2020
DNA-Origami-Based Fluorescence Brightness Standards for Convenient and Fast Protein Counting in Live Cells
Williams ND, Landajuela A, Kasula RK, Zhou W, Powell JT, Xi Z, Isaacs FJ, Berro J, Toomre D, Karatekin E, Lin C. DNA-Origami-Based Fluorescence Brightness Standards for Convenient and Fast Protein Counting in Live Cells. Nano Letters 2020, 20: 8890-8896. PMID: 33164530, PMCID: PMC7726105, DOI: 10.1021/acs.nanolett.0c03925.Peer-Reviewed Original ResearchConceptsCopies of proteinsBrightness standardsFluorescence microscopyProtein countingMammalian cellsFluorescent proteinCopy numberLive cellsConventional quantification techniquesBiological LaboratoryFluorescence microscopeProteinDNA origamiVersatile toolCellsBiologyCurrent quantification methodsCopiesOrganic dyesRetromer forms low order oligomers on supported lipid bilayers
Deatherage CL, Nikolaus J, Karatekin E, Burd CG. Retromer forms low order oligomers on supported lipid bilayers. Journal Of Biological Chemistry 2020, 295: 12305-12316. PMID: 32651229, PMCID: PMC7443500, DOI: 10.1074/jbc.ra120.013672.Peer-Reviewed Original ResearchConceptsLow-order oligomersAccessory factorsLipid bilayersMembrane-associated cargoesCoat protein complexIntegral membrane proteinsModel cargo proteinSingle-particle fluorescence microscopyRetromer sorting pathwayMembrane cargoNexin 3WASH complexCargo proteinsSorting pathwaysMembrane associationProtein complexesSNX3-retromerEndosomal systemMembrane proteinsEndosome membraneRecycling pathwayRetromerOligomeric interactionsIntrinsic propensityFluorescence microscopy
2016
Cholesterol Increases the Openness of SNARE-Mediated Flickering Fusion Pores
Stratton BS, Warner JM, Wu Z, Nikolaus J, Wei G, Wagnon E, Baddeley D, Karatekin E, O’Shaughnessy B. Cholesterol Increases the Openness of SNARE-Mediated Flickering Fusion Pores. Biophysical Journal 2016, 110: 1538-1550. PMID: 27074679, PMCID: PMC4833774, DOI: 10.1016/j.bpj.2016.02.019.Peer-Reviewed Original ResearchConceptsT-SNAREsFusion poreSoluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteinsLipid bilayer propertiesFactor attachment protein receptor proteinsN-ethylmaleimide-sensitive factor attachment protein receptor proteinsTotal internal reflection fluorescence microscopyCognate t-SNAREsFusion pore dynamicsPhysiological cholesterol levelsProtein receptor proteinsFlickering fusion poresReflection fluorescence microscopyIndividual fusion eventsV-SNAREBilayer propertiesFusion eventsPore flickeringReceptor proteinFluorescence microscopySmall unilamellar vesiclesLipid compositionFusion siteSnareExocytotic release
2011
Back Cover: Coupling Amperometry and Total Internal Reflection Fluorescence Microscopy at ITO Surfaces for Monitoring Exocytosis of Single Vesicles (Angew. Chem. Int. Ed. 22/2011)
Meunier A, Jouannot O, Fulcrand R, Fanget I, Bretou M, Karatekin E, Arbault S, Guille M, Darchen F, Lemaître F, Amatore C. Back Cover: Coupling Amperometry and Total Internal Reflection Fluorescence Microscopy at ITO Surfaces for Monitoring Exocytosis of Single Vesicles (Angew. Chem. Int. Ed. 22/2011). Angewandte Chemie International Edition 2011, 50 DOI: 10.1002/anie.201102239.Peer-Reviewed Original ResearchTotal internal reflection fluorescence microscopyReflection fluorescence microscopyFluorescence microscopySingle living cellsCellular organismsSingle exocytotic eventsMolecular messengersExocytotic eventsLiving cellsSingle vesiclesExtracellular mediumExocytosisKey mechanismOrganismsMessengerVesiclesCellsMicroscopy