2023
Correction: Carbon monoxide inhibition of apoptosis during ischemia-reperfusion lung injury is dependent on the p38 mitogen-activated protein kinase pathway and involves caspase 3
Zhang X, Shan P, Otterbein L, Alam J, Flavell R, Davis R, Choi A, Lee P. Correction: Carbon monoxide inhibition of apoptosis during ischemia-reperfusion lung injury is dependent on the p38 mitogen-activated protein kinase pathway and involves caspase 3. Journal Of Biological Chemistry 2023, 299: 105304. PMID: 37826982, PMCID: PMC10570935, DOI: 10.1016/j.jbc.2023.105304.Peer-Reviewed Original Research
2011
Cyclic Strain Delays the Expression of Tissue Factor Induced by Thrombin in Human Umbilical Vein Endothelial Cells
Yamashita N, Abe R, Nixon A, Rochier A, Madri J, Sumpio B. Cyclic Strain Delays the Expression of Tissue Factor Induced by Thrombin in Human Umbilical Vein Endothelial Cells. International Journal Of Angiology 2011, 20: 157-166. PMID: 22942631, PMCID: PMC3331651, DOI: 10.1055/s-0031-1284475.Peer-Reviewed Original ResearchHuman umbilical vein endothelial cellsUmbilical vein endothelial cellsVein endothelial cellsExtracellular signal-regulated protein kinase (ERK) inhibitorsProtein kinase inhibitorsEndothelial cellsEgr-1 levelsTF expressionERK activityERK inhibitorThrRNA expressionP38Messenger RNA expressionTF mRNA expressionCyclic strainCulture conditionsExpression of TFKinase inhibitorsExpressionStationary culture conditionsTissue factor expressionFactor expressionCellsMRNA expression
2010
Thrombospondin 1, Fibronectin, and Vitronectin are Differentially Dependent Upon RAS, ERK1/2, and p38 for Induction of Vascular Smooth Muscle Cell Chemotaxis
Willis AI, Sadowitz B, Fuse S, Maier KG, Lee TS, Wang XJ, Tuszynski GP, Sumpio BE, Gahtan V. Thrombospondin 1, Fibronectin, and Vitronectin are Differentially Dependent Upon RAS, ERK1/2, and p38 for Induction of Vascular Smooth Muscle Cell Chemotaxis. Vascular And Endovascular Surgery 2010, 45: 55-62. PMID: 21193465, DOI: 10.1177/1538574410387677.Peer-Reviewed Original ResearchMeSH KeywordsAnalysis of VarianceAnimalsCattleCells, CulturedChemotaxisFibronectinsHumansMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Muscle, Smooth, VascularMyocytes, Smooth Musclep38 Mitogen-Activated Protein KinasesProtein Kinase Inhibitorsras ProteinsThrombospondin 1TransfectionVitronectinConceptsVascular smooth muscle cellsThrombospondin-1Smooth muscle cell chemotaxisFarnesyl protein transferase inhibitorSignal transduction pathwaysProtein transferase inhibitorsVascular smooth muscle cell chemotaxisBovine vascular smooth muscle cellsTSP-1Ras N17Transduction pathwaysSecond messenger systemsP38Smooth muscle cellsERK1/2VSMC migrationTransferase inhibitorsPD098059Cell chemotaxisSB202190Muscle cellsMessenger systemsVitronectinRAChemotaxis
2009
Extrasynaptic NMDA Receptors Couple Preferentially to Excitotoxicity via Calpain-Mediated Cleavage of STEP
Xu J, Kurup P, Zhang Y, Goebel-Goody SM, Wu PH, Hawasli AH, Baum ML, Bibb JA, Lombroso PJ. Extrasynaptic NMDA Receptors Couple Preferentially to Excitotoxicity via Calpain-Mediated Cleavage of STEP. Journal Of Neuroscience 2009, 29: 9330-9343. PMID: 19625523, PMCID: PMC2737362, DOI: 10.1523/jneurosci.2212-09.2009.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAnimalsBrainCalpainCell DeathCells, CulturedCyclin-Dependent Kinase 5EndocytosisGlutamic AcidIn Vitro TechniquesMiceMice, KnockoutMitogen-Activated Protein Kinase 1Mitogen-Activated Protein Kinase 3Neuronsp38 Mitogen-Activated Protein KinasesProtein Tyrosine Phosphatases, Non-ReceptorRatsRats, Sprague-DawleyReceptors, N-Methyl-D-AspartateSynapsesConceptsStriatal-enriched protein tyrosine phosphataseCalpain cleavage sitesP38 activationCell deathCleavage siteExtracellular signal-regulated kinase 1/2Protein tyrosine phosphataseSignal-regulated kinase 1/2Promotes cell survivalActivation of p38Tyrosine phosphataseSubstrate bindingKinase 1/2ERK1/2 activationCalpain cleavageCell survivalNovel mechanismCalpain-mediated proteolysisReceptors coupleP38NMDAR stimulationPostsynaptic terminalsValid targetCleavage productsSTEP substrates
2005
Repetitive stretch of human dermal fibroblast activates p38 and ERK1/2 but not AKT and results in apoptosis
Nishimura K, Blume P, Ohgi S, Sumpio B. Repetitive stretch of human dermal fibroblast activates p38 and ERK1/2 but not AKT and results in apoptosis. Journal Of The American College Of Surgeons 2005, 201: s59-s60. DOI: 10.1016/j.jamcollsurg.2005.06.132.Peer-Reviewed Original Research
2003
Fibronectin blocks p38 and jnk activation by cyclic strain in Caco-2 cells
Zhang J, Li W, Sumpio BE, Basson MD. Fibronectin blocks p38 and jnk activation by cyclic strain in Caco-2 cells. Biochemical And Biophysical Research Communications 2003, 306: 746-749. PMID: 12810082, DOI: 10.1016/s0006-291x(03)01044-1.Peer-Reviewed Original ResearchConceptsIntestinal epithelial responsesIntestinal epithelial proliferationCaco-2 intestinal epithelial cellsIntestinal epithelial cellsHuman Caco-2 intestinal epithelial cellsCaco-2 cellsPlasma fibronectinInfectious conditionsEpithelial responseFibronectin levelsEpithelial proliferationIntestinal epitheliumEpithelial cellsRepetitive forcesBasement membraneCollagen ICollagen IVIntracellular signalingP38JNK activationActivationCellsStrain activationTissueFibronectin
1998
YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF‐α production and downregulation of the MAP kinases p38 and JNK
Palmer L, Hobbie S, Galán J, Bliska J. YopJ of Yersinia pseudotuberculosis is required for the inhibition of macrophage TNF‐α production and downregulation of the MAP kinases p38 and JNK. Molecular Microbiology 1998, 27: 953-965. PMID: 9535085, DOI: 10.1046/j.1365-2958.1998.00740.x.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial Outer Membrane ProteinsCalcium-Calmodulin-Dependent Protein KinasesCell LineCloning, MolecularDown-RegulationEnzyme ActivationGene Expression Regulation, BacterialGenetic Complementation TestImmunoblottingJNK Mitogen-Activated Protein KinasesLipopolysaccharidesMacrophagesMiceMitogen-Activated Protein KinasesMutationp38 Mitogen-Activated Protein KinasesTumor Necrosis Factor-alphaYersinia pseudotuberculosisConceptsY. pseudotuberculosisTNF-alpha productionMitogen-activated protein kinaseType III pathwayWild-type Y. pseudotuberculosisWild-type strainTNF-alphaPathogenic Yersinia sppYop genesYop proteinsYop secretionProtein kinaseMAP kinaseTranslational levelMutantsExposure of macrophagesYopJYersinia pseudotuberculosisSustained activationMacrophage TNF-α productionJNKP38Yersinia sppTumor necrosis factor alphaJ774A.1 murine macrophages
1987
Biochemical and Immunocytochemical Characterization of p38, an Integral Membrane Glycoprotein of Small Synaptic Vesicles
JAHN R, NAVONE F, GREENGARD P, DE CAMILLI P. Biochemical and Immunocytochemical Characterization of p38, an Integral Membrane Glycoprotein of Small Synaptic Vesicles. Annals Of The New York Academy Of Sciences 1987, 493: 497-499. DOI: 10.1111/j.1749-6632.1987.tb27235.x.Peer-Reviewed Original Research
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