Featured Publications
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 ResearchMeSH KeywordsBinding SitesCrystallography, X-RayExtracellular SpaceFibroblast Growth Factor-23Fibroblast Growth FactorsGlycoside HydrolasesHEK293 CellsHumansKlotho ProteinsLigandsMembrane ProteinsModels, MolecularProtein BindingProtein DomainsReceptors, Fibroblast Growth FactorSignal TransductionSubstrate Specificity
1999
Comparison of the Structures of β Amyloid Peptide (25–35) and Substance P in Trifluoroethanol/Water Solution
Lee S, Suh Y, Kim S, Kim Y. Comparison of the Structures of β Amyloid Peptide (25–35) and Substance P in Trifluoroethanol/Water Solution. Journal Of Biomolecular Structure And Dynamics 1999, 17: 381-391. PMID: 10563586, DOI: 10.1080/07391102.1999.10508369.Peer-Reviewed Original ResearchConceptsSubstance PTrifluoroethanol/water solutionTachykinin familyAmyloid peptidesBrains of patientsHydrophobic side chainsBeta-amyloid peptideNMR spectroscopyAqueous solutionΒ-amyloid peptideAlpha-helical structureAromatic ringConformational featuresWater solutionSide chainsTachykinin receptorsBeta amyloidSenile plaquesAlzheimer's diseaseThree-dimensional structureDiseaseReceptors