1997
A human homologue of the Drosophila Toll protein signals activation of adaptive immunity
Medzhitov R, Preston-Hurlburt P, Janeway C. A human homologue of the Drosophila Toll protein signals activation of adaptive immunity. Nature 1997, 388: 394-397. PMID: 9237759, DOI: 10.1038/41131.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsB7-1 AntigenCell LineCloning, MolecularDrosophilaDrosophila ProteinsHumansImmunityInsect ProteinsInterleukinsJurkat CellsMembrane GlycoproteinsMembrane ProteinsMiceMolecular Sequence DataMutationNF-kappa BReceptors, Cell SurfaceReceptors, ImmunologicRecombinant Fusion ProteinsSequence Homology, Amino AcidSignal TransductionT-LymphocytesToll-Like ReceptorsTransfectionConceptsDrosophila Toll proteinToll proteinCytoplasmic domainDrosophila TollHuman homologueLeucine-rich repeat domainNF-κB-controlled genesHuman cell linesRepeat domainActive mutantExtracellular domainNF-κBImmune responseInnate immune responseCo-stimulatory molecules B7.1Adaptive immune systemComponents of immunityInflammatory cytokines IL-1ProteinCell linesCo-stimulatory moleculesAntigen-presenting cellsAdaptive immune responsesNaive T cellsHomologues
1996
The Specificity and Orientation of a TCR to its Peptide–MHC Class II Ligands
Sant'Angelo D, Waterbury G, Preston-Hurlburt P, Yoon S, Medzhitov R, Hong S, Janeway C. The Specificity and Orientation of a TCR to its Peptide–MHC Class II Ligands. Immunity 1996, 4: 367-376. PMID: 8612131, DOI: 10.1016/s1074-7613(00)80250-2.Peer-Reviewed Original Research
1992
Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs
Rudensky A, Preston-Hurlburt, P, Al-Ramadi B, Rothbard J, Janeway C. Truncation variants of peptides isolated from MHC class II molecules suggest sequence motifs. Nature 1992, 359: 429-431. PMID: 1328884, DOI: 10.1038/359429a0.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntigen-Antibody ReactionsBacterial ProteinsBinding Sites, AntibodyCell LineChromatography, High Pressure LiquidHistocompatibility Antigens Class IIImmunoglobulin GImmunoglobulin Heavy ChainsImmunoglobulin Variable RegionMiceMice, Inbred C57BLMolecular Sequence DataPeptide FragmentsReceptors, TransferrinRepressor ProteinsSequence AlignmentSequence Homology, Amino AcidT-LymphocytesViral Envelope ProteinsConceptsMHC class II moleculesClass II moleculesMHC class IMajor histocompatibility complexCD4 T cell recognitionClass IForeign protein antigensMHC class IIT cell recognitionT cellsMHC moleculesClass IIProtein antigensHistocompatibility complexAntigenic peptidesOuter aspectPeptide-binding cleftAmino acid differencesAnchor residuesAllelic variantsSingle peptide sequenceDifferent allelic formsPeptidesTruncation variantsAllelic forms
1991
On the complexity of self
Rudensky A, Rath S, Preston-Hurlburt P, Murphy D, Janeway C. On the complexity of self. Nature 1991, 353: 660-662. PMID: 1656278, DOI: 10.1038/353660a0.Peer-Reviewed Original ResearchConceptsMHC class II moleculesClass II moleculesSelf peptidesT cellsY-AeSelf MHC class II moleculesCD4 T cellsMajor histocompatibility complex moleculesMHC class IIMHC class II complexesHistocompatibility complex moleculesClass II complexesIntrathymic selectionSelf antigensIntrathymic developmentNovel MHCClass IISequence analysis of peptides bound to MHC class II molecules
Rudensky A, Preston-Hurlburt P, Hong S, Barlow A, Janeway C. Sequence analysis of peptides bound to MHC class II molecules. Nature 1991, 353: 622-627. PMID: 1656276, DOI: 10.1038/353622a0.Peer-Reviewed Original Research
1990
The role of tyrosine at the ligand-binding site of the nicotinic acetylcholine receptor
Pearce S, Preston-Hurlburt P, Hawrot E. The role of tyrosine at the ligand-binding site of the nicotinic acetylcholine receptor. Proceedings Of The Royal Society B 1990, 241: 207-213. PMID: 1979446, DOI: 10.1098/rspb.1990.0087.Peer-Reviewed Original ResearchConceptsLigand-binding siteNegative subsiteInvariant tyrosine residueNicotinic acetylcholine receptorsValuable structural informationDetailed structural knowledgeReceptor ligand-binding siteCationic ligandsFluorescence spectroscopicAcetylcholine receptorsRole of tyrosineCritical residuesLigand recognitionTyrosine residuesLigand bindingStructural comparisonStructural informationPeptide fragmentsLigandsPosition 190Receptor actionNeurotransmitter receptorsSpecific ligandsStructural knowledgeResidues