PACT, a protein activator of the interferon-induced protein kinase, PKR.
about
DRBP76, a double-stranded RNA-binding nuclear protein, is phosphorylated by the interferon-induced protein kinase, PKRThe B56alpha regulatory subunit of protein phosphatase 2A is a target for regulation by double-stranded RNA-dependent protein kinase PKRThe role of PACT in the RNA silencing pathwayInteraction of human tRNA-dihydrouridine synthase-2 with interferon-induced protein kinase PKRMutual antagonism between the Ebola virus VP35 protein and the RIG-I activator PACT determines infection outcomeThe RNA-binding region of human TRBP interacts with microRNA precursors through two independent domainsThe 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)Inhibition of PACT-mediated activation of PKR by the herpes simplex virus type 1 Us11 protein.RDE-4 preferentially binds long dsRNA and its dimerization is necessary for cleavage of dsRNA to siRNA.A role of the double-stranded RNA-binding protein PACT in mouse ear development and hearingAntiviral actions of interferonsMolecular basis for PKR activation by PACT or dsRNAModular structure of PACT: distinct domains for binding and activating PKRA new pathway of translational regulation mediated by eukaryotic initiation factor 3The double-stranded RNA-binding protein, PACT, is required for postnatal anterior pituitary proliferationRAX, the PKR activator, sensitizes cells to inflammatory cytokines, serum withdrawal, chemotherapy, and viral infectionImpact of protein kinase PKR in cell biology: from antiviral to antiproliferative actionSmall interfering RNAs against the TAR RNA binding protein, TRBP, a Dicer cofactor, inhibit human immunodeficiency virus type 1 long terminal repeat expression and viral productionDoes protein kinase R mediate TNF-alpha- and ceramide-induced increases in expression and activation of matrix metalloproteinases in articular cartilage by a novel mechanism?Processing of pre-microRNAs by the Dicer-1-Loquacious complex in Drosophila cellsInvolvement of PKR and RNase L in translational control and induction of apoptosis after Hepatitis C polyprotein expression from a vaccinia virus recombinantRNA recognition by double-stranded RNA binding domains: a matter of shape and sequenceInterferon-inducible antiviral effectorsThe Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc FingersGeneration and comprehensive analysis of an influenza virus polymerase cellular interaction networkAnalysis of a binding difference between the two dsRNA-binding domains in TRBP reveals the modular function of a KR-helix motifRAX, a cellular activator for double-stranded RNA-dependent protein kinase during stress signalingA novel role for RAX, the cellular activator of PKR, in synergistically stimulating SV40 large T antigen-dependent gene expressionTwo dimerization domains in the trans-activation response RNA-binding protein (TRBP) individually reverse the protein kinase R inhibition of HIV-1 long terminal repeat expressionCharacterization 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 kinaseThe direct binding of the catalytic subunit of protein phosphatase 1 to the PKR protein kinase is necessary but not sufficient for inactivation and disruption of enzyme dimer formationTranslation inhibition in apoptosis: caspase-dependent PKR activation and eIF2-alpha phosphorylationPhosphorylation of specific serine residues in the PKR activation domain of PACT is essential for its ability to mediate apoptosisSerine 18 phosphorylation of RAX, the PKR activator, is required for PKR activation and consequent translation inhibitionInteraction between RAX and PKR modulates the effect of ethanol on protein synthesis and survival of neuronsSatratoxin G-induced apoptosis in PC-12 neuronal cells is mediated by PKR and caspase independentThe chemotherapeutic drug 5-fluorouracil promotes PKR-mediated apoptosis in a p53-independent manner in colon and breast cancer cellsMissense mutation in the second RNA binding domain reveals a role for Prkra (PACT/RAX) during skull developmentProapoptotic protein PACT is expressed at high levels in colonic epithelial cells in mice
P2860
Q22010241-A0D0BDDE-5824-4503-B483-33D31CB3F5AAQ22254335-F1249406-49AC-4E7D-BBB3-F8FC6C89736FQ24301564-84914143-89FD-46E8-95C5-B348F89615A8Q24304341-07DAEB57-79F8-4DE4-8806-5E9154FDA9E7Q24310145-364FF314-D02E-4E85-9B61-3E5E681C83B3Q24320118-E6042D5A-0F6D-4B78-B208-3B279E160F9FQ24534342-43E16FC5-1E4B-43EB-BB48-2AA815FA4969Q24538727-F0C7361E-E27D-409B-BF34-026B28C0566CQ24543937-548863F7-423B-4B51-8AF4-A4A8615D5510Q24546307-D10DC182-E970-45AD-B1E7-15B739BF09C5Q24550676-0B958256-A9F2-4E97-A609-321167B8EA47Q24550949-347A85B8-FE5A-4C36-B633-C86A78F68FF2Q24551001-40EE3D49-172C-46E2-8C2B-E0811A6AC989Q24595576-95E42044-1BAC-46AF-B173-E538084811BEQ24653603-D1A092D0-9BC0-4193-904C-418B3C68B9A9Q24671766-F1761ED8-F06A-4004-A4CB-A197691A0FCFQ24672548-D6AD7C6F-F6F2-4C47-A8A1-F32E60B51C51Q24682936-2572C22D-9BE0-467B-BDFD-20F2381F6C64Q24793070-60B81E73-85A3-4287-B62B-3C03575C9E39Q24810080-8386126C-3AF8-40E0-AB88-4BC513C2FF42Q24814549-809C0EEB-DE7F-4D66-8E86-A455F2E44F50Q27023888-790BE3E7-7E94-4F3D-AC65-E7CCA868B8CBQ27486790-9C42D626-0A1A-4ABF-95C3-8AB9BFAAC85BQ27653603-D02A1493-5C08-4241-9ED0-C5FACDA7AB6BQ28118085-8642E496-D1B1-4083-80A7-86460AFC9D88Q28141516-0193077B-D2FC-40E2-B653-BE9687B020BEQ28144380-4D556507-0B00-4937-8DCE-9ED83869AB9BQ28188726-492C7CE5-31A2-4C9D-B773-57CD9CE04D71Q28204738-CC407085-E64B-4E7C-BBEA-B85E69234404Q28204754-66D56D7F-E1FA-4C36-BAD0-AC686D9473E6Q28204764-8F65C01D-3CBB-45A6-A500-9C4F1DAD5F9CQ28215791-34340516-694E-46A2-B587-2A5AA05D1156Q28216131-A6A6351B-FD58-4951-AE26-138A50A793D5Q28264248-AFCECDB1-CDC8-4D9C-BA0B-B0B276F476D9Q28276027-A4780C7A-F20F-458A-88E1-BB41DD62F5CAQ28304609-1A403E0F-481D-4364-B848-A6EE46CB2E4AQ28390683-DE50EA75-AA3E-4F52-B7A8-5102CF0606B4Q28476682-EEC34B32-F23F-4185-BDEF-A41A582C69BBQ28478412-8A62998B-CD1E-434C-A6D1-8C83594C6D8DQ28505817-369566F3-EEB6-4776-A94C-AD83EA28D2D8
P2860
PACT, a protein activator of the interferon-induced protein kinase, PKR.
description
1998 nî lūn-bûn
@nan
1998 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի օգոստոսին 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
PACT, a protein activator of the interferon-induced protein kinase, PKR
@nl
PACT, a protein activator of the interferon-induced protein kinase, PKR.
@ast
PACT, a protein activator of the interferon-induced protein kinase, PKR.
@en
PACT, a protein activator of the interferon-induced protein kinase, PKR.
@en-gb
type
label
PACT, a protein activator of the interferon-induced protein kinase, PKR
@nl
PACT, a protein activator of the interferon-induced protein kinase, PKR.
@ast
PACT, a protein activator of the interferon-induced protein kinase, PKR.
@en
PACT, a protein activator of the interferon-induced protein kinase, PKR.
@en-gb
prefLabel
PACT, a protein activator of the interferon-induced protein kinase, PKR
@nl
PACT, a protein activator of the interferon-induced protein kinase, PKR.
@ast
PACT, a protein activator of the interferon-induced protein kinase, PKR.
@en
PACT, a protein activator of the interferon-induced protein kinase, PKR.
@en-gb
P2860
P356
P1433
P1476
PACT, a protein activator of the interferon-induced protein kinase, PKR.
@en
P2093
P2860
P304
P356
10.1093/EMBOJ/17.15.4379
P407
P577
1998-08-01T00:00:00Z