A single residue modulates tyrosine dephosphorylation, oligomerization, and nuclear accumulation of stat transcription factors.
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FOXP3 ensembles in T-cell regulationTyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformationsNovel drug targets for personalized precision medicine in relapsed/refractory diffuse large B-cell lymphoma: a comprehensive reviewDTX3L and ARTD9 inhibit IRF1 expression and mediate in cooperation with ARTD8 survival and proliferation of metastatic prostate cancer cellsA STAT3-decoy oligonucleotide induces cell death in a human colorectal carcinoma cell line by blocking nuclear transfer of STAT3 and STAT3-bound NF-κB.Rabies virus P protein interacts with STAT1 and inhibits interferon signal transduction pathways.Alternative ways of modulating JAK-STAT pathway: Looking beyond phosphorylation.Two glutamic acid residues in the DNA-binding domain are engaged in the release of STAT1 dimers from DNA.Clinically relevant dimer interface mutants of STAT1 transcription factor exhibit differential gene expression.A 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 Mutation in the SH2 domain of STAT2 prolongs tyrosine phosphorylation of STAT1 and promotes type I IFN-induced apoptosisGetting the message across, STAT! Design principles of a molecular signaling circuit.Impact of the N-Terminal Domain of STAT3 in STAT3-Dependent Transcriptional ActivitySignal transducer and activator of transcription (STAT) signalling and T-cell lymphomas.Protein tyrosine phosphatase Meg2 dephosphorylates signal transducer and activator of transcription 3 and suppresses tumor growth in breast cancer.STAT5 requires the N-domain to maintain hematopoietic stem cell repopulating function and appropriate lymphoid-myeloid lineage output.Nucleocytoplasmic shuttling by nucleoporins Nup153 and Nup214 and CRM1-dependent nuclear export control the subcellular distribution of latent Stat1.Recruitment of Stat1 to chromatin is required for interferon-induced serine phosphorylation of Stat1 transactivation domainIn vivo identification of novel STAT5 target genesRequirement of histone deacetylase1 (HDAC1) in signal transducer and activator of transcription 3 (STAT3) nucleocytoplasmic distribution.STAT nuclear translocation: potential for pharmacological intervention.The STAT3 NH2-terminal domain stabilizes enhanceosome assembly by interacting with the p300 bromodomain.Biology and significance of the JAK/STAT signalling pathways.Molecular basis for the recognition of phosphorylated STAT1 by importin alpha5.Downregulated Expression of PTPN9 Contributes to Human Hepatocellular Carcinoma Growth and Progression.STAT1-cooperative DNA binding distinguishes type 1 from type 2 interferon signaling.IL-6 signaling via the STAT3/SOCS3 pathway: functional analysis of the conserved STAT3 N-domainPurification and identification of the STAT5 protease in myeloid cells.Inhibition of interferon signaling by rabies virus phosphoprotein P: activation-dependent binding of STAT1 and STAT2.Alanine-scanning mutagenesis of human signal transducer and activator of transcription 1 to estimate loss- or gain-of-function variants.Interleukin 15 controls the generation of the restricted T cell receptor repertoire of gamma delta intestinal intraepithelial lymphocytes.Live cell imaging reveals continuous STAT6 nuclear traffickingA rapid conformational rearrangement of STAT1 dimers is required for termination rather than for amplification of interferon-γ signaling.The nucleocytoplasmic rabies virus P protein counteracts interferon signaling by inhibiting both nuclear accumulation and DNA binding of STAT1.Protein kinase Cdelta regulates apoptosis via activation of STAT1.Nuclear export determines the cytokine sensitivity of STAT transcription factors.
P2860
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P2860
A single residue modulates tyrosine dephosphorylation, oligomerization, and nuclear accumulation of stat transcription factors.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
A single residue modulates tyr ...... of stat transcription factors.
@en
A single residue modulates tyr ...... of stat transcription factors.
@nl
type
label
A single residue modulates tyr ...... of stat transcription factors.
@en
A single residue modulates tyr ...... of stat transcription factors.
@nl
prefLabel
A single residue modulates tyr ...... of stat transcription factors.
@en
A single residue modulates tyr ...... of stat transcription factors.
@nl
P2093
P2860
P356
P1476
A single residue modulates tyr ...... of stat transcription factors
@en
P2093
Andreas Begitt
Lisa Hendry
Thomas Meyer
P2860
P304
18998-19007
P356
10.1074/JBC.M400766200
P407
P577
2004-03-09T00:00:00Z