2000
Selective Inhibition of NF-κB Activation by a Peptide That Blocks the Interaction of NEMO with the IκB Kinase Complex
May M, D'Acquisto F, Madge L, Glöckner J, Pober J, Ghosh S. Selective Inhibition of NF-κB Activation by a Peptide That Blocks the Interaction of NEMO with the IκB Kinase Complex. Science 2000, 289: 1550-1554. PMID: 10968790, DOI: 10.1126/science.289.5484.1550.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAnti-Inflammatory Agents, Non-SteroidalCells, CulturedCOS CellsE-SelectinEndothelium, VascularGene Expression RegulationHeLa CellsHumansI-kappa B KinaseInflammationMiceMice, Inbred C57BLMolecular Sequence DataMutationNF-kappa BPeptidesPoint MutationProtein Serine-Threonine KinasesProtein Structure, TertiaryRecombinant Fusion ProteinsConceptsNF-kappaBBasal NF-kappaB activityExperimental mouse modelTranscription factor nuclear factorCytokine-induced NF-kappaB activationCell-permeable NBD peptideInhibitor of kappaBNF-κB activationNF-kappaB activityNF-kappaB activationAssociation of NEMOIKK complexAcute inflammationDevelopment of drugsProinflammatory activationInflammatory responseNBD peptideMouse modelProinflammatory stimuliIκB kinase (IKK) complexNuclear factorRegulatory protein NEMOInflammationSelective inhibitionExpression of genes
1996
Porcine endothelial CD86 is a major costimulator of xenogeneic human T cells: cloning, sequencing, and functional expression in human endothelial cells.
Maher SE, Karmann K, Min W, Hughes CC, Pober JS, Bothwell AL. Porcine endothelial CD86 is a major costimulator of xenogeneic human T cells: cloning, sequencing, and functional expression in human endothelial cells. The Journal Of Immunology 1996, 157: 3838-44. PMID: 8892613, DOI: 10.4049/jimmunol.157.9.3838.Peer-Reviewed Original ResearchAbataceptAmino Acid SequenceAnimalsAntigens, CDAntigens, DifferentiationAortaB7-2 AntigenBase SequenceCells, CulturedCHO CellsCloning, MolecularCricetinaeCricetulusCTLA-4 AntigenDNA, ComplementaryEndothelium, VascularHumansImmunoconjugatesInterleukin-2Lymphocyte ActivationMembrane GlycoproteinsMolecular Sequence DataSequence AlignmentSequence Homology, Amino AcidSpecies SpecificitySwineT-LymphocytesTransfectionUmbilical Veins
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
1980
Chapter 4 Complete Primary Structure of Human Histocompatibility Antigen Hla-B7: Evolutionary and Functional Implications
Strominger J, Engelhard V, Guild B, Kostyk T, Lancet D, de Castro J, Orr H, Parham P, Ploegh H, Pober J. Chapter 4 Complete Primary Structure of Human Histocompatibility Antigen Hla-B7: Evolutionary and Functional Implications. Current Topics In Developmental Biology 1980, 14: 97-113. PMID: 7460613, DOI: 10.1016/s0070-2153(08)60190-8.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsMeSH KeywordsAmino Acid SequenceDetergentsHLA AntigensHumansImmunoglobulinsLiposomesPapainProtein PrecursorsStructure-Activity RelationshipConceptsComplete primary structurePrimary structureCommon ancestral geneMajor histocompatibility complex (MHC) genesRecombinant DNA techniquesDevelopment of animalsAncestral genePrimitive organismsComplex genesDefense moleculesDNA techniquesGenesFunctional implicationsDefense functionsOrganismsDefense mechanismsRelated cellsGenomeCloningDuplicationHistocompatibility antigensCirculatory systemInvasionMembraneCells
1978
Phosphorylation in vivo and in vitro of human histocompatibility antigens (HLA-A and HLA-B) in the carboxy-terminal intracellular domain.
Pober JS, Guild BC, Strominger JL. Phosphorylation in vivo and in vitro of human histocompatibility antigens (HLA-A and HLA-B) in the carboxy-terminal intracellular domain. Proceedings Of The National Academy Of Sciences Of The United States Of America 1978, 75: 6002-6006. PMID: 282620, PMCID: PMC393105, DOI: 10.1073/pnas.75.12.6002.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceCell LineCell MembraneHLA AntigensHumansLymphocytesMacromolecular SubstancesMembrane ProteinsPhosphorylationProtein Kinases