2013
Substrate-Based Fragment Identification for the Development of Selective, Nonpeptidic Inhibitors of Striatal-Enriched Protein Tyrosine Phosphatase
Baguley TD, Xu HC, Chatterjee M, Nairn AC, Lombroso PJ, Ellman JA. Substrate-Based Fragment Identification for the Development of Selective, Nonpeptidic Inhibitors of Striatal-Enriched Protein Tyrosine Phosphatase. Journal Of Medicinal Chemistry 2013, 56: 7636-7650. PMID: 24083656, PMCID: PMC3875168, DOI: 10.1021/jm401037h.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBiphenyl CompoundsBlood-Brain BarrierBoronic AcidsCells, CulturedCerebral CortexHumansNeuronsPermeabilityPhosphorous AcidsProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleySmall Molecule LibrariesStereoisomerismStructure-Activity RelationshipSubstrate SpecificityConceptsSubstrate Activity ScreeningProtein tyrosine phosphatase activityProtein tyrosine phosphataseTyrosine phosphatase activityGlutamate receptor internalizationOptimization of fragmentsTyrosine phosphataseDual specificityReceptor internalizationDevelopment of SelectiveSTEP inhibitorPhosphatase activityAlzheimer's diseaseIonotropic glutamate receptorsSubstrate-based approachNonpeptidic inhibitorsPotential targetAD mouse modelDrug discoveryRat cortical neuronsActivity screeningCortical neuronsGlutamate receptorsMouse modelNeuropsychiatric disorders
2002
Stat6 and IRS-2 Cooperate in Interleukin 4 (IL-4)-Induced Proliferation and Differentiation but Are Dispensable for IL-4-Dependent Rescue from Apoptosis
Wurster A, Withers D, Uchida T, White M, Grusby M. Stat6 and IRS-2 Cooperate in Interleukin 4 (IL-4)-Induced Proliferation and Differentiation but Are Dispensable for IL-4-Dependent Rescue from Apoptosis. Molecular And Cellular Biology 2002, 22: 117-126. PMID: 11739727, PMCID: PMC134231, DOI: 10.1128/mcb.22.1.117-126.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisCell Cycle ProteinsCell DifferentiationCell DivisionCell SeparationCells, CulturedCyclin-Dependent Kinase Inhibitor p27Enzyme InhibitorsFlow CytometryInsulin Receptor Substrate ProteinsInterleukin-4Intracellular Signaling Peptides and ProteinsMiceMice, KnockoutPhosphatidylinositol 3-KinasesPhosphoproteinsSignal TransductionSTAT6 Transcription FactorTh2 CellsT-LymphocytesTrans-ActivatorsTumor Suppressor ProteinsConceptsIRS-2Protein tyrosine phosphatase activityProtein tyrosine phosphatase inhibitorTyrosine phosphatase activityTyrosine phosphatase inhibitorWild-type cellsIL-4 signal transductionIRS-2 expressionIL-4-induced proliferationCDK inhibitor p27Kip1Antiapoptotic effectPrimary T cellsPhosphatase inhibitorCytoplasmic tailSignal transductionDifferentiation eventsCooperative regulationGene expressionAntiapoptotic signalsCell developmentAntiapoptotic activityInterleukin-4 receptorPhosphatase activityPrimary lymphocytesSTAT6
1999
Differential Modulation of the Tyrosine Phosphorylation State of the Insulin Receptor by IRS (Insulin Receptor Subunit) Proteins
Solow B, Harada S, Goldstein B, Smith J, White M, Jarett L. Differential Modulation of the Tyrosine Phosphorylation State of the Insulin Receptor by IRS (Insulin Receptor Subunit) Proteins. Endocrinology 1999, 13: 1784-1798. PMID: 10517679, DOI: 10.1210/mend.13.10.0361.Peer-Reviewed Original ResearchMeSH KeywordsAdaptor Proteins, Signal TransducingAdaptor Proteins, Vesicular TransportAmino Acid MotifsAnimalsInsulinInsulin Receptor Substrate ProteinsMicePhosphatidylinositol 3-KinasesPhosphoproteinsPhosphorylationProtein Tyrosine PhosphatasesProteinsReceptor, InsulinRecombinant ProteinsSequence DeletionShc Signaling Adaptor ProteinsSignal TransductionSrc Homology 2 Domain-Containing, Transforming Protein 1Stem CellsTyrosineVanadatesConceptsInsulin receptor phosphorylationTyrosine kinase activityInsulin receptor tyrosine phosphorylationReceptor tyrosine phosphorylationTyrosine phosphorylationKinase activityIRS-1IRS-2Receptor phosphorylationInsulin receptorTyrosine-phosphorylated IRS-1Insulin stimulationProtein tyrosine phosphatase activityTyrosine phosphorylation stateProtein tyrosine phosphataseReceptor tyrosine kinase activityReceptor kinase activityInsulin receptor kinase activityInsulin receptor subunitsIRS proteinsPervanadate treatmentPhosphorylation stateDownstream eventsInsulin actionTyrosine residues
1996
Multiple Requirements for SHPTP2 in Epidermal Growth Factor-Mediated Cell Cycle Progression
Bennett A, Hausdorff S, O’Reilly A, Freeman R, Neel B. Multiple Requirements for SHPTP2 in Epidermal Growth Factor-Mediated Cell Cycle Progression. Molecular And Cellular Biology 1996, 16: 1189-1202. PMID: 8622663, PMCID: PMC231101, DOI: 10.1128/mcb.16.3.1189.Peer-Reviewed Original ResearchConceptsElk-1 transactivationS-phase entryMitogen-activated proteinMAP kinase activationGrowth factorKinase activationFusion proteinPlatelet-derived growth factorGlutathione S-transferase fusion proteinEpidermal growth factor stimulationS-transferase fusion proteinProtein tyrosine phosphatase activityTyrosyl phosphorylation sitesGrowth factor stimulationSignal transduction pathwaysSerum-induced S-phase entryGrowth factor signalingImmediate early responseNIH 3T3 cellsCell cycle progressionEpidermal growth factorSH2 domainPhosphorylation sitesEGF stimulationTransduction pathways
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