Interaction of influenza virus NS1 protein and the human homologue of Staufen in vivo and in vitro (Q24548910)

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R M Marión

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A Beloso

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J Ortín

Influenza virus NS1 protein inhibits pre-mRNA splicing and blocks mRNA nucleocytoplasmic transport

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language of work or name

English

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publication date

1 June 1999

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published in

Nucleic Acids Research

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volume

27

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issue

11

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page(s)

2241-7

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cites work

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7 January 2021

Binding of the influenza virus NS1 protein to double-stranded RNA inhibits the activation of the protein kinase that phosphorylates the elF-2 translation initiation factor

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Influenza A Virus Lacking the NS1 Gene Replicates in Interferon-Deficient Systems

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Amino acid replacements leading to temperature-sensitive defects of the NS1 protein of influenza A virus

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Cytoplasmic and nuclear virus-specific proteins in influenza virus-infected MDCK cells

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Expression of unspliced NS1 mRNA, spliced NS2 mRNA, and a spliced chimera mRNA from cloned influenza virus NS DNA in an SV40 vector

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Infectious influenza A and B virus variants with long carboxyl terminal deletions in the NS1 polypeptides

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SV40-transformed simian cells support the replication of early SV40 mutants

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staufen, a gene required to localize maternal RNAs in the Drosophila egg

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Nuclear transport of influenza virus polymerase PA protein.

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Diversity of coding strategies in influenza viruses

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Inscuteable and Staufen mediate asymmetric localization and segregation of prospero RNA during Drosophila neuroblast cell divisions.

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Extrinsic cues, intrinsic cues and microfilaments regulate asymmetric protein localization in Drosophila neuroblasts

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Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3'end formation of cellular pre-mRNAs

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Staufen-dependent localization of prospero mRNA contributes to neuroblast daughter-cell fate.

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Crystal structure of the unique RNA-binding domain of the influenza virus NS1 protein

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Segment 8 of the influenza virus genome is unique in coding for two polypeptides

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The smallest genome RNA segment of influenza virus contains two genes that may overlap

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Homozygous deletion of the alpha- and beta 1-interferon genes in human leukemia and derived cell lines

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Translational control by influenza virus. Identification of cis-acting sequences and trans-acting factors which may regulate selective viral mRNA translation

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Biochemical and genetic evidence for complex formation between the influenza A virus NS1 protein and the interferon-induced PKR protein kinase

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A primer vector system that allows temperature dependent gene amplification and expression in mammalian cells: regulation of the influenza virus NS1 gene expression

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The N-terminal half of the influenza virus NS1 protein is sufficient for nuclear retention of mRNA and enhancement of viral mRNA translation.

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Analysis of influenza A virus temperature-sensitive mutants with mutations in RNA segment 8.

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Binding of influenza A virus NS1 protein to dsRNA in vitro

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Influenza virus NS1 protein alters the subnuclear localization of cellular splicing components

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Influenza virus NS1 protein interacts with viral transcription-replication complexes in vivo

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Binding of the influenza virus NS1 protein to model genome RNAs

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The influenza virus NS1 protein is a poly(A)-binding protein that inhibits nuclear export of mRNAs containing poly(A)

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Influenza virus NS1 protein enhances the rate of translation initiation of viral mRNAs

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7 January 2021

A human sequence homologue of Staufen is an RNA-binding protein that is associated with polysomes and localizes to the rough endoplasmic reticulum

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7 January 2021

Mammalian staufen is a double-stranded-RNA- and tubulin-binding protein which localizes to the rough endoplasmic reticulum

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Use of a hybrid vaccinia virus-T7 RNA polymerase system for expression of target genes

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The mammalian staufen protein localizes to the somatodendritic domain of cultured hippocampal neurons: implications for its involvement in mRNA transport.

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7 January 2021

Identifiers

DOI

10.1093/NAR/27.11.2241

1 reference

1855380

1855380

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1 reference

1 reference