2018
Role of eIF3a in 4-amino-2-trifluoromethyl-phenyl retinate-induced cell differentiation in human chronic myeloid leukemia K562 cells
Li G, Wang K, Li Y, Ruan J, Wang C, Qian Y, Zu S, Dai B, Meng Y, Zhou R, Ge J, Chen F. Role of eIF3a in 4-amino-2-trifluoromethyl-phenyl retinate-induced cell differentiation in human chronic myeloid leukemia K562 cells. Gene 2018, 683: 195-209. PMID: 30340049, DOI: 10.1016/j.gene.2018.10.035.Peer-Reviewed Original ResearchConceptsMyeloid differentiation marker CD11bCyclin D1Trans retinoic acid (ATRA) derivativeK562 cellsAnti-tumor effectsChronic myeloid leukemia K562 cellsMyeloid leukemia cell differentiationRetinoic acid derivativesCell differentiationG0/G1 phaseExpression of eIF3aC-MycHuman chronic myeloid leukemia K562 cellsDifferentiation marker CD11bTumor cell proliferationRole of eIF3aActivation of ERK1/2Marker CD11bCML cellsLeukemia cell differentiationP-ERKLeukemia K562 cellsP-RafPhenyl retinateEIF3a expression
2015
Retracted: Posttranslational regulation of polycystin‐2 protein expression as a novel mechanism of cholangiocyte reaction and repair from biliary damage
Spirli C, Villani A, Mariotti V, Fabris L, Fiorotto R, Strazzabosco M. Retracted: Posttranslational regulation of polycystin‐2 protein expression as a novel mechanism of cholangiocyte reaction and repair from biliary damage. Hepatology 2015, 62: 1828-1839. PMID: 26313562, PMCID: PMC4681612, DOI: 10.1002/hep.28138.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulum stressorsGene expressionAutophagy pathwayExtracellular signal-regulated kinase 1/2 (ERK1/2) pathwayProtein expressionUbiquitin-like proteinSignal-regulated kinase 1/2 pathwayProteasome inhibitor MG-132HIF-1α transcriptional activityKinase 1/2 pathwayProtein kinase APC2 gene expressionPC2 expressionInhibitor MG-132Activation of ERK1/2Transient receptor potential (TRP) channel familyNonselective calcium channelPosttranslational regulationMember 1 proteinPolycystin-2Treatment of cholangiocytesKinase ATranscriptional activityChannel familyMG-132
2014
Rapamycin antagonizes TNF induction of VCAM-1 on endothelial cells by inhibiting mTORC2
Wang C, Qin L, Manes TD, Kirkiles-Smith NC, Tellides G, Pober JS. Rapamycin antagonizes TNF induction of VCAM-1 on endothelial cells by inhibiting mTORC2. Journal Of Experimental Medicine 2014, 211: 395-404. PMID: 24516119, PMCID: PMC3949571, DOI: 10.1084/jem.20131125.Peer-Reviewed Original ResearchMeSH KeywordsAnalysis of VarianceBlotting, WesternCell AdhesionChromatin ImmunoprecipitationDNA PrimersEndothelial CellsFlow CytometryHumansImmunoblottingMechanistic Target of Rapamycin Complex 2Microscopy, FluorescenceMultiprotein ComplexesOncogene Protein v-aktReal-Time Polymerase Chain ReactionSirolimusT-LymphocytesTOR Serine-Threonine KinasesTumor Necrosis Factor-alphaVascular Cell Adhesion Molecule-1ConceptsVascular cell adhesion molecule-1VCAM-1 expressionEndothelial cellsActivation of ERK1/2Cell adhesion molecule-1TNF inductionInfiltration of leukocytesAdhesion molecule-1Inhibition of TNFPotential therapeutic targetAbility of rapamycinAbility of TNFTranscription factor IRF-1Hyperactivation of ERK1/2Inhibition of ERK1/2Venular flowT cellsEndothelial expressionInflamed tissuesVascular endotheliumMolecule-1Therapeutic targetRapamycin pretreatmentRenal glomeruliTNF
2012
Inorganic Phosphate Stimulates Fibronectin Expression in Renal Fibroblasts
Chen Z, Chen D, McCarthy TL, Centrella M, Zhang Y, Moeckel GW. Inorganic Phosphate Stimulates Fibronectin Expression in Renal Fibroblasts. Cellular Physiology And Biochemistry 2012, 30: 151-159. PMID: 22759963, DOI: 10.1159/000339054.Peer-Reviewed Original ResearchInhibition of Hematopoietic Protein Tyrosine Phosphatase Augments and Prolongs ERK1/2 and p38 Activation
Tautz L, Sergienko E, Xu J, Liu W, Dahl R, Critton D, Su Y, Brown B, Chan X, Yang L, Bobkova E, Vasile S, Yuan H, Rascon J, Colayco S, Sidique S, Cosford N, Chung T, Mustelin T, Page R, Lombroso P. Inhibition of Hematopoietic Protein Tyrosine Phosphatase Augments and Prolongs ERK1/2 and p38 Activation. The FASEB Journal 2012, 26: 766.12-766.12. DOI: 10.1096/fasebj.26.1_supplement.766.12.Peer-Reviewed Original ResearchHematopoietic protein tyrosine phosphataseP38 activationProtein tyrosine phosphataseUnique amino acid residuesAmino acid residuesNew drug targetsCell cycle arrestMAP kinases ERK1/2Activation of ERK1/2Tyrosine phosphataseHePTPMutagenesis experimentsMAP kinaseKinases ERK1/2Acid residuesCatalytic pocketDrug targetsTransient activationCycle arrestT-cell acute lymphoblastic leukemiaERK1/2Prolonged activationHuman T cellsPharmacological inhibitionCancer cells
2011
FGF-dependent regulation of VEGF receptor 2 expression in mice
Murakami M, Nguyen LT, Hatanaka K, Schachterle W, Chen PY, Zhuang ZW, Black BL, Simons M. FGF-dependent regulation of VEGF receptor 2 expression in mice. Journal Of Clinical Investigation 2011, 121: 2668-2678. PMID: 21633168, PMCID: PMC3223828, DOI: 10.1172/jci44762.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCells, CulturedEndothelial CellsEnzyme ActivationFibroblast Growth FactorsHindlimbHumansIschemiaMiceMice, Inbred C57BLMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Neovascularization, PhysiologicProto-Oncogene Proteins c-etsSignal TransductionVascular Endothelial Growth Factor Receptor-2Vascular Endothelial Growth FactorsConceptsFGF-dependent regulationETS transcription factorsERK1/2-dependent mannerVEGF receptor-2 expressionActivation of ERK1/2Enhancer activationTranscriptional analysisTranscription factorsVEGFR2 expressionVascular morphogenesisFGF stimulationVEGF stimulationFGFVascular formationExpressionVascular integrityReceptor 2 expressionActivationMorphogenesisVEGFERK1/2Numerous studiesPathwayRegulationDownregulation
2010
Anaplasma phagocytophilum AptA modulates Erk1/2 signalling
Sukumaran B, Mastronunzio JE, Narasimhan S, Fankhauser S, Uchil PD, Levy R, Graham M, Colpitts TM, Lesser CF, Fikrig E. Anaplasma phagocytophilum AptA modulates Erk1/2 signalling. Cellular Microbiology 2010, 13: 47-61. PMID: 20716207, PMCID: PMC3005019, DOI: 10.1111/j.1462-5822.2010.01516.x.Peer-Reviewed Original ResearchConceptsA. phagocytophilum infectionPhagocytophilum infectionCommon tick-borne diseasesHuman granulocytic anaplasmosisActivation of ERK1/2ERK1/2 mitogen-activated protein kinasesA. phagocytophilum survivalPolymorphonuclear leucocytesMitogen-activated protein kinaseHuman neutrophilsObligate intracellular pathogensGranulocytic anaplasmosisIntracellular pathogensTick-borne diseasesInfectionERK1/2 activationAnaplasma phagocytophilumVimentinSurvivalActivationBacterial inclusionsHost proteinsIntermediate filament protein vimentinVirulence proteinsProtein vimentin
2006
The Striatal-Enriched Protein Tyrosine Phosphatase Gates Long-Term Potentiation and Fear Memory in the Lateral Amygdala
Paul S, Olausson P, Venkitaramani DV, Ruchkina I, Moran TD, Tronson N, Mills E, Hakim S, Salter MW, Taylor JR, Lombroso PJ. The Striatal-Enriched Protein Tyrosine Phosphatase Gates Long-Term Potentiation and Fear Memory in the Lateral Amygdala. Biological Psychiatry 2006, 61: 1049-1061. PMID: 17081505, PMCID: PMC1853327, DOI: 10.1016/j.biopsych.2006.08.005.Peer-Reviewed Original ResearchMeSH KeywordsAcoustic StimulationAminoacetonitrileAmygdalaAnimalsBehavior, AnimalCells, CulturedConditioning, ClassicalCycloheximideElectric StimulationEnzyme InhibitorsFearFemaleImmunohistochemistryIn Vitro TechniquesLong-Term PotentiationMemoryMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3NeostriatumPatch-Clamp TechniquesPoint MutationPregnancyProtein Synthesis InhibitorsProtein Tyrosine PhosphatasesRatsRats, Sprague-DawleyTranslocation, GeneticConceptsStriatal-enriched protein tyrosine phosphataseERK1/2 activationMitogen-activated protein kinaseProtein tyrosine phosphataseDe novo translationActivation of ERK1/2Tyrosine phosphataseProtein bindsKinase signalingProtein kinaseSequential recruitmentAmygdala-dependent memory formationERK pathwayMemory formationPrimary cell culturesNuclear translocationBiphasic activationLong-term potentiationTranslation blockTAT-STEPERKCell culturesERK1/2ActivationPathway
1998
Calcium-Independent Activation of Extracellular Signal-Regulated Kinases 1 and 2 by Cyclic Strain
Ikeda M, Takei T, Mills I, Sumpio B. Calcium-Independent Activation of Extracellular Signal-Regulated Kinases 1 and 2 by Cyclic Strain. Biochemical And Biophysical Research Communications 1998, 247: 462-465. PMID: 9642151, DOI: 10.1006/bbrc.1998.8811.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalciumCalcium Channel BlockersCalcium-Calmodulin-Dependent Protein KinasesCattleCells, CulturedChelating AgentsEgtazic AcidEndothelium, VascularEnzyme ActivationExtracellular SpaceGadoliniumHydroquinonesIntracellular FluidMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Mitogen-Activated Protein KinasesPhosphorylationStress, MechanicalConceptsEndothelial cellsActivation of ERK1/2Baseline phosphorylationExtracellular Ca2Normal extracellular Ca2Aortic endothelial cellsKinase 1Bovine aortic endothelial cellsStrain-induced activationCycles/minChannel blockersExtracellular signal-regulated kinases 1Signal-regulated kinases 1Calcium-independent activationBenzohydroquinoneERK1/2 activationERK1/2Free mediumEffect of Ca2ActivationCa2EGTA
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