TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress. - Wikidata - awgldk - TriplyDB

TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.

TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.

http://www.wikidata.org/entity/Q37033570

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Production of small RNAs by mammalian Dicer Pro-Apoptotic Kinase Levels in Cerebrospinal Fluid as Potential Future Biomarkers in Alzheimer's Disease TRBP and eIF6 homologue in Marsupenaeus japonicus play crucial roles in antiviral response Hepatitis C virus controls interferon production through PKR activation Missense mutation in the second RNA binding domain reveals a role for Prkra (PACT/RAX) during skull development Recombinant hTRBP and hPACT Modulate hAgo2-Catalyzed siRNA-Mediated Target RNA Cleavage In Vitro Characterization of the TRBP domain required for dicer interaction and function in RNA interference.MicroRNA Machinery Genes as Novel Biomarkers for Cancer Convergence of Domain Architecture, Structure, and Ligand Affinity in Animal and Plant RNA-Binding Proteins.'Black sheep' that don't leave the double-stranded RNA-binding domain fold RNA granule assembly and disassembly modulated by nuclear factor associated with double-stranded RNA 2 and nuclear factor 45 Unperturbed posttranscriptional regulatory Rev protein function and HIV-1 replication in astrocytes A role for human Dicer in pre-RISC loading of siRNAs.Distinguishable in vitro binding mode of monomeric TRBP and dimeric PACT with siRNA Ebolavirus proteins suppress the effects of small interfering RNA by direct interaction with the mammalian RNA interference pathway.dsRNA binding protein PACT/RAX in gene silencing, development and diseases.The stress granule protein G3BP1 recruits protein kinase R to promote multiple innate immune antiviral responses.Parallel action of AtDRB2 and RdDM in the control of transposable element expression Nucleofection induces transient eIF2α phosphorylation by GCN2 and PERK.Altered activation of protein kinase PKR and enhanced apoptosis in dystonia cells carrying a mutation in PKR activator protein PACT.Endocytosis of human immunodeficiency virus 1 (HIV-1) in astrocytes: a fiery path to its destination.HIV-1 RRE RNA acts as an RNA silencing suppressor by competing with TRBP-bound siRNAs The multiple functions of TRBP, at the hub of cell responses to viruses, stress, and cancer.Regulation of PACT-Mediated Protein Kinase Activation by the OV20.0 Protein of Orf Virus.dsRNA-dependent protein kinase PKR and its role in stress, signaling and HCV infection.Proteomic analysis of early HIV-1 nucleoprotein complexes.Movements of HIV-1 genomic RNA-APOBEC3F complexes and PKR reveal cytoplasmic and nuclear PKR defenses and HIV-1 evasion strategies.Recent advances in the molecular pathogenesis of dystonia-plus syndromes and heredodegenerative dystonias.Molecular basis for improved gene silencing by Dicer substrate interfering RNA compared with other siRNA variants mRNA decapping enzyme 1a (Dcp1a)-induced translational arrest through protein kinase R (PKR) activation requires the N-terminal enabled vasodilator-stimulated protein homology 1 (EVH1) domain.ADAR1 and PACT contribute to efficient translation of transcripts containing HIV-1 trans-activating response (TAR) element.Activation of the Antiviral Kinase PKR and Viral Countermeasures.Mapping the crossroads of immune activation and cellular stress response pathways.Human RNAi pathway: crosstalk with organelles and cells.HIV-1 endocytosis in astrocytes: a kiss of death or survival of the fittest?Dissecting the roles of TRBP and PACT in double-stranded RNA recognition and processing of noncoding RNAs.The cellular TAR RNA binding protein, TRBP, promotes HIV-1 replication primarily by inhibiting the activation of double-stranded RNA-dependent kinase PKR.The PKR activator, PACT, becomes a PKR inhibitor during HIV-1 replication.Stress-induced changes in miRNA biogenesis and functioning.The PKR activator PACT is induced by Aβ: involvement in Alzheimer's disease.

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TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.

http://www.wikidata.org/entity/Q37033570

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 20 October 2008

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.

@en

TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.

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type

label

TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.

@en

TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.

@nl

prefLabel

TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.

@en

TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.

@nl

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Molecular and Cellular Biology

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TRBP control of PACT-induced phosphorylation of protein kinase R is reversed by stress.

@en

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Antoine H F M Peters

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

Aïcha Daher

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Carlos E Melendez-Peña

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

Eliane F Meurs

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

Ghislaine Laraki

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

Madhurima Singh

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

Rekha C Patel

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Robert E Braun

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Sylvie Bannwarth

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P2860

Organization of the human tarbp2 gene reveals two promoters that are repressed in an astrocytic cell line

The role of PACT in the RNA silencing pathway

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

Human TRBP and PACT directly interact with each other and associate with dicer to facilitate the production of small interfering RNA

Interaction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKR

TRBP recruits the Dicer complex to Ago2 for microRNA processing and gene silencing

PACT, a protein activator of the interferon-induced protein kinase, PKR.

TRBP, a regulator of cellular PKR and HIV-1 virus expression, interacts with Dicer and functions in RNA silencing

The 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 PKR

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254-265

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scholarly article

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10.1128/MCB.01030-08

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P433

1

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29

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2008-10-20T00:00:00Z

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18936160

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phosphorylation

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2612476

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