Phosphorylation of tristetraprolin, a potential zinc finger transcription factor, by mitogen stimulation in intact cells and by mitogen-activated protein kinase in vitro
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The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritisEvidence that tristetraprolin binds to AU-rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA.Interactions of CCCH zinc finger proteins with mRNA. Binding of tristetraprolin-related zinc finger proteins to Au-rich elements and destabilization of mRNACytoplasmic localization of tristetraprolin involves 14-3-3-dependent and -independent mechanismsMAPKAP kinase 2 phosphorylates tristetraprolin on in vivo sites including Ser178, a site required for 14-3-3 bindingMK2-induced tristetraprolin:14-3-3 complexes prevent stress granule association and ARE-mRNA decayThe ARE-dependent mRNA-destabilizing activity of BRF1 is regulated by protein kinase BThe roles of TTP and BRF proteins in regulated mRNA decayTristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonucleaseRole of KSRP in control of type I interferon and cytokine expressionRegulation of AU-Rich Element RNA Binding Proteins by Phosphorylation and the Prolyl Isomerase Pin1Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85ZFP36L1 negatively regulates erythroid differentiation of CD34+ hematopoietic stem cells by interfering with the Stat5b pathwayDecreased sensitivity of tristetraprolin-deficient cells to p38 inhibitors suggests the involvement of tristetraprolin in the p38 signaling pathwayMitogen-activated protein kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stabilityExpression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-alpha mRNA and serve as a substrate for mitogen-activated protein kinasesRNA binding properties of the AU-rich element-binding recombinant Nup475/TIS11/tristetraprolin protein.Inhibition of tristetraprolin deadenylation by poly(A) binding protein.Characterization of the mRNA ligands bound by the RNA binding protein hnRNP A2 utilizing a novel in vivo technique.Identification of the anti-inflammatory protein tristetraprolin as a hyperphosphorylated protein by mass spectrometry and site-directed mutagenesisPhosphorylation site analysis of the anti-inflammatory and mRNA-destabilizing protein tristetraprolin.Identification of a major phosphopeptide in human tristetraprolin by phosphopeptide mapping and mass spectrometry.The mRNA-binding protein Zfp36 is upregulated by β-adrenergic stimulation and represses IL-6 production in 3T3-L1 adipocytesPolyubiquitinated tristetraprolin protects from TNF-induced, caspase-mediated apoptosisExpression, purification, and biochemical characterization of the antiinflammatory tristetraprolin: a zinc-dependent mRNA binding protein affected by posttranslational modifications.Immunological characterization of tristetraprolin as a low abundance, inducible, stable cytosolic proteinMyeloid ZFP36L1 does not regulate inflammation or host defense in mouse models of acute bacterial infectionZFP36-FOSB fusion defines a subset of epithelioid hemangioma with atypical featuresFenretinide corrects the imbalance between omega-6 to omega-3 polyunsaturated fatty acids and inhibits macrophage inflammatory mediators via the ERK pathway.C. elegans GLA-3 is a novel component of the MAP kinase MPK-1 signaling pathway required for germ cell survival.Helicobacter pylori infection induced alteration of gene expression in human gastric cells.Computational Model of MicroRNA Control of HIF-VEGF Pathway: Insights into the Pathophysiology of Ischemic Vascular Disease and CancerMetal binding properties and secondary structure of the zinc-binding domain of Nup475.Analysis of turnover and translation regulatory RNA-binding protein expression through binding to cognate mRNAs.The role of tristetraprolin in cancer and inflammation.Mitogen-activated protein kinase activation is not necessary for, but antagonizes, 3T3-L1 adipocytic differentiation.The inducibly expressed GTPase localizes to the endoplasmic reticulum, independently of GTP binding.Tristetraprolin (TTP): interactions with mRNA and proteins, and current thoughts on mechanisms of action.Phosphorylation of recombinant tristetraprolin in vitroTIS11 family proteins and their roles in posttranscriptional gene regulation.
P2860
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P2860
Phosphorylation of tristetraprolin, a potential zinc finger transcription factor, by mitogen stimulation in intact cells and by mitogen-activated protein kinase in vitro
description
1995 nî lūn-bûn
@nan
1995 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Phosphorylation of tristetrapr ...... ivated protein kinase in vitro
@ast
Phosphorylation of tristetrapr ...... ivated protein kinase in vitro
@en
Phosphorylation of tristetrapr ...... ivated protein kinase in vitro
@nl
type
label
Phosphorylation of tristetrapr ...... ivated protein kinase in vitro
@ast
Phosphorylation of tristetrapr ...... ivated protein kinase in vitro
@en
Phosphorylation of tristetrapr ...... ivated protein kinase in vitro
@nl
prefLabel
Phosphorylation of tristetrapr ...... ivated protein kinase in vitro
@ast
Phosphorylation of tristetrapr ...... ivated protein kinase in vitro
@en
Phosphorylation of tristetrapr ...... ivated protein kinase in vitro
@nl
P2093
P2860
P356
P1476
Phosphorylation of tristetrapr ...... ivated protein kinase in vitro
@en
P2093
G A Taylor
M J Thompson
P J Blackshear
P2860
P304
P356
10.1074/JBC.270.22.13341
P407
P577
1995-06-02T00:00:00Z