1998
The N-terminal domains target TNF receptor-associated factor-2 to the nucleus and display transcriptional regulatory activity.
Min W, Bradley JR, Galbraith JJ, Jones SJ, Ledgerwood EC, Pober JS. The N-terminal domains target TNF receptor-associated factor-2 to the nucleus and display transcriptional regulatory activity. The Journal Of Immunology 1998, 161: 319-24. PMID: 9647239, DOI: 10.4049/jimmunol.161.1.319.Peer-Reviewed Original ResearchMeSH KeywordsBiological TransportCell NucleusCells, CulturedCytoplasmEndothelium, VascularFluorescent Antibody Technique, IndirectHumansPeptide FragmentsProtein BiosynthesisProtein Structure, TertiaryProteinsReceptors, Tumor Necrosis FactorTNF Receptor-Associated Factor 2Transcription, GeneticTransfectionUmbilical VeinsConceptsFinger domainAmino-terminal RING finger domainNuclear localizationTNF receptor-associated factor 2Cytoplasmic signal transductionReceptor-associated factor 2Zinc finger domainTranscriptional regulatory activityAmino-terminal halfC-Jun N-terminal kinase (JNK) activationRING finger domainProminent nuclear localizationConfocal immunofluorescence microscopyWestern blottingTRAF2 moleculeAdaptor proteinDeletion mutantsSignal transductionSubcellular localizationGene transcriptionKinase activationHuman endothelial cellsTRAF2 proteinCell extractsHuman endothelial cell line
1992
Calcium/calmodulin transduces thrombin-stimulated secretion: studies in intact and minimally permeabilized human umbilical vein endothelial cells.
Birch KA, Pober JS, Zavoico GB, Means AR, Ewenstein BM. Calcium/calmodulin transduces thrombin-stimulated secretion: studies in intact and minimally permeabilized human umbilical vein endothelial cells. Journal Of Cell Biology 1992, 118: 1501-1510. PMID: 1522120, PMCID: PMC2289613, DOI: 10.1083/jcb.118.6.1501.Peer-Reviewed Original ResearchConceptsVon Willebrand factorEndothelial cellsProtein kinase CCell-permeant calcium chelatorExtracellular calcium chelator EGTAVWF secretionAgonist-induced elevationInhibitory peptidesSignal transduction pathwaysHuman umbilical vein endothelial cellsUmbilical vein endothelial cellsCultured endothelial cellsCalcium chelator EGTAPermeabilized human umbilical vein endothelial cellsVein endothelial cellsHuman endothelial cellsPhorbol esterRole of calmodulinSecond messenger pathwaysIntracellular calciumIntact human endothelial cellsTransduction pathwaysThrombin receptorCalcium ionophoreLarge intracellular protein
1982
[34] Proteolysis of rhodopsin
Pober J. [34] Proteolysis of rhodopsin. Methods In Enzymology 1982, 81: 236-239. PMID: 7047990, DOI: 10.1016/s0076-6879(82)81036-7.Peer-Reviewed Original ResearchConceptsLight-activated enzymesOrganization of rhodopsinMembrane proteinsPolypeptide sequenceHigh-resolution mappingConformational changesLimited proteolysisBovine rhodopsinCleavage siteRod outer segmentsRhodopsinProteolysisRegion of interactionDisk membranesResolution mappingSpecific sitesOuter segmentsValuable probe
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