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Literature summary for 2.7.7.48 extracted from

  • Ciancanelli, M.J.; Volchkova, V.A.; Shaw, M.L.; Volchkov, V.E.; Basler, C.F.
    Nipah virus sequesters inactive STAT1 in the nucleus via a P gene-encoded mechanism (2009), J. Virol., 83, 7828-7841.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
phosphoprotein P P is essential for RNA-dependent RNA polymerase function as cofactor. The amino terminus of P is essential for its function in a minireplicon assay. It binds to STAT1 and inhibits interferon-induced Tyr phosphorylation of STAT1, which is not required for P polymerase cofactor function, since mutations in the STAT1 binding motif of P, e.g. G121E, do not affect RNA polymerase function, but abrogate STAT1 inhibition, overview. The gene for NiV P encodes functions that sequester inactive STAT1 in the nucleus, preventing its activation and suggest that the W protein is the dominant inhibitor of STAT1 in NiV-infected cells Nipah henipavirus

Organism

Organism UniProt Comment Textmining
Nipah henipavirus
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NiV
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Synonyms

Synonyms Comment Organism
RNA-dependent RNA polymerase
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Nipah henipavirus