Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction.
about
Biological phosphoryl-transfer reactions: understanding mechanism and catalysisRas-catalyzed hydrolysis of GTP: a new perspective from model studiesThe structure of apo protein-tyrosine phosphatase 1B C215S mutant: More than just an S → O changeFunctional characterization and crystal structure of the C215D mutant of protein-tyrosine phosphatase-1BImpaired Acid Catalysis by Mutation of a Protein Loop Hinge Residue in a YopH Mutant Revealed by Crystal StructuresInsights into the Reaction of Protein-tyrosine Phosphatase 1B: CRYSTAL STRUCTURES FOR TRANSITION STATE ANALOGS OF BOTH CATALYTIC STEPSInvestigation of Catalytic Loop Structure, Dynamics, and Function Relationship of Yersinia Protein Tyrosine Phosphatase by Temperature-Jump Relaxation Spectroscopy and X-ray Structural DeterminationThe molecular details of WPD-loop movement differ in the protein-tyrosine phosphatases YopH and PTP1BMolecular Basis of Gain-of-Function LEOPARD Syndrome-Associated SHP2 MutationsThe X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implicationsThe mechanism of GTP hydrolysis by Ras probed by Fourier transform infrared spectroscopy.Isotope effects in the study of enzymatic phosphoryl transfer reactions.Kinetic isotope effects in Ras-catalyzed GTP hydrolysis: evidence for a loose transition state.Using NMR spectroscopy to elucidate the role of molecular motions in enzyme functionVisualization of intermediate and transition-state structures in protein-tyrosine phosphatase catalysisMechanistic study of protein phosphatase-1 (PP1), a catalytically promiscuous enzymeNew functional aspects of the atypical protein tyrosine phosphatase VHZ.Identification of catalytic metal ion ligands in ribozymes.Structural insight into effector proteins of Gram-negative bacterial pathogens that modulate the phosphoproteome of their host.Molecular basis for substrate specificity of protein-tyrosine phosphatase 1B.Kinetic isotope effects in the characterization of catalysis by protein tyrosine phosphatases.The Yersinia tyrosine phosphatase YopH targets a novel adhesion-regulated signalling complex in macrophages.Conformational motions regulate phosphoryl transfer in related protein tyrosine phosphatases.Residue 182 influences the second step of protein-tyrosine phosphatase-mediated catalysis.Probing the function of the conserved tryptophan in the flexible loop of the Yersinia protein-tyrosine phosphatase.Suramin is an active site-directed, reversible, and tight-binding inhibitor of protein-tyrosine phosphatases.RNA molecules that bind to and inhibit the active site of a tyrosine phosphatase.Altering the nucleophile specificity of a protein-tyrosine phosphatase-catalyzed reaction. Probing the function of the invariant glutamine residues.Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis.Metavanadate at the active site of the phosphatase VHZRelation between the flexibility of the WPD loop and the activity of the catalytic domain of protein tyrosine phosphatase SHP-1.The Caenorhabditis elegans mRNA 5'-capping enzyme. In vitro and in vivo characterization.The mechanism of dephosphorylation of extracellular signal-regulated kinase 2 by mitogen-activated protein kinase phosphatase 3.The catalytic mechanism of Cdc25A phosphatase.Kinetic and mechanistic studies of a cell cycle protein phosphatase Cdc14.Regulatory Mechanisms and Novel Therapeutic Targeting Strategies for Protein Tyrosine Phosphatases.Thermodynamic study of ligand binding to protein-tyrosine phosphatase 1B and its substrate-trapping mutants.
P2860
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P2860
Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年学术文章
@wuu
1995年学术文章
@zh-cn
1995年学术文章
@zh-hans
1995年学术文章
@zh-my
1995年学术文章
@zh-sg
1995年學術文章
@yue
1995年學術文章
@zh
1995年學術文章
@zh-hant
name
Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction.
@en
type
label
Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction.
@en
prefLabel
Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction.
@en
P2093
P356
P1433
P1476
Nature of the transition state of the protein-tyrosine phosphatase-catalyzed reaction.
@en
P2093
P304
13982-13987
P356
10.1021/BI00043A003
P407
P577
1995-10-01T00:00:00Z