2001
Three Pairs of Cysteine Residues Mediate Both Redox and Zn2+ Modulation of the NMDA Receptor
Choi Y, Chen H, Lipton S. Three Pairs of Cysteine Residues Mediate Both Redox and Zn2+ Modulation of the NMDA Receptor. Journal Of Neuroscience 2001, 21: 392-400. PMID: 11160420, PMCID: PMC6763802, DOI: 10.1523/jneurosci.21-02-00392.2001.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBinding SitesCells, CulturedCysteineDithiothreitolDose-Response Relationship, DrugDrug SynergismGlycineHistidineMesylatesMutagenesis, Site-DirectedN-MethylaspartateOocytesOxidation-ReductionPatch-Clamp TechniquesReceptors, N-Methyl-D-AspartateStructure-Activity RelationshipSulfhydryl ReagentsTransfectionXenopusZinc
2000
Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation
Choi Y, Tenneti L, Le D, Ortiz J, Bai G, Chen H, Lipton S. Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation. Nature Neuroscience 2000, 3: 15-21. PMID: 10607390, DOI: 10.1038/71090.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineChromatography, High Pressure LiquidCysteineDose-Response Relationship, DrugEthyl MethanesulfonateHumansIndicators and ReagentsIon TransportMesylatesMutagenesis, Site-DirectedNitric OxideNitroso CompoundsN-MethylaspartateOocytesPatch-Clamp TechniquesPeptide FragmentsReceptors, N-Methyl-D-AspartateS-NitrosothiolsTransfectionXenopus laevisConceptsS-nitrosylationMolecular basisIon channelsCritical cysteine residuesEndogenous S-nitrosylationSite-directed mutagenesisEndogenous nitric oxideIon channel activityNR2A subunitNitric oxideCysteine residuesSingle cysteineIon channel modulationChannel activityPhysiological conditionsSubunitsChannel modulationCell systemNMDA receptorsMutagenesisCysteineResiduesRegulationAlanineModulation
1997
Agonist-induced closure of constitutively open γ-aminobutyric acid channels with mutated M2 domains
Pan Z, Zhang D, Zhang X, Lipton S. Agonist-induced closure of constitutively open γ-aminobutyric acid channels with mutated M2 domains. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 6490-6495. PMID: 9177245, PMCID: PMC21077, DOI: 10.1073/pnas.94.12.6490.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCloning, MolecularFemaleGABA AgonistsGABA AntagonistsGamma-Aminobutyric AcidIon Channel GatingIon ChannelsMacromolecular SubstancesMembrane PotentialsMolecular Sequence DataMutagenesis, Site-DirectedOocytesOrganophosphorus CompoundsPoint MutationRatsReceptors, GABAReceptors, GlycineReceptors, NicotinicRecombinant ProteinsSequence AlignmentSequence Homology, Amino AcidVirulence Factors, BordetellaXenopus laevisConceptsLigand-gated ion channelsChannel gatingIon channelsAmino acid residuesAminobutyric acid channelsSingle-point mutantsAbsence of ligandChannel pore regionStructure-function relationshipsPoint mutantsAcid channelImportant new insightsAllosteric transitionSubunit resultsAcid residuesM2 domainConstitutive currentReceptor proteinPore regionAgonist bindingAgonist regulationSubstituting alanineM2 regionSpontaneous channel openingChannel opening
1995
Cloning of a gamma-aminobutyric acid type C receptor subunit in rat retina with a methionine residue critical for picrotoxinin channel block.
Zhang D, Pan Z, Zhang X, Brideau A, Lipton S. Cloning of a gamma-aminobutyric acid type C receptor subunit in rat retina with a methionine residue critical for picrotoxinin channel block. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 11756-11760. PMID: 8524843, PMCID: PMC40481, DOI: 10.1073/pnas.92.25.11756.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceChloride ChannelsCloning, MolecularDose-Response Relationship, DrugDrug ResistanceElectric ConductivityGABA AntagonistsIon ChannelsMethionineMolecular Sequence DataMutagenesis, Site-DirectedPicrotoxinProtein ConformationRatsReceptors, GABARetinaSequence Homology, Amino AcidSesterterpenesStructure-Activity RelationshipConceptsGABAC responsesRat retinaRho 2 subunitsGamma-aminobutyric acidPTX resistanceHeteromeric receptorsReceptor subunitsFunctional homomeric receptorsRho 1 receptorsGABA receptor subunitsInhibitory neurotransmissionMechanism of blockGABA receptorsMammalian retinaConvulsant picrotoxininHomomeric receptorsRat receptorRetinaIonotropic receptorsReceptorsChannel blockPicrotoxininSecond membrane-spanning regionNative receptorPredominant determinant
1994
Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor
Sullivan J, Traynelis S, Chen H, Escobar W, Heinemann S, Lipton S. Identification of two cysteine residues that are required for redox modulation of the NMDA subtype of glutamate receptor. Neuron 1994, 13: 929-936. PMID: 7524561, DOI: 10.1016/0896-6273(94)90258-5.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCysteineDithiothreitolElectrophysiologyFemaleIon Channel GatingIon ChannelsMolecular Sequence DataMutagenesis, Site-DirectedN-MethylaspartateOocytesOxidation-ReductionPatch-Clamp TechniquesRatsReceptors, N-Methyl-D-AspartateRecombinant ProteinsSpermineStructure-Activity RelationshipXenopus