1999
TNF recruits TRADD to the plasma membrane but not the trans-Golgi network, the principal subcellular location of TNF-R1.
Jones S, Ledgerwood E, Prins J, Galbraith J, Johnson D, Pober J, Bradley J. TNF recruits TRADD to the plasma membrane but not the trans-Golgi network, the principal subcellular location of TNF-R1. The Journal Of Immunology 1999, 162: 1042-8. PMID: 9916731, DOI: 10.4049/jimmunol.162.2.1042.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigens, CDAortaBrefeldin ACattleCell CompartmentationCell Line, TransformedCell MembraneEndothelium, VascularGolgi ApparatusHumansMicroscopy, ConfocalProteinsReceptors, Tumor Necrosis FactorReceptors, Tumor Necrosis Factor, Type ISubcellular FractionsTNF Receptor-Associated Factor 1TransfectionTumor Necrosis Factor-alphaU937 CellsConceptsTrans-Golgi networkPlasma membraneTNF-R1Golgi regionConfocal immunofluorescence microscopyHuman endothelial cell line ECV304Endothelial cell line ECV304Receptor-mediated endocytosisAdaptor proteinSubcellular localizationSubcellular locationCell fractionationBovine aortic endothelial cellsCoimmunoprecipitation studiesEndothelial cellsTRADDCell line U937Golgi apparatusSubcellular interactionsWestern blot analysisCell extractsMonocyte cell line U937Expression plasmidGolgiImmunofluorescence microscopy
1996
"Cytosolic" phospholipase A2 is in the nucleus of subconfluent endothelial cells but confined to the cytoplasm of confluent endothelial cells and redistributes to the nuclear envelope and cell junctions upon histamine stimulation.
Sierra-Honigmann MR, Bradley JR, Pober JS. "Cytosolic" phospholipase A2 is in the nucleus of subconfluent endothelial cells but confined to the cytoplasm of confluent endothelial cells and redistributes to the nuclear envelope and cell junctions upon histamine stimulation. Laboratory Investigation 1996, 74: 684-95. PMID: 8600319.Peer-Reviewed Original ResearchConceptsSubconfluent endothelial cellsConfluent endothelial cellsNuclear envelopeNuclear localizationConfocal immunofluorescence microscopyEndothelial cellsDose-dependent redistributionGrowth-arrested cellsSubcellular localizationCell density dependencePlasma membraneCell cycleCytoplasmic enzymeNuclear extractsCell junctionsPhospholipase A2 enzymeBovine endothelial cellsHeLa cellsImmunofluorescence microscopyCell lysatesCell nucleiIntercellular junctionsSubconfluent cellsPredominant MrAcid metabolism
1994
cAMP and tumor necrosis factor competitively regulate transcriptional activation through and nuclear factor binding to the cAMP-responsive element/activating transcription factor element of the endothelial leukocyte adhesion molecule-1 (E-selectin) promoter.
De Luca LG, Johnson DR, Whitley MZ, Collins T, Pober JS. cAMP and tumor necrosis factor competitively regulate transcriptional activation through and nuclear factor binding to the cAMP-responsive element/activating transcription factor element of the endothelial leukocyte adhesion molecule-1 (E-selectin) promoter. Journal Of Biological Chemistry 1994, 269: 19193-19196. PMID: 7518452, DOI: 10.1016/s0021-9258(17)32150-6.Peer-Reviewed Original ResearchConceptsConsensus cAMP-responsive elementCRE-binding proteinTranscription factor elementsTranscriptional activationCRE/ATF elementElectrophoretic mobility shift assaysMobility shift assaysTransient transfection assaysAntibody supershift assaysCAMP-responsive elementMigrating formPromoter elementsDNA sequencesFastest migrating formBovine aortic endothelial cellsShift assaysTransfection assaysPromoter responseSupershift assaysGene expressionFactor elementsC-JunAortic endothelial cellsEffects of TNFProtein
1979
Light-regulated enzymes of vertebrate retinal rods.
Pober JS, Bitensky MW. Light-regulated enzymes of vertebrate retinal rods. Advances In Second Messenger And Phosphoprotein Research 1979, 11: 265-301. PMID: 227247.Peer-Reviewed Original Research
1978
Transglutaminase-catalyzed insertion of a fluorescent probe into the protease-sensitive region of rhodopsin.
Pober JS, Iwanij V, Reich E, Stryer L. Transglutaminase-catalyzed insertion of a fluorescent probe into the protease-sensitive region of rhodopsin. Biochemistry 1978, 17: 2163-8. PMID: 27209, DOI: 10.1021/bi00604a021.Peer-Reviewed Original Research
1975
Light dissociates enzymatically-cleaved rhodopsin into two different fragments
Pober J, Stryer L. Light dissociates enzymatically-cleaved rhodopsin into two different fragments. Journal Of Molecular Biology 1975, 95: 477-481. PMID: 1171252, DOI: 10.1016/0022-2836(75)90204-1.Peer-Reviewed Original Research