A dynamically tuned double-stranded RNA binding mechanism for the activation of antiviral kinase PKR.
about
Dimerization and release of molecular chaperone inhibition facilitate activation of eukaryotic initiation factor-2 kinase in response to endoplasmic reticulum stressInteraction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKRThe RNA-binding region of human TRBP interacts with microRNA precursors through two independent domainsTRAF family proteins link PKR with NF-kappa B activationThe C-terminal, third conserved motif of the protein activator PACT plays an essential role in the activation of double-stranded-RNA-dependent protein kinase (PKR)The Hsp90 chaperone complex is both a facilitator and a repressor of the dsRNA-dependent kinase PKRTyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase.Molecular basis for PKR activation by PACT or dsRNAProtein kinase PKR and RNA adenosine deaminase ADAR1: new roles for old players as modulators of the interferon responsePKR-dependent mechanisms of gene expression from a subgenomic hepatitis C virus clone.Interferon-inducible antiviral effectorsRibosome-associated factor Y adopts a fold resembling a double-stranded RNA binding domain scaffoldCrystal Structure of the Avian Reovirus Inner Capsid Protein AThe structure of the PERK kinase domain suggests the mechanism for its activationIntrinsic Dynamics of an Extended Hydrophobic Core in the S. cerevisiae RNase III dsRBD Contributes to Recognition of Specific RNA Binding SitesMinihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3Translation inhibition in apoptosis: caspase-dependent PKR activation and eIF2-alpha phosphorylationRNA-binding proteins: modular design for efficient functionDimerization of ADAR2 is mediated by the double-stranded RNA binding domainC114 is a novel IL-11-inducible nuclear double-stranded RNA-binding protein that inhibits protein kinase RActivation of the protein kinase PKR by short double-stranded RNAs with single-stranded tails.Double-stranded RNA-activated protein kinase PKR of fishes and amphibians: varying the number of double-stranded RNA binding domains and lineage-specific duplications.Andes virus nucleocapsid protein interrupts protein kinase R dimerization to counteract host interference in viral protein synthesis.The binding site of the RNA-dependent protein kinase (PKR) on EBER1 RNA from Epstein-Barr virus.dsRNA Binding Domain of PKR Is Proteolytically Released by Enterovirus A71 to Facilitate Viral Replication.Characterization of a ranavirus inhibitor of the antiviral protein kinase PKRUnactivated PKR exists in an open conformation capable of binding nucleotidesHeterologous dimerization domains functionally substitute for the double-stranded RNA binding domains of the kinase PKR.Evidence for auto-inhibition by the N terminus of hADAR2 and activation by dsRNA binding.The role of human Dicer-dsRBD in processing small regulatory RNAsMolecular mechanism by which palmitate inhibits PKR autophosphorylation.Features of double-stranded RNA-binding domains of RNA helicase A are necessary for selective recognition and translation of complex mRNAsControlling activation of the RNA-dependent protein kinase by siRNAs using site-specific chemical modificationWest Nile virus infection does not induce PKR activation in rodent cells.IFIT1 Differentially Interferes with Translation and Replication of Alphavirus Genomes and Promotes Induction of Type I InterferonDuplex RNA-binding enzymes: headliners from neurobiology, virology, and development.Altered activation of protein kinase PKR and enhanced apoptosis in dystonia cells carrying a mutation in PKR activator protein PACT.Specificity of the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR for double-stranded RNA: insights from thermodynamics and small-angle X-ray scattering.Activation of PKR: an open and shut case?Functional domains and the antiviral effect of the double-stranded RNA-dependent protein kinase PKR from Paralichthys olivaceus.
P2860
Q24292499-5422A7ED-D72D-4843-9FB8-C8011AC37145Q24304341-78566AFA-7B0E-468F-8FB5-5B545352588DQ24320118-BDC7C5BC-AD6B-4E82-BA2B-96C0EA45AF8AQ24338458-8D4572EE-1545-4C94-BEED-35B95558069BQ24534342-5C320B8E-4AD2-4E64-BEC8-31BD01711690Q24535594-B98A64DF-6B3E-4B39-AAA0-5E0FCAE36ACDQ24535918-62618424-93C1-4A24-9C2D-D39AC456618AQ24550949-A1B7EA67-55EF-46AE-A73F-89345EED17CEQ27001020-A9A2B9D5-B124-4EAD-B421-D378EA8F918DQ27472907-0F403B82-D893-4AE2-B0E4-3FFA6F470D6DQ27486790-483633AC-C348-4613-84A1-AF54F75A4F79Q27639870-F9589C8D-48D2-45B1-BB08-2340F077B77EQ27652209-0F07C576-3027-44FB-B396-0207A0ECBBB5Q27667715-81067026-45C6-49A2-B3FF-29B619BF031BQ27675338-E4D85FEF-857D-4D36-A697-C1C21EA62BBFQ28211625-0566AAA6-0C24-4AF8-B640-A89745DB78CFQ28216131-905F33E1-2C2D-4066-9B76-27B7D8A68C34Q28300258-47283A58-F24F-47D1-846F-58D5EC6703EDQ28572537-987068D2-A75A-40F6-914A-F640E5F94FFDQ28587381-E0DE9B7F-6C2B-43AF-9FEB-2C4D5AD49C24Q31128979-11852365-672E-46FE-85B2-5DA7477E51B4Q33321981-B5039912-8B71-4FEE-A1CB-4B63DA44586DQ33359465-51714D08-D162-42C1-8CD2-FF7D4899D192Q33758060-30D96069-00C1-4EB5-8C08-D78CF0FF76EBQ33843219-BBE246AD-0FF0-4EA3-92D8-5F9F9175C8F8Q33850280-4977C96C-FB78-47D3-8A1E-F169F4E46BFEQ34034965-5270C259-0143-4FAE-98FD-1413F71E1272Q34080544-9E63D862-0826-49C9-B426-E060C86DFB51Q34366056-871F4628-8982-4320-AAB5-7E6E84CB1EA7Q34525711-6E51B45F-B6E3-474F-97A8-9CBAA9FC6E41Q34561217-DE01F0AC-DCDB-42E7-9CAA-3E90BC4281C8Q34568434-0B71401B-2FB6-4151-BB43-BEF89BE1F412Q35127967-F90C0CA1-BF6C-4702-A904-4090AF92BF6CQ35528928-64D7B08D-FEEF-4146-8D91-E84869CE9B83Q35557650-AC735D47-B69F-4A80-96C3-3190BC7D9779Q36006780-D168423D-3747-4174-A824-40A00A2B740AQ36049945-1A1E5A84-5827-44ED-81C9-63EB4EBA55C4Q36526187-AA272885-5087-454C-839D-479048DBB3AFQ36695833-7232B6A7-A429-43C4-B37D-A6E743BCE640Q36747691-3313909D-9D8D-45C6-9DD4-E964595DBC2C
P2860
A dynamically tuned double-stranded RNA binding mechanism for the activation of antiviral kinase PKR.
description
2000 nî lūn-bûn
@nan
2000年の論文
@ja
2000年学术文章
@wuu
2000年学术文章
@zh-cn
2000年学术文章
@zh-hans
2000年学术文章
@zh-my
2000年学术文章
@zh-sg
2000年學術文章
@yue
2000年學術文章
@zh
2000年學術文章
@zh-hant
name
A dynamically tuned double-str ...... ation of antiviral kinase PKR.
@en
type
label
A dynamically tuned double-str ...... ation of antiviral kinase PKR.
@en
prefLabel
A dynamically tuned double-str ...... ation of antiviral kinase PKR.
@en
P2093
P2860
P356
P1433
P1476
A dynamically tuned double-str ...... ation of antiviral kinase PKR.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/19.20.5567
P407
P577
2000-10-01T00:00:00Z