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
The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex
Hughes E, Cresswell P. The thiol oxidoreductase ERp57 is a component of the MHC class I peptide-loading complex. Current Biology 1998, 8: 709-713. PMID: 9637923, DOI: 10.1016/s0960-9822(98)70278-7.Peer-Reviewed Original ResearchAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersCalcium-Binding ProteinsCalreticulinEndoplasmic ReticulumHeat-Shock ProteinsHeLa CellsHistocompatibility Antigens Class IHumansImmunoglobulinsIsomerasesMembrane Transport ProteinsPeptidesProtein Disulfide Reductase (Glutathione)Protein Disulfide-IsomerasesRibonucleoproteins