Aniruddha Panda
Associate Research Scientist in Cell BiologyCards
About
Research
Publications
2024
A proteome-wide quantitative platform for nanoscale spatially resolved extraction of membrane proteins into native nanodiscs
Brown C, Ghosh S, McAllister R, Kumar M, Walker G, Sun E, Aman T, Panda A, Kumar S, Li W, Coleman J, Liu Y, Rothman J, Bhattacharyya M, Gupta K. A proteome-wide quantitative platform for nanoscale spatially resolved extraction of membrane proteins into native nanodiscs. Nature Methods 2024, 22: 412-421. PMID: 39609567, PMCID: PMC11810782, DOI: 10.1038/s41592-024-02517-x.Peer-Reviewed Original ResearchTarget membrane proteinsMembrane proteinsMembrane contextSynaptic vesicle membrane proteinVesicle membrane proteinsMammalian membrane proteinsMembrane-active polymersExtraction of membrane proteinsNative nanodiscsOrganellar membranesNative membrane environmentMultiprotein complexesMolecular contextCellular membranesMembrane environmentQuantitative platformBioanalytical approachesExtraction efficiencyOpen-access databasesProteinMembraneExtraction conditionsNanodiscsTarget MPDirect determination of membrane protein lipid complexes from cellular membranes through native top-down MS
Gupta K, Jung W, Panda A, Brown C. Direct determination of membrane protein lipid complexes from cellular membranes through native top-down MS. Biophysical Journal 2024, 123: 450a-451a. DOI: 10.1016/j.bpj.2023.11.2748.Peer-Reviewed Original ResearchCapturing membrane snapshots: A quantitative proteome-wide guide for high-throughput spatially resolved extraction of membrane proteins for structural/functional studies on native membranes
Brown C, Ghosh S, McAllister R, Coleman J, Sun E, Zheng H, Kumar S, Panda A, Rothman J, Bhattacharyya M, Gupta K. Capturing membrane snapshots: A quantitative proteome-wide guide for high-throughput spatially resolved extraction of membrane proteins for structural/functional studies on native membranes. Biophysical Journal 2024, 123: 68a-69a. DOI: 10.1016/j.bpj.2023.11.487.Peer-Reviewed Original Research
2023
Roles for diacylglycerol in synaptic vesicle priming and release revealed by complete reconstitution of core protein machinery
Sundaram R, Chatterjee A, Bera M, Grushin K, Panda A, Li F, Coleman J, Lee S, Ramakrishnan S, Ernst A, Gupta K, Rothman J, Krishnakumar S. Roles for diacylglycerol in synaptic vesicle priming and release revealed by complete reconstitution of core protein machinery. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2309516120. PMID: 37590407, PMCID: PMC10450444, DOI: 10.1073/pnas.2309516120.Peer-Reviewed Original ResearchConceptsCore protein machineryRelease-ready vesiclesSynaptic vesicle primingVesicle primingProtein machinerySingle-molecule imagingSNAREpin assemblyFunctional intermediatesFunctional reconstitutionMunc13DiacylglycerolCoordinated actionMunc18VesiclesMachineryComplete reconstitutionNew roleSelective effectDetailed characterizationChaperonesRate of caReconstitutionVAMP2ComplexinMutationsStudying 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 lipidsMembraneDirect determination of oligomeric organization of integral membrane proteins and lipids from intact customizable bilayer
Panda A, Giska F, Duncan A, Welch A, Brown C, McAllister R, Hariharan P, Goder J, Coleman J, Ramakrishnan S, Pincet F, Guan L, Krishnakumar S, Rothman J, Gupta K. Direct determination of oligomeric organization of integral membrane proteins and lipids from intact customizable bilayer. Nature Methods 2023, 20: 891-897. PMID: 37106230, PMCID: PMC10932606, DOI: 10.1038/s41592-023-01864-5.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsMembrane proteinsOligomeric organizationOligomeric stateNative mass spectrometry analysisFunctional oligomeric stateKey membrane componentMass spectrometry analysisNMS analysisTarget membraneLipid bindingMembrane componentsProteolipid vesiclesMembrane compositionLipid compositionSpectrometry analysisLipid membranesNeurotransmitter releaseProteinMembraneLipidsMembrane propertiesDirect determinationBilayersTransporters
2022
A Quantitative Native Mass Spectrometry Platform for Deconstructing Hierarchical Organization of Membrane Proteins and Lipids
Panda A, Giska F, Brown C, Coleman J, Rothman J, Gupta K. A Quantitative Native Mass Spectrometry Platform for Deconstructing Hierarchical Organization of Membrane Proteins and Lipids. The FASEB Journal 2022, 36 DOI: 10.1096/fasebj.2022.36.s1.0r472.Peer-Reviewed Original ResearchMembrane proteinsOligomeric stateSpecific lipidsBiophysical propertiesSugar transporter proteinsPhysiological membranesBacterial plasma membraneTarget membrane proteinsLipid bilayer environmentSynaptic vesicle proteinsLipid compositionMS/MS capabilitiesProtein oligomerizationCellular signalingOligomeric organizationVesicle proteinsMembrane curvaturePlasma membraneMacromolecular assembliesTransporter proteinsNative massOligomeric populationMS/MS analysisRegulatory roleDiverse setAnalysis of Lipid Signaling in Drosophila Photoreceptors using Mass Spectrometry.
Panda A, Thakur R, Kumari A, Raghu P. Analysis of Lipid Signaling in Drosophila Photoreceptors using Mass Spectrometry. Journal Of Visualized Experiments 2022 PMID: 35311809, DOI: 10.3791/63516.Peer-Reviewed Original ResearchConceptsTransient receptor potentialDrosophila photoreceptorsSensory transductionMembrane lipid phosphatidylinositolLipid mass spectrometryLipid phosphatidylinositolDrosophila mutantsLipid signalingSignaling lipidsClasses of lipidsCell biologyPhospholipase CβSpecific lipidsMolecular geneticsLipid speciesPhotoreceptor physiologySuch lipidsMass spectrometryMutantsPhotoreceptorsLipid analysisTransductionModel systemBiologyReceptor potentialA tunable lipid bilayer native MS platform for direct determination of hierarchical organization of membrane proteins and lipids at the membrane
Panda A, Giska F, Brown C, Coleman J, Rothman J, Gupta K. A tunable lipid bilayer native MS platform for direct determination of hierarchical organization of membrane proteins and lipids at the membrane. Biophysical Journal 2022, 121: 312a-313a. DOI: 10.1016/j.bpj.2021.11.1192.Peer-Reviewed Original Research
2019
Regulation of Membrane Turnover by Phosphatidic Acid: Cellular Functions and Disease Implications
Thakur R, Naik A, Panda A, Raghu P. Regulation of Membrane Turnover by Phosphatidic Acid: Cellular Functions and Disease Implications. Frontiers In Cell And Developmental Biology 2019, 7: 83. PMID: 31231646, PMCID: PMC6559011, DOI: 10.3389/fcell.2019.00083.Peer-Reviewed Original ResearchEukaryotic cellsPhosphatidic acidHuman disease geneticsPA functionSingle cell typeNovel genetic modelModel organismsSimplest glycerophospholipidCellular functionsDisease geneticsSignal transductionLipid biosynthesisPhospholipid biosynthesisCell biologyPLD inhibitorsMembrane transportHuman diseasesCell typesDisease implicationsMembrane turnoverGenetic modelsBiosynthesisProteinEnzymeCells