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-LymphocytesQuality control of transmembrane domain assembly in the tetraspanin CD82
Cannon K, Cresswell P. Quality control of transmembrane domain assembly in the tetraspanin CD82. The EMBO Journal 2001, 20: 2443-2453. PMID: 11350933, PMCID: PMC125455, DOI: 10.1093/emboj/20.10.2443.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumTransmembrane segmentsDomain assemblyER quality controlFirst transmembrane segmentMore transmembrane segmentsER membraneER lumenChaperone calnexinSeparate polypeptidesTetraspanin CD82TM-1Extracellular domainCalnexinNative structureCell surfaceTM-2Lipid bilayersCD82AssemblyQuality controlPrimary mechanismProlonged interactionPolypeptideCalreticulinGlycosylation and the Immune System
Rudd P, Elliott T, Cresswell P, Wilson I, Dwek R. Glycosylation and the Immune System. Science 2001, 291: 2370-2376. PMID: 11269318, DOI: 10.1126/science.291.5512.2370.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAntigen PresentationAntigen-Antibody ReactionsAntigen-Presenting CellsAntigens, CD1Carrier ProteinsCollectinsComplement System ProteinsEndoplasmic ReticulumEpitopesGlycoproteinsGlycosylationHistocompatibility AntigensHumansImmune SystemImmunoglobulinsPolysaccharidesProtein FoldingT-LymphocytesViral Envelope ProteinsConceptsImmune systemMajor histocompatibility complex antigensAntigen-presenting cellsAdaptive immune responsesCellular immune systemHistocompatibility complex antigensHumoral immune systemT cell receptor complexRheumatoid arthritisMannose-binding lectinAutoimmune diseasesCell receptor complexT cellsImmune responseComplex antigensPeptide antigensComplement componentsImmunoglobulin GAntigenKey moleculesReceptor complexSpecific glycoformsGlycoproteinGlycopeptide antigensArthritis
1997
Protein degradation: The ins and outs of the matter
Cresswell P, Hughes E. Protein degradation: The ins and outs of the matter. Current Biology 1997, 7: r552-r555. PMID: 9285707, DOI: 10.1016/s0960-9822(06)00279-x.Peer-Reviewed Original ResearchMisfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome
Hughes E, Hammond C, Cresswell P. Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 1896-1901. PMID: 9050876, PMCID: PMC20014, DOI: 10.1073/pnas.94.5.1896.Peer-Reviewed Original ResearchMeSH KeywordsAcetylcysteineBeta 2-MicroglobulinBlotting, WesternCysteine EndopeptidasesCysteine Proteinase InhibitorsCytoplasmEndoplasmic ReticulumEnzyme InhibitorsGlycosylationHistocompatibility Antigens Class IHumansKineticsLeupeptinsMultienzyme ComplexesProteasome Endopeptidase ComplexProtein FoldingSolubilityTransfectionTumor Cells, CulturedConceptsClass I heavy chainsMHC class I heavy chainMajor histocompatibility complex class I heavy chainsBeta2-microglobulinHeavy chainMHC class ICell linesCell line DaudiTAP-deficient cell linesSpecific irreversible inhibitorClass IHerpes simplex virus proteinDaudiVirus proteinsEndoplasmic reticulumIrreversible inhibitorSimilar accumulationLactacystinPeriod of hours