Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: role of complex formation and the E3 N-terminal domain.
about
Orthopoxvirus genes that mediate disease virulence and host tropismA new double-stranded RNA-binding protein that interacts with PKRADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editingA mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alphaImpact of protein kinase PKR in cell biology: from antiviral to antiproliferative actionA role for Z-DNA binding in vaccinia virus pathogenesisHuman Cytomegalovirus Strategies to Maintain and Promote mRNA TranslationCoronavirus gene 7 counteracts host defenses and modulates virus virulenceRegulation of mRNA Translation and Cellular Signaling by Hepatitis C Virus Nonstructural Protein NS5ADissection of Double-Stranded RNA Binding Protein B2 from BetanodavirusOverexpression of eukaryotic translation elongation factor 3 impairs Gcn2 protein activation.IRF3 and IRF7 phosphorylation in virus-infected cells does not require double-stranded RNA-dependent protein kinase R or Ikappa B kinase but is blocked by Vaccinia virus E3L proteinNuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinaseReplication of modified vaccinia virus Ankara in primary chicken embryo fibroblasts requires expression of the interferon resistance gene E3L.Double-stranded RNA-activated protein kinase PKR of fishes and amphibians: varying the number of double-stranded RNA binding domains and lineage-specific duplications.Vaccinia virus E3 protein prevents the antiviral action of ISG15Human Herpesvirus 6A Exhibits Restrictive Propagation with Limited Activation of the Protein Kinase R-eIF2α Stress Pathway.Diversity in viral anti-PKR mechanisms: a remarkable case of evolutionary convergenceInhibition of PKR activation by the proline-rich RNA binding domain of the herpes simplex virus type 1 Us11 protein.Both carboxy- and amino-terminal domains of the vaccinia virus interferon resistance gene, E3L, are required for pathogenesis in a mouse model.Characterization of a ranavirus inhibitor of the antiviral protein kinase PKRBiological function of the vaccinia virus Z-DNA-binding protein E3L: gene transactivation and antiapoptotic activity in HeLa cells.Heterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.Tipping the balance: antagonism of PKR kinase and ADAR1 deaminase functions by virus gene products.Molecular mechanisms of viral inhibitors of RIG-I-like receptors.Blockade of interferon induction and action by the E3L double-stranded RNA binding proteins of vaccinia virus.PACT and PKR: turning on NF-kappa B in the absence of virus.Recombinant modified vaccinia virus Ankara generating excess early double-stranded RNA transiently activates protein kinase R and triggers enhanced innate immune responses.Development of resistance to RNAi in mammalian cellsEbola virus VP35 protein binds double-stranded RNA and inhibits alpha/beta interferon production induced by RIG-I signaling.Myxoma virus protein M029 is a dual function immunomodulator that inhibits PKR and also conscripts RHA/DHX9 to promote expanded host tropism and viral replicationResistance of mRNA translation to acute endoplasmic reticulum stress-inducing agents in herpes simplex virus type 1-infected cells requires multiple virus-encoded functions.Viruses and the type I interferon antiviral system: induction and evasion.Innate immune evasion mediated by the Ambystoma tigrinum virus eukaryotic translation initiation factor 2alpha homologue.Vaccinia virus infection attenuates innate immune responses and antigen presentation by epidermal dendritic cells.Rapid evolution of protein kinase PKR alters sensitivity to viral inhibitors.An ADAR that edits transcripts encoding ion channel subunits functions as a dimer.RNA binding by a novel helical fold of b2 protein from wuhan nodavirus mediates the suppression of RNA interference and promotes b2 dimerization.The Ebola virus VP35 protein functions as a type I IFN antagonist.Functional analysis of the short isoform of orf virus protein OV20.0.
P2860
Q21285044-A0645C02-B993-4FBE-96FD-03B7456602C3Q24524116-D9E8843E-8F11-448C-8362-8C43A7A4A6C9Q24529861-F297C797-FEAD-4EB3-B25D-735F3D96EFCDQ24548092-E46DC2FF-8E9A-4AAA-AD68-D17C2A802B53Q24672548-A6A13434-28EC-443E-AE3B-B9490B320798Q24680885-C611FA5E-BA84-49B7-8646-79D71CF97A06Q26752742-4FEE682F-FC67-48F4-AC03-58FF829CA7AEQ27349527-A5F5A808-66B6-423A-B15A-0B27D5254BAAQ27469918-C908B79C-B2D8-430E-B97C-C5BD30FF78E0Q27480363-BEFC8836-0415-463F-9DA6-E887ED7F7644Q27940223-67797FB7-27C9-49CC-B6F4-76E70F3AAC2CQ28140837-37E22DBF-DCE2-4F41-9C33-F75B18ADFB96Q28204764-9EE7DEA3-A917-46DB-BDEA-94EDB1EB9B97Q33187731-86CE1D04-7CCB-4171-A42A-18487016F1B5Q33321981-3DA12B01-F32F-4D55-90B7-E2C292C2B7E5Q33349449-E5D79077-9C34-441B-8D6B-82698B0D0F81Q33564101-491D5449-B8A3-48EB-82C2-41CE06F79873Q33818201-9B16B8ED-3D2A-47C1-BA5B-4594CA86D41BQ33827148-4C0BCDE6-2A77-43D8-933F-2838781FB64DQ33835582-4A524327-58F7-4762-87E3-A99F7EA1E565Q33850280-78F34FBC-C089-4450-BE0C-D10EBB733368Q33943965-07DFD24A-B6DD-422A-A752-AD2E1D8A5955Q34080544-493FFAB9-E273-4C1C-8728-58372C92943EQ34208420-762A01B7-E8BB-4683-9E80-7D0DDE1BC5B7Q34253570-8D07E5CC-BAB8-4617-8A24-2FC9B1145CE2Q34337534-C7E48AA2-C36B-4CCE-801F-AE93042645BBQ34467902-D5647839-71DC-493D-9FEE-008BE21F7851Q34594898-4D91791B-3585-4352-A991-AFFE2ED2E672Q34619725-7D861B90-C9B4-473A-BFB0-D03F76F093FAQ34648134-916BD8F0-8A28-4C1C-8E20-05BD695DB6F8Q34819569-90176EBE-1965-459E-95D2-6409015B0E30Q35023672-8E662817-957D-40D7-A131-A5D2C9BC0C57Q35027514-A68DF221-E50C-42CA-B5D9-5BD3A651BC38Q35076729-E3EC6441-BC4A-41FF-9749-9DE00EE0F373Q35101495-334932C7-9552-4BD7-B6E4-3AB0E5688AB2Q35125960-767AFBA1-9F20-421E-8107-F1985D206124Q35160599-0DB8FC35-0C52-4759-8435-852B8E28DEE3Q35192679-0DFF1E97-F58D-47AB-BEBA-48AFAD17CC5EQ35422223-A2C96765-3104-4E5F-BBE6-B585C5F30B1EQ35488710-4599EC91-B968-4B07-B497-E77C35BB4941
P2860
Inhibition of double-stranded RNA-dependent protein kinase PKR by vaccinia virus E3: role of complex formation and the E3 N-terminal domain.
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Inhibition of double-stranded ...... and the E3 N-terminal domain.
@ast
Inhibition of double-stranded ...... and the E3 N-terminal domain.
@en
type
label
Inhibition of double-stranded ...... and the E3 N-terminal domain.
@ast
Inhibition of double-stranded ...... and the E3 N-terminal domain.
@en
prefLabel
Inhibition of double-stranded ...... and the E3 N-terminal domain.
@ast
Inhibition of double-stranded ...... and the E3 N-terminal domain.
@en
P2093
P2860
P356
P1476
Inhibition of double-stranded ...... and the E3 N-terminal domain.
@en
P2093
A G Hinnebusch
M T Garcia-Barrio
P R Romano
P2860
P304
P356
10.1128/MCB.18.12.7304
P407
P577
1998-12-01T00:00:00Z