Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: a model for changes in dynamics upon target binding.
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[1] P. Bernadó,et al. Interpretation of 15N NMR relaxation data of globular proteins using hydrodynamic calculations with HYDRONMR , 2002, Journal of biomolecular NMR.
[2] B. Sykes,et al. Structure, dynamics, and thermodynamics of the structural domain of troponin C in complex with the regulatory peptide 1-40 of troponin I. , 2001, Biochemistry.
[3] J. Brender,et al. Functional dynamics in the active site of the ribonuclease binase , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[4] V. Orekhov,et al. NMR study of monomer-dimer equilibrium of barstar in solution. , 2001, Journal of the American Chemical Society.
[5] R. Ellis,et al. Macromolecular crowding: an important but neglected aspect of the intracellular environment. , 2001, Current opinion in structural biology.
[6] J. García de la Torre,et al. HYDRONMR: prediction of NMR relaxation of globular proteins from atomic-level structures and hydrodynamic calculations. , 2000, Journal of magnetic resonance.
[7] 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.
[8] J. L. Goodman,et al. Relationships between protein structure and dynamics from a database of NMR-derived backbone order parameters. , 2000, Journal of molecular biology.
[9] L. Tabernero,et al. The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism. , 1999, Biochemistry.
[10] P. Driscoll,et al. NMR exchange broadening arising from specific low affinity protein self-association: Analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1 , 1999, Journal of biomolecular NMR.
[11] A G Marshall,et al. Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. , 1998, Biochemistry.
[12] N. Tjandra,et al. Direct Measurement of 15N Chemical Shift Anisotropy in Solution , 1998 .
[13] Marie Zhang,et al. Crystal Structure of a Human Low Molecular Weight Phosphotyrosyl Phosphatase , 1998, The Journal of Biological Chemistry.
[14] C. Kroenke,et al. Longitudinal and Transverse 1H−15N Dipolar/15N Chemical Shift Anisotropy Relaxation Interference: Unambiguous Determination of Rotational Diffusion Tensors and Chemical Exchange Effects in Biological Macromolecules , 1998 .
[15] V. Krishnan,et al. An empirical relationship between rotational correlation time and solvent accessible surface area , 1998, Journal of biomolecular NMR.
[16] A. Lane,et al. Eph receptors discriminate specific ligand oligomers to determine alternative signaling complexes, attachment, and assembly responses. , 1998, Genes & development.
[17] S. Opella,et al. Magnitudes and Orientations of the Principal Elements of the 1H Chemical Shift, 1H−15N Dipolar Coupling, and 15N Chemical Shift Interaction Tensors in 15Nε1-Tryptophan and 15Nπ-Histidine Side Chains Determined by Three-Dimensional Solid-State NMR Spectroscopy of Polycrystalline Samples , 1997 .
[18] G. Ramponi,et al. LMW-PTP is a negative regulator of insulin-mediated mitotic and metabolic signalling. , 1997, Biochemical and biophysical research communications.
[19] K Wüthrich,et al. The NMR solution conformation of unligated human cyclophilin A. , 1997, Journal of molecular biology.
[20] A. Palmer,et al. Rotational diffusion anisotropy of proteins from simultaneous analysis of 15N and 13Cα nuclear spin relaxation , 1997, Journal of biomolecular NMR.
[21] T. Mustelin,et al. Regulation of the Low Molecular Weight Phosphotyrosine Phosphatase by Phosphorylation at Tyrosines 131 and 132* , 1997, The Journal of Biological Chemistry.
[22] Z. Zhang,et al. Rapid loop dynamics of Yersinia protein tyrosine phosphatases. , 1997, Biochemistry.
[23] D. Cowburn,et al. The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration. , 1997, Journal of molecular biology.
[24] G. Ramponi,et al. Structural, catalytic, and functional properties of low M(r), phosphotyrosine protein phosphatases. Evidence of a long evolutionary history. , 1997, The international journal of biochemistry & cell biology.
[25] M. Zhou,et al. Crystal structure of bovine low molecular weight phosphotyrosyl phosphatase complexed with the transition state analog vanadate. , 1997, Biochemistry.
[26] B. Neel,et al. From Form to Function: Signaling by Protein Tyrosine Phosphatases , 1996, Cell.
[27] Ad Bax,et al. Protein Backbone Dynamics and 15N Chemical Shift Anisotropy from Quantitative Measurement of Relaxation Interference Effects , 1996 .
[28] G. Ramponi,et al. The Molecular Basis of the Differing Kinetic Behavior of the Two Low Molecular Mass Phosphotyrosine Protein Phosphatase Isoforms (*) , 1996, The Journal of Biological Chemistry.
[29] M. Billeter,et al. MOLMOL: a program for display and analysis of macromolecular structures. , 1996, Journal of molecular graphics.
[30] M. Bucciantini,et al. pp60 Phosphorylates and Activates Low Molecular Weight Phosphotyrosine-protein Phosphatase (*) , 1996, The Journal of Biological Chemistry.
[31] D. Barford,et al. Protein tyrosine phosphatases take off , 1995, Nature Structural Biology.
[32] J. Cavanagh. Protein NMR Spectroscopy: Principles and Practice , 1995 .
[33] S. Grzesiek,et al. NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.
[34] P. Wright,et al. Dynamics of the dihydrofolate reductase-folate complex: catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features. , 1995, Biochemistry.
[35] E. Fauman,et al. A ligand‐induced conformational change in the yersinia protein tyrosine phosphatase , 1995, Protein science : a publication of the Protein Society.
[36] D. Barford,et al. Structural basis for phosphotyrosine peptide recognition by protein tyrosine phosphatase 1B. , 1995, Science.
[37] A. Palmer,et al. Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme. , 1995, Journal of molecular biology.
[38] T. Hunter,et al. Protein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling , 1995, Cell.
[39] J. Michael Schurr,et al. A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization. , 1994, Journal of magnetic resonance. Series B.
[40] Z. Zhang,et al. Asp129 of low molecular weight protein tyrosine phosphatase is involved in leaving group protonation. , 1994, The Journal of biological chemistry.
[41] T. Logan,et al. Solution structure of a low molecular weight protein tyrosine phosphatase. , 1994, Biochemistry.
[42] Marie Zhang,et al. Crystal structure of bovine heart phosphotyrosyl phosphatase at 2.2-A resolution. , 1994, Biochemistry.
[43] Bruce A. Johnson,et al. NMR View: A computer program for the visualization and analysis of NMR data , 1994, Journal of biomolecular NMR.
[44] P. Nordlund,et al. The crystal structure of a low-molecular-weight phosphotyrosine protein phosphatase , 1994, Nature.
[45] E. Fauman,et al. Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 Å and the complex with tungstate , 1994, Nature.
[46] D. G. Davis,et al. Direct measurements of the dissociation-rate constant for inhibitor-enzyme complexes via the T1 rho and T2 (CPMG) methods. , 1994, Journal of magnetic resonance. Series B.
[47] T. Pawson,et al. Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation. , 1994, Biochemistry.
[48] Y. Thériault,et al. Backbone 1H, 13C, and 15N assignments and secondary structure of bovine low molecular weight phosphotyrosyl protein phosphatase. , 1994, Biochemistry.
[49] E. Oldfield,et al. Correlation between 15N NMR chemical shifts in proteins and secondary structure , 1994, Journal of biomolecular NMR.
[50] E. Oldfield,et al. Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach. , 1993, Science.
[51] A. Palmer,et al. Backbone dynamics of calcium-loaded calbindin D9k studied by two-dimensional proton-detected 15N NMR spectroscopy. , 1992, Biochemistry.
[52] J. Shabanowitz,et al. Sequencing, cloning, and expression of human red cell-type acid phosphatase, a cytoplasmic phosphotyrosyl protein phosphatase. , 1992, The Journal of biological chemistry.
[53] M H Saier,et al. Backbone dynamics of the Bacillus subtilis glucose permease IIA domain determined from 15N NMR relaxation measurements. , 1992, Biochemistry.
[54] H. Erickson,et al. Kinetics of protein-protein association explained by Brownian dynamics computer simulation. , 1992, Proceedings of the National Academy of Sciences of the United States of America.
[55] Ming-Ming Zhou,et al. Cloning, expression, and catalytic mechanism of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart. , 1992, Biochemistry.
[56] P. Wright,et al. Intramolecular motions of a zinc finger DNA-binding domain from Xfin characterized by proton-detected natural abundance carbon-13 heteronuclear NMR spectroscopy , 1991 .
[57] Z. Zhang,et al. Pre-steady-state and steady-state kinetic analysis of the low molecular weight phosphotyrosyl protein phosphatase from bovine heart. , 1991, The Journal of biological chemistry.
[58] Z. Zhang,et al. Purification and characterization of a low-molecular-weight acid phosphatase--a phosphotyrosyl-protein phosphatase from bovine heart. , 1990, Archives of biochemistry and biophysics.
[59] William H. Press,et al. Numerical recipes , 1990 .
[60] I. Campbell,et al. Comparison of techniques for 1H-detected heteronuclear 1H15N Spectroscopy , 1990 .
[61] L. Kay,et al. Comparison of different modes of two-dimensional reverse-correlation NMR for the study of proteins , 1990 .
[62] L. Kay,et al. Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. , 1989, Biochemistry.
[63] Y. Wo,et al. Purification and physicochemical characterization of a human placental acid phosphatase possessing phosphotyrosyl protein phosphatase activity. , 1988, Biochemistry.
[64] W. Press,et al. Numerical recipes in C. The art of scientific computing , 1987 .
[65] Jay L. Devore,et al. Probability and statistics for engineering and the sciences , 1982 .
[66] H. Wennerström. Nuclear magnetic relaxation induced by chemical exchange , 1972 .
[67] R. Heinrikson. Purification and characterization of a low molecular weight acid phosphatase from bovine liver. , 1969, The Journal of biological chemistry.
[68] S. Meiboom,et al. Nuclear Magnetic Resonance Study of the Protolysis of Trimethylammonium Ion in Aqueous Solution—Order of the Reaction with Respect to Solvent , 1963 .
[69] J. Hus,et al. Efficient analysis of macromolecular rotational diffusion from heteronuclear relaxation data , 2000, Journal of biomolecular NMR.
[70] J. Åqvist,et al. Computational modeling of catalysis and binding in low‐molecular‐weight protein tyrosine phosphatase , 1999 .
[71] Z. Zhang,et al. Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis. , 1998, Critical reviews in biochemistry and molecular biology.
[72] R. Richards,et al. A general two-site solution for the chemical exchange produced dependence of T2 upon the carr-Purcell pulse separation , 1972 .