Lynne Regan, PhD
Professor Emeritus of Molecular Biophysics and Biochemistry and of ChemistryDownloadHi-Res Photo
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Molecular Biophysics and Biochemistry
PO Box 208024, 333 Cedar Street
New Haven, CT 06520-8024
United States
About
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Titles
Professor Emeritus of Molecular Biophysics and Biochemistry and of Chemistry
Appointments
Molecular Biophysics and Biochemistry
EmeritusPrimary
Other Departments & Organizations
- Molecular Biophysics and Biochemistry
- Regan Lab
- Structural Biology
- Yale Cancer Center
- Yale Ventures
Education & Training
- PhD
- Massachusetts Institute of Technology (1987)
Research
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Overview
Research interests of the Regan lab encompass protein structure, folding and design; protein-protein interactions and protein-RNA interactions. Our research is problem based, and we use whatever techniques are most appropriate as a particular project develops. Our research ranges from fundamental studies of protein stability to the design of novel protein-based nano-materials. Our interest in protein-protein interactions ranges from the design of proteins with novel binding activities and characterization of their properties using a range of techniques including fluorescence, circular dichroism, surface plasmon resonance, NMR and x-ray crystallography to the specific inhibition of protein-protein interactions in vivo as a route to a novel class of anti-breast cancer agents. Our interest in protein-RNA interactions is focused on structure and function of Fragile X Mental Retardation Protein (FMRP). Fragile X Mental Retardation Syndrome is the most common cause of inherited mental retardation in humans, and is caused by lack of functional FMRP. Here our approaches range from structural studies of FMRP, to whole animal profiling of RNA and protein expression patterns in wild-type versus FMRP knock-out animals.
Medical Research Interests
Biochemistry; Biophysics; Chemistry; Fragile X Mental Retardation Protein; Fragile X Syndrome; Molecular Biology
ORCID
0000-0003-4719-2495- View Lab Website
Regan Lab
Research at a Glance
Yale Co-Authors
Frequent collaborators of Lynne Regan's published research.
Publications Timeline
A big-picture view of Lynne Regan's research output by year.
Research Interests
Research topics Lynne Regan is interested in exploring.
31Publications
2,346Citations
Chemistry
Molecular Biology
Publications
2025
Engineering Protein–Peptide Interfaces via Combinatorial Mutagenesis and Mass Photometric Screening
Hosseini B, Ashraf M, Kitchen P, Chembath A, Collighan R, Spickett C, Regan L, Hine A. Engineering Protein–Peptide Interfaces via Combinatorial Mutagenesis and Mass Photometric Screening. Biomolecules 2025, 15: 1183. PMID: 40867626, PMCID: PMC12384687, DOI: 10.3390/biom15081183.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsHydrophobic binding pocketTolerance to mutationsMass photometryLibrary of proteinsProtein-peptide interfacesIsopeptide bond formationSaturation mutagenesisCombinatorial mutagenesisProtein engineeringHydrophobic residuesOverlap PCRInteraction specificityStreptococcus pyogenesSpyTagSpyCatcherStable interactionBinding pocketMutagenesisProteinProtein mixturesBond formationLys31Asp7MutationsPyogenesA New Highly Specific and Soluble Protease for Precise Removal of N‑Terminal Purification Tags
Shams R, Regan L. A New Highly Specific and Soluble Protease for Precise Removal of N‑Terminal Purification Tags. ACS Omega 2025, 10: 30354-30364. PMID: 40727744, PMCID: PMC12290709, DOI: 10.1021/acsomega.5c01764.Peer-Reviewed Original ResearchAltmetricConceptsPurification tagCys-His-Asp catalytic triadN-terminal purification tagTurnip mosaic virusAffinity purification tagAmino acid identityAmino acidsOptimum enzyme activityActive siteAcid identityMosaic virusCatalytic triadCleavage specificityAffinity purificationC-terminusC-terminalSoluble proteasesCysteine proteasesViral proteaseBiotech applicationsProteaseEnzyme activityCatalytic efficiencyViral originAminoCell-Free Protein Synthesis as a Method to Rapidly Screen Machine Learning-Generated Protease Variants
Thornton E, Boyle J, Laohakunakorn N, Regan L. Cell-Free Protein Synthesis as a Method to Rapidly Screen Machine Learning-Generated Protease Variants. ACS Synthetic Biology 2025, 14: 1710-1718. PMID: 40304425, PMCID: PMC12090339, DOI: 10.1021/acssynbio.5c00062.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsSuper‐resolution imaging of proteins inside live mammalian cells with mLIVE‐PAINT
Bhaskar H, Gidden Z, Virdi G, Kleinjan D, Rosser S, Gandhi S, Regan L, Horrocks M. Super‐resolution imaging of proteins inside live mammalian cells with mLIVE‐PAINT. Protein Science 2025, 34: e70008. PMID: 39865341, PMCID: PMC11761688, DOI: 10.1002/pro.70008.Peer-Reviewed Original ResearchAltmetricMeSH Keywords and Concepts
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 Reviews, Practice Guidelines, Standards, and Consensus StatementsCitations
2015
Editorial overview: Mechanistic biology: Dynamic interactions in biology—sensing change
Booth P, Regan L. Editorial overview: Mechanistic biology: Dynamic interactions in biology—sensing change. Current Opinion In Chemical Biology 2015, 29: viii-ix. PMID: 26598929, DOI: 10.1016/j.cbpa.2015.11.003.Commentaries, Editorials and Letters
2012
The interface of protein structure, protein biophysics, and molecular evolution
Liberles D, Teichmann S, Bahar I, Bastolla U, Bloom J, Bornberg‐Bauer E, Colwell L, de Koning A, Dokholyan N, Echave J, Elofsson A, Gerloff D, Goldstein R, Grahnen J, Holder M, Lakner C, Lartillot N, Lovell S, Naylor G, Perica T, Pollock D, Pupko T, Regan L, Roger A, Rubinstein N, Shakhnovich E, Sjölander K, Sunyaev S, Teufel A, Thorne J, Thornton J, Weinreich D, Whelan S. The interface of protein structure, protein biophysics, and molecular evolution. Protein Science 2012, 21: 769-785. PMID: 22528593, PMCID: PMC3403413, DOI: 10.1002/pro.2071.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsCitationsAltmetricMeSH Keywords and ConceptsConceptsProtein structureMolecular evolutionProtein biophysicsHigh-throughput experimental dataMolecular population geneticsComplex mutational processesIn vitro biochemistryProtein structural biologyAmino acid substitutionsProtein evolutionStatic protein structuresEvolutionary ratesOrganismal fitnessPopulation geneticsCircular permutationProtein functionAcid substitutionsDomain rearrangementsBiological inferencesProtein modelsDisordered proteinsProtein biochemistryProtein geometryMutational processesStructural biology
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 ResearchCitationsMeSH Keywords and ConceptsConceptsHAT 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 ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsProtein-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 ResearchCitationsMeSH Keywords and ConceptsConceptsImportant 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
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Molecular Biophysics and Biochemistry
PO Box 208024, 333 Cedar Street
New Haven, CT 06520-8024
United States