Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA. (Q40319046)

19 September 2017

Binding of the influenza A virus NS1 protein to PKR mediates the inhibition of its activation by either PACT or double-stranded RNA. (English)

1 reference

19 September 2017

Shoudong Li

1

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19 September 2017

Ji-Young Min

series ordinal

2

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19 September 2017

Robert M Krug

series ordinal

3

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19 September 2017

Ganes C Sen

series ordinal

4

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19 September 2017

language of work or name

English

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publication date

8 February 2006

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19 September 2017

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19 September 2017

349

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19 September 2017

13-21

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19 September 2017

1

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Influenza virus NS1 protein counteracts PKR-mediated inhibition of replication.

19 September 2017

1 reference

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A novel RNA-binding motif in influenza A virus non-structural protein 1

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Biophysical characterization of the complex between double-stranded RNA and the N-terminal domain of the NS1 protein from influenza A virus: evidence for a novel RNA-binding mode

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The double-stranded RNA-dependent protein kinase PKR: structure and function

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The N- and C-terminal domains of the NS1 protein of influenza B virus can independently inhibit IRF-3 and beta interferon promoter activation

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

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Identification of double-stranded RNA-binding domains in the interferon-induced double-stranded RNA-activated p68 kinase

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Molecular mechanisms of interferon resistance mediated by viral-directed inhibition of PKR, the interferon-induced protein kinase

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The protein kinase PKR is required for p38 MAPK activation and the innate immune response to bacterial endotoxin

7 January 2021

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Binding of influenza A virus NS1 protein to dsRNA in vitro

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The double stranded RNA-activated protein kinase induced by interferon: dsRNA-PK.

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RAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signaling

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Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system

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

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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

7 January 2021

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Mechanism of interferon action: identification of a RNA binding domain within the N-terminal region of the human RNA-dependent P1/eIF-2 alpha protein kinase

7 January 2021

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The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR.

7 January 2021

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Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon

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A dynamically tuned double-stranded RNA binding mechanism for the activation of antiviral kinase PKR.

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Cellular antiviral responses against influenza A virus are countered at the posttranscriptional level by the viral NS1A protein via its binding to a cellular protein required for the 3' end processing of cellular pre-mRNAS

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PACT, a protein activator of the interferon-induced protein kinase, PKR.

7 January 2021

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PACT, a stress-modulated cellular activator of interferon-induced double-stranded RNA-activated protein kinase, PKR.

7 January 2021

1 reference

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Modular structure of PACT: distinct domains for binding and activating PKR

7 January 2021

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Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein

7 January 2021

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Influenza a virus M2 ion channel activity is essential for efficient replication in tissue culture

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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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Double-stranded RNA-independent dimerization of interferon-induced protein kinase PKR and inhibition of dimerization by the cellular P58IPK inhibitor

7 January 2021

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RNA binding by the novel helical domain of the influenza virus NS1 protein requires its dimer structure and a small number of specific basic amino acids

7 January 2021

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PKR; a sentinel kinase for cellular stress

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C114 is a novel IL-11-inducible nuclear double-stranded RNA-binding protein that inhibits protein kinase R

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

7 January 2021

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Mutant influenza viruses with a defective NS1 protein cannot block the activation of PKR in infected cells

7 January 2021

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https://api.crossref.org/works/10.1016%2FJ.VIROL.2006.01.005

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/J.VIROL.2006.01.005

1 reference

19 September 2017

1 reference