2019
A mitochondrial megachannel resides in monomeric F1FO ATP synthase
Mnatsakanyan N, Llaguno MC, Yang Y, Yan Y, Weber J, Sigworth FJ, Jonas EA. A mitochondrial megachannel resides in monomeric F1FO ATP synthase. Nature Communications 2019, 10: 5823. PMID: 31862883, PMCID: PMC6925261, DOI: 10.1038/s41467-019-13766-2.Peer-Reviewed Original ResearchConceptsATP synthase monomersMitochondrial permeability transition poreATP synthaseGiant unilamellar vesiclesMitochondrial megachannelOligomeric stateSmall unilamellar vesiclesF1Fo-ATP synthaseMitochondrial ATP synthaseMitochondrial inner membraneCryo-EM density mapsPermeability transition porePorcine heart mitochondriaUnilamellar vesiclesInner membraneMPTP activityTransition poreElectron cryomicroscopyChannel activityLipid compositionDimer formationHeart mitochondriaSynthaseChannel formationVesicles
2015
bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles
Zheng H, Lee S, Llaguno MC, Jiang QX. bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles. The Journal Of General Physiology 2015, 147: 77-93. PMID: 26712851, PMCID: PMC4692488, DOI: 10.1085/jgp.201511448.Peer-Reviewed Original ResearchConceptsMembrane proteinsIon channelsLipid compositionLipid bilayersMembrane systemLipid-protein interactionsVitro membrane systemSingle-molecule imagingVoltage-gated ion channelsGiant vesiclesUnilamellar naturePlanar electrodesPlanar lipid bilayersSuch proteinsMicroscopic imagingBiophysical analysisFast gating kineticsUnidirectional insertionProteinChannel activityProtein orientationGating kineticsModel systemBilayersSpecific ligands