Marc C Llaguno, PhD
Research ScientistDownloadHi-Res Photo
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Neuroscience
Primary
Additional Titles
Site Director, Cryo-Electron Microscopy YSM, Neuroscience
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Appointments
Neuroscience
Primary
Additional Titles
Site Director, Cryo-Electron Microscopy YSM, Neuroscience
Contact Info
Appointments
Neuroscience
Primary
Additional Titles
Site Director, Cryo-Electron Microscopy YSM, Neuroscience
Contact Info
About
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Titles
Research Scientist
Site Director, Cryo-Electron Microscopy YSM, Neuroscience
Appointments
Neuroscience
Research ScientistPrimary
Other Departments & Organizations
- Electron Microscopy
- Neuroscience
Education & Training
- PhD
- University of Pennsylvania, Physics (2004)
- BS
- University of the Philippines, Physics (1997)
Research
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Overview
Medical Research Interests
Cryoelectron Microscopy
ORCID
0000-0001-9568-9565- View Lab Website
CCMI Electron Microscopy Lab
Research at a Glance
Yale Co-Authors
Frequent collaborators of Marc C Llaguno's published research.
Publications Timeline
A big-picture view of Marc C Llaguno's research output by year.
Research Interests
Research topics Marc C Llaguno is interested in exploring.
Elizabeth Jonas, MD
Nelli Mnatsakanyan, PhD
Chenxiang Lin, PhD
Jing Wu
25Publications
7,210Citations
Cryoelectron Microscopy
Publications
2022
Mitochondrial ATP synthase c-subunit leak channel triggers cell death upon loss of its F1 subcomplex
Mnatsakanyan N, Park HA, Wu J, He X, Llaguno MC, Latta M, Miranda P, Murtishi B, Graham M, Weber J, Levy RJ, Pavlov EV, Jonas EA. Mitochondrial ATP synthase c-subunit leak channel triggers cell death upon loss of its F1 subcomplex. Cell Death & Differentiation 2022, 29: 1874-1887. PMID: 35322203, PMCID: PMC9433415, DOI: 10.1038/s41418-022-00972-7.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsMitochondrial permeability transitionATP synthase c-subunitCell deathMitochondrial ATP synthaseChannel activityCellular energy productionLeak channelsVoltage-gated ion channelsF1 subcomplexATP synthaseC subunitInner membraneProkaryotic hostsCell stressPermeability transitionIon channelsGating mechanismOsmotic changesLarge conductanceC-ringChannels triggersNeuronal deathF1SubcomplexOsmotic gradient
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 ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsATP 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
2017
Placing and shaping liposomes with reconfigurable DNA nanocages
Zhang Z, Yang Y, Pincet F, Llaguno M, Lin C. Placing and shaping liposomes with reconfigurable DNA nanocages. Nature Chemistry 2017, 9: 653-659. PMID: 28644472, PMCID: PMC5542812, DOI: 10.1038/nchem.2802.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsMembrane-bound vesiclesDNA cagesRegulated deformationsDNA nanocagesMembrane curvatureMembrane fusionConformational changesBiological membranesCell membraneLipid bilayer membranesMembrane mechanicsVesiclesDiverse structuresMembraneCellsBilayer membranesVersatile toolDelivery vesiclesToroid shapeLiposome shape
2016
bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles
Zheng H, Lee S, Llaguno M, Jiang Q. bSUM: A bead-supported unilamellar membrane system facilitating unidirectional insertion of membrane proteins into giant vesicles. Journal Of Cell Biology 2016, 212: 2122oia1. DOI: 10.1083/jcb.2122oia1.Peer-Reviewed Original Research
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. Journal Of General Physiology 2015, 147: 77-93. PMID: 26712851, PMCID: PMC4692488, DOI: 10.1085/jgp.201511448.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsMembrane 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
2014
Chemically functionalized carbon films for single molecule imaging
Llaguno MC, Xu H, Shi L, Huang N, Zhang H, Liu Q, Jiang QX. Chemically functionalized carbon films for single molecule imaging. Journal Of Structural Biology 2014, 185: 405-417. PMID: 24457027, PMCID: PMC3990355, DOI: 10.1016/j.jsb.2014.01.006.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsCarbon surfaceNanometer-thick carbon filmsBiological complexesCarbon filmsIndividual macromolecular complexesFunctionalized filmsBioactive ligandsChemical linkageSingle-molecule imagingSubnanogram levelActive siteStrong oxidationNanomolar levelsDNA/RNAMolecule imagingNegative-stain EMElectron microscopic imagingSelective enrichmentComplexesLigandsMacromolecular complexesFilmsProtein GSubnanomolar concentrationsLong-term storage
2012
Phase transitions in the assembly of multivalent signalling proteins
Li P, Banjade S, Cheng HC, Kim S, Chen B, Guo L, Llaguno M, Hollingsworth JV, King DS, Banani SF, Russo PS, Jiang QX, Nixon BT, Rosen MK. Phase transitions in the assembly of multivalent signalling proteins. Nature 2012, 483: 336-340. PMID: 22398450, PMCID: PMC3343696, DOI: 10.1038/nature10879.Commentaries, Editorials and LettersCitationsAltmetricMeSH Keywords and ConceptsMeSH KeywordsActin-Related Protein 2-3 ComplexAdaptor Proteins, Signal TransducingBinding SitesBiopolymersFluorescence Recovery After PhotobleachingHeLa CellsHumansLigandsMembrane ProteinsMultiprotein ComplexesOncogene ProteinsPhase TransitionPhosphorylationProline-Rich Protein DomainsProtein Structure, QuaternaryProteinsSignal Transductionsrc Homology DomainsWiskott-Aldrich Syndrome Protein, Neuronal
2011
Massive endocytosis driven by lipidic forces originating in the outer plasmalemmal monolayer: a new approach to membrane recycling and lipid domains
Fine M, Llaguno M, Lariccia V, Lin M, Yaradanakul A, Hilgemann D. Massive endocytosis driven by lipidic forces originating in the outer plasmalemmal monolayer: a new approach to membrane recycling and lipid domains. Journal Of General Physiology 2011, 137: 607-607. PMCID: PMC3105520, DOI: 10.1085/jgp.2010104691376c.Peer-Reviewed Original ResearchCitationsMassive calcium–activated endocytosis without involvement of classical endocytic proteins
Lariccia V, Fine M, Magi S, Lin M, Yaradanakul A, Llaguno M, Hilgemann D. Massive calcium–activated endocytosis without involvement of classical endocytic proteins. Journal Of General Physiology 2011, 137: 605-605. PMCID: PMC3105511, DOI: 10.1085/jgp.2010104681376c.Peer-Reviewed Original ResearchMassive endocytosis driven by lipidic forces originating in the outer plasmalemmal monolayer: a new approach to membrane recycling and lipid domains
Fine M, Llaguno MC, Lariccia V, Lin MJ, Yaradanakul A, Hilgemann DW. Massive endocytosis driven by lipidic forces originating in the outer plasmalemmal monolayer: a new approach to membrane recycling and lipid domains. Journal Of General Physiology 2011, 137: 137-154. PMID: 21242300, PMCID: PMC3032378, DOI: 10.1085/jgp.201010469.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsMassive endocytosisPlasma membraneBaby hamster kidneyFM 4HEK293 cellsActin cytoskeleton remodelingNonionic detergentMembrane rufflesProtein cyclingCytoskeleton remodelingMembrane recyclingCytoplasmic sideNa/Ca exchangerTriphosphate hydrolysisCytoplasmic ATPEndocytosisMembrane monolayersCell surfaceLipid domainsG protein cyclingOuter monolayerMembrane tracerVesiclesAmphipathic drugsNP-40
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