The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity (Q28295453)

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English	The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity	scientific article

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scholarly article

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The cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activity (English)

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molecular chaperones

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author name string

M W Melville

1

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S L Tan

2

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M Wambach

3

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J Song

4

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R I Morimoto

5

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M G Katze

6

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language of work or name

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publication date

5 February 1999

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Journal of Biological Chemistry

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274

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3797-803

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6

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Sindbis virus infection of neonatal mice results in a severe stress response

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Hsp90 is required for the activity of a hepatitis B virus reverse transcriptase

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Hepadnavirus assembly and reverse transcription require a multi-component chaperone complex which is incorporated into nucleocapsids

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Association of HSP70 with the adenovirus type 5 fiber protein in infected HEp-2 cells

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Heat-shock proteins as molecular chaperones

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The role of heat-shock proteins as molecular chaperones

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Molecular chaperones in cellular protein folding

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Chaperone functions of the heat shock proteins associated with steroid receptors

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Steroid receptor interactions with heat shock protein and immunophilin chaperones

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BAG-1 modulates the chaperone activity of Hsp70/Hsc70.

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Cdc37 is a molecular chaperone with specific functions in signal transduction

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Purification and partial characterization of a cellular inhibitor of the interferon-induced protein kinase of Mr 68,000 from influenza virus-infected cells

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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

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

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Enhancement of the interferon-induced double-stranded RNA-dependent protein kinase activity by Sindbis virus infection and heat-shock stress

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Inhibition of translational initiation by activators of the glucose-regulated stress protein and heat shock protein stress response systems. Role of the interferon-inducible double-stranded RNA-activated eukaryotic initiation factor 2alpha kinase

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Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticular calcium stores

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Calcium depletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis

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The molecular chaperone hsp40 regulates the activity of P58IPK, the cellular inhibitor of PKR.

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Regulation of interferon-induced protein kinase PKR: modulation of P58IPK inhibitory function by a novel protein, P52rIPK

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Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications

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Characterization of functional domains of the eukaryotic co-chaperone Hip

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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

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Expression and characterisation of the N-terminal fragment of the HsdS subunit of M.EcoR124I.

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Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle

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Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function

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Effect of yeast and human DnaJ homologs on clathrin uncoating by 70 kilodalton heat shock protein.

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Functional interaction of the auxilin J domain with the nucleotide- and substrate-binding modules of Hsc70.

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The T/t common exon of simian virus 40, JC, and BK polyomavirus T antigens can functionally replace the J-domain of the Escherichia coli DnaJ molecular chaperone

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Identifiers

10.1074/JBC.274.6.3797

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release_lrxj6xotjnckzodktnb2gmiamq

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