Jungyuen Choi
Research Associate PharmacologyAbout
Titles
Research Associate Pharmacology
Research
Research at a Glance
Yale Co-Authors
Frequent collaborators of Jungyuen Choi's published research.
Sangwon Lee, PhD
Francisco Tome
Yoshihisa Suzuki
Publications
2022
Isoform-specific inhibition of FGFR signaling achieved by a de-novo-designed mini-protein
Park JS, Choi J, Cao L, Mohanty J, Suzuki Y, Park A, Baker D, Schlessinger J, Lee S. Isoform-specific inhibition of FGFR signaling achieved by a de-novo-designed mini-protein. Cell Reports 2022, 41: 111545. PMID: 36288716, PMCID: PMC9636537, DOI: 10.1016/j.celrep.2022.111545.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsFibroblast growth factor receptorC isoformsFibroblast growth factor ligandsLigand-binding regionSilico design strategyIsoform-specific inhibitionGrowth factor ligandsAlternative splicingCellular signalingRegulated processGrowth factor receptorDevelopment of therapeuticsFGFR isoformsFactor ligandCellular analysisFactor receptorMechanistic insightsKlotho proteinSpecific interactionsMB7Distinct subsetsHigh affinitySplicingSignalingFGF
2019
Structures of ligand-occupied β-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity
Kuzina ES, Ung PM, Mohanty J, Tome F, Choi J, Pardon E, Steyaert J, Lax I, Schlessinger A, Schlessinger J, Lee S. Structures of ligand-occupied β-Klotho complexes reveal a molecular mechanism underlying endocrine FGF specificity and activity. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 7819-7824. PMID: 30944224, PMCID: PMC6475419, DOI: 10.1073/pnas.1822055116.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsFGF receptorsPleiotropic cellular responsesFibroblast growth factor (FGF) familyPrimary high-affinity receptorsKlotho proteinChimeric mutantsGrowth factor familyCatalytic subunitFGFR functionRegulatory interactionsTerminal tailPleiotropic cellular effectsFactor familyP motifS motifExtracellular domainMolecular mechanismsIntracellular signalingCellular responsesSame binding siteCellular effectsGeneral mechanismEndocrine FGFsBinary complexBinding sites
2018
Structures of β-klotho reveal a ‘zip code’-like mechanism for endocrine FGF signalling
Lee S, Choi J, Mohanty J, Sousa LP, Tome F, Pardon E, Steyaert J, Lemmon MA, Lax I, Schlessinger J. Structures of β-klotho reveal a ‘zip code’-like mechanism for endocrine FGF signalling. Nature 2018, 553: 501-505. PMID: 29342135, PMCID: PMC6594174, DOI: 10.1038/nature25010.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsMeSH KeywordsBinding SitesCrystallography, X-RayExtracellular SpaceFibroblast Growth Factor-23Fibroblast Growth FactorsGlycoside HydrolasesHEK293 CellsHumansKlotho ProteinsLigandsMembrane ProteinsModels, MolecularProtein BindingProtein DomainsReceptors, Fibroblast Growth FactorSignal TransductionSubstrate Specificity