2001
Defective Antigen Processing in GILT-Free Mice
Maric M, Arunachalam B, Phan U, Dong C, Garrett W, Cannon K, Alfonso C, Karlsson L, Flavell R, Cresswell P. Defective Antigen Processing in GILT-Free Mice. Science 2001, 294: 1361-1365. PMID: 11701933, DOI: 10.1126/science.1065500.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsAntigen PresentationAntigen-Presenting CellsAntigensCell LineDendritic CellsDisulfidesEpitopesHistocompatibility Antigens Class IIHybridomasHydrogen-Ion ConcentrationImmunizationMiceMice, Inbred C57BLMice, KnockoutMolecular Sequence DataMuramidaseOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsProtein ConformationProtein FoldingSpleenT-Lymphocytes
2000
Gamma-Interferon-inducibleLysosomal Thiol Reductase (GILT) MATURATION, ACTIVITY, AND MECHANISM OF ACTION*
Phan U, Arunachalam B, Cresswell P. Gamma-Interferon-inducibleLysosomal Thiol Reductase (GILT) MATURATION, ACTIVITY, AND MECHANISM OF ACTION*. Journal Of Biological Chemistry 2000, 275: 25907-25914. PMID: 10852914, DOI: 10.1074/jbc.m003459200.Peer-Reviewed Original ResearchEnzymatic 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
1995
HLA-DM induces clip dissociation from MHC class II αβ dimers and facilitates peptide loading
Denzin L, Cresswell P. HLA-DM induces clip dissociation from MHC class II αβ dimers and facilitates peptide loading. Cell 1995, 82: 155-165. PMID: 7606781, DOI: 10.1016/0092-8674(95)90061-6.Peer-Reviewed Original Research
1974
Papain-solubilized HL-A Antigens CHROMATOGRAPHIC AND ELECTROPHORETIC STUDIES OF THE TWO SUBUNITS FROM DIFFERENT SPECIFICITIES
Cresswell P, Robb R, Turner M, Strominger J. Papain-solubilized HL-A Antigens CHROMATOGRAPHIC AND ELECTROPHORETIC STUDIES OF THE TWO SUBUNITS FROM DIFFERENT SPECIFICITIES. Journal Of Biological Chemistry 1974, 249: 2828-2832. PMID: 4828322, DOI: 10.1016/s0021-9258(19)42705-1.Peer-Reviewed Original Research