The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase.
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Nucleocytoplasmic translocation of Stat1 is regulated by a leucine-rich export signal in the coiled-coil domainVaccinia virus blocks gamma interferon signal transduction: viral VH1 phosphatase reverses Stat1 activationIdentification of a nuclear Stat1 protein tyrosine phosphataseInhibition of Stat1-mediated gene activation by PIAS1Principles of interleukin (IL)-6-type cytokine signalling and its regulationInterleukin-6-type cytokine signalling through the gp130/Jak/STAT pathwayStat1-vitamin D receptor interactions antagonize 1,25-dihydroxyvitamin D transcriptional activity and enhance stat1-mediated transcription.Regulation of Jak2 through the ubiquitin-proteasome pathway involves phosphorylation of Jak2 on Y1007 and interaction with SOCS-1.GRIM-19, a death-regulatory gene product, suppresses Stat3 activity via functional interactionA Drosophila PIAS homologue negatively regulates stat92ESTAT3-dependent enhanceosome assembly and disassembly: synergy with GR for full transcriptional increase of the alpha 2-macroglobulin geneSignal transducers and activators of transcription as regulators of growth, apoptosis and breast development.Protein tyrosine phosphatases as wardens of STAT signalingNon-genomic STAT5-dependent effects at the endoplasmic reticulum and Golgi apparatus and STAT6-GFP in mitochondriaExpression of hepatitis C virus proteins inhibits signal transduction through the Jak-STAT pathwayInterferons and viruses: an evolutionary arms race of molecular interactionsShort-chain fatty acid derivatives stimulate cell proliferation and induce STAT-5 activationHigh STAT1 mRNA levels but not its tyrosine phosphorylation are associated with macrophage infiltration and bad prognosis in breast cancer.STAT signaling in the pathogenesis and treatment of cancerSubversion mechanisms by which Leishmania parasites can escape the host immune response: a signaling point of view.IL-10 inhibits macrophage activation and proliferation by distinct signaling mechanisms: evidence for Stat3-dependent and -independent pathwaysAnopheles gambiae Ag-STAT, a new insect member of the STAT family, is activated in response to bacterial infection.Implications of an antiparallel dimeric structure of nonphosphorylated STAT1 for the activation-inactivation cycle.Stat3 directly controls the expression of Tbx5, Nkx2.5, and GATA4 and is essential for cardiomyocyte differentiation of P19CL6 cells.The different functions of Stat5 and chromatin alteration through Stat5 proteinsTwo glutamic acid residues in the DNA-binding domain are engaged in the release of STAT1 dimers from DNA.Composition and assembly of STAT-targeting ubiquitin ligase complexes: paramyxovirus V protein carboxyl terminus is an oligomerization domain.Ebola virus VP24 binds karyopherin alpha1 and blocks STAT1 nuclear accumulationA small amphipathic alpha-helical region is required for transcriptional activities and proteasome-dependent turnover of the tyrosine-phosphorylated Stat5Transient oscillatory dynamics of interferon beta signaling in macrophagesA conserved motif in the linker domain of STAT1 transcription factor is required for both recognition and release from high-affinity DNA-binding sitesDysregulation of janus kinases and signal transducers and activators of transcription in cancer.DNA binding reduces the dissociation rate of STAT1 dimers and impairs the interdimeric exchange of protomers.A nuclear protein tyrosine phosphatase is required for the inactivation of Stat1.Inhibitor of κB kinase epsilon (IKK(epsilon)), STAT1, and IFIT2 proteins define novel innate immune effector pathway against West Nile virus infectionSuppression of the Sendai virus M protein through a novel short interfering RNA approach inhibits viral particle production but does not affect viral RNA synthesisNewcastle Disease Virus V Protein Targets Phosphorylated STAT1 to Block IFN-I Signaling.Getting the message across, STAT! Design principles of a molecular signaling circuit.DNA binding controls inactivation and nuclear accumulation of the transcription factor Stat1.Rapid inhibition of interleukin-6 signaling and Stat3 activation mediated by mitogen-activated protein kinases.
P2860
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P2860
The rapid inactivation of nuclear tyrosine phosphorylated Stat1 depends upon a protein tyrosine phosphatase.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
The rapid inactivation of nucl ...... protein tyrosine phosphatase.
@en
type
label
The rapid inactivation of nucl ...... protein tyrosine phosphatase.
@en
prefLabel
The rapid inactivation of nucl ...... protein tyrosine phosphatase.
@en
P2093
P2860
P1433
P1476
The rapid inactivation of nucl ...... a protein tyrosine phosphatase
@en
P2093
J E Darnell
M Salditt-Georgieff
R L Haspel
P2860
P304
P356
10.1002/J.1460-2075.1996.TB01016.X
P407
P577
1996-11-01T00:00:00Z