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
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
1992
Chemistry and functional role of the invariant chain
Cresswell P. Chemistry and functional role of the invariant chain. Current Opinion In Immunology 1992, 4: 87-92. PMID: 1317713, DOI: 10.1016/0952-7915(92)90131-w.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigensExocytosisGlycosylationHistocompatibility Antigens Class IIHLA-D AntigensHumansMiceMolecular StructurePeptide FragmentsProtein BindingProtein ConformationProtein Processing, Post-TranslationalStructure-Activity Relationship
1990
Transport and expression of HLA class-II glycoproteins
Cresswell P, Blum J, Davis J, Marks M. Transport and expression of HLA class-II glycoproteins. Immunologic Research 1990, 9: 190-199. PMID: 2121862, DOI: 10.1007/bf02918178.Peer-Reviewed Original ResearchB-LymphocytesCell LineEndocytosisEndopeptidasesGene Expression RegulationGenes, MHC Class IIHLA-D AntigensHumansLeupeptinsMembrane GlycoproteinsProtein Processing, Post-TranslationalThe transport of class I major histocompatibility complex antigens is determined by sequences in the α1 and α2 protein domains
Alexander J, Payne J, Shigekawa B, Frelinger J, Cresswell P. The transport of class I major histocompatibility complex antigens is determined by sequences in the α1 and α2 protein domains. Immunogenetics 1990, 31: 169-178. PMID: 2318516, DOI: 10.1007/bf00211552.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsAntigens, SurfaceBiological TransportCell LineElectricityElectrophoresis, Gel, Two-DimensionalExonsFlow CytometryGlycosylationHistocompatibility Antigens Class IHLA-B7 AntigenHumansMiceMolecular Sequence DataProtein ConformationProtein Processing, Post-TranslationalRecombinant ProteinsT-LymphocytesTransfection