2025
Native Top-down analysis of membrane protein complexes directly from in vitro and native membranes
Jung W, Panda A, Lee J, Ghosh S, Shaw J, Gupta K. Native Top-down analysis of membrane protein complexes directly from in vitro and native membranes. Molecular & Cellular Proteomics 2025, 100993. PMID: 40378922, DOI: 10.1016/j.mcpro.2025.100993.Peer-Reviewed Original ResearchNative mass spectrometryProtein complexesMembrane proteinsBAM complexTop-down MS/MSAnalysis of membrane protein complexesMembrane-associated protein complexesTarget membrane proteinsNative membranesIntegral membrane proteinsTop-down identificationMembrane protein complexesCell-derived membrane vesiclesMass spectrometryMembrane vesiclesOrganization of proteinsDestabilize lipid bilayersAntibiotic targetsProtein-lipid complexesHeteromeric natureSynthetic liposomesCellular membranesCo-factorNative membrane vesiclesTotal membranes
2024
Determining the membrane recruitment mechanisms of peripheral membrane proteins through native mass spectrometry directly from tunable lipid membranes
McAllister R, Jung W, Bhattacharyya M, Gupta K. Determining the membrane recruitment mechanisms of peripheral membrane proteins through native mass spectrometry directly from tunable lipid membranes. Biophysical Journal 2024, 123: 90a. DOI: 10.1016/j.bpj.2023.11.665.Peer-Reviewed Original Research
2023
Studying Membrane Protein–Lipid Specificity through Direct Native Mass Spectrometric Analysis from Tunable Proteoliposomes
Panda A, Brown C, Gupta K. Studying Membrane Protein–Lipid Specificity through Direct Native Mass Spectrometric Analysis from Tunable Proteoliposomes. Journal Of The American Society For Mass Spectrometry 2023, 34: 1917-1927. PMID: 37432128, PMCID: PMC10932607, DOI: 10.1021/jasms.3c00110.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsMembrane proteinsNative mass spectrometryTrafficking pathwaysPlasma membraneEukaryotic integral membrane proteinsEndoplasmic reticulumBiophysical propertiesMembrane protein assemblySynaptic vesiclesCellular trafficking pathwaysOrganellar membranesLipid specificityTransmembrane proteinProtein assembliesMembrane contextMass spectrometric analysisProteinNative mass spectrometric analysesVAMP2Lipid compositionExogenous ligandsLipid membranesIndividual lipidsMembrane
2021
A human apolipoprotein L with detergent-like activity kills intracellular pathogens
Gaudet RG, Zhu S, Halder A, Kim BH, Bradfield CJ, Huang S, Xu D, Mamiñska A, Nguyen TN, Lazarou M, Karatekin E, Gupta K, MacMicking JD. A human apolipoprotein L with detergent-like activity kills intracellular pathogens. Science 2021, 373 PMID: 34437126, PMCID: PMC8422858, DOI: 10.1126/science.abf8113.Peer-Reviewed Original ResearchMeSH KeywordsApolipoproteins LBacterial Outer MembraneBacteriolysisCell MembraneCell Membrane PermeabilityCells, CulturedCRISPR-Cas SystemsCytosolDetergentsGene EditingGram-Negative BacteriaGTP-Binding ProteinsHumansImmunity, InnateInterferon-gammaLipoproteinsMicrobial ViabilityO AntigensProtein DomainsSalmonella typhimuriumSolubilityConceptsSingle-particle cryo-electron microscopyCell-autonomous defenseCytosol-invasive bacteriaExpression of hundredsNative mass spectrometryCryo-electron microscopyHuman genesDetergent-like activityHost proteinsLipoprotein nanodiscsMammalian lipidsExtracellular transportImmune cytokine interferonCell typesDetergent-like propertiesApolipoprotein LLife-threatening infectionsPotent bactericidal agentsAnionic membranesProteinCytokine interferonNonimmune cellsMass spectrometryCellsMutagenesis
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