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 interactionPolypeptideCalreticulin
1998
Induction of transporter associated with antigen processing by interferon γ confers endothelial cell cytoprotection against natural killer-mediated lysis
Ayalon O, Hughes E, Cresswell P, Lee J, O’Donnell L, Pardi R, Bender J. Induction of transporter associated with antigen processing by interferon γ confers endothelial cell cytoprotection against natural killer-mediated lysis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 2435-2440. PMID: 9482903, PMCID: PMC19366, DOI: 10.1073/pnas.95.5.2435.Peer-Reviewed Original ResearchConceptsMHC IInduction of transportersEndothelial cellsNK-resistant cell linesNatural killer-mediated lysisMajor histocompatibility complex INK inhibitory receptorsNK effector cellsPretreatment of ECB-lymphoblastoid cell linesEC sensitivityDermal microvascular endothelial cellsMicrovascular endothelial cellsCell linesHuman umbilical vein endothelial cellsExpression/functionUmbilical vein endothelial cellsAdenoviral-mediated transductionVascular vulnerabilityVein endothelial cellsNK assaysEffector cellsEndothelial activationInhibitory receptorsDeficient targets
1994
Assembly and intracellular transport of HLA-DM and correction of the class II antigen-processing defect in T2 cells
Denzin L, Robbins N, Carboy-Newcomb C, Cresswell P. Assembly and intracellular transport of HLA-DM and correction of the class II antigen-processing defect in T2 cells. Immunity 1994, 1: 595-606. PMID: 7600288, DOI: 10.1016/1074-7613(94)90049-3.Peer-Reviewed Original ResearchAntigen PresentationAntigens, Differentiation, B-LymphocyteBase SequenceBiological TransportCell LineCell MembraneFlow CytometryHistocompatibility Antigens Class IIHLA-D AntigensHLA-DR3 AntigenHumansHybrid CellsKineticsMolecular Sequence DataMutationNeoplasm ProteinsPrecipitin TestsSodium Dodecyl SulfateTime FactorsTransfection
1992
HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides
Wei M, Cresswell P. HLA-A2 molecules in an antigen-processing mutant cell contain signal sequence-derived peptides. Nature 1992, 356: 443-446. PMID: 1557127, DOI: 10.1038/356443a0.Peer-Reviewed Original Research
1978
Rabbit antiserum to human B-cell alloantigens II. Mechanism of inhibition of stimulation in the mixed lymphocyte response
Geier S, Cresswell P. Rabbit antiserum to human B-cell alloantigens II. Mechanism of inhibition of stimulation in the mixed lymphocyte response. Cellular Immunology 1978, 35: 392-402. PMID: 145900, DOI: 10.1016/0008-8749(78)90158-2.Peer-Reviewed Original ResearchConceptsAntibody-dependent cell-mediated cytotoxicityMixed lymphocyte responseAnti-B cell serumLymphocyte responsesDependent cell-mediated cytotoxicityInhibition of monocyteHuman B cell alloantigensADCC effector cellsCell-mediated cytotoxicityImmunoglobulin-positive cellsB-cell alloantigensRabbit antiserumEffector cellsMLR suppressionImmune eliminationStimulator cellsPositive cellsLevel of inhibitionMarked reductionCell populationsChicken antiseraAntiserumSimilar specificityMechanism of inhibitionFc region
1977
Human B cell alloantigens: separation from other membrane molecules by affinity chromatography
Cresswell P. Human B cell alloantigens: separation from other membrane molecules by affinity chromatography. European Journal Of Immunology 1977, 7: 636-639. PMID: 303569, DOI: 10.1002/eji.1830070911.Peer-Reviewed Original ResearchMeSH KeywordsB-LymphocytesCell MembraneChromatography, AffinityDeoxycholic AcidHLA AntigensHumansIsoantigensMembrane ProteinsConceptsMolecular weight 35 000Sodium dodecyl sulfate gel electrophoresisDodecyl sulfate gel electrophoresisAffinity chromatographySulfate gel electrophoresisSoluble productsB-lymphoblastoid cell linesChromatographyMoleculesSodium deoxycholateLymphoblastoid cell linesGel electrophoresisAgarose columnIa-like alloantigensDeoxycholateCell linesHuman B cellsSeparationSpecific rabbit antibodiesB cellsColumnSerological activityElectrophoresisRabbit antibodiesMaterials
1975
Antisera to human B-lymphocyte membrane glycoproteins block stimulation in mixed lymphocyte culture
CRESSWELL P, GEIER S. Antisera to human B-lymphocyte membrane glycoproteins block stimulation in mixed lymphocyte culture. Nature 1975, 257: 147-149. PMID: 51476, DOI: 10.1038/257147a0.Peer-Reviewed Original ResearchPurification of papain-solubilized histocompatibility antigens from a cultured human lymphoblastoid line, RPMI 4265.
Turner M, Cresswell P, Parham P, Strominger J, Mann D, Sanderson A. Purification of papain-solubilized histocompatibility antigens from a cultured human lymphoblastoid line, RPMI 4265. Journal Of Biological Chemistry 1975, 250: 4512-4519. PMID: 1141219, DOI: 10.1016/s0021-9258(19)41332-x.Peer-Reviewed Original ResearchConceptsSodium dodecyl sulfate gel electrophoresisSephadex GDodecyl sulfate gel electrophoresisSulfate gel electrophoresisDiethylaminoethylcellulose columnSingle bandCharge heterogeneityM ureaPreparationDEAE-cellulose columnChromatographyM KClSeparationGel electrophoresisMultiple bandsColumnSialic acid
1974
The Immunoglobulin‐Like Structure of Human Histocompatibility Antigens
Strominger J, Cresswell P, Grey H, Humphreys R, Mann D, Mccune J, Parham P, Robb R, Sanderson A, Springer T, Terhorst C, Turner M. The Immunoglobulin‐Like Structure of Human Histocompatibility Antigens. Immunological Reviews 1974, 21: 126-143. PMID: 4139785, DOI: 10.1111/j.1600-065x.1974.tb01549.x.Peer-Reviewed Original ResearchAntigen-Antibody ComplexBeta-GlobulinsCarbon RadioisotopesCell LineCell MembraneCells, CulturedChromatographyChromatography, GelDetergentsElectrophoresisHistocompatibility AntigensImmune SeraImmunoglobulinsIodine RadioisotopesIsoantibodiesIsoelectric FocusingLymphocyte ActivationLymphocytesMolecular WeightNeuraminidasePapainTritiumImmunological Identity of the Small Subunit of HL-A Antigens and β2-Microglobulin and Its Turnover on the Cell Membrane
Cresswell P, Springer T, Strominger J, Turner M, Grey H, Kubo R. Immunological Identity of the Small Subunit of HL-A Antigens and β2-Microglobulin and Its Turnover on the Cell Membrane. Proceedings Of The National Academy Of Sciences Of The United States Of America 1974, 71: 2123-2127. PMID: 4134761, PMCID: PMC388399, DOI: 10.1073/pnas.71.5.2123.Peer-Reviewed Original Research
1973
THE SMALL SUBUNIT OF HL-A ANTIGENS IS ß2-MICROGLOBULIN
Grey H, Kubo R, Colon S, Poulik M, Cresswell P, Springer T, Turner M, Strominger J. THE SMALL SUBUNIT OF HL-A ANTIGENS IS ß2-MICROGLOBULIN. Journal Of Experimental Medicine 1973, 138: 1608-1612. PMID: 4128442, PMCID: PMC2139471, DOI: 10.1084/jem.138.6.1608.Peer-Reviewed Original Research