Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation. - Wikidata - wikimedia - TriplyDB

Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation.

Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation.

http://www.wikidata.org/entity/Q42085248

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Autoantibodies define a family of proteins with conserved double-stranded RNA-binding domains as well as DNA binding activity Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKR The RNA-binding region of human TRBP interacts with microRNA precursors through two independent domains Crystal structure of human DGCR8 core TRAF family proteins link PKR with NF-kappa B activation Structure and interactions of the translation initiation factor eIF1 Molecular mapping of the determinants involved in human Staufen-ribosome association Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase.A method to find tissue-specific novel sites of selective adenosine deamination.Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein.Molecular basis for PKR activation by PACT or dsRNA Modular structure of PACT: distinct domains for binding and activating PKR Impact of protein kinase PKR in cell biology: from antiviral to antiproliferative action RNA editing by adenosine deaminases that act on RNA New Insights into the Biological Role of Mammalian ADARs; the RNA Editing Proteins The ADAR protein family RNA recognition by double-stranded RNA binding domains: a matter of shape and sequence Interplay between interferon-mediated innate immunity and porcine reproductive and respiratory syndrome virus Interferon-inducible antiviral effectors RNA recognition by a Staufen double-stranded RNA-binding domain Structure of the reovirus outer capsid and dsRNA-binding protein sigma3 at 1.8 A resolution.A novel family of RNA tetraloop structure forms the recognition site for Saccharomyces cerevisiae RNase III.Solution structure of conserved AGNN tetraloops: insights into Rnt1p RNA processing Ribosome-associated factor Y adopts a fold resembling a double-stranded RNA binding domain scaffold The structure of the zinc finger domain from human splicing factor ZNF265 fold Crystal Structure of the Avian Reovirus Inner Capsid Protein A Structure of a Yeast RNase III dsRBD Complex with a Noncanonical RNA Substrate Provides New Insights into Binding Specificity of dsRBDs Intrinsic Dynamics of an Extended Hydrophobic Core in the S. cerevisiae RNase III dsRBD Contributes to Recognition of Specific RNA Binding Sites Structural insights into RISC assembly facilitated by dsRNA-binding domains of human RNA helicase A (DHX9)Solution structures of the double-stranded RNA-binding domains from RNA helicase A Structure of RDE-4 dsRBDs and mutational studies provide insights into dsRNA recognition in the Caenorhabditis elegans RNAi pathway Analysis of a binding difference between the two dsRNA-binding domains in TRBP reveals the modular function of a KR-helix motif Enhanced antiviral and antiproliferative properties of a STAT1 mutant unable to interact with the protein kinase PKR Minihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3 Proapoptotic protein PACT is expressed at high levels in colonic epithelial cells in mice Two rat brain staufen isoforms differentially bind RNA PKR deficiency alters E. coli-induced sickness behaviors but does not exacerbate neuroimmune responses or bacterial load Prediction of a novel RNA binding domain in crocodilepox Zimbabwe Gene 157.The protein kinase double-stranded RNA-dependent (PKR) enhances protection against disease cause by a non-viral pathogen.Functional characterization of and cooperation between the double-stranded RNA-binding motifs of the protein kinase PKR.

P2860

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P2860

Structure of the double-stranded RNA-binding domain of the protein kinase PKR reveals the molecular basis of its dsRNA-mediated activation.

http://www.wikidata.org/entity/Q42085248

description

1998 nî lūn-bûn

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1998年の論文

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1998年論文

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1998年論文

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1998年論文

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1998年論文

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1998年論文

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1998年论文

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1998年论文

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1998年论文

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name

Structure of the double-strand ...... its dsRNA-mediated activation.

@en

Structure of the double-strand ...... its dsRNA-mediated activation.

@nl

type

label

Structure of the double-strand ...... its dsRNA-mediated activation.

@en

Structure of the double-strand ...... its dsRNA-mediated activation.

@nl

prefLabel

Structure of the double-strand ...... its dsRNA-mediated activation.

@en

Structure of the double-strand ...... its dsRNA-mediated activation.

@nl

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The EMBO Journal

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Structure of the double-strand ...... its dsRNA-mediated activation.

@en

P2093

B R Williams

http://www.w3.org/2001/XMLSchema#string

B W Carpick

http://www.w3.org/2001/XMLSchema#string

J Qin

http://www.w3.org/2001/XMLSchema#string

S Nanduri

http://www.w3.org/2001/XMLSchema#string

Y Yang

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P2860

Molecular cloning and characterization of the human double-stranded RNA-activated protein kinase induced by interferon

Physical association between STAT1 and the interferon-inducible protein kinase PKR and implications for interferon and double-stranded RNA signaling pathways

Double-stranded-RNA-dependent protein kinase and TAR RNA-binding protein form homo- and heterodimers in vivo

Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at 2.1 A

NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

The Tat protein of human immunodeficiency virus type 1 is a substrate and inhibitor of the interferon-induced, virally activated protein kinase, PKR

The impact of direct refinement against 13C alpha and 13C beta chemical shifts on protein structure determination by NMR.

The impact of direct refinement against three-bond HN-C alpha H coupling constants on protein structure determination by NMR.

Minor-groove recognition of double-stranded RNA by the double-stranded RNA-binding domain from the RNA-activated protein kinase PKR.

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5458-5465

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10.1093/EMBOJ/17.18.5458

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18

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17

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13548443

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9736623

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1170871

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