2001
Quality 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
Misfolded 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
1995
Assembly, Intracellular Localization, and Nucleotide Binding Properties of the Human Peptide Transporters TAP1 and TAP2 Expressed by Recombinant Vaccinia Viruses (∗)
Russ G, Esquivel F, Yewdell J, Cresswell P, Spies T, Bennink J. Assembly, Intracellular Localization, and Nucleotide Binding Properties of the Human Peptide Transporters TAP1 and TAP2 Expressed by Recombinant Vaccinia Viruses (∗). Journal Of Biological Chemistry 1995, 270: 21312-21318. PMID: 7673167, DOI: 10.1074/jbc.270.36.21312.Peer-Reviewed Original ResearchMeSH KeywordsATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersCell LineDetergentsFluorescent Antibody TechniqueGlycosylationHumansMajor Histocompatibility ComplexMicroscopy, ConfocalNucleotidesProtein BindingRecombination, GeneticVaccinia virusMolecular Requirements for the Interaction of Class II Major Histocompatibility Complex Molecules and Invariant Chain with Calnexin (∗)
Arunachalam B, Cresswell P. Molecular Requirements for the Interaction of Class II Major Histocompatibility Complex Molecules and Invariant Chain with Calnexin (∗). Journal Of Biological Chemistry 1995, 270: 2784-2790. PMID: 7852350, DOI: 10.1074/jbc.270.6.2784.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 Research
1990
The 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