2001
Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus
Chin K, Cresswell P. Viperin (cig5), an IFN-inducible antiviral protein directly induced by human cytomegalovirus. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 15125-15130. PMID: 11752458, PMCID: PMC64994, DOI: 10.1073/pnas.011593298.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCells, CulturedCytomegalovirusDNA, ComplementaryHumansInterferon-alphaInterferon-betaMolecular Sequence DataOxidoreductases Acting on CH-CH Group DonorsProtein BiosynthesisProteinsSequence Homology, Amino AcidViral Envelope ProteinsVirus ReplicationDefective Antigen Processing in GILT-Free Mice
Maric M, Arunachalam B, Phan U, Dong C, Garrett W, Cannon K, Alfonso C, Karlsson L, Flavell R, Cresswell P. Defective Antigen Processing in GILT-Free Mice. Science 2001, 294: 1361-1365. PMID: 11701933, DOI: 10.1126/science.1065500.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsAntigen PresentationAntigen-Presenting CellsAntigensCell LineDendritic CellsDisulfidesEpitopesHistocompatibility Antigens Class IIHybridomasHydrogen-Ion ConcentrationImmunizationMiceMice, Inbred C57BLMice, KnockoutMolecular Sequence DataMuramidaseOxidoreductasesOxidoreductases Acting on Sulfur Group DonorsProtein ConformationProtein FoldingSpleenT-LymphocytesMultiple species express thiol oxidoreductases related to GILT
Phan U, Maric M, Dick T, Cresswell P. Multiple species express thiol oxidoreductases related to GILT. Immunogenetics 2001, 53: 342-346. PMID: 11491538, DOI: 10.1007/s002510100323.Peer-Reviewed Original Research
2000
Enzymatic reduction of disulfide bonds in lysosomes: Characterization of a Gamma-interferon-inducible lysosomal thiol reductase (GILT)
Arunachalam B, Phan U, Geuze H, Cresswell P. Enzymatic reduction of disulfide bonds in lysosomes: Characterization of a Gamma-interferon-inducible lysosomal thiol reductase (GILT). Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 745-750. PMID: 10639150, PMCID: PMC15401, DOI: 10.1073/pnas.97.2.745.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBinding SitesCOS CellsDisulfidesDNA, ComplementaryEndosomesEnzyme InductionHumansHydrogen-Ion ConcentrationInterferon-gammaLysosomesMannosephosphatesMicroscopy, ImmunoelectronMolecular Sequence DataMutagenesisOxidation-ReductionProtein Disulfide Reductase (Glutathione)Protein Processing, Post-TranslationalSequence Analysis, DNATumor Cells, CulturedConceptsGamma interferon inducible lysosomal thiol reductaseLysosomal thiol reductaseThiol reductaseDisulfide bondsC-terminal prosequenceEndocytic pathwayThioredoxin familyCysteine residuesDisulfide bond reductionEfficient proteolysisCell typesAmino acidsLysosomal systemEnzymeLysosomesSoluble glycoproteinReductaseActive siteBond reductionAntigen processingImportant roleEnzymatic reductionMutagenesisThioredoxinProsequence
1998
Genomic analysis of the Tapasin gene, located close to the TAP loci in the MHC
Herberg J, Sgouros J, Jones T, Copeman J, Humphray S, Sheer D, Cresswell P, Beck S, Trowsdale J. Genomic analysis of the Tapasin gene, located close to the TAP loci in the MHC. European Journal Of Immunology 1998, 28: 459-467. PMID: 9521053, DOI: 10.1002/(sici)1521-4141(199802)28:02<459::aid-immu459>3.0.co;2-z.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntiportersATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBase SequenceCentromereExonsGenes, MHC Class IHistocompatibility Antigens Class IHumansImmunoglobulinsIntronsMembrane Transport ProteinsMiceMolecular Sequence DataPhylogenyRatsConceptsTapasin geneMouse ESTsSyntenic positionsGenomic analysisSeparate exonsGene sequencesDistinct phylogenyEndoplasmic reticulumGenesK locusChromosome 17IgC domainFunctional significanceLociMHC class IClass IHLA-DP locusTAP2 genesEquivalent locationsTAP transporterTapasin moleculePhylogenyIntronsChromosomesESTsQuantitative Defect in Staphylococcal Enterotoxin A Binding and Presentation by HLA-DM-Deficient T2.AkCells Corrected by Transfection of HLA-DM Genes
Albert L, Denzin L, Ghumman B, Bangia N, Cresswell P, Watts T. Quantitative Defect in Staphylococcal Enterotoxin A Binding and Presentation by HLA-DM-Deficient T2.AkCells Corrected by Transfection of HLA-DM Genes. Cellular Immunology 1998, 183: 42-51. PMID: 9578718, DOI: 10.1006/cimm.1997.1236.Peer-Reviewed Original Research
1997
Negative Regulation by HLA-DO of MHC Class II-Restricted Antigen Processing
Denzin L, Sant'Angelo D, Hammond C, Surman M, Cresswell P. Negative Regulation by HLA-DO of MHC Class II-Restricted Antigen Processing. Science 1997, 278: 106-109. PMID: 9311912, DOI: 10.1126/science.278.5335.106.Peer-Reviewed Original ResearchConceptsHLA-DOII-like moleculeAntigen processingClass IIHLA-DMMajor histocompatibility complex classMHC class IIHistocompatibility complex classClass II moleculesII-CLIP complexesHLA-DM functionT cell linesB cellsChain-derived peptideAntigenic peptidesImportant modulatorCell linesDM functionInvariant chain-derived peptidesComplex classNegative regulationPeptidesA 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
HLA-DM Interactions with Intermediates in HLA-DR Maturation and a Role for HLA-DM in Stabilizing Empty HLA-DR Molecules
Denzin L, Hammond C, Cresswell P. HLA-DM Interactions with Intermediates in HLA-DR Maturation and a Role for HLA-DM in Stabilizing Empty HLA-DR Molecules. Journal Of Experimental Medicine 1996, 184: 2153-2166. PMID: 8976171, PMCID: PMC2196380, DOI: 10.1084/jem.184.6.2153.Peer-Reviewed Original ResearchConceptsClass II moleculesHLA-DR moleculesHLA-DMDR moleculesMajor histocompatibility complex classAntigenic peptidesEmpty class II moleculesCLIP dissociationHistocompatibility complex classMHC class II compartmentsHLA-DM moleculesClass II compartmentsII-CLIP complexesClass II dimersAlpha beta dimersAntigen processingBeta dimersDR complexesCell linesInvariant chain fragmentComplex classAssociationLow levels
1995
HLA-DM induces clip dissociation from MHC class II αβ dimers and facilitates peptide loading
Denzin L, Cresswell P. HLA-DM induces clip dissociation from MHC class II αβ dimers and facilitates peptide loading. Cell 1995, 82: 155-165. PMID: 7606781, DOI: 10.1016/0092-8674(95)90061-6.Peer-Reviewed Original ResearchMolecular 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
1994
In vivo and in vitro formation and dissociation of HLA-DR complexes with invariant chain-derived peptides
Avva R, Cresswell P. In vivo and in vitro formation and dissociation of HLA-DR complexes with invariant chain-derived peptides. Immunity 1994, 1: 763-774. PMID: 7895165, DOI: 10.1016/s1074-7613(94)80018-9.Peer-Reviewed Original ResearchConceptsHLA-DM expressionDR alpha beta dimersHLA-DR moleculesCLIP dissociationClass II moleculesHLA-DR complexInvariant chain peptideII-peptide complexesPrimary aliphatic aminesResidual fragmentsChain-derived peptideClass IIHLA-DMAliphatic aminesCarboxylic acidsSuch complexesUnbranched hydrocarbonsAlpha beta dimersChain peptideInvariant chain-derived peptidesComplexesVivoCLIP complexBeta dimersDissociationHuman 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 DataOligopeptidesMHC class l/β2-microglobulin complexes associate with TAP transporters before peptide binding
Ortmann B, Androlewicz M, Cresswell P. MHC class l/β2-microglobulin complexes associate with TAP transporters before peptide binding. Nature 1994, 368: 864-867. PMID: 8159247, DOI: 10.1038/368864a0.Peer-Reviewed Original ResearchAmino Acid SequenceAnimalsATP Binding Cassette Transporter, Subfamily B, Member 2ATP Binding Cassette Transporter, Subfamily B, Member 3ATP-Binding Cassette TransportersB-LymphocytesBeta 2-MicroglobulinBiological TransportCalcium-Binding ProteinsCalnexinCarrier ProteinsCell LineDigitoninEndoplasmic ReticulumHistocompatibility Antigens Class IHLA-A3 AntigenHumansMiceMolecular Sequence DataProtein BindingRabbitsSolubilityAssembly 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
HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides
Riberdy J, Newcomb J, Surman M, Barbosat J, Cresswell P. HLA-DR molecules from an antigen-processing mutant cell line are associated with invariant chain peptides. Nature 1992, 360: 474-477. PMID: 1448172, DOI: 10.1038/360474a0.Peer-Reviewed Original ResearchConceptsClass II moleculesInvariant chainMajor histocompatibility complex (MHC) class II moleculesCell linesHLA-DR moleculesClass II binding siteInvariant chain peptideHLA-DR3 moleculesMore MHCClass IIAntigen processingT2 transfectantsAntigenic peptidesHuman cell linesChain peptideVivo conditionsPeptidesLarge proportionProteolytic cleavageMutant cell linesCertain human cell linesEarly stagesTransfectantsHLA-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
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
1987
Localization of an epitope of beta-2 microglobulin that is shared with other members of the immunoglobulin superfamily
Parham P, Lutz P, Cresswell P. Localization of an epitope of beta-2 microglobulin that is shared with other members of the immunoglobulin superfamily. Immunogenetics 1987, 26: 323-326. PMID: 2443449, DOI: 10.1007/bf00346533.Peer-Reviewed Original ResearchConceptsBeta-2-microglobulin