Structural mechanism of oxidative regulation of the phosphatase Cdc25B via an intramolecular disulfide bond.
暂无分享,去创建一个
Carla Mattos | Jungsan Sohn | J. Rudolph | C. Mattos | G. Buhrman | J. Sohn | Johannes Rudolph | Greg Buhrman | Benjamin Parker | B. Parker
[1] D. Barford,et al. Visualization of the Cysteinyl-phosphate Intermediate of a Protein-tyrosine Phosphatase by X-ray Crystallography* , 1998, The Journal of Biological Chemistry.
[2] Michael P. Myers,et al. Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate , 2003, Nature.
[3] D O Morgan,et al. Cyclin-dependent kinases: engines, clocks, and microprocessors. , 1997, Annual review of cell and developmental biology.
[4] Woojin Jeong,et al. Reversible Inactivation of the Tumor Suppressor PTEN by H2O2 * , 2002, The Journal of Biological Chemistry.
[5] L. Johnson,et al. Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with phosphoCDK2. , 2001, Molecular cell.
[6] J. Rudolph,et al. Catalytic and chemical competence of regulation of cdc25 phosphatase by oxidation/reduction. , 2003, Biochemistry.
[7] J. Rudolph,et al. Catalytic mechanism of Cdc25. , 2002, Biochemistry.
[8] Terrence R. Burke,et al. Thermodynamic Study of Ligand Binding to Protein-tyrosine Phosphatase 1B and Its Substrate-trapping Mutants* , 2000, The Journal of Biological Chemistry.
[9] J. Rudolph,et al. Cdc25 phosphatases and cancer. , 2004, Chemistry & biology.
[10] Ian W. Davis,et al. Structure validation by Cα geometry: ϕ,ψ and Cβ deviation , 2003, Proteins.
[11] Axel T. Brunger,et al. Free R value: cross-validation in crystallography. , 1997 .
[12] J. Rudolph,et al. Dual-specific Cdc25B phosphatase: in search of the catalytic acid. , 2000, Biochemistry.
[13] K D Watenpaugh,et al. Crystal structure of the catalytic subunit of Cdc25B required for G2/M phase transition of the cell cycle. , 1999, Journal of molecular biology.
[14] Toshiyuki Fukada,et al. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. , 2002, Molecular cell.
[15] U. Strausfeld,et al. Dephosphorylation and activation of a p34cdc2/cyclin B complex in vitro by human CDC25 protein , 1991, Nature.
[16] B. Kennedy,et al. The structure of apo protein‐tyrosine phosphatase 1B C215S mutant: More than just an S → O change , 2001, Protein science : a publication of the Protein Society.
[17] S. Rhee. Redox signaling: hydrogen peroxide as intracellular messenger , 1999, Experimental & Molecular Medicine.
[18] Joanne I. Yeh,et al. Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation. , 1999, Biochemistry.
[19] Miles Congreve,et al. Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B , 2003, Nature.
[20] E. Fauman,et al. Crystal Structure of the Catalytic Domain of the Human Cell Cycle Control Phosphatase, Cdc25A , 1998, Cell.
[21] J. Denu,et al. Molecular Reactions of Protein PhosphatasesInsights from Structure and Chemistry , 2001 .
[22] E. Giannoni,et al. Two Vicinal Cysteines Confer a Peculiar Redox Regulation to Low Molecular Weight Protein Tyrosine Phosphatase in Response to Platelet-derived Growth Factor Receptor Stimulation* , 2001, The Journal of Biological Chemistry.
[23] J. Denu,et al. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implications for redox regulation. , 1998, Biochemistry.
[24] T. A. Jones,et al. Databases in protein crystallography. , 1998, Acta crystallographica. Section D, Biological crystallography.
[25] L. Tabernero,et al. Crystal structures of a low-molecular weight protein tyrosine phosphatase from Saccharomyces cerevisiae and its complex with the substrate p-nitrophenyl phosphate. , 2000, Biochemistry.
[26] H. Edelsbrunner,et al. Anatomy of protein pockets and cavities: Measurement of binding site geometry and implications for ligand design , 1998, Protein science : a publication of the Protein Society.
[27] J. Rudolph,et al. Specificity of natural and artificial substrates for human Cdc25A. , 2001, Analytical biochemistry.
[28] T. Finkel. Redox‐dependent signal transduction , 2000, FEBS letters.
[29] J. Zou,et al. Improved methods for building protein models in electron density maps and the location of errors in these models. , 1991, Acta crystallographica. Section A, Foundations of crystallography.
[30] T. Finkel,et al. Redox Regulation of Cdc25C* , 2002, The Journal of Biological Chemistry.
[31] G. Storz,et al. Redox regulation of OxyR requires specific disulfide bond formation involving a rapid kinetic reaction path , 2004, Nature Structural &Molecular Biology.
[32] B. Neel,et al. Combinatorial control of the specificity of protein tyrosine phosphatases. , 2001, Current opinion in cell biology.
[33] J. Dixon,et al. Active site labeling of the Yersinia protein tyrosine phosphatase: the determination of the pKa of the active site cysteine and the function of the conserved histidine 402. , 1993, Biochemistry.
[34] O. Olsen,et al. Electrostatic evaluation of the signature motif (H/V)CX5R(S/T) in protein-tyrosine phosphatases. , 1998, Biochemistry.
[35] L. Oberley,et al. Discrete Generation of Superoxide and Hydrogen Peroxide by T Cell Receptor Stimulation , 2002, The Journal of experimental medicine.