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 interactionPolypeptideCalreticulinA Role for Calnexin in the Assembly of the MHC Class I Loading Complex in the Endoplasmic Reticulum
Diedrich G, Bangia N, Pan M, Cresswell P. A Role for Calnexin in the Assembly of the MHC Class I Loading Complex in the Endoplasmic Reticulum. The Journal Of Immunology 2001, 166: 1703-1709. PMID: 11160214, DOI: 10.4049/jimmunol.166.3.1703.Peer-Reviewed Original ResearchAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersCalcium-Binding ProteinsCalnexinCalreticulinCell Line, TransformedDimerizationEndoplasmic ReticulumHeat-Shock ProteinsHeLa CellsHistocompatibility Antigens Class IHLA AntigensHumansImmunoglobulinsIsomerasesKineticsMajor Histocompatibility ComplexMembrane Transport ProteinsProtein BindingProtein Disulfide-IsomerasesRibonucleoproteinsTumor Cells, Cultured
1999
The N‐terminal region of tapasin is required to stabilize the MHC class I loading complex
Bangia N, Lehner P, Hughes E, Surman M, Cresswell P. The N‐terminal region of tapasin is required to stabilize the MHC class I loading complex. European Journal Of Immunology 1999, 29: 1858-1870. PMID: 10382748, DOI: 10.1002/(sici)1521-4141(199906)29:06<1858::aid-immu1858>3.0.co;2-c.Peer-Reviewed Original ResearchAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBase SequenceBeta 2-MicroglobulinBinding SitesBiological Transport, ActiveCalcium-Binding ProteinsCalreticulinCell LineDNA PrimersDrug StabilityHeat-Shock ProteinsHistocompatibility Antigens Class IHumansImmunoglobulinsIsomerasesKineticsMacromolecular SubstancesMembrane Transport ProteinsMolecular ChaperonesProtein BindingProtein Disulfide-IsomerasesRibonucleoproteins
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
1997
A Critical Role for Tapasin in the Assembly and Function of Multimeric MHC Class I-TAP Complexes
Ortmann B, Copeman J, Lehner P, Sadasivan B, Herberg J, Grandea A, Riddell S, Tampé R, Spies T, Trowsdale J, Cresswell P. A Critical Role for Tapasin in the Assembly and Function of Multimeric MHC Class I-TAP Complexes. Science 1997, 277: 1306-1309. PMID: 9271576, DOI: 10.1126/science.277.5330.1306.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAntigen PresentationAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersCalcium-Binding ProteinsCalreticulinCell LineCell Line, TransformedChromosome MappingChromosomes, Human, Pair 6Cloning, MolecularDimerizationEndoplasmic ReticulumGenetic LinkageHistocompatibility Antigens Class IHLA AntigensHumansImmunoglobulin GImmunoglobulinsMajor Histocompatibility ComplexMembrane Transport ProteinsMolecular Sequence DataRibonucleoproteinsSequence Homology, Amino AcidT-Lymphocytes, CytotoxicTumor Cells, Cultured
1996
Roles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAP
Sadasivan B, Lehner P, Ortmann B, Spies T, Cresswell P. Roles for Calreticulin and a Novel Glycoprotein, Tapasin, in the Interaction of MHC Class I Molecules with TAP. Immunity 1996, 5: 103-114. PMID: 8769474, DOI: 10.1016/s1074-7613(00)80487-2.Peer-Reviewed Original ResearchATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBeta 2-MicroglobulinCalcium-Binding ProteinsCalreticulinCell LineGlycoproteinsHistocompatibility Antigens Class IHLA-A AntigensHLA-B AntigensHLA-C AntigensHumansIndolizinesMolecular ChaperonesMutationPeptidesRibonucleoproteins