Dissociation time from DNA determines transcriptional function in a STAT1 linker mutant. - Wikidata - wikimedia - TriplyDB

Dissociation time from DNA determines transcriptional function in a STAT1 linker mutant.

Dissociation time from DNA determines transcriptional function in a STAT1 linker mutant.

http://www.wikidata.org/entity/Q40752172

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Inborn errors of human STAT1: allelic heterogeneity governs the diversity of immunological and infectious phenotypes Structural Basis of HIV-1 Activation by NF-κB—A Higher-Order Complex of p50:RelA Bound to the HIV-1 LTR Signal transducer and activator of transcription 5A/B in prostate and breast cancers Systematic characterization of the zinc-finger-containing proteins in the mouse transcriptome.Implications of an antiparallel dimeric structure of nonphosphorylated STAT1 for the activation-inactivation cycle.Characterization of a dominant-active STAT that promotes tumorigenesis in Drosophila.The DNA replication factor MCM5 is essential for Stat1-mediated transcriptional activation.Rapid GAL gene switch of Saccharomyces cerevisiae depends on nuclear Gal3, not nucleocytoplasmic trafficking of Gal3 and Gal80 Two glutamic acid residues in the DNA-binding domain are engaged in the release of STAT1 dimers from DNA.Structural and functional characterization of salmon STAT1, STAT2 and IRF9 homologs sheds light on interferon signaling in teleosts Transcription factor Stat5a/b as a therapeutic target protein for prostate cancer.A conserved motif in the linker domain of STAT1 transcription factor is required for both recognition and release from high-affinity DNA-binding sites Phosphorylation of the Gal4 DNA-binding domain is essential for activator mono-ubiquitylation and efficient promoter occupancy.Signal transducers and activators of transcription: insights into the molecular basis of oral cancer.DNA binding controls inactivation and nuclear accumulation of the transcription factor Stat1.ephrinB1 signals from the cell surface to the nucleus by recruitment of STAT3.Phosphorylation and an ATP-dependent process increase the dynamic exchange of H1 in chromatin.Mutations in the linker domain affect phospho-STAT3 function and suggest targets for interrupting STAT3 activity.Recruitment of Stat1 to chromatin is required for interferon-induced serine phosphorylation of Stat1 transactivation domain STAT nuclear translocation: potential for pharmacological intervention.Analysis of TFAP2A mutations in Branchio-Oculo-Facial Syndrome indicates functional complexity within the AP-2α DNA-binding domain Non-proteolytic regulation of p53-mediated transcription through destabilization of the activator.promoter complex by the proteasomal ATPases.Identification of the nuclear export signal and STAT-binding domains of the Nipah virus V protein reveals mechanisms underlying interferon evasion.Acetylation of Stat1 modulates NF-kappaB activity The conserved Leu-724 residue is required for both serine phosphorylation and co-activator recruitment for Stat1-mediated transcription activation in response to interferon-gamma.Functional relevance of the conserved DNA-binding domain of STAT2.The role of stat1b in zebrafish hematopoiesis.Signal transducer and activator of transcription 1 negatively regulates constitutive gamma interferon-inducible lysosomal thiol reductase expression.The minichromosome maintenance proteins 2-7 (MCM2-7) are necessary for RNA polymerase II (Pol II)-mediated transcription.Simian varicella virus inhibits the interferon gamma signalling pathway.Regulation of Stat1 protein expression by phenylalanine 172 in the coiled-coil domain.A rapid conformational rearrangement of STAT1 dimers is required for termination rather than for amplification of interferon-γ signaling.Dynamics of the hypoxia-inducible factor-1-vascular endothelial growth factor promoter complex.Independent and cooperative activation of chromosomal c-fos promoter by STAT3.Distinct transcriptional activation functions of STAT1alpha and STAT1beta on DNA and chromatin templates.Modification of the Stat1 SH2 domain broadly improves interferon efficacy in proportion to p300/CREB-binding protein coactivator recruitment.[Advances of the correlation between JAK-STAT3 signaling pathway and the biological behavior of non-small cell lung cancer].

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P2860

Dissociation time from DNA determines transcriptional function in a STAT1 linker mutant.

http://www.wikidata.org/entity/Q40752172

description

2002 nî lūn-bûn

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2002年の論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

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2002年論文

@zh-tw

2002年论文

@wuu

2002年论文

@zh

2002年论文

@zh-cn

name

Dissociation time from DNA determines transcriptional function in a STAT1 linker mutant.

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type

label

Dissociation time from DNA determines transcriptional function in a STAT1 linker mutant.

@en

prefLabel

Dissociation time from DNA determines transcriptional function in a STAT1 linker mutant.

@en

P1433

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Journal of Biological Chemistry

P1476

Dissociation time from DNA determines transcriptional function in a STAT1 linker mutant.

@en

P2093

Edward Yang

http://www.w3.org/2001/XMLSchema#string

James E Darnell

http://www.w3.org/2001/XMLSchema#string

Melissa A Henriksen

http://www.w3.org/2001/XMLSchema#string

Natalia Zakharova

http://www.w3.org/2001/XMLSchema#string

Olaf Schaefer

http://www.w3.org/2001/XMLSchema#string

P2860

Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA

Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei

How cells respond to interferons

Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions

Regulation of hormone-induced histone hyperacetylation and gene activation via acetylation of an acetylase

The lac repressor-operator interaction. 3. Kinetic studies

STATs and gene regulation

Ordered recruitment of chromatin modifying and general transcription factors to the IFN-beta promoter

Kinetics of p53 binding to promoter sites in vivo.

A single amino acid substitution in the v-Eyk intracellular domain results in activation of Stat3 and enhances cellular transformation.

P304

13455-13462

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scholarly article

P356

10.1074/JBC.M112038200

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16

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277

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2002-02-07T00:00:00Z

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11834743

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