DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR
about
The B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKRThe RNA binding protein nuclear factor 90 functions as both a positive and negative regulator of gene expression in mammalian cellsDRBP76 associates with Ebola virus VP35 and suppresses viral polymerase functionA physical and regulatory map of host-influenza interactions reveals pathways in H1N1 infectionPhosphorylation of the NFAR proteins by the dsRNA-dependent protein kinase PKR constitutes a novel mechanism of translational regulation and cellular defenseCharacterization of the interaction between the interferon-induced protein P56 and the Int6 protein encoded by a locus of insertion of the mouse mammary tumor virus.ADAR1 interacts with NF90 through double-stranded RNA and regulates NF90-mediated gene expression independently of RNA editingAntiviral actions of interferonsModular structure of PACT: distinct domains for binding and activating PKRA new pathway of translational regulation mediated by eukaryotic initiation factor 3IRF3 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 proteinCharacterization of two evolutionarily conserved, alternatively spliced nuclear phosphoproteins, NFAR-1 and -2, that function in mRNA processing and interact with the double-stranded RNA-dependent protein kinase, PKRNuclear factor 90 is a substrate and regulator of the eukaryotic initiation factor 2 kinase double-stranded RNA-activated protein kinaseMinihelix-containing RNAs mediate exportin-5-dependent nuclear export of the double-stranded RNA-binding protein ILF3High expression of nuclear factor 90 (NF90) leads to mitochondrial degradation in skeletal and cardiac musclesThe HILDA complex coordinates a conditional switch in the 3'-untranslated region of the VEGFA mRNAAlu mobile elements: from junk DNA to genomic gemsFunctional characterization of and cooperation between the double-stranded RNA-binding motifs of the protein kinase PKR.Identification of Ebp1 as a component of cytoplasmic bcl-2 mRNP (messenger ribonucleoprotein particle) complexes.Nuclear factor 90 negatively regulates influenza virus replication by interacting with viral nucleoprotein.NF90 selectively represses the translation of target mRNAs bearing an AU-rich signature motif.The 3'-untranslated regions of cytoskeletal muscle mRNAs inhibit translation by activating the double-stranded RNA-dependent protein kinase PKR.Tissue type-specific expression of the dsRNA-binding protein 76 and genome-wide elucidation of its target mRNAsInduction of p53, p21 and apoptosis by silencing the NF90/NF45 complex in human papilloma virus-transformed cervical carcinoma cells.L-Ilf3 and L-NF90 traffic to the nucleolus granular component: alternatively-spliced exon 3 encodes a nucleolar localization motifProtection from interferon-induced apoptosis by Epstein-Barr virus small RNAs is not mediated by inhibition of PKR.Novel rapidly evolving hominid RNAs bind nuclear factor 90 and display tissue-restricted distributionProtein kinase LegK2 is a type IV secretion system effector involved in endoplasmic reticulum recruitment and intracellular replication of Legionella pneumophilaNuclear Factor 90, a cellular dsRNA binding protein inhibits the HIV Rev-export function.Inhibition of PKR impairs angiogenesis through a VEGF pathway.Effects of length and location on the cellular response to double-stranded RNA.The NF45/NF90 Heterodimer Contributes to the Biogenesis of 60S Ribosomal Subunits and Influences Nucleolar Morphology.NF90 coordinately represses the senescence-associated secretory phenotype.NF45 and NF90 Bind HIV-1 RNA and Modulate HIV Gene ExpressionNFAR-1 and -2 modulate translation and are required for efficient host defense.Nuclear factor 45 (NF45) is a regulatory subunit of complexes with NF90/110 involved in mitotic controlExpression and Critical Role of Interleukin Enhancer Binding Factor 2 in Hepatocellular Carcinoma.Calcium-Dependent Protein Kinase in Ginger Binds with Importin-α through Its Junction Domain for Nuclear Localization, and Further Interacts with NAC Transcription FactorIlf3 and NF90 functions in RNA biology.HIV-1 replication and latency are regulated by translational control of cyclin T1
P2860
Q22254335-B6038203-2384-4EA2-B1EC-F3712BA3A2F5Q24291990-53CCC7E4-0208-4EE7-9674-F71001230275Q24292964-C09CFA5D-A48E-4D0D-85CF-C05589AE7E27Q24294658-84B92B8A-E25F-4821-B5A8-1FDE08A65F9FQ24310584-1B999BD5-1520-425A-B598-C0AAB4A02883Q24524346-4E4A4D8E-824B-4510-996E-2424E2127E20Q24529861-BC3436DE-362A-446A-AB05-445E01D1F576Q24550676-29611501-886B-4BD0-B4A6-1FFA1B5494BCQ24551001-897A739A-9149-4B10-AE62-EA4C52BB74AAQ24595576-259BA928-2F07-4614-9074-3584EDA5F03DQ28140837-99C25F2B-ACA1-4708-B341-32B30E454F28Q28204754-4A946E72-1864-44D3-8183-1B1ADF9BBA61Q28204764-00AE3B5A-5425-4AE3-ADE5-48473571FC51Q28211625-81C0F6F9-5CA1-45B0-90DC-3362F2D8EC28Q28482359-7A3D3DCB-D98D-4849-A9A6-9633D77C92DFQ28535448-E3CAEEC1-B325-4F12-8B2B-1A95B77D09A0Q28661722-631A3848-309F-4287-9E80-F875E44B781CQ31778073-FF2FEAB8-CB03-4D5D-8292-3C825FCC6557Q33231031-85F83C15-069A-4A55-95B1-9B0C738B8A3BQ33459671-C08718B4-49CF-4AFD-A2CC-E78352A229B0Q33566472-FEE3FBA8-7673-4AE8-B91D-ED58BCFDE137Q33583983-9D617801-22C5-461E-8360-B0786CCDBD7FQ33644256-6AC21F7C-E756-40C2-964C-B40B3E8D5E90Q33656171-76CE7753-6661-4A30-A46C-7AE47C2E3B29Q33979801-223903C9-2DF1-4454-B5F3-7BF1AB1C9B19Q34142897-ADF16AED-5EA9-4BF0-931C-ED63B7394754Q34687063-25384090-1110-4743-B742-40F04E86B467Q34931764-C13F31B3-4C13-42CD-B75B-8C62F711AFA7Q35241432-EC544F7D-E68F-4AED-93A2-79393519561FQ35542539-3B56B86F-D3FB-4DC5-9DD9-B216B1854D5DQ35880915-2447CBB0-5CBC-42E5-929B-E24CFBD6385EQ36070037-0935A53B-771A-4EB3-AC24-F9CD71E2376FQ36455196-84FB6BEF-30B2-4D86-BF40-B0FB835A6D80Q36645526-EA40A2D6-7F19-43B3-A34B-21574C1E5B47Q36670296-05051357-27E1-4DE5-8851-9D548DF6B932Q36748114-1DC5E8D6-B69D-4149-82EB-F92800621495Q37210275-2798AA8A-E10D-41E3-9CF1-A62654F3B976Q37584052-FC8BF9B1-F371-4634-9A47-07B1A3727F22Q38261272-C69FF3A7-DBCD-4E2D-91D9-8B3F63EAD424Q38273477-36417003-91CC-42EE-BE2E-C888D7512640
P2860
DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKR
description
1999 nî lūn-bûn
@nan
1999 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@ast
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@en
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@en-gb
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@nl
type
label
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@ast
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@en
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@en-gb
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@nl
prefLabel
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@ast
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@en
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@en-gb
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@nl
P2093
P2860
P3181
P356
P1476
DRBP76, a double-stranded RNA- ...... on-induced protein kinase, PKR
@en
P2093
B R Williams
D J Vestal
S Bandyopadhyay
P2860
P304
P3181
P356
10.1074/JBC.274.29.20432
P407
P577
1999-07-16T00:00:00Z