(Q42829686)

English

Activation of the I kappa B alpha kinase (IKK) complex by double-stranded RNA-binding defective and catalytic inactive mutants of the interferon-inducible protein kinase PKR.

scientific article published on April 2001

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

Activation of the I kappa B alpha kinase (IKK) complex by double-stranded RNA-binding defective and catalytic inactive mutants of the interferon-inducible protein kinase PKR. (English)

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

author name string

T Ishii

1

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

H Kwon

2

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

J Hiscott

3

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

G Mosialos

4

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

A E Koromilas

5

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

language of work or name

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publication date

1 April 2001

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Europe PubMed Central

PubMed publication ID

8 November 2017

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

20

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

15

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

1900-1912

1 reference

Europe PubMed Central

PubMed publication ID

8 November 2017

Activation of the dsRNA-dependent protein kinase, PKR, induces apoptosis through FADD-mediated death signaling

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Essential role for the dsRNA-dependent protein kinase PKR in innate immunity to viral infection

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The NF-kappa B and I kappa B proteins: new discoveries and insights

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Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation

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PKR stimulates NF-kappaB irrespective of its kinase function by interacting with the IkappaB kinase complex.

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Distinct roles for the NF-kappaB1 (p50) and c-Rel transcription factors in inflammatory arthritis

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JNK2 and IKKbeta are required for activating the innate response to viral infection

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

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Double-stranded-RNA-activated protein kinase PKR enhances transcriptional activation by tumor suppressor p53

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The double-stranded RNA activated protein kinase PKR physically associates with the tumor suppressor p53 protein and phosphorylates human p53 on serine 392 in vitro

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A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis

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JNK1: a protein kinase stimulated by UV light and Ha-Ras that binds and phosphorylates the c-Jun activation domain

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Phosphorylation of initiation factor 2 alpha by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast

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Mammalian eukaryotic initiation factor 2 alpha kinases functionally substitute for GCN2 protein kinase in the GCN4 translational control mechanism of yeast

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A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB

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Induction of apoptosis by double-stranded-RNA-dependent protein kinase (PKR) involves the alpha subunit of eukaryotic translation initiation factor 2 and NF-kappaB.

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Activation of NF-kappa B by the dsRNA-dependent protein kinase, PKR involves the I kappa B kinase complex.

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Translational control in mammalian cells

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TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways

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JNK or IKK, AP-1 or NF-kappaB, which are the targets for MEK kinase 1 action?

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Regulation of the interferon-induced PKR: can viruses cope?

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The death domain kinase RIP mediates the TNF-induced NF-kappaB signal

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Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase

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Double-stranded RNA-dependent protein kinase activates transcription factor NF-kappa B by phosphorylating I kappa B.

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The stress-activated protein kinase subfamily of c-Jun kinases

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Selective inhibition of l kappaB alpha phosphorylation and HIV-1 LTR-directed gene expression by novel antioxidant compounds

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Rel/NF-kappa B and I kappa B factors in oncogenesis

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IKK-1 and IKK-2: cytokine-activated IkappaB kinases essential for NF-kappaB activation

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Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase

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Tumor necrosis factor alpha-induced phosphorylation of I kappa B alpha is a signal for its degradation but not dissociation from NF-kappa B

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pEF-BOS, a powerful mammalian expression vector

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Advanced mammalian gene transfer: high titre retroviral vectors with multiple drug selection markers and a complementary helper-free packaging cell line

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The role of Rel/NF-kappa B proteins in viral oncogenesis and the regulation of viral transcription

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A cis-acting element in the 3'-untranslated region of human TNF-alpha mRNA renders splicing dependent on the activation of protein kinase PKR.

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Tumor necrosis factor alpha-induced activation of c-jun N-terminal kinase is mediated by TRAF2.

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Autophosphorylation in the activation loop is required for full kinase activity in vivo of human and yeast eukaryotic initiation factor 2alpha kinases PKR and GCN2

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IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase

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The vaccinia virus E3L gene product interacts with both the regulatory and the substrate binding regions of PKR: implications for PKR autoregulation

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Phosphorylation of protein-tyrosine phosphatase PTP-1B on identical sites suggests activation of a common signaling pathway during mitosis and stress response in mammalian cells

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Phosphorylation of eukaryotic translation initiation factor 2 mediates apoptosis in response to activation of the double-stranded RNA-dependent protein kinase

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Transformation of NIH 3T3 cells by microinjection of Ha-ras p21 protein

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How cells respond to interferons

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10.1038/SJ.ONC.1204267

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Europe PubMed Central

PubMed publication ID

8 November 2017

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https://api.fatcat.wiki/v0/release/ekiehnqzqrfwtmg4sab5wosd3a

24 November 2022

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Europe PubMed Central

PubMed publication ID

8 November 2017

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