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
1986
Two distinct monokines, interleukin 1 and tumor necrosis factor, each independently induce biosynthesis and transient expression of the same antigen on the surface of cultured human vascular endothelial cells.
Pober JS, Bevilacqua MP, Mendrick DL, Lapierre LA, Fiers W, Gimbrone MA. Two distinct monokines, interleukin 1 and tumor necrosis factor, each independently induce biosynthesis and transient expression of the same antigen on the surface of cultured human vascular endothelial cells. The Journal Of Immunology 1986, 136: 1680-7. PMID: 3485132, DOI: 10.4049/jimmunol.136.5.1680.Peer-Reviewed Original Research
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 ResearchMeSH KeywordsAnimalsCell MembraneElectrophoresis, Polyacrylamide GelMolecular WeightPeptide FragmentsPeptide HydrolasesPhotoreceptor CellsRetinal PigmentsRhodopsinConceptsLight-activated enzymesOrganization of rhodopsinMembrane proteinsPolypeptide sequenceHigh-resolution mappingConformational changesLimited proteolysisBovine rhodopsinCleavage siteRod outer segmentsRhodopsinProteolysisRegion of interactionDisk membranesResolution mappingSpecific sitesOuter segmentsValuable probe
1981
Purification of HLA-A2 antigen, fluorescent labeling of its intracellular region, and demonstration of an interaction between fluorescently labeled HLA-A2 antigen and lymphoblastoid cell cytoskeleton proteins in vitro.
Pober J, Guild B, Strominger J, Veatch W. Purification of HLA-A2 antigen, fluorescent labeling of its intracellular region, and demonstration of an interaction between fluorescently labeled HLA-A2 antigen and lymphoblastoid cell cytoskeleton proteins in vitro. Biochemistry 1981, 20: 5625-33. PMID: 6975122, DOI: 10.1021/bi00522a042.Peer-Reviewed Original ResearchMeSH KeywordsActinsAntibodies, MonoclonalCell MembraneElectrophoresis, Polyacrylamide GelFluorescent DyesHLA AntigensHLA-A2 AntigenHumansIodoacetamideLymphocytesMembrane ProteinsNaphthalenesulfonates