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, 1-10. PMID: 39609567, 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 MP
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 set