviral state in an MG132-sensitive manner, in part by inducing STAT1 instability. This activity of C maps to the first 23 amino acids (C(1-23)) of the 204-amino-acid (aa)-long protein (C(1-204)). C(1-23) was found to act as an independent viral element that induces STAT1 instability, since this peptide fused to green fluorescent protein (C(1-23)/GFP) is at least as active as C(1-204) in this respect. This peptide also induces the degradation of C(1-23)/GFP and other proteins to which it is fused. Most of C(1-204), and particularly its amino-terminal half, is predicted to be structurally disordered. C(1-23) as a peptide was found to be disordered by circular dichroism, and the first 11 aa have a strong potential to form an amphipathic alpha-helix in low concentrations of trifluoroethanol, which is thought to mimic protein-protein interaction. The critical degradation-determining sequence of C(1-23) was mapped by mutation to eight residues near its N terminus: (4)FLKKILKL(11). All the large hydrophobic residues of (4)FLKKILKL(11), plus its ability to form an amphipathic alpha-helix, were found to be critical for STAT1 degradation. In contrast, C(1-23)/GFP self-degradation did not require (8)ILKL(11), nor the ability to form an alpha-helix throughout this region. Remarkably, C(1-23)/GFP also stimulated C(1-204) degradation, and this degradation in trans required the same peptide determinants as for STAT1. Our results suggest that C(1-204) coordinates its dual activities of regulating viral RNA synthesis and counteracting the host innate antiviral response by sensing both its own intracellular concentration and that of STAT1."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.org/dc/terms/identifier"doi:10.1128/jvi.78.16.8799-8811.2004"xsd:string
http://purl.uniprot.org/citations/15280488http://purl.org/dc/terms/identifier"doi:10.1128/jvi.78.16.8799-8811.2004"xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/author"Martin S."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/author"Martin S."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/author"Marq J.B."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/author"Marq J.B."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/author"Garcin D."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/author"Garcin D."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/author"Iseni F."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/author"Iseni F."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/author"Kolakofsky D."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/author"Kolakofsky D."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/name"J. Virol."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/pages"8799-8811"xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/pages"8799-8811"xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/title"A short peptide at the amino terminus of the Sendai virus C protein acts as an independent element that induces STAT1 instability."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/title"A short peptide at the amino terminus of the Sendai virus C protein acts as an independent element that induces STAT1 instability."xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/volume"78"xsd:string
http://purl.uniprot.org/citations/15280488http://purl.uniprot.org/core/volume"78"xsd:string
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