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
Elucidation of the genetic basis of the antigen presentation defects in the mutant cell line .220 reveals polymorphism and alternative splicing of the tapasin gene
Copeman J, Bangia N, Cross J, Cresswell P. Elucidation of the genetic basis of the antigen presentation defects in the mutant cell line .220 reveals polymorphism and alternative splicing of the tapasin gene. European Journal Of Immunology 1998, 28: 3783-3791. PMID: 9842921, DOI: 10.1002/(sici)1521-4141(199811)28:11<3783::aid-immu3783>3.0.co;2-9.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersB-LymphocytesCell LineDNA, ComplementaryEndoplasmic ReticulumExonsHumansImmunoglobulinsMembrane Transport ProteinsMutationPolymorphism, GeneticReverse Transcriptase Polymerase Chain ReactionConceptsMutant cell linesEndoplasmic reticulumAlternative splicingN-terminal 49 amino acidsGenetic basisTapasin geneExon twoWild-type cellsFull-length transcriptsCell linesSingle nucleotide substitutionSignal peptideSecond intronNucleotide substitutionsPhysical associationSplice siteGlycoprotein tapasinPosition 240Amino acidsClass I moleculesSplicingOptimal bindingGenesI moleculesHeterodimers
1994
Human transporters associated with antigen processing possess a promiscuous peptide-binding site
Androlewicz M, Cresswell P. Human transporters associated with antigen processing possess a promiscuous peptide-binding site. Immunity 1994, 1: 7-14. PMID: 7889401, DOI: 10.1016/1074-7613(94)90004-3.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceAntigen PresentationATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBinding SitesBinding, CompetitiveBiological Transport, ActiveCarrier ProteinsCell LineHistocompatibility Antigens Class IHumansMolecular Sequence DataOligopeptidesAssembly and Transport of Class I MHC‐Peptide Complexes
Cresswell P, Androlewicz M, Ortmann B. Assembly and Transport of Class I MHC‐Peptide Complexes. Novartis Foundation Symposia 1994, 187: 150-169. PMID: 7796669, DOI: 10.1002/9780470514672.ch10.Peer-Reviewed Original ResearchConceptsTAP moleculesComplex moleculesPeptide derivativesMoleculesLonger peptidesClass I MHC-peptide complexesPeptide-binding siteComplexesClass I-peptide complexesPeptidesCompetition experimentsAssemblyAmino acidsDimersDerivativesClass I major histocompatibility complex moleculesWide rangeChainMHC-peptide complexesAcidTransportSurface