Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR. (Q34080544)

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Language	Label	Description	Also known as
English	Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR. (English)

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

author name string

Ung TL

1

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Cao C

2

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Lu J

3

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Ozato K

4

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Dever TE

5

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Europe PubMed Central

PubMed publication ID

30 July 2017

language of work or name

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publication date

1 July 2001

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

The EMBO Journal

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Europe PubMed Central

PubMed publication ID

30 July 2017

20

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

14

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

3728-3737

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

Pseudosubstrate inhibition of protein kinase PKR by swine pox virus C8L gene product

1 reference

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

1 reference

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Translation initiation: adept at adapting

1 reference

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Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls

1 reference

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Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18

1 reference

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1 reference

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Requirement of PKR dimerization mediated by specific hydrophobic residues for its activation by double-stranded RNA and its antigrowth effects in yeast

1 reference

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Identification and requirement of three ribosome binding domains in dsRNA-dependent protein kinase (PKR).

1 reference

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

1 reference

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Dimerization by translation initiation factor 2 kinase GCN2 is mediated by interactions in the C-terminal ribosome-binding region and the protein kinase domain

1 reference

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Disruption of cellular translational control by a viral truncated eukaryotic translation initiation factor 2alpha kinase homolog

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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

1 reference

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Interactions between LIM domains and the LIM domain-binding protein Ldb1

1 reference

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Effect of brain ischemia and reperfusion on the localization of phosphorylated eukaryotic initiation factor 2 alpha

1 reference

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Functional analysis of the nuclear LIM domain interactor NLI

1 reference

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Regulation of the protein kinase PKR by the vaccinia virus pseudosubstrate inhibitor K3L is dependent on residues conserved between the K3L protein and the PKR substrate eIF2alpha.

1 reference

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Activation of the Raf-1 kinase cascade by coumermycin-induced dimerization.

1 reference

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Interaction of the interferon-induced PKR protein kinase with inhibitory proteins P58IPK and vaccinia virus K3L is mediated by unique domains: implications for kinase regulation

1 reference

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1 reference

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Double-stranded (ds) RNA binding and not dimerization correlates with the activation of the dsRNA-dependent protein kinase (PKR).

1 reference

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1 reference

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1 reference

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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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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

https://pubmed.ncbi.nlm.nih.gov/11447114

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

A model for the double-stranded RNA (dsRNA)-dependent dimerization and activation of the dsRNA-activated protein kinase PKR.

1 reference

https://pubmed.ncbi.nlm.nih.gov/11447114

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Ribosome targeting of PKR is mediated by two double-stranded RNA-binding domains and facilitates in vivo phosphorylation of eukaryotic initiation factor-2

1 reference

https://pubmed.ncbi.nlm.nih.gov/11447114

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based on heuristic

inferred from PubMed ID database lookup

Inhibition of the double-stranded RNA-dependent protein kinase PKR by mammalian ribosomes

1 reference

https://pubmed.ncbi.nlm.nih.gov/11447114

12 December 2020

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inferred from PubMed ID database lookup

Identifiers

10.1093/EMBOJ/20.14.3728

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

30 July 2017

ResearchGate publication ID

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