2001
Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP)
Karttunen J, Lehner P, Gupta S, Hewitt E, Cresswell P. Distinct functions and cooperative interaction of the subunits of the transporter associated with antigen processing (TAP). Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 7431-7436. PMID: 11381133, PMCID: PMC34686, DOI: 10.1073/pnas.121180198.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SubstitutionAnimalsATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersAzidesBinding SitesCell LineHeLa CellsHumansLysineMajor Histocompatibility ComplexMutagenesis, Site-DirectedPeptide FragmentsPhotoaffinity LabelsProtein SubunitsRecombinant ProteinsTransfectionA 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
2000
Interaction of Human Immunodeficiency Virus Type 2 Vpx and Invariant Chain
Pancio H, Vander Heyden N, Kosuri K, Cresswell P, Ratner L. Interaction of Human Immunodeficiency Virus Type 2 Vpx and Invariant Chain. Journal Of Virology 2000, 74: 6168-6172. PMID: 10846101, PMCID: PMC112116, DOI: 10.1128/jvi.74.13.6168-6172.2000.Peer-Reviewed Original ResearchConceptsMajor histocompatibility complex class II antigen presentationHuman immunodeficiency virus type 2Class II antigen presentationHIV-2 VpxSimian immunodeficiency virusInvariant chainVirus type 2Immunodeficiency virusAntigen presentationVirion-associated proteinType 2VpxInfected cellsCellsFusion proteinCellular proteinsProteinS-transferase fusion protein
1998
The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules.
Hammond C, Denzin L, Pan M, Griffith J, Geuze H, Cresswell P. The tetraspan protein CD82 is a resident of MHC class II compartments where it associates with HLA-DR, -DM, and -DO molecules. The Journal Of Immunology 1998, 161: 3282-91. PMID: 9759843, DOI: 10.4049/jimmunol.161.7.3282.Peer-Reviewed Original ResearchAssembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors.
Deng Y, Gibbs J, Bačík I, Porgador A, Copeman J, Lehner P, Ortmann B, Cresswell P, Bennink J, Yewdell J. Assembly of MHC class I molecules with biosynthesized endoplasmic reticulum-targeted peptides is inefficient in insect cells and can be enhanced by protease inhibitors. The Journal Of Immunology 1998, 161: 1677-85. PMID: 9712031, DOI: 10.4049/jimmunol.161.4.1677.Peer-Reviewed Original ResearchMeSH KeywordsAedesAnimalsAntibodies, MonoclonalAntiportersCell LineEndoplasmic ReticulumH-2 AntigensHeLa CellsHumansImmunoglobulinsLymphocyte ActivationMacromolecular SubstancesMembrane Transport ProteinsMiceOligopeptidesOvalbuminPeptide FragmentsProtease InhibitorsRecombinant ProteinsT-LymphocytesVaccinia virusConceptsInsect cellsEndoplasmic reticulumVertebrate cellsHuman cellsHuman tapasinVaccinia virus-mediated expressionCell surface expressionProtease inhibitorsInefficient assemblyKbMHC class IMouse betaInsectsEfficient assemblyImmediate precursorSurface expressionAntigenic peptidesHeavy chainClass IRecombinant vaccinia virusVirus-mediated expressionAssemblyExpressionCellsVaccinia virusThe 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
The human cytomegalovirus US6 glycoprotein inhibits transporter associated with antigen processing-dependent peptide translocation
Lehner P, Karttunen J, Wilkinson G, Cresswell P. The human cytomegalovirus US6 glycoprotein inhibits transporter associated with antigen processing-dependent peptide translocation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 6904-6909. PMID: 9192664, PMCID: PMC21257, DOI: 10.1073/pnas.94.13.6904.Peer-Reviewed Original ResearchInterferon-γ Rapidly Increases Peptide Transporter (TAP) Subunit Expression and Peptide Transport Capacity in Endothelial Cells*
Ma W, Pober J, Johnson D, Lehner P, Cresswell P. Interferon-γ Rapidly Increases Peptide Transporter (TAP) Subunit Expression and Peptide Transport Capacity in Endothelial Cells*. Journal Of Biological Chemistry 1997, 272: 16585-16590. PMID: 9195970, DOI: 10.1074/jbc.272.26.16585.Peer-Reviewed Original Research
1995
Molecular 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