Structural bases of unphosphorylated STAT1 association and receptor binding (Q24298555)

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Gregory N Parker

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Michael A Pastorello

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Wei Wang

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John S McMurray

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James E Darnell

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Xiaomin Chen

STAT3 forms stable homodimers in the presence of divalent cations prior to activation.

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language of work or name

English

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publication date

18 March 2005

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761-71

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

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Stat recruitment by tyrosine-phosphorylated cytokine receptors: an ordered reversible affinity-driven process

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Sedimentation velocity analysis of highly heterogeneous systems.

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Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques

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STAT proteins: signal tranducers and activators of transcription

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Processing of X-ray diffraction data collected in oscillation mode

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

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Cytokine signaling in 2002: new surprises in the Jak/Stat pathway

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Observation of an unexpected third receptor molecule in the crystal structure of human interferon-gamma receptor complex

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The structure and activity of a monomeric interferon-gamma:alpha-chain receptor signaling complex

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Structure of an activated Dictyostelium STAT in its DNA-unbound form

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Three-dimensional structure of the Stat3beta homodimer bound to DNA

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Crystal structure of a complex between interferon-gamma and its soluble high-affinity receptor

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N-domain-dependent nonphosphorylated STAT4 dimers required for cytokine-driven activation

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Stats: transcriptional control and biological impact

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Cytoplasmic STAT proteins associate prior to activation.

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Preassociation of STAT1 with STAT2 and STAT3 in separate signalling complexes prior to cytokine stimulation

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The amino-terminal domain of human STAT4. Overproduction, purification, and biophysical characterization.

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Cellular physiology of STAT3: Where's the cytoplasmic monomer?

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STATs dimerize in the absence of phosphorylation

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A single residue modulates tyrosine dephosphorylation, oligomerization, and nuclear accumulation of stat transcription factors.

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Constitutive and IFN-gamma-induced nuclear import of STAT1 proceed through independent pathways

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Regulated nuclear import of the STAT1 transcription factor by direct binding of importin-alpha

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Improved methods for building protein models in electron density maps and the location of errors in these models

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Methods used in the structure determination of bovine mitochondrial F1 ATPase

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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

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A reinterpretation of the dimerization interface of the N-terminal domains of STATs

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STATs and Gene Regulation

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

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