Conformational motions regulate phosphoryl transfer in related protein tyrosine phosphatases.
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Regulation of the catalytic activity of the human phosphatase PTPN4 by its PDZ domainStructural Basis for Autoinhibition of CTP:Phosphocholine Cytidylyltransferase (CCT), the Regulatory Enzyme in Phosphatidylcholine Synthesis, by Its Membrane-binding Amphipathic HelixNitrate in the active site of protein tyrosine phosphatase 1B is a putative mimetic of the transition stateKeep on moving: discovering and perturbing the conformational dynamics of enzymesCoexistence of multiple minor states of fatty acid binding protein and their functional relevanceConservative tryptophan mutants of the protein tyrosine phosphatase YopH exhibit impaired WPD-loop function and crystallize with divanadate esters in their active sitesPopulation shuffling between ground and high energy excited states.An Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis.Exploring protein structure and dynamics through a project-oriented biochemistry laboratory module.Both protein dynamics and ligand concentration can shift the binding mechanism between conformational selection and induced fitEvaluating the uncertainty in exchange parameters determined from off-resonance R1ρ relaxation dispersion for systems in fast exchangeDysfunctional conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation.Mapping the Hydrogen Bond Networks in the Catalytic Subunit of Protein Kinase A Using H/D Fractionation FactorsCofactor-Mediated Conformational Dynamics Promote Product Release From Escherichia coli Dihydrofolate Reductase via an Allosteric Pathway.Substrate-modulated ADP/ATP-transporter dynamics revealed by NMR relaxation dispersion.Linkage between Fitness of Yeast Cells and Adenylate Kinase Catalysis.Reactions of Cg10062, a cis-3-Chloroacrylic Acid Dehalogenase Homologue, with Acetylene and Allene Substrates: Evidence for a Hydration-Dependent Decarboxylation.Enzyme Selectivity Fine-Tuned through Dynamic Control of a LoopDrug design from the cryptic inhibitor envelope.Using NMR spectroscopy to elucidate the role of molecular motions in enzyme functionStructural insight into effector proteins of Gram-negative bacterial pathogens that modulate the phosphoproteome of their host.Kinetic isotope effects in the characterization of catalysis by protein tyrosine phosphatases.Protein dynamics and function from solution state NMR spectroscopy.Recent advances in the development of protein tyrosine phosphatase 1B inhibitors for Type 2 diabetes.Conformational Rigidity and Protein Dynamics at Distinct Timescales Regulate PTP1B Activity and Allostery.Rate Constants and Mechanisms of Protein-Ligand Binding.A designed conformational shift to control protein binding specificity.Complexity of protein energy landscapes studied by solution NMR relaxation dispersion experiments.Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling.Defining the Structural Basis for Allosteric Product Release from E. coli Dihydrofolate Reductase Using NMR Relaxation Dispersion.Characterization of Protein Tyrosine Phosphatase 1B Inhibition by Chlorogenic Acid and Cichoric Acid.Kinetics of the Antibody Recognition Site in the Third IgG-Binding Domain of Protein G.Structural basis for ligand binding to an enzyme by a conformational selection pathway.Engineered control of enzyme structural dynamics and function.Leveraging Reciprocity to Identify and Characterize Unknown Allosteric Sites in Protein Tyrosine Phosphatases.Zinc ions modulate protein tyrosine phosphatase 1B activity.Thermodynamic and NMR Assessment of Ligand Cooperativity and Intersubunit Communication in Symmetric Dimers: Application to Thymidylate Synthase.Structural basis for cross-reactivity and conformation fluctuation of the major beech pollen allergen Fag s 1.An expanded allosteric network in PTP1B by multitemperature crystallography, fragment screening, and covalent tetheringMechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2
P2860
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P2860
Conformational motions regulate phosphoryl transfer in related protein tyrosine phosphatases.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Conformational motions regulat ...... protein tyrosine phosphatases.
@en
type
label
Conformational motions regulat ...... protein tyrosine phosphatases.
@en
prefLabel
Conformational motions regulat ...... protein tyrosine phosphatases.
@en
P2860
P356
P1433
P1476
Conformational motions regulat ...... protein tyrosine phosphatases
@en
P2093
J Patrick Loria
Sean K Whittier
P2860
P304
P356
10.1126/SCIENCE.1241735
P407
P577
2013-08-01T00:00:00Z