(Q39780931)

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Loss of function of the influenza A virus NS1 protein promotes apoptosis but this is not due to a failure to activate phosphatidylinositol 3-kinase (PI3K).

scientific article published on 31 October 2009

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scholarly article

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Europe PubMed Central

14 September 2017

Loss of function of the influenza A virus NS1 protein promotes apoptosis but this is not due to a failure to activate phosphatidylinositol 3-kinase (PI3K). (English)

1 reference

Europe PubMed Central

14 September 2017

author name string

David Jackson

1

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Europe PubMed Central

14 September 2017

Marian J Killip

2

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Europe PubMed Central

14 September 2017

Caroline S Galloway

3

1 reference

Europe PubMed Central

14 September 2017

Rupert J Russell

4

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Europe PubMed Central

14 September 2017

Richard E Randall

5

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Europe PubMed Central

14 September 2017

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publication date

31 October 2009

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Europe PubMed Central

14 September 2017

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Europe PubMed Central

14 September 2017

396

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Europe PubMed Central

14 September 2017

1

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Europe PubMed Central

14 September 2017

94-105

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Europe PubMed Central

14 September 2017

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Host defense, viruses and apoptosis

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A novel influenza A virus mitochondrial protein that induces cell death.

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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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Specificity and mechanism of action of some commonly used protein kinase inhibitors

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Influenza A virus NS1 protein activates the PI3K/Akt pathway to mediate antiapoptotic signaling responses

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Programmed cell death (apoptosis) in human monocytes infected by influenza A virus

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

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Virus clearance through apoptosis-dependent phagocytosis of influenza A virus-infected cells by macrophages

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TRIM25 RING-finger E3 ubiquitin ligase is essential for RIG-I-mediated antiviral activity

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Influenza A virus NS1 targets the ubiquitin ligase TRIM25 to evade recognition by the host viral RNA sensor RIG-I

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The influenza A virus PB1-F2 protein targets the inner mitochondrial membrane via a predicted basic amphipathic helix that disrupts mitochondrial function

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NS1 protein of influenza A virus inhibits the function of intracytoplasmic pathogen sensor, RIG-I

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Influenza A virus NS1 protein binds p85beta and activates phosphatidylinositol-3-kinase signaling

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Binding of influenza A virus NS1 protein to the inter-SH2 domain of p85 suggests a novel mechanism for phosphoinositide 3-kinase activation

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7 January 2021

The multifunctional NS1 protein of influenza A viruses

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Opposite effects of wortmannin and 2-(4-morpholinyl)-8-phenyl-1(4H)-benzopyran-4-one hydrochloride on toll-like receptor-mediated nitric oxide production: negative regulation of nuclear factor-{kappa}B by phosphoinositide 3-kinase

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A novel function of eIF2alpha kinases as inducers of the phosphoinositide-3 kinase signaling pathway

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LY294002 inhibits LPS-induced NO production through a inhibition of NF-kappaB activation: independent mechanism of phosphatidylinositol 3-kinase

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7 January 2021

Multiple anti-interferon actions of the influenza A virus NS1 protein

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Physiological significance of apoptosis in animal virus infection

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LY303511 (2-piperazinyl-8-phenyl-4H-1-benzopyran-4-one) acts via phosphatidylinositol 3-kinase-independent pathways to inhibit cell proliferation via mammalian target of rapamycin (mTOR)- and non-mTOR-dependent mechanisms

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Influenza a virus polymerase is an integral component of the CPSF30-NS1A protein complex in infected cells

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AKT/PKB signaling: navigating downstream

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10.1016/J.VIROL.2009.10.004

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Europe PubMed Central

14 September 2017

release_xxosw4qzijg4blvb7zpikktd44

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14 September 2017

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