2019
FABP7 Protects Astrocytes Against ROS Toxicity via Lipid Droplet Formation
Islam A, Kagawa Y, Miyazaki H, Shil SK, Umaru BA, Yasumoto Y, Yamamoto Y, Owada Y. FABP7 Protects Astrocytes Against ROS Toxicity via Lipid Droplet Formation. Molecular Neurobiology 2019, 56: 5763-5779. PMID: 30680690, DOI: 10.1007/s12035-019-1489-2.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinaseROS toxicityLipid droplet formationLD accumulationPeroxiredoxin 1Stress-activated protein kinase/c-Jun N-terminal kinaseProtein kinase/c-Jun N-terminal kinaseP38 mitogen-activated protein kinaseC-Jun N-terminal kinaseReactive oxygen species stressRole of FABP7ROS inductionU87 human glioma cell lineN-terminal kinaseOxygen species stressActivation of apoptosisFABP7 overexpressionProtein bindsProtein kinaseLD formationLong-chain fatty acidsROS stressHuman glioma cell linesLipid dynamicsWild-type astrocytes
2017
An ALS-Associated Mutant SOD1 Rapidly Suppresses KCNT1 (Slack) Na+-Activated K+ Channels in Aplysia Neurons
Zhang Y, Ni W, Horwich AL, Kaczmarek LK. An ALS-Associated Mutant SOD1 Rapidly Suppresses KCNT1 (Slack) Na+-Activated K+ Channels in Aplysia Neurons. Journal Of Neuroscience 2017, 37: 2258-2265. PMID: 28119399, PMCID: PMC5338764, DOI: 10.1523/jneurosci.3102-16.2017.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAplysiaBiophysicsCells, CulturedElectric StimulationEnzyme InhibitorsGanglia, InvertebrateHumansLuminescent ProteinsMembrane PotentialsMicroinjectionsMorpholinosMutationNerve Tissue ProteinsNeuronsPatch-Clamp TechniquesPotassium ChannelsPotassium Channels, Sodium-ActivatedRNA, Small InterferingSodiumSuperoxide Dismutase-1ConceptsAmyotrophic lateral sclerosisSuperoxide dismutase 1Mutant superoxide dismutase 1Potassium currentC-Jun N-terminal kinaseNeuronal excitabilityLateral sclerosisFatal adult-onset neurodegenerative diseaseN-terminal kinaseMutant human Cu/ZnNeuronal developmentDismutase 1Adult-onset neurodegenerative diseaseCurrent-clamp recordingsMotor neuron toxicityOutward potassium currentHuman Cu/ZnWild-type superoxide dismutase 1Neuron toxicityActivity of NaBag cell neuronsClamp recordingsNeuronal functionCell neuronsAction potentialsA Phosphoproteomic Screen Identifies a Guanine Nucleotide Exchange Factor for Rab3A Protein as a Mitogen-activated Protein (MAP) Kinase Phosphatase-5-regulated MAP Kinase Target in Interleukin 6 (IL-6) Secretion and Myogenesis*
Lee H, Min K, Yi JS, Shi H, Chang W, Jackson L, Bennett AM. A Phosphoproteomic Screen Identifies a Guanine Nucleotide Exchange Factor for Rab3A Protein as a Mitogen-activated Protein (MAP) Kinase Phosphatase-5-regulated MAP Kinase Target in Interleukin 6 (IL-6) Secretion and Myogenesis*. Journal Of Biological Chemistry 2017, 292: 3581-3590. PMID: 28096466, PMCID: PMC5339744, DOI: 10.1074/jbc.m116.769208.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAnimalsCell MovementCell ProliferationDual-Specificity PhosphatasesGene Expression Regulation, EnzymologicGuanine Nucleotide Exchange FactorsInterleukin-6MAP Kinase Signaling SystemMiceMice, KnockoutMuscle DevelopmentMuscle, SkeletalMutationMyoblastsPhosphorylationProteomicsrab3A GTP-Binding ProteinRegenerationSerineConceptsMitogen-activated protein kinaseMAPK phosphatase-5MAPK substratesExchange factorSer-169Guanine nucleotide exchange factorsNucleotide exchange factorsPhosphorylation-defective mutantSkeletal muscleP38 mitogen-activated protein kinaseC-Jun N-terminal kinaseMAPK-dependent signalingN-terminal kinaseSkeletal muscle functionSubstrate screenMAPK targetsSerine 169Rab3A proteinScreen identifiesRegenerative myogenesisPhosphatase 5Protein kinaseKinase targetsC2C12 myoblastsNegative regulator
2014
Renalase Prevents AKI Independent of Amine Oxidase Activity
Wang L, Velazquez H, Moeckel G, Chang J, Ham A, Lee HT, Safirstein R, Desir GV. Renalase Prevents AKI Independent of Amine Oxidase Activity. Journal Of The American Society Of Nephrology 2014, 25: 1226-1235. PMID: 24511138, PMCID: PMC4033373, DOI: 10.1681/asn.2013060665.Peer-Reviewed Original ResearchConceptsIschemic injuryCatecholamine levelsRecombinant renalaseAmine oxidase activityHuman proximal tubular cellsCisplatin-induced AKITreatment of AKIWild-type miceHK-2 cellsProximal tubular cellsOxidase activityKidney injuryRenal injuryC-Jun N-terminal kinaseExtracellular signal-regulated kinaseP38 mitogen-activated protein kinaseToxic injuryRenalase proteinTubular cellsSignal-regulated kinaseIntracellular signaling cascadesRenalaseInjuryMitogen-activated protein kinaseN-terminal kinasePigment Epithelium-Derived Factor (PEDF) Suppresses IL-1β-Mediated c-Jun N-Terminal Kinase (JNK) Activation to Improve Hepatocyte Insulin Signaling
Gattu AK, Birkenfeld AL, Iwakiri Y, Jay S, Saltzman M, Doll J, Protiva P, Samuel VT, Crawford SE, Chung C. Pigment Epithelium-Derived Factor (PEDF) Suppresses IL-1β-Mediated c-Jun N-Terminal Kinase (JNK) Activation to Improve Hepatocyte Insulin Signaling. Endocrinology 2014, 155: 1373-1385. PMID: 24456163, PMCID: PMC5393334, DOI: 10.1210/en.2013-1785.Peer-Reviewed Original ResearchMeSH KeywordsAdipocytesAnimalsEye ProteinsGene Expression RegulationGlucose Tolerance TestHepatocytesHumansInflammationInsulinInsulin ResistanceInterleukin-1betaJNK Mitogen-Activated Protein KinasesLiverMaleMetabolic SyndromeMetabolomicsMiceMice, Inbred C57BLMice, KnockoutMicrospheresNerve Growth FactorsObesityPalmitic AcidPhenotypeRNA InterferenceSerpinsSignal TransductionSuccinic AcidConceptsPigment epithelium-derived factorKO miceMetabolic syndromeIL-1βC-Jun N-terminal kinase (JNK) activationElevated pigment epithelium-derived factorIL-1β challengeHuman hepatocytesIL-1β expressionHuman metabolic syndromeEpithelium-derived factorPEDF-knockout miceInflammatory markersGlucose intoleranceSerum levelsC-Jun N-terminal kinaseKinase activationAntiinflammatory proteinHepatic insulinKnockout micePigment epitheliumN-terminal kinaseMiceSyndromeMetabolic homeostasis
2013
Increased Hippocampal CREB Phosphorylation in Dopamine D3 Receptor Knockout Mice Following Passive Avoidance Conditioning
D’Amico A, Scuderi S, Leggio G, Castorina A, Drago F, D’Agata V. Increased Hippocampal CREB Phosphorylation in Dopamine D3 Receptor Knockout Mice Following Passive Avoidance Conditioning. Neurochemical Research 2013, 38: 2516-2523. PMID: 24100927, DOI: 10.1007/s11064-013-1164-3.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinaseCAMP response element-binding proteinNuclear transcription factor cAMP response element-binding proteinTranscription factor cAMP response element-binding proteinExtracellular signal-regulated kinase 1/2C-Jun N-terminal kinaseCREB phosphorylationSignal-regulated kinase 1/2Response element-binding proteinElement-binding proteinProtein kinaseDe novo synthesisKinase 1/2ERK signalingAkt activationBinding proteinPhosphorylationPhosphorylation levelsP38 phosphorylationGenetic backgroundKnockout mice displayNovo synthesisKinaseSynaptic functionAktPlatelet‐derived growth factor‐D and Rho GTPases regulate recruitment of cancer‐associated fibroblasts in cholangiocarcinoma
Cadamuro M, Nardo G, Indraccolo S, Dall'Olmo L, Sambado L, Moserle L, Franceschet I, Colledan M, Massani M, Stecca T, Bassi N, Morton S, Spirli C, Fiorotto R, Fabris L, Strazzabosco M. Platelet‐derived growth factor‐D and Rho GTPases regulate recruitment of cancer‐associated fibroblasts in cholangiocarcinoma. Hepatology 2013, 58: 1042-1053. PMID: 23505219, PMCID: PMC3732815, DOI: 10.1002/hep.26384.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntineoplastic AgentsBenzamidesBile Duct NeoplasmsBile Ducts, IntrahepaticCell Line, TumorCell MovementCell ProliferationCells, CulturedCholangiocarcinomaEpithelial-Mesenchymal TransitionFibroblastsHeterograftsHumansImatinib MesylateIn Vitro TechniquesLymphokinesMaleMiceMice, SCIDPiperazinesPlatelet-Derived Growth FactorPyrimidinesrho GTP-Binding ProteinsSignal TransductionConceptsCancer-associated fibroblastsPlatelet-derived growth factorEpithelial-mesenchymal transitionCCA cellsSecretion of PDGFRole of PDGFGrowth factorAbundant stromal reactionAlpha-smooth muscle actinPDGF-D expressionNovel therapeutic approachesPotential therapeutic targetSmooth muscle actinCCA cell linesPDGF-D signalingFibroblast migrationC-Jun N-terminal kinaseEMT biomarkersImmunodeficient miceStromal reactionTherapeutic approachesStroma interactionsTherapeutic targetCholangiocarcinomaMesenchymal markers
2012
Both Internalization and AIP1 Association Are Required for Tumor Necrosis Factor Receptor 2-Mediated JNK Signaling
Ji W, Li Y, Wan T, Wang J, Zhang H, Chen H, Min W. Both Internalization and AIP1 Association Are Required for Tumor Necrosis Factor Receptor 2-Mediated JNK Signaling. Arteriosclerosis Thrombosis And Vascular Biology 2012, 32: 2271-2279. PMID: 22743059, PMCID: PMC3421067, DOI: 10.1161/atvbaha.112.253666.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsApoptosisBinding SitesCells, CulturedEndothelial CellsEnzyme ActivationHuman Umbilical Vein Endothelial CellsHumansJNK Mitogen-Activated Protein KinasesMiceMice, KnockoutNF-kappa BProtein Interaction Domains and MotifsProtein Transportras GTPase-Activating ProteinsReceptors, Tumor Necrosis Factor, Type IReceptors, Tumor Necrosis Factor, Type IISequence DeletionSignal TransductionTime FactorsTNF Receptor-Associated Factor 2TransfectionTumor Necrosis Factor-alphaConceptsJNK signalingApoptotic signalingJNK activationDomain IICaspase-dependent cell deathCell deathTNF receptor 1C-Jun N-terminal kinaseDependent cell survivalN-terminal kinaseNF-κB activationNF-κBDeletion analysisTNF responseLL motifPlasma membraneIntracellular regionCell survivalDomain IJNKSignalingDistinct rolesTNFR2 deletionProtein 1Specific deletion
2011
JNK2 Promotes Endothelial Cell Alignment under Flow
Hahn C, Wang C, Orr AW, Coon BG, Schwartz MA. JNK2 Promotes Endothelial Cell Alignment under Flow. PLOS ONE 2011, 6: e24338. PMID: 21909388, PMCID: PMC3164210, DOI: 10.1371/journal.pone.0024338.Peer-Reviewed Original ResearchConceptsMitogen-activated protein kinase c-Jun N-terminal kinaseProtein kinase c-Jun N-terminal kinaseC-Jun N-terminal kinaseActin stress fibersN-terminal kinaseFocal adhesionsBasement membrane proteinsMembrane proteinsLaminar shear stressStress fibersGene expressionJNK activityIntegrin activationJNK2 activationEndothelial cell alignmentJNK activationActivated JNKExtracellular matrixInflammatory gene expressionCell alignmentUnexpected connectionEndothelial cellsActivationPathwayCellsGenomic Differences Distinguish the Myofibroblast Phenotype of Distal Lung Fibroblasts from Airway Fibroblasts
Zhou X, Wu W, Hu H, Milosevic J, Konishi K, Kaminski N, Wenzel SE. Genomic Differences Distinguish the Myofibroblast Phenotype of Distal Lung Fibroblasts from Airway Fibroblasts. American Journal Of Respiratory Cell And Molecular Biology 2011, 45: 1256-1262. PMID: 21757679, PMCID: PMC3262668, DOI: 10.1165/rcmb.2011-0065oc.Peer-Reviewed Original ResearchConceptsGenomic differencesMicroarray analysisC-Jun N-terminal kinaseExtracellular matrix-associated moleculesMyofibroblast-like characteristicsDistinct genomic differencesN-terminal kinasePotential functional implicationsQuantitative real-time PCRMatrix-associated moleculesCytoskeletal organizationGene OntologyActin bindingLung fibroblastsReal-time PCRMyofibroblast phenotypeFunctional implicationsParenchymal fibroblastsAirway fibroblastsDifferentiated fibroblastsPathway activationDifferent phenotypesRegional fibroblastsFibroblastsPhenotype
2008
AIP1 Recruits Phosphatase PP2A to ASK1 in Tumor Necrosis Factor–Induced ASK1-JNK Activation
Min W, Lin Y, Tang S, Yu L, Zhang H, Wan T, Luhn T, Fu H, Chen H. AIP1 Recruits Phosphatase PP2A to ASK1 in Tumor Necrosis Factor–Induced ASK1-JNK Activation. Circulation Research 2008, 102: 840-848. PMID: 18292600, DOI: 10.1161/circresaha.107.168153.Peer-Reviewed Original ResearchConceptsASK1-JNK signalingASK1 dephosphorylationAssociation of PP2APP2A catalytic subunitCatalytic inactive formPP2A inhibitor okadaicASK1-JNK activationC-Jun N-terminal kinaseActivation of JNKEndothelial cellsN-terminal kinasePhosphatase PP2ACritical rolePotential phosphataseProtein phosphataseGAP domainInhibitor okadaicProtein familyCatalytic subunitC2 domainPP2AAIP1Novel memberApoptotic signalingRNA knockdown
2007
Mitogen-activated protein kinase phosphatase-1 (MKP-1): a critical regulator of innate immune responses
Chi H, Bennett A, Flavell R. Mitogen-activated protein kinase phosphatase-1 (MKP-1): a critical regulator of innate immune responses. Journal Of Organ Dysfunction 2007, 3: 72-81. DOI: 10.1080/17471060601137415.Peer-Reviewed Original ResearchProtein kinase phosphatase-1Kinase phosphatase-1Innate immune responseMKP-1Toll-like receptorsPhosphatase 1Dual-specificity phosphataseImmune responseC-Jun N-terminal kinaseMKP-1 deficiencyN-terminal kinaseIntracellular negative regulatorTranscriptional inductionExcessive innate immune responseNegative regulatorBiochemical activityCritical regulatorMicrobial pathogensPhysiological functionsPro-inflammatory cytokinesP38 MAPKInnate immunityAutoimmune arthritisDendritic cellsInflammatory mediators
2006
Varicella-Zoster Virus Infection of Human Fibroblast Cells Activates the c-Jun N-Terminal Kinase Pathway
Zapata HJ, Nakatsugawa M, Moffat JF. Varicella-Zoster Virus Infection of Human Fibroblast Cells Activates the c-Jun N-Terminal Kinase Pathway. Journal Of Virology 2006, 81: 977-990. PMID: 17079291, PMCID: PMC1797429, DOI: 10.1128/jvi.01470-06.Peer-Reviewed Original ResearchConceptsPhospho-c-JunC-JunPhospho-JNKKinase pathwayC-Jun N-terminal kinaseC-Jun N-terminal kinase (JNK) pathwayTranscription factor ATF-2N-terminal kinase pathwayProtein kinase pathwayImmunofluorescent confocal microscopyN-terminal kinaseBiochemical fractionationKinase assaysUseful drug targetC-Jun levelsATF-2Phosphorylated formVirus genesJNK pathwayDrug targetsHuman fibroblast cellsPhosphorylated JNKJNKMain activatorHuman foreskin fibroblastsG‐CSF‐mediated inhibition of JNK is a key mechanism for Lactobacillus rhamnosus‐induced suppression of TNF production in macrophages
Kim S, Sheikh H, Ha S, Martins A, Reid G. G‐CSF‐mediated inhibition of JNK is a key mechanism for Lactobacillus rhamnosus‐induced suppression of TNF production in macrophages. Cellular Microbiology 2006, 8: 1958-1971. PMID: 16889627, DOI: 10.1111/j.1462-5822.2006.00763.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBone Marrow CellsCell LineCytokinesEnterococcus faecalisEscherichia coliGranulocyte Colony-Stimulating FactorHumansInterleukin-10JNK Mitogen-Activated Protein KinasesLacticaseibacillus rhamnosusMacrophage ActivationMacrophagesMacrophages, PeritonealMiceMice, Inbred C57BLp38 Mitogen-Activated Protein KinasesPhosphorylationProbioticsSignal TransductionSTAT3 Transcription FactorTumor Necrosis Factor-alphaConceptsGranulocyte-colony stimulating factorTNF productionL. rhamnosus GGGr-1Rhamnosus GGReceptor knockout miceAnti-inflammatory effectsMonocytic cell line THP-1Human monocytic cell line THP-1Cell line THP-1Lipopolysaccharide-activated macrophagesActivation of STAT3C-Jun N-terminal kinaseImmunomodulatory effectsTumor necrosisImmunomodulatory propertiesKnockout miceParacrine routeStimulating factorMacrophagesTHP-1Subsequent inhibitionMouse macrophagesCulture supernatantsNovo protein synthesis
2004
Molecular cloning, isolation and characterisation of ERK3 gene from chewing-tobacco induced oral squamous cell carcinoma
Rai R, Mahale A, Saranath D. Molecular cloning, isolation and characterisation of ERK3 gene from chewing-tobacco induced oral squamous cell carcinoma. Oral Oncology 2004, 40: 705-712. PMID: 15172640, DOI: 10.1016/j.oraloncology.2004.01.010.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBlotting, NorthernBlotting, SouthernCarcinoma, Squamous CellCloning, MolecularDNA, ComplementaryDNA, NeoplasmGene ExpressionGene LibraryHumansMitogen-Activated Protein Kinase 6Mitogen-Activated Protein KinasesMolecular Sequence DataMouth NeoplasmsReverse Transcriptase Polymerase Chain ReactionTobacco, SmokelessConceptsOral cancer tissuesOral squamous cell carcinomaSquamous cell carcinomaPeripheral blood cellsNormal healthy individualsCancer tissuesExtracellular signal-regulated protein kinaseCell carcinomaOral cancerHealthy individualsNon-coding regionBlood cellsSerine/threonine kinaseSignal-regulated protein kinaseTobacco habitsC-Jun N-terminal kinaseFetal skeletal muscleMRNA transcript analysisNormal individualsN-terminal kinaseRegulation of mRNAPatient samplesRT-PCR analysisSkeletal muscleERK3 expression
2003
Receptor Activator of NF-κB Ligand Stimulates Recruitment of SHP-1 to the Complex Containing TNFR-Associated Factor 6 That Regulates Osteoclastogenesis
Zhang Z, Jimi E, Bothwell AL. Receptor Activator of NF-κB Ligand Stimulates Recruitment of SHP-1 to the Complex Containing TNFR-Associated Factor 6 That Regulates Osteoclastogenesis. The Journal Of Immunology 2003, 171: 3620-3626. PMID: 14500659, DOI: 10.4049/jimmunol.171.7.3620.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCarrier ProteinsCell DifferentiationCell LineCysteineGenetic VectorsGlycoproteinsIntracellular Signaling Peptides and ProteinsLigandsMacrophagesMembrane GlycoproteinsMiceMice, Inbred C57BLMice, Mutant StrainsNF-kappa BOsteoclastsOsteoprotegerinPhosphatidylinositol 3-KinasesPhosphorylationProtein Phosphatase 1Protein Serine-Threonine KinasesProtein SubunitsProtein TransportProtein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesProteinsProto-Oncogene ProteinsProto-Oncogene Proteins c-aktRANK LigandReceptor Activator of Nuclear Factor-kappa BReceptors, Cytoplasmic and NuclearReceptors, Tumor Necrosis FactorRetroviridaeSerinesrc Homology DomainsTNF Receptor-Associated Factor 6Transduction, GeneticTyrosineUp-RegulationConceptsSrc homology 2 domain-containing phosphatase 1Mitogen-activated protein kinaseExpression of SHPProtein kinaseBone marrow macrophagesSrc homology 2 domainTyrosine phosphatase SHP-1P38 mitogen-activated protein kinaseExtracellular signal-regulated kinaseC-Jun N-terminal kinasePhosphatase SHP-1Phosphatidylinositol-3 kinaseMarrow macrophagesAssociation of TRAF6Signal-regulated kinaseN-terminal kinaseMultinuclear osteoclast-like cellsPhosphorylation of AktP85 subunitPhosphatase 1Tyrosine phosphorylationPathways downstreamRANKL-induced phosphorylationRAW264.7 cellsKinase
2002
c-Jun N-terminal Kinase (JNK) Mediates Feedback Inhibition of the Insulin Signaling Cascade*
Lee Y, Giraud J, Davis R, White M. c-Jun N-terminal Kinase (JNK) Mediates Feedback Inhibition of the Insulin Signaling Cascade*. Journal Of Biological Chemistry 2002, 278: 2896-2902. PMID: 12417588, DOI: 10.1074/jbc.m208359200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBinding SitesCell LineConsensus SequenceCulture Media, ConditionedHumansInsulinInsulin Receptor Substrate ProteinsJNK Mitogen-Activated Protein KinasesMiceMice, KnockoutMitogen-Activated Protein Kinase 8Mitogen-Activated Protein Kinase 9Mitogen-Activated Protein KinasesMolecular Sequence DataPhosphoproteinsPhosphorylationRatsSignal TransductionTransfectionConceptsC-Jun N-terminal kinaseN-terminal kinaseDirect bindingInsulin-stimulated tyrosine phosphorylationInsulin receptor substrate-1Interaction of JNKInsulin Signaling CascadeReceptor substrate-1Mouse embryo fibroblastsActivation of JNKFeedback inhibitionNegative feedback regulatorPhosphorylation of IRS1Cellular proteinsCell-permeable peptideTyrosine phosphorylationInsulin signalSignaling cascadesIRS1 proteinJNK activitySubstrate-1Insulin stimulationEmbryo fibroblastsPhosphorylationAkt phosphorylation
2001
Sustained Activation of Extracellular Signal‐Regulated Kinase (ERK) Signaling in Human Prostate Cancer LNCaP Cells Depleted of Androgen
Drew L, Fine R, Raffo A, Petrylak D. Sustained Activation of Extracellular Signal‐Regulated Kinase (ERK) Signaling in Human Prostate Cancer LNCaP Cells Depleted of Androgen. The Prostate Journal 2001, 3: 105-117. DOI: 10.1046/j.1525-1411.2001.32003.x.Peer-Reviewed Original ResearchHuman prostate cancer LNCaP cellsERK phosphorylationMitogen-activated protein kinase cascadeProstate cancer LNCaP cellsProtein kinase cascadeC-Jun N-terminal kinaseMAPK kinase activityPhosphorylation/activityLNCaP cellsProtein levelsN-terminal kinaseMEK inhibitor U0126Formation of neuritesTyrosine kinase receptorsKinase cascadeExtracellular signalsAndrogen-sensitive human prostate cancer LNCaP cellsPhosphorylation statusKinase activityPotential role
1999
Dishevelled proteins lead to two signaling pathways. Regulation of LEF-1 and c-Jun N-terminal kinase in mammalian cells.
Li L, Yuan H, Xie W, Mao J, Caruso A, Sussman D, Wu D. Dishevelled proteins lead to two signaling pathways. Regulation of LEF-1 and c-Jun N-terminal kinase in mammalian cells. Journal Of Biological Chemistry 1999, 274: 33178. DOI: 10.1016/s0021-9258(17)46631-2.Peer-Reviewed Original ResearchC-Jun N-terminal kinaseN-terminal kinaseDishevelled proteinsMammalian cellsLEF-1KinaseProteinRegulationPathwayCellsDishevelled Proteins Lead to Two Signaling Pathways REGULATION OF LEF-1 AND c-Jun N-TERMINAL KINASE IN MAMMALIAN CELLS*
Li L, Yuan H, Xie W, Mao J, Caruso A, McMahon A, Sussman D, Wu D. Dishevelled Proteins Lead to Two Signaling Pathways REGULATION OF LEF-1 AND c-Jun N-TERMINAL KINASE IN MAMMALIAN CELLS*. Journal Of Biological Chemistry 1999, 274: 129-134. PMID: 9867820, DOI: 10.1074/jbc.274.1.129.Peer-Reviewed Original ResearchMeSH Keywords3T3 CellsAdaptor Proteins, Signal TransducingAnimalsbeta CateninCalcium-Calmodulin-Dependent Protein KinasesCell Cycle ProteinsCOS CellsCytoskeletal ProteinsDishevelled ProteinsDNA-Binding ProteinsEnzyme ActivationJNK Mitogen-Activated Protein KinasesLymphoid Enhancer-Binding Factor 1MiceMitogen-Activated Protein KinasesPhosphoproteinsSignal TransductionTrans-ActivatorsTranscription FactorsTranscription, GeneticUp-RegulationConceptsJNK activationMammalian cellsT-cell factorSmall G proteinsC-Jun N-terminal kinaseDominant negative mutantBeta-catenin levelsDifferent signaling pathwaysCOS-7 cellsN-terminal kinaseC-Jun NDishevelled proteinsDvl proteinsDEP domainDependent transcriptionNegative mutantPathway regulationKinase activityLEF-1Transcription activitySignaling pathwaysG proteinsNovel pathwayCell factorProtein
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