Role of the amino-terminal residues of the interferon-induced protein kinase in its activation by double-stranded RNA and heparin.
about
Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKRPACT, a protein activator of the interferon-induced protein kinase, PKR.Antiviral actions of interferonsModular structure of PACT: distinct domains for binding and activating PKRDouble-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivoControl of PKR protein kinase by hepatitis C virus nonstructural 5A protein: molecular mechanisms of kinase regulation.Expression of hepatitis C virus proteins interferes with the antiviral action of interferon independently of PKR-mediated control of protein synthesisIn vitro activation of the interferon-induced, double-stranded RNA-dependent protein kinase PKR by RNA from the 3' untranslated regions of human alpha-tropomyosin.Requirement of PKR dimerization mediated by specific hydrophobic residues for its activation by double-stranded RNA and its antigrowth effects in yeastDouble-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18The interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo.Unactivated PKR exists in an open conformation capable of binding nucleotidesThe use of analytical sedimentation velocity to extract thermodynamic linkage.Heparin activates PKR by inducing dimerization.Mechanistic characterization of the 5'-triphosphate-dependent activation of PKR: lack of 5'-end nucleobase specificity, evidence for a distinct triphosphate binding site, and a critical role for the dsRBD.A mutant cell line defective in response to double-stranded RNA and in regulating basal expression of interferon-stimulated genes.Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation.Identification of the heparin-binding domains of the interferon-induced protein kinase, PKRInteraction of PKR with single-stranded RNAStructure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation.
P2860
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P2860
Role of the amino-terminal residues of the interferon-induced protein kinase in its activation by double-stranded RNA and heparin.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
Role of the amino-terminal res ...... uble-stranded RNA and heparin.
@en
type
label
Role of the amino-terminal res ...... uble-stranded RNA and heparin.
@en
prefLabel
Role of the amino-terminal res ...... uble-stranded RNA and heparin.
@en
P2093
P1476
Role of the amino-terminal res ...... uble-stranded RNA and heparin.
@en
P2093
P304
18593-18598
P407
P577
1994-07-01T00:00:00Z