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
1999
Human epidermal Langerhans cells lack functional mannose receptors and a fully developed endosomal/lysosomal compartment for loading of HLA class II molecules
Mommaas A, Mulder A, Jordens R, Out C, Tan M, Cresswell P, Kluin P, Koning F. Human epidermal Langerhans cells lack functional mannose receptors and a fully developed endosomal/lysosomal compartment for loading of HLA class II molecules. European Journal Of Immunology 1999, 29: 571-580. PMID: 10064073, DOI: 10.1002/(sici)1521-4141(199902)29:02<571::aid-immu571>3.0.co;2-e.Peer-Reviewed Original ResearchConceptsHuman epidermal Langerhans cellsEpidermal Langerhans cellsLangerhans cellsT cellsAntigen-specific T cellsMannose receptorPeripheral blood mononuclear cellsHLA class II moleculesProtein antigensBlood-derived DCsBlood mononuclear cellsAntigen-presenting cellsNaive T cellsDendritic cell lineageClass II moleculesClass II compartmentsFunctional mannose receptorsLymph nodesAntigen uptakeMononuclear cellsMHC classEndocytic capacitySkin damageReceptor-mediated endocytosis pathwayAntigen
1998
Intracellular formation and cell surface expression of a complex of an intact lysosomal protein and MHC class II molecules.
Arunachalam B, Pan M, Cresswell P. Intracellular formation and cell surface expression of a complex of an intact lysosomal protein and MHC class II molecules. The Journal Of Immunology 1998, 160: 5797-806. PMID: 9637490, DOI: 10.4049/jimmunol.160.12.5797.Peer-Reviewed Original ResearchAllelesAnimalsCell Transformation, ViralElectrophoresis, Polyacrylamide GelFlow CytometryFluorescent Antibody Technique, IndirectHerpesvirus 4, HumanHistocompatibility Antigens Class IIHLA-D AntigensHLA-DR AntigensLysosomesMiceOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsProteinsRabbitsSodium Dodecyl SulfateSurface Properties
1996
HLA-DM Is Localized to Conventional and Unconventional MHC Class II–Containing Endocytic Compartments
Pierre P, Denzin L, Hammond C, Drake J, Amigorena S, Cresswell P, Mellman I. HLA-DM Is Localized to Conventional and Unconventional MHC Class II–Containing Endocytic Compartments. Immunity 1996, 4: 229-239. PMID: 8624813, DOI: 10.1016/s1074-7613(00)80431-8.Peer-Reviewed Original Research