2012
RAGE Expression in Human T Cells: A Link between Environmental Factors and Adaptive Immune Responses
Akirav EM, Preston-Hurlburt P, Garyu J, Henegariu O, Clynes R, Schmidt AM, Herold KC. RAGE Expression in Human T Cells: A Link between Environmental Factors and Adaptive Immune Responses. PLOS ONE 2012, 7: e34698. PMID: 22509345, PMCID: PMC3324532, DOI: 10.1371/journal.pone.0034698.Peer-Reviewed Original ResearchConceptsHuman immune responseT cellsImmune responseHuman T cellsRAGE expressionAntigen-specific T cellsAdaptive human immune responsesAdaptive immune cellsSpecific T cellsHealthy control subjectsAdaptive immune responsesExpression of RAGELevels of RAGEInnate immune responseAdvanced glycation endproductsActivated T cellsT cell activationIL-17AGlucose controlControl subjectsIL-5Immune cellsGlycation endproductsCell activationPatients
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
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