1998
MECHANISMS OF MHC CLASS I–RESTRICTED ANTIGEN PROCESSING
Pamer E, Cresswell P. MECHANISMS OF MHC CLASS I–RESTRICTED ANTIGEN PROCESSING. Annual Review Of Immunology 1998, 16: 323-358. PMID: 9597133, DOI: 10.1146/annurev.immunol.16.1.323.Peer-Reviewed Original Research
1994
Human transporters associated with antigen processing possess a promiscuous peptide-binding site
Androlewicz M, Cresswell P. Human transporters associated with antigen processing possess a promiscuous peptide-binding site. Immunity 1994, 1: 7-14. PMID: 7889401, DOI: 10.1016/1074-7613(94)90004-3.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceAntigen PresentationATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBinding SitesBinding, CompetitiveBiological Transport, ActiveCarrier ProteinsCell LineHistocompatibility Antigens Class IHumansMolecular Sequence DataOligopeptidesAssembly and Transport of Class I MHC‐Peptide Complexes
Cresswell P, Androlewicz M, Ortmann B. Assembly and Transport of Class I MHC‐Peptide Complexes. Novartis Foundation Symposia 1994, 187: 150-169. PMID: 7796669, DOI: 10.1002/9780470514672.ch10.Peer-Reviewed Original ResearchConceptsTAP moleculesComplex moleculesPeptide derivativesMoleculesLonger peptidesClass I MHC-peptide complexesPeptide-binding siteComplexesClass I-peptide complexesPeptidesCompetition experimentsAssemblyAmino acidsDimersDerivativesClass I major histocompatibility complex moleculesWide rangeChainMHC-peptide complexesAcidTransportSurface
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
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 ResearchConceptsMolecular 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
1973
Papain-Solubilized HL-A Antigens from Cultured Human Lymphocytes Contain Two Peptide Fragments
Cresswell P, Turner M, Strominger J. Papain-Solubilized HL-A Antigens from Cultured Human Lymphocytes Contain Two Peptide Fragments. Proceedings Of The National Academy Of Sciences Of The United States Of America 1973, 70: 1603-1607. PMID: 4514327, PMCID: PMC433551, DOI: 10.1073/pnas.70.5.1603.Peer-Reviewed Original ResearchMeSH KeywordsAntigen-Antibody ComplexBuffersCells, CulturedCentrifugation, Density GradientChromatography, GelElectrophoresis, Polyacrylamide GelGlucosamineGlycopeptidesHistocompatibility AntigensHumansIsotope LabelingLymphocytesMannoseMolecular WeightPapainPeptidesSodium Dodecyl SulfateSolubilityTritium