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 (Q36561302)

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scientific article published on August 1996

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English	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	scientific article published on August 1996

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scholarly article

1 reference

Europe PubMed Central

14 August 2017

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 (English)

1 reference

Europe PubMed Central

14 August 2017

object named as

vaccinia virus

1 reference

based on heuristic

inferred from title

author name string

M Gale

1

1 reference

Europe PubMed Central

14 August 2017

S L Tan

2

1 reference

Europe PubMed Central

14 August 2017

M Wambach

3

1 reference

Europe PubMed Central

14 August 2017

M G Katze

4

1 reference

Europe PubMed Central

14 August 2017

language of work or name

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publication date

1 August 1996

1 reference

Europe PubMed Central

14 August 2017

Molecular and Cellular Biology

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Europe PubMed Central

14 August 2017

16

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Europe PubMed Central

14 August 2017

4172-4181

1 reference

Europe PubMed Central

14 August 2017

8

1 reference

Europe PubMed Central

14 August 2017

Cloning, expression, and cellular localization of the oncogenic 58-kDa inhibitor of the RNA-activated human and mouse protein kinase

1 reference

https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=231414

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The P58 cellular inhibitor complexes with the interferon-induced, double-stranded RNA-dependent protein kinase, PKR, to regulate its autophosphorylation and activity

1 reference

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Use of the two-hybrid system to identify the domain of p53 involved in oligomerization

1 reference

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A template for the protein kinase family

1 reference

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Regulation of eukaryotic protein synthesis by initiation factors.

1 reference

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Identification of mutations in p53 that affect its binding to SV40 large T antigen by using the yeast two-hybrid system

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Eukaryotic DnaJ homologs and the specificity of Hsp70 activity

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The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases

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Recombinant vaccinia virus K3L gene product prevents activation of double-stranded RNA-dependent, initiation factor 2 alpha-specific protein kinase

1 reference

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The glycine-rich sequence of protein kinases: a multifunctional element

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Mechanism of interferon action: evidence for intermolecular autophosphorylation and autoactivation of the interferon-induced, RNA-dependent protein kinase PKR

1 reference

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

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Tetratrico peptide repeat interactions: to TPR or not to TPR?

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Protein kinases--structure and function.

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Both p16 and p21 families of cyclin-dependent kinase (CDK) inhibitors block the phosphorylation of cyclin-dependent kinases by the CDK-activating kinase

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

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Correlation of two-hybrid affinity data with in vitro measurements

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

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

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The 58-kilodalton inhibitor of the interferon-induced double-stranded RNA-activated protein kinase is a tetratricopeptide repeat protein with oncogenic properties

1 reference

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The 58,000-dalton cellular inhibitor of the interferon-induced double-stranded RNA-activated protein kinase (PKR) is a member of the tetratricopeptide repeat family of proteins

1 reference

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HIV-1 Tat directly interacts with the interferon-induced, double-stranded RNA-dependent kinase, PKR

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Adenovirus VAI RNA complexes with the 68 000 Mr protein kinase to regulate its autophosphorylation and activity

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Influenza virus regulates protein synthesis during infection by repressing autophosphorylation and activity of the cellular 68,000-Mr protein kinase

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The protein kinase family: conserved features and deduced phylogeny of the catalytic domains

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Identifiers

10.1128/MCB.16.8.4172

1 reference

Europe PubMed Central

14 August 2017

1 reference

Europe PubMed Central

14 August 2017

1 reference

Europe PubMed Central

14 August 2017

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