2015
Two Na+ Sites Control Conformational Change in a Neurotransmitter Transporter Homolog*
Tavoulari S, Margheritis E, Nagarajan A, DeWitt DC, Zhang YW, Rosado E, Ravera S, Rhoades E, Forrest LR, Rudnick G. Two Na+ Sites Control Conformational Change in a Neurotransmitter Transporter Homolog*. Journal Of Biological Chemistry 2015, 291: 1456-1471. PMID: 26582198, PMCID: PMC4714228, DOI: 10.1074/jbc.m115.692012.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SubstitutionAmino Acid Transport SystemsAquatic OrganismsBacterial ProteinsBinding SitesCysteineGram-Negative BacteriaLigandsLiposomesModels, MolecularMolecular Dynamics SimulationMutagenesis, Site-DirectedMutationPlasma Membrane Neurotransmitter Transport ProteinsProtein ConformationProtein FoldingProtein StabilityProteolipidsRecombinant ProteinsSodiumConceptsConformational changesTransmembrane helix 1Open conformational stateDependent conformational changesTransporter homologExtracellular gateProkaryotic homologCytoplasmic pathwayHelix 1Interaction networksIntermediary interactionsBiophysical assaysNeurotransmitter transportersSubstrate pathwayNa2 siteConformational statesHelix motionsLeuTDirect interactionDependent closureHomologMutantsDistinct stepsResiduesComputational analysis
2013
How do transporters couple solute movements?
Rudnick G. How do transporters couple solute movements? Molecular Membrane Biology 2013, 30: 355-359. PMID: 24147977, PMCID: PMC4077868, DOI: 10.3109/09687688.2013.842658.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus Statements
2009
Ligand Effects on Cross-linking Support a Conformational Mechanism for Serotonin Transport*
Tao Z, Zhang YW, Agyiri A, Rudnick G. Ligand Effects on Cross-linking Support a Conformational Mechanism for Serotonin Transport*. Journal Of Biological Chemistry 2009, 284: 33807-33814. PMID: 19837674, PMCID: PMC2797150, DOI: 10.1074/jbc.m109.071977.Peer-Reviewed Original ResearchConceptsN-terminal cyanogen bromide fragmentGamma-aminobutyric acid transporterCyanogen bromide fragmentsTransmembrane 1Cysteine residuesMutagenesis strategyAcid transportersConformational mechanismSerotonin transportCysteineCorresponding positionDisulfide CrossTransportersSynaptic cleftResiduesSame molecule
2008
Involvement of serotonin transporter extracellular loop 1 in serotonin binding and transport
Mao Y, Mao Y, Mathewson L, Mao Y, Mathewson L, Gesmonde J, Sato Y, Mao Y, Mathewson L, Gesmonde J, Sato Y, Holy M, Sitte H, Rudnick G. Involvement of serotonin transporter extracellular loop 1 in serotonin binding and transport. Molecular Membrane Biology 2008, 25: 115-127. PMID: 18307099, PMCID: PMC4510095, DOI: 10.1080/09687680701633257.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCell MembraneHeLa CellsHumansIndicators and ReagentsKineticsLigandsMesylatesMolecular Sequence DataMutant ProteinsProtein Structure, TertiaryRatsSequence DeletionSerotoninSerotonin Plasma Membrane Transport ProteinsStructure-Activity Relationship
2001
A Conformationally Sensitive Residue on the Cytoplasmic Surface of Serotonin Transporter*
Androutsellis-Theotokis A, Ghassemi F, Rudnick G. A Conformationally Sensitive Residue on the Cytoplasmic Surface of Serotonin Transporter*. Journal Of Biological Chemistry 2001, 276: 45933-45938. PMID: 11592963, DOI: 10.1074/jbc.m107462200.Peer-Reviewed Original Research
1997
The Third Transmembrane Domain of the Serotonin Transporter Contains Residues Associated with Substrate and Cocaine Binding*
Chen J, Sachpatzidis A, Rudnick G. The Third Transmembrane Domain of the Serotonin Transporter Contains Residues Associated with Substrate and Cocaine Binding*. Journal Of Biological Chemistry 1997, 272: 28321-28327. PMID: 9353288, DOI: 10.1074/jbc.272.45.28321.Peer-Reviewed Original ResearchAsparagineBinding SitesCarrier ProteinsCell LineCell MembraneCocaineCysteineEthyl MethanesulfonateHumansIndicators and ReagentsIsoleucineLigandsMembrane GlycoproteinsMembrane Transport ProteinsMesylatesMutagenesis, Site-DirectedNerve Tissue ProteinsProtein Structure, SecondarySerotoninSerotonin Plasma Membrane Transport ProteinsStructure-Activity RelationshipTyrosine
1994
Ligand binding to the serotonin transporter: equilibria, kinetics, and ion dependence.
Humphreys C, Wall S, Rudnick G. Ligand binding to the serotonin transporter: equilibria, kinetics, and ion dependence. Biochemistry 1994, 33: 9118-25. PMID: 8049215, DOI: 10.1021/bi00197a014.Peer-Reviewed Original Research
1990
Energetics of reserpine binding and occlusion by the chromaffin granule biogenic amine transporter.
Rudnick G, Steiner-Mordoch S, Fishkes H, Stern-Bach Y, Schuldiner S. Energetics of reserpine binding and occlusion by the chromaffin granule biogenic amine transporter. Biochemistry 1990, 29: 603-8. PMID: 2140052, DOI: 10.1021/bi00455a002.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmmonium SulfateBinding SitesBiogenic AminesCarbonyl Cyanide m-Chlorophenyl HydrazoneCarrier ProteinsChloridesChromaffin GranulesChromaffin SystemDetergentsElectrochemistryHydrogen-Ion ConcentrationIonophoresKineticsLigandsMembrane PotentialsReserpineThermodynamicsThiocyanatesTime FactorsUreaConceptsBiogenic amine transportersReserpine bindingChromaffin granule membrane vesiclesAmine transportersAmine transportMembrane vesiclesDead-end complexIon translocationTransportersSubstrate moleculesBindingM ureaDelta pHTranslocationTriton XSodium dodecyl sulfateNeutral substrate moleculesTransmembraneHigh-affinity site
1989
2-Iodoimipramine, a novel ligand for the serotonin transporter.
Humphreys C, Cassel D, Rudnick G. 2-Iodoimipramine, a novel ligand for the serotonin transporter. Molecular Pharmacology 1989, 36: 620-6. PMID: 2811859.Peer-Reviewed Original Research