Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domain. - Wikidata - awgldk - TriplyDB

Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domain.

Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domain.

http://www.wikidata.org/entity/Q41073163

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Tyrosine phosphorylation regulates the partitioning of STAT1 between different dimer conformations Host Intracellular Signaling Events and Pro-inflammatory Cytokine Production in African Trypanosomiasis Inborn errors of human STAT1: allelic heterogeneity governs the diversity of immunological and infectious phenotypes Protein tyrosine phosphatases as wardens of STAT signaling Inducible, dose-adjustable and time-restricted reconstitution of STAT1 deficiency in vivo Dimeric Quaternary Structure of the Prototypical Dual Specificity Phosphatase VH1 Structural and functional studies of STAT1 from Atlantic salmon (Salmo salar).Characterization of a dominant-active STAT that promotes tumorigenesis in Drosophila.Acetylation modulates prolactin receptor dimerization.Two glutamic acid residues in the DNA-binding domain are engaged in the release of STAT1 dimers from DNA.A novel form of human STAT1 deficiency impairing early but not late responses to interferons.Jak/STAT pathways in cytokine signaling and myeloproliferative disorders: approaches for targeted therapies.A fusion cytokine coupling GMCSF to IL9 induces heterologous receptor clustering and STAT1 hyperactivation through JAK2 promiscuity.Clinically relevant dimer interface mutants of STAT1 transcription factor exhibit differential gene expression.Promoter occupancy of STAT1 in interferon responses is regulated by processive transcription.Adenovirus sequesters phosphorylated STAT1 at viral replication centers and inhibits STAT dephosphorylation.Gain-of-function human STAT1 mutations impair IL-17 immunity and underlie chronic mucocutaneous candidiasis.A conserved motif in the linker domain of STAT1 transcription factor is required for both recognition and release from high-affinity DNA-binding sites The two faces of interferon-γ in cancer.DNA binding reduces the dissociation rate of STAT1 dimers and impairs the interdimeric exchange of protomers.IκB kinase epsilon (IKK(epsilon)) regulates the balance between type I and type II interferon responses.Dietary compounds as potent inhibitors of the signal transducers and activators of transcription (STAT) 3 regulatory network.Impact of the N-Terminal Domain of STAT3 in STAT3-Dependent Transcriptional Activity STAT5 requires the N-domain to maintain hematopoietic stem cell repopulating function and appropriate lymphoid-myeloid lineage output.Structural Basis of the Inhibition of STAT1 Activity by Sendai Virus C Protein.Identification of STAT2 serine 287 as a novel regulatory phosphorylation site in type I interferon-induced cellular responses Recruitment of Stat1 to chromatin is required for interferon-induced serine phosphorylation of Stat1 transactivation domain Wedelolactone, a naturally occurring coumestan, enhances interferon-γ signaling through inhibiting STAT1 protein dephosphorylation.STAT nuclear translocation: potential for pharmacological intervention.Understanding signaling cascades in melanoma Roles of unphosphorylated STATs in signaling.New and recurrent gain-of-function STAT1 mutations in patients with chronic mucocutaneous candidiasis from Eastern and Central Europe.Biology and significance of the JAK/STAT signalling pathways.Inteferons pen the JAK-STAT pathway.Novel non-canonical role of STAT1 in Natural Killer cell cytotoxicity.Cross-regulation of signaling pathways by interferon-gamma: implications for immune responses and autoimmune diseases.STAT1 and IRF8 in Vascular Inflammation and Cardiovascular Disease: Diagnostic and Therapeutic Potential.Negative regulation of type I IFN signaling by phosphorylation of STAT2 on T387.Molecular mechanism and structural basis of gain-of-function of STAT1 caused by pathogenic R274Q mutation.Protective effect of wogonin on proinflammatory cytokine generation via Jak1/3-STAT1/3 pathway in lipopolysaccharide stimulated BV2 microglial cells.

P2860

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P2860

Dephosphorylation of phosphotyrosine on STAT1 dimers requires extensive spatial reorientation of the monomers facilitated by the N-terminal domain.

http://www.wikidata.org/entity/Q41073163

description

2006 nî lūn-bûn

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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2006年论文

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2006年论文

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name

Dephosphorylation of phosphoty ...... ated by the N-terminal domain.

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Dephosphorylation of phosphoty ...... ated by the N-terminal domain.

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Dephosphorylation of phosphoty ...... ated by the N-terminal domain.

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Genes & Development

P1476

Dephosphorylation of phosphoty ...... ated by the N-terminal domain.

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P2093

Claudia Mertens

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

James E Darnell

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Minghao Zhong

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Ravi Krishnaraj

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Wenxin Zou

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Xiaomin Chen

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P2860

Signal Transduction and the Control of Gene Expression

A phosphotyrosine displacement mechanism for activation of Src by PTPalpha

Structural bases of unphosphorylated STAT1 association and receptor binding

Identification of a nuclear Stat1 protein tyrosine phosphatase

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

Domain alternation switches B(12)-dependent methionine synthase to the activation conformation

Structures of the N-terminal modules imply large domain motions during catalysis by methionine synthase

Structure of the amino-terminal protein interaction domain of STAT-4

Three-dimensional structure of the Stat3beta homodimer bound to DNA

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

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3372-3381

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10.1101/GAD.1485406

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24

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20

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2006-12-01T00:00:00Z

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1698445

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