1995
Disparate localization of 55-kd and 75-kd tumor necrosis factor receptors in human endothelial cells.
Bradley JR, Thiru S, Pober JS. Disparate localization of 55-kd and 75-kd tumor necrosis factor receptors in human endothelial cells. American Journal Of Pathology 1995, 146: 27-32. PMID: 7856733, PMCID: PMC1870772.Peer-Reviewed Original ResearchConceptsTumor necrosis factor receptorNecrosis factor receptorCell surfaceFactor receptorConfocal immunofluorescence microscopyDisparate localizationUndergoes endocytosisCultured human umbilical vein endothelial cellsHuman umbilical vein endothelial cellsEndothelial cellsUmbilical vein endothelial cellsReceptor clusteringGolgi apparatusHuman endothelial cellsCoated vesiclesVein endothelial cellsImmunofluorescence microscopyCellular distributionTNF receptorEndothelial cell activationCell activationReceptorsCytoplasmic vacuolesCellsEndocytosis
1993
Tumor necrosis factor activates human endothelial cells through the p55 tumor necrosis factor receptor but the p75 receptor contributes to activation at low tumor necrosis factor concentration.
Slowik MR, De Luca LG, Fiers W, Pober JS. Tumor necrosis factor activates human endothelial cells through the p55 tumor necrosis factor receptor but the p75 receptor contributes to activation at low tumor necrosis factor concentration. American Journal Of Pathology 1993, 143: 1724-30. PMID: 7504889, PMCID: PMC1887273.Peer-Reviewed Original ResearchConceptsEndothelial leukocyte adhesion molecule-1Endothelial cellsHuman endothelial cellsTumor necrosis factor concentrationsMonoclonal antibodiesNecrosis factor concentrationsLeukocyte adhesion molecule-1Major histocompatibility complex moleculesActivation of ECTumor necrosis factorAdhesion molecule-1Class I major histocompatibility complex moleculesLeukocyte adhesion moleculesTumor necrosis factor receptorELAM-1 inductionRecombinant human TNFHistocompatibility complex moleculesNecrosis factor receptorCultured endothelial cellsP75 receptorTumor necrosisNecrosis factorMolecule-1Receptor typesTNF receptor
1992
Thrombin and histamine rapidly stimulate the phosphorylation of the myristoylated alanine‐rich C‐kinase substrate in human umbilical vein endothelial cells: Evidence for distinct patterns of protein kinase activation
Jacobson B, Pober J, Fenton J, Ewenstein B. Thrombin and histamine rapidly stimulate the phosphorylation of the myristoylated alanine‐rich C‐kinase substrate in human umbilical vein endothelial cells: Evidence for distinct patterns of protein kinase activation. Journal Of Cellular Physiology 1992, 152: 166-176. PMID: 1320036, DOI: 10.1002/jcp.1041520121.Peer-Reviewed Original ResearchMeSH KeywordsCells, CulturedDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEndothelium, VascularEnzyme ActivationHistamineHumansIntracellular Signaling Peptides and ProteinsMembrane ProteinsMolecular WeightMyristoylated Alanine-Rich C Kinase SubstratePhosphorylationPrecipitin TestsProtein KinasesProteinsReceptors, Cell SurfaceThrombin
1991
Identification of a novel high molecular weight protein preferentially expressed by sinusoidal endothelial cells in normal human tissues.
Goerdt S, Walsh LJ, Murphy GF, Pober JS. Identification of a novel high molecular weight protein preferentially expressed by sinusoidal endothelial cells in normal human tissues. Journal Of Cell Biology 1991, 113: 1425-1437. PMID: 2045420, PMCID: PMC2289031, DOI: 10.1083/jcb.113.6.1425.Peer-Reviewed Original ResearchConceptsSinusoidal endothelial cellsEndothelial cellsPeripheral blood mononuclear cellsMS-1 antigenDendritic cell populationsEndothelial cell antigensBlood mononuclear cellsHigh endothelial venulesHuman umbilical vein endothelial cellsUmbilical vein endothelial cellsVein endothelial cellsLymph nodesKG-1 cellsNormal human tissuesMononuclear cellsLymphoid tissueAdrenal cortexEndothelial venulesCell line KG-1Cell line U937Cell antigensSplenic tissueSinusoidal endotheliumSplenic extractSpleen
1987
Identification of an inducible endothelial-leukocyte adhesion molecule.
Bevilacqua MP, Pober JS, Mendrick DL, Cotran RS, Gimbrone MA. Identification of an inducible endothelial-leukocyte adhesion molecule. Proceedings Of The National Academy Of Sciences Of The United States Of America 1987, 84: 9238-9242. PMID: 2827173, PMCID: PMC299728, DOI: 10.1073/pnas.84.24.9238.Peer-Reviewed Original ResearchConceptsHuman endothelial cellsCell surface proteinsEndothelial cell surface proteinsUnstimulated human endothelial cellsCell surface structuresHL-60 cellsSame polypeptideHL-60 adhesionCultured human endothelial cellsAdhesion assaysAdhesive interactionsH18/7Adhesion moleculesCytokine-stimulated human endothelial cellsDependent fashionCell surface antigensEndothelial cellsEndothelial leukocyte adhesion moleculeEndothelial leukocyte adhesion molecule-1AdhesionCellsAdhesion molecule-1Monoclonal antibodiesSites of inflammationLesser extent
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