2025
Ion selectivity in brackish groundwater desalination by electrodialysis: Experiments and theory
Shocron A, Monat L, Januszewski B, Dykstra J, Elimelech M, Nir O. Ion selectivity in brackish groundwater desalination by electrodialysis: Experiments and theory. Journal Of Membrane Science 2025, 719: 123668. DOI: 10.1016/j.memsci.2024.123668.Peer-Reviewed Original ResearchIon selectivityFlow channelNon-equilibrium effectsDesalination of brackish waterIon partitioningPost-treatment processIon-exchange membranesBrackish groundwater desalinationIncreasing current densityReverse osmosisSolute rejectionGlobal water shortageMass transport calculationsExchange membraneElectrodialysis systemCurrent densityElectrodialysisDesalinationGroundwater desalinationBrackish groundwaterExperimental measurementsBoundary layerMass transportIonsMembrane surface
2020
Tunable Electromechanical Nanopore Trap Reveals Populations of Peripheral Membrane Protein Binding Conformations
Hoogerheide D, Rostovtseva T, Jacobs D, Gurnev P, Bezrukov S. Tunable Electromechanical Nanopore Trap Reveals Populations of Peripheral Membrane Protein Binding Conformations. ACS Nano 2020, 15: 989-1001. PMID: 33369404, PMCID: PMC9019845, DOI: 10.1021/acsnano.0c07672.Peer-Reviewed Original ResearchConceptsVoltage-dependent anion channelMembrane surfaceSingle-molecule levelSame membrane surfaceIndividual proteinsAnion channelNeuronal proteinsLipid membranesBinding conformationsLipid surfaceLipid compositionProteinΑ-synucleinMembraneConformationOrders of magnitudeSurfaceUnbindingMitochondriaBindsObserved distributionNanoporesMoleculesΑSynTrapsCumulative hydropathic topology of a voltage‐gated sodium channel at atomic resolution
Xenakis M, Kapetis D, Yang Y, Heijman J, Waxman S, Lauria G, Faber C, Smeets H, Westra R, Lindsey P. Cumulative hydropathic topology of a voltage‐gated sodium channel at atomic resolution. Proteins Structure Function And Bioinformatics 2020, 88: 1319-1328. PMID: 32447794, DOI: 10.1002/prot.25951.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceArcobacterBacterial ProteinsBinding SitesHydrophobic and Hydrophilic InteractionsIon Channel GatingModels, MolecularProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandProtein Interaction Domains and MotifsSodiumThermodynamicsVoltage-Gated Sodium ChannelsConceptsVoltage-gated sodium channelsBacterial channelsPhysiological cellular activitySodium channelsCellular activitiesCell membraneBiological poresPore stabilityAtomic resolutionBiophysical significanceMembrane surfaceHydropathicityGenesProteinMutationsWide spectrumMembraneFunctional architectureAccumulationComputational frameworkSodium ionsPores
2019
Filament Nucleation Tunes Mechanical Memory in Active Polymer Networks
Yadav V, Banerjee D, Tabatabai A, Kovar D, Kim T, Banerjee S, Murrell M. Filament Nucleation Tunes Mechanical Memory in Active Polymer Networks. Advanced Functional Materials 2019, 29 PMID: 32523502, PMCID: PMC7286550, DOI: 10.1002/adfm.201905243.Peer-Reviewed Original ResearchPolymer networksShape memoryIsotropic materialsActive materialMaterial designMaterial functionalityLow nucleationChemical timescalesMembrane surfaceNucleationMechanical memoryEnergyMaterialsCritical nucleationFilament curvatureInternal energyDissipationDense networkTopological defectsGrand challenge
2010
Kinase Associated-1 Domains Drive MARK/PAR1 Kinases to Membrane Targets by Binding Acidic Phospholipids
Moravcevic K, Mendrola JM, Schmitz KR, Wang YH, Slochower D, Janmey PA, Lemmon MA. Kinase Associated-1 Domains Drive MARK/PAR1 Kinases to Membrane Targets by Binding Acidic Phospholipids. Cell 2010, 143: 966-977. PMID: 21145462, PMCID: PMC3031122, DOI: 10.1016/j.cell.2010.11.028.Peer-Reviewed Original ResearchConceptsKA1 domainBud neck localizationMembrane association domainAcidic phospholipidsImportance of phosphatidylserineAssociation domainMembrane associationMembrane localizationProtein kinaseC2 domainC-terminusMembrane targetsKinaseIntact proteinAnionic phospholipidsX-ray crystallographyNeck localizationPhosphatidylserinePhospholipidsCrucial roleDomainMembrane surfaceLocalizationTerminusRegulator
2008
Kinetic Modeling of the Assembly, Dynamic Steady State, and Contraction of the FtsZ Ring in Prokaryotic Cytokinesis
Surovtsev I, Morgan J, Lindahl P. Kinetic Modeling of the Assembly, Dynamic Steady State, and Contraction of the FtsZ Ring in Prokaryotic Cytokinesis. PLOS Computational Biology 2008, 4: e1000102. PMID: 18604268, PMCID: PMC2432035, DOI: 10.1371/journal.pcbi.1000102.Peer-Reviewed Original ResearchConceptsSame chemical modelMonomeric unitsPolymeric ringsRapid assemblyChemical modelProkaryotic cytokinesisMembrane surfaceFree energyUnfavorable processMonomeric FtsZKinetic modelingMechanistic complexityInterfacial reactionRingVivo behaviorDynamic steady stateMonomeric subunitsFtsZ polymerizationHydrolysisReactionRing formsAssemblyChapter 4 Protein Trafficking in Polarized Cells
Duffield A, Caplan MJ, Muth TR. Chapter 4 Protein Trafficking in Polarized Cells. International Review Of Cytology 2008, 270: 145-179. PMID: 19081536, DOI: 10.1016/s1937-6448(08)01404-4.Peer-Reviewed Original ResearchConceptsEpithelial cellsProtein traffickingBasolateral membrane surfaceLipid traffickingPolarized cellsDynamic regulationSpecific lipidsAdjacent epithelial cellsCell typesBasolateral surfaceApical surfaceCertain cellsMembrane surfaceTraffickingProtein contentCellsSortingNumber of sortingsImmune systemRecent advancesMechanismProteinRegulationEpitheliumLipids
1994
Characterization of Parietal Cell Functional Morphology Utilizing Isolated Gastric Gland Perfusion, Atomic Force and Confocal Microscopy
Modlin I, Waisbren S, Boron W, Soroka C, Goldenring J, Geibel J. Characterization of Parietal Cell Functional Morphology Utilizing Isolated Gastric Gland Perfusion, Atomic Force and Confocal Microscopy. NATO ASI Series 1994, 329-339. DOI: 10.1007/978-3-642-79301-1_38.Peer-Reviewed Original ResearchMembrane functionMembrane movementFunctional morphologyCell functionApical membrane surfaceConfocal fluorescence microscopyParietal cellsCytoskeletal transformationProton pumpGastric gland preparationProteolytic contentCell culture systemParietal cell functionFluorescence microscopyConfocal microscopySecretory processGland preparationsCulture systemCellsGastric glandsParietal cell preparationsCell preparationsMembrane surfaceLow pH
1989
Location and magnetic relaxation properties of the stable tyrosine radical in photosystem II.
Innes J, Brudvig G. Location and magnetic relaxation properties of the stable tyrosine radical in photosystem II. Biochemistry 1989, 28: 1116-25. PMID: 2540815, DOI: 10.1021/bi00429a028.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacterial ProteinsChlorophyllElectron Spin Resonance SpectroscopyFree RadicalsKineticsLight-Harvesting Protein ComplexesMathematicsMicrowavesModels, MolecularModels, TheoreticalMyoglobinPhotosynthetic Reaction Center Complex ProteinsPhotosystem II Protein ComplexPlant ProteinsProtein ConformationRhodobacter sphaeroidesThermodynamicsTyrosineWhalesConceptsMetal ionsPSII membranesPhotosystem IIProtein surfaceMicrowave power saturationReaction centersRaman relaxation mechanismMagnetic relaxation propertiesFree radicalsRelaxation enhancementDipolar relaxation enhancementIonsMembrane surfaceRelaxation propertiesSpin-lattice relaxationComplexesDipolar interactionsRadicalsRhodobacter sphaeroidesProtein structureD2 subunitsPower saturationDy3Relaxation mechanismSurface
1988
How actin binds and assembles onto plasma membranes from Dictyostelium discoideum.
Schwartz M, Luna E. How actin binds and assembles onto plasma membranes from Dictyostelium discoideum. Journal Of Cell Biology 1988, 107: 201-209. PMID: 3392099, PMCID: PMC2115166, DOI: 10.1083/jcb.107.1.201.Peer-Reviewed Original ResearchConceptsPolymerizationSuccessive monomersMembrane surfacePositive cooperativityActin trimerTight bindingAssembly stateHistidine-40Critical concentrationLow salt bufferDerivativesSalt bufferEthoxyformic anhydrideCooperativitySolutionMonomersMembraneAffinityMultivalencyOligomersAnhydrideActin nucleiBindingCross-linking experimentsActin oligomers
1978
Energy-dependence of phlorizin binding to isolated renal microvillus membranes
Aronson P. Energy-dependence of phlorizin binding to isolated renal microvillus membranes. The Journal Of Membrane Biology 1978, 42: 81-98. PMID: 671529, DOI: 10.1007/bf01870395.Peer-Reviewed Original Research
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply