Molecular Determinants of Substrate Recognition in Hematopoietic Protein-tyrosine Phosphatase

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New Insights into the Control of MAP Kinase Pathways

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PTP‐SL and STEP protein tyrosine phosphatases regulate the activation of the extracellular signal‐regulated kinases ERK1 and ERK2 by association through a kinase interaction motif

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Identification of an Extracellular Signal-regulated Kinase (ERK) Docking Site in Ribosomal S6 Kinase, a Sequence Critical for Activation by ERK in Vivo

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Visualization of the Cysteinyl-phosphate Intermediate of a Protein-tyrosine Phosphatase by X-ray Crystallography

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The Specificity of Extracellular Signal-regulated Kinase 2 Dephosphorylation by Protein Phosphatases

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Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase

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Molecular characterization of a protein-tyrosine-phosphatase enriched in striatum.

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The Mechanism of Dephosphorylation of Extracellular Signal-regulated Kinase 2 by Mitogen-activated Protein Kinase Phosphatase 3

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A MAP kinase docking site is required for phosphorylation and activation of p90rsk/MAPKAP kinase-1

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Differential regulation of FUS3 MAP kinase by tyrosine-specific phosphatases PTP2/PTP3 and dual-specificity phosphatase MSG5 in Saccharomyces cerevisiae.Preprint

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Mutation of Position 52 in ERK2 Creates a Nonproductive Binding Mode for Adenosine 5‘-Triphosphate,

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Inhibition of T Cell Signaling by Mitogen-activated Protein Kinase-targeted Hematopoietic Tyrosine Phosphatase (HePTP)

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Interdependent Domains Controlling the Enzymatic Activity of Mitogen-Activated Protein Kinase Kinase 1

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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity and Retains ERK2 in the Cytoplasm

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A Continuous Spectrophotometric and Fluorometric Assay for Protein Tyrosine Phosphatase Using Phosphotyrosine-Containing Peptides

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Structural Basis of Plasticity in Protein Tyrosine Phosphatase 1B Substrate Recognition,

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Multiple Regions of MAP Kinase Phosphatase 3 Are Involved in Its Recognition and Activation by ERK2

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Suramin Is an Active Site-directed, Reversible, and Tight-binding Inhibitor of Protein-tyrosine Phosphatases

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Mechanistic Studies on Protein Tyrosine Phosphatases

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Molecular Basis for Substrate Specificity of Protein-tyrosine Phosphatase 1B

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Cloning and expression of an inducible lymphoid‐specific, protein tyrosine phosphatase (HePTPase)

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Docking sites on mitogen-activated protein kinase (MAPK) kinases, MAPK phosphatases and the Elk-1 transcription factor compete for MAPK binding and are crucial for enzymic activity

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Substrate Recognition Domains within Extracellular Signal-regulated Kinase Mediate Binding and Catalytic Activation of Mitogen-activated Protein Kinase Phosphatase-3

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A Bipartite Mechanism for ERK2 Recognition by Its Cognate Regulators and Substrates

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Mechanistic Basis for Catalytic Activation of Mitogen-activated Protein Kinase Phosphatase 3 by Extracellular Signal-regulated Kinase

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Design and Characterization of an Improved Protein Tyrosine Phosphatase Substrate-Trapping Mutant

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Negative Regulation of T Cell Antigen Receptor Signal Transduction by Hematopoietic Tyrosine Phosphatase (HePTP)

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PTP-ER, a Novel Tyrosine Phosphatase, Functions Downstream of Ras1 to Downregulate MAP Kinase during Drosophila Eye Development

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Mechanism of Mitogen-activated Protein Kinase Phosphatase-3 Activation by ERK2

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Altering the Nucleophile Specificity of a Protein-tyrosine Phosphatase-catalyzed Reaction

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Tyrosine-Phosphorylated Extracellular Signal–Regulated Kinase Associates with the Golgi Complex during G2/M Phase of the Cell Cycle

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The Activity of the Extracellular Signal-regulated Kinase 2 Is Regulated by Differential Phosphorylation in the Activation Loop

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Probing the function of the conserved tryptophan in the flexible loop of the Yersinia protein‐tyrosine phosphatase

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Thermodynamic Study of Ligand Binding to Protein-tyrosine Phosphatase 1B and Its Substrate-trapping Mutants

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cDNA Cloning and Characterization of a Novel Receptor-type Protein Tyrosine Phosphatase Expressed Predominantly in the Brain

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Detection of partially phosphorylated forms of ERK by monoclonal antibodies reveals spatial regulation of ERK activity by phosphatases

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The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP

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Direct Suppression of TCR-Mediated Activation of Extracellular Signal-Regulated Kinase by Leukocyte Protein Tyrosine Phosphatase, a Tyrosine-Specific Phosphatase

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Distinct, Constitutively Active MAPK Phosphatases Function inXenopusOocytes: Implications for p42 MAPK Regulation In Vivo

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Residue 182 influences the second step of protein-tyrosine phosphatase-mediated catalysis

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Crystal structure of PTP-SL/PTPBR7 catalytic domain: implications for map kinase regulation 1 1Edited by D. Rees

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A Kinetic Approach for the Study of Protein Phosphatase-Catalyzed Regulation of Protein Kinase Activity

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MAP kinases and the control of nuclear events

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Specificity of Linear Motifs That Bind to a Common Mitogen-Activated Protein Kinase Docking Groove

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Docking Interactions Induce Exposure of Activation Loop in the MAP Kinase ERK2

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Protein Tyrosine Phosphatases: Structure, Function, and Implication in Human Disease

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Structural basis of docking interactions between ERK2 and MAP kinase phosphatase 3

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The catalytic region and PEST domain of PTPN18 distinctly regulate the HER2 phosphorylation and ubiquitination barcodes

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Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases

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MAPK-directed phosphatases preferentially regulate pro- and anti-inflammatory cytokines in experimental visceral leishmaniasis: involvement of distinct protein kinase C isoforms

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The MAP kinase ERK5 binds to and phosphorylates p90 RSK

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MAPK-specific tyrosine phosphatases: new targets for drug discovery?

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Diverse Levels of Sequence Selectivity and Catalytic Efficiency of Protein-Tyrosine Phosphatases

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Preferential redox regulation of cysteine‐based protein tyrosine phosphatases: structural and biochemical diversity

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Structure of the Hematopoietic Tyrosine Phosphatase (HePTP) Catalytic Domain: Structure of a KIM Phosphatase with Phosphate Bound at the Active Site

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Macrophages Survive Hyperoxia via Prolonged ERK Activation Due to Phosphatase Down-regulation

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Molecular mechanism of ERK dephosphorylation by striatal‐enriched protein tyrosine phosphatase

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Metal‐dependent protein phosphatase 1A functions as an extracellular signal‐regulated kinase phosphatase

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The catalytic role of the M2 metal ion in PP2Cα

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Protein Tyrosine Phosphatases: A new paradigm in an old signaling system?

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Reciprocal allosteric regulation of p38γ and PTPN3 involves a PDZ domain–modulated complex formation

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Structural Basis of Substrate Recognition by Hematopoietic Tyrosine Phosphatase,

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ERK2 Shows a Restrictive and Locally Selective Mechanism of Recognition by Its Tyrosine Phosphatase Inactivators Not Shared by Its Activator MEK1

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Phosphatase High-Throughput Screening Assay Design and Selection

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Molecular Basis for Phosphate Signaling by Prokaryotic and Eukaryotic Phosphatases

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A Kinetic Approach for the Study of Protein Phosphatase-Catalyzed Regulation of Protein Kinase Activity

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Structure of the Hematopoietic Tyrosine Phosphatase (HePTP) Catalytic Domain: Structure of a KIM Phosphatase with Phosphate Bound at the Active Site

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Structural Basis of Substrate Recognition by Hematopoietic Tyrosine Phosphatase,

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Structure ofEscherichia colityrosine kinase Etk reveals novel activation mechanism

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Crystal structure of human ERK1 kinase monophosphorylated at Tyr204

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