2000
Enzymatic reduction of disulfide bonds in lysosomes: Characterization of a Gamma-interferon-inducible lysosomal thiol reductase (GILT)
Arunachalam B, Phan U, Geuze H, Cresswell P. Enzymatic reduction of disulfide bonds in lysosomes: Characterization of a Gamma-interferon-inducible lysosomal thiol reductase (GILT). Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 745-750. PMID: 10639150, PMCID: PMC15401, DOI: 10.1073/pnas.97.2.745.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesCOS CellsDisulfidesDNA, ComplementaryEndosomesEnzyme InductionHumansHydrogen-Ion ConcentrationInterferon-gammaLysosomesMannosephosphatesMicroscopy, ImmunoelectronMolecular Sequence DataMutagenesisOxidation-ReductionProtein Disulfide Reductase (Glutathione)Protein Processing, Post-TranslationalSequence Analysis, DNATumor Cells, CulturedConceptsGamma interferon inducible lysosomal thiol reductaseLysosomal thiol reductaseThiol reductaseDisulfide bondsC-terminal prosequenceEndocytic pathwayThioredoxin familyCysteine residuesDisulfide bond reductionEfficient proteolysisCell typesAmino acidsLysosomal systemEnzymeLysosomesSoluble glycoproteinReductaseActive siteBond reductionAntigen processingImportant roleEnzymatic reductionMutagenesisThioredoxinProsequence
1998
Induction of transporter associated with antigen processing by interferon γ confers endothelial cell cytoprotection against natural killer-mediated lysis
Ayalon O, Hughes E, Cresswell P, Lee J, O’Donnell L, Pardi R, Bender J. Induction of transporter associated with antigen processing by interferon γ confers endothelial cell cytoprotection against natural killer-mediated lysis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 2435-2440. PMID: 9482903, PMCID: PMC19366, DOI: 10.1073/pnas.95.5.2435.Peer-Reviewed Original ResearchConceptsMHC IInduction of transportersEndothelial cellsNK-resistant cell linesNatural killer-mediated lysisMajor histocompatibility complex INK inhibitory receptorsNK effector cellsPretreatment of ECB-lymphoblastoid cell linesEC sensitivityDermal microvascular endothelial cellsMicrovascular endothelial cellsCell linesHuman umbilical vein endothelial cellsExpression/functionUmbilical vein endothelial cellsAdenoviral-mediated transductionVascular vulnerabilityVein endothelial cellsNK assaysEffector cellsEndothelial activationInhibitory receptorsDeficient targets
1997
The human cytomegalovirus US6 glycoprotein inhibits transporter associated with antigen processing-dependent peptide translocation
Lehner P, Karttunen J, Wilkinson G, Cresswell P. The human cytomegalovirus US6 glycoprotein inhibits transporter associated with antigen processing-dependent peptide translocation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 6904-6909. PMID: 9192664, PMCID: PMC21257, DOI: 10.1073/pnas.94.13.6904.Peer-Reviewed Original ResearchInterferon-γ Rapidly Increases Peptide Transporter (TAP) Subunit Expression and Peptide Transport Capacity in Endothelial Cells*
Ma W, Pober J, Johnson D, Lehner P, Cresswell P. Interferon-γ Rapidly Increases Peptide Transporter (TAP) Subunit Expression and Peptide Transport Capacity in Endothelial Cells*. Journal Of Biological Chemistry 1997, 272: 16585-16590. PMID: 9195970, DOI: 10.1074/jbc.272.26.16585.Peer-Reviewed Original Research
1996
Processing and delivery of peptides presented by MHC class I molecules
Lehner P, Cresswell P. Processing and delivery of peptides presented by MHC class I molecules. Current Opinion In Immunology 1996, 8: 59-67. PMID: 8729447, DOI: 10.1016/s0952-7915(96)80106-3.Peer-Reviewed Original ResearchAnimalsAntigen PresentationATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersCysteine EndopeptidasesCytotoxicity, ImmunologicEndoplasmic ReticulumEpitopesHistocompatibility Antigens Class IHumansInterferon-gammaMiceMice, KnockoutModels, MolecularMultienzyme ComplexesProteasome Endopeptidase Complex