2024
Applications of cell free protein synthesis in protein design
Thornton E, Paterson S, Stam M, Wood C, Laohakunakorn N, Regan L. Applications of cell free protein synthesis in protein design. Protein Science 2024, 33: e5148. PMID: 39180484, PMCID: PMC11344276, DOI: 10.1002/pro.5148.Peer-Reviewed Original Research
2009
A structural model for the HAT domain of Utp6 incorporating bioinformatics and genetics
Champion EA, Kundrat L, Regan L, Baserga SJ. A structural model for the HAT domain of Utp6 incorporating bioinformatics and genetics. Protein Engineering Design And Selection 2009, 22: 431-439. PMID: 19515729, PMCID: PMC2699269, DOI: 10.1093/protein/gzp022.Peer-Reviewed Original ResearchConceptsHAT domainRepeat motifsTetratricopeptide repeat (TPR) motifsKey functional rolesStructure-function relationshipsRNA metabolismLoss of functionMutagenesis studiesInteraction surfaceHomology modelingTertiary structureHomology modelFunctional roleMotifResiduesUTP6BioinformaticsProteinStructural contextDirect effectDomainMutagenesisGeneticsFunction mapsMutationsRedesign of a protein–peptide interaction: Characterization and applications
Jackrel ME, Valverde R, Regan L. Redesign of a protein–peptide interaction: Characterization and applications. Protein Science 2009, 18: 762-774. PMID: 19309728, PMCID: PMC2762588, DOI: 10.1002/pro.75.Peer-Reviewed Original ResearchConceptsProtein-peptide interactionsProtein-peptide pairsPurification applicationsRecognition pairsCorresponding peptide ligandsRepeat protein scaffoldsMolecular recognitionAntibody-antigen interactionsFacile replacementChemical considerationsProtein scaffoldsPeptide ligandsTypical antibody-antigen interactionsHarsh conditionsProtein designModerate affinityScaffoldsPractical applicationsAffinity purificationAffinityLigandsPropertiesInteractionSuccessful applicationDissociationAn AlphaScreen™-Based High-Throughput Screen to Identify Inhibitors of Hsp90-Cochaperone Interaction
Yi F, Zhu P, Southall N, Inglese J, Austin CP, Zheng W, Regan L. An AlphaScreen™-Based High-Throughput Screen to Identify Inhibitors of Hsp90-Cochaperone Interaction. SLAS DISCOVERY 2009, 14: 273-281. PMID: 19211782, PMCID: PMC3066041, DOI: 10.1177/1087057108330114.Peer-Reviewed Original ResearchConceptsImportant anticancer drug targetFirst high-throughput screenHigh-throughput screenChemical probesNovel anticancer drugsAnticancer drug targetSuch moleculesAnticancer drugsTPR2A domainDifferent interactionsCompoundsSmall molecule Hsp90 inhibitorsNovel typeSynthetic peptidesFurther optimizationDrug targetsC-terminal peptideAlphaScreen technologyPeptidesDMSOReported valuesMoleculesInteractionHsp90 inhibitorsBackground ratio
2008
A Novel Class of Small Molecule Inhibitors of Hsp90
Yi F, Regan L. A Novel Class of Small Molecule Inhibitors of Hsp90. ACS Chemical Biology 2008, 3: 645-654. PMID: 18785742, PMCID: PMC3282108, DOI: 10.1021/cb800162x.Peer-Reviewed Original ResearchConceptsGrowth-promoting proteinsChaperone heat shock protein 90Unregulated cellular proliferationHeat shock protein 90Inhibition of Hsp90Hydrolysis of ATPHuman breast cancer cell lines BT474Small molecule inhibitorsBreast cancer cell line BT474Hsp90 functionMultichaperone complexCorrect foldingAlphaScreen technologyProtein 90Hsp90Cell deathMolecule inhibitorsCell line BT474ATP analogCellular proliferationProteinNovel classCochaperonesApplicable strategyAnticancer agents