2016
Down-regulation of Insulin Receptor Substrate 1 during Hyperglycemia Induces Vascular Smooth Muscle Cell Dedifferentiation*
Xi G, Wai C, White M, Clemmons D. Down-regulation of Insulin Receptor Substrate 1 during Hyperglycemia Induces Vascular Smooth Muscle Cell Dedifferentiation*. Journal Of Biological Chemistry 2016, 292: 2009-2020. PMID: 28003360, PMCID: PMC5290970, DOI: 10.1074/jbc.m116.758987.Peer-Reviewed Original ResearchConceptsInsulin receptor substrate-1Receptor substrate-1IRS-1Differentiated stateSubstrate-1Aberrant signalingMetabolic stressVascular smooth muscle cell dedifferentiationIGF-I stimulationIRS-1 expressionVascular smooth muscle cell migrationScaffold proteinSHPS-1Transcription factorsSmooth muscle cell dedifferentiationSmooth muscle cell migrationMuscle cell dedifferentiationMuscle cell migrationReceptor signalsVSMC dedifferentiationCell migrationInsulin-like growth factor ICell dedifferentiationMajor risk factorDevelopment of atherosclerosis
2015
Compartment-Specific and Sequential Role of MyD88 and CARD9 in Chemokine Induction and Innate Defense during Respiratory Fungal Infection
Jhingran A, Kasahara S, Shepardson KM, Junecko BA, Heung LJ, Kumasaka DK, Knoblaugh SE, Lin X, Kazmierczak BI, Reinhart TA, Cramer RA, Hohl TM. Compartment-Specific and Sequential Role of MyD88 and CARD9 in Chemokine Induction and Innate Defense during Respiratory Fungal Infection. PLOS Pathogens 2015, 11: e1004589. PMID: 25621893, PMCID: PMC4306481, DOI: 10.1371/journal.ppat.1004589.Peer-Reviewed Original ResearchConceptsRespiratory fungal infectionsDistinct signal transduction pathwaysSignal transduction pathwaysNeutrophil recruitmentChemokine inductionGenetic deletionFungal infectionsFungal clearanceCellular compartmentsTransduction pathwaysC-type lectinProtein triggersLung epithelial cellsNeutrophil-dependent host defenseInterleukin-1 receptorReceptor signalsConidial uptakeLung neutrophil recruitmentLung-infiltrating neutrophilsNeutrophil chemokines CXCL1Sequential rolesMyD88-deficient miceHematopoietic compartmentProtein knockout miceMajor cellular source
2012
Phospholipase C mediates (±)-1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI)-, but not lysergic acid diethylamide (LSD)-elicited head bobs in rabbit medial prefrontal cortex
Schindler EA, Harvey JA, Aloyo VJ. Phospholipase C mediates (±)-1-(2,5-dimethoxy-4-iodophenyl)-2-aminopropane (DOI)-, but not lysergic acid diethylamide (LSD)-elicited head bobs in rabbit medial prefrontal cortex. Brain Research 2012, 1491: 98-108. PMID: 23123701, PMCID: PMC3559188, DOI: 10.1016/j.brainres.2012.10.057.Peer-Reviewed Original ResearchMeSH KeywordsAmphetaminesAnimalsBehavior, AnimalCerebral CortexEnzyme ActivationEnzyme InhibitorsEstrenesHallucinogensHead MovementsHydrolysisLysergic Acid DiethylamideMaleMicroinjectionsPhosphatidylinositolsPrefrontal CortexPyrrolidinonesRabbitsReceptor, Serotonin, 5-HT2ASerotonin AntagonistsSerotonin Receptor AgonistsSignal TransductionType C PhospholipasesConceptsMedial prefrontal cortexLysergic acid diethylamidePI hydrolysisReceptor antagonistPrefrontal cortexDimethoxy-4Acid diethylamidePhospholipase CDistinct pharmacological propertiesEffects of hallucinogensActivation of PLCTissue prismsSerotonergic receptorsReceptor mechanismsPhosphatidylinositol hydrolysisPharmacological propertiesIntracellular mechanismsPLC inhibitorPLC activationHead bobsTrien-17Receptor signalsHallucinogensNovel findingsAntagonist
2011
The Kinases MEKK2 and MEKK3 Regulate Transforming Growth Factor-β-Mediated Helper T Cell Differentiation
Chang X, Liu F, Wang X, Lin A, Zhao H, Su B. The Kinases MEKK2 and MEKK3 Regulate Transforming Growth Factor-β-Mediated Helper T Cell Differentiation. Immunity 2011, 34: 201-212. PMID: 21333552, PMCID: PMC3073014, DOI: 10.1016/j.immuni.2011.01.017.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBone Marrow TransplantationCell DifferentiationEnzyme ActivationForkhead Transcription FactorsLymphocyte CountLymphopeniaMAP Kinase Kinase Kinase 2MAP Kinase Kinase Kinase 3MAP Kinase Signaling SystemMiceMice, Inbred C57BLMice, KnockoutMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3PhosphorylationProtein Processing, Post-TranslationalProtein Structure, TertiaryReceptors, Antigen, T-CellSmad2 ProteinSmad3 ProteinSpecific Pathogen-Free OrganismsT-Lymphocytes, Helper-InducerT-Lymphocytes, RegulatoryTh17 CellsTransforming Growth Factor betaConceptsTh cell differentiationSevere experimental autoimmune encephalomyelitisGrowth factorExperimental autoimmune encephalomyelitisHelper T cell differentiationT helper cell differentiationCell differentiationT cell differentiationTGF-β signaling pathwaysTransforming Growth FactorHelper cell differentiationTGF-β stimulationCell receptor signalsAutoimmune encephalomyelitisTGF-β responseAbnormal accumulationImpaired phosphorylationReceptor signalsSignaling pathwaysMiceCellsKinase MEKK2DifferentiationWild-type cellsTregs
2005
Irs1 and Irs2 signaling is essential for hepatic glucose homeostasis and systemic growth
Dong X, Park S, Lin X, Copps K, Yi X, White M. Irs1 and Irs2 signaling is essential for hepatic glucose homeostasis and systemic growth. Journal Of Clinical Investigation 2005, 116: 101-114. PMID: 16374520, PMCID: PMC1319221, DOI: 10.1172/jci25735.Peer-Reviewed Original ResearchConceptsSystemic growthHundreds of genesInsulin receptor substrateHepatic nutrient homeostasisHepatic glucose homeostasisHeterologous pathwaysNutrient homeostasisReceptor substrateGene expressionGSK3beta phosphorylationReceptor signalsHepatic gene expressionLKO miceInsulin receptorGlucose homeostasisIRS2IRS1Hepatic genesHepatic insulin receptorAkt-FoxO1 pathwayHomeostasisGenesHepatic glycogen storesLKO liversPathway
1997
The 60 kDa Insulin Receptor Substrate Functions Like an IRS Protein (pp60IRS3) in Adipose Cells †
Smith-Hall J, Pons S, Patti M, Burks D, Yenush L, Sun X, Kahn C, White M. The 60 kDa Insulin Receptor Substrate Functions Like an IRS Protein (pp60IRS3) in Adipose Cells †. Biochemistry 1997, 36: 8304-8310. PMID: 9204876, DOI: 10.1021/bi9630974.Peer-Reviewed Original ResearchMeSH KeywordsAdipocytesAnimalsImmunosorbent TechniquesInsulinInsulin Receptor Substrate ProteinsIntracellular Signaling Peptides and ProteinsMaleMiceMolecular WeightPhosphatidylinositol 3-KinasesPhosphoproteinsPhosphotransferases (Alcohol Group Acceptor)PhosphotyrosineRatsRats, Sprague-DawleyReceptor, InsulinTestisConceptsIRS-1IRS proteinsInsulin receptor substrates functionIRS-2IRS protein familyTyrosine phosphorylated proteinsInsulin receptor signalsInsulin receptor substratePTB domainNPXY motifSH2 domainProtein familyPhosphorylated proteinsReceptor substrateInsulin stimulationReceptor signalsSubstrate functionP85New memberProteinRat adipocytesAdipose cellsAlternate pathwayFunctional characteristicsSynthetic peptides
1994
An intrinsic guanine nucleotide exchange inhibitor in Gi2 alpha. Significance of G-protein self-suppression which antagonizes receptor signal.
Okamoto T, Murayama Y, Strittmatter SM, Katada T, Asano S, Ogata E, Nishimoto I. An intrinsic guanine nucleotide exchange inhibitor in Gi2 alpha. Significance of G-protein self-suppression which antagonizes receptor signal. Journal Of Biological Chemistry 1994, 269: 13756-13759. PMID: 8188651, DOI: 10.1016/s0021-9258(17)36711-x.Peer-Reviewed Original ResearchConceptsIntrinsic guanineHeterotrimeric G-protein familyG proteinsReceptor signalsGi2 alphaG protein familyProto-oncogene productProtein familyC-terminusResidues 338Alpha subunitReceptor polypeptideBasal activityAlpha activationPolypeptideGuanineReceptor stimulationAlphaExchange inhibitorInhibitorsReceptorsTerminusSubunitsProteinGi2
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