Inhibitory sequences in the N-terminus of the double-stranded-RNA-dependent protein kinase, PKR, are important for regulating phosphorylation of eukaryotic initiation factor 2alpha (eIF2alpha). (Q43677683)

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scientific article published in February 2001

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English	Inhibitory sequences in the N-terminus of the double-stranded-RNA-dependent protein kinase, PKR, are important for regulating phosphorylation of eukaryotic initiation factor 2alpha (eIF2alpha).	scientific article published in February 2001

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

Inhibitory sequences in the N-terminus of the double-stranded-RNA-dependent protein kinase, PKR, are important for regulating phosphorylation of eukaryotic initiation factor 2alpha (eIF2alpha). (English)

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

phosphorylation

1 reference

based on heuristic

inferred from title

author name string

K M Vattem

1

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Europe PubMed Central

PubMed publication ID

25 November 2017

K A Staschke

2

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

S Zhu

3

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

R C Wek

4

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

language of work or name

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publication date

1 February 2001

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Europe PubMed Central

PubMed publication ID

25 November 2017

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

268

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Europe PubMed Central

PubMed publication ID

25 November 2017

4

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

1143-1153

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

PKR: a new name and new roles.

1 reference

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eIF-2 kinases: regulators of general and gene-specific translation initiation

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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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PKR; a sentinel kinase for cellular stress

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Double-stranded RNA-activated protein kinase mediates virus-induced apoptosis: a new role for an old actor

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

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

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Molecular mechanisms responsible for malignant transformation by regulatory and catalytic domain variants of the interferon-induced enzyme RNA-dependent protein kinase

1 reference

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

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Expression of a PKR dominant-negative mutant in myogenic cells interferes with the myogenic process

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Regulatable expression of the interferon-induced double-stranded RNA dependent protein kinase PKR induces apoptosis and fas receptor expression

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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

1 reference

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

1 reference

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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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Mechanism of interferon action motif I of the interferon-induced, RNA-dependent protein kinase (PKR) is sufficient to mediate RNA-binding activity

1 reference

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21 January 2018

Mutational analysis of the double-stranded RNA (dsRNA) binding domain of the dsRNA-activated protein kinase, PKR.

1 reference

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21 January 2018

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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21 January 2018

A conserved double-stranded RNA-binding domain

1 reference

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21 January 2018

Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.01979.X

21 January 2018

Molecular basis of double-stranded RNA-protein interactions: structure of a dsRNA-binding domain complexed with dsRNA.

1 reference

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21 January 2018

RNA recognition by a Staufen double-stranded RNA-binding domain

1 reference

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21 January 2018

Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivo

1 reference

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21 January 2018

The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo

1 reference

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21 January 2018

Specific mutations near the amino terminus of double-stranded RNA-dependent protein kinase (PKR) differentially affect its double-stranded RNA binding and dimerization properties

1 reference

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21 January 2018

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

1 reference

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21 January 2018

Autophosphorylation sites participate in the activation of the double-stranded-RNA-activated protein kinase PKR

1 reference

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.01979.X

21 January 2018

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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21 January 2018

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

1 reference

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21 January 2018

Proteins that interact with PKR.

1 reference

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

1 reference

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Homologous segments in three subunits of the guanine nucleotide exchange factor eIF2B mediate translational regulation by phosphorylation of eIF2.

1 reference

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Precise gene fusion by PCR.

1 reference

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Purification and activation of the double-stranded RNA-dependent eIF-2 kinase DAI

1 reference

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Glucose limitation induces GCN4 translation by activation of Gcn2 protein kinase

1 reference

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

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Structural requirements for double-stranded RNA binding, dimerization, and activation of the human eIF-2 alpha kinase DAI in Saccharomyces cerevisiae

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Identification and characterization of pancreatic eukaryotic initiation factor 2 alpha-subunit kinase, PEK, involved in translational control

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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

1 reference

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Mechanism of interferon action: autoregulation of RNA-dependent P1/eIF-2 alpha protein kinase (PKR) expression in transfected mammalian cells

1 reference

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Translational regulation by the interferon-induced double-stranded-RNA-activated 68-kDa protein kinase

1 reference

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

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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

https://api.crossref.org/works/10.1046%2FJ.1432-1327.2001.01979.X

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Regulation of protein synthesis by heme-regulated eIF-2 alpha kinase

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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21 January 2018

Identifiers

10.1046/J.1432-1327.2001.01979.X

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

25 November 2017

ResearchGate publication ID

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