Featured Publications
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 ResearchConceptsFGF 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
2015
FGF1 and FGF19 reverse diabetes by suppression of the hypothalamic–pituitary–adrenal axis
Perry RJ, Lee S, Ma L, Zhang D, Schlessinger J, Shulman GI. FGF1 and FGF19 reverse diabetes by suppression of the hypothalamic–pituitary–adrenal axis. Nature Communications 2015, 6: 6980. PMID: 25916467, PMCID: PMC4413509, DOI: 10.1038/ncomms7980.Peer-Reviewed Original ResearchMeSH KeywordsAcetyl Coenzyme AAdrenocorticotropic HormoneAnimalsCorticosteroneDiabetes Mellitus, ExperimentalDiabetes Mellitus, Type 1Fibroblast Growth Factor 1Fibroblast Growth FactorsGlucoseHypothalamo-Hypophyseal SystemInjections, IntraventricularInsulinLipolysisLiverMalePituitary-Adrenal SystemPyruvate CarboxylaseRats, Sprague-DawleyConceptsHepatic acetyl-CoA contentFibroblast growth factor 1Whole-body lipolysisHepatic glucose productionAcetyl-CoA contentGlucose productionAwake rat modelRecombinant fibroblast growth factor 1CoA contentIntra-arterial infusionGlucose-lowering effectType 1 diabetesGrowth factor-1Mechanism of actionReverse diabetesDiabetic rodentsICV injectionIntracerebroventricular injectionPlasma ACTHHPA axisAdrenal axisRat modelGlucose metabolismCorticosterone concentrationsFGF19
2003
Structures of neuropeptide γ from goldfish and mammalian neuropeptide γ, as determined by 1H NMR spectroscopy
Lee K, Lee S, Kim Y, Park NG. Structures of neuropeptide γ from goldfish and mammalian neuropeptide γ, as determined by 1H NMR spectroscopy. Chemical Biology & Drug Design 2003, 61: 274-285. PMID: 12662361, DOI: 10.1034/j.1399-3011.2003.00058.x.Peer-Reviewed Original ResearchConceptsAmino acid sequenceN-terminal regionAlpha-helical conformationAqueous TFE solutionAcid sequenceShort helixAlpha-helical structureC-terminal regionTerminal amino acid sequencePost-translational processingBeta-turn regionMammalian systemsTFE solutionC-terminusMet21Solution structureNeuropeptide γHelixBiological responsesGold fishBiological actionsSodium dodecyl sulfate micellesHis12Nuclear magnetic resonance spectroscopyNeuropeptide gamma
2000
Role of the Hinge Region and the Tryptophan Residue in the Synthetic Antimicrobial Peptides, Cecropin A(1−8)−Magainin 2(1−12) and Its Analogues, on Their Antibiotic Activities and Structures † , ‡
Oh D, Shin S, Lee S, Kang J, Kim S, Ryu P, Hahm K, Kim Y. Role of the Hinge Region and the Tryptophan Residue in the Synthetic Antimicrobial Peptides, Cecropin A(1−8)−Magainin 2(1−12) and Its Analogues, on Their Antibiotic Activities and Structures † , ‡. Biochemistry 2000, 39: 11855-11864. PMID: 11009597, DOI: 10.1021/bi000453g.Peer-Reviewed Original ResearchAmino Acid SequenceAmino Acid SubstitutionAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntineoplastic AgentsBacillus subtilisElectric ConductivityEscherichia coliHumansIon ChannelsJurkat CellsK562 CellsLipid BilayersMagaininsMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptide FragmentsProtein Structure, SecondaryProtein Structure, TertiaryTryptophanXenopus Proteins
1999
Studies of the Chemical Structure of Gangliosides in Deer Antler, Cervus nippon
Jhon G, Park S, Han S, Lee S, Kim Y, Chang Y. Studies of the Chemical Structure of Gangliosides in Deer Antler, Cervus nippon. Chemical And Pharmaceutical Bulletin 1999, 47: 123. PMID: 9987834, DOI: 10.1248/cpb.47.123.Peer-Reviewed Original ResearchConceptsHigh-field proton nuclear magnetic resonance spectroscopyFast atom bombardment mass spectrometry studiesProton nuclear magnetic resonance spectroscopyNuclear magnetic resonance spectroscopyGas chromatography/mass spectrometryChromatography/mass spectrometrySilica gel column chromatographyGel column chromatographyDirect compositional analysisDEAE-Sephadex AMagnetic resonance spectroscopyN-acetyl GM3Amperometric detectionChemical structurePrior derivatizationSpectrometry studiesStructural determinationTrifluoroacetic acidMass spectrometryResonance spectroscopyColumn chromatographyStandard monosaccharidesBiological activityStructure of gangliosidesCeramide moiety