Identification of a high-affinity phosphopeptide inhibitor of Stat3. (Q44363622)

2 December 2017

Identification of a high-affinity phosphopeptide inhibitor of Stat3. (English)

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2 December 2017

Zhiyong Ren

1

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2 December 2017

Larry A Cabell

series ordinal

2

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2 December 2017

Timothy S Schaefer

series ordinal

3

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2 December 2017

John S McMurray

series ordinal

4

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2 December 2017

language of work or name

English

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publication date

1 February 2003

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Bioorganic & Medicinal Chemistry Letters

2 December 2017

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2 December 2017

13

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2 December 2017

633-636

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2 December 2017

4

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The role of STATs in transcriptional control and their impact on cellular function

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How cells respond to interferons

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c-Src activates the DNA binding and transcriptional activity of Stat3 molecules: serine 727 is not required for transcriptional activation under certain circumstances

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Phosphotyrosyl peptides block Stat3-mediated DNA binding activity, gene regulation, and cell transformation

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Choice of STATs and other substrates specified by modular tyrosine-based motifs in cytokine receptors

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EGF receptor deletions define a region specifically mediating STAT transcription factor activation

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Stat3 recruitment by two distinct ligand-induced, tyrosine-phosphorylated docking sites in the interleukin-10 receptor intracellular domain

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Dimer stability as a determinant of differential DNA binding activity of Stat3 isoforms

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Characterization and binding specificity of the monomeric STAT3-SH2 domain

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Three-dimensional structure of the Stat3beta homodimer bound to DNA

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Synthesis of phosphotyrosine-containing peptides and their use as substrates for protein tyrosine phosphatases.

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Calorimetric investigation of proton linkage by monitoring both the enthalpy and association constant of binding: application to the interaction of the Src SH2 domain with a high-affinity tyrosyl phosphopeptide

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Inhibition of SH2 domain/phosphoprotein association by a nonhydrolyzable phosphonopeptide

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The crystal structures of the SH2 domain of p56lck complexed with two phosphonopeptides suggest a gated peptide binding site

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SH2 domains recognize specific phosphopeptide sequences

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Specific motifs recognized by the SH2 domains of Csk, 3BP2, fps/fes, GRB-2, HCP, SHC, Syk, and Vav

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Pseudoproline-containing analogues of morphiceptin and endomorphin-2: evidence for a cis Tyr-Pro amide bond in the bioactive conformation

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Structure of a specific peptide complex of the carboxy-terminal SH2 domain from the p85 alpha subunit of phosphatidylinositol 3-kinase

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Identifiers

DOI

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2 December 2017

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