2022
Proteasomal degradation within endocytic organelles can mediate antigen cross- presentation
Sengupta D, Graham M, Liu X, Cresswell P. Proteasomal degradation within endocytic organelles can mediate antigen cross- presentation. Molecular Immunology 2022, 150: 23. DOI: 10.1016/j.molimm.2022.05.080.Peer-Reviewed Original ResearchDendritic cellsMHC-I moleculesMouse bone marrow-derived dendritic cellsBone marrow-derived dendritic cellsMarrow-derived dendritic cellsAntigen processingConventional antigen processingMouse dendritic cellsMHC-I-peptide complexesSurface MHCMHCSurface expressionProteasome inhibitionPeptide loadingHuman B2Cell phagosomesCell typesActive proteasomesSpecific peptidesCellsPeptidesEndocytic compartmentsProteasomal degradationEndocytic pathway
2001
Maintenance of TCR clonality in T cells expressing genes for two TCR heterodimers
Sant'Angelo D, Cresswell P, Janeway C, Denzin L. Maintenance of TCR clonality in T cells expressing genes for two TCR heterodimers. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 6824-6829. PMID: 11381132, PMCID: PMC34437, DOI: 10.1073/pnas.121179998.Peer-Reviewed Original ResearchConceptsAllelic exclusionTCR heterodimerTCR proteinsCell surface expressionTCR lociT cellsCell surfaceFurther recombinationProteinAlpha chainBeta chainHeterodimersSurface expressionTransgenic miceTCR transgenic miceCellsAdditional mechanismExpressionTCR clonalityAssembly processGenesSecond TCRLociRNATCR
1998
Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors.
Deng Y, Gibbs J, Bačík I, Porgador A, Copeman J, Lehner P, Ortmann B, Cresswell P, Bennink J, Yewdell J. Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors. The Journal Of Immunology 1998, 161: 1677-85. PMID: 9712031, DOI: 10.4049/jimmunol.161.4.1677.Peer-Reviewed Original ResearchMeSH KeywordsAedesAnimalsAntibodies, MonoclonalAntiportersCell LineEndoplasmic ReticulumH-2 AntigensHeLa CellsHumansImmunoglobulinsLymphocyte ActivationMacromolecular SubstancesMembrane Transport ProteinsMiceOligopeptidesOvalbuminPeptide FragmentsProtease InhibitorsRecombinant ProteinsT-LymphocytesVaccinia virusConceptsInsect cellsEndoplasmic reticulumVertebrate cellsHuman cellsHuman tapasinVaccinia virus-mediated expressionCell surface expressionProtease inhibitorsInefficient assemblyKbMHC class IMouse betaInsectsEfficient assemblyImmediate precursorSurface expressionAntigenic peptidesHeavy chainClass IRecombinant vaccinia virusVirus-mediated expressionAssemblyExpressionCellsVaccinia virus
1990
Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding
Roche P, Cresswell P. Invariant chain association with HLA-DR molecules inhibits immunogenic peptide binding. Nature 1990, 345: 615-618. PMID: 2190094, DOI: 10.1038/345615a0.Peer-Reviewed Original ResearchConceptsClass II moleculesImmunogenic peptidesMHC moleculesClass II major histocompatibility complex moleculesClass II MHC moleculesMajor histocompatibility complex moleculesClass I MHC moleculesHLA-DR moleculesII MHC moleculesHistocompatibility complex moleculesI MHC moleculesClass I moleculesIntracellular class II moleculesCell surface expressionT lymphocytesPresent immunogenic peptidesClass IIProtein antigensClass IInvariant chain associationI moleculesCell surface glycoproteinSurface expressionInvariant chainFunctional dichotomy