The cellular 68,000-Mr protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection: implications for translational regulation.
about
Foot-and-mouth disease virus 3C protease induces cleavage of translation initiation factors eIF4A and eIF4G within infected cellsTranslational regulation by the interferon-induced double-stranded-RNA-activated 68-kDa protein kinaseInhibition of translation in cells infected with a poliovirus 2Apro mutant correlates with phosphorylation of the alpha subunit of eucaryotic initiation factor 2Inhibition of ribosome recruitment induces stress granule formation independently of eukaryotic initiation factor 2alpha phosphorylationPhosphorylation of HIV Tat by PKR increases interaction with TAR RNA and enhances transcriptionRegulation of mRNA Translation and Cellular Signaling by Hepatitis C Virus Nonstructural Protein NS5ATranslation of Sindbis virus mRNA: effects of sequences downstream of the initiating codonRNA-protein interactions in regulation of picornavirus RNA translationTranslation of viral mRNA without active eIF2: the case of picornavirusesProteinase 2Apro Is Essential for Enterovirus Replication in Type I Interferon-Treated CellsThe role of interferon antagonist, non-structural proteins in the pathogenesis and emergence of arboviruses.Rift Valley fever virus NSs protein promotes post-transcriptional downregulation of protein kinase PKR and inhibits eIF2alpha phosphorylation.In vitro activation of the interferon-induced, double-stranded RNA-dependent protein kinase PKR by RNA from the 3' untranslated regions of human alpha-tropomyosin.Purification and partial characterization of a cellular inhibitor of the interferon-induced protein kinase of Mr 68,000 from influenza virus-infected cells.Requirement of PKR dimerization mediated by specific hydrophobic residues for its activation by double-stranded RNA and its antigrowth effects in yeastAdenovirus inhibition of cellular protein synthesis is prevented by the drug 2-aminopurine.dsRNA Binding Domain of PKR Is Proteolytically Released by Enterovirus A71 to Facilitate Viral Replication.Double-stranded RNA-activated protein kinase (PKR) is negatively regulated by 60S ribosomal subunit protein L18Translational control of viral gene expression in eukaryotesThe interferon-inducible double-stranded RNA-activated protein kinase self-associates in vitro and in vivo.Antisense RNA: function and fate of duplex RNA in cells of higher eukaryotes.Cytopathogenesis and inhibition of host gene expression by RNA viruses.Translation without eIF2 promoted by poliovirus 2A protease.Tipping the balance: antagonism of PKR kinase and ADAR1 deaminase functions by virus gene products.Complementation of adenovirus virus-associated RNA I gene deletion by expression of a mutant eukaryotic translation initiation factor.Alphavirus minus-strand synthesis and persistence in mouse embryo fibroblasts derived from mice lacking RNase L and protein kinase R.Innate immune evasion mediated by the Ambystoma tigrinum virus eukaryotic translation initiation factor 2alpha homologue.Potential role of PKR in double-stranded RNA-induced macrophage activation.The role of Misshapen NCK-related kinase (MINK), a novel Ste20 family kinase, in the IRES-mediated protein translation of human enterovirus 71.The VP35 protein of Ebola virus inhibits the antiviral effect mediated by double-stranded RNA-dependent protein kinase PKR.Protein Kinase R Degradation Is Essential for Rift Valley Fever Virus Infection and Is Regulated by SKP1-CUL1-F-box (SCF)FBXW11-NSs E3 Ligase.Tumor suppressor function of the interferon-induced double-stranded RNA-activated protein kinase.Mutants of the RNA-dependent protein kinase (PKR) lacking double-stranded RNA binding domain I can act as transdominant inhibitors and induce malignant transformation.Degradation of the interferon-induced 68,000-M(r) protein kinase by poliovirus requires RNAModification of eukaryotic initiation factor 4F during infection by influenza virus.A poliovirus minireplicon containing an inactive 2A proteinase is expressed in vaccinia virus-infected cellsThe integrity of the stem structure of human immunodeficiency virus type 1 Tat-responsive sequence of RNA is required for interaction with the interferon-induced 68,000-Mr protein kinaseFunctional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free systemThe alpha subunit of eucaryotic initiation factor 2 is phosphorylated in mengovirus-infected mouse L cells.Activation of the translational suppressor 4E-BP1 following infection with encephalomyocarditis virus and poliovirus.
P2860
Q24524297-F1F18887-9134-4A05-873A-28228177D55AQ24562903-486BE6CF-78FA-4E77-9B8C-23E3A8F4115FQ24645301-D38002F7-AA06-4953-B0A8-D86DDAA1EA70Q24674083-B34B6358-3563-476C-B47B-54D0470C0C2DQ24806541-7DD16458-1AA4-4C1C-9391-5A679977C520Q27469918-4B770BB2-8C21-4CDA-9553-412432A8608AQ27486008-18B209E5-30BA-4811-87B3-97E60AE1B4C2Q27486105-3C56077F-5299-43C8-83E3-BCEF23BE2E16Q28479039-E65B8F77-7A55-44F2-A9B2-51BC8C5F3EE8Q29039070-9F72EB5C-20F5-4912-AD85-CBBB0352EFBEQ31034150-81FF7148-6120-42C4-AAAB-6AD0CBBEED54Q33406230-B39F2C9D-5E03-4044-BB12-D6D3F4795961Q33633828-F290101B-7A6B-4027-8F9B-9A61AE114C8CQ33743055-A5944F68-664D-4314-990B-98C0176A2A50Q33781640-3F1FB289-F9C3-4B7A-9D7D-3E55A010E7ECQ33792872-FAEF3A9E-E2CB-4EB9-8C5E-60E1D93ABD4EQ33843219-A6118C1D-1C34-4CB3-A2A2-E38ABA5D04C3Q33868563-3218869A-D7B6-49E2-8ECA-1330D97BC539Q33935121-C88AE380-A93C-4CD1-9437-144AA3FA24A0Q33965039-0E535307-791A-4367-BCE6-477456F9D283Q34010093-5A56C293-83D2-41E0-B16C-0182553B5A1FQ34010277-D81149BD-ABD4-4A51-945F-B5CAE3AAED8FQ34049312-376C613C-3835-4EB3-B529-051447277A9CQ34208420-A83D1FED-EF23-497A-BD87-CECEF84B3E54Q34322100-60B66C4D-2D15-4731-BF37-A37EB8918884Q34466906-A3447AF5-5BEE-4A4A-860B-7C417CEE3A63Q35076729-546DA665-4ED9-4412-BBCB-546F168D8D3CQ35115764-EC18E765-8D4D-40F6-801F-EC4592A6C502Q35154777-59B59B5C-BBF8-4331-89FE-B1FAAE2C764BQ35634367-A5DCC585-2EC5-4556-830E-775BF8DFDE40Q35912398-4379BE3B-E053-4814-84EF-FC07D86E2B49Q36039597-A34AF118-8603-443D-9326-1796945E641EQ36551384-ECD22EAB-1AF2-4D7D-9524-B4E35DC851BFQ36641030-1CC429C3-B050-4F4A-9485-918A10B3F019Q36646805-0FAB50E6-E846-4E79-A57E-C8CE5A6F3619Q36650966-4CF99C64-CB35-4B22-8A55-13DA41725C2AQ36679792-760EF3D1-7F6A-4E59-8C20-E1A83BB18668Q36747113-DF307B1E-AADE-4F55-87B9-1DDAF9F0EF70Q36783119-B2CF3C2D-54F1-46A6-A027-C6C3065DC3FEQ37592704-C98CBE3A-2E4D-42B8-BF02-5E2DC785C31B
P2860
The cellular 68,000-Mr protein kinase is highly autophosphorylated and activated yet significantly degraded during poliovirus infection: implications for translational regulation.
description
1989 nî lūn-bûn
@nan
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
1989年论文
@zh
1989年论文
@zh-cn
name
The cellular 68,000-Mr protein ...... for translational regulation.
@en
type
label
The cellular 68,000-Mr protein ...... for translational regulation.
@en
prefLabel
The cellular 68,000-Mr protein ...... for translational regulation.
@en
P2093
P2860
P1433
P1476
The cellular 68,000-Mr protein ...... s for translational regulation
@en
P2093
P2860
P304
P407
P577
1989-05-01T00:00:00Z