The ribonucleotide reductase R1 subunits of herpes simplex virus types 1 and 2 protect cells against TNFα- and FasL-induced apoptosis by interacting with caspase-8. (Q39627613)

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scientific article published on March 2011

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English	The ribonucleotide reductase R1 subunits of herpes simplex virus types 1 and 2 protect cells against TNFα- and FasL-induced apoptosis by interacting with caspase-8.	scientific article published on March 2011

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scholarly article

1 reference

Europe PubMed Central

13 September 2017

The ribonucleotide reductase R1 subunits of herpes simplex virus types 1 and 2 protect cells against TNFα- and FasL-induced apoptosis by interacting with caspase-8. (English)

1 reference

Europe PubMed Central

13 September 2017

Richard M Siegel

object named as

Richard M Siegel

5

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author name string

Florent Dufour

1

1 reference

Europe PubMed Central

13 September 2017

A Marie-Josée Sasseville

2

1 reference

Europe PubMed Central

13 September 2017

Stéphane Chabaud

3

1 reference

Europe PubMed Central

13 September 2017

Bernard Massie

4

1 reference

Europe PubMed Central

13 September 2017

Yves Langelier

6

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Europe PubMed Central

13 September 2017

publication date

1 March 2011

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Europe PubMed Central

13 September 2017

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Europe PubMed Central

13 September 2017

16

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Europe PubMed Central

13 September 2017

256-271

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Europe PubMed Central

13 September 2017

3

1 reference

Europe PubMed Central

13 September 2017

https://scigraph.springernature.com/pub.10.1007/s10495-010-0560-2

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1 reference

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Protective Role of Fas-FasL Signaling in Lethal Infection with Herpes Simplex Virus Type 2 in Mice

1 reference

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Robust expression of TNF-alpha, IL-1beta, RANTES, and IP-10 by human microglial cells during nonproductive infection with herpes simplex virus.

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Synergistic anti-herpes effect of TNF-alpha and IFN-gamma in human corneal epithelial cells compared with that in corneal fibroblasts

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Tumor necrosis factor-alpha and interleukin-1 beta play a critical role in the resistance against lethal herpes simplex virus encephalitis

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The R1 subunit of herpes simplex virus ribonucleotide reductase protects cells against apoptosis at, or upstream of, caspase-8 activation

1 reference

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Herpes simplex virus 1 precludes replenishment of the short-lived receptor of tumor necrosis factor alpha by virion host shutoff-dependent degradation of its mRNA.

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Death receptor signal transducers: nodes of coordination in immune signaling networks

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NF-kappaB inducers upregulate cFLIP, a cycloheximide-sensitive inhibitor of death receptor signaling

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Cellular FLICE-inhibitory protein splice variants inhibit different steps of caspase-8 activation at the CD95 death-inducing signaling complex

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Induction of TNF receptor I-mediated apoptosis via two sequential signaling complexes

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Fas-associated Death Domain Protein and Caspase-8 Are Not Recruited to the Tumor Necrosis Factor Receptor 1 Signaling Complex during Tumor Necrosis Factor-induced Apoptosis

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Death receptor-induced cell killing

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Tumor necrosis factor signaling.

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Life and death decisions: secondary complexes and lipid rafts in TNF receptor family signal transduction

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NF-kappaB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation

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Factor(s) present in herpes simplex virus type 1-infected cells can compensate for the loss of the large subunit of the viral ribonucleotide reductase: characterization of an ICP6 deletion mutant

1 reference

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The herpes simplex virus type 1 ribonucleotide reductase is a tight complex of the type alpha 2 beta 2 composed of 40K and 140K proteins, of which the latter shows multiple forms due to proteolysis

1 reference

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The herpes simplex virus type 2 R1 protein kinase (ICP10 PK) blocks apoptosis in hippocampal neurons, involving activation of the MEK/MAPK survival pathway

1 reference

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The unique N terminus of herpes simplex virus type 1 ribonucleotide reductase large subunit is phosphorylated by casein kinase 2, which may have a homologue in Escherichia coli

1 reference

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The R1 subunit of herpes simplex virus ribonucleotide reductase is a good substrate for host cell protein kinases but is not itself a protein kinase

1 reference

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Herpes simplex virus type 2 encodes a heat shock protein homologue with apoptosis regulatory functions

1 reference

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The R1 subunit of herpes simplex virus ribonucleotide reductase has chaperone-like activity similar to Hsp27.

1 reference

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Assembly of an active translation initiation factor complex by a viral protein

1 reference

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The ribonucleotide reductase domain of the R1 subunit of herpes simplex virus type 2 ribonucleotide reductase is essential for R1 antiapoptotic function

1 reference

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The Epstein-Barr virus (EBV) deubiquitinating enzyme BPLF1 reduces EBV ribonucleotide reductase activity.

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Death-effector filaments: novel cytoplasmic structures that recruit caspases and trigger apoptosis

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Two adjacent trimeric Fas ligands are required for Fas signaling and formation of a death-inducing signaling complex

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FLICE is predominantly expressed as two functionally active isoforms, caspase-8/a and caspase-8/b.

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HIV-1 protease processes procaspase 8 to cause mitochondrial release of cytochrome c, caspase cleavage and nuclear fragmentation

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Bcl-xL acts downstream of caspase-8 activation by the CD95 death-inducing signaling complex.

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Production of the R2 subunit of ribonucleotide reductase from herpes simplex virus with prokaryotic and eukaryotic expression systems: higher activity of R2 produced by eukaryotic cells related to higher iron-binding capacity

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ERK-1 MAP kinase prevents TNF-induced apoptosis through bad phosphorylation and inhibition of Bax translocation in HeLa Cells

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Intracellular internalization and signaling pathways triggered by the large subunit of HSV-2 ribonucleotide reductase (ICP10).

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The Fas-associated death domain protein/caspase-8/c-FLIP signaling pathway is involved in TNF-induced activation of ERK.

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Death effector domain-containing herpesvirus and poxvirus proteins inhibit both Fas- and TNFR1-induced apoptosis

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Activation of initiator caspases through a stable dimeric intermediate

1 reference

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Two mechanisms of caspase 9 processing in double-stranded RNA- and virus-triggered apoptosis.

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Fas- and tumor necrosis factor-induced apoptosis is inhibited by the poxvirus crmA gene product

1 reference

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Viral FLICE-inhibitory proteins (FLIPs) prevent apoptosis induced by death receptors

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The human papillomavirus 16 E6 protein binds to Fas-associated death domain and protects cells from Fas-triggered apoptosis.

1 reference

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21 January 2018

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10.1007/S10495-010-0560-2

1 reference

Europe PubMed Central

13 September 2017

1 reference

Europe PubMed Central

13 September 2017

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